HEADER SUGAR BINDING PROTEIN 03-JUL-24 9FY8 TITLE L2A5 FAB IN COMPLEX WITH STN-THR COMPND MOL_ID: 1; COMPND 2 MOLECULE: L2A5 FAB HEAVY CHAIN; COMPND 3 CHAIN: B, I; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: L2A5 FAB LIGHT CHAIN; COMPND 7 CHAIN: C, L; COMPND 8 ENGINEERED: YES; COMPND 9 MOL_ID: 3; COMPND 10 MOLECULE: HUMAN ANTI KAPPA VARIABLE HEAVY CHAIN; COMPND 11 CHAIN: D, V; COMPND 12 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_TAXID: 9606; SOURCE 4 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 5 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 6 MOL_ID: 2; SOURCE 7 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 8 ORGANISM_TAXID: 9606; SOURCE 9 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 10 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 11 MOL_ID: 3; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_TAXID: 9606; SOURCE 14 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS ANTIBODY, FAB, IMMUNE SYSTEM, SUGAR BINDING PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR M.E.LAUGIERI,J.ERENO ORBEA,J.JIMENEZ BARBERO,I.OYENARTE REVDAT 1 12-FEB-25 9FY8 0 JRNL AUTH C.O.SOARES,M.E.LAUGIERI,A.S.GROSSO,M.NATALE,H.COELHO, JRNL AUTH 2 S.BEHREN,J.YU,H.CAI,A.FRANCONETTI,I.OYENARTE,M.MAGNASCO, JRNL AUTH 3 A.GIMENO,N.RAMOS,W.CHAI,F.CORZANA,U.WESTERLIND, JRNL AUTH 4 J.JIMENEZ-BARBERO,A.S.PALMA,P.A.VIDEIRA,J.ERENO-ORBEA, JRNL AUTH 5 F.MARCELO JRNL TITL DECODING THE MOLECULAR BASIS OF THE SPECIFICITY OF AN JRNL TITL 2 ANTI-STN ANTIBODY. JRNL REF JACS AU V. 5 225 2025 JRNL REFN ESSN 2691-3704 JRNL PMID 39886580 JRNL DOI 10.1021/JACSAU.4C00921 REMARK 2 REMARK 2 RESOLUTION. 2.62 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX (1.21RC1_5109: ???) 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 : ML REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 2.62 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 53.61 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340 REMARK 3 COMPLETENESS FOR RANGE (%) : 97.4 REMARK 3 NUMBER OF REFLECTIONS : 34080 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.251 REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.306 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.980 REMARK 3 FREE R VALUE TEST SET COUNT : 1696 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 53.6100 - 6.0000 1.00 2811 148 0.2501 0.2717 REMARK 3 2 6.0000 - 4.7600 1.00 2783 141 0.2366 0.2886 REMARK 3 3 4.7600 - 4.1600 1.00 2801 142 0.2130 0.2681 REMARK 3 4 4.1600 - 3.7800 0.87 2439 112 0.2324 0.2956 REMARK 3 5 3.7800 - 3.5100 0.93 2575 132 0.2462 0.3091 REMARK 3 6 3.5100 - 3.3000 0.90 2471 151 0.2543 0.3121 REMARK 3 7 3.3000 - 3.1400 1.00 2751 136 0.2638 0.3267 REMARK 3 8 3.1400 - 3.0000 1.00 2767 164 0.2563 0.3515 REMARK 