HEADER VIRAL PROTEIN/IMMUNE SYSTEM 18-DEC-24 9ML8 TITLE CRYSTAL STRUCTURE OF THE SARS-COV-2 RBD IN COMPLEX WITH THE RABBIT TITLE 2 M8B-B1 FAB COMPND MOL_ID: 1; COMPND 2 MOLECULE: SPIKE PROTEIN S1; COMPND 3 CHAIN: A, B, C, D; COMPND 4 FRAGMENT: RECEPTOR-BINDING DOMAIN; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: M8B-B1 HEAVY CHAIN; COMPND 8 CHAIN: E, H, M, P; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: M8B-B1 LIGHT CHAIN; COMPND 12 CHAIN: F, L, N, Q; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: SEVERE ACUTE RESPIRATORY SYNDROME CORONAVIRUS SOURCE 3 2; SOURCE 4 ORGANISM_COMMON: SARS-COV-2, 2019-NCOV, COVID-19 VIRUS; SOURCE 5 ORGANISM_TAXID: 2697049; SOURCE 6 GENE: S, 2; SOURCE 7 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 8 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 9 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 10 MOL_ID: 2; SOURCE 11 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 12 ORGANISM_COMMON: RABBIT; SOURCE 13 ORGANISM_TAXID: 9986; SOURCE 14 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 15 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 16 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: ORYCTOLAGUS CUNICULUS; SOURCE 19 ORGANISM_COMMON: RABBIT; SOURCE 20 ORGANISM_TAXID: 9986; SOURCE 21 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 22 EXPRESSION_SYSTEM_COMMON: HUMAN; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 9606 KEYWDS IMMUNE SYSTEM, NEUTRALIZING ANTIBODY, VIRAL PROTEIN-IMMUNE SYSTEM KEYWDS 2 COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR C.FAN,P.J.BJORKMAN REVDAT 1 04-JUN-25 9ML8 0 JRNL AUTH C.FAN,J.R.KEEFFE,K.E.MALECEK,A.A.COHEN,A.P.WEST JR., JRNL AUTH 2 V.A.BAHARANI,A.V.RORICK,H.GAO,P.N.P.GNANAPRAGASAM,S.RHO, JRNL AUTH 3 J.ALVAREZ,L.N.SEGOVIA,T.HATZIIOANNOU,P.D.BIENIASZ, JRNL AUTH 4 P.J.BJORKMAN JRNL TITL CROSS-REACTIVE SARBECOVIRUS ANTIBODIES INDUCED BY MOSAIC RBD JRNL TITL 2 NANOPARTICLES. JRNL REF PROC.NATL.ACAD.SCI.USA V. 122 37122 2025 JRNL REFN ESSN 1091-6490 JRNL PMID 40402246 JRNL DOI 10.1073/PNAS.2501637122 REMARK 2 REMARK 2 RESOLUTION. 2.40 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2_5419 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 39.15 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 98.4 REMARK 3 NUMBER OF REFLECTIONS : 132911 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.223 REMARK 3 R VALUE (WORKING SET) : 0.223 REMARK 3 FREE R VALUE : 0.247 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 1.320 REMARK 3 FREE R VALUE TEST SET COUNT : 1757 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 39.1500 - 5.6400 0.97 10128 136 0.2105 0.1989 REMARK 3 2 5.6400 - 4.4800 1.00 10250 137 0.1784 0.1992 REMARK 3 3 4.4800 - 3.9100 0.96 9854 132 0.1842 0.2151 REMARK 3 4 3.9100 - 3.5500 0.99 10178 137 0.2101 0.2318 REMARK 3 5 3.5500 - 3.3000 0.99 10177 136 0.2336 0.2423 REMARK 3 6 3.3000 - 3.1100 1.00 10184 136 0.2444 0.2674 REMARK 3 7 3.1100 - 2.9500 0.99 10173 137 0.2525 0.3107 REMARK 3 8 2.9500 - 2.8200 0.95 9675 128 0.2483 0.2784 REMARK 3 9 2.8200 - 2.7100 0.99 10109 136 0.2609 0.2920 REMARK 3 10 2.7100 - 2.6200 0.99 10087 136 0.2743 0.3316 REMARK 3 11 2.6200 - 2.5400 0.99 10109 134 0.2657 0.3001 REMARK 3 12 2.5400 - 2.4600 0.99 10060 135 0.2754 0.3189 REMARK 3 13 2.4600 - 2.4000 0.99 10170 137 0.2836 0.3559 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) : 0.310 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 27.551 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 38.38 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 55.20 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.002 20215 REMARK 3 ANGLE : 0.530 27562 REMARK 3 CHIRALITY : 0.043 3053 REMARK 3 PLANARITY : 0.004 3519 REMARK 3 DIHEDRAL : 14.246 7218 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 12 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: (CHAIN 'A' AND RESID 333 THROUGH 528) REMARK 3 ORIGIN FOR THE GROUP (A): 40.5486 23.1486 15.5789 REMARK 3 T TENSOR REMARK 3 T11: 0.3259 T22: 0.4523 REMARK 3 T33: 0.2589 T12: -0.1160 REMARK 3 T13: -0.0662 T23: 0.0571 REMARK 3 L TENSOR REMARK 3 L11: 1.7075 L22: 1.7547 REMARK 3 L33: 1.3649 L12: 0.9209 REMARK 3 L13: -1.1026 L23: -0.7448 REMARK 3 S TENSOR REMARK 3 S11: -0.0039 S12: -0.0290 S13: -0.0862 REMARK 3 S21: -0.0566 S22: -0.0336 S23: -0.0176 REMARK 3 S31: -0.1732 S32: 0.0320 S33: 0.0108 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: (CHAIN 'B' AND RESID 333 THROUGH 528) REMARK 3 ORIGIN FOR THE GROUP (A): -19.9242 14.4212 15.5808 REMARK 3 T TENSOR REMARK 3 T11: 0.4120 T22: 0.3325 REMARK 3 T33: 0.2863 T12: 0.1164 REMARK 3 T13: -0.0868 T23: -0.0642 REMARK 3 L TENSOR REMARK 3 L11: 2.0013 L22: 2.0523 REMARK 3 L33: 1.4979 L12: -1.3603 REMARK 3 L13: 1.0627 L23: -1.1310 REMARK 3 S TENSOR REMARK 3 S11: 0.0302 S12: 0.1068 S13: -0.1281 REMARK 3 S21: 0.0844 S22: 0.0147 S23: -0.1049 REMARK 3 S31: -0.0119 S32: -0.0797 S33: -0.0423 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: (CHAIN 'C' AND RESID 333 THROUGH 528) REMARK 3 ORIGIN FOR THE GROUP (A): -20.0700 50.1605 100.5805 REMARK 3 T TENSOR REMARK 3 T11: 0.4803 T22: 0.3972 REMARK 3 T33: 0.3373 T12: -0.1550 REMARK 3 T13: 0.1167 T23: -0.1045 REMARK 3 L TENSOR REMARK 3 L11: 1.9449 L22: 2.1082 REMARK 3 L33: 1.2474 L12: 1.3888 REMARK 3 L13: -0.9845 L23: -1.6270 REMARK 3 S TENSOR REMARK 3 S11: 0.1482 S12: -0.2654 S13: 0.2340 REMARK 3 S21: 0.0251 S22: -0.0763 S23: -0.0846 REMARK 3 S31: -0.0343 S32: -0.1887 S33: -0.0484 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: (CHAIN 'D' AND RESID 333 THROUGH 528) REMARK 3 ORIGIN FOR THE GROUP (A): 40.8331 40.8872 100.5801 REMARK 3 T TENSOR REMARK 3 T11: 0.4626 T22: 0.5847 REMARK 3 T33: 0.3858 T12: 0.1746 REMARK 3 T13: 0.1101 T23: 0.1355 REMARK 3 L TENSOR REMARK 3 L11: 2.7591 L22: 2.0133 REMARK 3 L33: 0.8846 L12: -2.1068 REMARK 3 L13: 1.5844 L23: -0.7181 REMARK 3 S TENSOR REMARK 3 S11: -0.1484 S12: -0.2639 S13: 0.1456 REMARK 3 S21: 0.3873 S22: 0.2061 S23: 0.1530 REMARK 3 S31: 0.0406 S32: -0.0994 S33: -0.0442 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: (CHAIN 'E' AND RESID 2 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): -3.2634 2.2361 55.0350 