HEADER ANTITUMOR PROTEIN 16-JAN-25 9I1Q TITLE HER3 RECEPTOR IN COMPLEX WITH THE FAB FRAGMENT OF TK-HU A3 MONOCLONAL TITLE 2 ANTIBODY COMPND MOL_ID: 1; COMPND 2 MOLECULE: RECEPTOR TYROSINE-PROTEIN KINASE ERBB-3; COMPND 3 CHAIN: A, B, C, D; COMPND 4 SYNONYM: PROTO-ONCOGENE-LIKE PROTEIN C-ERBB-3,TYROSINE KINASE-TYPE COMPND 5 CELL SURFACE RECEPTOR HER3; COMPND 6 EC: 2.7.10.1; COMPND 7 ENGINEERED: YES; COMPND 8 OTHER_DETAILS: EXTRACELLULAR DOMAIN; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: LIGHT CHAIN HA3-FAB; COMPND 11 CHAIN: E, F, G, H; COMPND 12 ENGINEERED: YES; COMPND 13 MOL_ID: 3; COMPND 14 MOLECULE: HEAVY CHAIN HA3-FAB; COMPND 15 CHAIN: I, J, K, L; COMPND 16 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: ERBB3, HER3; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS GROWTH FACTOR RECEPTOR, MONOCLONAL ANTIBODY, CANCER, COMPLEX, KEYWDS 2 ANTITUMOR PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR G.BULFARO,C.SAVINO,A.COSTANZO,F.FATA,B.VALLONE,L.C.MONTEMIGLIO REVDAT 1 15-OCT-25 9I1Q 0 JRNL AUTH A.MUZI,R.ARRIGA,G.BULFARO,F.FATA,A.COSTANZO,V.CHIARINI, JRNL AUTH 2 M.CAPPELLETTI,F.F.FERRARA,F.BUCCI,L.C.MONTEMIGLIO,C.SAVINO, JRNL AUTH 3 E.MARRA,G.CILIBERTO,L.AURISICCHIO,B.VALLONE,G.ROSCILLI JRNL TITL NOVEL HUMANIZED ANTI-HER3 ANTIBODIES: STRUCTURAL JRNL TITL 2 CHARACTERIZATION AND THERAPEUTIC ACTIVITY JRNL REF ANTIBODIES V. 14 2025 JRNL REFN ISSN 2073-4468 JRNL DOI 10.3390/ANTIB14040084 REMARK 2 REMARK 2 RESOLUTION. 2.80 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 49.00 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 64.6 REMARK 3 NUMBER OF REFLECTIONS : 81346 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.212 REMARK 3 R VALUE (WORKING SET) : 0.209 REMARK 3 FREE R VALUE : 0.263 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.010 REMARK 3 FREE R VALUE TEST SET COUNT : 4076 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 49.0000 - 8.5900 0.98 4215 222 0.1919 0.2080 REMARK 3 2 8.5900 - 6.8200 0.99 4191 199 0.2115 0.2345 REMARK 3 3 6.8200 - 5.9600 0.99 4177 191 0.2088 0.2414 REMARK 3 4 5.9600 - 5.4200 0.99 4112 210 0.1917 0.2218 REMARK 3 5 5.4200 - 5.0300 1.00 4147 215 0.1682 0.2160 REMARK 3 6 5.0300 - 4.7300 0.99 4087 221 0.1551 0.2083 REMARK 3 7 4.7300 - 4.5000 0.99 4105 193 0.1540 0.2137 REMARK 3 8 4.5000 - 4.3000 0.99 4150 188 0.1647 0.2231 REMARK 3 9 4.3000 - 4.1400 1.00 4115 207 0.1802 0.2566 REMARK 3 10 4.1400 - 3.9900 0.99 4089 231 0.1990 0.2652 REMARK 3 11 3.9900 - 3.8900 0.96 3129 148 0.2217 0.3091 REMARK 3 12 3.8600 - 3.7600 0.96 3750 200 0.2275 0.2897 REMARK 3 13 3.7600 - 3.6600 0.95 3804 244 0.2449 0.3386 REMARK 3 14 3.6600 - 3.5700 0.56 2298 152 0.2578 0.3400 REMARK 3 15 3.5700 - 3.4900 0.76 3091 182 0.2697 0.3362 REMARK 3 16 3.4900 - 3.4300 0.66 1956 113 0.2704 0.3399 REMARK 3 17 3.4100 - 3.3500 0.61 2497 146 0.2757 0.3637 REMARK 3 18 3.3500 - 3.2800 0.58 2379 106 0.2854 0.3524 REMARK 3 19 3.2800 - 3.2200 0.53 2166 129 0.2856 0.2912 REMARK 3 20 3.2200 - 3.1700 0.46 1867 81 0.2886 0.3261 REMARK 3 21 3.1700 - 3.1200 0.40 1646 108 0.2914 0.3327 REMARK 3 22 3.1200 - 3.0700 0.37 1485 87 0.3081 0.4476 REMARK 3 23 3.0700 - 3.0300 0.31 1262 71 0.3239 0.4048 REMARK 3 24 3.0200 - 2.9800 0.27 1105 46 0.3193 0.3746 REMARK 3 25 2.9800 - 2.9400 0.22 920 46 0.3479 0.6239 REMARK 3 26 2.9400 - 2.9000 0.19 775 46 0.3374 0.3380 REMARK 3 27 2.9000 - 2.8700 0.16 661 41 0.3616 0.5061 REMARK 3 28 2.8700 - 2.8300 0.14 576 24 0.4072 0.7386 REMARK 3 29 2.8300 - 2.8000 0.13 515 29 0.4179 0.4611 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) : 0.360 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.090 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 32521 REMARK 3 ANGLE : 1.130 44194 REMARK 3 CHIRALITY : 0.073 4983 REMARK 3 PLANARITY : 0.009 5704 REMARK 3 DIHEDRAL : 6.527 4601 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 55 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 8 THROUGH 113 ) REMARK 3 ORIGIN FOR THE GROUP (A): 44.7914 -18.8631 106.2130 REMARK 3 T TENSOR REMARK 3 T11: 0.5055 T22: 2.2128 REMARK 3 T33: 0.5353 T12: -0.0875 REMARK 3 T13: -0.2103 T23: 0.0978 REMARK 3 L TENSOR REMARK 3 L11: 1.2349 L22: 1.9604 REMARK 3 L33: 1.2350 L12: -0.3583 REMARK 3 L13: 1.2242 L23: -0.1797 REMARK 3 S TENSOR REMARK 3 S11: -0.1147 S12: 0.1913 S13: -0.0063 REMARK 3 S21: 0.4104 S22: 0.1314 S23: -0.6264 REMARK 3 S31: 0.2737 S32: 0.8996 S33: -0.4318 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 114 THROUGH 318 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.0835 -16.6643 94.2604 REMARK 3 T TENSOR REMARK 3 T11: 0.4442 T22: 1.8438 REMARK 3 T33: 0.4415 T12: -0.2807 REMARK 3 T13: 0.0561 T23: 0.0587 REMARK 3 L TENSOR REMARK 3 L11: 0.0748 L22: 0.3841 REMARK 3 L33: 0.0052 L12: -0.1921 REMARK 3 L13: -0.0641 L23: 0.0817 REMARK 3 S TENSOR REMARK 3 S11: 0.1215 S12: -0.0946 S13: -0.1271 REMARK 3 S21: -0.0179 S22: -0.1839 S23: -0.2113 REMARK 3 S31: -0.3816 S32: 0.9796 S33: 0.0363 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 319 THROUGH 611 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.8249 -26.0664 108.4143 REMARK 3 T TENSOR REMARK 3 T11: 0.2285 T22: 0.1975 REMARK 3 T33: 0.1522 T12: 0.1244 REMARK 3 T13: 0.1019 T23: -0.0027 REMARK 3 L TENSOR REMARK 3 L11: 0.7709 L22: 0.9377 REMARK 3 L33: 4.9177 L12: 0.6248 REMARK 3 L13: -0.5321 L23: -1.0987 REMARK 3 S TENSOR REMARK 3 S11: -0.0796 S12: -0.0932 S13: 0.0380 REMARK 3 S21: -0.0356 S22: 0.1358 S23: -0.0449 REMARK 3 S31: 0.0515 S32: -0.0426 S33: -0.0112 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 7 THROUGH 193 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.9086 -47.8680 20.8422 REMARK 3 T TENSOR REMARK 3 T11: 0.4407 T22: 0.3193 REMARK 3 T33: 0.1461 T12: 0.1048 REMARK 3 T13: -0.0607 T23: 0.0291 REMARK 3 L TENSOR REMARK 3 L11: 1.7363 L22: 2.0107 REMARK 3 L33: 2.2537 L12: 0.2018 REMARK 3 L13: -0.3137 L23: -0.2174 REMARK 3 S TENSOR REMARK 3 S11: 0.2342 S12: 0.5051 S13: -0.3322 REMARK 3 S21: -0.5884 S22: 0.1227 S23: 0.1928 REMARK 3 S31: 0.8575 S32: 0.0681 S33: -0.0018 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 194 THROUGH 323 ) REMARK 3 ORIGIN FOR THE GROUP (A): 28.9141 -33.6167 26.2184 REMARK 3 T TENSOR REMARK 3 T11: 0.3166 T22: 0.4996 REMARK 3 T33: 0.3516 T12: -0.1106 REMARK 3 T13: 0.2135 T23: -0.0202 REMARK 3 L TENSOR REMARK 3 L11: 0.6543 L22: 0.9424 REMARK 3 L33: 0.9388 L12: -0.0787 REMARK 3 L13: -0.1814 L23: 0.1723 REMARK 3 S TENSOR REMARK 3 S11: -0.2743 S12: 0.1744 S13: -0.1636 REMARK 3 S21: -0.5260 S22: 0.1413 S23: -0.5885 REMARK 3 S31: -0.2485 S32: 0.3545 S33: -0.0599 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 324 THROUGH 567 ) REMARK 3 ORIGIN FOR THE GROUP (A): 55.6730 -14.1173 1.1029 REMARK 3 T TENSOR REMARK 3 T11: 0.5196 T22: 0.5559 REMARK 3 T33: 0.6379 T12: 0.0440 REMARK 3 T13: 0.3080 T23: 0.1179 REMARK 3 L TENSOR REMARK 3 L11: 0.9316 L22: 0.0354 REMARK 3 L33: 3.9110 L12: -0.0621 REMARK 3 L13: -1.6880 L23: -0.0988 REMARK 3 S TENSOR REMARK 3 S11: -0.2053 S12: -0.0849 S13: -0.0614 REMARK 3 S21: -0.0467 S22: -0.0596 S23: -0.0554 REMARK 3 S31: 0.5363 S32: 0.1446 S33: 0.2120 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'B' AND (RESID 568 THROUGH 613 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.3035 -10.4097 40.7998 REMARK 3 T TENSOR REMARK 3 T11: 0.5212 T22: 0.9258 REMARK 3 T33: 0.7440 T12: 0.1086 REMARK 3 T13: 0.3215 T23: 0.0883 REMARK 3 L TENSOR REMARK 3 L11: 0.4515 L22: 0.8782 REMARK 3 L33: 1.9558 L12: -0.2626 REMARK 3 L13: -0.8225 L23: -0.0916 REMARK 3 S TENSOR REMARK 3 S11: -0.0915 S12: -0.1506 S13: 0.0886 REMARK 3 S21: 0.2037 S22: 0.2229 S23: 0.6567 REMARK 3 S31: 0.1044 S32: -0.9457 S33: 0.0689 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 8 THROUGH 178 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.6247 -39.7042 150.0763 REMARK 3 T TENSOR REMARK 3 T11: 0.6452 T22: 0.6611 REMARK 3 T33: 0.3608 T12: 0.0382 REMARK 3 T13: 0.1641 T23: 0.0943 REMARK 3 L TENSOR REMARK 3 L11: 2.6775 L22: 4.8228 REMARK 3 L33: 4.0785 L12: 1.9045 REMARK 3 L13: -0.0472 L23: -0.7062 REMARK 3 S TENSOR REMARK 3 S11: -0.0275 S12: -0.5396 S13: -0.5463 REMARK 3 S21: 0.4663 S22: -0.6483 S23: -0.1849 REMARK 3 S31: 1.0790 S32: 0.3971 S33: 0.5298 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 179 THROUGH 332 ) REMARK 3 ORIGIN FOR THE GROUP (A): 0.3155 -24.2168 156.5723 REMARK 3 T TENSOR REMARK 3 T11: 0.5667 T22: 1.3914 REMARK 3 T33: 0.5223 T12: -0.1866 REMARK 3 T13: 0.0368 T23: 0.1775 REMARK 3 L TENSOR REMARK 3 L11: 1.6834 L22: 0.0259 REMARK 3 L33: 2.3507 L12: 0.3214 REMARK 3 L13: -2.0787 L23: -0.3630 REMARK 3 S TENSOR REMARK 3 S11: 0.1042 S12: -0.5851 S13: 0.0011 REMARK 3 S21: 0.1367 S22: -0.0354 S23: -0.1556 REMARK 3 S31: -0.4416 S32: 1.3242 S33: -0.0601 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 333 THROUGH 497 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.5265 -9.6124 127.9632 REMARK 3 T TENSOR REMARK 3 T11: 0.4529 T22: 1.3903 REMARK 3 T33: 0.4786 T12: -0.2507 REMARK 3 T13: -0.0922 T23: 0.0684 REMARK 3 L TENSOR REMARK 3 L11: 1.5191 L22: 1.5533 REMARK 3 L33: 2.5549 L12: -0.9693 REMARK 3 L13: -1.0450 L23: 0.3101 REMARK 3 S TENSOR REMARK 3 S11: -0.2855 S12: 0.4191 S13: 0.3575 REMARK 3 S21: 0.2667 S22: 0.0323 S23: -0.1566 REMARK 3 S31: -0.2130 S32: 0.6197 S33: 0.0759 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: CHAIN 'C' AND (RESID 498 THROUGH 586 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.2764 2.8013 159.6052 REMARK 3 T TENSOR REMARK 3 T11: 1.4739 T22: 1.8930 REMARK 3 T33: 1.0632 T12: 0.0463 REMARK 3 T13: -0.2512 T23: -0.2729 REMARK 3 L TENSOR REMARK 3 L11: 0.0022 L22: -0.0035 REMARK 3 L33: 0.0065 L12: 0.0042 REMARK 3 L13: -0.0085 L23: -0.0016 REMARK 3 S TENSOR REMARK 3 S11: -0.2254 S12: -0.6954 S13: 0.3633 REMARK 3 S21: 0.1268 S22: 0.3244 S23: 0.0309 REMARK 3 S31: -0.0598 S32: 0.6136 S33: 0.0213 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 7 THROUGH 221 ) REMARK 3 ORIGIN FOR THE GROUP (A): 30.7059 25.6871 36.8282 REMARK 3 T TENSOR REMARK 3 T11: 0.3247 T22: 0.8171 REMARK 3 T33: 0.6316 T12: 0.2574 REMARK 3 T13: 0.1465 T23: 0.2970 REMARK 3 L TENSOR REMARK 3 L11: 1.3076 L22: 1.1342 REMARK 3 L33: 3.2536 L12: 0.1384 REMARK 3 L13: 0.6319 L23: -0.9054 REMARK 3 S TENSOR REMARK 3 S11: -0.2819 S12: -0.6507 S13: -0.4380 REMARK 3 S21: -0.1212 S22: 0.0089 S23: 0.1367 REMARK 3 S31: 0.4586 S32: 0.4160 S33: 0.1632 REMARK 3 TLS GROUP : 13 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 222 THROUGH 260 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.7848 19.6188 48.9865 REMARK 3 T TENSOR REMARK 3 T11: 0.1825 T22: 0.7783 REMARK 3 T33: 0.5417 T12: 0.0741 REMARK 3 T13: 0.2176 T23: 0.3983 REMARK 3 L TENSOR REMARK 3 L11: 1.8489 L22: 0.4271 REMARK 3 L33: 0.2260 L12: 0.5841 REMARK 3 L13: 0.2218 L23: 0.1452 REMARK 3 S TENSOR REMARK 3 S11: 0.0701 S12: -0.0138 S13: -0.2717 REMARK 3 S21: -0.0348 S22: 0.2394 S23: 0.1928 REMARK 3 S31: -0.0941 S32: -0.9113 S33: 0.0275 REMARK 3 TLS GROUP : 14 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 261 THROUGH 349 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.9415 10.4900 20.2801 REMARK 3 T TENSOR REMARK 3 T11: 0.4861 T22: 1.1504 REMARK 3 T33: 0.5267 T12: -0.0203 REMARK 3 T13: 0.0202 T23: -0.0294 REMARK 3 L TENSOR REMARK 3 L11: 4.4380 L22: 0.3745 REMARK 3 L33: 3.6249 L12: -0.7584 REMARK 3 L13: -4.0050 L23: 0.5983 REMARK 3 S TENSOR REMARK 3 S11: 0.0359 S12: 0.7317 S13: -0.1322 REMARK 3 S21: -0.3104 S22: 0.5292 S23: 0.3107 REMARK 3 S31: 0.1985 S32: -0.2573 S33: -0.4592 REMARK 3 TLS GROUP : 15 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 350 THROUGH 542 ) REMARK 3 ORIGIN FOR THE GROUP (A): 94.6463 12.6001 13.5928 REMARK 3 T TENSOR REMARK 3 T11: 0.4235 T22: 0.7912 REMARK 3 T33: 0.2567 T12: -0.1060 REMARK 3 T13: 0.0677 T23: -0.2122 REMARK 3 L TENSOR REMARK 3 L11: 0.1775 L22: 0.7620 REMARK 3 L33: 2.5493 L12: -0.2607 REMARK 3 L13: 0.0985 L23: 0.8892 REMARK 3 S TENSOR REMARK 3 S11: 0.2860 S12: 0.4674 S13: -0.2213 REMARK 3 S21: -0.1572 S22: 0.1771 S23: -0.0451 REMARK 3 S31: 0.3877 S32: -0.0878 S33: -0.2391 REMARK 3 TLS GROUP : 16 REMARK 3 SELECTION: CHAIN 'D' AND (RESID 543 THROUGH 611 ) REMARK 3 ORIGIN FOR THE GROUP (A): 75.6803 34.7538 52.1807 REMARK 3 T TENSOR REMARK 3 T11: 0.2346 T22: 0.3146 REMARK 3 T33: 0.5557 T12: 0.0398 REMARK 3 T13: 0.3134 T23: 0.0985 REMARK 3 L TENSOR REMARK 3 L11: 1.6587 L22: 1.5971 REMARK 3 L33: 1.4282 L12: 0.5700 REMARK 3 L13: 1.4179 L23: 0.2954 REMARK 3 S TENSOR REMARK 3 S11: -0.0607 S12: -0.0449 S13: 0.3831 REMARK 3 S21: 0.2348 S22: 0.1345 S23: 0.9114 REMARK 3 S31: -0.3115 S32: -0.5444 S33: 0.0691 REMARK 3 TLS GROUP : 17 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 1 THROUGH 13 ) REMARK 3 ORIGIN FOR THE GROUP (A): -11.4554 -3.0541 79.0698 REMARK 3 T TENSOR REMARK 3 T11: 0.6335 T22: 0.3903 REMARK 3 T33: 0.2178 T12: -0.0632 REMARK 3 T13: -0.0481 T23: 0.1655 REMARK 3 L TENSOR REMARK 3 L11: 1.1317 L22: 2.2076 REMARK 3 L33: 0.9244 L12: -0.7222 REMARK 3 L13: -0.2086 L23: 0.3963 REMARK 3 S TENSOR REMARK 3 S11: 0.3776 S12: -0.3928 S13: -0.1346 REMARK 3 S21: 0.7321 S22: -0.1943 S23: -0.4367 REMARK 3 S31: 0.7929 S32: -0.1581 S33: -0.0510 REMARK 3 TLS GROUP : 18 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 14 THROUGH 53 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.6722 2.3762 79.8910 REMARK 3 T TENSOR REMARK 3 T11: 0.4431 T22: 0.3054 REMARK 3 T33: 0.1668 T12: -0.1182 REMARK 