HEADER HYDROLASE 25-APR-25 9R19 TITLE CRYSTAL STRUCTURE OF HUMAN ACE2 IN COMPLEX WITH VHH B07 AND VHH B10 COMPND MOL_ID: 1; COMPND 2 MOLECULE: PROCESSED ANGIOTENSIN-CONVERTING ENZYME 2; COMPND 3 CHAIN: A, B, C; COMPND 4 ENGINEERED: YES; COMPND 5 OTHER_DETAILS: GSG LINKER LVPR CLEAVED THROMBIN SITE; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: VHH B10; COMPND 8 CHAIN: D, E, F; COMPND 9 ENGINEERED: YES; COMPND 10 OTHER_DETAILS: AAA : LINKER EQKLISEEDLN : C-MYC TAG GAA : LINKER COMPND 11 HHHHHH : HIS-TAG GS : LINKER; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: VHH B07; COMPND 14 CHAIN: G, H, I; COMPND 15 ENGINEERED: YES; COMPND 16 OTHER_DETAILS: AAA : LINKER EQKLISEEDLN : C-MYC TAG GAA : LINKER COMPND 17 HHHHHH : HIS-TAG GS : LINKER SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: ACE2, UNQ868/PRO1885; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: EXPI293FTM GNTI; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 11 ORGANISM_TAXID: 30538; SOURCE 12 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 14 EXPRESSION_SYSTEM_STRAIN: TG1 CELLS; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 17 ORGANISM_TAXID: 30538; SOURCE 18 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 19 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 20 EXPRESSION_SYSTEM_STRAIN: TG1 KEYWDS HUMAN ACE2, VHH, STRUCTURAL PROTEIN, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR S.BLACHIER,M.C.VANEY,I.FERNANDEZ,A.ARBABIAN,F.A.R.REY,A.HAOUZ, AUTHOR 2 A.BRELOT REVDAT 1 17-SEP-25 9R19 0 JRNL AUTH S.BLACHIER,M.C.VANEY,I.FERNANDEZ,A.ARBABIAN,F.A.R.REY, JRNL AUTH 2 A.HAOUZ,A.BRELOT JRNL TITL CRYSTAL STRUCTURE OF HUMAN ACE2 IN COMPLEX WITH VHH B07 AND JRNL TITL 2 VHH B10 JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 2.69 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.4 (10-JUL-2024) REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER, REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN, REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.30 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 3 NUMBER OF REFLECTIONS : 83594 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM REMARK 3 R VALUE (WORKING + TEST SET) : 0.221 REMARK 3 R VALUE (WORKING SET) : 0.220 REMARK 3 FREE R VALUE : 0.255 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 4180 REMARK 3 ESTIMATED ERROR OF FREE R VALUE : NULL REMARK 3 REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN. REMARK 3 TOTAL NUMBER OF BINS USED : 51 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.69 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.71 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 91.41 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 1672 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.3436 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1589 REMARK 3 BIN R VALUE (WORKING SET) : 0.3412 REMARK 3 BIN FREE R VALUE : 0.3914 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.96 REMARK 3 BIN FREE R VALUE TEST SET COUNT : NULL REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : NULL REMARK 3 REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT. REMARK 3 PROTEIN ATOMS : 20118 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 186 REMARK 3 SOLVENT ATOMS : 104 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 63.78 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 70.18 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : 2.23610 REMARK 3 B22 (A**2) : -3.19620 REMARK 3 B33 (A**2) : 0.96010 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : 5.38970 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.380 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 1.098 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.325 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 1.912 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.338 REMARK 3 REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797 REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601 REMARK 3 REMARK 3 CORRELATION COEFFICIENTS. REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.932 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.914 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 20846 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 28324 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 7161 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 3592 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 20846 ; 10.000 ; HARMONIC REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL REMARK 3 CHIRAL IMPROPER TORSION : 2647 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL REMARK 3 IDEAL-DIST CONTACT TERM : 16114 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.007 REMARK 3 BOND ANGLES (DEGREES) : 0.87 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.66 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 18.60 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 9 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 41.5484 -20.7453 3.8393 REMARK 3 T TENSOR REMARK 3 T11: -0.1437 T22: 0.0960 REMARK 3 T33: -0.0673 T12: -0.0323 REMARK 3 T13: 0.0051 T23: 0.0117 REMARK 3 L TENSOR REMARK 3 L11: 1.4355 L22: 0.5769 REMARK 3 L33: 1.1271 L12: -0.0905 REMARK 3 L13: 0.5560 L23: -0.2976 REMARK 3 S TENSOR REMARK 3 S11: -0.0516 S12: 0.0974 S13: 0.0747 REMARK 3 S21: -0.0018 S22: -0.0006 S23: -0.0003 REMARK 3 S31: -0.0475 S32: 0.1046 S33: 0.0522 