REMARK 3 T TENSOR REMARK 3 T11: 0.3051 T22: 0.2672 REMARK 3 T33: 0.3083 T12: 0.0014 REMARK 3 T13: 0.0982 T23: -0.0398 REMARK 3 L TENSOR REMARK 3 L11: 0.4898 L22: 3.1004 REMARK 3 L33: 1.5960 L12: 0.1247 REMARK 3 L13: -0.3301 L23: 1.1054 REMARK 3 S TENSOR REMARK 3 S11: 0.0009 S12: -0.1265 S13: -0.0285 REMARK 3 S21: 0.6631 S22: -0.1800 S23: 0.4858 REMARK 3 S31: 0.2054 S32: -0.0855 S33: 0.0112 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: (CHAIN 'F' AND RESID 1 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5257 18.5429 63.0864 REMARK 3 T TENSOR REMARK 3 T11: 0.4351 T22: 0.3187 REMARK 3 T33: 0.4041 T12: -0.0392 REMARK 3 T13: 0.1411 T23: -0.1230 REMARK 3 L TENSOR REMARK 3 L11: 0.1426 L22: 3.1342 REMARK 3 L33: 2.3923 L12: 0.0684 REMARK 3 L13: -0.6567 L23: 1.7963 REMARK 3 S TENSOR REMARK 3 S11: 0.0469 S12: 0.0126 S13: 0.1706 REMARK 3 S21: 0.7054 S22: -0.4505 S23: 0.7524 REMARK 3 S31: 0.3170 S32: 0.2673 S33: -0.0744 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: (CHAIN 'H' AND RESID 2 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 28.2815 6.6513 55.0704 REMARK 3 T TENSOR REMARK 3 T11: 0.2586 T22: 0.3448 REMARK 3 T33: 0.3243 T12: 0.0034 REMARK 3 T13: -0.0523 T23: -0.0782 REMARK 3 L TENSOR REMARK 3 L11: 2.8007 L22: 0.7468 REMARK 3 L33: 1.2959 L12: 0.0028 REMARK 3 L13: 1.0447 L23: 0.7075 REMARK 3 S TENSOR REMARK 3 S11: -0.1793 S12: -0.6245 S13: 0.3927 REMARK 3 S21: 0.2056 S22: -0.0638 S23: -0.0379 REMARK 3 S31: -0.0006 S32: -0.2192 S33: -0.0049 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: (CHAIN 'L' AND RESID 1 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): 44.7366 11.7324 63.0530 REMARK 3 T TENSOR REMARK 3 T11: 0.3633 T22: 0.4404 REMARK 3 T33: 0.3971 T12: 0.0364 REMARK 3 T13: -0.1179 T23: -0.0923 REMARK 3 L TENSOR REMARK 3 L11: 2.6797 L22: 0.1212 REMARK 3 L33: 2.3314 L12: -0.0590 REMARK 3 L13: 1.4190 L23: 0.6691 REMARK 3 S TENSOR REMARK 3 S11: -0.3435 S12: -0.5742 S13: 0.5471 REMARK 3 S21: 0.0310 S22: 0.1256 S23: -0.0711 REMARK 3 S31: 0.2463 S32: -0.2870 S33: 0.0357 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: (CHAIN 'M' AND RESID 2 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): -3.2009 62.0986 61.2368 REMARK 3 T TENSOR REMARK 3 T11: 0.3425 T22: 0.2307 REMARK 3 T33: 0.3579 T12: -0.0155 REMARK 3 T13: -0.1147 T23: -0.0483 REMARK 3 L TENSOR REMARK 3 L11: 0.8494 L22: 3.1444 REMARK 3 L33: 1.6845 L12: -0.0223 REMARK 3 L13: 0.3345 L23: 1.3575 REMARK 3 S TENSOR REMARK 3 S11: -0.0548 S12: 0.1564 S13: -0.0037 REMARK 3 S21: -0.7275 S22: -0.1703 S23: 0.4462 REMARK 3 S31: -0.3123 S32: -0.0471 S33: 0.0002 REMARK 3 TLS GROUP : 10 REMARK 3 SELECTION: (CHAIN 'N' AND RESID 1 THROUGH 213) REMARK 3 ORIGIN FOR THE GROUP (A): -8.5025 45.8382 53.2417 REMARK 3 T TENSOR REMARK 3 T11: 0.4530 T22: 0.3388 REMARK 3 T33: 0.4395 T12: 0.0593 REMARK 3 T13: -0.1157 T23: -0.1295 REMARK 3 L TENSOR REMARK 3 L11: 0.0040 L22: 2.8208 REMARK 3 L33: 1.3592 L12: 0.1818 REMARK 3 L13: 0.4455 L23: 1.6469 REMARK 3 S TENSOR REMARK 3 S11: 0.0822 S12: 0.0533 S13: -0.1545 REMARK 3 S21: -0.6571 S22: -0.3097 S23: 0.6695 REMARK 3 S31: -0.4034 S32: -0.0742 S33: 0.1441 REMARK 3 TLS GROUP : 11 REMARK 3 SELECTION: (CHAIN 'P' AND RESID 2 THROUGH 214) REMARK 3 ORIGIN FOR THE GROUP (A): 28.3098 57.6212 61.2052 REMARK 3 T TENSOR REMARK 3 T11: 0.2317 T22: 0.3078 REMARK 3 T33: 0.3692 T12: -0.0109 REMARK 3 T13: 0.0285 T23: -0.1198 REMARK 3 L TENSOR REMARK 3 L11: 2.9179 L22: 0.8519 REMARK 3 L33: 1.2794 L12: -0.2133 REMARK 3 L13: -1.2860 L23: 0.5686 REMARK 3 S TENSOR REMARK 3 S11: -0.1767 S12: 0.5919 S13: -0.5241 REMARK 3 S21: -0.1547 S22: -0.0670 S23: 0.0157 REMARK 3 S31: 0.0906 S32: -0.3006 S33: 0.0824 REMARK 3 TLS GROUP : 12 REMARK 3 SELECTION: (CHAIN 'Q' AND RESID 1 THROUGH 212) REMARK 3 ORIGIN FOR THE GROUP (A): 44.8231 52.5172 53.3697 REMARK 3 T TENSOR REMARK 3 T11: 0.3619 T22: 0.4348 REMARK 3 T33: 0.4919 T12: -0.0307 REMARK 3 T13: 0.1106 T23: -0.1232 REMARK 3 L TENSOR REMARK 3 L11: 2.7368 L22: -0.0126 REMARK 3 L33: 2.3092 L12: 0.0595 REMARK 3 L13: -1.2707 L23: 0.6649 REMARK 3 S TENSOR REMARK 3 S11: -0.3697 S12: 0.5590 S13: -0.7436 REMARK 3 S21: 0.0122 S22: 0.0862 S23: -0.1003 REMARK 3 S31: -0.3304 S32: -0.3334 S33: 0.0872 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 9ML8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-DEC-24. REMARK 100 THE DEPOSITION ID IS D_1000290167. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 11-JUN-24 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 : SSRL REMARK 200 BEAMLINE : BL12-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795 REMARK 200 MONOCHROMATOR : SI(111) REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 133293 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.400 REMARK 200 RESOLUTION RANGE LOW (A) : 39.150 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 98.5 REMARK 200 DATA REDUNDANCY : 7.200 REMARK 200 R MERGE (I) : 0.17200 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 7.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.44 REMARK 200 COMPLETENESS FOR SHELL (%) : 99.1 REMARK 200 DATA REDUNDANCY IN SHELL : 7.40 REMARK 200 R MERGE FOR SHELL (I) : 0.98900 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.300 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 (%): 59.67 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.05 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M LITHIUM SULFATE 0.1 SODIUM REMARK 280 CITRATE 20% (W/V) PEG 1,000, VAPOR DIFFUSION, SITTING DROP, REMARK 280 TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z REMARK 290 4555 -X+1/2,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 87.53700 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 86.72050 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 87.53700 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 86.72050 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3, 4 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, G 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: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, E, 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: 3 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, M, N, J 