3 T13: -0.0410 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 1.6596 L22: 3.5491 REMARK 3 L33: 1.0912 L12: 0.3272 REMARK 3 L13: -0.1021 L23: 0.9874 REMARK 3 S TENSOR REMARK 3 S11: -0.1160 S12: -0.1335 S13: -0.0309 REMARK 3 S21: 0.0858 S22: -0.0915 S23: 0.0438 REMARK 3 S31: 0.9274 S32: -0.6684 S33: 0.0952 REMARK 3 TLS GROUP : 19 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 54 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): -29.4700 3.3958 79.1430 REMARK 3 T TENSOR REMARK 3 T11: 0.3812 T22: 0.5663 REMARK 3 T33: 0.3465 T12: -0.2866 REMARK 3 T13: 0.0286 T23: -0.0972 REMARK 3 L TENSOR REMARK 3 L11: 1.9272 L22: 2.8626 REMARK 3 L33: 4.5446 L12: -0.0425 REMARK 3 L13: 0.7455 L23: 1.6856 REMARK 3 S TENSOR REMARK 3 S11: 0.1137 S12: -0.0462 S13: 0.0698 REMARK 3 S21: 0.1284 S22: -0.2555 S23: 0.6851 REMARK 3 S31: 0.4026 S32: -0.6746 S33: 0.3737 REMARK 3 TLS GROUP : 20 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 67 THROUGH 119 ) REMARK 3 ORIGIN FOR THE GROUP (A): -19.1684 -3.2540 75.0430 REMARK 3 T TENSOR REMARK 3 T11: 0.5350 T22: 0.1559 REMARK 3 T33: 0.2859 T12: -0.1889 REMARK 3 T13: -0.0823 T23: 0.0479 REMARK 3 L TENSOR REMARK 3 L11: 1.5976 L22: 2.7741 REMARK 3 L33: 2.4007 L12: -0.0987 REMARK 3 L13: -0.4781 L23: 1.1953 REMARK 3 S TENSOR REMARK 3 S11: -0.1060 S12: -0.1615 S13: -0.0799 REMARK 3 S21: 0.0779 S22: -0.2848 S23: 0.2405 REMARK 3 S31: 0.9754 S32: -0.4839 S33: 0.1619 REMARK 3 TLS GROUP : 21 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 120 THROUGH 156 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.8934 -11.0319 44.1580 REMARK 3 T TENSOR REMARK 3 T11: 0.2564 T22: 0.1536 REMARK 3 T33: 0.3697 T12: 0.0585 REMARK 3 T13: -0.1287 T23: -0.0938 REMARK 3 L TENSOR REMARK 3 L11: 5.9763 L22: 4.9888 REMARK 3 L33: 5.3773 L12: -1.2064 REMARK 3 L13: -0.1286 L23: -0.6284 REMARK 3 S TENSOR REMARK 3 S11: 0.5488 S12: 0.0110 S13: -0.4158 REMARK 3 S21: 0.2837 S22: 0.1578 S23: -0.4850 REMARK 3 S31: 0.3775 S32: 0.8017 S33: -0.2010 REMARK 3 TLS GROUP : 22 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 157 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): -9.1660 -11.5418 52.4230 REMARK 3 T TENSOR REMARK 3 T11: 0.5698 T22: 0.4731 REMARK 3 T33: 0.4703 T12: -0.0833 REMARK 3 T13: -0.3376 T23: -0.0235 REMARK 3 L TENSOR REMARK 3 L11: 1.9716 L22: 4.3109 REMARK 3 L33: 3.6376 L12: -0.3419 REMARK 3 L13: 0.1710 L23: 1.7426 REMARK 3 S TENSOR REMARK 3 S11: 0.4316 S12: 0.0523 S13: -0.3891 REMARK 3 S21: 0.6901 S22: -0.0909 S23: -0.5079 REMARK 3 S31: 0.6101 S32: 0.5775 S33: -0.4111 REMARK 3 TLS GROUP : 23 REMARK 3 SELECTION: CHAIN 'E' AND (RESID 181 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -4.6189 -15.6559 39.9627 REMARK 3 T TENSOR REMARK 3 T11: 0.5744 T22: 0.5226 REMARK 3 T33: 0.5303 T12: 0.1835 REMARK 3 T13: -0.0313 T23: -0.3627 REMARK 3 L TENSOR REMARK 3 L11: 4.5710 L22: 5.1182 REMARK 3 L33: 4.0425 L12: 0.7982 REMARK 3 L13: -1.0678 L23: 1.2226 REMARK 3 S TENSOR REMARK 3 S11: -0.0245 S12: 0.6248 S13: -0.7236 REMARK 3 S21: -0.2333 S22: 0.3422 S23: -1.1420 REMARK 3 S31: 0.8729 S32: 0.8493 S33: -0.2249 REMARK 3 TLS GROUP : 24 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 1 THROUGH 80 ) REMARK 3 ORIGIN FOR THE GROUP (A): 3.8766 42.9189 57.6655 REMARK 3 T TENSOR REMARK 3 T11: 0.2189 T22: 0.0427 REMARK 3 T33: 0.1206 T12: 0.0735 REMARK 3 T13: 0.0608 T23: -0.0123 REMARK 3 L TENSOR REMARK 3 L11: 1.2332 L22: 1.9235 REMARK 3 L33: 1.1923 L12: -0.4328 REMARK 3 L13: -0.1810 L23: 0.0492 REMARK 3 S TENSOR REMARK 3 S11: 0.0215 S12: 0.0307 S13: 0.0835 REMARK 3 S21: 0.4242 S22: 0.0651 S23: -0.0319 REMARK 3 S31: -0.0306 S32: 0.1176 S33: -0.0143 REMARK 3 TLS GROUP : 25 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 81 THROUGH 134 ) REMARK 3 ORIGIN FOR THE GROUP (A): -0.6711 42.4241 76.6762 REMARK 3 T TENSOR REMARK 3 T11: 0.6244 T22: 0.0972 REMARK 3 T33: 0.0595 T12: -0.0212 REMARK 3 T13: 0.0071 T23: 0.0570 REMARK 3 L TENSOR REMARK 3 L11: 0.3495 L22: 0.0713 REMARK 3 L33: 2.0898 L12: -0.1245 REMARK 3 L13: -0.4566 L23: 0.3643 REMARK 3 S TENSOR REMARK 3 S11: -0.1924 S12: -0.0980 S13: -0.0523 REMARK 3 S21: 0.5245 S22: 0.1805 S23: -0.0448 REMARK 3 S31: 0.1965 S32: 0.2173 S33: -0.0331 REMARK 3 TLS GROUP : 26 REMARK 3 SELECTION: CHAIN 'F' AND (RESID 135 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): -7.8195 37.1131 95.8644 REMARK 3 T TENSOR REMARK 3 T11: 1.6820 T22: 0.1712 REMARK 3 T33: 0.4531 T12: -0.0587 REMARK 3 T13: 0.2645 T23: 0.0691 REMARK 3 L TENSOR REMARK 3 L11: 0.3500 L22: 0.4089 REMARK 3 L33: 0.4674 L12: 0.1867 REMARK 3 L13: -0.3985 L23: -0.0711 REMARK 3 S TENSOR REMARK 3 S11: -0.3000 S12: -0.2586 S13: -0.3080 REMARK 3 S21: 0.8588 S22: -0.0726 S23: 0.0916 REMARK 3 S31: 0.5606 S32: -0.0803 S33: -0.0433 REMARK 3 TLS GROUP : 27 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 1 THROUGH 112 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.0468 15.2719 71.3151 REMARK 3 T TENSOR REMARK 3 T11: 0.2916 T22: 1.0376 REMARK 3 T33: 0.3408 T12: 0.3031 REMARK 3 T13: 0.1424 T23: 0.1847 REMARK 3 L TENSOR REMARK 3 L11: 1.8451 L22: 1.2199 REMARK 3 L33: 2.1343 L12: 0.9505 REMARK 3 L13: -1.2241 L23: 0.3428 REMARK 3 S TENSOR REMARK 3 S11: -0.0177 S12: 0.0062 S13: -0.3678 REMARK 3 S21: -0.0329 S22: -0.2855 S23: -0.4006 REMARK 3 S31: 0.5632 S32: 0.6855 S33: 0.3109 REMARK 3 TLS GROUP : 28 REMARK 3 SELECTION: CHAIN 'G' AND (RESID 113 THROUGH 220 ) REMARK 3 ORIGIN FOR THE GROUP (A): 8.4009 15.4753 106.3823 REMARK 3 T TENSOR REMARK 3 T11: 0.3873 T22: 0.6876 REMARK 3 T33: 0.4313 T12: 0.0197 REMARK 3 T13: 0.1586 T23: 0.0540 REMARK 3 L TENSOR REMARK 3 L11: 1.4127 L22: 5.5638 REMARK 3 L33: 4.5095 L12: 1.2698 REMARK 3 L13: 0.5245 L23: 0.6876 REMARK 3 S TENSOR REMARK 3 S11: -0.0169 S12: -0.0792 S13: 0.2212 REMARK 3 S21: 0.9119 S22: -0.0796 S23: 0.7112 REMARK 3 S31: 0.1754 S32: 0.0251 S33: 0.2018 REMARK 3 TLS GROUP : 29 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 37 ) REMARK 3 ORIGIN FOR THE GROUP (A): 60.2596 72.5463 69.1106 REMARK 3 T TENSOR REMARK 3 T11: 0.3058 T22: 1.5847 REMARK 3 T33: 0.4586 T12: -0.0751 REMARK 3 T13: -0.0131 T23: 0.1864 REMARK 3 L TENSOR REMARK 3 L11: 3.0262 L22: 0.6180 REMARK 3 L33: 0.6704 L12: 0.7277 REMARK 3 L13: -0.5021 L23: -0.1131 REMARK 3 S TENSOR REMARK 3 S11: -0.1438 S12: -0.5075 S13: -0.2598 REMARK 3 S21: 0.1004 S22: -0.1246 S23: -0.1851 REMARK 3 S31: 0.0173 S32: 0.0234 S33: 0.1370 REMARK 3 TLS GROUP : 30 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 38 THROUGH 66 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.9591 68.8590 62.2342 REMARK 3 T TENSOR REMARK 3 T11: 0.4037 T22: 1.1886 REMARK 3 T33: 0.6406 T12: 0.0538 REMARK 3 T13: 0.0894 T23: 0.3710 REMARK 3 L TENSOR REMARK 3 L11: 3.9398 L22: 2.0664 REMARK 3 L33: 2.8569 L12: 0.4433 REMARK 3 L13: 0.4389 L23: -1.8426 REMARK 3 S TENSOR REMARK 3 S11: -0.2723 S12: -0.5146 S13: -0.6600 REMARK 3 S21: -0.0433 S22: -0.1176 S23: 0.0256 REMARK 3 S31: 0.5460 S32: 0.6012 S33: 0.3540 REMARK 3 TLS GROUP : 31 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 67 THROUGH 121 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.9358 66.8079 60.7466 REMARK 3 T TENSOR REMARK 3 T11: 0.3802 T22: 1.1649 REMARK 3 T33: 0.7110 T12: 0.2549 REMARK 3 T13: 0.1423 T23: 0.1944 REMARK 3 L TENSOR REMARK 3 L11: 1.9124 L22: 0.4914 REMARK 3 L33: 3.1390 L12: 0.2020 REMARK 3 L13: -1.6041 L23: -0.9619 REMARK 3 S TENSOR REMARK 3 S11: -0.3809 S12: -0.4378 S13: -0.7762 REMARK 3 S21: -0.1097 S22: -0.4112 S23: -0.2385 REMARK 3 S31: 0.9726 S32: 1.0043 S33: 0.5123 REMARK 3 TLS GROUP : 32 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 122 THROUGH 151 ) REMARK 3 ORIGIN FOR THE GROUP (A): 69.8011 65.1766 29.7645 REMARK 3 T TENSOR REMARK 3 T11: 0.5262 T22: 0.7631 REMARK 3 T33: 0.9457 T12: 0.1727 REMARK 3 T13: 0.2110 T23: -0.0107 REMARK 3 L TENSOR REMARK 3 L11: 3.2791 L22: 1.9456 REMARK 3 L33: 7.6200 L12: 1.1215 REMARK 3 L13: -2.8674 L23: -1.0661 REMARK 3 S TENSOR REMARK 3 S11: -0.1747 S12: 0.0527 S13: -0.1822 REMARK 3 S21: -0.0409 S22: 0.0341 S23: -0.5538 REMARK 3 S31: 0.6537 S32: 0.1039 S33: 0.3039 REMARK 3 TLS GROUP : 33 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 152 THROUGH 180 ) REMARK 3 ORIGIN FOR THE GROUP (A): 72.5097 63.6468 36.4099 REMARK 3 T TENSOR REMARK 3 T11: 0.8193 T22: 0.9763 REMARK 3 T33: 1.1042 T12: 0.3294 REMARK 3 T13: 0.0904 T23: 0.3378 REMARK 3 L TENSOR REMARK 3 L11: 0.3578 L22: 1.4356 REMARK 3 L33: 1.3680 L12: -0.7163 REMARK 3 L13: -0.6874 L23: 1.3922 REMARK 3 S TENSOR REMARK 3 S11: -0.1745 S12: -0.0812 S13: 0.2460 REMARK 3 S21: -0.5001 S22: -0.4774 S23: -0.4040 REMARK 3 S31: 0.7109 S32: 0.7457 S33: 0.5529 REMARK 3 TLS GROUP : 34 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 181 THROUGH 218 ) REMARK 3 ORIGIN FOR THE GROUP (A): 76.2399 62.1145 26.1852 REMARK 3 T TENSOR REMARK 3 T11: 1.3744 T22: 1.2108 REMARK 3 T33: 1.0069 T12: 0.4408 REMARK 3 T13: 0.5903 T23: 0.3016 REMARK 3 L TENSOR REMARK 3 L11: 1.4666 L22: 0.8817 REMARK 3 L33: 2.2836 L12: 0.4288 REMARK 3 L13: 0.9342 L23: 0.3127 REMARK 3 S TENSOR REMARK 3 S11: -0.5371 S12: -0.1067 S13: -0.2963 REMARK 3 S21: -0.5939 S22: -0.0904 S23: -0.2415 REMARK 3 S31: 2.4794 S32: 0.3978 S33: 0.4129 REMARK 3 TLS GROUP : 35 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 221 THROUGH 304 ) REMARK 3 ORIGIN FOR THE GROUP (A): -5.0078 64.8211 63.0240 REMARK 3 T TENSOR REMARK 3 T11: 0.2039 T22: 0.1171 REMARK 3 T33: 0.1974 T12: 0.0293 REMARK 3 T13: 0.0735 T23: -0.0349 REMARK 3 L TENSOR REMARK 3 L11: 2.5906 L22: 2.4327 REMARK 3 L33: 2.8215 L12: 0.1230 REMARK 3 L13: -0.8289 L23: 0.3122 REMARK 3 S TENSOR REMARK 3 S11: 0.0284 S12: -0.1692 S13: 0.3502 REMARK 3 S21: 0.3316 S22: 0.0671 S23: 0.0296 REMARK 3 S31: -0.4155 S32: -0.2697 S33: 0.0115 REMARK 3 TLS GROUP : 36 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 305 THROUGH 346 ) REMARK 3 ORIGIN FOR THE GROUP (A): -6.1557 58.5925 68.2953 REMARK 3 T TENSOR REMARK 3 T11: 0.3022 T22: 0.1613 REMARK 3 T33: 0.3073 T12: 0.0653 REMARK 3 T13: 0.1132 T23: -0.0461 REMARK 3 L TENSOR REMARK 3 L11: 0.5788 L22: 1.1602 REMARK 3 L33: 2.7453 L12: 0.2982 REMARK 3 L13: -0.3190 L23: 0.4746 REMARK 3 S TENSOR REMARK 3 S11: 0.0650 S12: -0.1852 S13: -0.0579 REMARK 3 S21: 0.2437 S22: -0.1465 S23: 0.1643 REMARK 3 S31: 0.0985 S32: -0.4305 S33: 0.0293 REMARK 3 TLS GROUP : 37 REMARK 3 SELECTION: CHAIN 'I' AND (RESID 347 THROUGH 443 ) REMARK 3 ORIGIN FOR THE GROUP (A): -1.6566 52.9786 94.2193 REMARK 3 T TENSOR REMARK 3 T11: 1.0668 T22: -0.0037 REMARK 3 T33: 0.1607 T12: -0.0150 REMARK 3 T13: 0.1266 T23: -0.3357 REMARK 3 L TENSOR REMARK 3 L11: 0.2692 L22: 1.2161 REMARK 3 L33: 0.5495 L12: -0.1088 REMARK 3 L13: -0.1662 L23: 0.7104 REMARK 3 S TENSOR REMARK 3 S11: -0.0421 S12: -0.2388 S13: 0.1589 REMARK 3 S21: 0.3595 S22: 0.1717 S23: -0.2507 REMARK 3 S31: -0.0386 S32: 0.1519 S33: -0.3450 REMARK 3 TLS GROUP : 38 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 221 THROUGH 304 ) REMARK 3 ORIGIN FOR THE GROUP (A): -12.9161 21.3983 69.8065 REMARK 3 T TENSOR REMARK 3 T11: 0.2942 T22: 0.1168 REMARK 3 T33: 0.3620 T12: -0.0125 REMARK 3 T13: 0.0546 T23: 0.0336 REMARK 3 L TENSOR REMARK 3 L11: 2.8213 L22: 1.9227 REMARK 3 L33: 2.5910 L12: -0.2870 REMARK 3 L13: 0.3852 L23: -0.2644 REMARK 3 S TENSOR REMARK 3 S11: -0.0559 S12: 0.0427 S13: 0.3861 REMARK 3 S21: 0.0533 S22: 0.0312 S23: 0.0015 REMARK 3 S31: -0.5575 S32: 0.0267 S33: 0.0899 REMARK 3 TLS GROUP : 39 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 305 THROUGH 347 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9835 13.9811 65.7826 REMARK 3 T TENSOR REMARK 3 T11: 0.1130 T22: 0.1555 REMARK 3 T33: 0.3454 T12: 0.0312 REMARK 3 T13: 0.0225 T23: 0.0988 REMARK 3 L TENSOR REMARK 3 L11: 0.4759 L22: 1.0895 REMARK 3 L33: 3.6137 L12: -0.1120 REMARK 3 L13: -0.5096 L23: 1.1613 REMARK 3 S TENSOR REMARK 3 S11: 0.1024 S12: 0.2526 S13: 0.1136 REMARK 3 S21: 0.0807 S22: -0.1376 S23: -0.2222 REMARK 3 S31: -0.0920 S32: -0.0377 S33: 0.0651 REMARK 3 TLS GROUP : 40 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 348 THROUGH 361 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.9711 -9.5735 35.6606 REMARK 3 T TENSOR REMARK 3 T11: 0.4973 T22: 0.5927 REMARK 3 T33: 0.6001 T12: -0.0737 REMARK 3 T13: -0.0564 T23: -0.2249 REMARK 3 L TENSOR REMARK 3 L11: 1.0034 L22: 0.1717 REMARK 3 L33: 2.5233 L12: 0.0285 REMARK 3 L13: -1.5073 L23: -0.2541 REMARK 3 S TENSOR REMARK 3 S11: -0.1905 S12: 1.6281 S13: -1.0761 REMARK 3 S21: -0.5240 S22: 0.5617 S23: -0.6189 REMARK 3 S31: 0.9697 S32: -0.4266 S33: -0.3646 REMARK 3 TLS GROUP : 41 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 362 THROUGH 404 ) REMARK 3 ORIGIN FOR THE GROUP (A): -10.9606 1.7455 47.7156 REMARK 3 T TENSOR REMARK 3 T11: 0.1308 T22: 0.2193 REMARK 3 T33: 0.4167 T12: 0.0738 REMARK 3 T13: 0.0046 T23: 0.0624 REMARK 3 L TENSOR REMARK 3 L11: 0.1814 L22: 2.2469 REMARK 3 L33: 2.9475 L12: -0.6367 REMARK 3 L13: -0.2719 L23: 0.8610 REMARK 3 S TENSOR REMARK 3 S11: -0.0653 S12: 0.3710 S13: 0.5061 REMARK 3 S21: -0.1023 S22: -0.1306 S23: 0.2977 REMARK 3 S31: 0.1065 S32: 0.2152 S33: 0.1742 REMARK 3 TLS GROUP : 42 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 405 THROUGH 421 ) REMARK 3 ORIGIN FOR THE GROUP (A): -22.5871 -4.3552 39.2060 REMARK 3 T TENSOR REMARK 3 T11: 0.2269 T22: 0.3849 REMARK 3 T33: 0.5316 T12: -0.0917 REMARK 3 T13: -0.1954 T23: -0.0774 REMARK 3 L TENSOR REMARK 3 L11: 2.3389 L22: 1.6444 REMARK 3 L33: 