HEADER IMMUNE SYSTEM 10-JUN-24 9C7D TITLE HUMAN MONOCLONAL ANTIBODY MAD22-38 BOUND TO THE N-TERMINUS OF CLEAVED TITLE 2 CIRCUMSPOROZOITE PROTEIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: MONOCLONAL ANTIBODY MAD22-38 FAB HEAVY CHAIN; COMPND 3 CHAIN: H; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: MONOCLONAL ANTIBODY MAD22-38 FAB LIGHT CHAIN; COMPND 7 CHAIN: L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: CIRCUMSPOROZOITE PROTEIN; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: CS,PFCSP; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 6 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 15 MOL_ID: 3; SOURCE 16 SYNTHETIC: YES; SOURCE 17 ORGANISM_SCIENTIFIC: PLASMODIUM FALCIPARUM 3D7; SOURCE 18 ORGANISM_TAXID: 36329 KEYWDS ANTIBODY, MALARIA, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR R.MOSKOVITZ,I.A.WILSON REVDAT 1 25-DEC-24 9C7D 0 JRNL AUTH C.DACON,R.MOSKOVITZ,K.SWEARINGEN,L.DA SILVA PEREIRA, JRNL AUTH 2 Y.FLORES-GARCIA,M.ALESHNICK,S.KANATANI,B.FLYNN, JRNL AUTH 3 A.MOLINA-CRUZ,K.WOLLENBERG,M.TRAVER,P.KIRTLEY,L.PURSER, JRNL AUTH 4 M.DILLON,B.BONILLA,A.FRANCO,S.PETROS,J.KRITZBERG,C.TUCKER, JRNL AUTH 5 G.G.PAEZ,P.GUPTA,M.J.SHEARS,J.PAZZI,J.M.EDGAR,A.A.TENG, JRNL AUTH 6 A.BELMONTE,K.ODA,S.DOUMBO,L.KRYMSKAYA,J.SKINNER,S.LI, JRNL AUTH 7 S.GHOSAL,K.KAYENTAO,A.ONGOIBA,A.VAUGHAN,J.J.CAMPO,B.TRAORE, JRNL AUTH 8 C.BARILLAS-MURY,W.WIJAYALATH,A.IDRIS,P.D.CROMPTON,P.SINNIS, JRNL AUTH 9 B.K.WILDER,F.ZAVALA,R.A.SEDER,I.A.WILSON,J.TAN JRNL TITL PROTECTIVE ANTIBODIES TARGET CRYPTIC EPITOPE UNMASKED BY JRNL TITL 2 CLEAVAGE OF MALARIA SPOROZOITE PROTEIN JRNL REF SCIENCE 2024 JRNL REFN ESSN 1095-9203 JRNL DOI 10.1126/SCIENCE.ADR0510 REMARK 2 REMARK 2 RESOLUTION. 1.99 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21RC1_5127 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.99 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 44.40 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 3 NUMBER OF REFLECTIONS : 34294 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.186 REMARK 3 R VALUE (WORKING SET) : 0.184 REMARK 3 FREE R VALUE : 0.232 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.040 REMARK 3 FREE R VALUE TEST SET COUNT : 1729 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 44.4000 - 4.5600 0.97 2861 168 0.1530 0.1760 REMARK 3 2 4.5600 - 3.6200 0.99 2802 125 0.1440 0.1800 REMARK 3 3 3.6200 - 3.1600 0.97 2716 145 0.1707 0.2112 REMARK 3 4 3.1600 - 2.8700 0.99 2710 158 0.1969 0.2837 REMARK 3 5 2.8700 - 2.6700 0.98 2737 135 0.2064 0.2604 REMARK 3 6 2.6700 - 2.5100 0.97 2665 153 0.2151 0.2886 REMARK 3 7 2.5100 - 2.3800 0.96 2603 159 0.2204 0.3020 REMARK 3 8 2.3800 - 2.2800 0.98 2750 115 0.2172 0.2546 REMARK 3 9 2.2800 - 2.1900 0.99 2687 143 0.2105 0.2483 REMARK 3 10 2.1900 - 2.1200 0.99 2722 126 0.2207 0.2677 REMARK 3 11 2.1200 - 2.0500 0.99 2678 149 0.2368 0.3039 REMARK 3 12 2.0500 - 1.9900 0.97 2634 153 0.2770 0.3358 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.265 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.217 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 29.40 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 31.89 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.014 3547 REMARK 3 ANGLE : 1.357 4839 REMARK 3 CHIRALITY : 0.076 564 REMARK 3 PLANARITY : 0.010 603 REMARK 3 DIHEDRAL : 16.977 1234 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 9C7D COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-JUN-24. REMARK 100 THE DEPOSITION ID IS D_1000284961. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 18-NOV-23 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 8 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : NSLS-II REMARK 200 BEAMLINE : 17-ID-2 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97934 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER2 XE 16M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : DENZO REMARK 200 DATA SCALING SOFTWARE : SCALEPACK REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 34343 REMARK 200 RESOLUTION RANGE HIGH (A) : 1.990 REMARK 200 RESOLUTION RANGE LOW (A) : 44.400 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.9 REMARK 200 DATA REDUNDANCY : 6.600 REMARK 200 R MERGE (I) : 0.16000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 6.4400 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.99 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 2.03 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : 1.62500 REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 2.400 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 (%): 51.48 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG 3350, 0.2 M AMMONIUM CHLORIDE, REMARK 280 PH 8, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 277K 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 36.90150 REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 44.39850 REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 38.17750 REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 44.39850 REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 36.90150 REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 38.17750 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: TRIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 TOTAL BURIED SURFACE AREA: 5720 ANGSTROM**2 REMARK 350 SURFACE AREA OF THE COMPLEX: 19820 ANGSTROM**2 REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -7.0 KCAL/MOL REMARK 350 APPLY THE FOLLOWING TO CHAINS: H, L, B, A 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 SER H 215 REMARK 465 CYS H 216 REMARK 465 CYS L 213 REMARK 465 PRO B 104 REMARK 465 ASN B 105 REMARK 465 ALA B 106 REMARK 465 ASN B 107 REMARK 465 PRO B 108 REMARK 465 ASN B 109 REMARK 465 VAL B 110 REMARK 465 ASP B 111 REMARK 465 PRO B 112 REMARK 465 ASN B 113 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 ALA H 15 -2.21 69.61 REMARK 500 SER H 127 -158.39 -170.75 REMARK 500 ASP H 144 60.09 64.95 REMARK 500 SER L 30 -128.78 51.57 REMARK 500 ALA L 51 -41.50 73.80 REMARK 500 SER L 78 72.25 47.52 REMARK 500 LYS L 127 -14.49 -49.31 REMARK 500 ASN L 139 63.56 64.65 REMARK 500 ASN L 153 2.36 57.90 REMARK 500 REMARK 500 REMARK: NULL DBREF 9C7D H 1 216 PDB 9C7D 9C7D 1 216 DBREF 9C7D L 1 213 PDB 9C7D 9C7D 1 213 DBREF 9C7D B 96 113 UNP Q7K740 CSP_PLAF7 96 113 SEQRES 1 H 227 GLN LEU GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 H 227 PRO ALA GLU THR LEU SER LEU THR CYS THR VAL SER GLY SEQRES 3 H 227 GLY SER ILE SER SER SER SER TYR TYR TRP GLY TRP ILE SEQRES 4 H 227 ARG GLN PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY SER SEQRES 