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: D, P, Q, 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 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 ARG A 328 REMARK 465 PHE A 329 REMARK 465 PRO A 330 REMARK 465 ASN A 331 REMARK 465 ILE A 332 REMARK 465 LYS A 529 REMARK 465 SER A 530 REMARK 465 THR A 531 REMARK 465 ASN A 532 REMARK 465 LEU A 533 REMARK 465 HIS A 534 REMARK 465 HIS A 535 REMARK 465 HIS A 536 REMARK 465 HIS A 537 REMARK 465 HIS A 538 REMARK 465 HIS A 539 REMARK 465 ARG B 328 REMARK 465 PHE B 329 REMARK 465 PRO B 330 REMARK 465 ASN B 331 REMARK 465 ILE B 332 REMARK 465 LYS B 529 REMARK 465 SER B 530 REMARK 465 THR B 531 REMARK 465 ASN B 532 REMARK 465 LEU B 533 REMARK 465 HIS B 534 REMARK 465 HIS B 535 REMARK 465 HIS B 536 REMARK 465 HIS B 537 REMARK 465 HIS B 538 REMARK 465 HIS B 539 REMARK 465 ARG C 328 REMARK 465 PHE C 329 REMARK 465 PRO C 330 REMARK 465 ASN C 331 REMARK 465 ILE C 332 REMARK 465 LYS C 529 REMARK 465 SER C 530 REMARK 465 THR C 531 REMARK 465 ASN C 532 REMARK 465 LEU C 533 REMARK 465 HIS C 534 REMARK 465 HIS C 535 REMARK 465 HIS C 536 REMARK 465 HIS C 537 REMARK 465 HIS C 538 REMARK 465 HIS C 539 REMARK 465 ARG D 328 REMARK 465 PHE D 329 REMARK 465 PRO D 330 REMARK 465 ASN D 331 REMARK 465 ILE D 332 REMARK 465 LYS D 529 REMARK 465 SER D 530 REMARK 465 THR D 531 REMARK 465 ASN D 532 REMARK 465 LEU D 533 REMARK 465 HIS D 534 REMARK 465 HIS D 535 REMARK 465 HIS D 536 REMARK 465 HIS D 537 REMARK 465 HIS D 538 REMARK 465 HIS D 539 REMARK 465 SER E 128 REMARK 465 LYS E 129 REMARK 465 SER E 130 REMARK 465 THR E 131 REMARK 465 SER E 132 REMARK 465 GLY E 133 REMARK 465 GLY E 134 REMARK 465 SER E 215 REMARK 465 CYS E 216 REMARK 465 ASP E 217 REMARK 465 LYS E 218 REMARK 465 CYS F 214 REMARK 465 SER H 128 REMARK 465 LYS H 129 REMARK 465 SER H 130 REMARK 465 THR H 131 REMARK 465 SER H 132 REMARK 465 GLY H 133 REMARK 465 GLY H 134 REMARK 465 SER H 215 REMARK 465 CYS H 216 REMARK 465 ASP H 217 REMARK 465 LYS H 218 REMARK 465 CYS L 214 REMARK 465 SER M 128 REMARK 465 LYS M 129 REMARK 465 SER M 130 REMARK 465 THR M 131 REMARK 465 SER M 132 REMARK 465 GLY M 133 REMARK 465 GLY M 134 REMARK 465 SER M 215 REMARK 465 CYS M 216 REMARK 465 ASP M 217 REMARK 465 LYS M 218 REMARK 465 CYS N 214 REMARK 465 SER P 128 REMARK 465 LYS P 129 REMARK 465 SER P 130 REMARK 465 THR P 131 REMARK 465 SER P 132 REMARK 465 GLY P 133 REMARK 465 GLY P 134 REMARK 465 SER P 215 REMARK 465 CYS P 216 REMARK 465 ASP P 217 REMARK 465 LYS P 218 REMARK 465 CYS Q 214 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OE1 GLN H 171 OG SER H 177 2.18 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: TORSION ANGLES REMARK 500 REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS: REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2) REMARK 500 REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI- REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400 REMARK 500 REMARK 500 M RES CSSEQI PSI PHI REMARK 500 SER E 30 14.06 -140.79 REMARK 500 ASP E 144 65.78 60.74 REMARK 500 ALA F 51 -13.25 72.54 REMARK 500 SER F 52 -13.90 -141.34 REMARK 500 SER H 30 18.31 -140.61 REMARK 500 ASP H 144 66.04 61.21 REMARK 500 ALA L 51 -12.89 72.30 REMARK 500 SER L 52 -13.36 -142.56 REMARK 500 ASP M 144 65.82 60.43 REMARK 500 ALA N 51 -12.34 73.06 REMARK 500 SER N 52 -14.22 -141.31 REMARK 500 SER P 30 16.93 -140.51 REMARK 500 ASP P 144 62.21 61.31 REMARK 500 ALA Q 51 -11.34 72.97 REMARK 500 SER Q 52 -14.45 -143.24 REMARK 500 ASP Q 95A 29.80 -140.75 REMARK 500 REMARK 500 REMARK: NULL REMARK 525 REMARK 525 SOLVENT REMARK 525 REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER; REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE REMARK 525 NUMBER; I=INSERTION CODE): REMARK 525 REMARK 525 M RES CSSEQI REMARK 525 HOH B 663 DISTANCE = 7.14 ANGSTROMS REMARK 525 HOH N 452 DISTANCE = 7.09 ANGSTROMS REMARK 525 HOH P 380 DISTANCE = 7.57 ANGSTROMS REMARK 525 HOH P 381 DISTANCE = 7.94 ANGSTROMS DBREF 9ML8 A 328 533 UNP P0DTC2 SPIKE_SARS2 328 533 DBREF 9ML8 B 328 533 UNP P0DTC2 SPIKE_SARS2 328 533 DBREF 9ML8 C 328 533 UNP P0DTC2 SPIKE_SARS2 328 533 DBREF 9ML8 D 328 533 UNP P0DTC2 SPIKE_SARS2 328 533 DBREF 9ML8 E 2 218 PDB 9ML8 9ML8 2 218 DBREF 9ML8 F 1 214 PDB 9ML8 9ML8 1 214 DBREF 9ML8 H 2 218 PDB 9ML8 9ML8 2 218 DBREF 9ML8 L 1 214 PDB 9ML8 9ML8 1 214 DBREF 9ML8 M 2 218 PDB 9ML8 9ML8 2 218 DBREF 9ML8 N 1 214 PDB 9ML8 9ML8 1 214 DBREF 9ML8 P 2 218 PDB 9ML8 9ML8 2 218 DBREF 9ML8 Q 1 214 PDB 9ML8 9ML8 1 214 SEQADV 9ML8 HIS A 534 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS A 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS A 536 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS A 537 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS A 538 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS A 539 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS B 534 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS B 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS B 536 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS B 537 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS B 538 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS B 539 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS C 534 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS C 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS C 536 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS C 537 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS C 538 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS C 539 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS D 534 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS D 535 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS D 536 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS D 537 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS D 538 UNP P0DTC2 EXPRESSION TAG SEQADV 9ML8 HIS D 539 UNP P0DTC2 EXPRESSION TAG SEQRES 1 A 212 ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU SEQRES 2 A 212 VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP SEQRES 3 A 212 ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER SEQRES 4 A 212 VAL LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS SEQRES 5 A 212 TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE SEQRES 6 A 212 THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP SEQRES 7 A 212 GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE SEQRES 8 A 212 ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY SEQRES 9 A 212 CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS SEQRES 10 A 212 VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG SEQRES 11 A 212 LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR SEQRES 12 A 212 GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL SEQRES 13 A 212 GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY SEQRES 14 A 212 PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG SEQRES 15 A 212 VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA SEQRES 16 A 212 THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU HIS HIS SEQRES 17 A 212 HIS HIS HIS HIS SEQRES 1 B 212 ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU SEQRES 2 B 212 VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP SEQRES 3 B 212 ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER SEQRES 4 B 212 VAL LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS SEQRES 5 B 212 TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE SEQRES 6 B 212 THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP SEQRES 7 B 212 GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE SEQRES 8 B 212 ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY SEQRES 9 B 212 CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS SEQRES 10 B 212 VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG SEQRES 11 B 212 LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR SEQRES 12 B 212 GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL SEQRES 13 B 212 GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY SEQRES 14 B 212 PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG SEQRES 15 B 212 VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA SEQRES 16 B 212 THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU HIS HIS SEQRES 17 B 212 HIS HIS HIS HIS SEQRES 1 C 212 ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU SEQRES 2 C 212 VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP SEQRES 3 C 212 ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER SEQRES 4 C 212 VAL LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS SEQRES 5 C 212 TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE SEQRES 6 C 212 THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP SEQRES 7 C 212 GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE SEQRES 8 C 212 ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY SEQRES 9 C 212 CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS SEQRES 10 C 212 VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG SEQRES 11 C 212 LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR SEQRES 12 C 212 GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL SEQRES 13 C 212 GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY SEQRES 14 C 212 PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG SEQRES 15 C 212 VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA SEQRES 16 C 212 THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU HIS HIS SEQRES 17 C 212 HIS HIS HIS HIS SEQRES 1 D 212 ARG PHE PRO ASN ILE THR ASN LEU CYS PRO PHE GLY GLU SEQRES 2 D 212 VAL PHE ASN ALA THR ARG PHE ALA SER VAL TYR ALA TRP SEQRES 3 D 212 ASN ARG LYS ARG ILE SER ASN CYS VAL ALA ASP TYR SER SEQRES 4 D 212 VAL LEU TYR ASN SER ALA SER PHE SER THR PHE LYS CYS SEQRES 5 D 212 TYR GLY VAL SER PRO THR LYS LEU ASN ASP LEU CYS PHE SEQRES 6 D 212 THR ASN VAL TYR ALA ASP SER PHE VAL ILE ARG GLY ASP SEQRES 7 D 212 GLU VAL ARG GLN ILE ALA PRO GLY GLN THR GLY LYS ILE SEQRES 8 D 212 ALA ASP TYR ASN TYR LYS LEU PRO ASP ASP PHE THR GLY SEQRES 9 D 212 CYS VAL ILE ALA TRP ASN SER ASN ASN LEU ASP SER LYS SEQRES 10 D 212 VAL GLY GLY ASN TYR ASN TYR LEU TYR ARG LEU PHE ARG SEQRES 11 D 212 LYS SER ASN LEU LYS PRO PHE GLU ARG ASP ILE SER THR SEQRES 12 D 212 GLU ILE TYR GLN ALA GLY SER THR PRO CYS ASN GLY VAL SEQRES 13 D 212 GLU GLY PHE ASN CYS TYR PHE PRO LEU GLN SER TYR GLY SEQRES 14 D 212 PHE GLN PRO THR ASN GLY VAL GLY TYR GLN PRO TYR ARG SEQRES 15 D 212 VAL VAL VAL LEU SER PHE GLU LEU LEU HIS ALA PRO ALA SEQRES 16 D 212 THR VAL CYS GLY PRO LYS LYS SER THR ASN LEU HIS HIS SEQRES 17 D 212 HIS HIS HIS HIS SEQRES 1 E 235 GLN SER LEU GLU GLU SER GLY GLY ASP LEU VAL LYS PRO SEQRES 2 E 235 GLY ALA SER LEU THR LEU THR CYS THR ALA SER GLY PHE SEQRES 3 E 235 SER PHE SER GLY SER TYR TYR MET CYS TRP VAL ARG GLN SEQRES 4 E 235 ALA PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS ILE TYR SEQRES 5 E 235 ASP GLY SER TYR ASP GLY SER SER ASP ASN ALA TYR TYR SEQRES 6 E 235 ALA SER TRP ALA LYS GLY ARG PHE THR ILE SER LYS THR SEQRES 7 E 235 SER SER THR THR VAL THR LEU GLN MET THR SER LEU THR SEQRES 8 E 235 ALA ALA ASP THR ALA THR TYR PHE CYS ALA ARG GLY VAL SEQRES 9 E 235 TYR PHE TYR ALA GLY HIS PHE VAL ILE MET ARG TYR PHE SEQRES 10 E 235 VAL LEU TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 11 E 235 GLY GLN PRO LYS ALA PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 E 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 E 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 E 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 E 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 E 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 E 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 E 235 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 E 235 LYS SEQRES 1 F 217 ALA GLN VAL LEU THR GLN THR PRO SER SER VAL SER ALA SEQRES 2 F 217 ALA VAL GLY GLY THR VAL SER ILE SER CYS GLN SER SER SEQRES 3 F 217 GLN SER VAL TYR SER ASN TYR LEU SER TRP TYR GLN GLN SEQRES 4 F 217 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASP ALA SEQRES 5 F 217 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 6 F 217 SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER GLY SEQRES 7 F 217 VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN GLY SEQRES 8 F 217 SER TYR TYR SER SER ASP TRP TYR PRO PHE GLY GLY GLY SEQRES 9 F 217 THR GLU VAL VAL