HEADER VIRAL PROTEIN, HYDROLASE/IMMUNE SYSTEM 06-JAN-25 9MQV TITLE CRYSTAL STRUCTURE OF HUMAN 1122A11 FAB IN COMPLEX WITH INFLUENZA VIRUS TITLE 2 NEURAMINIDASE FROM A/SINGAPORE/INFIMH-16-0019/2016 (H3N2) COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEURAMINIDASE; COMPND 3 CHAIN: A; COMPND 4 EC: 3.2.1.18; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: 1122A11 FAB IGG1 HEAVY CHAIN; COMPND 8 CHAIN: H; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: 1122A11 FAB LAMBDA LIGHT CHAIN; COMPND 12 CHAIN: L; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: INFLUENZA A VIRUS; SOURCE 3 ORGANISM_TAXID: 11320; SOURCE 4 GENE: NA; SOURCE 5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 13 EXPRESSION_SYSTEM_STRAIN: EXPICHO; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_COMMON: HUMAN; SOURCE 17 ORGANISM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 20 EXPRESSION_SYSTEM_STRAIN: EXPICHO KEYWDS HYDROLASE, IMMUNE SYSTEM, INFLUENZA VIRUS, NEURAMINIDASE, KEYWDS 2 NEUTRALIZATION, SUBSTRATE MIMICRY, VIRAL PROTEIN, HYDROLASE-IMMUNE KEYWDS 3 SYSTEM COMPLEX EXPDTA X-RAY DIFFRACTION AUTHOR X.ZHU,I.A.WILSON REVDAT 1 23-JUL-25 9MQV 0 JRNL AUTH X.ZHU,A.M.KHALIL,M.S.PIEPENBRINK,W.YU,Y.MA, JRNL AUTH 2 L.MARTINEZ-SOBRIDO,I.A.WILSON,J.J.KOBIE JRNL TITL STRUCTURE AND FUNCTION OF A CROSS-NEUTRALIZING INFLUENZA JRNL TITL 2 NEURAMINIDASE ANTIBODY THAT ACCOMMODATES RECENT N2 NA ASN245 JRNL TITL 3 GLYCOSYLATION. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 40631320 JRNL DOI 10.1101/2025.06.30.662356 REMARK 2 REMARK 2 RESOLUTION. 2.20 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.19.2_4158: ???) 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) : 2.20 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 38.63 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.5 REMARK 3 NUMBER OF REFLECTIONS : 51678 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.170 REMARK 3 R VALUE (WORKING SET) : 0.169 REMARK 3 FREE R VALUE : 0.204 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.150 REMARK 3 FREE R VALUE TEST SET COUNT : 2660 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 38.6300 - 5.8600 0.98 2642 148 0.1706 0.1821 REMARK 3 2 5.8600 - 4.6500 1.00 2571 199 0.1269 0.1452 REMARK 3 3 4.6500 - 4.0700 1.00 2649 108 0.1186 0.1640 REMARK 3 4 4.0700 - 3.6900 1.00 2553 158 0.1419 0.1957 REMARK 3 5 3.6900 - 3.4300 1.00 2616 130 0.1481 0.1751 REMARK 3 6 3.4300 - 3.2300 1.00 2610 120 0.1706 0.2299 REMARK 3 7 3.2300 - 3.0700 0.99 2541 160 0.1827 0.2303 REMARK 3 8 3.0700 - 2.9300 1.00 2616 140 0.1859 0.2324 REMARK 3 9 2.9300 - 2.8200 1.00 2543 170 0.1857 0.2259 REMARK 3 10 2.8200 - 2.7200 1.00 2619 115 0.1948 0.2270 REMARK 3 11 2.7200 - 2.6400 1.00 2549 158 0.2033 0.2520 REMARK 3 12 2.6400 - 2.5600 1.00 2576 138 0.2017 0.2264 REMARK 3 13 2.5600 - 2.4900 0.99 2545 146 0.2064 0.2630 REMARK 3 14 2.4900 - 2.4300 1.00 2594 117 0.2100 0.2475 REMARK 3 15 2.4300 - 2.3800 1.00 2584 143 0.2138 0.2625 REMARK 3 16 2.3800 - 2.3300 1.00 2581 97 0.2229 0.2285 REMARK 3 17 2.3300 - 2.2800 