HEADER CARBOHYDRATE 05-AUG-25 9S8W TITLE HUMAN HEPARANASE IN COMPLEX WITH NEUTRALIZING ANTIBODY A54 FAB TITLE 2 FRAGMENT COMPND MOL_ID: 1; COMPND 2 MOLECULE: HEPARANASE; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: ENDO-GLUCORONIDASE,HEPARANASE-1,HPA1; COMPND 5 EC: 3.2.1.166; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: HEPARANASE 8 KDA SUBUNIT; COMPND 9 CHAIN: B; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: A54 FAB HEAVY CHAIN; COMPND 13 CHAIN: H; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: A54 FAB LIGHT CHAIN; COMPND 17 CHAIN: L; COMPND 18 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: HPSE, HEP, HPA, HPA1, HPR1, HPSE1, HSE1; SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: HPSE, HEP, HPA, HPA1, HPR1, HPSE1, HSE1; SOURCE 13 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 17 ORGANISM_TAXID: 10090; SOURCE 18 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 10090; SOURCE 20 MOL_ID: 4; SOURCE 21 ORGANISM_SCIENTIFIC: MUS MUSCULUS; SOURCE 22 ORGANISM_TAXID: 10090; SOURCE 23 EXPRESSION_SYSTEM: MUS MUSCULUS; SOURCE 24 EXPRESSION_SYSTEM_TAXID: 10090 KEYWDS HEPARANASE, CARBOHYDRATE, GLYCOSAMINOGLYCAN, HYDROLASE, ANTIBODY, FAB EXPDTA X-RAY DIFFRACTION AUTHOR L.WU REVDAT 1 24-SEP-25 9S8W 0 JRNL AUTH U.BARASH,M.FARHOUD,M.ODEH,E.HUBERMAN,L.WU,I.VLODAVSKY JRNL TITL HEPARANASE-NEUTRALIZING MONOCLONAL ANTIBODY (MAB A54) JRNL TITL 2 ATTENUATES TUMOR GROWTH AND METASTASIS. JRNL REF CELLS V. 14 2025 JRNL REFN ESSN 2073-4409 JRNL PMID 40940793 JRNL DOI 10.3390/CELLS14171379 REMARK 2 REMARK 2 RESOLUTION. 3.49 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : REFMAC 5.8.0425 REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER, REMARK 3 : NICHOLLS,WINN,LONG,VAGIN REMARK 3 REMARK 3 REFINEMENT TARGET : NULL REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.49 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 107.44 REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL REMARK 3 COMPLETENESS FOR RANGE (%) : 63.4 REMARK 3 NUMBER OF REFLECTIONS : 9227 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : FREE R-VALUE REMARK 3 FREE R VALUE TEST SET SELECTION : NULL REMARK 3 R VALUE (WORKING + TEST SET) : NULL REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.323 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 465 REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.49 REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.58 REMARK 3 REFLECTION IN BIN (WORKING SET) : 24 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 2.68 REMARK 3 BIN R VALUE (WORKING SET) : 0.3880 REMARK 3 BIN FREE R VALUE SET COUNT : 3 REMARK 3 BIN FREE R VALUE : 0.2400 REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 6983 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 66 REMARK 3 SOLVENT ATOMS : 31 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 143.2 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -0.23700 REMARK 3 B22 (A**2) : -0.23700 REMARK 3 B33 (A**2) : 0.47500 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 0.00000 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED OVERALL COORDINATE ERROR. REMARK 3 ESU BASED ON R VALUE (A): NULL REMARK 3 ESU BASED ON FREE R VALUE (A): 1.200 REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.900 REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 130.966 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.928 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.833 REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7230 ; 0.008 ; 0.012 REMARK 3 BOND LENGTHS OTHERS (A): 6691 ; 0.001 ; 0.016 REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 9836 ; 1.813 ; 1.821 REMARK 3 BOND ANGLES OTHERS (DEGREES): 15485 ; 0.628 ; 1.744 REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 891 ; 6.650 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 31 ; 3.139 ; 5.000 REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1178 ;15.776 ;10.000 REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): NULL ; NULL ; NULL REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1105 ; 0.085 ; 0.200 REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8396 ; 0.007 ; 0.020 REMARK 3 GENERAL PLANES OTHERS (A): 1632 ; 0.001 ; 0.020 REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): 1238 ; 0.210 ; 0.200 REMARK 3 NON-BONDED CONTACTS OTHERS (A): 81 ; 0.270 ; 0.200 REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): 3484 ; 0.184 ; 0.200 REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): 132 ; 0.136 ; 0.200 REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL REMARK 3 REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3579 ; 2.760 ; 6.816 REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3579 ; 2.760 ; 6.816 REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4465 ; 4.764 ;12.262 REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): 4466 ; 4.763 ;12.262 REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3651 ; 3.238 ; 7.190 REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): 3651 ; 3.238 ; 7.190 REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5371 ; 5.684 ;13.149 REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): 5372 ; 5.684 ;13.148 REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL REMARK 3 REMARK 3 NCS RESTRAINTS STATISTICS REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : Ap 159 Ap 273 REMARK 3 ORIGIN FOR THE GROUP (A): -10.1943 7.7100 34.2310 REMARK 3 T TENSOR REMARK 3 T11: 0.1523 T22: 1.3572 REMARK 3 T33: 0.6275 T12: 0.2087 REMARK 3 T13: -0.1928 T23: -0.2867 REMARK 3 L TENSOR REMARK 3 L11: 4.1636 L22: 5.6003 REMARK 3 L33: 3.7303 L12: 2.3357 REMARK 3 L13: -0.5632 L23: -1.9848 REMARK 3 S TENSOR REMARK 3 S11: 0.4588 S12: -0.2634 S13: -0.3389 REMARK 3 S21: -0.0671 S22: -0.2893 S23: 0.9955 REMARK 3 S31: -0.3915 S32: -0.8224 S33: -0.1695 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : Ap 274 Ap 447 REMARK 3 ORIGIN FOR THE GROUP (A): 7.9266 5.2888 48.4260 REMARK 3 T TENSOR REMARK 3 T11: 0.0882 T22: 1.3193 REMARK 3 T33: 0.2275 T12: -0.0499 REMARK 3 T13: 0.0197 T23: -0.0596 REMARK 3 L TENSOR REMARK 3 L11: 2.5660 L22: 5.3471 REMARK 3 L33: 4.3165 L12: -0.8382 REMARK 3 L13: 1.7547 L23: -1.7035 REMARK 3 S TENSOR REMARK 3 S11: 0.0907 S12: -0.6129 S13: -0.0802 REMARK 3 S21: 0.3887 S22: -0.4978 S23: 0.1889 REMARK 3 S31: -0.3002 S32: -0.2874 S33: 0.4071 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 NUMBER OF COMPONENTS GROUP : 1 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 RESIDUE RANGE : Ap 448 Ap 543 REMARK 3 ORIGIN FOR THE GROUP (A): 12.9380 -1.7755 66.1639 REMARK 3 T TENSOR REMARK 3 T11: 0.4271 T22: 1.7310 REMARK 3 T33: 0.1991 T12: -0.1719 REMARK 3 T13: -0.0031 T23: 0.1385 REMARK 3 L TENSOR REMARK 3 L11: 2.4912 L22: 5.6993 REMARK 3 L33: 3.2796 L12: -0.1797 REMARK 3 L13: 0.9848 L23: 1.0632 REMARK 3 S TENSOR REMARK 3 S11: 0.0399 S12: -1.1810 S13: -0.1541 REMARK 3 S21: 1.5284 S22: -0.1614 S23: 0.0963 REMARK 3 S31: 0.1748 S32: -0.3539 S33: 0.1215 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 4.2237 3.8319 52.6271 REMARK 3 T TENSOR REMARK 3 T11: 0.2017 T22: 1.4536 REMARK 3 T33: 0.2543 T12: 0.0609 REMARK 3 T13: 0.1257 T23: 0.0566 REMARK 3 L TENSOR REMARK 3 L11: 5.4570 L22: 3.5495 REMARK 3 L33: 4.5623 L12: 1.1368 REMARK 3 L13: 3.0041 L23: 0.1882 REMARK 3 S TENSOR REMARK 3 S11: 0.2094 S12: -0.2426 S13: -0.2803 REMARK 3 S21: -0.0874 S22: 0.0860 S23: -0.1698 REMARK 3 S31: -0.5139 S32: -0.6638 S33: -0.2954 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): -10.0452 -3.4532 41.9071 REMARK 3 T TENSOR REMARK 3 T11: 0.4988 T22: 1.3778 REMARK 3 T33: 0.6727 T12: -0.3288 REMARK 3 T13: -0.0604 T23: 0.1440 REMARK 3 L TENSOR REMARK 3 L11: 3.8253 L22: 2.3473 REMARK 3 L33: 0.6433 L12: -2.9816 REMARK 3 L13: 0.7880 L23: -0.6953 REMARK 3 S TENSOR REMARK 3 S11: 0.0704 S12: -0.1724 S13: -0.7048 REMARK 3 S21: -0.1548 S22: 0.0826 S23: 0.5678 REMARK 3 S31: 0.5034 S32: -0.3845 S33: -0.1531 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 29.1393 -0.4364 15.6612 REMARK 3 T TENSOR REMARK 3 T11: 0.2273 T22: 0.6551 REMARK 3 T33: 0.6005 T12: 0.0073 REMARK 3 T13: 0.1960 T23: 0.1347 REMARK 3 L TENSOR REMARK 3 L11: 3.7497 L22: 4.6042 REMARK 3 L33: 7.4895 L12: -0.9967 REMARK 3 L13: -2.4587 L23: 0.7704 REMARK 3 S TENSOR REMARK 3 S11: -0.5755 S12: -0.0176 S13: -0.5729 REMARK 3 S21: -0.5814 S22: -0.4178 S23: -0.4564 REMARK 3 S31: 0.4977 S32: 0.5315 S33: 0.9933 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 47.2246 -3.4962 -1.4641 REMARK 3 T TENSOR REMARK 3 T11: 1.0608 T22: 1.4228 REMARK 3 T33: 1.4415 T12: 0.1401 REMARK 3 T13: 0.7538 T23: 0.4614 REMARK 3 L TENSOR REMARK 3 L11: 2.1573 L22: 12.7237 REMARK 3 L33: 6.2561 L12: -2.5101 REMARK 3 L13: 1.4464 L23: 3.4758 REMARK 3 S TENSOR REMARK 3 S11: -0.3386 S12: 0.8813 S13: 0.0237 REMARK 3 S21: -0.5454 S22: -0.3074 S23: -1.9534 REMARK 3 S31: 0.2267 S32: 1.7103 S33: 0.6460 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 27.5751 21.1231 15.1442 REMARK 3 T TENSOR REMARK 3 T11: 0.6598 T22: 0.5554 REMARK 3 T33: 0.3614 T12: -0.0764 REMARK 3 T13: -0.1392 T23: 0.0497 REMARK 3 L TENSOR REMARK 3 L11: 7.9824 L22: 4.3962 REMARK 3 L33: 10.0803 L12: 0.0025 REMARK 3 L13: -4.1361 L23: -0.3165 REMARK 3 S TENSOR REMARK 3 S11: 0.5818 S12: -0.5797 S13: 0.6262 REMARK 3 S21: -0.5623 S22: -0.3258 S23: -0.2849 