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): -0.8267 -30.4539 38.8797 REMARK 3 T TENSOR REMARK 3 T11: -0.1889 T22: 0.2963 REMARK 3 T33: -0.0800 T12: -0.0450 REMARK 3 T13: -0.0277 T23: 0.1173 REMARK 3 L TENSOR REMARK 3 L11: 0.9973 L22: 0.5936 REMARK 3 L33: 1.7330 L12: 0.1161 REMARK 3 L13: 0.4317 L23: 0.0002 REMARK 3 S TENSOR REMARK 3 S11: -0.0017 S12: -0.1445 S13: -0.1102 REMARK 3 S21: 0.0941 S22: -0.1162 S23: -0.0552 REMARK 3 S31: 0.0057 S32: 0.1411 S33: 0.1179 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 10.9107 -13.2357 87.4515 REMARK 3 T TENSOR REMARK 3 T11: -0.1155 T22: 0.1850 REMARK 3 T33: -0.0782 T12: -0.0513 REMARK 3 T13: -0.0749 T23: 0.0824 REMARK 3 L TENSOR REMARK 3 L11: 1.3212 L22: 0.7956 REMARK 3 L33: 2.5551 L12: 0.5280 REMARK 3 L13: 0.4768 L23: 0.5674 REMARK 3 S TENSOR REMARK 3 S11: -0.1539 S12: -0.0167 S13: 0.3599 REMARK 3 S21: -0.0316 S22: 0.0121 S23: 0.1906 REMARK 3 S31: -0.2519 S32: 0.0204 S33: 0.1418 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { D|* } REMARK 3 ORIGIN FOR THE GROUP (A): 50.2455 -5.3913 41.2760 REMARK 3 T TENSOR REMARK 3 T11: -0.1987 T22: 0.0342 REMARK 3 T33: -0.1431 T12: -0.0172 REMARK 3 T13: -0.0323 T23: -0.0818 REMARK 3 L TENSOR REMARK 3 L11: 4.3142 L22: 8.0468 REMARK 3 L33: 7.7553 L12: 0.5546 REMARK 3 L13: 1.6463 L23: 3.8905 REMARK 3 S TENSOR REMARK 3 S11: 0.0582 S12: -0.3686 S13: 0.2364 REMARK 3 S21: 0.1892 S22: 0.0886 S23: -0.2012 REMARK 3 S31: -0.2532 S32: 0.1398 S33: -0.1468 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { E|* } REMARK 3 ORIGIN FOR THE GROUP (A): -9.6500 2.4146 15.3490 REMARK 3 T TENSOR REMARK 3 T11: -0.2256 T22: -0.2073 REMARK 3 T33: 0.3094 T12: 0.0667 REMARK 3 T13: -0.0654 T23: 0.1502 REMARK 3 L TENSOR REMARK 3 L11: 13.4418 L22: 10.7109 REMARK 3 L33: 6.9547 L12: 1.5980 REMARK 3 L13: -0.6374 L23: -2.2003 REMARK 3 S TENSOR REMARK 3 S11: 0.0276 S12: 0.4712 S13: 2.3355 REMARK 3 S21: 0.0539 S22: 0.0678 S23: 0.5443 REMARK 3 S31: -1.1079 S32: -0.0461 S33: -0.0954 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { F|* } REMARK 3 ORIGIN FOR THE GROUP (A): 50.6683 -20.2824 98.8502 REMARK 3 T TENSOR REMARK 3 T11: -0.4989 T22: 0.4602 REMARK 3 T33: -0.1765 T12: 0.0596 REMARK 3 T13: -0.0487 T23: -0.2686 REMARK 3 L TENSOR REMARK 3 L11: 17.5940 L22: 4.1047 REMARK 3 L33: 9.3642 L12: 0.4327 REMARK 3 L13: 1.1878 L23: -0.1860 REMARK 3 S TENSOR REMARK 3 S11: 0.2699 S12: 1.4619 S13: -0.9822 REMARK 3 S21: -0.1393 S22: 0.0909 S23: -0.7455 REMARK 3 S31: 0.1004 S32: 1.6305 S33: -0.3608 REMARK 3 REMARK 3 TLS GROUP : 7 REMARK 3 SELECTION: { G|* } REMARK 3 ORIGIN FOR THE GROUP (A): -0.1431 -8.8159 -12.9156 REMARK 3 T TENSOR REMARK 3 T11: -0.2600 T22: 0.0032 REMARK 3 T33: -0.0519 T12: -0.0585 REMARK 3 T13: -0.0331 T23: 0.0734 REMARK 3 L TENSOR REMARK 3 L11: 9.7664 L22: 4.2489 REMARK 3 L33: 7.6632 L12: -1.6055 REMARK 3 L13: 1.3706 L23: -3.4489 REMARK 3 S TENSOR REMARK 3 S11: -0.1287 S12: -0.0209 S13: -0.2468 REMARK 3 S21: -0.1852 S22: 0.2300 S23: 0.5818 REMARK 3 S31: 0.2891 S32: -0.3354 S33: -0.1013 REMARK 3 REMARK 3 TLS GROUP : 8 REMARK 3 SELECTION: { H|* } REMARK 3 ORIGIN FOR THE GROUP (A): 40.7214 -27.7374 59.7885 REMARK 3 T TENSOR REMARK 3 T11: -0.7074 T22: 1.3001 REMARK 3 T33: -0.3701 T12: -0.1177 REMARK 3 T13: -0.1457 T23: 0.5102 REMARK 3 L TENSOR REMARK 3 L11: 13.3108 L22: 0.6323 REMARK 3 L33: 15.5502 L12: -0.7270 REMARK 3 L13: -3.5579 L23: -0.2793 REMARK 3 S TENSOR REMARK 3 S11: -0.3605 S12: -1.5164 S13: -0.4851 REMARK 3 S21: 0.0705 S22: 0.0555 S23: -0.4027 REMARK 3 S31: 0.3591 S32: 2.5973 S33: 0.3050 REMARK 3 REMARK 3 TLS GROUP : 9 REMARK 3 SELECTION: { I|* } REMARK 3 ORIGIN FOR THE GROUP (A): 4.0683 10.3898 47.6619 REMARK 3 T TENSOR REMARK 3 T11: 0.0611 T22: 0.0542 REMARK 3 T33: -0.1644 T12: -0.2947 REMARK 3 T13: -0.3683 T23: 0.6406 REMARK 3 L TENSOR REMARK 3 L11: 7.4791 L22: 11.3445 REMARK 3 L33: 13.0819 L12: 3.9729 REMARK 3 L13: 5.3257 L23: -2.9596 REMARK 3 S TENSOR REMARK 3 S11: -0.1765 S12: 0.2360 S13: 1.1595 REMARK 3 S21: -0.0238 S22: -0.3866 S23: 0.4266 REMARK 3 S31: -1.3716 S32: -0.2123 S33: 0.5631 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9R19 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-APR-25. REMARK 100 THE DEPOSITION ID IS D_1292147351. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 25-OCT-24 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 7.5 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1. REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 83613 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.690 REMARK 200 RESOLUTION RANGE LOW (A) : 48.370 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.8 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : 0.22000 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) : 2.69 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.76 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.48000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL 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 (%): 54.00 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5 10% (W/V) 2-PROPANOL REMARK 280 20% (W/V) PEG 4K, VAPOR DIFFUSION, TEMPERATURE 291K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 54.07500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1, 2, 3 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, D, 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, H 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, 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 