1.00 2602 118 0.2318 0.3017 REMARK 3 18 2.2800 - 2.2400 0.99 2559 137 0.2508 0.2661 REMARK 3 19 2.2400 - 2.2000 0.96 2468 158 0.2842 0.3378 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.11 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.250 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.820 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 39.00 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 : 0.003 6600 REMARK 3 ANGLE : 0.586 8975 REMARK 3 CHIRALITY : 0.044 1047 REMARK 3 PLANARITY : 0.004 1127 REMARK 3 DIHEDRAL : 5.942 1012 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 82 THROUGH 267 ) REMARK 3 ORIGIN FOR THE GROUP (A): 16.3593 14.6839 24.9758 REMARK 3 T TENSOR REMARK 3 T11: 0.2271 T22: 0.2434 REMARK 3 T33: 0.2178 T12: -0.0214 REMARK 3 T13: -0.0038 T23: -0.0319 REMARK 3 L TENSOR REMARK 3 L11: 0.7587 L22: 0.8363 REMARK 3 L33: 0.5628 L12: -0.0824 REMARK 3 L13: 0.1286 L23: 0.1322 REMARK 3 S TENSOR REMARK 3 S11: 0.0310 S12: -0.1432 S13: 0.0531 REMARK 3 S21: 0.1341 S22: 0.0112 S23: -0.0578 REMARK 3 S31: -0.0368 S32: 0.0656 S33: -0.0361 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 268 THROUGH 351 ) REMARK 3 ORIGIN FOR THE GROUP (A): 36.8755 17.4890 25.6542 REMARK 3 T TENSOR REMARK 3 T11: 0.3093 T22: 0.3707 REMARK 3 T33: 0.3817 T12: -0.0409 REMARK 3 T13: -0.0494 T23: -0.0575 REMARK 3 L TENSOR REMARK 3 L11: 1.9113 L22: 1.4031 REMARK 3 L33: 1.5881 L12: -0.0809 REMARK 3 L13: -0.1562 L23: 0.3982 REMARK 3 S TENSOR REMARK 3 S11: -0.0589 S12: -0.1027 S13: 0.1571 REMARK 3 S21: 0.0140 S22: 0.0393 S23: -0.2234 REMARK 3 S31: -0.1981 S32: 0.2419 S33: -0.0260 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 352 THROUGH 406 ) REMARK 3 ORIGIN FOR THE GROUP (A): 38.3476 4.3225 21.3645 REMARK 3 T TENSOR REMARK 3 T11: 0.2352 T22: 0.3130 REMARK 3 T33: 0.3322 T12: -0.0012 REMARK 3 T13: -0.0403 T23: -0.0407 REMARK 3 L TENSOR REMARK 3 L11: 1.9740 L22: 1.3709 REMARK 3 L33: 1.2264 L12: 0.0384 REMARK 3 L13: 0.4626 L23: 0.0185 REMARK 3 S TENSOR REMARK 3 S11: 0.1038 S12: -0.0598 S13: -0.1374 REMARK 3 S21: 0.1394 S22: -0.0063 S23: -0.3214 REMARK 3 S31: 0.0243 S32: 0.2549 S33: -0.0947 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: CHAIN 'A' AND (RESID 407 THROUGH 468 ) REMARK 3 ORIGIN FOR THE GROUP (A): 23.8782 1.8344 16.9052 REMARK 3 T TENSOR REMARK 3 T11: 0.1732 T22: 0.2301 REMARK 3 T33: 0.2579 T12: -0.0113 REMARK 3 T13: -0.0088 T23: -0.0284 REMARK 3 L TENSOR REMARK 3 L11: 1.6562 L22: 1.7532 REMARK 3 L33: 1.0863 L12: -0.1907 REMARK 3 L13: 0.2687 L23: -0.4619 REMARK 3 S TENSOR REMARK 3 S11: -0.0089 S12: 0.0327 S13: -0.0114 REMARK 3 S21: -0.0258 S22: 0.0454 S23: -0.0390 REMARK 3 S31: 0.0164 S32: 0.0267 S33: -0.1120 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 1 THROUGH 87 ) REMARK 3 ORIGIN FOR THE GROUP (A): 34.0955 26.0491 -8.9629 REMARK 3 T TENSOR REMARK 3 T11: 0.2877 T22: 0.3009 REMARK 3 T33: 0.3244 T12: -0.0442 REMARK 3 T13: 0.0718 T23: -0.0861 REMARK 3 L TENSOR REMARK 3 L11: 1.2520 L22: 2.9655 REMARK 3 L33: 2.7130 L12: 0.8638 REMARK 3 L13: -0.6731 