HEADER HYDROLASE 06-SEP-23 8QGX TITLE COMPLEX BETWEEN HUMAN NEUTROPHIL ELASTASE WITH NANOBODY NBE201 COMPND MOL_ID: 1; COMPND 2 MOLECULE: NEUTROPHIL ELASTASE; COMPND 3 CHAIN: A; COMPND 4 MOL_ID: 2; COMPND 5 MOLECULE: NBE201; COMPND 6 CHAIN: B; COMPND 7 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 TISSUE: SPUTUM; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 8 ORGANISM_TAXID: 9844; SOURCE 9 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 11 EXPRESSION_SYSTEM_STRAIN: WK6; SOURCE 12 EXPRESSION_SYSTEM_PLASMID: PHEN6 KEYWDS NANOBODY, ELASTASE, INHIBITOR, SERINE PROTEASE, HYDROLASE EXPDTA X-RAY DIFFRACTION AUTHOR F.MORALES-YANEZ,P.REDEGHIERI,J.MORAY,M.DUMOULIN,F.KERFF REVDAT 1 25-DEC-24 8QGX 0 JRNL AUTH P.REDEGHIERI,J.MORAY,F.KERFF,S.GOHY,T.LEAL,S.MUYLDERMANS, JRNL AUTH 2 R.VANBEVER,F.J.MORALES-YANEZ,M.DUMOULIN JRNL TITL ENZYMATIC, STRUCTURAL, AND BIOPHYSICAL CHARACTERIZATION OF A JRNL TITL 2 SINGLE-DOMAIN ANTIBODY (VHH) SELECTIVELY AND TIGHTLY JRNL TITL 3 INHIBITING NEUTROPHIL ELASTASE AND EXHIBITING FAVORABLE JRNL TITL 4 DEVELOPABILITY PROPERTIES. JRNL REF PROTEIN SCI. V. 33 E5227 2024 JRNL REFN ESSN 1469-896X JRNL PMID 39604162 JRNL DOI 10.1002/PRO.5227 REMARK 2 REMARK 2 RESOLUTION. 2.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : BUSTER 2.10.3 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) : 2.30 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.54 REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 18530 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) : 0.226 REMARK 3 R VALUE (WORKING SET) : 0.224 REMARK 3 FREE R VALUE : 0.271 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000 REMARK 3 FREE R VALUE TEST SET COUNT : 927 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 : 9 REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30 REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 2.44 REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 99.70 REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2962 REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2628 REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2814 REMARK 3 BIN R VALUE (WORKING SET) : 0.2596 REMARK 3 BIN FREE R VALUE : 0.3270 REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 5.00 REMARK 3 BIN FREE R VALUE TEST SET COUNT : 148 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 : 2566 REMARK 3 NUCLEIC ACID ATOMS : 0 REMARK 3 HETEROGEN ATOMS : 81 REMARK 3 SOLVENT ATOMS : 18 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : 84.99 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : -3.93530 REMARK 3 B22 (A**2) : -6.96550 REMARK 3 B33 (A**2) : 10.90080 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 COORDINATE ERROR. REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.430 REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : 0.297 REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.233 REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL 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 : 0.944 REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.908 REMARK 3 REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15 REMARK 3 TERM COUNT WEIGHT FUNCTION. REMARK 3 BOND LENGTHS : 5310 ; 2.000 ; HARMONIC REMARK 3 BOND ANGLES : 9557 ; 