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 616 REMARK 465 SER A 617 REMARK 465 GLY A 618 REMARK 465 LEU A 619 REMARK 465 VAL A 620 REMARK 465 PRO A 621 REMARK 465 ARG A 622 REMARK 465 SER B 19 REMARK 465 ASP B 615 REMARK 465 GLY B 616 REMARK 465 SER B 617 REMARK 465 GLY B 618 REMARK 465 LEU B 619 REMARK 465 VAL B 620 REMARK 465 PRO B 621 REMARK 465 ARG B 622 REMARK 465 SER C 19 REMARK 465 GLY C 616 REMARK 465 SER C 617 REMARK 465 GLY C 618 REMARK 465 LEU C 619 REMARK 465 VAL C 620 REMARK 465 PRO C 621 REMARK 465 ARG C 622 REMARK 465 MET D -1 REMARK 465 ALA D 0 REMARK 465 ALA D 127 REMARK 465 ALA D 128 REMARK 465 ALA D 129 REMARK 465 GLU D 130 REMARK 465 GLN D 131 REMARK 465 LYS D 132 REMARK 465 LEU D 133 REMARK 465 ILE D 134 REMARK 465 SER D 135 REMARK 465 GLU D 136 REMARK 465 GLU D 137 REMARK 465 ASP D 138 REMARK 465 LEU D 139 REMARK 465 ASN D 140 REMARK 465 GLY D 141 REMARK 465 ALA D 142 REMARK 465 ALA D 143 REMARK 465 HIS D 144 REMARK 465 HIS D 145 REMARK 465 HIS D 146 REMARK 465 HIS D 147 REMARK 465 HIS D 148 REMARK 465 HIS D 149 REMARK 465 GLY D 150 REMARK 465 SER D 151 REMARK 465 MET E -1 REMARK 465 ALA E 0 REMARK 465 GLN E 1 REMARK 465 SER E 126 REMARK 465 ALA E 127 REMARK 465 ALA E 128 REMARK 465 ALA E 129 REMARK 465 GLU E 130 REMARK 465 GLN E 131 REMARK 465 LYS E 132 REMARK 465 LEU E 133 REMARK 465 ILE E 134 REMARK 465 SER E 135 REMARK 465 GLU E 136 REMARK 465 GLU E 137 REMARK 465 ASP E 138 REMARK 465 LEU E 139 REMARK 465 ASN E 140 REMARK 465 GLY E 141 REMARK 465 ALA E 142 REMARK 465 ALA E 143 REMARK 465 HIS E 144 REMARK 465 HIS E 145 REMARK 465 HIS E 146 REMARK 465 HIS E 147 REMARK 465 HIS E 148 REMARK 465 HIS E 149 REMARK 465 GLY E 150 REMARK 465 SER E 151 REMARK 465 MET F -1 REMARK 465 ALA F 0 REMARK 465 GLN F 1 REMARK 465 SER F 125 REMARK 465 SER F 126 REMARK 465 ALA F 127 REMARK 465 ALA F 128 REMARK 465 ALA F 129 REMARK 465 GLU F 130 REMARK 465 GLN F 131 REMARK 465 LYS F 132 REMARK 465 LEU F 133 REMARK 465 ILE F 134 REMARK 465 SER F 135 REMARK 465 GLU F 136 REMARK 465 GLU F 137 REMARK 465 ASP F 138 REMARK 465 LEU F 139 REMARK 465 ASN F 140 REMARK 465 GLY F 141 REMARK 465 ALA F 142 REMARK 465 ALA F 143 REMARK 465 HIS F 144 REMARK 465 HIS F 145 REMARK 465 HIS F 146 REMARK 465 HIS F 147 REMARK 465 HIS F 148 REMARK 465 HIS F 149 REMARK 465 GLY F 150 REMARK 465 SER F 151 REMARK 465 MET G -1 REMARK 465 ALA G 0 REMARK 465 GLU G 120 REMARK 465 GLN G 121 REMARK 465 LYS G 122 REMARK 465 LEU G 123 REMARK 465 ILE G 124 REMARK 465 SER G 125 REMARK 465 GLU G 126 REMARK 465 GLU G 127 REMARK 465 ASP G 128 REMARK 465 LEU G 129 REMARK 465 ASN G 130 REMARK 465 GLY G 131 REMARK 465 ALA G 132 REMARK 465 ALA G 133 REMARK 465 HIS G 134 REMARK 465 HIS G 135 REMARK 465 HIS G 136 REMARK 465 HIS G 137 REMARK 465 HIS G 138 REMARK 465 HIS G 139 REMARK 465 GLY G 140 REMARK 465 SER G 141 REMARK 465 MET H -1 REMARK 465 ALA H 0 REMARK 465 ALA H 117 REMARK 465 ALA H 118 REMARK 465 ALA H 119 REMARK 465 GLU H 120 REMARK 465 GLN H 121 REMARK 465 LYS H 122 REMARK 465 LEU H 123 REMARK 465 ILE H 124 REMARK 465 SER H 125 REMARK 465 GLU H 126 REMARK 465 GLU H 127 REMARK 465 ASP H 128 REMARK 465 LEU H 129 REMARK 465 ASN H 130 REMARK 465 GLY H 131 REMARK 465 ALA H 132 REMARK 465 ALA H 133 REMARK 465 HIS H 134 REMARK 465 HIS H 135 REMARK 465 HIS H 136 REMARK 465 HIS H 137 REMARK 465 HIS H 138 REMARK 465 HIS H 139 REMARK 465 GLY H 140 REMARK 465 SER H 141 REMARK 465 MET I -1 REMARK 465 ALA I 0 REMARK 465 GLU I 1 REMARK 465 VAL I 2 REMARK 465 ALA I 117 REMARK 465 ALA I 118 REMARK 465 ALA I 119 REMARK 465 GLU I 120 REMARK 465 GLN I 121 REMARK 465 LYS I 122 REMARK 465 LEU I 123 REMARK 465 ILE I 124 REMARK 465 SER I 125 REMARK 465 GLU I 126 REMARK 465 GLU I 127 REMARK 465 ASP I 128 REMARK 465 LEU I 129 REMARK 465 ASN I 130 REMARK 465 GLY I 131 REMARK 465 ALA I 132 REMARK 465 ALA I 133 REMARK 465 HIS I 134 REMARK 465 HIS I 135 REMARK 465 HIS I 136 REMARK 465 HIS I 137 REMARK 465 HIS I 138 REMARK 465 HIS I 139 REMARK 465 GLY I 140 REMARK 465 SER I 141 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 ND2 ASN C 322 O5 NAG C 701 2.14 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 ILE A 54 102.46 -59.79 REMARK 500 HIS A 195 36.10 73.44 REMARK 500 SER A 254 -7.32 82.32 REMARK 500 VAL A 293 8.01 -68.52 REMARK 500 VAL A 339 -67.21 70.30 REMARK 500 ASP A 471 1.78 -67.95 REMARK 500 CYS A 498 64.63 -151.17 REMARK 500 HIS B 195 39.18 72.05 REMARK 500 SER B 254 -7.29 81.27 REMARK 500 VAL B 293 9.49 -69.85 REMARK 500 VAL B 339 -68.26 71.16 REMARK 500 ASP B 471 4.31 -69.31 REMARK 500 CYS B 498 62.96 -151.91 REMARK 500 ASN C 53 78.50 -153.61 REMARK 500 HIS C 195 38.00 71.96 REMARK 500 SER C 254 -7.26 82.20 REMARK 500 VAL C 293 6.90 -68.36 REMARK 500 VAL C 339 -68.36 70.96 REMARK 500 ASP C 494 -169.88 -76.55 REMARK 500 ASN D 107 70.45 -117.43 REMARK 500 THR E 91 109.75 -59.42 REMARK 500 ASN E 107 74.29 -118.93 REMARK 500 ASN F 107 74.07 -117.20 REMARK 500 REMARK 500 REMARK: NULL DBREF 9R19 A 19 615 UNP Q9BYF1 ACE2_HUMAN 19 615 DBREF 9R19 B 19 615 UNP Q9BYF1 ACE2_HUMAN 19 615 DBREF 9R19 C 19 615 UNP Q9BYF1 ACE2_HUMAN 19 615 DBREF 9R19 D -1 151 PDB 9R19 9R19 -1 151 DBREF 9R19 E -1 151 PDB 9R19 9R19 -1 151 DBREF 9R19 F -1 151 PDB 9R19 9R19 -1 151 DBREF 9R19 G -1 141 PDB 9R19 9R19 -1 141 DBREF 9R19 H -1 141 PDB 9R19 9R19 -1 141 DBREF 9R19 I -1 141 PDB 9R19 9R19 -1 141 SEQADV 9R19 GLY A 616 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 SER A 617 