3 9 3.0000 - 2.8900 1.00 2755 149 0.2603 0.3308 REMARK 3 10 2.8900 - 2.7900 1.00 2710 155 0.2679 0.3222 REMARK 3 11 2.7900 - 2.7000 1.00 2797 125 0.2798 0.3710 REMARK 3 12 2.7000 - 2.6200 0.99 2724 141 0.3053 0.3690 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) : 0.470 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.540 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : NULL REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL 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 : 0.002 NULL REMARK 3 ANGLE : 0.525 NULL REMARK 3 CHIRALITY : 0.039 1283 REMARK 3 PLANARITY : 0.005 1410 REMARK 3 DIHEDRAL : 12.710 2734 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 9FY8 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 04-JUL-24. REMARK 100 THE DEPOSITION ID IS D_1292139592. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 30-JAN-23 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 : I24 REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 0.97951 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 : 34129 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.620 REMARK 200 RESOLUTION RANGE LOW (A) : 97.892 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 97.6 REMARK 200 DATA REDUNDANCY : 5.130 REMARK 200 R MERGE (I) : 0.20000 REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 4.5000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.67 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.08 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : 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 (%): 51.44 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.53 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BISTRIS:HCL, PH6.5, 25% (W/V) PEG REMARK 280 3350, 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 64.07200 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 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: B, C, D, 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 350 REMARK 350 BIOMOLECULE: 2 REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: I, L, V, E 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 400 REMARK 400 COMPOUND REMARK 400 ACTIVATION OF AN ABERRANT GLYCOSYLATION PATHWAY IN CANCER CELLS CAN REMARK 400 LEAD TO EXPRESSION OF THE ONCO-FOETAL SIALYL-TN (STN) ANTIGEN. 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 B 131 REMARK 465 GLY B 132 REMARK 465 LYS B 213 REMARK 465 SER B 214 REMARK 465 CYS B 215 REMARK 465 SER C 39 REMARK 465 GLY C 40 REMARK 465 CYS C 215 REMARK 465 UNK D 1 REMARK 465 UNK D 26 REMARK 465 SER D 119 REMARK 465 SER D 120 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 HIS D 123 REMARK 465 HIS D 124 REMARK 465 HIS D 125 REMARK 465 HIS D 126 REMARK 465 LYS I 129 