REMARK 3 S31: -1.8733 S32: 0.3135 S33: -0.2560 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 NUMBER OF COMPONENTS GROUP : 0 REMARK 3 COMPONENTS C SSSEQI TO C SSSEQI REMARK 3 ORIGIN FOR THE GROUP (A): 42.7977 5.1980 -16.1631 REMARK 3 T TENSOR REMARK 3 T11: 1.4921 T22: 1.0445 REMARK 3 T33: 0.7029 T12: 0.1717 REMARK 3 T13: 0.3582 T23: 0.2210 REMARK 3 L TENSOR REMARK 3 L11: 4.6760 L22: 5.9081 REMARK 3 L33: 5.5419 L12: 0.6137 REMARK 3 L13: -2.1660 L23: 0.6714 REMARK 3 S TENSOR REMARK 3 S11: -0.0893 S12: 0.8582 S13: -0.7821 REMARK 3 S21: -2.1909 S22: -0.3426 S23: -0.3994 REMARK 3 S31: 0.3125 S32: 0.1359 S33: 0.4319 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : MASK BULK SOLVENT REMARK 3 PARAMETERS FOR MASK CALCULATION REMARK 3 VDW PROBE RADIUS : 1.20 REMARK 3 ION PROBE RADIUS : 0.80 REMARK 3 SHRINKAGE RADIUS : 0.80 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR REMARK 3 RIDING POSITIONS REMARK 4 REMARK 4 9S8W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1292149975. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 24-SEP-19 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 : DIAMOND REMARK 200 BEAMLINE : I04-1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.91589 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XIA2 REMARK 200 DATA SCALING SOFTWARE : STARANISO REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 9227 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.490 REMARK 200 RESOLUTION RANGE LOW (A) : 107.440 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 86.8 REMARK 200 DATA REDUNDANCY : 15.00 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 9.2000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.49 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.87 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) : NULL REMARK 200 FOR SHELL : 1.700 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 53.07 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M SODIUM NITRATE 20% PEG3350, REMARK 280 VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,-Y,Z+1/2 REMARK 290 3555 -Y+1/2,X+1/2,Z+1/4 REMARK 290 4555 Y+1/2,-X+1/2,Z+3/4 REMARK 290 5555 -X+1/2,Y+1/2,-Z+1/4 REMARK 290 6555 X+1/2,-Y+1/2,-Z+3/4 REMARK 290 7555 Y,X,-Z REMARK 290 8555 -Y,-X,-Z+1/2 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 214.89050 REMARK 290 SMTRY1 3 0.000000 -1.000000 0.000000 34.86900 REMARK 290 SMTRY2 3 1.000000 0.000000 0.000000 34.86900 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 107.44525 REMARK 290 SMTRY1 4 0.000000 1.000000 0.000000 34.86900 REMARK 290 SMTRY2 4 -1.000000 0.000000 0.000000 34.86900 REMARK 290 SMTRY3 4 0.000000 0.000000 1.000000 322.33575 REMARK 290 SMTRY1 5 -1.000000 0.000000 0.000000 34.86900 REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 34.86900 REMARK 290 SMTRY3 5 0.000000 0.000000 -1.000000 107.44525 REMARK 290 SMTRY1 6 1.000000 0.000000 0.000000 34.86900 REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 34.86900 REMARK 290 SMTRY3 6 0.000000 0.000000 -1.000000 322.33575 REMARK 290 SMTRY1 7 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY2 