L23: -0.9512 REMARK 3 S TENSOR REMARK 3 S11: -0.2090 S12: 0.2134 S13: -0.1570 REMARK 3 S21: -0.4845 S22: 0.0565 S23: -0.2614 REMARK 3 S31: 0.0999 S32: 0.1852 S33: 0.1227 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 88 THROUGH 136 ) REMARK 3 ORIGIN FOR THE GROUP (A): 31.2009 34.3360 -10.5090 REMARK 3 T TENSOR REMARK 3 T11: 0.2701 T22: 0.2610 REMARK 3 T33: 0.3332 T12: -0.0453 REMARK 3 T13: 0.0311 T23: -0.0706 REMARK 3 L TENSOR REMARK 3 L11: 0.2872 L22: 2.7337 REMARK 3 L33: 1.2059 L12: -0.0748 REMARK 3 L13: -0.0816 L23: -1.3607 REMARK 3 S TENSOR REMARK 3 S11: 0.0322 S12: 0.0249 S13: 0.0624 REMARK 3 S21: -0.2669 S22: -0.0101 S23: -0.0669 REMARK 3 S31: 0.0415 S32: -0.0052 S33: 0.0005 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: CHAIN 'H' AND (RESID 137 THROUGH 231 ) REMARK 3 ORIGIN FOR THE GROUP (A): 32.4543 55.0635 -35.7198 REMARK 3 T TENSOR REMARK 3 T11: 0.7525 T22: 0.5044 REMARK 3 T33: 0.7852 T12: 0.1181 REMARK 3 T13: 0.0168 T23: 0.0641 REMARK 3 L TENSOR REMARK 3 L11: 1.8780 L22: 3.1798 REMARK 3 L33: 3.4268 L12: -0.1623 REMARK 3 L13: 0.8210 L23: -1.2524 REMARK 3 S TENSOR REMARK 3 S11: -0.0474 S12: 0.2414 S13: 0.5409 REMARK 3 S21: -0.4086 S22: -0.3432 S23: -1.0870 REMARK 3 S31: 0.7576 S32: 0.1341 S33: 0.3486 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 1 THROUGH 106 ) REMARK 3 ORIGIN FOR THE GROUP (A): 25.5158 45.2110 2.2300 REMARK 3 T TENSOR REMARK 3 T11: 0.4454 T22: 0.2521 REMARK 3 T33: 0.3167 T12: -0.0132 REMARK 3 T13: 0.0969 T23: -0.0252 REMARK 3 L TENSOR REMARK 3 L11: 1.7196 L22: 3.8409 REMARK 3 L33: 2.9083 L12: -0.4938 REMARK 3 L13: 0.1489 L23: -1.7068 REMARK 3 S TENSOR REMARK 3 S11: 0.0621 S12: -0.1716 S13: 0.2242 REMARK 3 S21: 0.5106 S22: 0.0907 S23: 0.2573 REMARK 3 S31: -0.7666 S32: -0.0529 S33: -0.1301 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: CHAIN 'L' AND (RESID 106A THROUGH 212 ) REMARK 3 ORIGIN FOR THE GROUP (A): 18.6250 53.5713 -26.5329 REMARK 3 T TENSOR REMARK 3 T11: 0.6913 T22: 0.5298 REMARK 3 T33: 0.4703 T12: -0.1680 REMARK 3 T13: -0.1107 T23: 0.1294 REMARK 3 L TENSOR REMARK 3 L11: 1.5184 L22: 2.9894 REMARK 3 L33: 4.3471 L12: 0.2144 REMARK 3 L13: 0.7435 L23: 1.0482 REMARK 3 S TENSOR REMARK 3 S11: 0.1679 S12: 0.0084 S13: -0.0771 REMARK 3 S21: -0.4361 S22: 0.0843 S23: 0.3593 REMARK 3 S31: 0.5961 S32: -0.8764 S33: -0.2431 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 9MQV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-25. REMARK 100 THE DEPOSITION ID IS D_1000291571. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 05-FEB-21 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8.0 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) : 0.97946 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS3 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : HKL-3000 REMARK 200 DATA SCALING SOFTWARE : HKL-3000 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 51700 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.200 REMARK 200 RESOLUTION RANGE LOW (A) : 38.630 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.6 REMARK 200 DATA REDUNDANCY : 12.