HEADER IMMUNE SYSTEM 25-SEP-24 9GVN TITLE DEPEMOKIMAB FAB IN COMPLEX WITH INTERLEUKIN 5 COMPND MOL_ID: 1; COMPND 2 MOLECULE: INTERLEUKIN-5; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: IL-5,B-CELL DIFFERENTIATION FACTOR I,EOSINOPHIL COMPND 5 DIFFERENTIATION FACTOR,T-CELL REPLACING FACTOR,TRF; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: FAB HEAVY CHAIN; COMPND 9 CHAIN: C, E; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: FAB LIGHT CHAIN; COMPND 13 CHAIN: D, F; COMPND 14 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: IL5; SOURCE 6 EXPRESSION_SYSTEM: DROSOPHILA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7215; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 15 ORGANISM_TAXID: 9606; SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS IL-5, ANTIBODY, COMPLEX, EPITOPE, CYTOKINE, GLYCOPROTEIN, KEYWDS 2 IMMUNOGLOBULIN FOLD, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR D.O.SOMERS REVDAT 1 14-JAN-26 9GVN 0 JRNL AUTH M.ORECCHIA,K.WELBECK,J.DEXTER,L.HOOK,C.AKINSEYE,M.KOT, JRNL AUTH 2 A.LEWIS,D.SOMERS,T.BHINDER,P.HAMBLIN,S.ELSEY,D.WILLE,S.GRANT JRNL TITL GENERATION AND PRECLINICAL ASSESSMENT OF DEPEMOKIMAB, AN JRNL TITL 2 ENHANCED IL-5 ANTAGONIST MONOCLONAL ANTIBODY JRNL REF HELIYON V. 12 2026 JRNL REFN ESSN 2405-8440 JRNL DOI 10.1016/J.HELIYON.2025.E44247 REMARK 2 REMARK 2 RESOLUTION. 1.93 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.11.8 (16-JUL-2021) 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) : 1.93 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 192.46 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 55.5 REMARK 3 NUMBER OF REFLECTIONS : 90317 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) : 0.185 REMARK 3 R VALUE (WORKING SET) : 0.183 REMARK 3 FREE R VALUE : 0.209 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.990 REMARK 3 FREE R VALUE TEST SET COUNT : 4508 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 : NULL REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 1.93 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.11 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 4.71 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : NULL REMARK 3 BIN R VALUE (WORKING + TEST SET) : NULL REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 1721 REMARK 3 BIN R VALUE (WORKING SET) : 0.2691 REMARK 3 BIN FREE R VALUE : 0.2527 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.76 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 : 8367 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 93 REMARK 3 SOLVENT ATOMS : 772 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 67.44 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -5.71630 REMARK 3 B22 (A**2) : 1.78980 REMARK 3 B33 (A**2) : 3.92650 REMARK 3 B12 (A**2) : 0.00000 REMARK 3 B13 (A**2) : -0.57690 REMARK 3 B23 (A**2) : 0.00000 REMARK 3 REMARK 3 ESTIMATED COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.250 