7 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 8 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY2 8 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY3 8 0.000000 0.000000 -1.000000 214.89050 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, H, L, C REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 LYS A 158 REMARK 465 SER A 426 REMARK 465 LYS A 427 REMARK 465 ARG A 428 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 ARG L 234 NE CZ NH1 NH2 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 O TYR H 128 HG SER L 114 1.50 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 PHE A 258 72.36 -102.89 REMARK 500 SER A 345 -165.89 -165.74 REMARK 500 LEU A 419 -159.05 -118.60 REMARK 500 ASN A 439 109.99 -53.78 REMARK 500 LEU H 30 50.79 -108.65 REMARK 500 CYS H 41 75.48 -166.74 REMARK 500 THR H 74 -72.07 -68.31 REMARK 500 ASP H 92 85.14 -151.67 REMARK 500 ALA H 111 -179.27 -173.40 REMARK 500 ALA H 116 -163.25 -108.98 REMARK 500 GLN H 201 66.09 -113.68 REMARK 500 SER H 202 -64.26 66.12 REMARK 500 SER H 233 32.69 75.55 REMARK 500 GLU L 46 -130.02 52.69 REMARK 500 VAL L 48 63.13 -102.37 REMARK 500 PHE L 51 -114.26 56.36 REMARK 500 ALA L 74 -45.23 68.89 REMARK 500 GLU L 78 -179.27 -63.86 REMARK 500 PRO L 164 -176.64 -68.01 REMARK 500 SER L 185 114.49 -161.19 REMARK 500 LYS L 192 -60.40 -93.08 REMARK 500 ASP L 207 -4.19 84.00 REMARK 500 REMARK 500 REMARK: NULL DBREF 9S8W A 158 543 UNP Q9Y251 HPSE_HUMAN 158 543 DBREF 9S8W B 36 109 UNP Q9Y251 HPSE_HUMAN 36 109 DBREF 9S8W H 20 241 PDB 9S8W 9S8W 20 241 DBREF 9S8W L 20 237 PDB 9S8W 9S8W 20 237 SEQADV 9S8W ARG A 307 UNP Q9Y251 LYS 307 VARIANT SEQRES 1 A 386 LYS LYS PHE LYS ASN SER THR TYR SER ARG SER SER VAL SEQRES 2 A 386 ASP VAL LEU TYR THR PHE ALA ASN CYS SER GLY LEU ASP SEQRES 3 A 386 LEU ILE PHE GLY LEU ASN ALA LEU LEU ARG THR ALA ASP SEQRES 4 A 386 LEU GLN TRP ASN SER SER ASN ALA GLN LEU LEU LEU ASP SEQRES 5 A 386 TYR CYS SER SER LYS GLY TYR ASN ILE SER TRP GLU LEU SEQRES 6 A 386 GLY ASN GLU PRO ASN SER PHE LEU LYS LYS ALA ASP ILE SEQRES 7 A 386 PHE ILE ASN GLY SER GLN LEU GLY GLU ASP PHE ILE GLN SEQRES 8 A 386 LEU HIS LYS LEU LEU ARG LYS SER THR PHE LYS ASN ALA SEQRES 9 A 386 LYS LEU TYR GLY PRO ASP VAL GLY GLN PRO ARG ARG LYS SEQRES 10 A 386 THR ALA LYS MET LEU LYS SER PHE LEU LYS ALA GLY GLY SEQRES 11 A 386 GLU VAL ILE ASP SER VAL THR TRP HIS HIS TYR TYR LEU SEQRES 12 A 386 ASN GLY ARG THR ALA THR ARG GLU ASP PHE LEU ASN PRO SEQRES 13 A 386 ASP VAL LEU ASP ILE PHE ILE SER SER VAL GLN LYS VAL SEQRES 14 A 386 PHE GLN VAL VAL GLU SER THR ARG PRO GLY LYS LYS VAL SEQRES 15 A 386 TRP LEU GLY GLU THR SER SER ALA TYR GLY GLY GLY ALA SEQRES 16 A 386 PRO LEU LEU SER ASP THR PHE ALA ALA GLY PHE MET TRP SEQRES 17 A 386 LEU ASP LYS LEU GLY LEU SER ALA ARG MET GLY ILE GLU SEQRES 18 A 386 VAL VAL MET ARG GLN VAL PHE PHE GLY ALA GLY ASN TYR SEQRES 19 A 386 HIS LEU VAL ASP GLU ASN PHE ASP PRO LEU PRO ASP TYR SEQRES 20 A 386 TRP LEU SER LEU LEU PHE LYS LYS LEU VAL GLY THR LYS SEQRES 21 A 386 VAL LEU MET ALA SER VAL GLN GLY SER LYS ARG ARG LYS SEQRES 22 A 386 LEU ARG VAL TYR LEU