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : 0.13000 REMARK 200 FOR THE DATA SET : 18.1000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.25 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : 1.00000 REMARK 200 FOR SHELL : 1.100 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 (%): 56.25 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.81 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M TRI-POTASSIUM CITRATE AND 20% REMARK 280 (W/V) POLYETHYLENE GLYCOL 3350, PH 8.0, VAPOR DIFFUSION, SITTING REMARK 280 DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 4 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 -Y,X,Z REMARK 290 4555 Y,-X,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 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DODECAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DODECAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 52530 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 121970 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 44.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, H, L, B, C, D, E 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 BIOMT1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT3 2 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 3 0.000000 -1.000000 0.000000 0.00000 REMARK 350 BIOMT2 3 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 3 0.000000 0.000000 1.000000 0.00000 REMARK 350 BIOMT1 4 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT2 4 -1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT3 4 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 GLY A 75 REMARK 465 SER A 76 REMARK 465 PRO A 77 REMARK 465 SER A 78 REMARK 465 ARG A 79 REMARK 465 SER A 80 REMARK 465 GLY A 81 REMARK 465 ALA A 246 REMARK 465 THR A 247 REMARK 465 GLY A 248 REMARK 465 LYS A 249 REMARK 465 ALA A 250 REMARK 465 ILE A 469 REMARK 465 SER H 130 REMARK 465 LYS H 131 REMARK 465 SER H 132 REMARK 465 THR H 133 REMARK 465 SER H 134 REMARK 465 GLY H 135 REMARK 465 HIS H 232 REMARK 465 HIS H 233 REMARK 465 HIS H 234 REMARK 465 HIS H 235 REMARK 465 HIS H 236 REMARK 465 GLU L 213 REMARK 465 CYS L 214 REMARK 465 SER L 215 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 PHE A 100 -50.46 -126.81 REMARK 500 ASN A 200 51.27 -158.19 REMARK 500 ASP A 221 68.68 -153.99 REMARK 500 ILE A 222 86.22 63.78 REMARK 500 THR A 225 -151.52 -135.21 REMARK 500 CYS A 291 -156.45 -122.06 REMARK 500 SER A 315 -146.98 -147.78 REMARK 500 SER A 404 -137.96 -116.66 REMARK 500 TYR H 100J -73.32 -117.41 REMARK 500 SER H 112 139.99 -170.01 REMARK 500 ASP H 146 75.32 52.34 REMARK 500 ASP L 51 -44.51 71.90 REMARK 500 ASN L 52 19.45 -150.81 REMARK 500 SER L 94 -6.95 70.60 REMARK 500 ASP L 151 -91.85 56.62 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 CA A 501 CA REMARK 620 N RES CSSEQI ATOM REMARK 620 1 ASP A 293 O REMARK 620 2 GLY A 297 O 74.0 REMARK 620 3 ASP A 324 OD2 98.6 101.7 REMARK 620 4 HIS A 347 O 97.9 146.4 111.7 REMARK 620 5 HOH A 632 O 157.3 98.8 104.0 