5.2447 L12: -1.1738 REMARK 3 L13: -0.0511 L23: -1.8065 REMARK 3 S TENSOR REMARK 3 S11: -0.0553 S12: 0.6249 S13: -0.1186 REMARK 3 S21: -0.6685 S22: -0.1276 S23: 0.9899 REMARK 3 S31: 0.4170 S32: -0.9222 S33: -0.0048 REMARK 3 TLS GROUP : 43 REMARK 3 SELECTION: CHAIN 'J' AND (RESID 422 THROUGH 443 ) REMARK 3 ORIGIN FOR THE GROUP (A): -13.8037 6.2717 39.2429 REMARK 3 T TENSOR REMARK 3 T11: 0.3498 T22: 0.3676 REMARK 3 T33: 0.4776 T12: 0.1295 REMARK 3 T13: -0.0137 T23: 0.0232 REMARK 3 L TENSOR REMARK 3 L11: 4.4893 L22: 6.6409 REMARK 3 L33: 9.4094 L12: 5.1336 REMARK 3 L13: 5.8321 L23: 5.5917 REMARK 3 S TENSOR REMARK 3 S11: 0.0595 S12: 0.7176 S13: 0.2558 REMARK 3 S21: -0.3921 S22: 0.2740 S23: 0.5484 REMARK 3 S31: -0.1511 S32: 0.0635 S33: -0.2872 REMARK 3 TLS GROUP : 44 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 221 THROUGH 254 ) REMARK 3 ORIGIN FOR THE GROUP (A): 35.7882 35.8327 82.1836 REMARK 3 T TENSOR REMARK 3 T11: 0.7880 T22: 1.5227 REMARK 3 T33: 0.5634 T12: -0.3955 REMARK 3 T13: -0.3814 T23: 0.1660 REMARK 3 L TENSOR REMARK 3 L11: 0.5168 L22: 0.2457 REMARK 3 L33: 0.9338 L12: 0.1824 REMARK 3 L13: 0.4057 L23: 0.1774 REMARK 3 S TENSOR REMARK 3 S11: -0.2607 S12: 0.1782 S13: 0.3001 REMARK 3 S21: 0.1356 S22: -0.1159 S23: -0.3662 REMARK 3 S31: -0.4051 S32: 0.8347 S33: 0.1907 REMARK 3 TLS GROUP : 45 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 255 THROUGH 274 ) REMARK 3 ORIGIN FOR THE GROUP (A): 26.9225 31.5944 76.5609 REMARK 3 T TENSOR REMARK 3 T11: 0.4621 T22: 1.0136 REMARK 3 T33: 0.3538 T12: -0.2866 REMARK 3 T13: -0.1797 T23: 0.0139 REMARK 3 L TENSOR REMARK 3 L11: 1.9633 L22: 1.8921 REMARK 3 L33: 5.4128 L12: -0.2562 REMARK 3 L13: 2.7756 L23: 0.7814 REMARK 3 S TENSOR REMARK 3 S11: -0.1768 S12: 0.2063 S13: 0.3760 REMARK 3 S21: -0.0188 S22: -0.2418 S23: -0.0167 REMARK 3 S31: -0.3578 S32: 0.3838 S33: 0.2948 REMARK 3 TLS GROUP : 46 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 275 THROUGH 347 ) REMARK 3 ORIGIN FOR THE GROUP (A): 29.9352 35.4643 78.9159 REMARK 3 T TENSOR REMARK 3 T11: 0.6240 T22: 1.2168 REMARK 3 T33: 0.4913 T12: -0.3579 REMARK 3 T13: -0.3338 T23: 0.1131 REMARK 3 L TENSOR REMARK 3 L11: 0.2964 L22: 0.7825 REMARK 3 L33: 1.7201 L12: -0.2515 REMARK 3 L13: 0.6238 L23: 0.0012 REMARK 3 S TENSOR REMARK 3 S11: -0.3064 S12: -0.1308 S13: 0.4524 REMARK 3 S21: 0.2212 S22: -0.2598 S23: -0.4900 REMARK 3 S31: -0.7655 S32: 1.0346 S33: 0.3568 REMARK 3 TLS GROUP : 47 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 348 THROUGH 361 ) REMARK 3 ORIGIN FOR THE GROUP (A): 17.7958 13.1925 114.0675 REMARK 3 T TENSOR REMARK 3 T11: 1.0712 T22: 1.3917 REMARK 3 T33: 0.8394 T12: 0.4337 REMARK 3 T13: 0.1524 T23: 0.2421 REMARK 3 L TENSOR REMARK 3 L11: 7.4295 L22: 2.9867 REMARK 3 L33: 5.4148 L12: -1.7055 REMARK 3 L13: 1.3298 L23: -2.5470 REMARK 3 S TENSOR REMARK 3 S11: -0.3641 S12: -1.7576 S13: -1.8474 REMARK 3 S21: 1.1931 S22: 0.3239 S23: 0.4455 REMARK 3 S31: 0.9522 S32: 0.4007 S33: 0.0923 REMARK 3 TLS GROUP : 48 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 362 THROUGH 427 ) REMARK 3 ORIGIN FOR THE GROUP (A): 22.8030 21.2742 104.8002 REMARK 3 T TENSOR REMARK 3 T11: 0.5637 T22: 0.8719 REMARK 3 T33: 0.3081 T12: 0.0763 REMARK 3 T13: -0.1042 T23: 0.0732 REMARK 3 L TENSOR REMARK 3 L11: 5.2527 L22: 6.5306 REMARK 3 L33: 6.2275 L12: -0.1568 REMARK 3 L13: 3.0470 L23: -0.5340 REMARK 3 S TENSOR REMARK 3 S11: -0.0840 S12: -0.4244 S13: -0.2706 REMARK 3 S21: 0.6022 S22: -0.2385 S23: -0.7855 REMARK 3 S31: -0.1362 S32: 1.1229 S33: 0.2468 REMARK 3 TLS GROUP : 49 REMARK 3 SELECTION: CHAIN 'K' AND (RESID 428 THROUGH 443 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.8031 26.0091 112.1196 REMARK 3 T TENSOR REMARK 3 T11: 0.6720 T22: 1.3314 REMARK 3 T33: 0.6029 T12: 0.1952 REMARK 3 T13: -0.2705 T23: 0.0069 REMARK 3 L TENSOR REMARK 3 L11: 1.5989 L22: 6.1514 REMARK 3 L33: 6.3805 L12: -1.6727 REMARK 3 L13: 3.1907 L23: -3.1377 REMARK 3 S TENSOR REMARK 3 S11: -0.5103 S12: -0.0780 S13: -0.1442 REMARK 3 S21: 0.8208 S22: 0.8593 S23: -0.1125 REMARK 3 S31: -0.5871 S32: -0.2371 S33: -0.3145 REMARK 3 TLS GROUP : 50 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 221 THROUGH 237 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.2199 87.9891 44.5181 REMARK 3 T TENSOR REMARK 3 T11: 0.2865 T22: 0.5681 REMARK 3 T33: 0.3607 T12: -0.0439 REMARK 3 T13: 0.0311 T23: -0.0992 REMARK 3 L TENSOR REMARK 3 L11: 8.8874 L22: 7.1457 REMARK 3 L33: 6.3015 L12: 4.5903 REMARK 3 L13: -5.2428 L23: -3.1147 REMARK 3 S TENSOR REMARK 3 S11: 0.5306 S12: 0.0296 S13: 0.4576 REMARK 3 S21: 0.0003 S22: 0.3534 S23: -0.4894 REMARK 3 S31: -0.6894 S32: 0.5659 S33: -0.6146 REMARK 3 TLS GROUP : 51 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 238 THROUGH 312 ) REMARK 3 ORIGIN FOR THE GROUP (A): 47.8357 89.8641 55.1107 REMARK 3 T TENSOR REMARK 3 T11: 0.2936 T22: 0.7814 REMARK 3 T33: 0.4933 T12: -0.0864 REMARK 3 T13: 0.0663 T23: -0.1972 REMARK 3 L TENSOR REMARK 3 L11: 7.1679 L22: 2.2531 REMARK 3 L33: 1.5518 L12: 0.2401 REMARK 3 L13: -1.6679 L23: -0.4871 REMARK 3 S TENSOR REMARK 3 S11: 0.2424 S12: -1.0475 S13: 0.9230 REMARK 3 S21: 0.0665 S22: 0.0697 S23: -0.0283 REMARK 3 S31: -0.7313 S32: 0.4368 S33: -0.2924 REMARK 3 TLS GROUP : 52 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 313 THROUGH 346 ) REMARK 3 ORIGIN FOR THE GROUP (A): 50.9922 82.0464 51.0851 REMARK 3 T TENSOR REMARK 3 T11: 0.0988 T22: 0.5783 REMARK 3 T33: 0.3473 T12: -0.0403 REMARK 3 T13: -0.0421 T23: 0.0435 REMARK 3 L TENSOR REMARK 3 L11: 5.0432 L22: 1.7926 REMARK 3 L33: 6.7390 L12: -0.8891 REMARK 3 L13: -2.8269 L23: 0.4151 REMARK 3 S TENSOR REMARK 3 S11: 0.4089 S12: -0.3762 S13: -0.1127 REMARK 3 S21: -0.0929 S22: 0.0191 S23: -0.3207 REMARK 3 S31: -0.3300 S32: -0.0640 S33: -0.3397 REMARK 3 TLS GROUP : 53 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 347 THROUGH 362 ) REMARK 3 ORIGIN FOR THE GROUP (A): 62.7281 60.1979 23.7923 REMARK 3 T TENSOR REMARK 3 T11: 1.2812 T22: 0.9858 REMARK 3 T33: 1.9369 T12: -0.1357 REMARK 3 T13: 0.7691 T23: -0.3296 REMARK 3 L TENSOR REMARK 3 L11: 2.2046 L22: 2.3721 REMARK 3 L33: 4.1886 L12: -1.4585 REMARK 3 L13: 0.2296 L23: 2.2712 REMARK 3 S TENSOR REMARK 3 S11: -0.7991 S12: 0.3616 S13: -2.2139 REMARK 3 S21: -0.7121 S22: 0.3745 S23: -1.0379 REMARK 3 S31: 1.7352 S32: 0.0551 S33: 0.4171 REMARK 3 TLS GROUP : 54 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 363 THROUGH 402 ) REMARK 3 ORIGIN FOR THE GROUP (A): 59.7287 72.2510 33.2178 REMARK 3 T TENSOR REMARK 3 T11: 0.4394 T22: 0.8116 REMARK 3 T33: 0.8177 T12: -0.0645 REMARK 3 T13: 0.3985 T23: -0.1401 REMARK 3 L TENSOR REMARK 3 L11: 4.2562 L22: 0.9000 REMARK 3 L33: 2.7501 L12: 1.3735 REMARK 3 L13: 0.2913 L23: -0.1656 REMARK 3 S TENSOR REMARK 3 S11: -0.6074 S12: 0.0644 S13: -0.9276 REMARK 3 S21: -0.0162 S22: -0.4277 S23: 0.4424 REMARK 3 S31: 0.7931 S32: -0.1638 S33: 0.1229 REMARK 3 TLS GROUP : 55 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 403 THROUGH 439 ) REMARK 3 ORIGIN FOR THE GROUP (A): 54.6842 68.5655 27.3589 REMARK 3 T TENSOR REMARK 3 T11: 0.6268 T22: 1.4224 REMARK 3 T33: 1.2121 T12: -0.2564 REMARK 3 T13: 0.2048 T23: -0.5203 REMARK 3 L TENSOR REMARK 3 L11: 2.7289 L22: 0.2805 REMARK 3 L33: 5.3866 L12: 0.2180 REMARK 3 L13: -1.0222 L23: -1.2278 REMARK 3 S TENSOR REMARK 3 S11: -0.5725 S12: 0.6963 S13: -0.9784 REMARK 3 S21: -0.5330 S22: -0.3568 S23: 0.7125 REMARK 3 S31: 1.1402 S32: -1.5853 S33: 0.8987 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 9I1Q COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 16-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1292144613. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 29-NOV-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : ELETTRA REMARK 200 BEAMLINE : 11.2C REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC REMARK 200 DATA SCALING SOFTWARE : AUTOPROC REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 82868 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.550 REMARK 200 RESOLUTION RANGE LOW (A) : 96.760 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 87.6 REMARK 200 DATA REDUNDANCY : 6.500 REMARK 200 R MERGE (I) : 0.12000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 12.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.55 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.94 REMARK 200 COMPLETENESS FOR SHELL (%) : 63.7 REMARK 200 DATA REDUNDANCY IN SHELL : 6.40 REMARK 200 R MERGE FOR SHELL (I) : 1.02900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 1.900 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHASER REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 55.81 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M KSCN, 0.1 M BIS-TRIS PROPANE PH REMARK 280 8.5, 14% PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE REMARK 280 293.15K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,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 49.40500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 15490 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 75900 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 5.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C, M, N, P 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: E, J REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 -43.27526 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 -49.40500 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 266.89435 REMARK 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 9010 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 60670 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 33.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, Q 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: B, O REMARK 350 BIOMT1 2 -1.000000 0.000000 0.000000 98.03000 REMARK 350 BIOMT2 2 0.000000 1.000000 0.000000 49.40500 REMARK 350 BIOMT3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 350 REMARK 350 BIOMOLECULE: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3900 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19700 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -32.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: F, I 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 REMARK 350 BIOMOLECULE: 4 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3960 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19780 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: G, K 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 REMARK 350 BIOMOLECULE: 5 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 20110 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 SER A 1 REMARK 465 GLU A 2 REMARK 465 VAL A 3 REMARK 465 GLY A 4 REMARK 465 ASN A 5 REMARK 465 SER A 6 REMARK 465 GLN A 7 REMARK 465 GLY A 16 REMARK 465 LEU A 17 REMARK 465 SER A 18 REMARK 465 VAL A 19 REMARK 465 THR A 20 REMARK 465 GLY A 21 REMARK 465 ASP A 22 REMARK 465 ALA A 23 REMARK 465 GLU A 24 REMARK 465 ASN A 25 REMARK 465 GLN A 26 REMARK 465 TYR A 27 REMARK 465 GLN A 28 REMARK 465 THR A 29 REMARK 465 LEU A 30 REMARK 465 TYR A 31 REMARK 465 LYS A 32 REMARK 465 GLY A 612 REMARK 465 GLN A 613 REMARK 465 THR A 614 REMARK 465 LEU A 615 REMARK 465 VAL A 616 REMARK 465 LEU A 617 REMARK 465 ILE A 618 REMARK 465 GLY A 619 REMARK 465 LYS A 620 REMARK 465 THR A 621 REMARK 465 HIS A 622 REMARK 465 LEU A 623 REMARK 465 THR A 624 REMARK 465 VAL A 625 REMARK 465 ASP A 626 REMARK 465 HIS A 627 REMARK 465 HIS A 628 REMARK 465 HIS A 629 REMARK 465 HIS A 630 REMARK 465 HIS A 631 REMARK 465 HIS A 632 REMARK 465 SER B 1 REMARK 465 GLU B 2 REMARK 465 VAL B 3 REMARK 465 GLY B 4 REMARK 465 ASN B 5 REMARK 465 SER B 6 REMARK 465 LEU B 14 REMARK 465 ASN B 15 REMARK 465 GLY B 16 REMARK 465 LEU B 17 REMARK 465 SER B 18 REMARK 465 VAL B 19 REMARK 465 THR B 20 REMARK 465 GLY B 21 REMARK 465 ASP B 22 REMARK 465 ALA B 23 REMARK 465 GLU B 24 REMARK 465 ASN B 25 REMARK 465 GLN B 26 REMARK 465 TYR B 27 REMARK 465 GLN B 28 REMARK 465 THR B 29 REMARK 465 ARG B 456 REMARK 465 GLY B 457 REMARK 465 PRO B 458 REMARK 465 THR B 614 REMARK 465 LEU B 615 REMARK 465 VAL B 616 REMARK 465 LEU B 617 REMARK 465 ILE B 618 REMARK 465 GLY B 619 REMARK 465 LYS B 620 REMARK 465 THR B 621 REMARK 465 HIS B 622 REMARK 465 LEU B 623 REMARK 465 THR B 624 REMARK 465 VAL B 625 REMARK 465 ASP B 626 REMARK 465 HIS B 627 REMARK 465 HIS B 628 REMARK 465 HIS B 629 REMARK 465 HIS B 630 REMARK 465 HIS B 631 REMARK 465 HIS B 632 REMARK 465 SER C 1 REMARK 465 GLU C 2 REMARK 465 VAL C 3 REMARK 465 GLY C 4 REMARK 465 ASN C 5 REMARK 465 SER C 6 REMARK 465 GLN C 7 REMARK 465 LEU C 14 REMARK 465 ASN C 15 REMARK 465 GLY C 16 REMARK 465 LEU C 17 REMARK 465 SER C 18 REMARK 465 VAL C 19 REMARK 465 THR C 20 REMARK 465 GLY C 21 REMARK 465 ASP C 22 REMARK 465 ALA C 23 REMARK 465 GLU C 24 REMARK 465 ASN C 25 REMARK 465 GLN C 26 REMARK 465 TYR C 27 REMARK 465 GLN C 28 REMARK 465 THR C 29 REMARK 465 LEU C 30 REMARK 465 GLY C 519 REMARK 465 GLU C 520 REMARK 465 PRO C 521 REMARK 465 ARG C 522 REMARK 465 GLN C 556 REMARK 465 CYS C 557 REMARK 465 ALA C 558 REMARK 465 HIS C 559 REMARK 465 PHE C 560 REMARK 465 ARG C 561 REMARK 465 ASP C 562 REMARK 465 GLY C 563 REMARK 465 PRO C 564 REMARK 465 HIS C 565 REMARK 465 CYS C 566 REMARK 465 VAL C 567 REMARK 465 SER C 568 REMARK 465 SER C 569 REMARK 465 CYS C 570 REMARK 465 PRO C 571 REMARK 465 HIS C 572 REMARK 465 GLY C 573 REMARK 465 VAL C 574 REMARK 