2.000 ; HARMONIC REMARK 3 TORSION ANGLES : 1177 ; 2.000 ; SINUSOIDAL REMARK 3 TRIGONAL CARBON PLANES : NULL ; NULL ; NULL REMARK 3 GENERAL PLANES : 863 ; 5.000 ; HARMONIC REMARK 3 ISOTROPIC THERMAL FACTORS : 5310 ; 20.000 ; 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 : 361 ; 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 : 5798 ; 4.000 ; SEMIHARMONIC REMARK 3 REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES. REMARK 3 BOND LENGTHS (A) : 0.010 REMARK 3 BOND ANGLES (DEGREES) : 1.13 REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.62 REMARK 3 OTHER TORSION ANGLES (DEGREES) : 15.78 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : 2 REMARK 3 REMARK 3 TLS GROUP : 1 REMARK 3 SELECTION: { A|* } REMARK 3 ORIGIN FOR THE GROUP (A): -8.8646 1.6342 -22.8571 REMARK 3 T TENSOR REMARK 3 T11: 0.8629 T22: -0.0483 REMARK 3 T33: -0.2527 T12: 0.0570 REMARK 3 T13: 0.0203 T23: -0.0156 REMARK 3 L TENSOR REMARK 3 L11: 0.6400 L22: 0.5784 REMARK 3 L33: 1.9687 L12: 0.7313 REMARK 3 L13: -0.1422 L23: 0.3032 REMARK 3 S TENSOR REMARK 3 S11: -0.0815 S12: 0.0234 S13: 0.0856 REMARK 3 S21: -0.1403 S22: 0.1240 S23: -0.0701 REMARK 3 S31: 0.3398 S32: 0.1194 S33: -0.0425 REMARK 3 REMARK 3 TLS GROUP : 2 REMARK 3 SELECTION: { B|* } REMARK 3 ORIGIN FOR THE GROUP (A): -25.4811 23.7002 -10.4758 REMARK 3 T TENSOR REMARK 3 T11: 0.9119 T22: -0.0502 REMARK 3 T33: -0.2506 T12: 0.0629 REMARK 3 T13: 0.0041 T23: 0.0008 REMARK 3 L TENSOR REMARK 3 L11: 0.2174 L22: 0.8913 REMARK 3 L33: 0.2859 L12: -1.0813 REMARK 3 L13: -0.7068 L23: 1.9198 REMARK 3 S TENSOR REMARK 3 S11: -0.0473 S12: -0.1233 S13: 0.0193 REMARK 3 S21: -0.0308 S22: 0.0516 S23: -0.0275 REMARK 3 S31: 0.0225 S32: -0.1344 S33: -0.0043 REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8QGX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 06-SEP-23. REMARK 100 THE DEPOSITION ID IS D_1292133210. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 12-FEB-22 REMARK 200 TEMPERATURE (KELVIN) : 293 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SOLEIL REMARK 200 BEAMLINE : PROXIMA 1 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.9786 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XDS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18530 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.300 REMARK 200 RESOLUTION RANGE LOW (A) : 48.540 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.7 REMARK 200 DATA REDUNDANCY : 13.20 REMARK 200 R MERGE (I) : 0.12800 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 11.6000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.42 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.91400 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 (%): 53.99 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.67 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: THE CRYSTALS WERE GROWN AT 20OC USING REMARK 280 THE SITTING DROP VAPOR DIFFUSION METHOD. THE DROP CONTAINED 0.2 REMARK 280 UL OF HNE IN COMPLEX WITH NBE201 AT A CONCENTRATION OF 15 MG/ML REMARK 280 AND 0.2 UL OF 0.1M HEPES PH7 BUFFER WITH 10 PER CENT (V/V) REMARK 280 POLYETHYLENE GLYCOL 5000 MONOMETHYL ETHER AND 5 PER CENT (V/V) REMARK 280 TACSIMATE. THE CRYSTALS WERE TRANSFERRED TO A CRYOPROTECTANT REMARK 280 SOLUTION CONTAINING 33 