HIS CYS THR ASN THR ASP ASN PRO SEQRES 23 A 386 ARG TYR LYS GLU GLY ASP LEU THR LEU TYR ALA ILE ASN SEQRES 24 A 386 LEU HIS ASN VAL THR LYS TYR LEU ARG LEU PRO TYR PRO SEQRES 25 A 386 PHE SER ASN LYS GLN VAL ASP LYS TYR LEU LEU ARG PRO SEQRES 26 A 386 LEU GLY PRO HIS GLY LEU LEU SER LYS SER VAL GLN LEU SEQRES 27 A 386 ASN GLY LEU THR LEU LYS MET VAL ASP ASP GLN THR LEU SEQRES 28 A 386 PRO PRO LEU MET GLU LYS PRO LEU ARG PRO GLY SER SER SEQRES 29 A 386 LEU GLY LEU PRO ALA PHE SER TYR SER PHE PHE VAL ILE SEQRES 30 A 386 ARG ASN ALA LYS VAL ALA ALA CYS ILE SEQRES 1 B 74 GLN ASP VAL VAL ASP LEU ASP PHE PHE THR GLN GLU PRO SEQRES 2 B 74 LEU HIS LEU VAL SER PRO SER PHE LEU SER VAL THR ILE SEQRES 3 B 74 ASP ALA ASN LEU ALA THR ASP PRO ARG PHE LEU ILE LEU SEQRES 4 B 74 LEU GLY SER PRO LYS LEU ARG THR LEU ALA ARG GLY LEU SEQRES 5 B 74 SER PRO ALA TYR LEU ARG PHE GLY GLY THR LYS THR ASP SEQRES 6 B 74 PHE LEU ILE PHE ASP PRO LYS LYS GLU SEQRES 1 H 222 GLN VAL GLN LEU GLN GLN SER GLY ALA GLU LEU ALA LYS SEQRES 2 H 222 PRO GLY ALA SER VAL ARG MET SER CYS LYS ALA SER GLY SEQRES 3 H 222 TYR THR PHE THR ASN TYR TRP MET HIS TRP VAL LYS GLN SEQRES 4 H 222 ARG PRO GLY GLN GLY LEU GLU TRP ILE GLY TYR ILE ASN SEQRES 5 H 222 PRO THR THR GLY TYR THR GLU TYR ASN GLN LYS PHE LYS SEQRES 6 H 222 ASP LYS ALA THR LEU THR ALA ASP LYS SER SER SER THR SEQRES 7 H 222 ALA TYR MET GLN LEU SER SER LEU THR SER GLU ASP SER SEQRES 8 H 222 ALA VAL TYR TYR CYS ALA ARG GLY GLY ALA GLY TYR ASP SEQRES 9 H 222 TYR ASP GLU ASP TYR ALA MET ASP TYR TRP GLY GLN GLY SEQRES 10 H 222 THR SER VAL THR VAL SER SER ALA LYS THR THR PRO PRO SEQRES 11 H 222 SER VAL TYR PRO LEU ALA PRO GLY SER ALA ALA GLN THR SEQRES 12 H 222 ASN SER MET VAL THR LEU GLY CYS LEU VAL LYS GLY TYR SEQRES 13 H 222 PHE PRO GLU PRO VAL THR VAL THR TRP ASN SER GLY SER SEQRES 14 H 222 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 222 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL PRO SEQRES 16 H 222 SER SER PRO ARG PRO SER GLU THR VAL THR CYS ASN VAL SEQRES 17 H 222 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE SEQRES 18 H 222 VAL SEQRES 1 L 218 ASP ILE VAL LEU THR GLN SER PRO ALA SER LEU ALA VAL SEQRES 2 L 218 SER LEU GLY GLN ARG ALA THR ILE SER CYS ARG ALA SER SEQRES 3 L 218 GLU SER VAL GLU TYR PHE GLY THR SER TYR MET ASN TRP SEQRES 4 L 218 TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU LEU ILE SEQRES 5 L 218 TYR LEU ALA SER ILE LEU GLU SER GLY ILE PRO ALA ARG SEQRES 6 L 218 PHE SER GLY SER GLY SER GLY THR ASP PHE THR LEU ASN SEQRES 7 L 218 ILE HIS PRO VAL GLU GLU GLU ASP ALA ALA THR TYR TYR SEQRES 8 L 218 CYS GLN GLN SER ASN GLU ASP PRO TYR THR PHE GLY GLY SEQRES 9 L 218 GLY THR LYS LEU GLU ILE LYS ARG ALA ASP ALA ALA PRO SEQRES 10 L 218 THR VAL SER ILE PHE PRO PRO SER SER GLU GLN LEU THR SEQRES 11 L 218 SER GLY GLY ALA SER VAL VAL CYS PHE LEU ASN ASN PHE SEQRES 12 L 218 TYR PRO LYS ASP ILE ASN VAL LYS TRP LYS ILE ASP GLY SEQRES 13 L 218 SER GLU ARG GLN ASN GLY VAL LEU ASN SER TRP THR ASP SEQRES 14 L 218 GLN ASP SER LYS ASP SER THR TYR SER MET SER SER THR SEQRES 15 L 218 LEU THR LEU THR LYS ASP