465 LEU C 575 REMARK 465 GLY C 576 REMARK 465 ALA C 577 REMARK 465 LYS C 578 REMARK 465 GLY C 579 REMARK 465 PRO C 580 REMARK 465 ILE C 581 REMARK 465 TYR C 582 REMARK 465 VAL C 587 REMARK 465 GLN C 588 REMARK 465 ASN C 589 REMARK 465 GLU C 590 REMARK 465 CYS C 591 REMARK 465 ARG C 592 REMARK 465 PRO C 593 REMARK 465 CYS C 594 REMARK 465 HIS C 595 REMARK 465 GLU C 596 REMARK 465 ASN C 597 REMARK 465 CYS C 598 REMARK 465 THR C 599 REMARK 465 GLN C 600 REMARK 465 GLY C 601 REMARK 465 CYS C 602 REMARK 465 LYS C 603 REMARK 465 GLY C 604 REMARK 465 PRO C 605 REMARK 465 GLU C 606 REMARK 465 LEU C 607 REMARK 465 GLN C 608 REMARK 465 ASP C 609 REMARK 465 CYS C 610 REMARK 465 LEU C 611 REMARK 465 GLY C 612 REMARK 465 GLN C 613 REMARK 465 THR C 614 REMARK 465 LEU C 615 REMARK 465 VAL C 616 REMARK 465 LEU C 617 REMARK 465 ILE C 618 REMARK 465 GLY C 619 REMARK 465 LYS C 620 REMARK 465 THR C 621 REMARK 465 HIS C 622 REMARK 465 LEU C 623 REMARK 465 THR C 624 REMARK 465 VAL C 625 REMARK 465 ASP C 626 REMARK 465 HIS C 627 REMARK 465 HIS C 628 REMARK 465 HIS C 629 REMARK 465 HIS C 630 REMARK 465 HIS C 631 REMARK 465 HIS C 632 REMARK 465 SER D 1 REMARK 465 GLU D 2 REMARK 465 VAL D 3 REMARK 465 GLY D 4 REMARK 465 ASN D 5 REMARK 465 SER D 6 REMARK 465 GLY D 16 REMARK 465 LEU D 17 REMARK 465 SER D 18 REMARK 465 VAL D 19 REMARK 465 THR D 20 REMARK 465 GLY D 21 REMARK 465 ASP D 22 REMARK 465 ALA D 23 REMARK 465 GLU D 24 REMARK 465 ASN D 25 REMARK 465 GLN D 26 REMARK 465 TYR D 27 REMARK 465 GLN D 28 REMARK 465 GLY D 612 REMARK 465 GLN D 613 REMARK 465 THR D 614 REMARK 465 LEU D 615 REMARK 465 VAL D 616 REMARK 465 LEU D 617 REMARK 465 ILE D 618 REMARK 465 GLY D 619 REMARK 465 LYS D 620 REMARK 465 THR D 621 REMARK 465 HIS D 622 REMARK 465 LEU D 623 REMARK 465 THR D 624 REMARK 465 VAL D 625 REMARK 465 ASP D 626 REMARK 465 HIS D 627 REMARK 465 HIS D 628 REMARK 465 HIS D 629 REMARK 465 HIS D 630 REMARK 465 HIS D 631 REMARK 465 HIS D 632 REMARK 465 GLU H 219 REMARK 465 CYS H 220 REMARK 465 SER I 357 REMARK 465 THR I 358 REMARK 465 PRO L 440 REMARK 465 LYS L 441 REMARK 465 SER L 442 REMARK 465 CYS L 443 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 ASN A 296 CB CG OD1 ND2 REMARK 470 LEU C 33 CG CD1 CD2 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 GLU A 74 OE1 OE2 REMARK 480 SER A 76 OG REMARK 480 ARG A 84 NH1 NH2 REMARK 480 ASN A 107 CG OD1 ND2 REMARK 480 SER A 109 OG REMARK 480 ARG A 116 NH1 NH2 REMARK 480 GLN A 119 OE1 NE2 REMARK 480 LYS A 135 CE NZ REMARK 480 ARG A 149 NE CZ NH1 NH2 REMARK 480 ARG A 151 CG CD NE CZ NH1 NH2 REMARK 480 SER A 163 OG REMARK 480 GLU A 169 CG CD OE1 OE2 REMARK 480 LYS A 172 CD CE NZ REMARK 480 GLU A 181 OE1 OE2 REMARK 480 LYS A 188 CB CG CD CE NZ REMARK 480 THR A 189 OG1 CG2 REMARK 480 ILE A 190 O CG1 CG2 CD1 REMARK 480 ASN A 205 ND2 REMARK 480 ASP A 210 CG OD1 OD2 REMARK 480 ARG A 239 CD NE CZ NH1 NH2 REMARK 480 GLN A 242 CG CD OE1 NE2 REMARK 480 LYS A 248 NZ REMARK 480 LYS A 260 NZ REMARK 480 TYR A 263 OH REMARK 480 HIS A 273 N CB CG ND1 CD2 CE1 NE2 REMARK 480 ASN A 274 CG OD1 ND2 REMARK 480 GLN A 279 CG CD OE1 NE2 REMARK 480 ARG A 284 CG CD NE CZ NH1 NH2 REMARK 480 ASP A 289 CB CG OD1 OD2 REMARK 480 LYS A 290 CE NZ REMARK 480 ASP A 294 N CA CB CG OD1 OD2 REMARK 480 LYS A 295 CD CE NZ REMARK 480 LYS A 299 CE NZ REMARK 480 LYS A 310 NZ REMARK 480 GLU A 313 CD OE1 OE2 REMARK 480 GLN A 322 CD OE1 NE2 REMARK 480 ILE A 346 CG1 CD1 REMARK 480 TRP A 354 CE3 CZ2 CZ3 CH2 REMARK 480 ILE A 357 CD1 REMARK 480 GLU A 363 CG CD OE1 OE2 REMARK 480 ARG A 372 NE CZ NH1 NH2 REMARK 480 ARG A 407 CD NE CZ NH1 NH2 REMARK 480 LYS A 415 CD CE NZ REMARK 480 ARG A 425 CZ NH1 NH2 REMARK 480 LYS A 428 CD CE NZ REMARK 480 ARG A 441 NE CZ NH1 NH2 REMARK 480 GLN A 442 OE1 NE2 REMARK 480 SER A 448 OG REMARK 480 LYS A 453 CG CD CE NZ REMARK 480 GLU A 460 CG CD OE1 OE2 REMARK 480 GLU A 461 CG CD OE1 OE2 REMARK 480 LYS A 466 CE NZ REMARK 480 ARG A 472 CG CD NE CZ NH1 NH2 REMARK 480 LEU A 484 CD1 CD2 REMARK 480 ARG A 502 NH1 NH2 REMARK 480 GLU A 520 O CG CD OE1 OE2 REMARK 480 GLU A 527 CG CD OE1 OE2 REMARK 480 GLU A 529 CD OE1 OE2 REMARK 480 GLU A 536 OE1 OE2 REMARK 480 GLU A 541 CG CD OE1 OE2 REMARK 480 ARG A 561 CZ NH1 NH2 REMARK 480 HIS A 572 CG ND1 CD2 CE1 NE2 REMARK 480 LYS A 578 CG CD CE NZ REMARK 480 VAL A 587 CA CB CG1 CG2 REMARK 480 GLN A 588 CD OE1 NE2 REMARK 480 GLN A 600 CG CD OE1 NE2 REMARK 480 LYS A 603 CG CD CE NZ REMARK 480 GLU A 606 CD OE1 OE2 REMARK 480 LEU A 611 CD1 CD2 REMARK 480 LYS B 32 CG CD CE NZ REMARK 480 LEU B 33 CD1 CD2 REMARK 480 ARG B 36 CD NE CZ NH1 NH2 REMARK 480 MET B 41 SD CE REMARK 480 GLU B 74 OE1 OE2 REMARK 480 SER B 76 OG REMARK 480 ARG B 84 NH1 NH2 REMARK 480 ASN B 107 CG OD1 ND2 REMARK 480 SER B 109 OG REMARK 480 ARG B 116 NH1 NH2 REMARK 480 GLN B 119 OE1 NE2 REMARK 480 LYS B 135 CE NZ REMARK 480 ARG B 151 CG CD NE CZ NH1 NH2 REMARK 480 GLU B 169 CG CD OE1 OE2 REMARK 480 LYS B 172 CD CE NZ REMARK 480 GLU B 181 OE1 OE2 REMARK 480 ASN B 205 ND2 REMARK 480 ARG B 239 CD NE CZ NH1 NH2 REMARK 480 LYS B 248 NZ REMARK 480 LYS B 260 NZ REMARK 480 TYR B 263 OH REMARK 480 HIS B 273 N CB CG ND1 CD2 CE1 NE2 REMARK 480 ASN B 274 CG OD1 ND2 REMARK 480 ARG B 284 CG CD NE CZ NH1 NH2 REMARK 480 ASP B 289 CB CG OD1 OD2 REMARK 480 LYS B 290 CE NZ REMARK 480 ASP B 294 N CA CB CG OD1 OD2 REMARK 480 LYS B 295 CD CE NZ REMARK 480 LYS B 299 CE NZ REMARK 480 GLU B 302 CD OE1 OE2 REMARK 480 LYS B 310 NZ REMARK 480 GLU B 313 CD OE1 OE2 REMARK 480 GLN B 322 CD OE1 NE2 REMARK 480 ILE B 346 CG1 CD1 REMARK 480 TRP B 354 CE3 CZ2 CZ3 CH2 REMARK 480 ILE B 357 CD1 REMARK 480 GLU B 363 CG CD OE1 OE2 REMARK 480 ARG B 372 NE CZ NH1 NH2 REMARK 480 ARG B 407 CD NE CZ NH1 NH2 REMARK 480 LYS B 415 CD CE NZ REMARK 480 ARG B 425 CZ NH1 NH2 REMARK 480 LYS B 428 CD CE NZ REMARK 480 ARG B 441 NE CZ NH1 NH2 REMARK 480 SER B 448 OG REMARK 480 LYS B 453 CG CD CE NZ REMARK 480 GLU B 460 CG CD OE1 OE2 REMARK 480 GLU B 461 CG CD OE1 OE2 REMARK 480 LYS B 466 CE NZ REMARK 480 ARG B 472 CG CD NE CZ NH1 NH2 REMARK 480 LEU B 484 CD1 CD2 REMARK 480 ARG B 502 NH1 NH2 REMARK 480 GLU B 527 CG CD OE1 OE2 REMARK 480 GLU B 529 CD OE1 OE2 REMARK 480 GLU B 536 OE1 OE2 REMARK 480 GLU B 541 CG CD OE1 OE2 REMARK 480 ARG B 561 CZ NH1 NH2 REMARK 480 HIS B 572 CG ND1 CD2 CE1 NE2 REMARK 480 LYS B 578 CG CD CE NZ REMARK 480 VAL B 587 CA CB CG1 CG2 REMARK 480 GLN B 588 CD OE1 NE2 REMARK 480 GLU B 590 CD OE1 OE2 REMARK 480 ARG B 592 CZ NH1 NH2 REMARK 480 GLN B 600 CG CD OE1 NE2 REMARK 480 LYS B 603 CG CD CE NZ REMARK 480 GLU B 606 CD OE1 OE2 REMARK 480 ARG C 36 CD NE CZ NH1 NH2 REMARK 480 GLU C 74 OE1 OE2 REMARK 480 SER C 76 OG REMARK 480 ARG C 84 NH1 NH2 REMARK 480 ASN C 107 CG OD1 ND2 REMARK 480 SER C 109 OG REMARK 480 ARG C 116 NH1 NH2 REMARK 480 GLN C 119 OE1 NE2 REMARK 480 LYS C 135 CE NZ REMARK 480 ARG C 149 NE CZ NH1 NH2 REMARK 480 ARG C 151 CG CD NE CZ NH1 NH2 REMARK 480 SER C 163 OG REMARK 480 GLU C 169 CG CD OE1 OE2 REMARK 480 LYS C 172 CD CE NZ REMARK 480 GLU C 181 OE1 OE2 REMARK 480 LYS C 188 CB CG CD CE NZ REMARK 480 THR C 189 OG1 CG2 REMARK 480 ILE C 190 O CG1 CG2 CD1 REMARK 480 GLN C 194 CD OE1 NE2 REMARK 480 ASN C 205 ND2 REMARK 480 ASP C 210 CG OD1 OD2 REMARK 480 ARG C 239 CD NE CZ NH1 NH2 REMARK 480 GLN C 242 CG CD OE1 NE2 REMARK 480 LYS C 248 NZ REMARK 480 LYS C 260 NZ REMARK 480 TYR C 263 OH REMARK 480 HIS C 273 N CB CG ND1 CD2 CE1 NE2 REMARK 480 ASN C 274 CG OD1 ND2 REMARK 480 GLN C 279 CG CD OE1 NE2 REMARK 480 ARG C 284 CG CD NE CZ NH1 NH2 REMARK 480 ASP C 289 CB CG OD1 OD2 REMARK 480 LYS C 290 CE NZ REMARK 480 ASP C 294 N CA CB CG OD1 OD2 REMARK 480 LYS C 295 CD CE NZ REMARK 480 LYS C 299 CE NZ REMARK 480 GLU C 302 CD OE1 OE2 REMARK 480 LYS C 310 NZ REMARK 480 GLU C 313 CD OE1 OE2 REMARK 480 GLN C 322 CD OE1 NE2 REMARK 480 ILE C 346 CG1 CD1 REMARK 480 TRP C 354 CE3 CZ2 CZ3 CH2 REMARK 480 ILE C 357 CD1 REMARK 480 GLU C 363 CG CD OE1 OE2 REMARK 480 ARG C 372 NE CZ NH1 NH2 REMARK 480 ARG C 407 CD NE CZ NH1 NH2 REMARK 480 LYS C 415 CD CE NZ REMARK 480 ARG C 425 CZ NH1 NH2 REMARK 480 LYS C 428 CD CE NZ REMARK 480 GLN C 442 OE1 NE2 REMARK 480 SER C 448 OG REMARK 480 LYS C 453 CG CD CE NZ REMARK 480 GLU C 460 CG CD OE1 OE2 REMARK 480 GLU C 461 CG CD OE1 OE2 REMARK 480 LYS C 466 CE NZ REMARK 480 ARG C 472 CG CD NE CZ NH1 NH2 REMARK 480 ARG C 502 NH1 NH2 REMARK 480 GLU C 527 CG CD OE1 OE2 REMARK 480 GLU C 529 CD OE1 OE2 REMARK 480 LEU D 30 CD1 CD2 REMARK 480 TYR D 31 CZ REMARK 480 LYS D 32 CG CD CE NZ REMARK 480 LEU D 33 CD1 CD2 REMARK 480 ARG D 36 CD NE CZ NH1 NH2 REMARK 480 MET D 41 SD CE REMARK 480 GLU D 74 OE1 OE2 REMARK 480 SER D 76 OG REMARK 480 ARG D 84 NH1 NH2 REMARK 480 ASN D 107 CG OD1 ND2 REMARK 480 SER D 109 OG REMARK 480 ARG D 116 NH1 NH2 REMARK 480 GLN D 119 OE1 NE2 REMARK 480 LYS D 135 CE NZ REMARK 480 ARG D 149 NE CZ NH1 NH2 REMARK 480 ARG D 151 CG CD NE CZ NH1 NH2 REMARK 480 SER D 163 OG REMARK 480 GLU D 169 CG CD OE1 OE2 REMARK 480 LYS D 172 CD CE NZ REMARK 480 GLU D 181 OE1 OE2 REMARK 480 GLN D 194 CD OE1 NE2 REMARK 480 ASN D 205 ND2 REMARK 480 ASP D 210 CG OD1 OD2 REMARK 480 ARG D 239 CD NE CZ NH1 NH2 REMARK 480 GLN D 242 CG CD OE1 NE2 REMARK 480 LYS D 248 NZ REMARK 480 LYS D 260 NZ REMARK 480 TYR D 263 OH REMARK 480 GLN D 279 CG CD OE1 NE2 REMARK 480 ASP D 289 CB CG OD1 OD2 REMARK 480 LYS D 290 CE NZ REMARK 480 LYS D 295 CD CE NZ REMARK 480 LYS D 299 CE NZ REMARK 480 GLU D 302 CD OE1 OE2 REMARK 480 LYS D 310 NZ REMARK 480 GLU D 313 CD OE1 OE2 REMARK 480 GLN D 322 CD OE1 NE2 REMARK 480 ILE D 346 CG1 CD1 REMARK 480 TRP D 354 CE3 CZ2 CZ3 CH2 REMARK 480 ILE D 357 CD1 REMARK 480 GLU D 363 CG CD OE1 OE2 REMARK 480 ARG D 372 NE CZ NH1 NH2 REMARK 480 ARG D 407 CD NE CZ NH1 NH2 REMARK 480 LYS D 415 CD CE NZ REMARK 480 ARG D 425 CZ NH1 NH2 REMARK 480 LYS D 428 CD CE NZ REMARK 480 ARG D 441 NE CZ NH1 NH2 REMARK 480 GLN D 442 OE1 NE2 REMARK 480 SER D 448 OG REMARK 480 LYS D 453 CG CD CE NZ REMARK 480 GLU D 460 CG CD OE1 OE2 REMARK 480 GLU D 461 CG CD OE1 OE2 REMARK 480 LYS D 466 CE NZ REMARK 480 ARG D 472 CG CD NE CZ NH1 NH2 REMARK 480 LEU D 484 CD1 CD2 REMARK 480 ARG D 502 NH1 NH2 REMARK 480 GLU D 520 O CG CD OE1 OE2 REMARK 480 GLU D 527 CG CD OE1 OE2 REMARK 480 GLU D 529 CD OE1 OE2 REMARK 480 ARG D 561 CZ NH1 NH2 REMARK 480 HIS D 572 CG ND1 CD2 CE1 NE2 REMARK 480 LYS D 578 CG CD CE NZ REMARK 480 GLU D 590 CD OE1 OE2 REMARK 480 ARG D 592 CZ NH1 NH2 REMARK 480 GLN D 600 CG CD OE1 NE2 REMARK 480 LYS D 603 CG CD CE NZ REMARK 480 GLU D 606 CD OE1 OE2 REMARK 480 LEU D 611 CD1 CD2 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 36 47.77 -86.35 REMARK 500 ASP A 93 18.69 57.96 REMARK 500 ASN A 103 49.42 -97.79 REMARK 500 ARG A 113 -16.77 -143.41 REMARK 500 THR A 121 -55.88 -125.98 REMARK 500 HIS A 138 36.34 73.58 REMARK 500 ILE A 147 -62.15 -90.23 REMARK 500 GLN A 206 56.74 -117.21 REMARK 500 HIS A 229 -66.45 -137.78 REMARK 500 HIS A 258 56.25 -98.11 REMARK 500 TYR A 263 74.42 -100.24 REMARK 500 ASP A 278 -69.75 -90.74 REMARK 500 GLN A 279 -65.63 -131.47 REMARK 500 ASP A 289 31.63 -90.29 REMARK 500 PHE A 390 46.25 -86.58 REMARK 500 ASN A 406 -125.69 59.11 REMARK 500 SER A 421 143.97 -170.36 REMARK 500 TYR A 445 -11.52 75.12 REMARK 500 ASN A 503 -82.49 -122.12 REMARK 500 ASN A 515 53.15 -90.82 REMARK 500 GLU A 536 -2.39 74.12 REMARK 500 HIS A 559 -94.99 -100.56 REMARK 500 ASN A 597 30.27 -85.51 REMARK 500 GLN A 600 -114.01 52.30 REMARK 500 SER B 109 34.21 -96.32 REMARK 500 HIS B 138 -3.83 79.35 REMARK 500 THR B 187 -7.78 -144.12 REMARK 500 HIS B 229 -87.28 -126.03 REMARK 500 HIS B 258 44.36 -98.24 REMARK 500 HIS B 273 -125.62 49.32 REMARK 500 ASP B 278 -72.17 -77.55 REMARK 500 GLN B 279 -69.17 -129.04 REMARK 500 ASN B 406 -124.14 60.24 REMARK 500 ASN B 440 78.93 -108.09 REMARK 500 TYR B 445 -5.57 82.96 REMARK 500 ASP B 464 76.18 -119.38 REMARK 500 ASN B 503 -78.88 -127.60 REMARK 500 PHE B 516 -72.36 -83.60 REMARK 500 ASN B 518 145.11 -176.98 REMARK 500 HIS B 559 -103.01 -102.81 REMARK 500 GLN B 600 -1.97 84.12 REMARK 500 CYS C 10 117.89 -161.91 REMARK 500 LYS C 32 -164.54 62.27 REMARK 500 LEU C 33 127.26 -171.93 REMARK 500 TYR C 34 39.92 -91.88 REMARK 500 ARG C 62 17.36 -142.74 REMARK 500 LYS C 95 -29.05 -140.41 REMARK 500 LEU C 117 50.82 -113.71 REMARK 500 HIS C 138 -1.32 77.76 REMARK 500 ASP C 150 106.42 -56.62 REMARK 500 REMARK 500 THIS ENTRY HAS 129 RAMACHANDRAN OUTLIERS. REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 36 0.14 SIDE CHAIN REMARK 500 ARG C 116 0.11 SIDE CHAIN REMARK 500 ARG D 469 0.15 SIDE CHAIN REMARK 500 ARG E 148 0.11 SIDE CHAIN REMARK 500 ARG F 148 0.10 SIDE CHAIN REMARK 500 ARG H 59 0.20 SIDE CHAIN REMARK 500 ARG H 148 0.08 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL DBREF 9I1Q A 1 624 UNP P21860 ERBB3_HUMAN 20 643 DBREF 9I1Q B 1 624 UNP P21860 ERBB3_HUMAN 20 643 DBREF 9I1Q C 1 624 UNP P21860 ERBB3_HUMAN 20 643 DBREF 9I1Q D 1 624 UNP P21860 ERBB3_HUMAN 20 643 DBREF 9I1Q E 1 220 PDB 9I1Q 9I1Q 1 220 DBREF 9I1Q F 1 220 PDB 9I1Q 9I1Q 1 220 DBREF 9I1Q G 1 220 PDB 9I1Q 9I1Q 1 220 DBREF 9I1Q H 1 220 PDB 9I1Q 9I1Q 1 220 DBREF 9I1Q I 221 443 PDB 9I1Q 9I1Q 221 443 DBREF 9I1Q J 221 443 PDB 9I1Q 9I1Q 221 443 DBREF 9I1Q K 221 443 PDB 9I1Q 9I1Q 221 443 DBREF 9I1Q L 221 443 PDB 9I1Q 9I1Q 221 443 SEQADV 9I1Q VAL A 625 UNP P21860 EXPRESSION TAG SEQADV 9I1Q ASP A 626 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS A 627 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS A 628 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS A 629 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS A 630 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS A 631 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS A 632 UNP P21860 EXPRESSION TAG SEQADV 9I1Q VAL B 625 UNP P21860 EXPRESSION TAG SEQADV 9I1Q ASP B 626 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS B 627 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS B 628 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS B 629 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS B 630 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS B 631 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS B 632 UNP P21860 EXPRESSION TAG SEQADV 9I1Q VAL C 625 UNP P21860 EXPRESSION TAG SEQADV 9I1Q ASP C 626 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS C 627 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS C 628 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS C 629 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS C 630 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS C 631 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS C 632 UNP P21860 EXPRESSION TAG SEQADV 9I1Q VAL D 625 UNP P21860 EXPRESSION TAG SEQADV 9I1Q ASP D 626 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS D 627 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS D 628 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS D 629 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS D 630 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS D 631 UNP P21860 EXPRESSION TAG SEQADV 9I1Q HIS D 632 UNP P21860 EXPRESSION TAG SEQRES 1 A 632 SER GLU VAL GLY ASN SER GLN ALA VAL CYS PRO GLY THR SEQRES 2 A 632 LEU ASN GLY LEU SER VAL THR GLY ASP ALA GLU ASN GLN SEQRES 3 A 632 TYR GLN THR LEU TYR LYS LEU TYR GLU ARG CYS GLU VAL SEQRES 4 A 632 VAL MET GLY ASN LEU GLU ILE VAL LEU THR GLY HIS ASN SEQRES 5 A 632 ALA ASP LEU SER PHE LEU GLN TRP ILE ARG GLU VAL THR SEQRES 6 A 632 GLY TYR VAL LEU VAL ALA MET ASN GLU PHE SER THR LEU SEQRES 7 A 632 PRO LEU PRO ASN LEU ARG VAL VAL ARG GLY THR GLN VAL SEQRES 8 A 632 TYR ASP GLY LYS PHE ALA ILE PHE VAL MET LEU ASN TYR SEQRES 9 A 632 ASN THR ASN SER SER HIS ALA LEU ARG GLN LEU ARG LEU SEQRES 10 A 632 THR GLN LEU THR GLU ILE LEU SER GLY GLY VAL TYR ILE SEQRES 11 A 632 GLU LYS ASN ASP LYS LEU CYS HIS MET ASP THR ILE ASP SEQRES 12 A 632 TRP ARG ASP ILE VAL ARG ASP ARG ASP ALA GLU ILE VAL SEQRES 13 A 632 VAL LYS ASP ASN GLY ARG SER CYS PRO PRO CYS HIS GLU SEQRES 14 A 632 VAL CYS LYS GLY ARG CYS TRP GLY PRO GLY SER GLU ASP SEQRES 15 A 632 CYS GLN THR LEU THR LYS THR ILE CYS ALA PRO GLN CYS SEQRES 16 A 632 ASN GLY HIS CYS PHE GLY PRO ASN PRO ASN GLN CYS CYS SEQRES 17 A 632 HIS ASP GLU CYS ALA GLY GLY CYS SER GLY PRO GLN ASP SEQRES 18 A 632 THR ASP CYS PHE ALA CYS ARG HIS PHE ASN ASP SER GLY SEQRES 19 A 632 ALA CYS VAL PRO ARG CYS PRO GLN PRO LEU VAL TYR ASN SEQRES 20 A 632 LYS LEU THR PHE GLN LEU GLU PRO ASN PRO HIS THR LYS SEQRES 21 A 632 TYR GLN TYR GLY GLY VAL CYS VAL ALA SER CYS PRO HIS SEQRES 22 A 632 ASN PHE VAL VAL ASP GLN THR SER CYS VAL ARG ALA CYS SEQRES 23 A 632 PRO PRO ASP LYS MET GLU VAL ASP LYS ASN GLY LEU LYS SEQRES 24 A 632 MET CYS GLU PRO CYS GLY GLY LEU CYS PRO LYS ALA CYS SEQRES 25 A 632 GLU GLY THR GLY SER GLY SER ARG PHE GLN THR VAL ASP SEQRES 26 A 632 SER SER ASN ILE ASP GLY PHE VAL ASN CYS THR LYS ILE SEQRES 27 A 632 LEU GLY ASN LEU ASP PHE LEU ILE THR GLY LEU ASN GLY SEQRES 28 A 632 ASP PRO TRP HIS LYS ILE PRO ALA LEU ASP PRO GLU LYS SEQRES 29 A 632 LEU ASN VAL PHE ARG THR VAL ARG GLU ILE THR GLY TYR SEQRES 30 A 632 LEU ASN ILE GLN SER TRP PRO PRO HIS MET HIS ASN PHE SEQRES 31 A 632 SER VAL PHE SER ASN LEU THR THR ILE GLY GLY ARG SER SEQRES 32 A 632 LEU TYR ASN ARG GLY PHE SER LEU LEU ILE MET LYS ASN SEQRES 33 A 632 LEU ASN VAL THR SER LEU GLY PHE ARG SER LEU LYS GLU SEQRES 34 A 632 ILE SER ALA GLY ARG ILE TYR ILE SER ALA ASN ARG GLN SEQRES 35 A 632 LEU CYS TYR HIS HIS SER LEU ASN TRP THR LYS VAL LEU SEQRES 36 A 632 ARG GLY PRO THR GLU GLU ARG LEU ASP ILE LYS HIS ASN SEQRES 37 A 632 ARG PRO ARG ARG ASP CYS VAL ALA GLU GLY LYS VAL CYS SEQRES 38 A 632 ASP PRO LEU CYS SER SER GLY GLY CYS TRP GLY PRO GLY SEQRES 39 A 632 PRO GLY GLN CYS LEU SER CYS ARG ASN TYR SER ARG GLY SEQRES 40 A 632 GLY VAL CYS VAL THR HIS CYS ASN PHE LEU ASN GLY GLU SEQRES 41 A 632 PRO ARG GLU PHE ALA HIS GLU ALA GLU CYS PHE SER CYS SEQRES 42 A 632 HIS PRO GLU CYS GLN PRO MET GLU GLY THR ALA THR CYS SEQRES 43 A 632 ASN GLY SER GLY SER ASP THR CYS ALA GLN CYS ALA HIS SEQRES 44 A 632 PHE ARG ASP GLY PRO HIS CYS VAL SER SER CYS PRO HIS SEQRES 45 A 632 GLY VAL LEU GLY ALA LYS GLY PRO ILE TYR LYS TYR PRO SEQRES 46 A 632 ASP VAL GLN ASN GLU CYS ARG PRO CYS HIS GLU ASN CYS SEQRES 47 A 632 THR GLN GLY CYS LYS GLY PRO GLU LEU GLN ASP CYS LEU SEQRES 48 A 632 GLY GLN THR LEU VAL LEU ILE GLY LYS THR HIS LEU THR SEQRES 49 A 632 VAL ASP HIS HIS HIS HIS HIS HIS SEQRES 1 B 632 SER GLU VAL GLY ASN SER GLN ALA VAL CYS PRO GLY THR SEQRES 2 B 632 LEU ASN GLY LEU SER VAL THR GLY ASP ALA GLU ASN GLN SEQRES 3 B 632 TYR GLN THR LEU TYR LYS LEU TYR GLU ARG CYS GLU VAL SEQRES 4 B 632 VAL MET GLY ASN LEU GLU ILE VAL LEU THR GLY HIS ASN SEQRES 5 B 632 ALA ASP LEU SER PHE LEU GLN TRP ILE ARG GLU VAL THR SEQRES 6 B 632 GLY TYR VAL LEU VAL ALA MET ASN GLU PHE SER THR LEU SEQRES 7 B 632 PRO LEU PRO ASN LEU ARG VAL VAL ARG GLY THR GLN VAL SEQRES 8 B 632 TYR ASP GLY LYS PHE ALA ILE PHE VAL MET LEU ASN TYR SEQRES 9 B 632 ASN THR ASN SER SER HIS ALA LEU ARG GLN LEU ARG LEU SEQRES 10 B 632 THR GLN LEU THR GLU ILE LEU SER GLY GLY VAL TYR ILE SEQRES 11 B 632 GLU LYS ASN ASP LYS LEU CYS HIS MET ASP THR ILE ASP SEQRES 12 B 632 TRP ARG ASP ILE VAL ARG ASP ARG ASP ALA GLU ILE VAL SEQRES 13 B 632 VAL LYS ASP ASN GLY ARG SER CYS PRO PRO CYS HIS GLU SEQRES 14 B 632 VAL CYS LYS GLY ARG CYS TRP GLY PRO GLY SER GLU ASP SEQRES 15 B 632 CYS GLN THR LEU THR LYS THR ILE CYS ALA PRO GLN CYS SEQRES 16 B 632 ASN GLY HIS CYS PHE GLY PRO ASN PRO ASN GLN CYS CYS SEQRES 17 B 632 HIS ASP GLU CYS ALA GLY GLY CYS SER GLY PRO GLN ASP SEQRES 18 B 632 THR ASP CYS PHE ALA CYS ARG HIS PHE ASN ASP SER GLY SEQRES 19 B 632 ALA CYS VAL PRO ARG CYS PRO GLN PRO LEU VAL TYR ASN SEQRES 20 B 632 LYS LEU THR PHE GLN LEU GLU PRO ASN PRO HIS THR LYS SEQRES 21 B 632 TYR GLN TYR GLY GLY VAL CYS VAL ALA SER CYS PRO HIS SEQRES 22 B 632 ASN PHE VAL VAL ASP GLN THR SER CYS VAL ARG ALA CYS SEQRES 23 B 632 PRO PRO ASP LYS MET GLU VAL ASP LYS ASN GLY LEU LYS SEQRES 24 B 632 MET CYS GLU PRO CYS GLY GLY LEU CYS PRO LYS ALA CYS SEQRES 25 B 632 GLU GLY THR GLY SER GLY SER ARG PHE GLN THR VAL ASP SEQRES 26 B 632 SER SER ASN ILE ASP GLY PHE VAL ASN CYS THR LYS ILE SEQRES 27 B 632 LEU GLY ASN LEU ASP PHE LEU ILE THR GLY LEU ASN GLY SEQRES 28 B 632 ASP PRO TRP HIS LYS ILE PRO ALA LEU ASP PRO GLU LYS SEQRES 29 B 632 LEU ASN VAL PHE ARG THR VAL ARG GLU ILE THR GLY TYR SEQRES 30 B 632 LEU ASN ILE GLN SER TRP PRO PRO HIS MET HIS ASN PHE SEQRES 31 B 632 SER VAL PHE SER ASN LEU THR THR ILE GLY GLY ARG SER SEQRES 32 B 632 LEU TYR ASN ARG GLY PHE SER LEU LEU ILE MET LYS ASN SEQRES 33 B 632 LEU ASN VAL THR SER LEU GLY PHE ARG SER LEU LYS GLU SEQRES 34 B 632 ILE SER ALA GLY ARG ILE TYR ILE SER ALA ASN ARG GLN SEQRES 35 B 632 LEU CYS TYR HIS HIS SER LEU ASN TRP THR LYS VAL LEU SEQRES 36 B 632 ARG GLY PRO THR GLU GLU ARG LEU ASP ILE LYS HIS ASN SEQRES 37 B 632 ARG PRO ARG ARG ASP CYS VAL ALA GLU GLY LYS VAL CYS SEQRES 38 B 632 ASP PRO LEU CYS SER SER GLY GLY CYS TRP GLY PRO GLY SEQRES 39 B 632 PRO GLY GLN CYS LEU SER CYS ARG ASN TYR SER ARG GLY SEQRES 40 B 632 GLY VAL CYS VAL THR HIS CYS ASN PHE LEU ASN GLY GLU SEQRES 41 B 632 PRO ARG GLU PHE ALA HIS GLU ALA GLU CYS PHE SER CYS SEQRES 42 B 632 HIS PRO GLU CYS GLN PRO MET GLU GLY THR ALA THR CYS SEQRES 43 B 632 ASN GLY SER GLY SER ASP THR CYS ALA GLN CYS ALA HIS SEQRES 44 B 632 PHE ARG ASP GLY PRO HIS CYS VAL SER SER CYS PRO HIS SEQRES 45 B 632 GLY VAL LEU GLY ALA LYS GLY PRO ILE TYR LYS TYR PRO SEQRES 46 B 632 ASP VAL GLN ASN GLU CYS ARG PRO CYS HIS GLU ASN CYS SEQRES 47 B 632 THR GLN GLY CYS LYS GLY PRO GLU LEU GLN ASP CYS LEU SEQRES 48 B 632 GLY GLN THR LEU VAL LEU ILE GLY LYS THR HIS LEU THR SEQRES 49 B 632 VAL ASP HIS HIS HIS HIS HIS HIS SEQRES 1 C 632 SER GLU VAL GLY ASN SER GLN ALA VAL CYS PRO GLY THR SEQRES 2 C 632 LEU ASN GLY LEU SER VAL THR GLY ASP ALA GLU ASN GLN SEQRES 3 C 632 TYR GLN THR LEU TYR LYS LEU TYR GLU ARG CYS GLU VAL SEQRES 4 C 632 VAL MET GLY ASN LEU GLU ILE VAL LEU THR GLY HIS ASN SEQRES 5 C 632 ALA ASP LEU SER PHE LEU GLN TRP ILE ARG GLU VAL THR SEQRES 6 C 632 GLY TYR VAL LEU VAL ALA MET ASN GLU PHE SER THR LEU SEQRES 7 C 632 PRO LEU PRO ASN LEU ARG VAL VAL ARG GLY THR GLN VAL SEQRES 8 C 632 TYR ASP GLY LYS PHE ALA ILE PHE VAL MET LEU ASN TYR SEQRES 9 C 632 ASN THR ASN SER SER HIS ALA LEU ARG GLN LEU ARG LEU SEQRES 10 C 632 THR GLN LEU THR GLU ILE LEU SER GLY GLY VAL TYR ILE SEQRES 11 C 632 GLU LYS ASN ASP LYS LEU CYS HIS MET ASP THR ILE ASP SEQRES 12 C 632 TRP ARG ASP ILE VAL ARG ASP ARG ASP ALA GLU ILE VAL SEQRES 13 C 632 VAL LYS ASP ASN GLY ARG SER CYS PRO PRO CYS HIS GLU SEQRES 14 C 632 VAL CYS LYS GLY ARG CYS TRP GLY PRO GLY SER GLU ASP SEQRES 15 C 632 CYS GLN THR LEU THR LYS THR ILE CYS ALA PRO GLN CYS SEQRES 16 C 632 ASN GLY HIS CYS PHE GLY PRO ASN PRO ASN GLN CYS CYS SEQRES 17 C 632 HIS ASP GLU CYS ALA GLY GLY CYS SER GLY PRO GLN ASP SEQRES 18 C 632 THR ASP CYS PHE ALA CYS ARG HIS PHE ASN ASP SER GLY SEQRES 19 C 632 ALA CYS VAL PRO ARG CYS PRO GLN PRO LEU VAL TYR ASN SEQRES 20 C 632 LYS LEU THR PHE GLN LEU GLU PRO ASN PRO HIS THR LYS SEQRES 21 C 632 TYR GLN TYR GLY GLY VAL CYS VAL ALA SER CYS PRO HIS SEQRES 22 C 632 ASN PHE VAL VAL ASP GLN THR SER CYS VAL ARG ALA CYS SEQRES 23 C 632 PRO PRO ASP LYS MET GLU VAL ASP LYS ASN GLY LEU LYS SEQRES 24 C 632 MET CYS GLU PRO CYS GLY GLY LEU CYS PRO LYS ALA CYS SEQRES 25 C 632 GLU GLY THR GLY SER GLY SER ARG PHE GLN THR VAL ASP SEQRES 26 C 632 SER SER ASN ILE ASP GLY PHE VAL ASN CYS THR LYS ILE SEQRES 27 C 632 LEU GLY ASN LEU ASP PHE LEU ILE THR GLY LEU ASN GLY SEQRES 28 C 632 ASP PRO TRP HIS LYS ILE PRO ALA LEU ASP PRO GLU LYS SEQRES 29 C 632 LEU ASN VAL PHE ARG THR VAL ARG GLU ILE THR GLY TYR SEQRES 30 C 632 LEU ASN ILE GLN SER TRP PRO PRO HIS MET HIS ASN PHE SEQRES 31 C 632 SER VAL PHE SER ASN LEU THR THR ILE GLY GLY ARG SER SEQRES 32 C 632 LEU TYR ASN ARG GLY PHE SER LEU LEU ILE MET LYS ASN SEQRES 33 C 632 LEU ASN VAL THR SER LEU GLY PHE ARG SER LEU LYS GLU SEQRES 34 C 632 ILE SER ALA GLY ARG ILE TYR ILE SER ALA ASN ARG GLN SEQRES 35 C 632 LEU CYS TYR HIS HIS SER LEU ASN TRP THR LYS VAL LEU SEQRES 36 C 632 ARG GLY PRO THR GLU GLU ARG LEU ASP ILE LYS HIS ASN SEQRES 37 C 632 ARG PRO ARG ARG ASP CYS VAL ALA GLU GLY LYS VAL CYS SEQRES 38 C 632 ASP PRO LEU CYS SER SER GLY GLY CYS TRP GLY PRO GLY SEQRES 39 C 632 PRO GLY GLN CYS LEU SER CYS ARG ASN TYR SER ARG GLY SEQRES 40 C 632 GLY VAL CYS VAL THR HIS CYS ASN PHE LEU ASN GLY GLU SEQRES 41 C 632 PRO ARG GLU PHE ALA HIS GLU ALA GLU CYS PHE SER CYS SEQRES 42 C 632 HIS PRO GLU CYS GLN PRO MET GLU GLY THR ALA THR CYS SEQRES 43 C 632 ASN GLY SER GLY SER ASP THR CYS ALA GLN CYS ALA HIS SEQRES 44 C 632 PHE ARG ASP GLY PRO HIS CYS VAL SER SER CYS PRO HIS SEQRES 45 C 632 GLY VAL LEU GLY ALA LYS GLY PRO ILE TYR LYS TYR PRO SEQRES 46 C 632 ASP VAL GLN ASN GLU CYS ARG PRO CYS HIS GLU ASN CYS SEQRES 47 C 632 THR GLN GLY CYS LYS GLY PRO GLU LEU GLN ASP CYS LEU SEQRES 48 C 632 GLY GLN THR LEU VAL LEU ILE GLY LYS THR HIS LEU THR SEQRES 49 C 632 VAL ASP HIS HIS HIS HIS HIS HIS SEQRES 1 D 632 SER GLU VAL GLY ASN SER GLN ALA VAL CYS PRO GLY THR SEQRES 2 D 632 LEU ASN GLY LEU SER VAL THR GLY ASP ALA GLU ASN GLN SEQRES 3 D 632 TYR GLN THR LEU TYR LYS LEU TYR GLU ARG CYS GLU VAL SEQRES 4 D 632 VAL MET GLY ASN LEU GLU ILE VAL LEU THR GLY HIS ASN SEQRES 5 D 632 ALA ASP LEU SER PHE LEU GLN TRP ILE ARG GLU VAL THR SEQRES 6 D 632 GLY TYR VAL LEU VAL ALA MET ASN GLU PHE SER THR LEU SEQRES 7 D 632 PRO LEU PRO ASN LEU ARG VAL VAL ARG GLY THR GLN VAL SEQRES 8 D 632 TYR ASP GLY LYS PHE ALA ILE PHE VAL MET LEU ASN TYR SEQRES 9 D 632 ASN THR ASN SER SER HIS ALA LEU ARG GLN LEU ARG LEU SEQRES 10 D 632 THR GLN LEU THR GLU ILE LEU SER GLY GLY VAL TYR ILE SEQRES 11 D 632 GLU LYS ASN ASP LYS LEU CYS HIS MET ASP THR ILE ASP SEQRES 12 D 632 TRP ARG ASP ILE VAL ARG ASP ARG ASP ALA GLU ILE VAL SEQRES 13 D 632 VAL LYS ASP ASN GLY ARG SER CYS PRO PRO CYS HIS GLU SEQRES 14 D 632 VAL CYS LYS GLY ARG CYS TRP GLY PRO GLY SER GLU ASP SEQRES 15 D 632 CYS GLN THR LEU THR LYS THR ILE CYS ALA PRO GLN CYS SEQRES 16 D 632 ASN GLY HIS CYS PHE GLY PRO ASN PRO ASN GLN CYS CYS SEQRES 17 D 632 HIS ASP GLU CYS ALA GLY GLY CYS SER GLY PRO GLN ASP SEQRES 18 D 632 THR ASP CYS PHE ALA CYS ARG HIS PHE ASN ASP SER GLY SEQRES 19 D 632 ALA CYS VAL PRO ARG CYS PRO GLN PRO LEU VAL TYR ASN SEQRES 20 D 632 LYS LEU THR PHE GLN LEU GLU PRO ASN PRO HIS THR LYS SEQRES 21 D 632 TYR GLN TYR GLY GLY VAL CYS VAL ALA SER CYS PRO HIS SEQRES 22 D 632 ASN PHE VAL VAL ASP GLN THR SER CYS VAL ARG ALA CYS SEQRES 23 D 632 PRO PRO ASP LYS MET GLU VAL ASP LYS ASN GLY LEU LYS SEQRES 24 D 632 MET CYS GLU PRO CYS GLY GLY LEU CYS PRO LYS ALA CYS SEQRES 25 D 632 GLU GLY THR GLY SER GLY SER ARG PHE GLN THR VAL ASP SEQRES 26 D 632 SER SER ASN ILE ASP GLY PHE VAL ASN CYS THR LYS