REMARK 465 SER I 130 REMARK 465 THR I 131 REMARK 465 SER I 132 REMARK 465 LYS I 214 REMARK 465 SER I 215 REMARK 465 CYS I 216 REMARK 465 CYS L 215 REMARK 465 UNK V 1 REMARK 465 SER V 120 REMARK 465 HIS V 121 REMARK 465 HIS V 122 REMARK 465 HIS V 123 REMARK 465 HIS V 124 REMARK 465 HIS V 125 REMARK 465 HIS V 126 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 TYR B 33 155.28 66.25 REMARK 500 MET B 48 -74.11 -95.60 REMARK 500 ARG B 66 22.59 -149.76 REMARK 500 ASP B 143 82.38 64.15 REMARK 500 THR C 50 -49.18 67.88 REMARK 500 ASN C 139 74.88 51.15 REMARK 500 LYS C 170 -60.85 -96.61 REMARK 500 LYS C 191 -52.09 -127.36 REMARK 500 UNK D 51 -167.60 -78.34 REMARK 500 UNK D 54 -15.80 117.89 REMARK 500 UNK D 56 -168.93 60.30 REMARK 500 UNK D 105 52.61 83.86 REMARK 500 SER I 15 -16.11 77.35 REMARK 500 TYR I 33 152.62 68.22 REMARK 500 ARG I 67 17.16 -153.18 REMARK 500 ASN I 77 49.78 74.71 REMARK 500 ASP I 144 75.48 63.70 REMARK 500 THR L 50 -52.30 68.94 REMARK 500 SER L 92 -76.92 -104.35 REMARK 500 ASN L 139 72.34 55.10 REMARK 500 PRO L 142 -169.51 -74.67 REMARK 500 UNK V 53 97.17 -62.65 REMARK 500 UNK V 54 -19.77 136.80 REMARK 500 UNK V 56 -171.13 66.92 REMARK 500 UNK V 105 45.55 89.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 630 REMARK 630 MOLECULE TYPE: OLIGOSACCHARIDE ANTIGEN REMARK 630 MOLECULE NAME: THREONINE REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 630 SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.) REMARK 630 REMARK 630 M RES C SSSEQI REMARK 630 THR B 301 REMARK 630 THR I 301 REMARK 630 SOURCE: NULL REMARK 630 TAXONOMY: NULL REMARK 630 SUBCOMP: NULL REMARK 630 DETAILS: SIALYL-TN (STN) ANTIGEN IS A TRUNCATED O-GLYCAN REMARK 630 CONTAINING A SIALIC ACID ALPHA-2,6 LINKED TO N-ACETYLGALACTOSAMINE REMARK 630 (GALNAC) ALPHA-O-THREONINE OR TO N-ACETYLGALACTOSAMINE (GALNAC) REMARK 630 ALPHA-O-SERINE. REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9FXT RELATED DB: PDB DBREF 9FY8 B 1 215 PDB 9FY8 9FY8 1 215 DBREF 9FY8 C 1 215 PDB 9FY8 9FY8 1 215 DBREF 9FY8 D 1 126 PDB 9FY8 9FY8 1 126 DBREF 9FY8 I 1 216 PDB 9FY8 9FY8 1 216 DBREF 9FY8 L 1 215 PDB 9FY8 9FY8 1 215 DBREF 9FY8 V 1 126 PDB 9FY8 9FY8 1 126 SEQRES 1 B 216 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 B 216 PRO SER GLN SER LEU SER LEU THR CYS SER VAL ILE GLY SEQRES 3 B 216 TYR SER ILE THR SER GLY TYR TYR TRP ASN TRP ILE ARG SEQRES 4 B 216 GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY SER ILE SEQRES 5 B 216 ASN TYR ASP GLY SER ASN ILE TYR ASN PRO SER LEU LYS SEQRES 6 B 216 ASP ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN SEQRES 7 B 216 PHE PHE LEU LYS LEU ASN SER VAL THR THR GLU ASP THR SEQRES 8 B 216 ALA THR TYR TYR CYS ALA ARG GLY GLY ASP TYR TRP GLY SEQRES 9 B 216 GLN GLY THR SER VAL THR