75.9 REMARK 620 N 1 2 3 4 DBREF1 9MQV A 82 469 UNP A0A5B8WQ58_9INFA DBREF2 9MQV A A0A5B8WQ58 82 469 DBREF 9MQV H 1 236 PDB 9MQV 9MQV 1 236 DBREF 9MQV L 1 215 PDB 9MQV 9MQV 1 215 SEQADV 9MQV GLY A 75 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV SER A 76 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV PRO A 77 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV SER A 78 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV ARG A 79 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV SER A 80 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV GLY A 81 UNP A0A5B8WQ5 EXPRESSION TAG SEQADV 9MQV ILE A 212 UNP A0A5B8WQ5 VAL 212 CONFLICT SEQADV 9MQV ASN A 329 UNP A0A5B8WQ5 SER 329 CONFLICT SEQRES 1 A 395 GLY SER PRO SER ARG SER GLY ALA GLU TYR ARG ASN TRP SEQRES 2 A 395 SER LYS PRO GLN CYS GLY ILE THR GLY PHE ALA PRO PHE SEQRES 3 A 395 SER LYS ASP ASN SER ILE ARG LEU SER ALA GLY GLY ASP SEQRES 4 A 395 ILE TRP VAL THR ARG GLU PRO TYR VAL SER CYS ASP PRO SEQRES 5 A 395 ASP LYS CYS TYR GLN PHE ALA LEU GLY GLN GLY THR THR SEQRES 6 A 395 LEU ASN ASN VAL HIS SER ASN ASN THR VAL ARG ASP ARG SEQRES 7 A 395 THR PRO TYR ARG THR LEU LEU MET ASN GLU LEU GLY VAL SEQRES 8 A 395 PRO PHE HIS LEU GLY THR LYS GLN VAL CYS ILE ALA TRP SEQRES 9 A 395 SER SER SER SER CYS HIS ASP GLY LYS ALA TRP LEU HIS SEQRES 10 A 395 VAL CYS ILE THR GLY ASP ASP LYS ASN ALA THR ALA SER SEQRES 11 A 395 PHE ILE TYR ASN GLY ARG LEU ILE ASP SER VAL VAL SER SEQRES 12 A 395 TRP SER LYS ASP ILE LEU ARG THR GLN GLU SER GLU CYS SEQRES 13 A 395 VAL CYS ILE ASN GLY THR CYS THR VAL VAL MET THR ASP SEQRES 14 A 395 GLY ASN ALA THR GLY LYS ALA ASP THR LYS ILE LEU PHE SEQRES 15 A 395 ILE GLU GLU GLY LYS ILE VAL HIS THR SER LYS LEU SER SEQRES 16 A 395 GLY SER ALA GLN HIS VAL GLU GLU CYS SER CYS TYR PRO SEQRES 17 A 395 ARG TYR PRO GLY VAL ARG CYS VAL CYS ARG ASP ASN TRP SEQRES 18 A 395 LYS GLY SER ASN ARG PRO ILE VAL ASP ILE ASN ILE LYS SEQRES 19 A 395 ASP HIS SER ILE VAL SER SER TYR VAL CYS SER GLY LEU SEQRES 20 A 395 VAL GLY ASP THR PRO ARG LYS ASN ASP SER SER SER SER SEQRES 21 A 395 SER HIS CYS LEU ASN PRO ASN ASN GLU GLU GLY GLY HIS SEQRES 22 A 395 GLY VAL LYS GLY TRP ALA PHE ASP ASP GLY ASN ASP VAL SEQRES 23 A 395 TRP MET GLY ARG THR ILE ASN GLU THR SER ARG LEU GLY SEQRES 24 A 395 TYR GLU THR PHE LYS VAL VAL GLU GLY TRP SER ASN PRO SEQRES 25 A 395 LYS SER LYS LEU GLN ILE ASN ARG GLN VAL ILE VAL ASP SEQRES 26 A 395 ARG GLY ASP ARG SER GLY TYR SER GLY ILE PHE SER VAL SEQRES 27 A 395 GLU GLY LYS SER CYS ILE ASN ARG CYS PHE TYR VAL GLU SEQRES 28 A 395 LEU ILE ARG GLY ARG LYS GLU GLU THR GLU VAL LEU TRP SEQRES 29 A 395 THR SER ASN SER ILE VAL VAL PHE CYS GLY THR SER GLY SEQRES 30 A 395 THR TYR GLY THR GLY SER TRP PRO ASP GLY ALA ASP LEU SEQRES 31 A 395 ASN LEU MET HIS ILE SEQRES 1 H 238 GLN VAL GLN LEU VAL GLN SER GLY ALA GLU VAL SER LYS SEQRES 2 H 238 PRO GLY ALA SER VAL LYS VAL SER CYS LYS ALA SER GLY SEQRES 3 H 238 TYR SER PHE THR SER GLN SER LEU GLY TRP VAL ARG GLN SEQRES 4 H 238 ALA PRO GLY GLN GLY LEU GLU TRP MET GLY ILE