VAL LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 F 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 F 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 F 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 F 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 F 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 F 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 F 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 F 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 H 235 GLN SER LEU GLU GLU SER GLY GLY ASP LEU VAL LYS PRO SEQRES 2 H 235 GLY ALA SER LEU THR LEU THR CYS THR ALA SER GLY PHE SEQRES 3 H 235 SER PHE SER GLY SER TYR TYR MET CYS TRP VAL ARG GLN SEQRES 4 H 235 ALA PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS ILE TYR SEQRES 5 H 235 ASP GLY SER TYR ASP GLY SER SER ASP ASN ALA TYR TYR SEQRES 6 H 235 ALA SER TRP ALA LYS GLY ARG PHE THR ILE SER LYS THR SEQRES 7 H 235 SER SER THR THR VAL THR LEU GLN MET THR SER LEU THR SEQRES 8 H 235 ALA ALA ASP THR ALA THR TYR PHE CYS ALA ARG GLY VAL SEQRES 9 H 235 TYR PHE TYR ALA GLY HIS PHE VAL ILE MET ARG TYR PHE SEQRES 10 H 235 VAL LEU TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 11 H 235 GLY GLN PRO LYS ALA PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 H 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 H 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 H 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 H 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 H 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 H 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 H 235 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 H 235 LYS SEQRES 1 L 217 ALA GLN VAL LEU THR GLN THR PRO SER SER VAL SER ALA SEQRES 2 L 217 ALA VAL GLY GLY THR VAL SER ILE SER CYS GLN SER SER SEQRES 3 L 217 GLN SER VAL TYR SER ASN TYR LEU SER TRP TYR GLN GLN SEQRES 4 L 217 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASP ALA SEQRES 5 L 217 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 6 L 217 SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER GLY SEQRES 7 L 217 VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN GLY SEQRES 8 L 217 SER TYR TYR SER SER ASP TRP TYR PRO PHE GLY GLY GLY SEQRES 9 L 217 THR GLU VAL VAL VAL LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 L 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 L 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 L 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 L 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 L 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 L 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 L 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 L 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 M 235 GLN SER LEU GLU GLU SER GLY GLY ASP LEU VAL LYS PRO SEQRES 2 M 235 GLY ALA SER LEU THR LEU THR CYS THR ALA SER GLY PHE SEQRES 3 M 235 SER PHE SER GLY SER TYR TYR MET CYS TRP VAL ARG GLN SEQRES 4 M 235 ALA PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS ILE TYR SEQRES 5 M 235 ASP GLY SER TYR ASP GLY SER SER ASP ASN ALA TYR TYR SEQRES 6 M 235 ALA SER TRP ALA LYS GLY ARG PHE THR ILE SER LYS THR SEQRES 7 M 235 SER SER THR THR VAL THR LEU GLN MET THR SER LEU THR SEQRES 8 M 235 ALA ALA ASP THR ALA THR TYR PHE CYS ALA ARG GLY VAL SEQRES 9 M 235 TYR PHE TYR ALA GLY HIS PHE VAL ILE MET ARG TYR PHE SEQRES 10 M 235 VAL LEU TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 11 M 235 GLY GLN PRO LYS ALA PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 M 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 M 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 M 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 M 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 M 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 M 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 M 235 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 M 235 LYS SEQRES 1 N 217 ALA GLN VAL LEU THR GLN THR PRO SER SER VAL SER ALA SEQRES 2 N 217 ALA VAL GLY GLY THR VAL SER ILE SER CYS GLN SER SER SEQRES 3 N 217 GLN SER VAL TYR SER ASN TYR LEU SER TRP TYR GLN GLN SEQRES 4 N 217 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASP ALA SEQRES 5 N 217 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 6 N 217 SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER GLY SEQRES 7 N 217 VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN GLY SEQRES 8 N 217 SER TYR TYR SER SER ASP TRP TYR PRO PHE GLY GLY GLY SEQRES 9 N 217 THR GLU VAL VAL VAL LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 N 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 N 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 N 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 N 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 N 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 N 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 N 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 N 217 THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 P 235 GLN SER LEU GLU GLU SER GLY GLY ASP LEU VAL LYS PRO SEQRES 2 P 235 GLY ALA SER LEU THR LEU THR CYS THR ALA SER GLY PHE SEQRES 3 P 235 SER PHE SER GLY SER TYR TYR MET CYS TRP VAL ARG GLN SEQRES 4 P 235 ALA PRO GLY LYS GLY LEU GLU TRP ILE ALA CYS ILE TYR SEQRES 5 P 235 ASP GLY SER TYR ASP GLY SER SER ASP ASN ALA TYR TYR SEQRES 6 P 235 ALA SER TRP ALA LYS GLY ARG PHE THR ILE SER LYS THR SEQRES 7 P 235 SER SER THR THR VAL THR LEU GLN MET THR SER LEU THR SEQRES 8 P 235 ALA ALA ASP THR ALA THR TYR PHE CYS ALA ARG GLY VAL SEQRES 9 P 235 TYR PHE TYR ALA GLY HIS PHE VAL ILE MET ARG TYR PHE SEQRES 10 P 235 VAL LEU TRP GLY PRO GLY THR LEU VAL THR VAL SER SER SEQRES 11 P 235 GLY GLN PRO LYS ALA PRO SER VAL PHE PRO LEU ALA PRO SEQRES 12 P 235 SER SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY SEQRES 13 P 235 CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SEQRES 14 P 235 SER TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR SEQRES 15 P 235 PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SEQRES 16 P 235 SER SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR SEQRES 17 P 235 GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN SEQRES 18 P 235 THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS ASP SEQRES 19 P 235 LYS SEQRES 1 Q 217 ALA GLN VAL LEU THR GLN THR PRO SER SER VAL SER ALA SEQRES 2 Q 217 ALA VAL GLY GLY THR VAL SER ILE SER CYS GLN SER SER SEQRES 3 Q 217 GLN SER VAL TYR SER ASN TYR LEU SER TRP TYR GLN GLN SEQRES 4 Q 217 LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE TYR ASP ALA SEQRES 5 Q 217 SER THR LEU ALA SER GLY VAL PRO SER ARG PHE LYS GLY SEQRES 6 Q 217 SER GLY SER GLY THR GLN PHE THR LEU THR ILE SER GLY SEQRES 7 Q 217 VAL GLN CYS ASP ASP ALA ALA THR TYR TYR CYS GLN GLY SEQRES 8 Q 217 SER TYR TYR SER SER ASP TRP TYR PRO PHE GLY GLY GLY SEQRES 9 Q 217 THR GLU VAL VAL VAL LYS ARG THR VAL ALA ALA PRO SER SEQRES 10 Q 217 VAL PHE ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER SEQRES 11 Q 217 GLY THR ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR SEQRES 12 Q 217 PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA SEQRES 13 Q 217 LEU GLN SER GLY ASN SER GLN GLU SER VAL THR GLU GLN SEQRES 14 Q 217 ASP SER LYS ASP SER THR TYR SER LEU SER SER THR LEU SEQRES 15 Q 217 THR LEU SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR SEQRES 16 Q 217 ALA CYS GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL SEQRES 17 Q 217 THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG G 1 14 HET NAG G 2 14 HET NAG I 1 14 HET NAG I 2 14 HET NAG J 1 14 HET NAG J 2 14 HET NAG K 1 14 HET NAG K 2 14 HET SO4 A 601 5 HET SO4 C 601 5 HET SO4 D 601 5 HET SO4 F 301 5 HET SO4 L 301 5 HET SO4 N 301 5 HET SO4 Q 301 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM SO4 SULFATE 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 FORMUL 13 NAG 8(C8 H15 N O6) FORMUL 17 SO4 7(O4 S 2-) FORMUL 24 HOH *755(H2 O) HELIX 1 AA1 PRO A 337 ASN A 343 1 7 HELIX 2 AA2 TYR A 365 ASN A 370 1 6 HELIX 3 AA3 PRO A 384 ASP A 389 5 6 HELIX 4 AA4 ASP A 405 ILE A 410 5 6 HELIX 5 AA5 GLY A 416 ASN A 422 1 7 HELIX 6 AA6 SER A 438 SER A 443 1 6 HELIX 7 AA7 GLY A 502 TYR A 505 5 4 HELIX 8 AA8 PRO B 337 ASN B 343 1 7 HELIX 9 AA9 SER B 349 TRP B 353 5 5 HELIX 10 AB1 TYR B 365 ASN B 370 1 6 HELIX 11 AB2 SER B 383 ASP B 389 5 7 HELIX 12 AB3 ASP B 405 ILE B 410 5 6 HELIX 13 AB4 GLY B 416 ASN B 422 1 7 HELIX 14 AB5 SER B 438 SER B 443 1 6 HELIX 15 AB6 GLY B 502 TYR B 505 5 4 HELIX 16 AB7 PRO C 337 ASN C 343 1 7 HELIX 17 AB8 SER C 349 TRP C 353 5 5 HELIX 18 AB9 TYR C 365 ASN C 370 1 6 HELIX 19 AC1 SER C 383 ASP C 389 5 7 HELIX 20 AC2 ASP C 405 ILE C 410 5 6 HELIX 21 AC3 GLY C 416 ASN C 422 1 7 HELIX 22 AC4 SER C 438 SER C 443 1 6 HELIX 23 AC5 GLY C 502 TYR C 505 5 4 HELIX 24 AC6 PRO D 337 ASN D 343 1 7 HELIX 25 AC7 ASP D 364 SER D 371 1 8 HELIX 26 AC8 PRO D 384 ASP D 389 5 6 HELIX 27 AC9 ASP D 405 ILE D 410 5 6 HELIX 28 AD1 GLY D 416 ASN D 422 1 7 HELIX 29 AD2 SER D 438 SER D 443 1 6 HELIX 30 AD3 GLY D 502 TYR D 505 5 4 HELIX 31 AD4 THR E 83 THR E 87 5 5 HELIX 32 AD5 PRO E 185 GLY E 190 5 6 HELIX 33 AD6 LYS E 201 ASN E 204 5 4 HELIX 34 AD7 VAL F 28 ASN F 31 5 4 HELIX 35 AD8 GLN F 79 ALA F 83 5 5 HELIX 36 AD9 SER F 121 LYS F 126 1 6 HELIX 37 AE1 LYS F 183 GLU F 187 1 5 HELIX 38 AE2 THR H 83 THR H 87 5 5 HELIX 39 AE3 SER H 156 ALA H 158 5 3 HELIX 40 AE4 SER H 187 GLN H 192 1 6 HELIX 41 AE5 LYS H 201 ASN H 204 5 4 HELIX 42 AE6 VAL L 28 ASN L 31 5 4 HELIX 43 AE7 GLN L 79 ALA L 83 5 5 HELIX 44 AE8 SER L 121 GLY L 128 1 8 HELIX 45 AE9 LYS L 183 GLU L 187 1 5 HELIX 46 AF1 THR M 83 THR M 87 5 5 HELIX 47 AF2 SER M 156 ALA M 158 5 3 HELIX 48 AF3 PRO M 185 LEU M 189 5 5 HELIX 49 AF4 LYS M 201 ASN M 204 5 4 HELIX 50 AF5 VAL N 28 ASN N 31 5 4 HELIX 51 AF6 GLN N 79 ALA N 83 5 5 HELIX 52 AF7 GLU N 123 GLY N 128 1 6 HELIX 53 AF8 LYS N 183 GLU N 187 1 5 HELIX 54 AF9 THR P 83 THR P 87 5 5 HELIX 55 AG1 SER P 156 ALA P 158 5 3 HELIX 56 AG2 PRO P 185 GLY P 190 5 6 HELIX 57 AG3 LYS P 201 ASN P 204 5 4 HELIX 58 AG4 VAL Q 28 ASN Q 31 5 4 HELIX 59 AG5 GLN Q 79 ALA Q 83 5 5 HELIX 60 AG6 SER Q 121 LYS Q 126 1 6 HELIX 61 AG7 LYS Q 183 GLU Q 187 1 5 SHEET 1 AA1 5 ASN A 354 ILE A 358 0 SHEET 2 AA1 5 ASN A 394 ARG A 403 -1 O VAL A 395 N ILE A 358 SHEET 3 AA1 5 PRO A 507 GLU A 516 -1 O VAL A 510 N PHE A 400 SHEET 4 AA1 5 GLY A 431 ASN A 437 -1 N ILE A 434 O VAL A 511 SHEET 5 AA1 5 THR A 376 TYR A 380 -1 N LYS A 378 O VAL A 433 SHEET 1 AA2 3 CYS A 361 VAL A 362 0 SHEET 2 AA2 3 VAL A 524 CYS A 525 1 O CYS A 525 N CYS A 361 SHEET 3 AA2 3 CYS A 391 PHE A 392 -1 N PHE A 392 O VAL A 524 SHEET 1 AA3 2 LEU A 452 ARG A 454 0 SHEET 2 AA3 2 LEU A 492 SER A 494 -1 O GLN A 493 N TYR A 453 SHEET 1 AA4 2 TYR A 473 GLN A 474 0 SHEET 2 AA4 2 CYS A 488 TYR A 489 -1 O TYR A 489 N TYR A 473 SHEET 1 AA5 5 ASN B 354 ILE B 358 0 SHEET 2 AA5 5 ASN B 394 ARG B 403 -1 O VAL B 395 N ILE B 358 SHEET 3 AA5 5 PRO B 507 GLU B 516 -1 O VAL B 510 N PHE B 400 SHEET 4 AA5 5 GLY B 431 ASN B 437 -1 N ILE B 434 O VAL B 511 SHEET 5 AA5 5 THR B 376 TYR B 380 -1 N TYR B 380 O GLY B 431 SHEET 1 AA6 3 CYS B 361 VAL B 362 0 SHEET 2 AA6 3 VAL B 524 CYS B 525 1 O CYS B 525 N CYS B 361 SHEET 3 AA6 3 CYS B 391 PHE B 392 -1 N PHE B 392 O VAL B 524 SHEET 1 AA7 2 LEU B 452 ARG B 454 0 SHEET 2 AA7 2 LEU B 492 SER B 494 -1 O GLN B 493 N TYR B 453 SHEET 1 AA8 2 TYR B 473 GLN B 474 0 SHEET 2 AA8 2 CYS B 488 TYR B 489 -1 O TYR B 489 N TYR B 473 SHEET 1 AA9 5 ASN C 354 ILE C 358 0 SHEET 2 AA9 5 ASN C 394 ARG C 403 -1 O VAL C 395 N ILE C 358 SHEET 3 AA9 5 PRO C 507 GLU C 516 -1 O VAL C 510 N PHE C 400 SHEET 4 AA9 5 GLY C 431 ASN C 437 -1 N ILE C 434 O VAL C 511 SHEET 5 AA9 5 THR C 376 TYR C 380 -1 N TYR C 380 O GLY C 431 SHEET 1 AB1 3 CYS C 361 VAL C 362 0 SHEET 2 AB1 3 VAL C 524 CYS C 525 1 O CYS C 525 N CYS C 361 SHEET 3 AB1 3 CYS C 391 PHE C 392 -1 N PHE C 392 O VAL C 524 SHEET 1 AB2 2 LEU C 452 ARG C 454 0 SHEET 2 AB2 2 LEU C 492 SER C 494 -1 O GLN C 493 N TYR C 453 SHEET 1 AB3 2 TYR C 473 GLN C 474 0 SHEET 2 AB3 2 CYS C 488 TYR C 489 -1 O TYR C 489 N TYR C 473 SHEET 1 AB4 5 ASN D 354 ILE D 358 0 SHEET 2 AB4 5 ASN D 394 ARG D 403 -1 O VAL D 395 N ILE D 358 SHEET 3 AB4 5 PRO D 507 GLU D 516 -1 O VAL D 510 N PHE D 400 SHEET 4 AB4 5 GLY D 431 ASN D 437 -1 N ILE D 434 O VAL D 511 SHEET 5 AB4 5 THR D 376 TYR D 380 -1 N TYR