VAL SER SER ALA SER THR LYS SEQRES 10 B 216 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 11 B 216 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 B 216 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 B 216 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 B 216 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 B 216 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 B 216 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 B 216 LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 C 215 ASP ILE VAL LEU THR GLN THR PRO ALA ILE MET SER ALA SEQRES 2 C 215 SER PRO GLY GLU LYS VAL THR LEU THR CYS SER ALA SER SEQRES 3 C 215 SER SER VAL SER TYR MET HIS TRP PHE GLN GLN LYS SER SEQRES 4 C 215 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS SEQRES 5 C 215 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 C 215 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 C 215 ALA GLU ASP ALA ALA ALA TYR TYR CYS GLN GLN TRP SER SEQRES 8 C 215 SER ASP PRO PRO MET LEU THR PHE GLY ALA GLY THR LYS SEQRES 9 C 215 LEU GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 C 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 C 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 C 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 C 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 C 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 C 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 C 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 C 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 D 126 UNK VAL GLN LEU UNK UNK SER GLY GLY GLY UNK VAL GLN SEQRES 2 D 126 UNK GLY UNK SER LEU UNK LEU SER CYS UNK ALA UNK UNK SEQRES 3 D 126 UNK UNK UNK UNK UNK UNK UNK UNK TRP UNK ARG GLN UNK SEQRES 4 D 126 PRO GLY UNK UNK ARG GLU UNK VAL UNK UNK UNK UNK UNK SEQRES 5 D 126 UNK UNK UNK UNK UNK UNK UNK UNK ASP SER UNK UNK GLY SEQRES 6 D 126 ARG PHE THR UNK SER UNK ASP UNK UNK UNK UNK UNK UNK SEQRES 7 D 126 UNK LEU GLN UNK UNK UNK LEU UNK UNK UNK ASP UNK ALA SEQRES 8 D 126 UNK TYR TYR CYS UNK UNK UNK UNK UNK UNK UNK UNK UNK SEQRES 9 D 126 UNK UNK UNK UNK UNK TRP GLY UNK GLY THR UNK VAL THR SEQRES 10 D 126 VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 I 216 GLU VAL GLN LEU GLN GLU SER GLY PRO GLY LEU VAL LYS SEQRES 2 I 216 PRO SER GLN SER LEU SER LEU THR CYS SER VAL ILE GLY SEQRES 3 I 216 TYR SER ILE THR SER GLY TYR TYR TRP ASN TRP ILE ARG SEQRES 4 I 216 GLN PHE PRO GLY ASN LYS LEU GLU TRP MET GLY SER ILE SEQRES 5 I 216 ASN TYR ASP GLY SER ASN ILE TYR ASN PRO SER LEU LYS SEQRES 6 I 216 ASP ARG ILE SER ILE THR ARG ASP THR SER LYS ASN GLN SEQRES 7 I 216 PHE PHE LEU LYS LEU ASN SER VAL THR THR GLU ASP THR SEQRES 8 I 216 ALA THR TYR TYR CYS ALA ARG GLY GLY ASP TYR TRP GLY SEQRES 