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.185 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.158 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : 0.179 REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : 0.157 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 : 0.952 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.938 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 8653 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 11776 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 2950 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 1427 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 8653 ; 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 : 1180 ; 5.000 ; SEMIHARMONIC REMARK 3 SUM OF OCCUPANCIES : 1 ; 1.000 ; HARMONIC 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 : 6769 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.008 REMARK 3 BOND ANGLES (DEGREES) : 0.99 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.30 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 16.66 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 6 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): 68.6652 7.7813 39.3283 REMARK 3 T TENSOR REMARK 3 T11: -0.1323 T22: 0.1314 REMARK 3 T33: -0.2111 T12: -0.1332 REMARK 3 T13: 0.0318 T23: -0.0249 REMARK 3 L TENSOR REMARK 3 L11: 1.6623 L22: 3.1830 REMARK 3 L33: 5.0506 L12: 0.2900 REMARK 3 L13: 0.2579 L23: 1.9006 REMARK 3 S TENSOR REMARK 3 S11: 0.0613 S12: -0.2476 S13: 0.1336 REMARK 3 S21: 0.4000 S22: 0.1035 S23: -0.0616 REMARK 3 S31: -0.3272 S32: 0.8257 S33: -0.1648 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): 63.4809 3.9603 23.5666 REMARK 3 T TENSOR REMARK 3 T11: -0.2153 T22: 0.0269 REMARK 3 T33: -0.0606 T12: -0.0042 REMARK 3 T13: 0.0083 T23: 0.0135 REMARK 3 L TENSOR REMARK 3 L11: 1.3377 L22: 1.4813 REMARK 3 L33: 1.8477 L12: 0.4683 REMARK 3 L13: 0.3664 L23: 0.3702 REMARK 3 S TENSOR REMARK 3 S11: 0.0894 S12: 0.0441 S13: 0.1477 REMARK 3 S21: 0.0768 S22: -0.0943 S23: 0.0571 REMARK 3 S31: -0.1246 S32: 0.3752 S33: 0.0049 REMARK 3 REMARK 3 TLS GROUP : 3 REMARK 3 SELECTION: { C|* } REMARK 3 ORIGIN FOR THE GROUP (A): 23.2610 8.8011 5.0434 REMARK 3 T TENSOR REMARK 3 T11: -0.1462 T22: -0.1987 REMARK 3 T33: -0.0043 T12: 0.0116 REMARK 3 T13: -0.0121 T23: -0.0301 REMARK 3 L TENSOR REMARK 3 L11: 3.2468 L22: 0.8574 REMARK 3 L33: 0.5625 L12: -0.6067 REMARK 3 L13: 0.5797 L23: -0.4416 REMARK 3 S TENSOR REMARK 3 S11: -0.0045 S12: -0.0642 S13: 0.2407 REMARK 3 S21: 0.0466 S22: -0.0242 S23: 0.0880 REMARK 3 S31: 0.0318 S32: 0.0274 S33: 0.0287 REMARK 3 REMARK 3 TLS GROUP : 4 REMARK 3 SELECTION: { D|* } REMARK 3 ORIGIN FOR THE GROUP (A): 14.9924 -1.3285 17.3698 REMARK 3 T TENSOR REMARK 3 T11: -0.1901 T22: -0.0607 REMARK 3 T33: -0.0237 T12: 0.0153 REMARK 3 T13: 0.0105 T23: 0.0306 REMARK 3 L TENSOR REMARK 3 L11: 4.4757 L22: 0.5130 REMARK 3 L33: 0.2550 L12: 0.1649 REMARK 3 L13: 0.8496 L23: 0.0674 REMARK 3 S TENSOR REMARK 3 S11: 0.0043 S12: -0.7830 S13: -0.0371 REMARK 3 S21: 0.0710 S22: 0.0085 S23: 0.2154 REMARK 3 S31: 0.0453 S32: -0.1311 S33: -0.0128 REMARK 3 REMARK 3 TLS GROUP : 5 REMARK 3 SELECTION: { E|* } REMARK 3 ORIGIN FOR THE GROUP (A): 47.9908 1.1576 77.8920 REMARK 3 T TENSOR REMARK 3 T11: 0.6871 T22: -0.2652 REMARK 3 T33: -0.3383 T12: -0.0188 REMARK 3 T13: 0.4346 T23: -0.0210 REMARK 3 L TENSOR REMARK 3 L11: 3.2953 L22: 2.1871 REMARK 3 L33: 4.3700 L12: 0.4759 REMARK 3 L13: -3.0280 L23: -0.5444 REMARK 3 S TENSOR REMARK 3 S11: -0.1162 S12: -0.3368 S13: -0.1722 REMARK 3 S21: 1.1340 S22: -0.0419 S23: 0.4827 REMARK 3 S31: 0.1211 S32: 0.4940 S33: 0.1581 REMARK 3 REMARK 3 TLS GROUP : 6 REMARK 3 SELECTION: { F|* } REMARK 3 ORIGIN FOR THE GROUP (A): 33.3306 10.8590 73.4514 REMARK 3 T TENSOR REMARK 3 T11: 0.4917 T22: -0.2023 REMARK 3 T33: -0.0539 T12: -0.0174 REMARK 3 T13: 0.5955 T23: -0.0269 REMARK 3 L TENSOR REMARK 3 L11: 3.2000 L22: 1.2415 REMARK 3 L33: 6.9629 L12: -0.1324 REMARK 3 L13: -4.4780 L23: 0.4040 REMARK 3 S TENSOR REMARK 3 S11: -0.0196 S12: 0.5593 S13: -0.0271 REMARK 3 S21: 0.8104 S22: -0.0136 S23: 0.6898 REMARK 3 S31: -0.1128 S32: -0.8295 S33: 0.0333 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9GVN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 25-SEP-24. REMARK 100 THE DEPOSITION ID IS D_1292142031. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 20-JUN-16 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 : I02 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97949 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : AUTOPROC 1.1.7 REMARK 200 DATA SCALING SOFTWARE : AUTOPROC 1.1.7 REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 90317 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.933 REMARK 200 RESOLUTION RANGE LOW (A) : 192.462 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 55.5 REMARK 200 DATA REDUNDANCY : 3.400 REMARK 200 R MERGE (I) : 0.04300 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 13.7000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.93 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.20 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 0.56000 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.000 REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: FOURIER SYNTHESIS REMARK 200 SOFTWARE USED: NULL REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): NULL REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS EDO_P8K, MORPHEUS CARBOXYLIC REMARK 280 ACIDS, MORPHEUS BUFFER SYSTEM 2, VAPOR DIFFUSION, HANGING DROP, REMARK 280 TEMPERATURE 293K 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 32.93500 REMARK 290 SMTRY3 2 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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 20460 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 47340 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -100.