ILE SEQRES 27 D 632 LEU GLY ASN LEU ASP PHE LEU ILE THR GLY LEU ASN GLY SEQRES 28 D 632 ASP PRO TRP HIS LYS ILE PRO ALA LEU ASP PRO GLU LYS SEQRES 29 D 632 LEU ASN VAL PHE ARG THR VAL ARG GLU ILE THR GLY TYR SEQRES 30 D 632 LEU ASN ILE GLN SER TRP PRO PRO HIS MET HIS ASN PHE SEQRES 31 D 632 SER VAL PHE SER ASN LEU THR THR ILE GLY GLY ARG SER SEQRES 32 D 632 LEU TYR ASN ARG GLY PHE SER LEU LEU ILE MET LYS ASN SEQRES 33 D 632 LEU ASN VAL THR SER LEU GLY PHE ARG SER LEU LYS GLU SEQRES 34 D 632 ILE SER ALA GLY ARG ILE TYR ILE SER ALA ASN ARG GLN SEQRES 35 D 632 LEU CYS TYR HIS HIS SER LEU ASN TRP THR LYS VAL LEU SEQRES 36 D 632 ARG GLY PRO THR GLU GLU ARG LEU ASP ILE LYS HIS ASN SEQRES 37 D 632 ARG PRO ARG ARG ASP CYS VAL ALA GLU GLY LYS VAL CYS SEQRES 38 D 632 ASP PRO LEU CYS SER SER GLY GLY CYS TRP GLY PRO GLY SEQRES 39 D 632 PRO GLY GLN CYS LEU SER CYS ARG ASN TYR SER ARG GLY SEQRES 40 D 632 GLY VAL CYS VAL THR HIS CYS ASN PHE LEU ASN GLY GLU SEQRES 41 D 632 PRO ARG GLU PHE ALA HIS GLU ALA GLU CYS PHE SER CYS SEQRES 42 D 632 HIS PRO GLU CYS GLN PRO MET GLU GLY THR ALA THR CYS SEQRES 43 D 632 ASN GLY SER GLY SER ASP THR CYS ALA GLN CYS ALA HIS SEQRES 44 D 632 PHE ARG ASP GLY PRO HIS CYS VAL SER SER CYS PRO HIS SEQRES 45 D 632 GLY VAL LEU GLY ALA LYS GLY PRO ILE TYR LYS TYR PRO SEQRES 46 D 632 ASP VAL GLN ASN GLU CYS ARG PRO CYS HIS GLU ASN CYS SEQRES 47 D 632 THR GLN GLY CYS LYS GLY PRO GLU LEU GLN ASP CYS LEU SEQRES 48 D 632 GLY GLN THR LEU VAL LEU ILE GLY LYS THR HIS LEU THR SEQRES 49 D 632 VAL ASP HIS HIS HIS HIS HIS HIS SEQRES 1 E 220 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 E 220 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 E 220 GLN SER LEU LEU HIS SER TYR GLY ASN THR TYR LEU GLU SEQRES 4 E 220 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 E 220 ILE TYR ARG VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 E 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 E 220 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 E 220 TYR CYS PHE GLN GLY SER HIS VAL PRO PHE THR PHE GLY SEQRES 9 E 220 GLN GLY THR LYS LEU GLU ILE LYS ARG ARG THR VAL ALA SEQRES 10 E 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 E 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 E 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 E 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 E 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 E 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 E 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 E 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 F 220 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 F 220 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 F 220 GLN SER LEU LEU HIS SER TYR GLY ASN THR TYR LEU GLU SEQRES 4 F 220 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 F 220 ILE TYR ARG VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 F 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 F 220 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 F 220 TYR CYS PHE GLN GLY SER HIS VAL PRO PHE THR PHE GLY SEQRES 9 F 220 GLN GLY THR LYS LEU GLU ILE LYS ARG ARG THR VAL ALA SEQRES 10 F 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 F 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 F 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 F 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 F 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 F 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 F 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 F 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 G 220 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 G 220 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 G 220 GLN SER LEU LEU HIS SER TYR GLY ASN THR TYR LEU GLU SEQRES 4 G 220 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 G 220 ILE TYR ARG VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 G 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 G 220 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 G 220 TYR CYS PHE GLN GLY SER HIS VAL PRO PHE THR PHE GLY SEQRES 9 G 220 GLN GLY THR LYS LEU GLU ILE LYS ARG ARG THR VAL ALA SEQRES 10 G 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 G 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 G 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 G 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 G 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 G 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 G 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 G 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 220 ASP ILE VAL MET THR GLN THR PRO LEU SER LEU SER VAL SEQRES 2 H 220 THR PRO GLY GLN PRO ALA SER ILE SER CYS LYS SER SER SEQRES 3 H 220 GLN SER LEU LEU HIS SER TYR GLY ASN THR TYR LEU GLU SEQRES 4 H 220 TRP TYR LEU GLN LYS PRO GLY GLN SER PRO GLN LEU LEU SEQRES 5 H 220 ILE TYR ARG VAL SER ASN ARG PHE SER GLY VAL PRO ASP SEQRES 6 H 220 ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU SEQRES 7 H 220 LYS ILE SER ARG VAL GLU ALA GLU ASP VAL GLY VAL TYR SEQRES 8 H 220 TYR CYS PHE GLN GLY SER HIS VAL PRO PHE THR PHE GLY SEQRES 9 H 220 GLN GLY THR LYS LEU GLU ILE LYS ARG ARG THR VAL ALA SEQRES 10 H 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 H 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 H 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 H 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 H 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 H 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 H 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 H 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 I 223 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 I 223 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 I 223 PHE SER LEU SER THR TYR GLY MET GLY VAL GLY TRP ILE SEQRES 4 I 223 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASN SEQRES 5 I 223 ILE TRP TRP ASN ASP ASP LYS TYR TYR SER SER SER LEU SEQRES 6 I 223 LYS THR ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 I 223 GLN VAL VAL LEU THR MET THR ASN MET ASP PRO VAL ASP SEQRES 8 I 223 THR ALA THR TYR TYR CYS VAL GLN ILE ALA ASN PRO TYR SEQRES 9 I 223 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 I 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 I 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 I 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 I 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 I 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 I 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 I 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 I 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 I 223 SER CYS SEQRES 1 J 223 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 J 223 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 J 223 PHE SER LEU SER THR TYR GLY MET GLY VAL GLY TRP ILE SEQRES 4 J 223 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASN SEQRES 5 J 223 ILE TRP TRP ASN ASP ASP LYS TYR TYR SER SER SER LEU SEQRES 6 J 223 LYS THR ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 J 223 GLN VAL VAL LEU THR MET THR ASN MET ASP PRO VAL ASP SEQRES 8 J 223 THR ALA THR TYR TYR CYS VAL GLN ILE ALA ASN PRO TYR SEQRES 9 J 223 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 J 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 J 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 J 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 J 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 J 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 J 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 J 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 J 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 J 223 SER CYS SEQRES 1 K 223 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 K 223 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 K 223 PHE SER LEU SER THR TYR GLY MET GLY VAL GLY TRP ILE SEQRES 4 K 223 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASN SEQRES 5 K 223 ILE TRP TRP ASN ASP ASP LYS TYR TYR SER SER SER LEU SEQRES 6 K 223 LYS THR ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 K 223 GLN VAL VAL LEU THR MET THR ASN MET ASP PRO VAL ASP SEQRES 8 K 223 THR ALA THR TYR TYR CYS VAL GLN ILE ALA ASN PRO TYR SEQRES 9 K 223 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 K 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 K 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 K 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 K 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 K 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 K 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 K 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 K 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 K 223 SER CYS SEQRES 1 L 223 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 L 223 PRO THR GLN THR LEU THR LEU THR CYS THR PHE SER GLY SEQRES 3 L 223 PHE SER LEU SER THR TYR GLY MET GLY VAL GLY TRP ILE SEQRES 4 L 223 ARG GLN PRO PRO GLY LYS ALA LEU GLU TRP LEU ALA ASN SEQRES 5 L 223 ILE TRP TRP ASN ASP ASP LYS TYR TYR SER SER SER LEU SEQRES 6 L 223 LYS THR ARG LEU THR ILE SER LYS ASP THR SER LYS ASN SEQRES 7 L 223 GLN VAL VAL LEU THR MET THR ASN MET ASP PRO VAL ASP SEQRES 8 L 223 THR ALA THR TYR TYR CYS VAL GLN ILE ALA ASN PRO TYR SEQRES 9 L 223 TRP TYR PHE ASP VAL TRP GLY GLN GLY THR THR VAL THR SEQRES 10 L 223 VAL SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO SEQRES 11 L 223 LEU ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA SEQRES 12 L 223 ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO SEQRES 13 L 223 VAL THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY SEQRES 14 L 223 VAL HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU SEQRES 15 L 223 TYR SER LEU SER SER VAL VAL THR VAL PRO SER SER SER SEQRES 16 L 223 LEU GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS SEQRES 17 L 223 PRO SER ASN THR LYS VAL ASP LYS LYS VAL GLU PRO LYS SEQRES 18 L 223 SER CYS HET NAG M 1 14 HET NAG M 2 14 HET BMA M 3 11 HET NAG N 1 14 HET NAG N 2 14 HET BMA N 3 11 HET MAN N 4 11 HET NAG O 1 14 HET NAG O 2 14 HET BMA O 3 11 HET NAG P 1 14 HET NAG P 2 14 HET NAG Q 1 14 HET NAG Q 2 14 HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 14 HET NAG A 704 14 HET NAG A 705 14 HET NAG A 706 14 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET NAG B 705 14 HET NAG B 706 14 HET SCN B 707 3 HET NAG C 701 14 HET NAG C 702 14 HET NAG C 703 14 HET NAG C 704 14 HET NAG C 705 14 HET SCN C 706 3 HET NAG D 701 14 HET NAG D 702 14 HET NAG D 703 14 HET NAG D 704 14 HET NAG D 705 14 HET NAG D 706 14 HET NAG D 707 14 HET SCN D 708 3 HET SCN D 709 3 HET SCN H 301 3 HET SCN H 302 3 HET SCN I 501 3 HET SCN I 502 3 HET SCN L 501 3 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM SCN THIOCYANATE ION 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 HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE FORMUL 13 NAG 34(C8 H15 N O6) FORMUL 13 BMA 3(C6 H12 O6) FORMUL 14 MAN C6 H12 O6 FORMUL 30 SCN 9(C N S 1-) FORMUL 51 HOH *105(H2 O) HELIX 1 AA1 SER A 56 ILE A 61 5 6 HELIX 2 AA2 VAL A 91 GLY A 94 5 4 HELIX 3 AA3 ASN A 328 VAL A 333 5 6 HELIX 4 AA4 LEU A 345 ASN A 350 1 6 HELIX 5 AA5 ASP A 361 VAL A 371 5 11 HELIX 6 AA6 PHE A 390 SER A 394 5 5 HELIX 7 AA7 ASN A 450 LEU A 455 1 6 HELIX 8 AA8 PRO A 470 GLY A 478 1 9 HELIX 9 AA9 GLY A 550 CYS A 554 5 5 HELIX 10 AB1 LEU B 55 GLN B 59 5 5 HELIX 11 AB2 ASP B 143 ILE B 147 5 5 HELIX 12 AB3 ASN B 203 CYS B 207 5 5 HELIX 13 AB4 ASN B 328 VAL B 333 5 6 HELIX 14 AB5 LEU B 345 GLY B 351 1 7 HELIX 15 AB6 ASP B 361 VAL B 371 5 11 HELIX 16 AB7 PHE B 390 SER B 394 5 5 HELIX 17 AB8 ASN B 450 LEU B 455 1 6 HELIX 18 AB9 PRO B 470 GLY B 478 1 9 HELIX 19 AC1 GLY B 494 CYS B 498 5 5 HELIX 20 AC2 GLY B 550 CYS B 554 5 5 HELIX 21 AC3 GLU B 606 CYS B 610 5 5 HELIX 22 AC4 ASP C 54 GLN C 59 5 6 HELIX 23 AC5 VAL C 91 GLY C 94 5 4 HELIX 24 AC6 ASN C 328 PHE C 332 5 5 HELIX 25 AC7 LEU C 345 ASN C 350 1 6 HELIX 26 AC8 ASP C 361 VAL C 371 5 11 HELIX 27 AC9 PHE C 390 SER C 394 5 5 HELIX 28 AD1 ASN C 450 LEU C 455 1 6 HELIX 29 AD2 PRO C 470 GLU C 477 1 8 HELIX 30 AD3 GLY C 494 CYS C 498 5 5 HELIX 31 AD4 LEU D 55 GLN D 59 5 5 HELIX 32 AD5 VAL D 91 GLY D 94 5 4 HELIX 33 AD6 ASP D 143 ILE D 147 5 5 HELIX 34 AD7 ASN D 203 CYS D 207 5 5 HELIX 35 AD8 ASN D 328 PHE D 332 5 5 HELIX 36 AD9 LEU D 345 ASN D 350 1 6 HELIX 37 AE1 ASP D 361 VAL D 371 5 11 HELIX 38 AE2 PHE D 390 SER D 394 5 5 HELIX 39 AE3 ASN D 450 LEU D 455 1 6 HELIX 40 AE4 PRO D 470 GLY D 478 1 9 HELIX 41 AE5 GLY D 494 CYS D 498 5 5 HELIX 42 AE6 GLY D 550 CYS D 554 5 5 HELIX 43 AE7 GLU D 606 CYS D 610 5 5 HELIX 44 AE8 GLU E 84 VAL E 88 5 5 HELIX 45 AE9 SER E 127 GLY E 134 1 8 HELIX 46 AF1 LYS E 189 HIS E 195 1 7 HELIX 47 AF2 GLU F 84 VAL F 88 5 5 HELIX 48 AF3 SER F 127 LYS F 132 1 6 HELIX 49 AF4 LYS F 189 HIS F 195 1 7 HELIX 50 AF5 GLU G 84 VAL G 88 5 5 HELIX 51 AF6 SER G 127 LYS G 132 1 6 HELIX 52 AF7 LYS G 189 HIS G 195 1 7 HELIX 53 AF8 GLU H 84 VAL H 88 5 5 HELIX 54 AF9 SER H 127 LYS H 132 1 6 HELIX 55 AG1 LYS H 189 HIS H 195 1 7 HELIX 56 AG2 ASP I 308 THR I 312 5 5 HELIX 57 AG3 SER I 383 ALA I 385 5 3 HELIX 58 AG4 SER I 414 LEU I 416 5 3 HELIX 59 AG5 LYS I 428 ASN I 431 5 4 HELIX 60 AG6 ASP J 308 THR J 312 5 5 HELIX 61 AG7 SER