9 I 216 GLN GLY THR SER VAL THR VAL SER SER ALA SER THR LYS SEQRES 10 I 216 GLY PRO SER VAL PHE PRO LEU ALA PRO SER SER LYS SER SEQRES 11 I 216 THR SER GLY GLY THR ALA ALA LEU GLY CYS LEU VAL LYS SEQRES 12 I 216 ASP TYR PHE PRO GLU PRO VAL THR VAL SER TRP ASN SER SEQRES 13 I 216 GLY ALA LEU THR SER GLY VAL HIS THR PHE PRO ALA VAL SEQRES 14 I 216 LEU GLN SER SER GLY LEU TYR SER LEU SER SER VAL VAL SEQRES 15 I 216 THR VAL PRO SER SER SER LEU GLY THR GLN THR TYR ILE SEQRES 16 I 216 CYS ASN VAL ASN HIS LYS PRO SER ASN THR LYS VAL ASP SEQRES 17 I 216 LYS ARG VAL GLU PRO LYS SER CYS SEQRES 1 L 215 ASP ILE VAL LEU THR GLN THR PRO ALA ILE MET SER ALA SEQRES 2 L 215 SER PRO GLY GLU LYS VAL THR LEU THR CYS SER ALA SER SEQRES 3 L 215 SER SER VAL SER TYR MET HIS TRP PHE GLN GLN LYS SER SEQRES 4 L 215 GLY THR SER PRO LYS ARG TRP ILE TYR ASP THR SER LYS SEQRES 5 L 215 LEU ALA SER GLY VAL PRO ALA ARG PHE SER GLY SER GLY SEQRES 6 L 215 SER GLY THR SER TYR SER LEU THR ILE SER SER MET GLU SEQRES 7 L 215 ALA GLU ASP ALA ALA ALA TYR TYR CYS GLN GLN TRP SER SEQRES 8 L 215 SER ASP PRO PRO MET LEU THR PHE GLY ALA GLY THR LYS SEQRES 9 L 215 LEU GLU LEU LYS ARG THR VAL ALA ALA PRO SER VAL PHE SEQRES 10 L 215 ILE PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR SEQRES 11 L 215 ALA SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG SEQRES 12 L 215 GLU ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SEQRES 13 L 215 SER GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER SEQRES 14 L 215 LYS ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SEQRES 15 L 215 SER LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS SEQRES 16 L 215 GLU VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SEQRES 17 L 215 SER PHE ASN ARG GLY GLU CYS SEQRES 1 V 126 UNK VAL GLN LEU UNK UNK SER GLY GLY GLY UNK VAL GLN SEQRES 2 V 126 UNK GLY UNK SER LEU UNK LEU SER CYS UNK ALA UNK UNK SEQRES 3 V 126 UNK UNK UNK UNK UNK UNK UNK UNK TRP UNK ARG GLN UNK SEQRES 4 V 126 PRO GLY UNK UNK ARG GLU UNK VAL UNK UNK UNK UNK UNK SEQRES 5 V 126 UNK UNK UNK UNK UNK UNK UNK UNK ASP SER UNK UNK GLY SEQRES 6 V 126 ARG PHE THR UNK SER UNK ASP UNK UNK UNK UNK UNK UNK SEQRES 7 V 126 UNK LEU GLN UNK UNK UNK LEU UNK UNK UNK ASP UNK ALA SEQRES 8 V 126 UNK TYR TYR CYS UNK UNK UNK UNK UNK UNK UNK UNK UNK SEQRES 9 V 126 UNK UNK UNK UNK UNK TRP GLY UNK GLY THR UNK VAL THR SEQRES 10 V 126 VAL SER SER HIS HIS HIS HIS HIS HIS HET A2G A 1 14 HET SIA A 2 20 HET A2G E 1 14 HET SIA E 2 20 HET THR B 301 8 HET THR I 301 8 HETNAM A2G 2-ACETAMIDO-2-DEOXY-ALPHA-D-GALACTOPYRANOSE HETNAM SIA N-ACETYL-ALPHA-NEURAMINIC ACID HETNAM THR THREONINE HETSYN A2G N-ACETYL-ALPHA-D-GALACTOSAMINE; 2-ACETAMIDO-2-DEOXY- HETSYN 2 A2G ALPHA-D-GALACTOSE; 2-ACETAMIDO-2-DEOXY-D-GALACTOSE; 