PER CENT (V/V) POLYETHYLENE GLYCOL 6000 REMARK 280 AND 33 PER CENT (V/V) GLYCEROL BEFORE BEING FROZEN IN LIQUID REMARK 280 NITROGEN., VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X+1/2,-Y,Z+1/2 REMARK 290 3555 -X,Y+1/2,-Z+1/2 REMARK 290 4555 X+1/2,-Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 32.49000 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 42.46000 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 36.50000 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 42.46000 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 32.49000 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 36.50000 REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL REMARK 300 REMARK 300 BIOMOLECULE: 1 REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON REMARK 300 BURIED SURFACE AREA. REMARK 350 REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS REMARK 350 GIVEN BELOW. BOTH NON-CRYSTALLOGRAPHIC AND REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN. REMARK 350 REMARK 350 BIOMOLECULE: 1 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 3850 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 14860 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 8.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D REMARK 350 BIOMT1 1 1.000000 0.000000 0.000000 0.00000 REMARK 350 BIOMT2 1 0.000000 1.000000 0.000000 0.00000 REMARK 350 BIOMT3 1 0.000000 0.000000 1.000000 0.00000 REMARK 465 REMARK 465 MISSING RESIDUES REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 465 REMARK 465 M RES C SSSEQI REMARK 465 ARG A 147 REMARK 465 ASN A 148 REMARK 465 HIS B 124 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 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 HIS A 71 -65.24 -134.68 REMARK 500 ASN B 77 40.82 22.09 REMARK 500 REMARK 500 REMARK: NULL DBREF 8QGX A 16 243 UNP P08246 ELNE_HUMAN 30 247 DBREF 8QGX B 1 129 PDB 8QGX 8QGX 1 129 SEQRES 1 A 218 ILE VAL GLY GLY ARG ARG ALA ARG PRO HIS ALA TRP PRO SEQRES 2 A 218 PHE MET VAL SER LEU GLN LEU ARG GLY GLY HIS PHE CYS SEQRES 3 A 218 GLY ALA THR LEU ILE ALA PRO ASN PHE VAL MET SER ALA SEQRES 4 A 218 ALA HIS CYS VAL ALA ASN VAL ASN VAL ARG ALA VAL ARG SEQRES 5 A 218 VAL VAL LEU GLY ALA HIS ASN LEU SER ARG ARG GLU PRO SEQRES 6 A 218 THR ARG GLN VAL PHE ALA VAL GLN ARG ILE PHE GLU ASN SEQRES 7 A 218 GLY TYR ASP PRO VAL ASN LEU LEU ASN ASP ILE VAL ILE SEQRES 8 A 218 LEU GLN LEU ASN GLY SER ALA THR ILE ASN ALA ASN VAL SEQRES 9 A 218 GLN VAL ALA GLN LEU PRO ALA GLN GLY ARG ARG LEU GLY SEQRES 10 A 218 ASN GLY VAL GLN CYS LEU ALA MET GLY TRP GLY LEU LEU SEQRES 11 A 218 GLY ARG ASN ARG GLY ILE ALA SER VAL LEU GLN GLU LEU SEQRES 12 A 218 ASN VAL THR VAL VAL THR SER LEU CYS ARG ARG SER ASN SEQRES 13 A 218 VAL CYS THR LEU VAL ARG GLY ARG GLN ALA GLY VAL CYS SEQRES 14 A 218 PHE GLY ASP SER GLY SER PRO LEU VAL CYS ASN GLY LEU SEQRES 15 A 218 ILE HIS GLY ILE ALA SER PHE VAL ARG GLY GLY CYS ALA SEQRES 16 A 218 SER GLY LEU TYR PRO ASP ALA PHE ALA PRO VAL ALA GLN SEQRES 17 A 218 PHE VAL ASN TRP ILE ASP SER ILE ILE GLN SEQRES 1 B 129 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 129 ALA GLY GLY SER LEU ARG LEU SER CYS VAL VAL PRO GLY SEQRES 3 B 129 ARG THR ILE SER LEU TYR ARG MET GLY TRP PHE ARG GLN SEQRES 4 B 129 