J 383 ALA J 385 5 3 HELIX 62 AG8 SER J 414 GLY J 417 5 4 HELIX 63 AG9 LYS J 428 ASN J 431 5 4 HELIX 64 AH1 THR K 295 LYS K 297 5 3 HELIX 65 AH2 ASP K 308 THR K 312 5 5 HELIX 66 AH3 SER K 383 ALA K 385 5 3 HELIX 67 AH4 SER K 414 LEU K 416 5 3 HELIX 68 AH5 LYS K 428 ASN K 431 5 4 HELIX 69 AH6 ASP L 308 THR L 312 5 5 HELIX 70 AH7 SER L 383 ALA L 385 5 3 HELIX 71 AH8 PRO L 412 GLY L 417 5 6 HELIX 72 AH9 LYS L 428 ASN L 431 5 4 SHEET 1 AA1 5 VAL A 9 PRO A 11 0 SHEET 2 AA1 5 VAL A 39 MET A 41 1 O MET A 41 N CYS A 10 SHEET 3 AA1 5 GLU A 63 VAL A 64 1 O GLU A 63 N VAL A 40 SHEET 4 AA1 5 VAL A 85 VAL A 86 1 O VAL A 85 N VAL A 64 SHEET 5 AA1 5 GLU A 122 ILE A 123 1 O GLU A 122 N VAL A 86 SHEET 1 AA2 5 LEU A 44 VAL A 47 0 SHEET 2 AA2 5 VAL A 68 ALA A 71 1 O LEU A 69 N LEU A 44 SHEET 3 AA2 5 PHE A 96 MET A 101 1 O MET A 101 N VAL A 70 SHEET 4 AA2 5 GLY A 127 GLU A 131 1 O TYR A 129 N VAL A 100 SHEET 5 AA2 5 ILE A 155 LYS A 158 1 O VAL A 156 N ILE A 130 SHEET 1 AA3 2 THR A 77 PRO A 79 0 SHEET 2 AA3 2 GLN A 114 ARG A 116 1 O ARG A 116 N LEU A 78 SHEET 1 AA4 2 CYS A 212 CYS A 216 0 SHEET 2 AA4 2 CYS A 224 CYS A 227 -1 O ALA A 226 N ALA A 213 SHEET 1 AA5 2 PHE A 230 ASP A 232 0 SHEET 2 AA5 2 ALA A 235 VAL A 237 -1 O ALA A 235 N ASP A 232 SHEET 1 AA6 2 LEU A 244 ASN A 247 0 SHEET 2 AA6 2 GLN A 252 PRO A 255 -1 O GLN A 252 N ASN A 247 SHEET 1 AA7 2 TYR A 261 TYR A 263 0 SHEET 2 AA7 2 VAL A 266 VAL A 268 -1 O VAL A 266 N TYR A 263 SHEET 1 AA8 2 VAL A 276 VAL A 277 0 SHEET 2 AA8 2 CYS A 282 VAL A 283 -1 O VAL A 283 N VAL A 276 SHEET 1 AA9 2 LYS A 290 VAL A 293 0 SHEET 2 AA9 2 MET A 300 PRO A 303 -1 O GLU A 302 N MET A 291 SHEET 1 AB1 5 LEU A 342 PHE A 344 0 SHEET 2 AB1 5 LEU A 378 ILE A 380 1 O ASN A 379 N LEU A 342 SHEET 3 AB1 5 PHE A 409 MET A 414 1 O LEU A 412 N ILE A 380 SHEET 4 AB1 5 ARG A 434 SER A 438 1 O TYR A 436 N ILE A 413 SHEET 5 AB1 5 LEU A 463 LYS A 466 1 O ASP A 464 N ILE A 435 SHEET 1 AB2 3 GLU A 373 ILE A 374 0 SHEET 2 AB2 3 THR A 398 ILE A 399 1 O THR A 398 N ILE A 374 SHEET 3 AB2 3 GLU A 429 ILE A 430 1 O GLU A 429 N ILE A 399 SHEET 1 AB3 2 TYR A 504 ARG A 506 0 SHEET 2 AB3 2 VAL A 509 VAL A 511 -1 O VAL A 511 N TYR A 504 SHEET 1 AB4 2 GLU A 523 HIS A 526 0 SHEET 2 AB4 2 GLU A 529 SER A 532 -1 O GLU A 529 N HIS A 526 SHEET 1 AB5 2 PHE A 560 ASP A 562 0 SHEET 2 AB5 2 HIS A 565 VAL A 567 -1 O VAL A 567 N PHE A 560 SHEET 1 AB6 3 HIS A 572 LEU A 575 0 SHEET 2 AB6 3 PRO A 580 PRO A 585 -1 O ILE A 581 N VAL A 574 SHEET 3 AB6 3 CYS A 591 PRO A 593 -1 O ARG A 592 N TYR A 584 SHEET 1 AB7 5 VAL B 9 CYS B 10 0 SHEET 2 AB7 5 VAL B 39 VAL B 40 1 O VAL B 39 N CYS B 10 SHEET 3 AB7 5 GLU B 63 VAL B 64 1 O GLU B 63 N VAL B 40 SHEET 4 AB7 5 VAL B 85 VAL B 86 1 O VAL B 85 N VAL B 64 SHEET 5 AB7 5 GLU B 122 ILE B 123 1 O GLU B 122 N VAL B 86 SHEET 1 AB8 5 LEU B 44 VAL B 47 0 SHEET 2 AB8 5 VAL B 68 ALA B 71 1 O LEU B 69 N ILE B 46 SHEET 3 AB8 5 PHE B 96 MET B 101 1 O PHE B 99 N VAL B 70 SHEET 4 AB8 5 GLY B 127 GLU B 131 1 O GLY B 127 N ALA B 97 SHEET 5 AB8 5 ILE B 155 LYS B 158 1 O VAL B 156 N VAL B 128 SHEET 1 AB9 2 THR B 77 PRO B 79 0 SHEET 2 AB9 2 GLN B 114 ARG B 116 1 O GLN B 114 N LEU B 78 SHEET 1 AC1 2 CYS B 212 CYS B 216 0 SHEET 2 AC1 2 CYS B 224 CYS B 227 -1 O ALA B 226 N ALA B 213 SHEET 1 AC2 2 PHE B 230 ASP B 232 0 SHEET 2 AC2 2 ALA B 235 VAL B 237 -1 O ALA B 235 N ASP B 232 SHEET 1 AC3 2 LEU B 244 ASN B 247 0 SHEET 2 AC3 2 GLN B 252 PRO B 255 -1 O GLU B 254 N VAL B 245 SHEET 1 AC4 2 TYR B 261 TYR B 263 0 SHEET 2 AC4 2 VAL B 266 VAL B 268 -1 O VAL B 268 N TYR B 261 SHEET 1 AC5 2 VAL B 276 VAL B 277 0 SHEET 2 AC5 2 CYS B 282 VAL B 283 -1 O VAL B 283 N VAL B 276 SHEET 1 AC6 2 LYS B 290 LYS B 295 0 SHEET 2 AC6 2 LEU B 298 PRO B 303 -1 O LEU B 298 N LYS B 295 SHEET 1 AC7 5 ALA B 311 CYS B 312 0 SHEET 2 AC7 5 LYS B 337 ILE B 338 1 O LYS B 337 N CYS B 312 SHEET 3 AC7 5 GLU B 373 ILE B 374 1 O GLU B 373 N ILE B 338 SHEET 4 AC7 5 THR B 398 ILE B 399 1 O THR B 398 N ILE B 374 SHEET 5 AC7 5 GLU B 429 ILE B 430 1 O GLU B 429 N ILE B 399 SHEET 1 AC8 5 LEU B 342 PHE B 344 0 SHEET 2 AC8 5 LEU B 378 ILE B 380 1 O ASN B 379 N LEU B 342 SHEET 3 AC8 5 PHE B 409 MET B 414 1 O LEU B 412 N ILE B 380 SHEET 4 AC8 5 ARG B 434 SER B 438 1 O TYR B 436 N ILE B 413 SHEET 5 AC8 5 LEU B 463 LYS B 466 1 O ASP B 464 N ILE B 435 SHEET 1 AC9 2 TYR B 504 ARG B 506 0 SHEET 2 AC9 2 VAL B 509 VAL B 511 -1 O VAL B 511 N TYR B 504 SHEET 1 AD1 2 GLU B 523 HIS B 526 0 SHEET 2 AD1 2 GLU B 529 SER B 532 -1 O GLU B 529 N HIS B 526 SHEET 1 AD2 2 PHE B 560 ASP B 562 0 SHEET 2 AD2 2 HIS B 565 VAL B 567 -1 O VAL B 567 N PHE B 560 SHEET 1 AD3 3 HIS B 572 VAL B 574 0 SHEET 2 AD3 3 ILE B 581 PRO B 585 -1 O ILE B 581 N VAL B 574 SHEET 3 AD3 3 CYS B 591 PRO B 593 -1 O ARG B 592 N TYR B 584 SHEET 1 AD4 4 VAL C 39 VAL C 40 0 SHEET 2 AD4 4 GLU C 63 VAL C 64 1 O GLU C 63 N VAL C 40 SHEET 3 AD4 4 VAL C 85 VAL C 86 1 O VAL C 85 N VAL C 64 SHEET 4 AD4 4 GLU C 122 ILE C 123 1 O GLU C 122 N VAL C 86 SHEET 1 AD5 5 LEU C 44 VAL C 47 0 SHEET 2 AD5 5 VAL C 68 ALA C 71 1 O LEU C 69 N LEU C 44 SHEET 3 AD5 5 PHE C 96 MET C 101 1 O MET C 101 N VAL C 70 SHEET 4 AD5 5 GLY C 127 GLU C 131 1 O TYR C 129 N VAL C 100 SHEET 5 AD5 5 ILE C 155 LYS C 158 1 O VAL C 156 N ILE C 130 SHEET 1 AD6 2 THR C 77 PRO C 79 0 SHEET 2 AD6 2 GLN C 114 ARG C 116 1 O ARG C 116 N LEU C 78 SHEET 1 AD7 4 ALA C 235 VAL C 237 0 SHEET 2 AD7 4 PHE C 230 ASP C 232 -1 N ASP C 232 O ALA C 235 SHEET 3 AD7 4 VAL C 266 VAL C 268 1 O CYS C 267 N ASN C 231 SHEET 4 AD7 4 TYR C 261 TYR C 263 -1 N TYR C 261 O VAL C 268 SHEET 1 AD8 2 VAL C 245 TYR C 246 0 SHEET 2 AD8 2 LEU C 253 GLU C 254 -1 O GLU C 254 N VAL C 245 SHEET 1 AD9 2 VAL C 276 ASP C 278 0 SHEET 2 AD9 2 SER C 281 VAL C 283 -1 O VAL C 283 N VAL C 276 SHEET 1 AE1 2 LYS C 290 LYS C 295 0 SHEET 2 AE1 2 LEU C 298 PRO C 303 -1 O MET C 300 N VAL C 293 SHEET 1 AE2 5 LEU C 342 PHE C 344 0 SHEET 2 AE2 5 LEU C 378 ILE C 380 1 O ASN C 379 N LEU C 342 SHEET 3 AE2 5 PHE C 409 MET C 414 1 O LEU C 412 N ILE C 380 SHEET 4 AE2 5 ARG C 434 SER C 438 1 O TYR C 436 N ILE C 413 SHEET 5 AE2 5 LEU C 463 LYS C 466 1 O ASP C 464 N ILE C 435 SHEET 1 AE3 3 GLU C 373 ILE C 374 0 SHEET 2 AE3 3 THR C 398 ILE C 399 1 O THR C 398 N ILE C 374 SHEET 3 AE3 3 GLU C 429 ILE C 430 1 O GLU C 429 N ILE C 399 SHEET 1 AE4 2 TYR C 504 ARG C 506 0 SHEET 2 AE4 2 VAL C 509 VAL C 511 -1 O VAL C 511 N TYR C 504 SHEET 1 AE5 2 PHE C 524 HIS C 526 0 SHEET 2 AE5 2 GLU C 529 PHE C 531 -1 O PHE C 531 N PHE C 524 SHEET 1 AE6 5 VAL D 9 CYS D 10 0 SHEET 2 AE6 5 VAL D 39 VAL D 40 1 O VAL D 39 N CYS D 10 SHEET 3 AE6 5 GLU D 63 VAL D 64 1 O GLU D 63 N VAL D 40 SHEET 4 AE6 5 VAL D 85 VAL D 86 1 O VAL D 85 N VAL D 64 SHEET 5 AE6 5 GLU D 122 ILE D 123 1 O GLU D 122 N VAL D 86 SHEET 1 AE7 5 LEU D 44 VAL D 47 0 SHEET 2 AE7 5 VAL D 68 ALA D 71 1 O LEU D 69 N ILE D 46 SHEET 3 AE7 5 PHE D 96 MET D 101 1 O PHE D 99 N VAL D 70 SHEET 4 AE7 5 GLY D 127 GLU D 131 1 O TYR D 129 N VAL D 100 SHEET 5 AE7 5 ILE D 155 LYS D 158 1 O VAL D 156 N ILE D 130 SHEET 1 AE8 2 THR D 77 LEU D 78 0 SHEET 2 AE8 2 GLN D 114 LEU D 115 1 O GLN D 114 N LEU D 78 SHEET 1 AE9 2 CYS D 212 CYS D 216 0 SHEET 2 AE9 2 CYS D 224 CYS D 227 -1 O ALA D 226 N ALA D 213 SHEET 1 AF1 2 PHE D 230 ASP D 232 0 SHEET 2 AF1 2 ALA D 235 VAL D 237 -1 O VAL D 237 N PHE D 230 SHEET 1 AF2 2 LEU D 244 ASN D 247 0 SHEET 2 AF2 2 GLN D 252 PRO D 255 -1 O GLU D 254 N VAL D 245 SHEET 1 AF3 2 TYR D 261 TYR D 263 0 SHEET 2 AF3 2 VAL D 266 VAL D 268 -1 O VAL D 268 N TYR D 261 SHEET 1 AF4 2 VAL D 276 ASP D 278 0 SHEET 2 AF4 2 SER D 281 VAL D 283 -1 O SER D 281 N ASP D 278 SHEET 1 AF5 2 LYS D 290 LYS D 295 0 SHEET 2 AF5 2 LEU D 298 PRO D 303 -1 O GLU D 302 N MET D 291 SHEET 1 AF6 5 ALA D 311 GLU D 313 0 SHEET 2 AF6 5 LYS D 337 LEU D 339 1 O LEU D 339 N CYS D 312 SHEET 3 AF6 5 GLU D 373 ILE D 374 1 O GLU D 373 N ILE D 338 SHEET 4 AF6 5 THR D 398 ILE D 399 1 O THR D 398 N ILE D 374 SHEET 5 AF6 5 GLU D 429 ILE D 430 1 O GLU D 429 N ILE D 399 SHEET 1 AF7 5 LEU D 342 PHE D 344 0 SHEET 2 AF7 5 LEU D 378 ILE D 380 1 O ASN D 379 N LEU D 342 SHEET 3 AF7 5 PHE D 409 MET D 414 1 O LEU D 412 N ILE D 380 SHEET 4 AF7 5 ARG D 434 SER D 438 1 O TYR D 436 N ILE D 413 SHEET 5 AF7 5 LEU D 463 LYS D 466 1 O ASP D 464 N ILE D 435 SHEET 1 AF8 4 VAL D 509 VAL D 511 0 SHEET 2 AF8 4 TYR D 504 ARG D 506 -1 N TYR D 504 O VAL D 511 SHEET 3 AF8 4 GLU D 529 SER D 532 1 O CYS D 530 N SER D 505 SHEET 4 AF8 4 GLU D 523 HIS D 526 -1 N PHE D 524 O PHE D 531 SHEET 1 AF9 2 PHE D 560 ASP D 562 0 SHEET 2 AF9 2 HIS D 565 VAL D 567 -1 O VAL D 567 N PHE D 560 SHEET 1 AG1 3 HIS D 572 VAL D 574 0 SHEET 2 AG1 3 ILE D 581 PRO D 585 -1 O ILE D 581 N VAL D 574 SHEET 3 AG1 3 CYS D 591 PRO D 593 -1 O ARG D 592 N TYR D 584 SHEET 1 AG2 4 MET E 4 GLN E 6 0 SHEET 2 AG2 4 ALA E 19 SER E 25 -1 O LYS E 24 N THR E 5 SHEET 3 AG2 4 ASP E 75 ILE E 80 -1 O LEU E 78 N ILE E 21 SHEET 4 AG2 4 PHE E 67 SER E 72 -1 N SER E 70 O THR E 77 SHEET 1 AG3 6 SER E 10 VAL E 13 0 SHEET 2 AG3 6 THR E 107 ILE E 111 1 O GLU E 110 N LEU E 11 SHEET 3 AG3 6 GLY E 89 GLN E 95 -1 N TYR E 91 O THR E 107 SHEET 4 AG3 6 LEU E 38 GLN E 43 -1 N TYR E 41 O TYR E 92 SHEET 5 AG3 6 GLN E 50 TYR E 54 -1 O GLN E 50 N LEU E 42 SHEET 6 AG3 6 ASN E 58 ARG E 59 -1 O ASN E 58 N TYR E 54 SHEET 1 AG4 4 SER E 10 VAL E 13 0 SHEET 2 AG4 4 THR E 107 ILE E 111 1 O GLU E 110 N LEU E 11 SHEET 3 AG4 4 GLY E 89 GLN E 95 -1 N TYR E 91 O THR E 107 SHEET 4 AG4 4 THR E 102 PHE E 103 -1 O THR E 102 N GLN E 95 SHEET 1 AG5 2 LEU E 30 SER E 32 0 SHEET 2 AG5 2 ASN E 35 THR E 36 -1 O ASN E 35 N HIS E 31 SHEET 1 AG6 4 SER E 120 PHE E 124 0 SHEET 2 AG6 4 THR E 135 PHE E 145 -1 O LEU E 141 N PHE E 122 SHEET 3 AG6 4 TYR E 179 SER E 188 -1 O LEU E 181 N LEU E 142 SHEET 4 AG6 4 SER E 165 VAL E 169 -1 N GLN E 166 O THR E 184 SHEET 1 AG7 4 ALA E 159 LEU E 160 0 SHEET 2 AG7 4 ALA E 150 VAL E 156 -1 N VAL E 156 O ALA E 159 SHEET 3 AG7 4 VAL E 197 HIS E 204 -1 O THR E 203 N LYS E 151 SHEET 4 AG7 4 VAL E 211 ASN E 216 -1 O VAL E 211 N VAL E 202 SHEET 1 AG8 4 MET F 4 THR F 7 0 SHEET 2 AG8 4 ALA F 19 SER F 25 -1 O LYS F 24 N THR F 5 SHEET 3 AG8 4 ASP F 75 ILE F 80 -1 O ILE F 80 N ALA F 19 SHEET 4 AG8 4 PHE F 67 SER F 72 -1 N SER F 70 O THR F 77 SHEET 1 AG9 6 SER F 10 VAL F 13 0 SHEET 2 AG9 6 THR F 107 ILE F 111 1 O GLU F 110 N LEU F 11 SHEET 3 AG9 6 GLY F 89 GLN F 95 -1 N GLY F 89 O LEU F 109 SHEET 4 AG9 6 LEU F 38 GLN F 43 -1 N TYR F 41 O TYR F 92 SHEET 5 AG9 6 GLN F 50 TYR F 54 -1 O GLN F 50 N LEU F 42 SHEET 6 AG9 6 ASN F 58 ARG F 59 -1 O ASN F 58 N TYR F 54 SHEET 1 AH1 4 SER F 10 VAL F 13 0 SHEET 2 AH1 4 THR F 107 ILE F 111 1 O GLU F 110 N LEU F 11 SHEET 3 AH1 4 GLY F 89 GLN F 95 -1 N GLY F 89 O LEU F 109 SHEET 4 AH1 4 THR F 102 PHE F 103 -1 O THR F 102 N GLN F 95 SHEET 1 AH2 2 LEU F 30 SER F 32 0 SHEET 2 AH2 2 ASN F 35 THR F 36 -1 O ASN F 35 N HIS F 31 SHEET 1 AH3 4 SER F 120 PHE F 124 0 SHEET 2 AH3 4 THR F 135 PHE F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AH3 4 TYR F 179 SER F 188 -1 O LEU F 181 N LEU F 142 SHEET 4 AH3 4 SER F 165 VAL F 169 -1 N GLN F 166 O THR F 184 SHEET 1 AH4 4 ALA F 159 LEU F 160 0 SHEET 2 AH4 4 ALA F 150 VAL F 156 -1 N VAL F 156 O ALA F 159 SHEET 3 AH4 4 TYR F 198 HIS F 204 -1 O THR F 203 N LYS F 151 SHEET 4 AH4 4 VAL F 211 PHE F 215 -1 O VAL F 211 N VAL F 202 SHEET 1 AH5 4 MET G 4 THR G 7 0 SHEET 2 AH5 4 ALA G 19 SER G 25 -1 O SER G 22 N THR G 7 SHEET 3 AH5 4 ASP G 75 ILE G 80 -1 O LEU G 78 N ILE G 21 SHEET 4 AH5 4 PHE G 67 SER G 72 -1 N SER G 70 O THR G 77 SHEET 1 AH6 6 SER G 10 VAL G 13 0 SHEET 2 AH6 6 THR G 107 ILE G 111 1 O GLU G 110 N LEU G 11 SHEET 3 AH6 6 GLY G 89 GLN G 95 -1 N TYR G 91 O THR G 107 SHEET 4 AH6 6 LEU G 38 GLN G 43 -1 N GLN G 43 O VAL G 90 SHEET 5 AH6 6 GLN G 50 TYR G 54 -1 O GLN G 50 N LEU G 42 SHEET 6 AH6 6 ASN G 58 ARG G 59 -1 O ASN G 58 N TYR G 54 SHEET 1 AH7 4 SER G 10 VAL G 13 0 SHEET 2 AH7 4 THR G 107 ILE G 111 1 O GLU G 110 N LEU G 11 SHEET 3 AH7 4 GLY G 89 GLN G 95 -1 N TYR G 91 O THR G 107 SHEET 4 AH7 4 THR G 102 PHE G 103 -1 O THR G 102 N GLN G 95 SHEET 1 AH8 2 LEU G 30 SER G 32 0 SHEET 2 AH8 2 ASN G 35 THR G 36 -1 O ASN G 35 N SER G 32 SHEET 1 AH9 4 SER G 120 PHE G 124 0 SHEET 2 AH9 4 THR G 135 PHE G 145 -1 O LEU G 141 N PHE G 122 SHEET 3 AH9 4 TYR G 179 SER G 188 -1 O LEU G 181 N LEU G 142 SHEET 4 AH9 4 SER G 165 VAL G 169 -1 N GLN G 166 O THR G 184 SHEET 1 AI1 4 ALA G 159 GLN G 161 0 SHEET 2 AI1 4 ALA G 150 VAL G 156 -1 N VAL G 156 O ALA G 159 SHEET 3 AI1 4 VAL G 197 HIS G 204 -1 O GLU G 201 N GLN G 153 SHEET 4 AI1 4 VAL G 211 ASN G 216 -1 O VAL G 211 N VAL G 202 SHEET 1 AI2 4 MET H 4 THR H 7 0 SHEET 2 AI2 4 ALA H 19 SER H 25 -1 O LYS H 24 N THR H 5 SHEET 3 AI2 4 ASP H 75 ILE H 80 -1 O PHE H 76 N CYS H 23 SHEET 4 AI2 4 PHE H 67 SER H 72 -1 N SER H 70 O THR H 77 SHEET 1 AI3 6 SER H 10 VAL H 13 0 SHEET 2 AI3 6 THR H 107 ILE H 111 1 O GLU H 110 N LEU H 11 SHEET 3 AI3 6 GLY H 89 GLN H 95 -1 N GLY H 89 O LEU H 109 SHEET 4 AI3 6 LEU H 38 GLN H 43 -1 N TYR H 41 O TYR H 92 SHEET 5 AI3 6 GLN H 50 TYR H 54 -1 O LEU H 52 N TRP H 40 SHEET 6 AI3 6 ASN H 58 ARG H 59 -1 O ASN H 58 N TYR H 54 SHEET 1 AI4 4 SER H 10 VAL H 13 0 SHEET 2 AI4 4 THR H 107 ILE H 111 1 O GLU H 110 N LEU H 11 SHEET 3 AI4 4 GLY H 89 GLN H 95 -1 N GLY H 89 O LEU H 109 SHEET 4 AI4 4 THR H 102 PHE H 103 -1 O THR H 102 N GLN H 95 SHEET 1 AI5 2 LEU H 30 SER H 32 0 SHEET 2 AI5 2 ASN H 35 THR H 36 -1 O ASN H 35 N HIS H 31 SHEET 1 AI6 4 VAL H 121 PHE H 124 0 SHEET 2 AI6 4 