2- HETSYN 3 A2G ACETAMIDO-2-DEOXY-GALACTOSE; N-ACETYL-2-DEOXY-2-AMINO- HETSYN 4 A2G GALACTOSE HETSYN SIA N-ACETYLNEURAMINIC ACID; SIALIC ACID; ALPHA-SIALIC HETSYN 2 SIA ACID; O-SIALIC ACID FORMUL 7 A2G 2(C8 H15 N O6) FORMUL 7 SIA 2(C11 H19 N O9) FORMUL 9 THR 2(C4 H9 N O3) FORMUL 11 HOH *139(H2 O) HELIX 1 AA1 THR B 86 THR B 90 5 5 HELIX 2 AA2 SER B 155 ALA B 157 5 3 HELIX 3 AA3 SER B 186 LEU B 188 5 3 HELIX 4 AA4 GLU C 78 ALA C 82 5 5 HELIX 5 AA5 SER C 122 LYS C 127 1 6 HELIX 6 AA6 LYS C 184 GLU C 188 1 5 HELIX 7 AA7 UNK D 86 UNK D 90 5 5 HELIX 8 AA8 LEU I 64 ASP I 66 5 3 HELIX 9 AA9 THR I 87 THR I 91 5 5 HELIX 10 AB1 SER I 156 ALA I 158 5 3 HELIX 11 AB2 SER I 187 LEU I 189 5 3 HELIX 12 AB3 GLU L 78 ALA L 82 5 5 HELIX 13 AB4 SER L 122 LYS L 127 1 6 HELIX 14 AB5 LYS L 184 LYS L 189 1 6 HELIX 15 AB6 UNK V 86 UNK V 90 5 5 SHEET 1 AA1 4 GLN B 3 SER B 7 0 SHEET 2 AA1 4 LEU B 18 ILE B 25 -1 O SER B 23 N GLN B 5 SHEET 3 AA1 4 GLN B 77 LEU B 82 -1 O LEU B 82 N LEU B 18 SHEET 4 AA1 4 ILE B 67 SER B 68 -1 N SER B 68 O LYS B 81 SHEET 1 AA2 4 GLN B 3 SER B 7 0 SHEET 2 AA2 4 LEU B 18 ILE B 25 -1 O SER B 23 N GLN B 5 SHEET 3 AA2 4 GLN B 77 LEU B 82 -1 O LEU B 82 N LEU B 18 SHEET 4 AA2 4 ARG B 71 ASP B 72 -1 N ASP B 72 O GLN B 77 SHEET 1 AA3 6 LEU B 11 VAL B 12 0 SHEET 2 AA3 6 THR B 106 VAL B 110 1 O THR B 109 N VAL B 12 SHEET 3 AA3 6 ALA B 91 ARG B 97 -1 N TYR B 93 O THR B 106 SHEET 4 AA3 6 TRP B 35 GLN B 39 -1 N ILE B 37 O TYR B 94 SHEET 5 AA3 6 LEU B 45 ILE B 51 -1 O MET B 48 N TRP B 36 SHEET 6 AA3 6 ASN B 57 TYR B 59 -1 O ILE B 58 N SER B 50 SHEET 1 AA4 4 LEU B 11 VAL B 12 0 SHEET 2 AA4 4 THR B 106 VAL B 110 1 O THR B 109 N VAL B 12 SHEET 3 AA4 4 ALA B 91 ARG B 97 -1 N TYR B 93 O THR B 106 SHEET 4 AA4 4 TYR B 101 TRP B 102 -1 O TYR B 101 N ARG B 97 SHEET 1 AA5 4 SER B 119 LEU B 123 0 SHEET 2 AA5 4 THR B 134 TYR B 144 -1 O GLY B 138 N LEU B 123 SHEET 3 AA5 4 TYR B 175 PRO B 184 -1 O VAL B 183 N ALA B 135 SHEET 4 AA5 4 VAL B 162 THR B 164 -1 N HIS B 163 O VAL B 180 SHEET 1 AA6 4 SER B 119 LEU B 123 0 SHEET 2 AA6 4 THR B 134 TYR B 144 -1 O GLY B 138 N LEU B 123 SHEET 3 AA6 4 TYR B 175 PRO B 184 -1 O VAL B 183 N ALA B 135 SHEET 4 AA6 4 VAL B 168 LEU B 169 -1 N VAL B 168 O SER B 176 SHEET 1 AA7 3 THR B 150 TRP B 153 0 SHEET 2 AA7 3 ILE B 194 HIS B 199 -1 O ASN B 196 N SER B 152 SHEET 3 AA7 3 THR B 204 ARG B 209 -1 O VAL B 206 N VAL B 197 SHEET 1 AA8 3 LEU C 4 THR C 7 0 SHEET 2 AA8 3 VAL C 19 VAL C 29 -1 O SER C 24 N THR C 5 SHEET 3 AA8 3 PHE C 61 ILE C 74 -1 O LEU C 72 N LEU C 21 SHEET 1 AA9 6 ILE C 10 ALA C 13 0 SHEET 2 AA9 6 THR C 103 LEU C 107 1 O LYS C 104 N MET C 11 SHEET 3 AA9 6 ALA C 83 SER C 91 -1 N ALA C 83 O LEU C 105 SHEET 4 AA9 6 MET C 32 GLN C 37 -1 N HIS C 33 O GLN C 88 SHEET 5 AA9 6 LYS C 44 TYR C 48 -1 O ILE