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, J REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 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 ILE A 1 REMARK 465 PRO A 2 REMARK 465 THR A 3 REMARK 465 SER A 115 REMARK 465 ILE B 1 REMARK 465 PRO B 2 REMARK 465 SER B 115 REMARK 465 SER C 136 REMARK 465 THR C 137 REMARK 465 SER C 138 REMARK 465 GLY C 139 REMARK 465 CYS C 222 REMARK 465 ASP C 223 REMARK 465 LYS C 224 REMARK 465 THR C 225 REMARK 465 HIS C 226 REMARK 465 CYS D 220 REMARK 465 LYS E 135 REMARK 465 SER E 136 REMARK 465 THR E 137 REMARK 465 SER E 138 REMARK 465 GLY E 139 REMARK 465 LYS E 220 REMARK 465 SER E 221 REMARK 465 CYS E 222 REMARK 465 ASP E 223 REMARK 465 LYS E 224 REMARK 465 THR E 225 REMARK 465 HIS E 226 REMARK 465 CYS F 220 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 VAL B 60 98.98 -68.78 REMARK 500 THR C 15 -16.94 84.25 REMARK 500 ASP C 150 64.28 61.97 REMARK 500 ALA D 57 -32.44 68.11 REMARK 500 LYS D 196 -51.87 -122.95 REMARK 500 THR E 15 -11.66 74.12 REMARK 500 SER E 65 17.37 54.02 REMARK 500 LEU E 130 75.90 -114.08 REMARK 500 ALA F 57 -34.65 70.15 REMARK 500 SER F 83 70.63 49.03 REMARK 500 ASN F 144 71.55 45.74 REMARK 500 LYS F 175 -57.04 -120.25 REMARK 500 REMARK 500 REMARK: NULL DBREF 9GVN A 1 115 UNP P05113 IL5_HUMAN 20 134 DBREF 9GVN B 1 115 UNP P05113 IL5_HUMAN 20 134 DBREF 9GVN C 1 226 PDB 9GVN 9GVN 1 226 DBREF 9GVN D 1 220 PDB 9GVN 9GVN 1 220 DBREF 9GVN E 1 226 PDB 9GVN 9GVN 1 226 DBREF 9GVN F 1 220 PDB 9GVN 9GVN 1 220 SEQRES 1 A 115 ILE PRO THR GLU ILE PRO THR SER ALA LEU VAL LYS GLU SEQRES 2 A 115 THR LEU ALA LEU LEU SER THR HIS ARG THR LEU LEU ILE SEQRES 3 A 115 ALA ASN GLU THR LEU ARG ILE PRO VAL PRO VAL HIS LYS SEQRES 4 A 115 ASN HIS GLN LEU CYS THR GLU GLU ILE PHE GLN GLY ILE SEQRES 5 A 115 GLY THR LEU GLU SER GLN THR VAL GLN GLY GLY THR VAL SEQRES 6 A 115 GLU ARG LEU PHE LYS ASN LEU SER LEU ILE LYS LYS TYR SEQRES 7 A 115 ILE ASP GLY GLN LYS LYS LYS CYS GLY GLU GLU ARG ARG SEQRES 8 A 115 ARG VAL ASN GLN PHE LEU ASP TYR LEU GLN GLU PHE LEU SEQRES 9 A 115 GLY VAL MET ASN THR GLU TRP ILE ILE GLU SER SEQRES 1 B 115 ILE PRO THR GLU ILE PRO THR SER ALA LEU VAL LYS GLU SEQRES 2 B 115 THR LEU ALA LEU LEU SER THR HIS ARG THR LEU LEU ILE SEQRES 3 B 115 ALA ASN GLU THR LEU ARG ILE PRO VAL PRO VAL HIS LYS SEQRES 4 B 115 ASN HIS GLN LEU CYS THR GLU GLU ILE PHE GLN GLY ILE SEQRES 5 B 115 GLY THR LEU GLU SER GLN THR VAL GLN GLY GLY THR VAL SEQRES 6 B 115 GLU ARG LEU PHE LYS ASN LEU SER LEU ILE LYS LYS TYR SEQRES 7 B 115 ILE ASP GLY GLN LYS LYS LYS CYS GLY GLU GLU ARG ARG SEQRES 8 B 115 ARG VAL ASN GLN PHE LEU ASP TYR LEU GLN GLU PHE LEU SEQRES 9 B 115 GLY VAL MET ASN THR GLU TRP ILE ILE GLU SER SEQRES 1 C 226 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 C 226 PRO THR GLN THR LEU THR LEU THR CYS THR VAL SER GLY SEQRES 3 C 226 PHE SER LEU THR GLY SER SER VAL HIS TRP VAL ARG GLN SEQRES 4 C 226 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 C 226 ALA SER GLY GLY THR ASP TYR ASN SER ALA LEU MET SER SEQRES 6 C 226 ARG LEU SER ILE SER LYS ASP THR SER