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 GLY A 618 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 LEU A 619 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 VAL A 620 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 PRO A 621 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 ARG A 622 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 GLY B 616 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 SER B 617 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 GLY B 618 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 LEU B 619 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 VAL B 620 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 PRO B 621 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 ARG B 622 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 GLY C 616 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 SER C 617 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 GLY C 618 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 LEU C 619 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 VAL C 620 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 PRO C 621 UNP Q9BYF1 EXPRESSION TAG SEQADV 9R19 ARG C 622 UNP Q9BYF1 EXPRESSION TAG SEQRES 1 A 604 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS SEQRES 2 A 604 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER SEQRES 3 A 604 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU SEQRES 4 A 604 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER SEQRES 5 A 604 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR SEQRES 6 A 604 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN SEQRES 7 A 604 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER SEQRES 8 A 604 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR SEQRES 9 A 604 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO SEQRES 10 A 604 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU SEQRES 11 A 604 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG SEQRES 12 A 604 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS SEQRES 13 A 604 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS SEQRES 14 A 604 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY SEQRES 15 A 604 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP SEQRES 16 A 604 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL SEQRES 17 A 604 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS SEQRES 18 A 604 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR SEQRES 19 A 604 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS SEQRES 20 A 604 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU SEQRES 21 A 604 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE SEQRES 22 A 604 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA SEQRES 23 A 604 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER SEQRES 24 A 604 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN SEQRES 25 A 604 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL SEQRES 26 A 604 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE SEQRES 27 A 604 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE SEQRES 28 A 604 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP SEQRES 29 A 604 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY SEQRES 30 A 604 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET SEQRES 31 A 604 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE SEQRES 32 A 604 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR SEQRES 33 A 604 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL SEQRES 34 A 604 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG SEQRES 35 A 604 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP SEQRES 36 A 604 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY SEQRES 37 A 604 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP SEQRES 38 A 604 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE SEQRES 39 A 604 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE SEQRES 40 A 604 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO SEQRES 41 A 604 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY SEQRES 42 A 604 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU SEQRES 43 A 604 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS SEQRES 44 A 604 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO SEQRES 45 A 604 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE SEQRES 46 A 604 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP GLY SEQRES 47 A 604 SER GLY LEU VAL PRO ARG SEQRES 1 B 604 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS SEQRES 2 B 604 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER SEQRES 3 B 604 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU SEQRES 4 B 604 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER SEQRES 5 B 604 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR SEQRES 6 B 604 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN SEQRES 7 B 604 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER SEQRES 8 B 604 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR SEQRES 9 B 604 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO SEQRES 10 B 604 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU SEQRES 11 B 604 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG SEQRES 12 B 604 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS SEQRES 13 B 604 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS SEQRES 14 B 604 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY SEQRES 15 B 604 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP SEQRES 16 B 604 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL SEQRES 17 B 604 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS SEQRES 18 B 604 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR SEQRES 19 B 604 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS SEQRES 20 B 604 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU SEQRES 21 B 604 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE SEQRES 22 B 604 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA SEQRES 23 B 604 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER SEQRES 24 B 604 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN SEQRES 25 B 604 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL SEQRES 26 B 604 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE SEQRES 27 B 604 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE SEQRES 28 B 604 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP SEQRES 29 B 604 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY SEQRES 30 B 604 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET SEQRES 31 B 604 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE SEQRES 32 B 604 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR SEQRES 33 B 604 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL SEQRES 34 B 604 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG SEQRES 35 B 604 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP SEQRES 36 B 604 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY SEQRES 37 B 604 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP SEQRES 38 B 604 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE SEQRES 39 B 604 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE SEQRES 40 B 604 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO SEQRES 41 B 604 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY SEQRES 42 B 604 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU SEQRES 43 B 604 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS SEQRES 44 B 604 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO SEQRES 45 B 604 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE SEQRES 46 B 604 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP GLY SEQRES 47 B 604 SER GLY LEU VAL PRO ARG SEQRES 1 C 604 SER THR ILE GLU GLU GLN ALA LYS THR PHE LEU ASP LYS SEQRES 2 C 604 PHE ASN HIS GLU ALA GLU ASP LEU PHE TYR GLN SER SER SEQRES 3 C 604 LEU ALA SER TRP ASN TYR ASN THR ASN ILE THR GLU GLU SEQRES 4 C 604 ASN VAL GLN ASN MET ASN ASN ALA GLY ASP LYS TRP SER SEQRES 5 C 604 ALA PHE LEU LYS GLU GLN SER THR LEU ALA GLN MET TYR SEQRES 6 C 604 PRO LEU GLN GLU ILE GLN ASN LEU THR VAL LYS LEU GLN SEQRES 7 C 604 LEU GLN ALA LEU GLN GLN ASN GLY SER SER VAL LEU SER SEQRES 8 C 604 GLU ASP LYS SER LYS ARG LEU ASN THR ILE LEU ASN THR SEQRES 9 C 604 MET SER THR ILE TYR SER THR GLY LYS VAL CYS ASN PRO SEQRES 10 C 604 ASP ASN PRO GLN GLU CYS LEU LEU LEU GLU PRO GLY LEU SEQRES 11 C 604 ASN GLU ILE MET ALA ASN SER LEU ASP TYR ASN GLU ARG SEQRES 12 C 604 LEU TRP ALA TRP GLU SER TRP ARG SER GLU VAL GLY LYS SEQRES 13 C 604 GLN LEU ARG PRO LEU TYR GLU GLU TYR VAL VAL LEU LYS SEQRES 14 C 604 ASN GLU MET ALA ARG ALA ASN HIS TYR GLU ASP TYR GLY SEQRES 15 C 604 ASP TYR TRP ARG GLY ASP TYR GLU VAL ASN GLY VAL ASP SEQRES 16 C 604 GLY TYR ASP TYR SER ARG GLY GLN LEU ILE GLU ASP VAL SEQRES 17 C 604 GLU HIS THR PHE GLU GLU ILE LYS PRO LEU TYR GLU HIS SEQRES 18 C 604 LEU HIS ALA TYR VAL ARG ALA LYS LEU MET ASN ALA TYR SEQRES 19 C 604 PRO SER TYR ILE SER PRO ILE GLY CYS LEU PRO ALA HIS SEQRES 20 C 604 LEU LEU GLY ASP MET TRP GLY ARG PHE TRP THR ASN LEU SEQRES 21 C 604 TYR SER LEU THR VAL PRO PHE GLY GLN LYS PRO ASN ILE SEQRES 22 C 604 ASP VAL THR ASP ALA MET VAL ASP GLN ALA TRP ASP ALA SEQRES 23 C 604 GLN ARG ILE PHE LYS GLU ALA GLU LYS PHE PHE VAL SER SEQRES 24 C 604 VAL GLY LEU PRO ASN MET THR GLN GLY PHE TRP GLU ASN SEQRES 25 C 604 SER MET LEU THR ASP PRO GLY ASN VAL GLN LYS ALA VAL SEQRES 26 C 604 CYS HIS PRO THR ALA TRP ASP LEU GLY LYS GLY ASP PHE SEQRES 27 C 604 ARG ILE LEU MET CYS THR LYS VAL THR MET ASP ASP PHE SEQRES 28 C 604 LEU THR ALA HIS HIS GLU MET GLY HIS ILE GLN TYR ASP SEQRES 29 C 604 MET ALA TYR ALA ALA GLN PRO PHE LEU LEU ARG ASN GLY SEQRES 30 C 604 ALA ASN GLU GLY PHE HIS GLU ALA VAL GLY GLU ILE MET SEQRES 31 C 604 SER LEU SER ALA ALA THR PRO LYS HIS LEU LYS SER ILE SEQRES 32 C 604 GLY LEU LEU SER PRO ASP PHE GLN GLU ASP ASN GLU THR SEQRES 33 C 604 GLU ILE ASN PHE LEU LEU LYS GLN ALA LEU THR ILE VAL SEQRES 34 C 604 GLY THR LEU PRO PHE THR TYR MET LEU GLU LYS TRP ARG SEQRES 35 C 604 TRP MET VAL PHE LYS GLY GLU ILE PRO LYS ASP GLN TRP SEQRES 36 C 604 MET LYS LYS TRP TRP GLU MET LYS ARG GLU ILE VAL GLY SEQRES 37 C 604 VAL VAL GLU PRO VAL PRO HIS ASP GLU THR TYR CYS ASP SEQRES 38 C 604 PRO ALA SER LEU PHE HIS VAL SER ASN ASP TYR SER PHE SEQRES 39 C 604 ILE ARG TYR TYR THR ARG THR LEU TYR GLN PHE GLN PHE SEQRES 40 C 604 GLN GLU ALA LEU CYS GLN ALA ALA LYS HIS GLU GLY PRO SEQRES 41 C 604 LEU HIS LYS CYS ASP ILE SER ASN SER THR GLU ALA GLY SEQRES 42 C 604 GLN LYS LEU PHE ASN MET LEU ARG LEU GLY LYS SER GLU SEQRES 43 C 604 PRO TRP THR LEU ALA LEU GLU ASN VAL VAL GLY ALA LYS SEQRES 44 C 604 ASN MET ASN VAL ARG PRO LEU LEU ASN TYR PHE GLU PRO SEQRES 45 C 604 LEU PHE THR TRP LEU LYS ASP GLN ASN LYS ASN