ILE ASN SEQRES 5 H 238 PRO SER GLY GLY ILE THR ASN TYR ALA HIS LYS PHE GLN SEQRES 6 H 238 GLY ARG VAL THR MET THR ARG ASP THR SER THR SER THR SEQRES 7 H 238 VAL TYR MET GLU LEU SER SER LEU ARG SER GLU ASP THR SEQRES 8 H 238 ALA LEU TYR TYR CYS VAL ARG ASP LEU SER HIS TYR ASN SEQRES 9 H 238 GLU VAL GLY HIS ASP ARG ALA TYR TYR TYR GLY MET ASP SEQRES 10 H 238 ILE TRP GLY GLN GLY THR THR VAL THR VAL SER SER ALA SEQRES 11 H 238 SER THR LYS GLY PRO SER VAL PHE PRO LEU ALA PRO SER SEQRES 12 H 238 SER LYS SER THR SER GLY GLY THR ALA ALA LEU GLY CYS SEQRES 13 H 238 LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL THR VAL SER SEQRES 14 H 238 TRP ASN SER GLY ALA LEU THR SER GLY VAL HIS THR PHE SEQRES 15 H 238 PRO ALA VAL LEU GLN SER SER GLY LEU TYR SER LEU SER SEQRES 16 H 238 SER VAL VAL THR VAL PRO SER SER SER LEU GLY THR GLN SEQRES 17 H 238 THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SER ASN THR SEQRES 18 H 238 LYS VAL ASP LYS ARG VAL GLU PRO LYS SER CYS HIS HIS SEQRES 19 H 238 HIS HIS HIS HIS SEQRES 1 L 212 SER TYR GLU LEU ILE GLN PRO PRO SER VAL SER VAL SER SEQRES 2 L 212 PRO GLY GLN THR ALA SER ILE THR CYS SER GLY ASP LYS SEQRES 3 L 212 LEU GLY LYS LYS TYR THR CYS TRP TYR GLN GLN LYS PRO SEQRES 4 L 212 GLY GLN SER PRO VAL LEU VAL ILE TYR GLN ASP ASN LYS SEQRES 5 L 212 ARG PRO SER GLY ILE PRO GLU ARG PHE SER GLY SER ASN SEQRES 6 L 212 SER GLY ASN THR ALA THR LEU THR ILE SER GLY THR GLN SEQRES 7 L 212 ALA MET ASP GLU ALA ASP TYR TYR CYS GLN ALA TRP ASP SEQRES 8 L 212 SER SER ALA VAL VAL PHE GLY GLY GLY THR LYS LEU THR SEQRES 9 L 212 VAL LEU GLY GLN PRO LYS ALA ALA PRO SER VAL THR LEU SEQRES 10 L 212 PHE PRO PRO SER SER GLU GLU LEU GLN ALA ASN LYS ALA SEQRES 11 L 212 THR LEU VAL CYS LEU ILE SER ASP PHE TYR PRO GLY ALA SEQRES 12 L 212 VAL THR VAL ALA TRP LYS ALA ASP SER SER PRO VAL LYS SEQRES 13 L 212 ALA GLY VAL GLU THR THR THR PRO SER LYS GLN SER ASN SEQRES 14 L 212 ASN LYS TYR ALA ALA SER SER TYR LEU SER LEU THR PRO SEQRES 15 L 212 GLU GLN TRP LYS SER HIS ARG SER TYR SER CYS GLN VAL SEQRES 16 L 212 THR HIS GLU GLY SER THR VAL GLU LYS THR VAL ALA PRO SEQRES 17 L 212 THR GLU CYS SER HET NAG B 1 14 HET NAG B 2 14 HET BMA B 3 11 HET NAG C 1 14 HET NAG C 2 14 HET BMA C 3 11 HET MAN C 4 11 HET MAN C 5 11 HET MAN C 6 11 HET MAN C 7 11 HET MAN C 8 11 HET NAG D 1 14 HET NAG D 2 14 HET BMA D 3 11 HET NAG E 1 14 HET NAG E 2 14 HET CA A 501 1 HET NAG A 502 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM CA CALCIUM 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 4 NAG 9(C8 H15 N O6) FORMUL 4 BMA 3(C6 H12 O6) FORMUL 5 MAN 5(C6 H12 O6) FORMUL 8 CA CA 2+ FORMUL 10 HOH *365(H2 O) HELIX 1 AA1 ASN A 104 ALA A 110 1 7 HELIX 2 AA2 ASN A 142 ASN A 146 5 5 HELIX 3 AA3 ASP A 463 MET A 467 5 5 HELIX 4 AA4 SER H 28 GLN H 32 5 5 HELIX 5 AA5 HIS H 61 GLN H 64 5 4 HELIX 6 AA6 ARG H 83 THR H 87 5 5 HELIX 7 AA7 TYR H 99 GLY H 100C 5 5 HELIX 8 AA8 SER H 163 ALA H 165 5 3 HELIX 9 AA9 SER H 196 LEU H 198 5 3 HELIX 10 AB1 LYS L 27 LYS L 31 5 5 HELIX 11 AB2 GLN L 79 GLU L 83 5 5 HELIX 12 AB3 SER L 