ARG ASN GLN VAL SEQRES 7 C 226 VAL LEU THR MET THR ASN MET ASP PRO VAL ASP THR ALA SEQRES 8 C 226 THR TYR TYR CYS ALA ARG ASP PRO PRO SER GLY LEU LEU SEQRES 9 C 226 ARG LEU ASP TYR TRP GLY ARG GLY THR LEU VAL THR VAL SEQRES 10 C 226 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 C 226 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 C 226 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 C 226 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 C 226 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 C 226 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 C 226 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 C 226 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 18 C 226 CYS ASP LYS THR HIS SEQRES 1 D 220 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 D 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 D 220 GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU SEQRES 4 D 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 D 220 LEU ILE TYR GLY ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 D 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 D 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 D 220 TYR TYR CYS GLN ASN VAL HIS SER PHE PRO PHE THR PHE SEQRES 9 D 220 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA SEQRES 10 D 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 D 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 D 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 D 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 D 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 D 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 D 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 D 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS SEQRES 1 E 226 GLN VAL THR LEU ARG GLU SER GLY PRO ALA LEU VAL LYS SEQRES 2 E 226 PRO THR GLN THR LEU THR LEU THR CYS THR VAL SER GLY SEQRES 3 E 226 PHE SER LEU THR GLY SER SER VAL HIS TRP VAL ARG GLN SEQRES 4 E 226 PRO PRO GLY LYS GLY LEU GLU TRP LEU GLY VAL ILE TRP SEQRES 5 E 226 ALA SER GLY GLY THR ASP TYR ASN SER ALA LEU MET SER SEQRES 6 E 226 ARG LEU SER ILE SER LYS ASP THR SER ARG ASN GLN VAL SEQRES 7 E 226 VAL LEU THR MET THR ASN MET ASP PRO VAL ASP THR ALA SEQRES 8 E 226 THR TYR TYR CYS ALA ARG ASP PRO PRO SER GLY LEU LEU SEQRES 9 E 226 ARG LEU ASP TYR TRP GLY ARG GLY THR LEU VAL THR VAL SEQRES 10 E 226 SER SER ALA SER THR LYS GLY PRO SER VAL PHE PRO LEU SEQRES 11 E 226 ALA PRO SER SER LYS SER THR SER GLY GLY THR ALA ALA SEQRES 12 E 226 LEU GLY CYS LEU VAL LYS ASP TYR PHE PRO GLU PRO VAL SEQRES 13 E 226 THR VAL SER TRP ASN SER GLY ALA LEU THR SER GLY VAL SEQRES 14 E 226 HIS THR PHE PRO ALA VAL LEU GLN SER SER GLY LEU TYR SEQRES 15 E 226 SER LEU SER SER VAL VAL THR VAL PRO SER SER SER LEU SEQRES 16 E 226 GLY THR GLN THR TYR ILE CYS ASN VAL ASN HIS LYS PRO SEQRES 17 E 226 SER ASN THR LYS VAL ASP LYS ARG VAL GLU PRO LYS SER SEQRES 18 E 226 CYS ASP LYS THR HIS SEQRES 1 F 220 ASP