SER PHE SEQRES 46 C 604 VAL GLY TRP SER THR ASP TRP SER PRO TYR ALA ASP GLY SEQRES 47 C 604 SER GLY LEU VAL PRO ARG SEQRES 1 D 153 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 D 153 VAL GLN ALA GLY ASP SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 D 153 SER GLY ARG THR PHE SER SER TYR ALA MET GLY TRP PHE SEQRES 4 D 153 ARG GLN ALA LEU GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 D 153 ILE SER GLY SER GLY THR SER THR TYR TYR THR ASP SER SEQRES 6 D 153 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 D 153 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 D 153 ASP THR ALA VAL TYR TYR CYS ALA ARG ALA LYS GLY PHE SEQRES 9 D 153 SER THR ILE TYR ASN GLN ASP GLU GLY ARG TYR ASP TYR SEQRES 10 D 153 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER ALA ALA SEQRES 11 D 153 ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN GLY SEQRES 12 D 153 ALA ALA HIS HIS HIS HIS HIS HIS GLY SER SEQRES 1 E 153 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 E 153 VAL GLN ALA GLY ASP SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 E 153 SER GLY ARG THR PHE SER SER TYR ALA MET GLY TRP PHE SEQRES 4 E 153 ARG GLN ALA LEU GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 E 153 ILE SER GLY SER GLY THR SER THR TYR TYR THR ASP SER SEQRES 6 E 153 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 E 153 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 E 153 ASP THR ALA VAL TYR TYR CYS ALA ARG ALA LYS GLY PHE SEQRES 9 E 153 SER THR ILE TYR ASN GLN ASP GLU GLY ARG TYR ASP TYR SEQRES 10 E 153 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER ALA ALA SEQRES 11 E 153 ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN GLY SEQRES 12 E 153 ALA ALA HIS HIS HIS HIS HIS HIS GLY SER SEQRES 1 F 153 MET ALA GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU SEQRES 2 F 153 VAL GLN ALA GLY ASP SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 F 153 SER GLY ARG THR PHE SER SER TYR ALA MET GLY TRP PHE SEQRES 4 F 153 ARG GLN ALA LEU GLY LYS GLU ARG GLU PHE VAL ALA VAL SEQRES 5 F 153 ILE SER GLY SER GLY THR SER THR TYR TYR THR ASP SER SEQRES 6 F 153 VAL LYS GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS SEQRES 7 F 153 ASN THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU SEQRES 8 F 153 ASP THR ALA VAL TYR TYR CYS ALA ARG ALA LYS GLY PHE SEQRES 9 F 153 SER THR ILE TYR ASN GLN ASP GLU GLY ARG TYR ASP TYR SEQRES 10 F 153 TRP GLY GLN GLY THR GLN VAL THR VAL SER SER ALA ALA SEQRES 11 F 153 ALA GLU GLN LYS LEU ILE SER GLU GLU ASP LEU ASN GLY SEQRES 12 F 153 ALA ALA HIS HIS HIS HIS HIS HIS GLY SER SEQRES 1 G 143 MET ALA GLU VAL GLN LEU GLN ALA SER GLY GLY GLY LEU SEQRES 2 G 143 VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 G 143 SER ARG SER THR PHE SER THR ASN THR ILE GLY TRP TYR SEQRES 4 G 143 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA SER SEQRES 5 G 143 ILE SER THR SER GLY ASN THR TYR TYR PRO ASP SER VAL SEQRES 6 G 143 LYS GLY ARG PHE ALA ILE SER ARG ASP ASN ALA GLU ASN SEQRES 7 G 143 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 G 143 THR ALA VAL TYR TYR CYS ASN THR PRO SER ARG ARG ILE SEQRES 9 G 143 SER ASN PHE TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 G 143 SER ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU ASP SEQRES 11 G 143 LEU ASN GLY ALA ALA HIS HIS HIS HIS HIS HIS GLY SER SEQRES 1 H 143 MET ALA GLU VAL GLN LEU GLN ALA SER GLY GLY GLY LEU SEQRES 2 H 143 VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 H 143 SER ARG SER THR PHE SER THR ASN THR ILE GLY TRP TYR SEQRES 4 H 143 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA SER SEQRES 5 H 143 ILE SER THR SER GLY ASN THR TYR TYR PRO ASP SER VAL SEQRES 6 H 143 LYS GLY ARG PHE ALA ILE SER ARG ASP ASN ALA GLU ASN SEQRES 7 H 143 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 H 143 THR ALA VAL TYR TYR CYS ASN THR PRO SER ARG ARG ILE SEQRES 9 H 143 SER ASN PHE TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 H 143 SER ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU ASP SEQRES 11 H 143 LEU ASN GLY ALA ALA HIS HIS HIS HIS HIS HIS GLY SER SEQRES 1 I 143 MET ALA GLU VAL GLN LEU GLN ALA SER GLY GLY GLY LEU SEQRES 2 I 143 VAL GLN ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SEQRES 3 I 143 SER ARG SER THR PHE SER THR ASN THR ILE GLY TRP TYR SEQRES 4 I 143 ARG GLN ALA PRO GLY LYS GLN ARG GLU LEU VAL ALA SER SEQRES 5 I 143 ILE SER THR SER GLY ASN THR TYR TYR PRO ASP SER VAL SEQRES 6 I 143 LYS GLY ARG PHE ALA ILE SER ARG ASP ASN ALA GLU ASN SEQRES 7 I 143 THR VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP SEQRES 8 I 143 THR ALA VAL TYR TYR CYS ASN THR PRO SER ARG ARG ILE SEQRES 9 I 143 SER ASN PHE TRP GLY GLN GLY THR GLN VAL THR VAL SER SEQRES 10 I 143 SER ALA ALA ALA GLU GLN LYS LEU ILE SER GLU GLU ASP SEQRES 11 I 143 LEU ASN GLY ALA ALA HIS HIS HIS HIS HIS HIS GLY SER HET NAG A 701 14 HET NAG A 702 14 HET NAG A 703 14 HET NAG A 704 14 HET CL A 705 1 HET CL A 706 1 HET NAG B 701 14 HET NAG B 702 14 HET NAG B 703 14 HET NAG B 704 14 HET CL B 705 1 HET CL B 706 1 HET NAG C 701 14 HET NAG C 702 14 HET NAG C 703 14 HET NAG C 704 14 HET NAG C 705 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM CL CHLORIDE 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 10 NAG 13(C8 H15 N O6) FORMUL 14 CL 4(CL 1-) FORMUL 27 HOH *104(H2 O) HELIX 1 AA1 THR A 20 ASN A 53 1 34 HELIX 2 AA2 THR A 55 GLN A 81 1 27 HELIX 3 AA3 MET A 82 TYR A 83 5 2 HELIX 4 AA4 PRO A 