THR H 135 PHE H 145 -1 O VAL H 139 N PHE H 124 SHEET 3 AI6 4 TYR H 179 SER H 188 -1 O LEU H 181 N LEU H 142 SHEET 4 AI6 4 SER H 165 VAL H 169 -1 N SER H 168 O SER H 182 SHEET 1 AI7 4 ALA H 159 LEU H 160 0 SHEET 2 AI7 4 VAL H 152 VAL H 156 -1 N VAL H 156 O ALA H 159 SHEET 3 AI7 4 VAL H 197 VAL H 202 -1 O ALA H 199 N LYS H 155 SHEET 4 AI7 4 VAL H 211 ASN H 216 -1 O PHE H 215 N TYR H 198 SHEET 1 AI8 4 THR I 223 SER I 227 0 SHEET 2 AI8 4 LEU I 238 SER I 245 -1 O THR I 241 N SER I 227 SHEET 3 AI8 4 GLN I 299 MET I 304 -1 O VAL I 300 N CYS I 242 SHEET 4 AI8 4 LEU I 289 ASP I 294 -1 N ASP I 294 O GLN I 299 SHEET 1 AI9 6 LEU I 231 VAL I 232 0 SHEET 2 AI9 6 THR I 334 VAL I 338 1 O THR I 337 N VAL I 232 SHEET 3 AI9 6 ALA I 313 ILE I 320 -1 N ALA I 313 O VAL I 336 SHEET 4 AI9 6 GLY I 255 GLN I 261 -1 N ILE I 259 O TYR I 316 SHEET 5 AI9 6 GLU I 268 TRP I 274 -1 O ILE I 273 N VAL I 256 SHEET 6 AI9 6 LYS I 279 TYR I 281 -1 O TYR I 280 N ASN I 272 SHEET 1 AJ1 4 LEU I 231 VAL I 232 0 SHEET 2 AJ1 4 THR I 334 VAL I 338 1 O THR I 337 N VAL I 232 SHEET 3 AJ1 4 ALA I 313 ILE I 320 -1 N ALA I 313 O VAL I 336 SHEET 4 AJ1 4 VAL I 329 TRP I 330 -1 O VAL I 329 N GLN I 319 SHEET 1 AJ2 4 SER I 347 LEU I 351 0 SHEET 2 AJ2 4 THR I 362 TYR I 372 -1 O GLY I 366 N LEU I 351 SHEET 3 AJ2 4 TYR I 403 PRO I 412 -1 O TYR I 403 N TYR I 372 SHEET 4 AJ2 4 HIS I 391 THR I 392 -1 N HIS I 391 O VAL I 408 SHEET 1 AJ3 4 SER I 347 LEU I 351 0 SHEET 2 AJ3 4 THR I 362 TYR I 372 -1 O GLY I 366 N LEU I 351 SHEET 3 AJ3 4 TYR I 403 PRO I 412 -1 O TYR I 403 N TYR I 372 SHEET 4 AJ3 4 VAL I 396 LEU I 397 -1 N VAL I 396 O SER I 404 SHEET 1 AJ4 3 THR I 378 TRP I 381 0 SHEET 2 AJ4 3 TYR I 421 HIS I 427 -1 O ASN I 424 N SER I 380 SHEET 3 AJ4 3 THR I 432 VAL I 438 -1 O VAL I 434 N VAL I 425 SHEET 1 AJ5 4 THR J 223 SER J 227 0 SHEET 2 AJ5 4 LEU J 238 SER J 245 -1 O THR J 243 N ARG J 225 SHEET 3 AJ5 4 GLN J 299 MET J 304 -1 O VAL J 300 N CYS J 242 SHEET 4 AJ5 4 LEU J 289 ASP J 294 -1 N SER J 292 O VAL J 301 SHEET 1 AJ6 6 LEU J 231 VAL J 232 0 SHEET 2 AJ6 6 THR J 334 VAL J 338 1 O THR J 337 N VAL J 232 SHEET 3 AJ6 6 ALA J 313 ILE J 320 -1 N TYR J 315 O THR J 334 SHEET 4 AJ6 6 GLY J 255 GLN J 261 -1 N ILE J 259 O TYR J 316 SHEET 5 AJ6 6 GLU J 268 TRP J 274 -1 O ALA J 271 N TRP J 258 SHEET 6 AJ6 6 LYS J 279 TYR J 281 -1 O TYR J 280 N ASN J 272 SHEET 1 AJ7 4 LEU J 231 VAL J 232 0 SHEET 2 AJ7 4 THR J 334 VAL J 338 1 O THR J 337 N VAL J 232 SHEET 3 AJ7 4 ALA J 313 ILE J 320 -1 N TYR J 315 O THR J 334 SHEET 4 AJ7 4 VAL J 329 TRP J 330 -1 O VAL J 329 N GLN J 319 SHEET 1 AJ8 4 VAL J 348 LEU J 351 0 SHEET 2 AJ8 4 THR J 362 TYR J 372 -1 O GLY J 366 N LEU J 351 SHEET 3 AJ8 4 TYR J 403 PRO J 412 -1 O TYR J 403 N TYR J 372 SHEET 4 AJ8 4 VAL J 390 THR J 392 -1 N HIS J 391 O VAL J 408 SHEET 1 AJ9 4 VAL J 348 LEU J 351 0 SHEET 2 AJ9 4 THR J 362 TYR J 372 -1 O GLY J 366 N LEU J 351 SHEET 3 AJ9 4 TYR J 403 PRO J 412 -1 O TYR J 403 N TYR J 372 SHEET 4 AJ9 4 VAL J 396 LEU J 397 -1 N VAL J 396 O SER J 404 SHEET 1 AK1 3 THR J 378 TRP J 381 0 SHEET 2 AK1 3 ILE J 422 HIS J 427 -1 O ASN J 424 N SER J 380 SHEET 3 AK1 3 THR J 432 LYS J 437 -1 O THR J 432 N HIS J 427 SHEET 1 AK2 4 THR K 223 SER K 227 0 SHEET 2 AK2 4 LEU K 238 SER K 245 -1 O THR K 243 N ARG K 225 SHEET 3 AK2 4 GLN K 299 MET K 304 -1 O VAL K 300 N CYS K 242 SHEET 4 AK2 4 THR K 290 ASP K 294 -1 N SER K 292 O VAL K 301 SHEET 1 AK3 6 LEU K 231 VAL K 232 0 SHEET 2 AK3 6 THR K 334 VAL K 338 1 O THR K 337 N VAL K 232 SHEET 3 AK3 6 ALA K 313 ILE K 320 -1 N ALA K 313 O VAL K 336 SHEET 4 AK3 6 GLY K 255 GLN K 261 -1 N ILE K 259 O TYR K 316 SHEET 5 AK3 6 GLU K 268 TRP K 274 -1 O LEU K 270 N TRP K 258 SHEET 6 AK3 6 LYS K 279 TYR K 281 -1 O TYR K 280 N ASN K 272 SHEET 1 AK4 4 LEU K 231 VAL K 232 0 SHEET 2 AK4 4 THR K 334 VAL K 338 1 O THR K 337 N VAL K 232 SHEET 3 AK4 4 ALA K 313 ILE K 320 -1 N ALA K 313 O VAL K 336 SHEET 4 AK4 4 VAL K 329 TRP K 330 -1 O VAL K 329 N GLN K 319 SHEET 1 AK5 4 VAL K 348 LEU K 351 0 SHEET 2 AK5 4 THR K 362 TYR K 372 -1 O GLY K 366 N LEU K 351 SHEET 3 AK5 4 TYR K 403 PRO K 412 -1 O VAL K 411 N ALA K 363 SHEET 4 AK5 4 VAL K 390 THR K 392 -1 N HIS K 391 O VAL K 408 SHEET 1 AK6 4 VAL K 348 LEU K 351 0 SHEET 2 AK6 4 THR K 362 TYR K 372 -1 O GLY K 366 N LEU K 351 SHEET 3 AK6 4 TYR K 403 PRO K 412 -1 O VAL K 411 N ALA K 363 SHEET 4 AK6 4 VAL K 396 LEU K 397 -1 N VAL K 396 O SER K 404 SHEET 1 AK7 3 THR K 378 TRP K 381 0 SHEET 2 AK7 3 TYR K 421 HIS K 427 -1 O ASN K 424 N SER K 380 SHEET 3 AK7 3 THR K 432 VAL K 438 -1 O THR K 432 N HIS K 427 SHEET 1 AK8 4 THR L 223 SER L 227 0 SHEET 2 AK8 4 LEU L 238 SER L 245 -1 O SER L 245 N THR L 223 SHEET 3 AK8 4 GLN L 299 MET L 304 -1 O VAL L 300 N CYS L 242 SHEET 4 AK8 4 THR L 290 ASP L 294 -1 N ASP L 294 O GLN L 299 SHEET 1 AK9 6 LEU L 231 VAL L 232 0 SHEET 2 AK9 6 THR L 334 VAL L 338 1 O THR L 337 N VAL L 232 SHEET 3 AK9 6 ALA L 313 ILE L 320 -1 N ALA L 313 O VAL L 336 SHEET 4 AK9 6 GLY L 255 GLN L 261 -1 N ILE L 259 O TYR L 316 SHEET 5 AK9 6 GLU L 268 TRP L 274 -1 O GLU L 268 N ARG L 260 SHEET 6 AK9 6 LYS L 279 TYR L 281 -1 O TYR L 280 N ASN L 272 SHEET 1 AL1 4 LEU L 231 VAL L 232 0 SHEET 2 AL1 4 THR L 334 VAL L 338 1 O THR L 337 N VAL L 232 SHEET 3 AL1 4 ALA L 313 ILE L 320 -1 N ALA L 313 O VAL L 336 SHEET 4 AL1 4 VAL L 329 TRP L 330 -1 O VAL L 329 N GLN L 319 SHEET 1 AL2 4 SER L 347 LEU L 351 0 SHEET 2 AL2 4 ALA L 363 TYR L 372 -1 O LYS L 370 N SER L 347 SHEET 3 AL2 4 TYR L 403 VAL L 411 -1 O LEU L 405 N VAL L 369 SHEET 4 AL2 4 VAL L 390 THR L 392 -1 N HIS L 391 O VAL L 408 SHEET 1 AL3 4 SER L 347 LEU L 351 0 SHEET 2 AL3 4 ALA L 363 TYR L 372 -1 O LYS L 370 N SER L 347 SHEET 3 AL3 4 TYR L 403 VAL L 411 -1 O LEU L 405 N VAL L 369 SHEET 4 AL3 4 VAL L 396 LEU L 397 -1 N VAL L 396 O SER L 404 SHEET 1 AL4 3 THR L 378 TRP L 381 0 SHEET 2 AL4 3 TYR L 421 ASN L 426 -1 O ASN L 424 N SER L 380 SHEET 3 AL4 3 LYS L 433 VAL L 438 -1 O LYS L 436 N CYS L 423 SSBOND 1 CYS A 10 CYS A 37 1555 1555 2.02 SSBOND 2 CYS A 137 CYS A 164 1555 1555 2.03 SSBOND 3 CYS A 167 CYS A 175 1555 1555 2.03 SSBOND 4 CYS A 171 CYS A 183 1555 1555 2.03 SSBOND 5 CYS A 191 CYS A 199 1555 1555 2.03 SSBOND 6 CYS A 195 CYS A 207 1555 1555 2.03 SSBOND 7 CYS A 208 CYS A 216 1555 1555 2.03 SSBOND 8 CYS A 212 CYS A 224 1555 1555 2.03 SSBOND 9 CYS A 227 CYS A 236 1555 1555 2.03 SSBOND 10 CYS A 240 CYS A 267 1555 1555 2.03 SSBOND 11 CYS A 271 CYS A 282 1555 1555 2.03 SSBOND 12 CYS A 286 CYS A 301 1555 1555 2.03 SSBOND 13 CYS A 304 CYS A 308 1555 1555 2.02 SSBOND 14 CYS A 312 CYS A 335 1555 1555 2.03 SSBOND 15 CYS A 444 CYS A 474 1555 1555 2.03 SSBOND 16 CYS A 481 CYS A 490 1555 1555 2.03 SSBOND 17 CYS A 485 CYS A 498 1555 1555 2.03 SSBOND 18 CYS A 501 CYS A 510 1555 1555 2.03 SSBOND 19 CYS A 514 CYS A 530 1555 1555 2.03 SSBOND 20 CYS A 533 CYS A 546 1555 1555 2.03 SSBOND 21 CYS A 537 CYS A 554 1555 1555 2.03 SSBOND 22 CYS A 557 CYS A 566 1555 1555 2.01 SSBOND 23 CYS A 570 CYS A 591 1555 1555 2.03 SSBOND 24 CYS A 594 CYS A 602 1555 1555 2.03 SSBOND 25 CYS A 598 CYS A 610 1555 1555 2.03 SSBOND 26 CYS B 10 CYS B 37 1555 1555 2.04 SSBOND 27 CYS B 137 CYS B 164 1555 1555 2.03 SSBOND 28 CYS B 167 CYS B 175 1555 1555 2.03 SSBOND 29 CYS B 171 CYS B 183 1555 1555 2.03 SSBOND 30 CYS B 191 CYS B 199 1555 1555 2.03 SSBOND 31 CYS B 195 CYS B 207 1555 1555 2.03 SSBOND 32 CYS B 208 CYS B 216 1555 1555 2.03 SSBOND 33 CYS B 212 CYS B 224 1555 1555 2.03 SSBOND 34 CYS B 227 CYS B 236 1555 1555 2.03 SSBOND 35 CYS B 240 CYS B 267 1555 1555 2.03 SSBOND 36 CYS B 271 CYS B 282 1555 1555 2.03 SSBOND 37 CYS B 286 CYS B 301 1555 1555 2.03 SSBOND 38 CYS B 304 CYS B 308 1555 1555 2.04 SSBOND 39 CYS B 312 CYS B 335 1555 1555 2.03 SSBOND 40 CYS B 444 CYS B 474 1555 1555 2.03 SSBOND 41 CYS B 481 CYS B 490 1555 1555 2.03 SSBOND 42 CYS B 485 CYS B 498 1555 1555 2.03 SSBOND 43 CYS B 501 CYS B 510 1555 1555 2.03 SSBOND 44 CYS B 514 CYS B 530 1555 1555 2.03 SSBOND 45 CYS B 533 CYS B 546 1555 1555 2.03 SSBOND 46 CYS B 537 CYS B 554 1555 1555 2.03 SSBOND 47 CYS B 557 CYS B 566 1555 1555 2.01 SSBOND 48 CYS B 570 CYS B 591 1555 1555 2.03 SSBOND 49 CYS B 594 CYS B 602 1555 1555 2.03 SSBOND 50 CYS B 598 CYS B 610 1555 1555 2.03 SSBOND 51 CYS C 10 CYS C 37 1555 1555 2.04 SSBOND 52 CYS C 137 CYS C 164 1555 1555 2.02 SSBOND 53 CYS C 167 CYS C 175 1555 1555 2.02 SSBOND 54 CYS C 171 CYS C 183 1555 1555 2.03 SSBOND 55 CYS C 191 CYS C 199 1555 1555 2.03 SSBOND 56 CYS C 195 CYS C 207 1555 1555 2.04 SSBOND 57 CYS C 208 CYS C 216 1555 1555 2.03 SSBOND 58 CYS C 212 CYS C 224 1555 1555 2.03 SSBOND 59 CYS C 227 CYS C 236 1555 1555 2.04 SSBOND 60 CYS C 240 CYS C 267 1555 1555 2.03 SSBOND 61 CYS C 271 CYS C 282 1555 1555 2.03 SSBOND 62 CYS C 286 CYS C 301 1555 1555 2.03 SSBOND 63 CYS C 304 CYS C 308 1555 1555 2.03 SSBOND 64 CYS C 312 CYS C 335 1555 1555 2.03 SSBOND 65 CYS C 444 CYS C 474 1555 1555 2.03 SSBOND 66 CYS C 481 CYS C 490 1555 1555 2.03 SSBOND 67 CYS C 485 CYS C 498 1555 1555 2.03 SSBOND 68 CYS C 501 CYS C 510 1555 1555 2.03 SSBOND 69 CYS C 514 CYS C 530 1555 1555 2.03 SSBOND 70 CYS C 533 CYS C 546 1555 1555 2.03 SSBOND 71 CYS C 537 CYS C 554 1555 1555 2.03 SSBOND 72 CYS D 10 CYS D 37 1555 1555 2.03 SSBOND 73 CYS D 137 CYS D 164 1555 1555 2.03 SSBOND 74 CYS D 167 CYS D 175 1555 1555 2.03 SSBOND 75 CYS D 171 CYS D 183 1555 1555 2.03 SSBOND 76 CYS D 191 CYS D 199 1555 1555 2.03 SSBOND 77 CYS D 195 CYS D 207 1555 1555 2.03 SSBOND 78 CYS D 208 CYS D 216 1555 1555 2.03 SSBOND 79 CYS D 212 CYS D 224 1555 1555 2.03 SSBOND 80 CYS D 227 CYS D 236 1555 1555 2.03 SSBOND 81 CYS D 240 CYS D 267 1555 1555 2.03 SSBOND 82 CYS D 271 CYS D 282 1555 1555 2.03 SSBOND 83 CYS D 286 CYS D 301 1555 1555 2.03 SSBOND 84 CYS D 304 CYS D 308 1555 1555 2.03 SSBOND 85 CYS D 312 CYS D 335 1555 1555 2.03 SSBOND 86 CYS D 444 CYS D 474 1555 1555 2.03 SSBOND 87 CYS D 481 CYS D 490 1555 1555 2.03 SSBOND 88 CYS D 485 CYS D 498 1555 1555 2.03 SSBOND 89 CYS D 501 CYS D 510 1555 1555 2.03 SSBOND 90 CYS D 514 CYS D 530 1555 1555 2.03 SSBOND 91 CYS D 533 CYS D 546 1555 1555 2.03 SSBOND 92 CYS D 537 CYS D 554 1555 1555 2.03 SSBOND 93 CYS D 557 CYS D 566 1555 1555 2.03 SSBOND 94 CYS D 570 CYS D 591 1555 1555 2.03 SSBOND 95 CYS D 594 CYS D 602 1555 1555 2.03 SSBOND 96 CYS D 598 CYS D 610 1555 1555 2.03 SSBOND 97 CYS E 23 CYS E 93 1555 1555 2.04 SSBOND 98 CYS E 140 CYS E 200 1555 1555 2.04 SSBOND 99 CYS E 220 CYS J 443 1555 1555 2.04 SSBOND 100 CYS F 23 CYS F 93 1555 1555 2.04 SSBOND 101 CYS F 140 CYS F 200 1555 1555 2.04 SSBOND 102 CYS F 220 CYS I 443 1555 1555 2.04 SSBOND 103 CYS G 23 CYS G 93 1555 1555 2.02 SSBOND 104 CYS G 140 CYS G 200 1555 1555 2.03 SSBOND 105 CYS G 220 CYS K 443 1555 1555 2.03 SSBOND 106 CYS H 23 CYS H 93 1555 1555 2.04 SSBOND 107 CYS H 140 CYS H 200 1555 1555 2.03 SSBOND 108 CYS I 242 CYS I 317 1555 1555 2.03 SSBOND 109 CYS I 367 CYS I 423 1555 1555 2.03 SSBOND 110 CYS J 242 CYS J 317 1555 1555 2.04 SSBOND 111 CYS J 367 CYS J 423 1555 1555 2.03 SSBOND 112 CYS K 242 CYS K 317 1555 1555 2.03 SSBOND 113 CYS K 367 CYS K 423 1555 1555 2.02 SSBOND 114 CYS L 242 CYS L 317 1555 1555 2.03 SSBOND 115 CYS L 367 CYS L 423 1555 1555 2.03 LINK ND2 ASN A 231 C1 NAG A 701 1555 1555 1.44 LINK ND2 ASN A 334 C1 NAG A 704 1555 1555 1.44 LINK ND2 ASN A 389 C1 NAG N 1 1555 1555 1.41 LINK ND2 ASN A 395 C1 NAG M 1 1555 1555 1.43 LINK ND2 ASN A 418 C1 NAG A 702 1555 1555 1.44 LINK ND2 ASN A 450 C1 NAG A 703 1555 1555 1.44 LINK ND2 ASN A 547 C1 NAG A 706 1555 1555 1.45 LINK ND2 ASN A 597 C1 NAG A 705 1555 1555 1.44 LINK ND2 ASN B 231 C1 NAG B 701 1555 1555 1.44 LINK ND2 ASN B 334 C1 NAG B 706 1555 1555 1.44 LINK ND2 ASN B 389 C1 NAG O 1 1555 1555 1.44 LINK ND2 ASN B 395 C1 NAG B 702 1555 1555 1.45 LINK ND2 ASN B 418 C1 NAG B 703 1555 1555 1.43 LINK ND2 ASN B 450 C1 NAG B 704 1555 1555 1.45 LINK ND2 ASN B 503 C1 NAG B 705 1555 1555 1.45 LINK ND2 ASN C 231 C1 NAG C 701 1555 1555 1.44 LINK ND2 ASN C 334 C1 NAG C 702 1555 1555 1.44 LINK ND2 ASN C 389 C1 NAG P 1 1555 1555 1.44 LINK ND2 ASN C 395 C1 NAG C 703 1555 1555 1.45 LINK ND2 ASN C 418 C1 NAG C 704 1555 1555 1.44 LINK ND2 ASN C 450 C1 NAG C 705 1555 1555 1.44 LINK ND2 ASN D 231 C1 NAG D 701 1555 1555 1.44 LINK ND2 ASN D 334 C1 NAG D 702 1555 1555 1.45 LINK ND2 ASN D 389 C1 NAG Q 1 1555 1555 1.43 LINK ND2 ASN D 395 C1 NAG D 707 1555 1555 1.45 LINK ND2 ASN D 418 C1 NAG D 703 1555 1555 1.44 LINK ND2 ASN D 450 C1 NAG D 704 1555 1555 1.44 LINK ND2 ASN D 547 C1 NAG D 706 1555 1555 1.46 LINK ND2 ASN D 597 C1 NAG D 705 1555 1555 1.44 LINK O4 NAG M 1 C1 NAG M 2 1555 1555 1.39 LINK O4 NAG M 2 C1 BMA M 3 1555 1555 1.39 LINK O4 NAG N 1 C1 NAG N 2 1555 1555 1.39 LINK O4 NAG N 2 C1 BMA N 3 1555 1555 1.39 LINK O6 BMA N 3 C1 MAN N 4 1555 1555 1.40 LINK O4 NAG O 1 C1 NAG O 2 1555 1555 1.44 LINK O4 NAG O 2 C1 BMA O 3 1555 1555 1.45 LINK O4 NAG P 1 C1 NAG P 2 1555 1555 1.44 LINK O4 NAG Q 1 C1 NAG Q 2 1555 1555 1.44 CISPEP 1 GLU A 520 PRO A 521 0 0.20 CISPEP 2 THR F 7 PRO F 8 0 -10.29 CISPEP 3 VAL F 99 PRO F 100 0 -4.29 CISPEP 4 THR G 7 PRO G 8 0 15.72 CISPEP 5 VAL G 99 PRO G 100 0 1.59 CISPEP 6 TYR G 146 PRO G 147 0 3.05 CISPEP 7 THR H 7 PRO H 8 0 4.67 CISPEP 8 VAL H 99 PRO H 100 0 -14.10 CISPEP 9 PHE L 373 PRO L 374 0 -0.58 CRYST1 98.030 98.810 270.380 90.00 99.21 90.00 P 1 21 1 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 0.010201 0.000000 0.001654 0.00000 SCALE2 0.000000 0.010120 0.000000 0.00000 SCALE3 0.000000 0.000000 0.003747 0.00000