ILE VAL MET THR GLN SER PRO ASP SER LEU ALA VAL SEQRES 2 F 220 SER LEU GLY GLU ARG ALA THR ILE ASN CYS LYS SER SER SEQRES 3 F 220 GLN SER LEU LEU ASN SER GLY ASN GLN LYS ASN TYR LEU SEQRES 4 F 220 ALA TRP TYR GLN GLN LYS PRO GLY GLN PRO PRO LYS LEU SEQRES 5 F 220 LEU ILE TYR GLY ALA SER THR ARG GLU SER GLY VAL PRO SEQRES 6 F 220 ASP ARG PHE SER GLY SER GLY SER GLY THR ASP PHE THR SEQRES 7 F 220 LEU THR ILE SER SER LEU GLN ALA GLU ASP VAL ALA VAL SEQRES 8 F 220 TYR TYR CYS GLN ASN VAL HIS SER PHE PRO PHE THR PHE SEQRES 9 F 220 GLY GLY GLY THR LYS LEU GLU ILE LYS ARG THR VAL ALA SEQRES 10 F 220 ALA PRO SER VAL PHE ILE PHE PRO PRO SER ASP GLU GLN SEQRES 11 F 220 LEU LYS SER GLY THR ALA SER VAL VAL CYS LEU LEU ASN SEQRES 12 F 220 ASN PHE TYR PRO ARG GLU ALA LYS VAL GLN TRP LYS VAL SEQRES 13 F 220 ASP ASN ALA LEU GLN SER GLY ASN SER GLN GLU SER VAL SEQRES 14 F 220 THR GLU GLN ASP SER LYS ASP SER THR TYR SER LEU SER SEQRES 15 F 220 SER THR LEU THR LEU SER LYS ALA ASP TYR GLU LYS HIS SEQRES 16 F 220 LYS VAL TYR ALA CYS GLU VAL THR HIS GLN GLY LEU SER SEQRES 17 F 220 SER PRO VAL THR LYS SER PHE ASN ARG GLY GLU CYS HET NAG J 1 14 HET NAG J 2 14 HET MAN J 3 11 HET MAN J 4 11 HET MAN J 5 11 HET FUC J 6 10 HET EDO B 201 4 HET GOL C 301 6 HET GOL D 301 6 HET GOL D 302 6 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM EDO 1,2-ETHANEDIOL HETNAM GOL GLYCEROL 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 MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE HETSYN EDO ETHYLENE GLYCOL HETSYN GOL GLYCERIN; PROPANE-1,2,3-TRIOL FORMUL 7 NAG 2(C8 H15 N O6) FORMUL 7 MAN 3(C6 H12 O6) FORMUL 7 FUC C6 H12 O5 FORMUL 8 EDO C2 H6 O2 FORMUL 9 GOL 3(C3 H8 O3) FORMUL 12 HOH *772(H2 O) HELIX 1 AA1 PRO A 6 ARG A 22 1 17 HELIX 2 AA2 THR A 23 LEU A 25 5 3 HELIX 3 AA3 ASN A 40 LEU A 43 5 4 HELIX 4 AA4 CYS A 44 GLN A 58 1 15 HELIX 5 AA5 GLY A 62 LYS A 85 1 24 HELIX 6 AA6 ARG A 92 GLU A 110 1 19 HELIX 7 AA7 PRO B 6 ARG B 22 1 17 HELIX 8 AA8 THR B 23 LEU B 25 5 3 HELIX 9 AA9 ASN B 40 LEU B 43 5 4 HELIX 10 AB1 CYS B 44 GLN B 58 1 15 HELIX 11 AB2 GLY B 62 LYS B 85 1 24 HELIX 12 AB3 ARG B 92 GLU B 110 1 19 HELIX 13 AB4 ASP C 86 THR C 90 5 5 HELIX 14 AB5 SER C 162 ALA C 164 5 3 HELIX 15 AB6 SER C 193 LEU C 195 5 3 HELIX 16 AB7 LYS C 207 ASN C 210 5 4 HELIX 17 AB8 GLN D 85 VAL D 89 5 5 HELIX 18 AB9 SER D 127 LYS D 132 1 6 HELIX 19 AC1 LYS D 189 LYS D 194 1 6 HELIX 20 AC2 SER E 61 MET E 64 5 4 HELIX 21 AC3 ASP E 86 THR E 90 5 5 HELIX 22 AC4 SER E 162 ALA E 164 5 3 HELIX 23 AC5 SER E 193 LEU E 195 5 3 HELIX 24 AC6 LYS E 207 ASN E 210 5 4 HELIX 25 AC7 GLN F 85 VAL F 89 5 5 HELIX 26 AC8 SER F 127 LYS F 132 1 6 HELIX 27 AC9 LYS F 189 GLU F 193 1 5 SHEET 1 AA1 2 ILE A 33 PRO A 34 0 SHEET 2 AA1 2 ARG B 90 ARG B 91 -1 O ARG B 91 N ILE A 33 SHEET 1 AA2 2 ARG A 90 ARG A 91 0 SHEET 2 AA2 2 ILE B 33 PRO B 34 -1 O ILE B 33 N ARG A 91 SHEET 1 AA3 4 THR C 3 SER C 7 0 SHEET 2 AA3 4 LEU C 18 SER C 25 -1 O THR C 21 N SER C 7 SHEET 3 AA3 4 GLN C 77 MET C 82 -1 