84 ILE A 88 5 5 HELIX 5 AA5 ASN A 90 GLN A 101 1 12 HELIX 6 AA6 ASN A 103 LEU A 108 5 6 HELIX 7 AA7 SER A 109 GLY A 130 1 22 HELIX 8 AA8 PRO A 146 SER A 155 1 10 HELIX 9 AA9 ASP A 157 VAL A 172 1 16 HELIX 10 AB1 VAL A 172 ASN A 194 1 23 HELIX 11 AB2 ASP A 198 GLY A 205 1 8 HELIX 12 AB3 ASP A 206 GLU A 208 5 3 HELIX 13 AB4 SER A 218 TYR A 252 1 35 HELIX 14 AB5 HIS A 265 LEU A 267 5 3 HELIX 15 AB6 TRP A 275 ASN A 277 5 3 HELIX 16 AB7 LEU A 278 VAL A 283 1 6 HELIX 17 AB8 VAL A 293 GLN A 300 1 8 HELIX 18 AB9 ASP A 303 VAL A 318 1 16 HELIX 19 AC1 THR A 324 SER A 331 1 8 HELIX 20 AC2 THR A 365 TYR A 385 1 21 HELIX 21 AC3 ALA A 386 GLN A 388 5 3 HELIX 22 AC4 PRO A 389 ARG A 393 5 5 HELIX 23 AC5 ASN A 397 THR A 414 1 18 HELIX 24 AC6 THR A 414 ILE A 421 1 8 HELIX 25 AC7 ASP A 431 VAL A 447 1 17 HELIX 26 AC8 GLY A 448 GLY A 466 1 19 HELIX 27 AC9 PRO A 469 ASP A 471 5 3 HELIX 28 AD1 GLN A 472 ILE A 484 1 13 HELIX 29 AD2 ASP A 499 SER A 502 5 4 HELIX 30 AD3 LEU A 503 ASN A 508 1 6 HELIX 31 AD4 ILE A 513 ALA A 533 1 21 HELIX 32 AD5 PRO A 538 CYS A 542 5 5 HELIX 33 AD6 SER A 547 ARG A 559 1 13 HELIX 34 AD7 PRO A 565 GLY A 575 1 11 HELIX 35 AD8 VAL A 581 PHE A 588 1 8 HELIX 36 AD9 PHE A 588 ASN A 599 1 12 HELIX 37 AE1 ILE B 21 THR B 52 1 32 HELIX 38 AE2 THR B 55 GLN B 81 1 27 HELIX 39 AE3 MET B 82 TYR B 83 5 2 HELIX 40 AE4 PRO B 84 ILE B 88 5 5 HELIX 41 AE5 ASN B 90 GLN B 101 1 12 HELIX 42 AE6 ASN B 103 LEU B 108 5 6 HELIX 43 AE7 SER B 109 GLY B 130 1 22 HELIX 44 AE8 PRO B 146 SER B 155 1 10 HELIX 45 AE9 ASP B 157 VAL B 172 1 16 HELIX 46 AF1 VAL B 172 ASN B 194 1 23 HELIX 47 AF2 ASP B 198 GLY B 205 1 8 HELIX 48 AF3 ASP B 206 GLU B 208 5 3 HELIX 49 AF4 SER B 218 TYR B 252 1 35 HELIX 50 AF5 HIS B 265 LEU B 267 5 3 HELIX 51 AF6 TRP B 275 ASN B 277 5 3 HELIX 52 AF7 LEU B 278 VAL B 283 1 6 HELIX 53 AF8 VAL B 293 GLN B 300 1 8 HELIX 54 AF9 ASP B 303 VAL B 318 1 16 HELIX 55 AG1 THR B 324 SER B 331 1 8 HELIX 56 AG2 THR B 365 TYR B 385 1 21 HELIX 57 AG3 ALA B 386 GLN B 388 5 3 HELIX 58 AG4 PRO B 389 ARG B 393 5 5 HELIX 59 AG5 ASN B 397 ALA B 413 1 17 HELIX 60 AG6 THR B 414 ILE B 421 1 8 HELIX 61 AG7 ASP B 431 VAL B 447 1 17 HELIX 62 AG8 GLY B 448 GLY B 466 1 19 HELIX 63 AG9 PRO B 469 ASP B 471 5 3 HELIX 64 AH1 GLN B 472 ILE B 484 1 13 HELIX 65 AH2 ASP B 499 SER B 502 5 4 HELIX 66 AH3 LEU B 503 ASN B 508 1 6 HELIX 67 AH4 ILE B 513 ALA B 533 1 21 HELIX 68 AH5 PRO B 538 CYS B 542 5 5 HELIX 69 AH6 SER B 547 ARG B 559 1 13 HELIX 70 AH7 PRO B 565 GLY B 575 1 11 HELIX 71 AH8 VAL B 581 PHE B 588 1 8 HELIX 72 AH9 PHE B 588 ASN B 599 1 12 HELIX 73 AI1 ILE C 21 ASN C 53 1 33 HELIX 74 AI2 THR C 55 GLN C 81 1 27 HELIX 75 AI3 MET C 82 TYR C 83 5 2 HELIX 76 AI4 PRO C 84 ILE C 88 5 5 HELIX 77 AI5 ASN C 90 GLN C 101 1 12 HELIX 78 AI6 ASN C 103 LEU C 108 5 6 HELIX 79 AI7 SER C 109 GLY C 130 1 22 HELIX 80 AI8 PRO C 146 SER C 155 1 10 HELIX 81 AI9 ASP C 157 VAL C 172 1 16 HELIX 82 AJ1 VAL C 172 ASN C 194 1 23 HELIX 83 AJ2 ASP C 198 GLY C 205 1 8 HELIX 84 AJ3 ASP C 206 GLU C 208 5 3 HELIX 85 AJ4 SER C 218 TYR C 252 1 35 HELIX 86 AJ5 HIS C 265 LEU C 267 5 3 HELIX 87 AJ6 TRP C 275 ASN C 277 5 3 HELIX 88 AJ7 LEU C 278 VAL C 283 1 6 HELIX 89 AJ8 VAL C 293 GLN C 300 1 8 HELIX 90 AJ9 ASP C 303 VAL C 318 1 16 HELIX 91 AK1 THR C 324 SER C 331 1 8 HELIX 92 AK2 THR C 365 TYR C 385 1 21 HELIX 93 AK3 ALA C 386 GLN C 388 5 3 HELIX 94 AK4 PRO C 389 ARG C 393 5 5 HELIX 95 AK5 ASN C 397 THR C 414 1 18 HELIX 96 AK6 THR C 414 ILE C 421 1 8 HELIX 97 AK7 ASP C 431 VAL C 447 1 17 HELIX 98 AK8 GLY C 448 GLY C 466 1 19 HELIX 99 AK9 PRO C 469 ASP C 471 5 3 HELIX 100 AL1 GLN C 472 ILE C 484 1 13 HELIX 101 AL2 ASP C 499 SER C 502 5 4 HELIX 102 AL3 LEU C 503 ASN C 508 1 6 HELIX 103 AL4 ILE C 513 ALA C 533 1 21 HELIX 104 AL5 PRO C 538 CYS C 542 5 5 HELIX 105 AL6 SER C 547 ARG C 559 1 13 HELIX 106 AL7 PRO C 565 GLY C 575 1 11 HELIX 107 AL8 VAL C 581 PHE C 588 1 8 HELIX 108 AL9 PHE C 588 ASN C 599 1 12 HELIX 109 AM1 LYS C 600 SER C 602 5 3 HELIX 110 AM2 THR D 28 TYR D 32 5 5 HELIX 111 AM3 LYS D 87 THR D 91 5 5 HELIX 112 AM4 ASP D 109 GLY D 111 5 3 HELIX 113 AM5 THR E 28 TYR E 32 5 5 HELIX 114 AM6 LYS E 87 THR E 91 5 5 HELIX 115 AM7 ASP E 109 GLY E 111 5 3 HELIX 116 AM8 THR F 28 TYR F 32 5 5 HELIX 117 AM9 LYS F 87 THR F 91 5 5 HELIX 118 AN1 ASP F 109 GLY F 111 5 3 HELIX 119 AN2 SER G 25 ASN G 32 1 8 HELIX 120 AN3 LYS G 86 THR G 90 5 5 HELIX 121 AN4 THR G 97 SER G 103 1 7 HELIX 122 AN5 SER H 25 ASN H 32 1 8 HELIX 123 AN6 LYS H 86 THR H 90 5 5 HELIX 124 AN7 THR H 97 SER H 103 1 7 HELIX 125 AN8 SER I 25 ASN I 32 1 8 HELIX 126 AN9 LYS I 86 THR I 90 5 5 HELIX 127 AO1 THR I 97 ASN I 104 1 8 SHEET 1 AA1 2 LYS A 131 ASN A 134 0 SHEET 2 AA1 2 ASN A 137 LEU A 143 -1 O LEU A 142 N VAL A 132 SHEET 1 AA2 2 LEU A 262 PRO A 263 0 SHEET 2 AA2 2 VAL A 487 VAL A 488 1 O VAL A 488 N LEU A 262 SHEET 1 AA3 2 THR A 347 GLY A 352 0 SHEET 2 AA3 2 ASP A 355 LEU A 359 -1 O ARG A 357 N TRP A 349 SHEET 1 AA4 2 LYS B 131 ASN B 134 0 SHEET 2 AA4 2 ASN B 137 LEU B 143 -1 O LEU B 142 N VAL B 132 SHEET 1 AA5 2 LEU B 262 PRO B 263 0 SHEET 2 AA5 2 VAL B 487 VAL B 488 1 O VAL B 488 N LEU B 262 SHEET 1 AA6 2 THR B 347 ASP B 350 0 SHEET 2 AA6 2 PHE B 356 LEU B 359 -1 O ARG B 357 N TRP B 349 SHEET 1 AA7 2 LYS C 131 ASN C 134 0 SHEET 2 AA7 2 ASN C 137 LEU C 143 -1 O LEU C 142 N VAL C 132 SHEET 1 AA8 2 LEU C 262 PRO C 263 0 SHEET 2 AA8 2 VAL C 487 VAL C 488 1 O VAL C 488 N LEU C 262 SHEET 1 AA9 2 THR C 347 GLY C 352 0 SHEET 2 AA9 2 ASP C 355 LEU C 359 -1 O ARG C 357 N TRP C 349 SHEET 1 AB1 4 LEU D 4 SER D 7 0 SHEET 2 AB1 4 LEU D 18 ALA D 24 -1 O SER D 21 N SER D 7 SHEET 3 AB1 4 THR D 78 MET D 83 -1 O LEU D 81 N LEU D 20 SHEET 4 AB1 4 PHE D 68 ASP D 73 -1 N SER D 71 O TYR D 80 SHEET 1 AB2 6 LEU D 11 GLN D 13 0 SHEET 2 AB2 6 THR D 120 SER D 125 1 O THR D 123 N VAL D 12 SHEET 3 AB2 6 ALA D 92 ALA D 99 -1 N TYR D 94 O THR D 120 SHEET 4 AB2 6 MET D 34 GLN D 39 -1 N GLY D 35 O ALA D 97 SHEET 5 AB2 6 GLU D 46 ILE D 51 -1 O GLU D 46 N ARG D 38 SHEET 6 AB2 6 THR D 58 TYR D 60 -1 O TYR D 59 N VAL D 50 SHEET 1 AB3 4 LEU D 11 GLN D 13 0 SHEET 2 AB3 4 THR D 120 SER D 125 1 O THR D 123 N VAL D 12 SHEET 3 AB3 4 ALA D 92 ALA D 99 -1 N TYR D 94 O THR D 120 SHEET 4 AB3 4 TYR D 113 TRP D 116 -1 O TYR D 115 N ARG D 98 SHEET 1 AB4 4 LEU E 4 SER E 7 0 SHEET 2 AB4 4 LEU E 18 ALA E 24 -1 O SER E 21 N SER E 7 SHEET 3 AB4 4 THR E 78 MET E 83 -1 O LEU E 81 N LEU E 20 SHEET 4 AB4 4 PHE E 68 ASP E 73 -1 N THR E 69 O GLN E 82 SHEET 1 AB5 6 LEU E 11 GLN E 13 0 SHEET 2 AB5 6 THR E 120 SER E 125 1 O THR E 123 N VAL E 12 SHEET 3 AB5 6 ALA E 92 ALA E 99 -1 N TYR E 94 O THR E 120 SHEET 4 AB5 6 MET E 34 GLN E 39 -1 N GLY E 35 O ALA E 97 SHEET 5 AB5 6 GLU E 46 ILE E 51 -1 O GLU E 46 N ARG E 38 SHEET 6 AB5 6 THR E 58 TYR E 60 -1 O TYR E 59 N VAL E 50 SHEET 1 AB6 4 LEU E 11 GLN E 13 0 SHEET 2 AB6 4 THR E 120 SER E 125 1 O THR E 123 N VAL E 12 SHEET 3 AB6 4 ALA E 92 ALA E 99 -1 N TYR E 94 O THR E 120 SHEET 4 AB6 4 TYR E 113 TRP E 116 -1 O TYR E 115 N ARG E 98 SHEET 1 AB7 4 LEU F 4 SER F 7 0 SHEET 2 AB7 4 LEU F 18 ALA F 24 -1 O SER F 21 N SER F 7 SHEET 3 AB7 4 THR F 78 MET F 83 -1 O MET F 83 N LEU F 18 SHEET 4 AB7 4 PHE F 68 ASP F 73 -1 N SER F 71 O TYR F 80 SHEET 1 AB8 5 THR F 58 TYR F 60 0 SHEET 2 AB8 5 ARG F 45 ILE F 51 -1 N VAL F 50 O TYR F 59 SHEET 3 AB8 5 MET F 34 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 4 AB8 5 ALA F 92 ALA F 99 -1 O ALA F 97 N GLY F 35 SHEET 5 AB8 5 TYR F 113 TRP F 116 -1 O TYR F 115 N ARG F 98 SHEET 1 AB9 5 THR F 58 TYR F 60 0 SHEET 2 AB9 5 ARG F 45 ILE F 51 -1 N VAL F 50 O TYR F 59 SHEET 3 AB9 5 MET F 34 GLN F 39 -1 N ARG F 38 O GLU F 46 SHEET 4 AB9 5 ALA F 92 ALA F 99 -1 O ALA F 97 N GLY F 35 SHEET 5 AB9 5 THR F 120 VAL F 122 -1 O THR F 120 N TYR F 94 SHEET 1 AC1 4 GLN G 5 SER G 7 0 SHEET 2 AC1 4 SER G 17 ALA G 23 -1 O SER G 21 N SER G 7 SHEET 3 AC1 4 THR G 77 ASN G 83 -1 O MET G 82 N LEU G 18 SHEET 4 AC1 4 PHE G 67 ASP G 72 -1 N ALA G 68 O GLN G 81 SHEET 1 AC2 6 LEU G 11 VAL G 12 0 SHEET 2 AC2 6 THR G 110 VAL G 114 1 O THR G 113 N VAL G 12 SHEET 3 AC2 6 ALA G 91 ASN G 96 -1 N TYR G 93 O THR G 110 SHEET 4 AC2 6 ILE G 34 GLN G 39 -1 N TYR G 37 O TYR G 94 SHEET 5 AC2 6 ARG G 45 ILE G 51 -1 O ALA G 49 N TRP G 36 SHEET 6 AC2 6 THR G 57 TYR G 58 -1 O TYR G 58 N SER G 50 SHEET 1 AC3 4 GLN H 5 SER H 7 0 SHEET 2 AC3 4 SER H 17 ALA H 23 -1 O SER H 21 N SER H 7 SHEET 3 AC3 4 THR H 77 ASN H 83 -1 O MET H 82 N LEU H 18 SHEET 4 AC3 4 PHE H 67 ASP H 72 -1 N ASP H 72 O THR H 77 SHEET 1 AC4 6 LEU H 11 VAL H 12 0 SHEET 2 AC4 6 THR H 110 VAL H 114 1 O THR H 113 N VAL H 12 SHEET 3 AC4 6 ALA H 91 ASN H 96 -1 N TYR H 93 O THR H 110 SHEET 4 AC4 6 ILE H 34 GLN H 39 -1 N TYR H 37 O TYR H 94 SHEET 5 AC4 6 ARG H 45 ILE H 51 -1 O ALA H 49 N TRP H 36 SHEET 6 AC4 6 THR H 57 TYR H 58 -1 O TYR H 58 N SER H 50 SHEET 1 AC5 4 GLN I 5 SER I 7 0 SHEET 2 AC5 4 SER I 17 ALA I 23 -1 O SER I 21 N SER I 7 SHEET 3 AC5 4 THR I 77 ASN I 83 -1 O MET I 82 N LEU I 18 SHEET 4 AC5 4 ILE I 69 ASP I 72 -1 N ASP I 72 O THR I 77 SHEET 1 AC6 6 LEU I 11 VAL I 12 0 SHEET 2 AC6 6 THR I 110 VAL I 114 1 O THR I 113 N VAL I 12 SHEET 3 AC6 6 ALA I 91 ASN I 96 -1 N TYR I 93 O THR I 110 SHEET 4 AC6 6 ILE I 34 GLN I 39 -1 N TYR I 37 O TYR I 94 SHEET 5 AC6 6 ARG I 45 ILE I 51 -1 O ALA I 49 N TRP I 36 SHEET 6 AC6 6 THR I 57 TYR I 58 -1 O TYR I 58 N SER I 50 SSBOND 1 CYS A 133 CYS A 141 1555 1555 2.05 SSBOND 2 CYS A 344 CYS A 361 1555 1555 2.04 SSBOND 3 CYS A 530 CYS A 542 1555 1555 2.04 SSBOND 4 CYS B 133 CYS B 141 1555 1555 2.04 SSBOND 5 CYS B 344 CYS B 361 1555 1555 2.03 SSBOND 6 CYS B 530 CYS B 542 1555 1555 2.04 SSBOND 7 CYS C 133 CYS C 141 1555 1555 2.04 SSBOND 8 CYS C 344 CYS C 361 1555 1555 2.04 SSBOND 9 CYS C 530 CYS C 542 1555 1555 2.04 SSBOND 10 CYS D 22 CYS D 96 1555 1555 2.04 SSBOND 11 CYS E 22 CYS E 96 1555 1555 2.04 SSBOND 12 CYS F 22 CYS F 96 1555 1555 2.04 SSBOND 13 CYS G 22 CYS G 95 1555 1555 2.03 SSBOND 14 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 15 CYS I 22 CYS I 95 1555 1555 2.04 LINK ND2 ASN A 53 C1 NAG A 701 1555 1555 1.43 LINK ND2 ASN A 90 C1 NAG A 703 1555 1555 1.43 LINK ND2 ASN A 103 C1 NAG A 704 1555 1555 1.43 LINK ND2 ASN A 546 C1 NAG A 702 1555 1555 1.42 LINK ND2 ASN B 53 C1 NAG B 701 1555 1555 1.43 LINK ND2 ASN B 90 C1 NAG B 702 1555 1555 1.43 LINK ND2 ASN B 103 C1 NAG B 703 1555 1555 1.43 LINK ND2 ASN B 322 C1 NAG B 704 1555 1555 1.43 LINK ND2 ASN C 53 C1 NAG C 702 1555 1555 1.43 LINK ND2 ASN C 90 C1 NAG C 704 1555 1555 1.43 LINK ND2 ASN C 322 C1 NAG C 701 1555 1555 1.43 LINK ND2 ASN C 432 C1 NAG C 705 1555 1555 1.43 LINK ND2 ASN C 546 C1 NAG C 703 1555 1555 1.43 CISPEP 1 GLU A 145 PRO A 146 0 5.17 CISPEP 2 GLU B 145 PRO B 146 0 6.26 CISPEP 3 GLU C 145 PRO C 146 0 5.06 CRYST1 97.920 108.150 146.100 90.00 98.89 90.00 P 1 21 1 6 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 0.010212 0.000000 0.001597 0.00000 SCALE2 0.000000 0.009246 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006928 0.00000