5 H 227 ILE TYR TYR THR GLY SER THR TYR TYR ASN PRO SER LEU SEQRES 6 H 227 LYS SER ARG VAL THR ILE SER VAL ASP THR SER LYS ASN SEQRES 7 H 227 GLN PHE SER LEU LYS LEU ARG SER VAL THR ALA ALA ASP SEQRES 8 H 227 THR ALA VAL TYR TYR CYS ALA SER ILE GLY TRP ALA VAL SEQRES 9 H 227 PRO GLY LYS ARG TYR TYR PHE ASP TYR TRP GLY GLN GLY SEQRES 10 H 227 THR LEU VAL THR VAL SER SER ALA SER THR LYS GLY PRO SEQRES 11 H 227 SER VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER SEQRES 12 H 227 GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR SEQRES 13 H 227 PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA SEQRES 14 H 227 LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SEQRES 15 H 227 SER SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL SEQRES 16 H 227 PRO SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN SEQRES 17 H 227 VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS SEQRES 18 H 227 VAL GLU PRO LYS SER CYS SEQRES 1 L 213 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 213 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA ASN SEQRES 3 L 213 HIS SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 213 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 213 SER LEU GLN SER GLY VAL PRO SER PHE ARG PHE SER GLY SEQRES 6 L 213 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 7 L 213 LEU GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SEQRES 8 L 213 SER TYR TYR THR PRO TRP THR PHE GLY PRO GLY THR LYS SEQRES 9 L 213 VAL ASP ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 213 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 213 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 213 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 213 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 213 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 213 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 213 GLU VAL THR GLN GLY THR THR SER VAL THR LYS SER PHE SEQRES 17 L 213 ASN ARG GLY GLU CYS SEQRES 1 B 18 PCA PRO ALA ASP GLY ASN PRO ASP PRO ASN ALA ASN PRO SEQRES 2 B 18 ASN VAL ASP PRO ASN MODRES 9C7D PCA B 96 GLN MODIFIED RESIDUE HET PCA B 96 8 HET NAG A 1 14 HET NAG A 2 14 HET BMA A 3 11 HET MAN A 4 11 HET MAN A 5 11 HET FUC A 6 10 HETNAM PCA PYROGLUTAMIC ACID HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM FUC ALPHA-L-FUCOPYRANOSE HETSYN NAG N-ACETYL-BETA-D-GLUCOSAMINE; 2-ACETAMIDO-2-DEOXY-BETA- HETSYN 2 NAG D-GLUCOSE; 2-ACETAMIDO-2-DEOXY-D-GLUCOSE; 2-ACETAMIDO- HETSYN 3 NAG 2-DEOXY-GLUCOSE; N-ACETYL-D-GLUCOSAMINE HETSYN BMA BETA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN MAN ALPHA-D-MANNOSE; D-MANNOSE; MANNOSE HETSYN FUC ALPHA-L-FUCOSE; 6-DEOXY-ALPHA-L-GALACTOPYRANOSE; L- HETSYN 2 FUC FUCOSE; FUCOSE FORMUL 3 PCA C5 H7 N O3 FORMUL 4 NAG 2(C8 H15 N O6) FORMUL 4 BMA C6 H12 O6 FORMUL 4 MAN 2(C6 H12 O6) FORMUL 4 FUC C6 H12 O5 FORMUL 5 HOH *253(H2 O) HELIX 1 AA1 THR H 73 LYS H 75 5 3 HELIX 2 AA2 THR H 83 THR H 87 5 5 HELIX 3 AA3 SER H 127 LYS H 129 5 3 HELIX 4 AA4 SER H 156 ALA H 158 5 3 HELIX 5 AA5 SER H 187 LEU H 189 5 3 HELIX 6 AA6 LYS H 201 ASN H 204 5 4 HELIX 7 AA7 GLN L 80 PHE L 84 5 5 HELIX 8 AA8 SER L 122 LYS L 127 1 6 HELIX 9 AA9 LYS L 184 LYS L 189 1 6 SHEET 1 AA1 4 GLN H 3 GLU H 6 0 SHEET 2 AA1 4 LEU H 18 SER H 25 -1 O THR H 23 N GLN H 5 SHEET 3 