O VAL C 78 N CYS C 22 SHEET 4 AA3 4 LEU C 67 ASP C 72 -1 N SER C 70 O VAL C 79 SHEET 1 AA4 6 LEU C 11 VAL C 12 0 SHEET 2 AA4 6 THR C 113 VAL C 117 1 O THR C 116 N VAL C 12 SHEET 3 AA4 6 ALA C 91 ASP C 98 -1 N TYR C 93 O THR C 113 SHEET 4 AA4 6 SER C 33 GLN C 39 -1 N VAL C 37 O TYR C 94 SHEET 5 AA4 6 GLU C 46 ILE C 51 -1 O LEU C 48 N TRP C 36 SHEET 6 AA4 6 THR C 57 TYR C 59 -1 O ASP C 58 N VAL C 50 SHEET 1 AA5 4 LEU C 11 VAL C 12 0 SHEET 2 AA5 4 THR C 113 VAL C 117 1 O THR C 116 N VAL C 12 SHEET 3 AA5 4 ALA C 91 ASP C 98 -1 N TYR C 93 O THR C 113 SHEET 4 AA5 4 TYR C 108 TRP C 109 -1 O TYR C 108 N ARG C 97 SHEET 1 AA6 4 SER C 126 LEU C 130 0 SHEET 2 AA6 4 THR C 141 TYR C 151 -1 O LEU C 147 N PHE C 128 SHEET 3 AA6 4 TYR C 182 PRO C 191 -1 O VAL C 190 N ALA C 142 SHEET 4 AA6 4 VAL C 169 THR C 171 -1 N HIS C 170 O VAL C 187 SHEET 1 AA7 4 SER C 126 LEU C 130 0 SHEET 2 AA7 4 THR C 141 TYR C 151 -1 O LEU C 147 N PHE C 128 SHEET 3 AA7 4 TYR C 182 PRO C 191 -1 O VAL C 190 N ALA C 142 SHEET 4 AA7 4 VAL C 175 LEU C 176 -1 N VAL C 175 O SER C 183 SHEET 1 AA8 3 THR C 157 TRP C 160 0 SHEET 2 AA8 3 ILE C 201 HIS C 206 -1 O ASN C 203 N SER C 159 SHEET 3 AA8 3 THR C 211 ARG C 216 -1 O VAL C 213 N VAL C 204 SHEET 1 AA9 4 MET D 4 SER D 7 0 SHEET 2 AA9 4 ALA D 19 SER D 25 -1 O LYS D 24 N THR D 5 SHEET 3 AA9 4 ASP D 76 ILE D 81 -1 O PHE D 77 N CYS D 23 SHEET 4 AA9 4 PHE D 68 SER D 73 -1 N SER D 69 O THR D 80 SHEET 1 AB1 6 SER D 10 SER D 14 0 SHEET 2 AB1 6 THR D 108 LYS D 113 1 O GLU D 111 N LEU D 11 SHEET 3 AB1 6 ALA D 90 ASN D 96 -1 N ALA D 90 O LEU D 110 SHEET 4 AB1 6 LEU D 39 GLN D 44 -1 N GLN D 44 O VAL D 91 SHEET 5 AB1 6 LYS D 51 TYR D 55 -1 O LEU D 53 N TRP D 41 SHEET 6 AB1 6 THR D 59 ARG D 60 -1 O THR D 59 N TYR D 55 SHEET 1 AB2 2 LEU D 30 ASN D 31 0 SHEET 2 AB2 2 LYS D 36 ASN D 37 -1 O LYS D 36 N ASN D 31 SHEET 1 AB3 4 SER D 120 PHE D 124 0 SHEET 2 AB3 4 THR D 135 PHE D 145 -1 O LEU D 141 N PHE D 122 SHEET 3 AB3 4 TYR D 179 SER D 188 -1 O LEU D 181 N LEU D 142 SHEET 4 AB3 4 SER D 165 VAL D 169 -1 N GLN D 166 O THR D 184 SHEET 1 AB4 4 ALA D 159 LEU D 160 0 SHEET 2 AB4 4 LYS D 151 VAL D 156 -1 N VAL D 156 O ALA D 159 SHEET 3 AB4 4 VAL D 197 THR D 203 -1 O GLU D 201 N GLN D 153 SHEET 4 AB4 4 VAL D 211 ASN D 216 -1 O VAL D 211 N VAL D 202 SHEET 1 AB5 4 THR E 3 SER E 7 0 SHEET 2 AB5 4 LEU E 18 SER E 25 -1 O THR E 21 N SER E 7 SHEET 3 AB5 4 GLN E 77 MET E 82 -1 O MET E 82 N LEU E 18 SHEET 4 AB5 4 ILE E 69 ASP E 72 -1 N ASP E 72 O GLN E 77 SHEET 1 AB6 6 LEU E 11 VAL E 12 0 SHEET 2 AB6 6 THR E 113 VAL E 117 1 O THR E 116 N VAL E 12 SHEET 3 AB6 6 ALA E 91 ASP E 98 -1 N TYR E 93 O THR E 113 SHEET 4 AB6 6 SER E 33 GLN E 39 -1 N VAL E 37 O TYR E 94 SHEET 5 AB6 6 GLU E 46 ILE E 51 -1 O LEU E 48 N TRP E 36 SHEET 6 AB6 6 THR E 57 TYR E 59 -1 O ASP E 58 N VAL E 50 SHEET 1 AB7 4 LEU E 11 VAL E 12 0 SHEET 2 AB7 4 THR E 113 VAL E 117 1 O THR E 116 N VAL E 12 SHEET 3 AB7 4 ALA E 91 ASP E 98 -1 N TYR E 93 O THR E 113 SHEET 4 AB7 4 TYR E 108 TRP E 