D 380 O GLY D 431 SHEET 1 AB5 3 CYS D 361 VAL D 362 0 SHEET 2 AB5 3 VAL D 524 CYS D 525 1 O CYS D 525 N CYS D 361 SHEET 3 AB5 3 CYS D 391 PHE D 392 -1 N PHE D 392 O VAL D 524 SHEET 1 AB6 2 LEU D 452 ARG D 454 0 SHEET 2 AB6 2 LEU D 492 SER D 494 -1 O GLN D 493 N TYR D 453 SHEET 1 AB7 2 TYR D 473 GLN D 474 0 SHEET 2 AB7 2 CYS D 488 TYR D 489 -1 O TYR D 489 N TYR D 473 SHEET 1 AB8 4 SER E 3 SER E 7 0 SHEET 2 AB8 4 LEU E 18 SER E 25 -1 O SER E 25 N SER E 3 SHEET 3 AB8 4 THR E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AB8 4 PHE E 67 LYS E 71 -1 N THR E 68 O GLN E 81 SHEET 1 AB9 6 LEU E 11 VAL E 12 0 SHEET 2 AB9 6 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AB9 6 ALA E 88 TYR E 99 -1 N TYR E 90 O THR E 107 SHEET 4 AB9 6 TYR E 34 GLN E 39 -1 N VAL E 37 O PHE E 91 SHEET 5 AB9 6 GLU E 46 TYR E 52 -1 O ILE E 51 N MET E 35 SHEET 6 AB9 6 ALA E 57 TYR E 59 -1 O TYR E 58 N CYS E 50 SHEET 1 AC1 4 LEU E 11 VAL E 12 0 SHEET 2 AC1 4 THR E 107 VAL E 111 1 O THR E 110 N VAL E 12 SHEET 3 AC1 4 ALA E 88 TYR E 99 -1 N TYR E 90 O THR E 107 SHEET 4 AC1 4 VAL E 100D TRP E 103 -1 O ARG E 100G N VAL E 96 SHEET 1 AC2 4 SER E 120 LEU E 124 0 SHEET 2 AC2 4 ALA E 136 TYR E 145 -1 O LEU E 141 N PHE E 122 SHEET 3 AC2 4 TYR E 176 VAL E 184 -1 O LEU E 178 N VAL E 142 SHEET 4 AC2 4 VAL E 163 THR E 165 -1 N HIS E 164 O VAL E 181 SHEET 1 AC3 4 SER E 120 LEU E 124 0 SHEET 2 AC3 4 ALA E 136 TYR E 145 -1 O LEU E 141 N PHE E 122 SHEET 3 AC3 4 TYR E 176 VAL E 184 -1 O LEU E 178 N VAL E 142 SHEET 4 AC3 4 VAL E 169 LEU E 170 -1 N VAL E 169 O SER E 177 SHEET 1 AC4 3 THR E 151 TRP E 154 0 SHEET 2 AC4 3 TYR E 194 HIS E 200 -1 O ASN E 197 N SER E 153 SHEET 3 AC4 3 THR E 205 VAL E 211 -1 O VAL E 211 N TYR E 194 SHEET 1 AC5 4 LEU F 4 THR F 7 0 SHEET 2 AC5 4 THR F 18 SER F 25 -1 O GLN F 24 N THR F 5 SHEET 3 AC5 4 GLN F 70 SER F 76 -1 O LEU F 73 N ILE F 21 SHEET 4 AC5 4 PHE F 62 SER F 67 -1 N SER F 65 O THR F 72 SHEET 1 AC6 6 SER F 10 ALA F 13 0 SHEET 2 AC6 6 THR F 102 VAL F 106 1 O VAL F 105 N VAL F 11 SHEET 3 AC6 6 THR F 85 GLY F 90 -1 N TYR F 86 O THR F 102 SHEET 4 AC6 6 LEU F 33 GLN F 38 -1 N GLN F 38 O THR F 85 SHEET 5 AC6 6 LYS F 45 TYR F 49 -1 O LYS F 45 N GLN F 37 SHEET 6 AC6 6 THR F 53 LEU F 54 -1 O THR F 53 N TYR F 49 SHEET 1 AC7 4 SER F 114 PHE F 118 0 SHEET 2 AC7 4 THR F 129 PHE F 139 -1 O VAL F 133 N PHE F 118 SHEET 3 AC7 4 TYR F 173 SER F 182 -1 O LEU F 179 N VAL F 132 SHEET 4 AC7 4 SER F 159 VAL F 163 -1 N GLN F 160 O THR F 178 SHEET 1 AC8 4 ALA F 153 LEU F 154 0 SHEET 2 AC8 4 LYS F 145 VAL F 150 -1 N VAL F 150 O ALA F 153 SHEET 3 AC8 4 VAL F 191 THR F 197 -1 O ALA F 193 N LYS F 149 SHEET 4 AC8 4 VAL F 205 ASN F 210 -1 O LYS F 207 N CYS F 194 SHEET 1 AC9 4 SER H 3 SER H 7 0 SHEET 2 AC9 4 LEU H 18 SER H 25 -1 O THR H 21 N SER H 7 SHEET 3 AC9 4 THR H 77 MET H 82 -1 O MET H 82 N LEU H 18 SHEET 4 AC9 4 PHE H 67 SER H 74 -1 N THR H 68 O GLN H 81 SHEET 1 AD1 6 LEU H 11 VAL H 12 0 SHEET 2 AD1 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD1 6 ALA H 88 TYR H 99 -1 N TYR H 90 O THR H 107 SHEET 4 AD1 6 TYR H 34 GLN H 39 -1 N TYR H 34 O GLY H 95 SHEET 5 AD1 6 GLU H 46 TYR H 52 -1 O ILE H 51 N MET H 35 SHEET 6 AD1 6 ALA H 57 TYR H 59 -1 O TYR H 58 N CYS H 50 SHEET 1 AD2 4 LEU H 11 VAL H 12 0 SHEET 2 AD2 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AD2 4 ALA H 88 TYR H 99 -1 N TYR H 90 O THR H 107 SHEET 4 AD2 4 VAL H 100D TRP H 103 -1 O ARG H 100G N VAL H 96 SHEET 1 AD3 4 SER H 120 LEU H 124 0 SHEET 2 AD3 4 ALA H 136 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AD3 4 TYR H 176 VAL H 184 -1 O LEU H 178 N VAL H 142 SHEET 4 AD3 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AD4 4 SER H 120 LEU H 124 0 SHEET 2 AD4 4 ALA H 136 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AD4 4 TYR H 176 VAL H 184 -1 O LEU H 178 N VAL H 142 SHEET 4 AD4 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AD5 3 THR H 151 TRP H 154 0 SHEET 2 AD5 3 TYR H 194 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AD5 3 THR H 205 VAL H 211 -1 O VAL H 211 N TYR H 194 SHEET 1 AD6 4 LEU L 4 THR L 7 0 SHEET 2 AD6 4 THR L 18 SER L 25 -1 O GLN L 24 N THR L 5 SHEET 3 AD6 4 GLN L 70 SER L 76 -1 O LEU L 73 N ILE L 21 SHEET 4 AD6 4 PHE L 62 SER L 67 -1 N LYS L 63 O THR L 74 SHEET 1 AD7 6 SER L 10 ALA L 13 0 SHEET 2 AD7 6 THR L 102 VAL L 106 1 O VAL L 105 N VAL L 11 SHEET 3 AD7 6 THR L 85 GLY L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AD7 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 85 SHEET 5 AD7 6 LYS L 45 TYR L 49 -1 O LYS L 45 N GLN L 37 SHEET 6 AD7 6 THR L 53 LEU L 54 -1 O THR L 53 N TYR L 49 SHEET 1 AD8 4 SER L 114 PHE L 118 0 SHEET 2 AD8 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116 SHEET 3 AD8 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AD8 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AD9 4 ALA L 153 LEU L 154 0 SHEET 2 AD9 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AD9 4 VAL L 191 THR L 197 -1 O ALA L 193 N LYS L 149 SHEET 4 AD9 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SHEET 1 AE1 4 SER M 3 SER M 7 0 SHEET 2 AE1 4 LEU M 18 SER M 25 -1 O THR M 23 N GLU M 5 SHEET 3 AE1 4 THR M 77 MET M 82 -1 O MET M 82 N LEU M 18 SHEET 4 AE1 4 PHE M 67 LYS M 71 -1 N THR M 68 O GLN M 81 SHEET 1 AE2 6 LEU M 11 VAL M 12 0 SHEET 2 AE2 6 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 3 AE2 6 ALA M 88 TYR M 99 -1 N TYR M 90 O THR M 107 SHEET 4 AE2 6 TYR M 34 GLN M 39 -1 N VAL M 37 O PHE M 91 SHEET 5 AE2 6 GLU M 46 TYR M 52 -1 O ILE M 51 N MET M 35 SHEET 6 AE2 6 ALA M 57 TYR M 59 -1 O TYR M 58 N CYS M 50 SHEET 1 AE3 4 LEU M 11 VAL M 12 0 SHEET 2 AE3 4 THR M 107 VAL M 111 1 O THR M 110 N VAL M 12 SHEET 3 AE3 4 ALA M 88 TYR M 99 -1 N TYR M 90 O THR M 107 SHEET 4 AE3 4 VAL M 100D TRP M 103 -1 O ARG M 100G N VAL M 96 SHEET 1 AE4 4 SER M 120 LEU M 124 0 SHEET 2 AE4 4 ALA M 136 TYR M 145 -1 O LEU M 141 N PHE M 122 SHEET 3 AE4 4 TYR M 176 VAL M 184 -1 O LEU M 178 N VAL M 142 SHEET 4 AE4 4 VAL M 163 THR M 165 -1 N HIS M 164 O VAL M 181 SHEET 1 AE5 4 SER M 120 LEU M 124 0 SHEET 2 AE5 4 ALA M 136 TYR M 145 -1 O LEU M 141 N PHE M 122 SHEET 3 AE5 4 TYR M 176 VAL M 184 -1 O LEU M 178 N VAL M 142 SHEET 4 AE5 4 VAL M 169 LEU M 170 -1 N VAL M 169 O