121 ALA L 127 1 7 HELIX 13 AB4 THR L 182 SER L 188 1 7 SHEET 1 AA1 4 GLY A 96 LYS A 102 0 SHEET 2 AA1 4 THR A 439 THR A 449 -1 O VAL A 445 N SER A 101 SHEET 3 AA1 4 ILE A 418 GLY A 429 -1 N LEU A 426 O SER A 442 SHEET 4 AA1 4 SER A 407 GLU A 413 -1 N VAL A 412 O ASN A 419 SHEET 1 AA2 4 TRP A 115 CYS A 124 0 SHEET 2 AA2 4 CYS A 129 THR A 139 -1 O PHE A 132 N TYR A 121 SHEET 3 AA2 4 THR A 157 GLU A 162 -1 O LEU A 159 N ALA A 133 SHEET 4 AA2 4 LYS A 172 ILE A 176 -1 O CYS A 175 N LEU A 158 SHEET 1 AA3 4 SER A 179 HIS A 184 0 SHEET 2 AA3 4 TRP A 189 ASP A 197 -1 O VAL A 192 N SER A 181 SHEET 3 AA3 4 ASN A 200 TYR A 207 -1 O SER A 204 N CYS A 193 SHEET 4 AA3 4 ARG A 210 VAL A 216 -1 O VAL A 215 N ALA A 203 SHEET 1 AA4 4 VAL A 231 ILE A 233 0 SHEET 2 AA4 4 THR A 236 THR A 242 -1 O THR A 238 N VAL A 231 SHEET 3 AA4 4 THR A 252 GLU A 258 -1 O LYS A 253 N MET A 241 SHEET 4 AA4 4 LYS A 261 LYS A 267 -1 O SER A 266 N ILE A 254 SHEET 1 AA5 4 GLU A 276 ARG A 283 0 SHEET 2 AA5 4 GLY A 286 ARG A 292 -1 O GLY A 286 N ARG A 283 SHEET 3 AA5 4 PRO A 301 ILE A 305 -1 O ILE A 305 N VAL A 287 SHEET 4 AA5 4 ILE A 312 TYR A 316 -1 O VAL A 313 N ASP A 304 SHEET 1 AA6 4 ALA A 353 ASP A 356 0 SHEET 2 AA6 4 ASP A 359 ARG A 364 -1 O TRP A 361 N PHE A 354 SHEET 3 AA6 4 LEU A 372 VAL A 379 -1 O GLU A 375 N ARG A 364 SHEET 4 AA6 4 GLN A 391 ARG A 403 -1 O ASP A 402 N GLY A 373 SHEET 1 AA7 4 GLN H 3 GLN H 6 0 SHEET 2 AA7 4 VAL H 18 SER H 25 -1 O LYS H 23 N VAL H 5 SHEET 3 AA7 4 THR H 77 LEU H 82 -1 O MET H 80 N VAL H 20 SHEET 4 AA7 4 VAL H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AA8 6 GLU H 10 SER H 12 0 SHEET 2 AA8 6 THR H 107 VAL H 111 1 O THR H 110 N SER H 12 SHEET 3 AA8 6 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA8 6 SER H 33 GLN H 39 -1 N VAL H 37 O TYR H 91 SHEET 5 AA8 6 LEU H 45 ILE H 51 -1 O ILE H 51 N LEU H 34 SHEET 6 AA8 6 THR H 57 TYR H 59 -1 O ASN H 58 N ILE H 50 SHEET 1 AA9 4 GLU H 10 SER H 12 0 SHEET 2 AA9 4 THR H 107 VAL H 111 1 O THR H 110 N SER H 12 SHEET 3 AA9 4 ALA H 88 ASP H 95 -1 N TYR H 90 O THR H 107 SHEET 4 AA9 4 MET H 100L TRP H 103 -1 O ILE H 102 N ARG H 94 SHEET 1 AB1 4 SER H 120 LEU H 124 0 SHEET 2 AB1 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 AB1 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 138 SHEET 4 AB1 4 VAL H 171 THR H 173 -1 N HIS H 172 O VAL H 190 SHEET 1 AB2 4 SER H 120 LEU H 124 0 SHEET 2 AB2 4 THR H 137 TYR H 147 -1 O LEU H 143 N PHE H 122 SHEET 3 AB2 4 TYR H 185 PRO H 194 -1 O VAL H 193 N ALA H 138 SHEET 4 AB2 4 VAL H 177 LEU H 178 -1 N VAL H 177 O SER H 186 SHEET 1 AB3 3 THR H 153 TRP H 157 0 SHEET 2 AB3 3 ILE H 207 HIS H 212 -1 O ASN H 209 N SER H 156 SHEET 3 AB3 3 THR H 217 ARG H 222 -1 O THR H 217 N HIS H 212 SHEET 1 AB4 5 SER L 9 VAL L 13 0 SHEET 2 AB4 5 THR L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AB4 5 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AB4 5 CYS L 34 GLN L 38 -1 N GLN L 38 O ASP L 85 SHEET 5 AB4 5 VAL L 45 ILE L 48 -1 O VAL L 45 N GLN L 37 SHEET 1 AB5 4 SER L 9 VAL L 13 0 SHEET 2 AB5 4 THR L 102 VAL