GLU TYR GLU ARG HIS ASN SER SEQRES 16 L 218 TYR THR CYS GLU ALA THR HIS LYS THR SER THR SER PRO SEQRES 17 L 218 ILE VAL LYS SER PHE ASN ARG ASN GLU CYS HET NAG C 1 27 HET FUC C 2 21 HET NAG A 601 28 HET NAG A 602 28 HET NAG A 603 28 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE 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 FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 5 NAG 4(C8 H15 N O6) FORMUL 5 FUC C6 H12 O5 FORMUL 9 HOH *31(H2 O) HELIX 1 AA1 SER A 166 SER A 180 1 15 HELIX 2 AA2 SER A 201 LYS A 214 1 14 HELIX 3 AA3 GLU A 225 ASN A 227 5 3 HELIX 4 AA4 SER A 228 ASP A 234 1 7 HELIX 5 AA5 ASN A 238 LYS A 255 1 18 HELIX 6 AA6 ARG A 272 GLY A 287 1 16 HELIX 7 AA7 THR A 306 LEU A 311 1 6 HELIX 8 AA8 ASN A 312 ASP A 317 1 6 HELIX 9 AA9 ASP A 317 SER A 332 1 16 HELIX 10 AB1 THR A 358 ALA A 360 5 3 HELIX 11 AB2 ALA A 361 GLY A 376 1 16 HELIX 12 AB3 LEU A 401 LEU A 413 1 13 HELIX 13 AB4 HIS A 486 SER A 490 5 5 HELIX 14 AB5 VAL A 539 ILE A 543 5 5 HELIX 15 AB6 ASN B 64 ASP B 68 5 5 HELIX 16 AB7 ARG B 70 GLY B 76 1 7 HELIX 17 AB8 SER B 77 LEU B 87 1 11 HELIX 18 AB9 GLY B 96 ASP B 100 5 5 HELIX 19 AC1 THR H 47 TYR H 51 5 5 HELIX 20 AC2 GLN H 81 LYS H 84 5 4 HELIX 21 AC3 LYS H 93 SER H 96 5 4 HELIX 22 AC4 THR H 106 SER H 110 5 5 HELIX 23 AC5 ASP H 123 ASP H 127 5 5 HELIX 24 AC6 SER H 216 GLU H 221 1 6 HELIX 25 AC7 GLU L 102 ALA L 106 5 5 HELIX 26 AC8 SER L 144 GLY L 151 1 8 SHEET 1 AA1 2 SER A 163 TYR A 165 0 SHEET 2 AA1 2 LEU B 102 PHE B 104 1 O ILE B 103 N SER A 163 SHEET 1 AA2 9 LEU A 182 LEU A 188 0 SHEET 2 AA2 9 SER A 219 LEU A 222 1 O GLU A 221 N LEU A 188 SHEET 3 AA2 9 LEU A 263 VAL A 268 1 O TYR A 264 N TRP A 220 SHEET 4 AA2 9 SER A 292 ASN A 301 1 O HIS A 296 N VAL A 268 SHEET 5 AA2 9 LYS A 338 TYR A 348 1 O TRP A 340 N VAL A 293 SHEET 6 AA2 9 VAL A 379 PHE A 386 1 O VAL A 379 N LEU A 341 SHEET 7 AA2 9 LEU B 57 ASP B 62 1 O THR B 60 N PHE A 385 SHEET 8 AA2 9 ALA B 90 GLY B 95 1 O ARG B 93 N ILE B 61 SHEET 9 AA2 9 LEU A 182 LEU A 188 1 N ASP A 183 O ALA B 90 SHEET 1 AA3 4 LEU A 498 THR A 499 0 SHEET 2 AA3 4 VAL A 493 LEU A 495 -1 N LEU A 495 O LEU A 498 SHEET 3 AA3 4 VAL A 475 PRO A 482 -1 N ARG A 481 O GLN A 494 SHEET 4 AA3 4 LYS A 514 PRO A 515 -1 O LYS A 514 N LYS A 477 SHEET 1 AA4 8 LEU A 498 THR A 499 0 SHEET 2 AA4 8 VAL A 493 LEU A 495 -1 N LEU A 495 O LEU A 498 SHEET 3 AA4 8 VAL A 475 PRO A 482 -1 N ARG A 481 O GLN A 494 SHEET 4 AA4 8 SER A 528 ILE A 534 -1 O PHE A 531 N TYR A 478 SHEET 5 AA4 8 LEU A 450 ASN A 456 -1 N LEU A 452 O PHE A 532 SHEET 6 AA4 8 LEU A 431 THR A 438 -1 N HIS A 436 O THR A 451 SHEET 7 AA4 8 VAL A 414 VAL A 418 -1 N GLY A 415 O CYS A 437 SHEET 8 AA4 8 HIS B 50 LEU B 51 -1 O HIS B 50 N VAL A 418 SHEET 1 AA5 4 MET A 420 VAL A 423 0 SHEET 2 AA5 4 VAL B 38 PHE B 44 -1 O PHE B 44 N MET A 420 SHEET 3 AA5 4 LYS A 462 ARG A 465 1 N ARG A 465 O VAL B 39 SHEET 4 AA5 4 LEU A 522 LEU A 524 -1 O LEU A 522 N LEU A 464 SHEET 1 AA6 4 GLN H 22 GLN H 25 0 SHEET 2 AA6 4 VAL H 37 SER H 44 -1 O LYS H 42 N GLN H 24 SHEET 3 AA6 4 THR H 97 LEU H 102 -1 O MET H 100 N MET H 39 SHEET 4 AA6 4 ALA H 87 ASP H 92 -1 N THR H 