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA GLY ILE ASN SEQRES 5 B 129 TRP SER GLY ASP MET THR ASP TYR VAL ASP SER VAL LYS SEQRES 6 B 129 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 B 129 VAL TYR LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 B 129 ALA ILE TYR TYR CYS THR ALA ASP PRO LYS LEU LEU PRO SEQRES 9 B 129 LEU ALA ASP SER SER TYR GLY TYR TRP GLY GLN GLY THR SEQRES 10 B 129 GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS HET NAG C 1 28 HET NAG C 2 28 HET FUC C 3 21 HET NAG D 1 28 HET NAG D 2 28 HET FUC D 3 21 HET PO4 A 301 5 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETNAM PO4 PHOSPHATE ION HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 3 NAG 4(C8 H15 N O6) FORMUL 3 FUC 2(C6 H12 O5) FORMUL 5 PO4 O4 P 3- FORMUL 6 HOH *18(H2 O) HELIX 1 AA1 ALA A 55 VAL A 59 5 5 HELIX 2 AA2 ASN A 62A VAL A 65 5 5 HELIX 3 AA3 PHE A 234 GLN A 243 1 10 HELIX 4 AA4 ASN B 74 LYS B 76 5 3 HELIX 5 AA5 LYS B 87 THR B 91 5 5 SHEET 1 AA1 8 ARG A 20 ARG A 21 0 SHEET 2 AA1 8 GLN A 156 VAL A 164 -1 O GLU A 157 N ARG A 20 SHEET 3 AA1 8 VAL A 181 LEU A 184 -1 O LEU A 184 N THR A 162 SHEET 4 AA1 8 ASP A 226 PRO A 230 -1 O PHE A 228 N VAL A 181 SHEET 5 AA1 8 LEU A 208 PHE A 215 -1 N ILE A 212 O ALA A 229 SHEET 6 AA1 8 PRO A 198 CYS A 201 -1 N CYS A 201 O LEU A 208 SHEET 7 AA1 8 GLN A 135 GLY A 140 -1 N LEU A 137 O VAL A 200 SHEET 8 AA1 8 GLN A 156 VAL A 164 -1 O LEU A 158 N ALA A 138 SHEET 1 AA2 7 GLN A 81 PHE A 83 0 SHEET 2 AA2 7 ARG A 65A LEU A 68 -1 N LEU A 68 O GLN A 81 SHEET 3 AA2 7 MET A 30 LEU A 35 -1 N SER A 32 O VAL A 67 SHEET 4 AA2 7 GLY A 39 ALA A 48 -1 O CYS A 42 N LEU A 33 SHEET 5 AA2 7 PHE A 51 SER A 54 -1 O MET A 53 N THR A 45 SHEET 6 AA2 7 VAL A 104 LEU A 108 -1 O LEU A 106 N VAL A 52 SHEET 7 AA2 7 VAL A 85 GLU A 90 -1 N GLN A 86 O GLN A 107 SHEET 1 AA3 4 GLN B 5 SER B 7 0 SHEET 2 AA3 4 LEU B 18 VAL B 23 -1 O SER B 21 N SER B 7 SHEET 3 AA3 4 THR B 78 MET B 83 -1 O MET B 83 N LEU B 18 SHEET 4 AA3 4 PHE B 68 ASP B 73 -1 N THR B 69 O GLU B 82 SHEET 1 AA4 6 GLY B 10 VAL B 12 0 SHEET 2 AA4 6 THR B 117 VAL B 121 1 O GLN B 118 N GLY B 10 SHEET 3 AA4 6 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 117 SHEET 4 AA4 6 ARG B 33 GLN B 39 -1 N GLY B 35 O THR B 97 SHEET 5 AA4 6 GLU B 46 ILE B 51 -1 O ALA B 49 N TRP B 36 SHEET 6 AA4 6 THR B 58 TYR B 60 -1 O ASP B 59 N GLY B 50 SHEET 1 AA5 4 GLY B 10 VAL B 12 0 SHEET 2 AA5 4 THR B 117 VAL B 121 1 O GLN B 118 N GLY B 10 SHEET 3 AA5 4 ALA B 92 ASP B 99 -1 N TYR B 94 O THR B 117 SHEET 4 AA5 4 TYR B 112 TRP B 113 -1 O TYR B 112 N ALA B 98 SSBOND 1 CYS A 42 CYS A 58 1555 1555 2.04 SSBOND 2 CYS A 136 CYS A 201 1555 1555 2.06 SSBOND 3 CYS A 168 CYS A 182 1555 1555 2.03 SSBOND 4 CYS A 191 CYS A 220 1555 1555 2.04 SSBOND 5 CYS B 22 CYS B 96 1555 1555 2.02 LINK ND2 ASN A 109 C1 NAG C 1 1555 1555 1.44 LINK ND2 ASN A 159 C1 NAG D 1 1555 1555 1.44 LINK O4 NAG C 1 C1 NAG C 2 1555 1555 1.42 LINK O6 NAG C 1 C1 FUC C 3 1555 1555 1.40 LINK O4 NAG D 1 C1 NAG D 2 1555 1555 1.44 LINK O6 NAG D 1 C1 FUC D 3 1555 1555 1.40 CRYST1 64.980 73.000 84.920 90.00 90.00 90.00 P 21 21 21 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 0.015389 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013699 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011776 0.00000