L 106 1 O LYS L 103 N VAL L 11 SHEET 3 AB5 4 ALA L 84 ASP L 92 -1 N ALA L 84 O LEU L 104 SHEET 4 AB5 4 ALA L 95 PHE L 98 -1 O VAL L 97 N ALA L 90 SHEET 1 AB6 3 ALA L 19 SER L 24 0 SHEET 2 AB6 3 THR L 70 ILE L 75 -1 O ALA L 71 N CYS L 23 SHEET 3 AB6 3 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB7 4 SER L 114 PHE L 118 0 SHEET 2 AB7 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB7 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 139 SHEET 4 AB7 4 VAL L 159 THR L 161 -1 N GLU L 160 O TYR L 178 SHEET 1 AB8 4 SER L 114 PHE L 118 0 SHEET 2 AB8 4 ALA L 130 PHE L 139 -1 O VAL L 133 N PHE L 118 SHEET 3 AB8 4 TYR L 173 LEU L 181 -1 O TYR L 173 N PHE L 139 SHEET 4 AB8 4 SER L 165 LYS L 166 -1 N SER L 165 O ALA L 174 SHEET 1 AB9 4 SER L 153 VAL L 155 0 SHEET 2 AB9 4 THR L 145 ALA L 150 -1 N ALA L 150 O SER L 153 SHEET 3 AB9 4 TYR L 192 HIS L 198 -1 O GLN L 195 N ALA L 147 SHEET 4 AB9 4 SER L 203 VAL L 209 -1 O VAL L 205 N VAL L 196 SSBOND 1 CYS A 92 CYS A 417 1555 1555 2.04 SSBOND 2 CYS A 124 CYS A 129 1555 1555 2.03 SSBOND 3 CYS A 175 CYS A 193 1555 1555 2.03 SSBOND 4 CYS A 183 CYS A 230 1555 1555 2.04 SSBOND 5 CYS A 232 CYS A 237 1555 1555 2.03 SSBOND 6 CYS A 278 CYS A 291 1555 1555 2.04 SSBOND 7 CYS A 280 CYS A 289 1555 1555 2.03 SSBOND 8 CYS A 318 CYS A 337 1555 1555 2.04 SSBOND 9 CYS A 421 CYS A 447 1555 1555 2.04 SSBOND 10 CYS H 22 CYS H 92 1555 1555 2.04 SSBOND 11 CYS H 142 CYS H 208 1555 1555 2.04 SSBOND 12 CYS L 23 CYS L 88 1555 1555 2.04 SSBOND 13 CYS L 134 CYS L 194 1555 1555 2.03 LINK ND2 ASN A 146 C1 NAG D 1 1555 1555 1.44 LINK ND2 ASN A 200 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 234 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 329 C1 NAG A 502 1555 1555 1.44 LINK ND2 ASN A 367 C1 NAG B 1 1555 1555 1.44 LINK O4 NAG B 1 C1 NAG B 2 1555 1555 1.43 LINK O4 NAG B 2 C1 BMA B 3 1555 1555 1.45 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.44 LINK O4 NAG C 2 C1 BMA C 3 1555 1555 1.44 LINK O3 BMA C 3 C1 MAN C 4 1555 1555 1.44 LINK O6 BMA C 3 C1 MAN C 6 1555 1555 1.44 LINK O2 MAN C 4 C1 MAN C 5 1555 1555 1.44 LINK O3 MAN C 6 C1 MAN C 7 1555 1555 1.45 LINK O6 MAN C 6 C1 MAN C 8 1555 1555 1.44 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O4 NAG D 2 C1 BMA D 3 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O ASP A 293 CA CA A 501 1555 1555 2.51 LINK O GLY A 297 CA CA A 501 1555 1555 2.60 LINK OD2 ASP A 324 CA CA A 501 1555 1555 2.71 LINK O HIS A 347 CA CA A 501 1555 1555 2.66 LINK CA CA A 501 O HOH A 632 1555 1555 2.73 CISPEP 1 TYR A 284 PRO A 285 0 4.15 CISPEP 2 THR A 325 PRO A 326 0 4.58 CISPEP 3 ARG A 430 LYS A 431 0 3.53 CISPEP 4 PHE H 148 PRO H 149 0 -10.69 CISPEP 5 GLU H 150 PRO H 151 0 20.61 CISPEP 6 TYR L 140 PRO L 141 0 2.36 CRYST1 115.900 115.900 76.775 90.00 90.00 90.00 P 4 4 ORIGX1 1.000000 0.000000 0.000000 0.00000 ORIGX2 0.000000 1.000000 0.000000 0.00000 ORIGX3 0.000000 0.000000 1.000000 0.00000 SCALE1 0.008628 0.000000 0.000000 0.00000 SCALE2 0.000000 0.008628 0.000000 0.00000 SCALE3 0.000000 0.000000 0.013025 0.00000