90 O TYR H 99 SHEET 1 AA7 5 THR H 77 TYR H 79 0 SHEET 2 AA7 5 GLU H 65 ILE H 70 -1 N TYR H 69 O GLU H 78 SHEET 3 AA7 5 MET H 53 GLN H 58 -1 N LYS H 57 O GLU H 65 SHEET 4 AA7 5 ALA H 111 CYS H 115 -1 O TYR H 114 N VAL H 56 SHEET 5 AA7 5 THR H 137 VAL H 139 -1 O VAL H 139 N ALA H 111 SHEET 1 AA8 4 SER H 150 LEU H 154 0 SHEET 2 AA8 4 MET H 165 TYR H 175 -1 O LEU H 171 N TYR H 152 SHEET 3 AA8 4 LEU H 204 PRO H 214 -1 O TYR H 205 N TYR H 175 SHEET 4 AA8 4 VAL H 193 THR H 195 -1 N HIS H 194 O SER H 210 SHEET 1 AA9 4 SER H 150 LEU H 154 0 SHEET 2 AA9 4 MET H 165 TYR H 175 -1 O LEU H 171 N TYR H 152 SHEET 3 AA9 4 LEU H 204 PRO H 214 -1 O TYR H 205 N TYR H 175 SHEET 4 AA9 4 VAL H 199 GLN H 201 -1 N GLN H 201 O LEU H 204 SHEET 1 AB1 3 THR H 181 THR H 183 0 SHEET 2 AB1 3 THR H 224 HIS H 229 -1 O ALA H 228 N THR H 181 SHEET 3 AB1 3 THR H 234 LYS H 239 -1 O VAL H 236 N VAL H 227 SHEET 1 AB2 4 LEU L 23 THR L 24 0 SHEET 2 AB2 4 ALA L 38 ALA L 44 -1 O ARG L 43 N THR L 24 SHEET 3 AB2 4 ASP L 93 ILE L 98 -1 O PHE L 94 N CYS L 42 SHEET 4 AB2 4 SER L 86 SER L 90 -1 N SER L 88 O THR L 95 SHEET 1 AB3 6 SER L 29 SER L 33 0 SHEET 2 AB3 6 THR L 125 LYS L 130 1 O GLU L 128 N LEU L 30 SHEET 3 AB3 6 THR L 108 GLN L 113 -1 N TYR L 109 O THR L 125 SHEET 4 AB3 6 MET L 56 GLN L 61 -1 N ASN L 57 O GLN L 112 SHEET 5 AB3 6 LEU L 69 TYR L 72 -1 O LEU L 70 N TRP L 58 SHEET 6 AB3 6 ILE L 76 LEU L 77 -1 O ILE L 76 N TYR L 72 SHEET 1 AB4 4 SER L 29 SER L 33 0 SHEET 2 AB4 4 THR L 125 LYS L 130 1 O GLU L 128 N LEU L 30 SHEET 3 AB4 4 THR L 108 GLN L 113 -1 N TYR L 109 O THR L 125 SHEET 4 AB4 4 THR L 120 PHE L 121 -1 O THR L 120 N GLN L 113 SHEET 1 AB5 4 SER L 139 PHE L 141 0 SHEET 2 AB5 4 GLY L 152 PHE L 162 -1 O VAL L 156 N PHE L 141 SHEET 3 AB5 4 TYR L 196 THR L 205 -1 O LEU L 204 N ALA L 153 SHEET 4 AB5 4 VAL L 182 LEU L 183 -1 N LEU L 183 O THR L 201 SHEET 1 AB6 4 SER L 176 ARG L 178 0 SHEET 2 AB6 4 ASN L 168 ILE L 173 -1 N ILE L 173 O SER L 176 SHEET 3 AB6 4 SER L 214 THR L 220 -1 O THR L 216 N LYS L 172 SHEET 4 AB6 4 ILE L 228 ASN L 233 -1 O LYS L 230 N CYS L 217 SSBOND 1 CYS A 437 CYS A 542 1555 1555 2.03 SSBOND 2 CYS H 41 CYS H 115 1555 1555 2.03 SSBOND 3 CYS H 170 CYS H 225 1555 1555 2.02 SSBOND 4 CYS L 42 CYS L 111 1555 1555 2.05 SSBOND 5 CYS L 157 CYS L 217 1555 1555 2.02 LINK ND2 ASN A 200 C1 NAG A 602 1555 1555 1.49 LINK ND2 ASN A 217 C1 NAG A 603 1555 1555 1.47 LINK ND2 ASN A 238 C1 NAG A 601 1555 1555 1.49 LINK ND2 ASN A 459 C1 NAG C 1 1555 1555 1.48 LINK O6 NAG C 1 C1 FUC C 2 1555 1555 1.42 CISPEP 1 GLY A 265 PRO A 266 0 1.33 CISPEP 2 GLN A 383 VAL A 384 0 -3.30 CISPEP 3 TYR A 468 PRO A 469 0 -7.13 CISPEP 4 GLY A 484 PRO A 485 0 8.80 CISPEP 5 SER B 88 PRO B 89 0 -3.38 CISPEP 6 PHE H 176 PRO H 177 0 -10.34 CISPEP 7 GLU H 178 PRO H 179 0 -8.56 CISPEP 8 HIS L 99 PRO L 100 0 10.92 CISPEP 9 ASP L 117 PRO L 118 0 7.35 CISPEP 10 TYR L 163 PRO L 164 0 0.05 CRYST1 69.738 69.738 429.781 90.00 90.00 90.00 P 41 21 2 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 0.014339 0.000000 0.000000 0.00000 SCALE2 0.000000 0.014339 0.000000 0.00000 SCALE3 0.000000 0.000000 0.002327 0.00000