C 47 N TRP C 34 SHEET 6 AA9 6 LYS C 52 LEU C 53 -1 O LYS C 52 N TYR C 48 SHEET 1 AB1 4 ILE C 10 ALA C 13 0 SHEET 2 AB1 4 THR C 103 LEU C 107 1 O LYS C 104 N MET C 11 SHEET 3 AB1 4 ALA C 83 SER C 91 -1 N ALA C 83 O LEU C 105 SHEET 4 AB1 4 MET C 96 PHE C 99 -1 O THR C 98 N GLN C 89 SHEET 1 AB2 4 SER C 115 PHE C 119 0 SHEET 2 AB2 4 THR C 130 PHE C 140 -1 O LEU C 136 N PHE C 117 SHEET 3 AB2 4 TYR C 174 SER C 183 -1 O LEU C 176 N LEU C 137 SHEET 4 AB2 4 SER C 160 VAL C 164 -1 N SER C 163 O SER C 177 SHEET 1 AB3 4 ALA C 154 LEU C 155 0 SHEET 2 AB3 4 ALA C 145 VAL C 151 -1 N VAL C 151 O ALA C 154 SHEET 3 AB3 4 VAL C 192 HIS C 199 -1 O GLU C 196 N GLN C 148 SHEET 4 AB3 4 VAL C 206 ASN C 211 -1 O VAL C 206 N VAL C 197 SHEET 1 AB4 4 LEU D 4 SER D 7 0 SHEET 2 AB4 4 LEU D 18 ALA D 24 -1 O SER D 21 N SER D 7 SHEET 3 AB4 4 UNK D 77 UNK D 82 -1 O LEU D 80 N LEU D 20 SHEET 4 AB4 4 PHE D 67 ASP D 72 -1 N ASP D 72 O UNK D 77 SHEET 1 AB5 6 GLY D 10 UNK D 11 0 SHEET 2 AB5 6 THR D 114 THR D 117 1 O THR D 117 N GLY D 10 SHEET 3 AB5 6 ALA D 91 UNK D 98 -1 N TYR D 93 O THR D 114 SHEET 4 AB5 6 UNK D 32 GLN D 38 -1 N UNK D 36 O TYR D 94 SHEET 5 AB5 6 GLU D 45 UNK D 50 -1 O UNK D 48 N TRP D 35 SHEET 6 AB5 6 UNK D 57 UNK D 59 -1 O UNK D 58 N UNK D 49 SHEET 1 AB6 4 GLY D 10 UNK D 11 0 SHEET 2 AB6 4 THR D 114 THR D 117 1 O THR D 117 N GLY D 10 SHEET 3 AB6 4 ALA D 91 UNK D 98 -1 N TYR D 93 O THR D 114 SHEET 4 AB6 4 UNK D 107 TRP D 110 -1 O UNK D 109 N UNK D 97 SHEET 1 AB7 4 GLN I 3 SER I 7 0 SHEET 2 AB7 4 LEU I 18 ILE I 25 -1 O THR I 21 N SER I 7 SHEET 3 AB7 4 GLN I 78 LEU I 83 -1 O LEU I 83 N LEU I 18 SHEET 4 AB7 4 ILE I 68 SER I 69 -1 N SER I 69 O LYS I 82 SHEET 1 AB8 4 GLN I 3 SER I 7 0 SHEET 2 AB8 4 LEU I 18 ILE I 25 -1 O THR I 21 N SER I 7 SHEET 3 AB8 4 GLN I 78 LEU I 83 -1 O LEU I 83 N LEU I 18 SHEET 4 AB8 4 ARG I 72 ASP I 73 -1 N ASP I 73 O GLN I 78 SHEET 1 AB9 6 LEU I 11 VAL I 12 0 SHEET 2 AB9 6 THR I 107 VAL I 111 1 O THR I 110 N VAL I 12 SHEET 3 AB9 6 ALA I 92 ALA I 97 -1 N TYR I 94 O THR I 107 SHEET 4 AB9 6 TRP I 35 GLN I 40 -1 N ILE I 38 O TYR I 95 SHEET 5 AB9 6 LEU I 46 ILE I 52 -1 O ILE I 52 N TRP I 35 SHEET 6 AB9 6 ASN I 58 TYR I 60 -1 O ILE I 59 N SER I 51 SHEET 1 AC1 4 SER I 120 LEU I 124 0 SHEET 2 AC1 4 THR I 135 TYR I 145 -1 O LEU I 141 N PHE I 122 SHEET 3 AC1 4 TYR I 176 PRO I 185 -1 O VAL I 184 N ALA I 136 SHEET 4 AC1 4 VAL I 163 THR I 165 -1 N HIS I 164 O VAL I 181 SHEET 1 AC2 4 SER I 120 LEU I 124 0 SHEET 2 AC2 4 THR I 135 TYR I 145 -1 O LEU I 141 N PHE I 122 SHEET 3 AC2 4 TYR I 176 PRO I 185 -1 O VAL I 184 N ALA I 136 SHEET 4 AC2 4 VAL I 169 LEU I 170 -1 N VAL I 169 O SER I 177 SHEET 1 AC3 3 THR I 151 TRP I 154 0 SHEET 2 AC3 3 TYR I 194 HIS I 200 -1 O ASN I 197 N SER I 153 SHEET 3 AC3 3 THR I 205 VAL I 211 -1 O