AA1 4 GLN H 77 LEU H 82 -1 O PHE H 78 N CYS H 22 SHEET 4 AA1 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA2 6 GLY H 10 VAL H 12 0 SHEET 2 AA2 6 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA2 6 ALA H 88 ALA H 98 -1 N ALA H 88 O VAL H 109 SHEET 4 AA2 6 TYR H 35 GLN H 39 -1 N ILE H 37 O TYR H 91 SHEET 5 AA2 6 GLU H 46 ILE H 51 -1 O ILE H 48 N TRP H 36 SHEET 6 AA2 6 THR H 57 TYR H 59 -1 O TYR H 58 N SER H 50 SHEET 1 AA3 4 GLY H 10 VAL H 12 0 SHEET 2 AA3 4 THR H 107 VAL H 111 1 O THR H 110 N VAL H 12 SHEET 3 AA3 4 ALA H 88 ALA H 98 -1 N ALA H 88 O VAL H 109 SHEET 4 AA3 4 ARG H 100C TRP H 103 -1 O TYR H 102 N SER H 94 SHEET 1 AA4 4 SER H 120 LEU H 124 0 SHEET 2 AA4 4 THR H 135 TYR H 145 -1 O LEU H 141 N PHE H 122 SHEET 3 AA4 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA4 4 VAL H 163 THR H 165 -1 N HIS H 164 O VAL H 181 SHEET 1 AA5 4 THR H 131 SER H 132 0 SHEET 2 AA5 4 THR H 135 TYR H 145 -1 O THR H 135 N SER H 132 SHEET 3 AA5 4 TYR H 176 PRO H 185 -1 O VAL H 184 N ALA H 136 SHEET 4 AA5 4 VAL H 169 LEU H 170 -1 N VAL H 169 O SER H 177 SHEET 1 AA6 3 THR H 151 TRP H 154 0 SHEET 2 AA6 3 ILE H 195 HIS H 200 -1 O ASN H 197 N SER H 153 SHEET 3 AA6 3 THR H 205 LYS H 210 -1 O VAL H 207 N VAL H 198 SHEET 1 AA7 4 MET L 4 SER L 7 0 SHEET 2 AA7 4 VAL L 19 ALA L 25 -1 O THR L 22 N SER L 7 SHEET 3 AA7 4 ASP L 71 ILE L 76 -1 O ILE L 76 N VAL L 19 SHEET 4 AA7 4 PHE L 63 SER L 68 -1 N SER L 64 O THR L 75 SHEET 1 AA8 6 SER L 10 SER L 14 0 SHEET 2 AA8 6 THR L 103 LYS L 108 1 O ASP L 106 N LEU L 11 SHEET 3 AA8 6 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 105 SHEET 4 AA8 6 LEU L 33 GLN L 38 -1 N GLN L 38 O THR L 86 SHEET 5 AA8 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AA8 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AA9 4 SER L 10 SER L 14 0 SHEET 2 AA9 4 THR L 103 LYS L 108 1 O ASP L 106 N LEU L 11 SHEET 3 AA9 4 ALA L 85 GLN L 91 -1 N ALA L 85 O VAL L 105 SHEET 4 AA9 4 THR L 98 PHE L 99 -1 O THR L 98 N GLN L 91 SHEET 1 AB1 4 SER L 115 PHE L 119 0 SHEET 2 AB1 4 THR L 130 PHE L 140 -1 O ASN L 138 N SER L 115 SHEET 3 AB1 4 TYR L 174 SER L 183 -1 O LEU L 176 N LEU L 137 SHEET 4 AB1 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AB2 4 ALA L 154 LEU L 155 0 SHEET 2 AB2 4 LYS L 146 VAL L 151 -1 N VAL L 151 O ALA L 154 SHEET 3 AB2 4 VAL L 192 GLN L 199 -1 O GLU L 196 N GLN L 148 SHEET 4 AB2 4 THR L 202 ASN L 209 -1 O VAL L 204 N VAL L 197 SSBOND 1 CYS H 22 CYS H 92 1555 1555 2.18 SSBOND 2 CYS H 140 CYS H 196 1555 1555 2.12 SSBOND 3 CYS L 23 CYS L 89 1555 1555 2.15 SSBOND 4 CYS L 135 CYS L 195 1555 1555 2.07 LINK ND2 ASN L 26 C1 NAG A 1 1555 1555 1.44 LINK C PCA B 96 N PRO B 97 1555 1555 1.34 LINK O4 NAG A 1 C1 NAG A 2 1555 1555 1.42 LINK O6 NAG A 1 C1 FUC A 6 1555 1555 1.44 LINK O4 NAG A 2 C1 BMA A 3 1555 1555 1.43 LINK O3 BMA A 3 C1 MAN A 4 1555 1555 1.45 LINK O6 BMA A 3 C1 MAN A 5 1555 1555 1.46 CISPEP 1 VAL H 99 PRO H 100 0 -9.10 CISPEP 2 PHE H 146 PRO H 147 0 -13.40 CISPEP 3 GLU H 148 PRO H 149 0 0.57 CISPEP 4 SER L 7 PRO L 8 0 -5.57 CISPEP 5 THR L 95 PRO L 96 0 2.93 CISPEP 6 TYR L 141 PRO L 142 0 0.05 CRYST1 73.803 76.355 88.797 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 0.013550 0.000000 0.000000 0.00000 SCALE2 0.000000 0.013097 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011262 0.00000