SER M 177 SHEET 1 AE6 3 THR M 151 TRP M 154 0 SHEET 2 AE6 3 TYR M 194 HIS M 200 -1 O ASN M 197 N SER M 153 SHEET 3 AE6 3 THR M 205 VAL M 211 -1 O VAL M 211 N TYR M 194 SHEET 1 AE7 4 LEU N 4 THR N 7 0 SHEET 2 AE7 4 THR N 18 SER N 25 -1 O GLN N 24 N THR N 5 SHEET 3 AE7 4 GLN N 70 SER N 76 -1 O LEU N 73 N ILE N 21 SHEET 4 AE7 4 PHE N 62 SER N 67 -1 N SER N 65 O THR N 72 SHEET 1 AE8 6 SER N 10 ALA N 13 0 SHEET 2 AE8 6 THR N 102 VAL N 106 1 O VAL N 105 N VAL N 11 SHEET 3 AE8 6 THR N 85 GLY N 90 -1 N TYR N 86 O THR N 102 SHEET 4 AE8 6 LEU N 33 GLN N 38 -1 N SER N 34 O GLN N 89 SHEET 5 AE8 6 LYS N 45 TYR N 49 -1 O LYS N 45 N GLN N 37 SHEET 6 AE8 6 THR N 53 LEU N 54 -1 O THR N 53 N TYR N 49 SHEET 1 AE9 4 SER N 114 PHE N 118 0 SHEET 2 AE9 4 THR N 129 PHE N 139 -1 O LEU N 135 N PHE N 116 SHEET 3 AE9 4 TYR N 173 SER N 182 -1 O LEU N 179 N VAL N 132 SHEET 4 AE9 4 SER N 159 VAL N 163 -1 N GLN N 160 O THR N 178 SHEET 1 AF1 4 ALA N 153 LEU N 154 0 SHEET 2 AF1 4 LYS N 145 VAL N 150 -1 N VAL N 150 O ALA N 153 SHEET 3 AF1 4 VAL N 191 THR N 197 -1 O THR N 197 N LYS N 145 SHEET 4 AF1 4 VAL N 205 ASN N 210 -1 O LYS N 207 N CYS N 194 SHEET 1 AF2 4 SER P 3 SER P 7 0 SHEET 2 AF2 4 LEU P 18 SER P 25 -1 O THR P 21 N SER P 7 SHEET 3 AF2 4 THR P 77 MET P 82 -1 O MET P 82 N LEU P 18 SHEET 4 AF2 4 PHE P 67 LYS P 71 -1 N THR P 68 O GLN P 81 SHEET 1 AF3 6 LEU P 11 VAL P 12 0 SHEET 2 AF3 6 THR P 107 VAL P 111 1 O THR P 110 N VAL P 12 SHEET 3 AF3 6 ALA P 88 TYR P 99 -1 N TYR P 90 O THR P 107 SHEET 4 AF3 6 TYR P 34 GLN P 39 -1 N TYR P 34 O GLY P 95 SHEET 5 AF3 6 GLU P 46 TYR P 52 -1 O ILE P 48 N TRP P 36 SHEET 6 AF3 6 ALA P 57 TYR P 59 -1 O TYR P 58 N CYS P 50 SHEET 1 AF4 4 LEU P 11 VAL P 12 0 SHEET 2 AF4 4 THR P 107 VAL P 111 1 O THR P 110 N VAL P 12 SHEET 3 AF4 4 ALA P 88 TYR P 99 -1 N TYR P 90 O THR P 107 SHEET 4 AF4 4 VAL P 100D TRP P 103 -1 O ARG P 100G N VAL P 96 SHEET 1 AF5 4 SER P 120 LEU P 124 0 SHEET 2 AF5 4 ALA P 136 TYR P 145 -1 O LEU P 141 N PHE P 122 SHEET 3 AF5 4 TYR P 176 VAL P 184 -1 O VAL P 184 N ALA P 136 SHEET 4 AF5 4 VAL P 163 THR P 165 -1 N HIS P 164 O VAL P 181 SHEET 1 AF6 4 SER P 120 LEU P 124 0 SHEET 2 AF6 4 ALA P 136 TYR P 145 -1 O LEU P 141 N PHE P 122 SHEET 3 AF6 4 TYR P 176 VAL P 184 -1 O VAL P 184 N ALA P 136 SHEET 4 AF6 4 VAL P 169 LEU P 170 -1 N VAL P 169 O SER P 177 SHEET 1 AF7 3 THR P 151 TRP P 154 0 SHEET 2 AF7 3 ILE P 195 HIS P 200 -1 O ASN P 197 N SER P 153 SHEET 3 AF7 3 THR P 205 ARG P 210 -1 O VAL P 207 N VAL P 198 SHEET 1 AF8 4 LEU Q 4 THR Q 7 0 SHEET 2 AF8 4 THR Q 18 SER Q 25 -1 O GLN Q 24 N THR Q 5 SHEET 3 AF8 4 GLN Q 70 SER Q 76 -1 O LEU Q 73 N ILE Q 21 SHEET 4 AF8 4 PHE Q 62 SER Q 67 -1 N SER Q 65 O THR Q 72 SHEET 1 AF9 6 SER Q 10 ALA Q 14 0 SHEET 2 AF9 6 THR Q 102 LYS Q 107 1 O GLU Q 103 N VAL Q 11 SHEET 3 AF9 6 THR Q 85 GLY Q 90 -1 N TYR Q 86 O THR Q 102 SHEET 4 AF9 6 LEU Q 33 GLN Q 38 -1 N GLN Q 38 O THR Q 85 SHEET 5 AF9 6 LYS Q 45 TYR Q 49 -1 O LYS Q 45 N GLN Q 37 SHEET 6 AF9 6 THR Q 53 LEU Q 54 -1 O THR Q 53 N TYR Q 49 SHEET 1 AG1 4 SER Q 114 PHE Q 118 0 SHEET 2 AG1 4 THR Q 129 PHE Q 139 -1 O LEU Q 135 N PHE Q 116 SHEET 3 AG1 4 TYR Q 173 SER Q 182 -1 O LEU Q 179 N VAL Q 132 SHEET 4 AG1 4 SER Q 159 VAL Q 163 -1 N GLN Q 160 O THR Q 178 SHEET 1 AG2 4 ALA Q 153 LEU Q 154 0 SHEET 2 AG2 4 LYS Q 145 VAL Q 150 -1 N VAL Q 150 O ALA Q 153 SHEET 3 AG2 4 VAL Q 191 THR Q 197 -1 O GLU Q 195 N GLN Q 147 SHEET 4 AG2 4 VAL Q 205 ASN Q 210 -1 O VAL Q 205 N VAL Q 196 SSBOND 1 CYS A 336 CYS A 361 1555 1555 2.03 SSBOND 2 CYS A 379 CYS A 432 1555 1555 2.04 SSBOND 3 CYS A 391 CYS A 525 1555 1555 2.04 SSBOND 4 CYS A 480 CYS A 488 1555 1555 2.03 SSBOND 5 CYS B 336 CYS B 361 1555 1555 2.03 SSBOND 6 CYS B 379 CYS B 432 1555 1555 2.04 SSBOND 7 CYS B 391 CYS B 525 1555 1555 2.03 SSBOND 8 CYS B 480 CYS B 488 1555 1555 2.03 SSBOND 9 CYS C 336 CYS C 361 1555 1555 2.03 SSBOND 10 CYS C 379 CYS C 432 1555 1555 2.04 SSBOND 11 CYS C 391 CYS C 525 1555 1555 2.03 SSBOND 12 CYS C 480 CYS C 488 1555 1555 2.03 SSBOND 13 CYS D 336 CYS D 361 1555 1555 2.03 SSBOND 14 CYS D 379 CYS D 432 1555 1555 2.03 SSBOND 15 CYS D 391 CYS D 525 1555 1555 2.03 SSBOND 16 CYS D 480 CYS D 488 1555 1555 2.03 SSBOND 17 CYS E 22 CYS E 92 1555 1555 2.03 SSBOND 18 CYS E 35A CYS E 50 1555 1555 2.04 SSBOND 19 CYS E 140 CYS E 196 1555 1555 2.03 SSBOND 20 CYS F 23 CYS F 88 1555 1555 2.04 SSBOND 21 CYS F 134 CYS F 194 1555 1555 2.03 SSBOND 22 CYS H 22 CYS H 92 1555 1555 2.03 SSBOND 23 CYS H 35A CYS H 50 1555 1555 2.04 SSBOND 24 CYS H 140 CYS H 196 1555 1555 2.03 SSBOND 25 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 26 CYS L 134 CYS L 194 1555 1555 2.03 SSBOND 27 CYS M 22 CYS M 92 1555 1555 2.03 SSBOND 28 CYS M 35A CYS M 50 1555 1555 2.04 SSBOND 29 CYS M 140 CYS M 196 1555 1555 2.03 SSBOND 30 CYS N 23 CYS N 88 1555 1555 2.04 SSBOND 31 CYS N 134 CYS N 194 1555 1555 2.03 SSBOND 32 CYS P 22 CYS P 92 1555 1555 2.03 SSBOND 33 CYS P 35A CYS P 50 1555 1555 2.04 SSBOND 34 CYS P 140 CYS P 196 1555 1555 2.03 SSBOND 35 CYS Q 23 CYS Q 88 1555 1555 2.04 SSBOND 36 CYS Q 134 CYS Q 194 1555 1555 2.03 LINK ND2 ASN A 343 C1 NAG G 1 1555 1555 1.44 LINK ND2 ASN B 343 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN C 343 C1 NAG J 1 1555 1555 1.44 LINK ND2 ASN D 343 C1 NAG K 1 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.44 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 LINK O4 NAG K 1 C1 NAG K 2 1555 1555 1.44 CISPEP 1 PHE E 146 PRO E 147 0 -5.58 CISPEP 2 GLU E 148 PRO E 149 0 -3.55 CISPEP 3 THR F 7 PRO F 8 0 -7.93 CISPEP 4 TYR F 140 PRO F 141 0 -1.91 CISPEP 5 PHE H 146 PRO H 147 0 -3.24 CISPEP 6 GLU H 148 PRO H 149 0 0.30 CISPEP 7 THR L 7 PRO L 8 0 -7.19 CISPEP 8 TYR L 140 PRO L 141 0 1.72 CISPEP 9 PHE M 146 PRO M 147 0 -4.61 CISPEP 10 GLU M 148 PRO M 149 0 -3.76 CISPEP 11 THR N 7 PRO N 8 0 -8.48 CISPEP 12 TYR N 140 PRO N 141 0 1.92 CISPEP 13 PHE P 146 PRO P 147 0 -3.78 CISPEP 14 GLU P 148 PRO P 149 0 -3.13 CISPEP 15 THR Q 7 PRO Q 8 0 -7.32 CISPEP 16 TYR Q 140 PRO Q 141 0 2.50 CRYST1 175.074 173.441 129.928 90.00 116.55 90.00 C 1 2 1 16 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 0.005712 0.000000 0.002854 0.00000 SCALE2 0.000000 0.005766 0.000000 0.00000 SCALE3 0.000000 0.000000 0.008604 0.00000