VAL I 207 N VAL I 198 SHEET 1 AC4 3 LEU L 4 THR L 7 0 SHEET 2 AC4 3 VAL L 19 VAL L 29 -1 O THR L 22 N THR L 7 SHEET 3 AC4 3 PHE L 61 ILE L 74 -1 O LEU L 72 N LEU L 21 SHEET 1 AC5 6 ILE L 10 ALA L 13 0 SHEET 2 AC5 6 THR L 103 LEU L 107 1 O LYS L 104 N MET L 11 SHEET 3 AC5 6 ALA L 84 SER L 91 -1 N TYR L 85 O THR L 103 SHEET 4 AC5 6 HIS L 33 GLN L 37 -1 N HIS L 33 O GLN L 88 SHEET 5 AC5 6 LYS L 44 TYR L 48 -1 O ILE L 47 N TRP L 34 SHEET 6 AC5 6 LYS L 52 LEU L 53 -1 O LYS L 52 N TYR L 48 SHEET 1 AC6 4 ILE L 10 ALA L 13 0 SHEET 2 AC6 4 THR L 103 LEU L 107 1 O LYS L 104 N MET L 11 SHEET 3 AC6 4 ALA L 84 SER L 91 -1 N TYR L 85 O THR L 103 SHEET 4 AC6 4 MET L 96 PHE L 99 -1 O MET L 96 N SER L 91 SHEET 1 AC7 4 SER L 115 PHE L 119 0 SHEET 2 AC7 4 THR L 130 PHE L 140 -1 O VAL L 134 N PHE L 119 SHEET 3 AC7 4 TYR L 174 SER L 183 -1 O LEU L 176 N LEU L 137 SHEET 4 AC7 4 SER L 160 VAL L 164 -1 N GLN L 161 O THR L 179 SHEET 1 AC8 3 ALA L 145 VAL L 151 0 SHEET 2 AC8 3 VAL L 192 HIS L 199 -1 O GLU L 196 N GLN L 148 SHEET 3 AC8 3 VAL L 206 ASN L 211 -1 O VAL L 206 N VAL L 197 SHEET 1 AC9 4 LEU V 4 SER V 7 0 SHEET 2 AC9 4 LEU V 18 ALA V 24 -1 O SER V 21 N SER V 7 SHEET 3 AC9 4 UNK V 77 UNK V 82 -1 O UNK V 82 N LEU V 18 SHEET 4 AC9 4 PHE V 67 ASP V 72 -1 N SER V 70 O UNK V 79 SHEET 1 AD1 6 GLY V 10 VAL V 12 0 SHEET 2 AD1 6 THR V 114 VAL V 118 1 O THR V 117 N VAL V 12 SHEET 3 AD1 6 ALA V 91 UNK V 98 -1 N TYR V 93 O THR V 114 SHEET 4 AD1 6 UNK V 32 GLN V 38 -1 N UNK V 36 O TYR V 94 SHEET 5 AD1 6 GLU V 45 UNK V 50 -1 O UNK V 48 N TRP V 35 SHEET 6 AD1 6 UNK V 57 UNK V 59 -1 O UNK V 58 N UNK V 49 SHEET 1 AD2 4 GLY V 10 VAL V 12 0 SHEET 2 AD2 4 THR V 114 VAL V 118 1 O THR V 117 N VAL V 12 SHEET 3 AD2 4 ALA V 91 UNK V 98 -1 N TYR V 93 O THR V 114 SHEET 4 AD2 4 UNK V 107 TRP V 110 -1 O UNK V 109 N UNK V 97 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.03 SSBOND 2 CYS B 139 CYS B 195 1555 1555 2.03 SSBOND 3 CYS C 23 CYS C 87 1555 1555 2.03 SSBOND 4 CYS C 135 CYS C 195 1555 1555 2.03 SSBOND 5 CYS I 22 CYS I 96 1555 1555 2.03 SSBOND 6 CYS L 135 CYS L 195 1555 1555 2.03 LINK OG1 THR B 301 C1 A2G A 1 1555 1555 1.40 LINK OG1 THR I 301 C1 A2G E 1 1555 1555 1.41 LINK O6 A2G A 1 C2 SIA A 2 1555 1555 1.40 LINK O6 A2G E 1 C2 SIA E 2 1555 1555 1.40 CISPEP 1 PHE B 145 PRO B 146 0 -1.68 CISPEP 2 GLU B 147 PRO B 148 0 -6.18 CISPEP 3 THR C 7 PRO C 8 0 -2.99 CISPEP 4 TYR C 141 PRO C 142 0 0.39 CISPEP 5 PHE I 146 PRO I 147 0 -4.28 CISPEP 6 GLU I 148 PRO I 149 0 -2.33 CISPEP 7 THR L 7 PRO L 8 0 -1.86 CISPEP 8 TYR L 141 PRO L 142 0 3.54 CRYST1 47.331 128.144 98.896 90.00 98.17 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 0.021128 0.000000 0.003034 0.00000 SCALE2 0.000000 0.007804 0.000000 0.00000 SCALE3 0.000000 0.000000 0.010215 0.00000