109 -1 O TYR E 108 N ARG E 97 SHEET 1 AB8 4 SER E 126 LEU E 130 0 SHEET 2 AB8 4 THR E 141 TYR E 151 -1 O LEU E 147 N PHE E 128 SHEET 3 AB8 4 TYR E 182 PRO E 191 -1 O TYR E 182 N TYR E 151 SHEET 4 AB8 4 VAL E 169 THR E 171 -1 N HIS E 170 O VAL E 187 SHEET 1 AB9 4 SER E 126 LEU E 130 0 SHEET 2 AB9 4 THR E 141 TYR E 151 -1 O LEU E 147 N PHE E 128 SHEET 3 AB9 4 TYR E 182 PRO E 191 -1 O TYR E 182 N TYR E 151 SHEET 4 AB9 4 VAL E 175 LEU E 176 -1 N VAL E 175 O SER E 183 SHEET 1 AC1 3 THR E 157 TRP E 160 0 SHEET 2 AC1 3 TYR E 200 HIS E 206 -1 O ASN E 203 N SER E 159 SHEET 3 AC1 3 THR E 211 VAL E 217 -1 O VAL E 213 N VAL E 204 SHEET 1 AC2 4 MET F 4 SER F 7 0 SHEET 2 AC2 4 ALA F 19 SER F 25 -1 O LYS F 24 N THR F 5 SHEET 3 AC2 4 ASP F 76 ILE F 81 -1 O LEU F 79 N ILE F 21 SHEET 4 AC2 4 PHE F 68 SER F 73 -1 N SER F 69 O THR F 80 SHEET 1 AC3 6 SER F 10 SER F 14 0 SHEET 2 AC3 6 THR F 108 LYS F 113 1 O GLU F 111 N LEU F 11 SHEET 3 AC3 6 VAL F 91 ASN F 96 -1 N TYR F 92 O THR F 108 SHEET 4 AC3 6 LEU F 39 GLN F 44 -1 N GLN F 44 O VAL F 91 SHEET 5 AC3 6 LYS F 51 TYR F 55 -1 O LEU F 53 N TRP F 41 SHEET 6 AC3 6 THR F 59 ARG F 60 -1 O THR F 59 N TYR F 55 SHEET 1 AC4 2 LEU F 30 ASN F 31 0 SHEET 2 AC4 2 LYS F 36 ASN F 37 -1 O LYS F 36 N ASN F 31 SHEET 1 AC5 4 SER F 120 PHE F 124 0 SHEET 2 AC5 4 THR F 135 PHE F 145 -1 O LEU F 141 N PHE F 122 SHEET 3 AC5 4 TYR F 179 SER F 188 -1 O SER F 183 N CYS F 140 SHEET 4 AC5 4 SER F 165 GLN F 166 -1 N GLN F 166 O THR F 184 SHEET 1 AC6 4 ALA F 159 LEU F 160 0 SHEET 2 AC6 4 ALA F 150 VAL F 156 -1 N VAL F 156 O ALA F 159 SHEET 3 AC6 4 VAL F 197 HIS F 204 -1 O GLU F 201 N GLN F 153 SHEET 4 AC6 4 VAL F 211 ASN F 216 -1 O VAL F 211 N VAL F 202 SSBOND 1 CYS A 44 CYS B 86 1555 1555 2.05 SSBOND 2 CYS A 86 CYS B 44 1555 1555 2.06 SSBOND 3 CYS C 22 CYS C 95 1555 1555 2.09 SSBOND 4 CYS C 146 CYS C 202 1555 1555 2.07 SSBOND 5 CYS D 23 CYS D 94 1555 1555 2.10 SSBOND 6 CYS D 140 CYS D 200 1555 1555 2.02 SSBOND 7 CYS E 22 CYS E 95 1555 1555 2.05 SSBOND 8 CYS E 146 CYS E 202 1555 1555 2.03 SSBOND 9 CYS F 23 CYS F 94 1555 1555 2.05 SSBOND 10 CYS F 140 CYS F 200 1555 1555 2.04 LINK ND2 ASN B 28 C1 NAG J 1 1555 1555 1.43 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.39 LINK O6 NAG J 1 C1 FUC J 6 1555 1555 1.40 LINK O4 NAG J 2 C1 MAN J 3 1555 1555 1.41 LINK O3 MAN J 3 C1 MAN J 4 1555 1555 1.40 LINK O6 MAN J 3 C1 MAN J 5 1555 1555 1.40 CISPEP 1 PHE C 152 PRO C 153 0 -11.04 CISPEP 2 GLU C 154 PRO C 155 0 1.18 CISPEP 3 SER D 7 PRO D 8 0 -0.32 CISPEP 4 PHE D 100 PRO D 101 0 -10.09 CISPEP 5 TYR D 146 PRO D 147 0 0.59 CISPEP 6 PHE E 152 PRO E 153 0 -2.93 CISPEP 7 GLU E 154 PRO E 155 0 5.97 CISPEP 8 SER F 7 PRO F 8 0 -0.77 CISPEP 9 PHE F 100 PRO F 101 0 -8.84 CISPEP 10 TYR F 146 PRO F 147 0 3.02 CRYST1 86.684 65.870 193.754 90.00 96.62 90.00 P 1 21 1 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 0.011536 0.000000 0.001339 0.00000 SCALE2 0.000000 0.015181 0.000000 0.00000 SCALE3 0.000000 0.000000 0.005196 0.00000