HEADER IMMUNE SYSTEM 05-AUG-25 9PX5 TITLE CRYSTAL STRUCTURE OF FAB 7268 IN COMPLEX WITH MBP-TREM2 IG DOMAIN TITLE 2 FUSION COMPND MOL_ID: 1; COMPND 2 MOLECULE: MALTOSE/MALTODEXTRIN-BINDING PERIPLASMIC PROTEIN,TRIGGERING COMPND 3 RECEPTOR EXPRESSED ON MYELOID CELLS 2; COMPND 4 CHAIN: A; COMPND 5 FRAGMENT: IG DOMAIN OF TREM-2; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: 7268 FAB HEAVY CHAIN; COMPND 9 CHAIN: H; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: 7268 FAB LIGHT CHAIN; COMPND 13 CHAIN: L; COMPND 14 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: ESCHERICHIA COLI, HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 562, 9606; SOURCE 5 GENE: MALE, B4034, JW3994, TREM2; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK293; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 10029; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 16 ORGANISM_TAXID: 9606; SOURCE 17 EXPRESSION_SYSTEM: CRICETULUS GRISEUS; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 10029 KEYWDS FAB, ANTIBODY, COMPLEX, IMMUNE SYSTEM EXPDTA X-RAY DIFFRACTION AUTHOR J.W.ARNDT,Q.CHAO,H.A.COOKE,A.D.S.ALMEIDA REVDAT 1 10-SEP-25 9PX5 0 JRNL AUTH A.DA SILVA ALMEIDA,M.L.GEDDIE,A.BHATE,C.QUAN,J.W.ARNDT, JRNL AUTH 2 Y.JIAO,J.C.SANTORO,L.NOIMAN,R.VIJAYAKUMAR,J.SANCHEZ-SALAZAR, JRNL AUTH 3 A.DATTA,G.ANTOGNETTI,C.A.HARTANA,X.F.WANG,B.A.SMITH, JRNL AUTH 4 D.BARTLETT,D.DUNCAN,C.C.LIU,K.OTERO GUTIERREZ,T.O.CAMERON, JRNL AUTH 5 S.KOIRALA,H.A.COOKE JRNL TITL BUILDING A POTENT TREM2 AGONISTIC, BIPARATOPIC, COMMON LIGHT JRNL TITL 2 CHAIN ANTIBODY. JRNL REF MABS V. 17 46554 2025 JRNL REFN ESSN 1942-0870 JRNL PMID 40803893 JRNL DOI 10.1080/19420862.2025.2546554 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.21.2-5419_1692 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) : 3.70 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 47.05 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.350 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 3 NUMBER OF REFLECTIONS : 13219 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.249 REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.268 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.020 REMARK 3 FREE R VALUE TEST SET COUNT : 663 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 47.0500 - 6.3200 0.98 2556 136 0.2187 0.2249 REMARK 3 2 6.3200 - 5.0200 0.99 2517 132 0.2498 0.2668 REMARK 3 3 5.0200 - 4.3900 0.99 2481 131 0.2309 0.2683 REMARK 3 4 4.3900 - 3.9900 1.00 2488 131 0.2734 0.3079 REMARK 3 5 3.9900 - 3.7000 0.99 2514 133 0.3459 0.3770 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) : 0.570 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.420 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 6759 REMARK 3 ANGLE : 0.491 9283 REMARK 3 CHIRALITY : 0.040 1076 REMARK 3 PLANARITY : 0.004 1206 REMARK 3 DIHEDRAL : 10.489 2244 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 9PX5 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-AUG-25. REMARK 100 THE DEPOSITION ID IS D_1000298663. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 09-APR-22 REMARK 200 TEMPERATURE (KELVIN) : 100 REMARK 200 PH : 6 REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SLS REMARK 200 BEAMLINE : X06SA REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000039 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 : AIMLESS REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 13219 REMARK 200 RESOLUTION RANGE HIGH (A) : 3.700 REMARK 200 RESOLUTION RANGE LOW (A) : 50.000 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.2 REMARK 200 DATA REDUNDANCY : 7.100 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 5.3000 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.70 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 4.00 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: MOLREP REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 59.51 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.04 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 11% PEG 8000, 240MM AMMONIUM SULFATE, REMARK 280 100MM MES, PH 6, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y,-Z REMARK 290 3555 X+1/2,Y+1/2,Z 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 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 59.95000 REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 32.11500 REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 59.95000 REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 32.11500 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 APPLY THE FOLLOWING TO CHAINS: A, H, L, B 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 LYS A -349 REMARK 465 THR A -348 REMARK 465 ALA A -209 REMARK 465 LYS A -208 REMARK 465 GLY A -207 REMARK 465 LYS A -206 REMARK 465 ASN A 68 REMARK 465 LEU A 69 REMARK 465 TRP A 70 REMARK 465 LEU A 71 REMARK 465 LEU A 72 REMARK 465 SER A 73 REMARK 465 PHE A 74 REMARK 465 LEU A 75 REMARK 465 ARG A 76 REMARK 465 ARG A 77 REMARK 465 TRP A 78 REMARK 465 PRO A 132 REMARK 465 LEU A 133 REMARK 465 ASP A 134 REMARK 465 HIS A 135 REMARK 465 HIS A 136 REMARK 465 HIS A 137 REMARK 465 HIS A 138 REMARK 465 HIS A 139 REMARK 465 HIS A 140 REMARK 465 HIS A 141 REMARK 465 HIS A 142 REMARK 465 CYS H 226 REMARK 470 REMARK 470 MISSING ATOM REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 470 I=INSERTION CODE): REMARK 470 M RES CSSEQI ATOMS REMARK 470 GLU A-347 CG CD OE1 OE2 REMARK 470 GLU A-346 CG CD OE1 OE2 REMARK 470 LYS A-344 CG CD CE NZ REMARK 470 LYS A-335 CG CD CE NZ REMARK 470 LYS A-325 CG CD CE NZ REMARK 470 LYS A-324 CG CD CE NZ REMARK 470 LYS A-321 CG CD CE NZ REMARK 470 ASP A-320 CG OD1 OD2 REMARK 470 LYS A-316 CG CD CE NZ REMARK 470 LYS A-308 CG CD CE NZ REMARK 470 GLU A-305 CG CD OE1 OE2 REMARK 470 LYS A-304 CG CD CE NZ REMARK 470 LYS A-262 CG CD CE NZ REMARK 470 ASN A-232 CG OD1 ND2 REMARK 470 LYS A-231 CG CD CE NZ REMARK 470 LEU A-229 CG CD1 CD2 REMARK 470 LEU A-228 CG CD1 CD2 REMARK 470 PRO A-227 CG CD REMARK 470 ASN A-226 CG OD1 ND2 REMARK 470 LYS A-223 CG CD CE NZ REMARK 470 LEU A-215 CG CD1 CD2 REMARK 470 ASP A-214 CG OD1 OD2 REMARK 470 LYS A-213 CG CD CE NZ REMARK 470 GLU A-212 CG CD OE1 OE2 REMARK 470 LEU A-211 CG CD1 CD2 REMARK 470 LYS A-210 CG CD CE NZ REMARK 470 LYS A-180 CG CD CE NZ REMARK 470 TYR A-179 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 LYS A-175 CG CD CE NZ REMARK 470 ASP A-173 CG OD1 OD2 REMARK 470 ILE A-172 CG1 CG2 CD1 REMARK 470 LYS A-171 CG CD CE NZ REMARK 470 ASP A-170 CG OD1 OD2 REMARK 470 LYS A-161 CG CD CE NZ REMARK 470 LYS A-150 CG CD CE NZ REMARK 470 ASN A-149 CG OD1 ND2 REMARK 470 LYS A-148 CG CD CE NZ REMARK 470 GLU A-136 CG CD OE1 OE2 REMARK 470 LYS A -99 CG CD CE NZ REMARK 470 LYS A -94 CG CD CE NZ REMARK 470 LYS A -73 CG CD CE NZ REMARK 470 GLU A -72 CG CD OE1 OE2 REMARK 470 GLU A -69 CG CD OE1 OE2 REMARK 470 LYS A -55 CG CD CE NZ REMARK 470 LYS A -53 CG CD CE NZ REMARK 470 LYS A -45 CG CD CE NZ REMARK 470 LYS A -37 CG CD CE NZ REMARK 470 GLU A -28 CG CD OE1 OE2 REMARK 470 GLN A -25 CG CD OE1 NE2 REMARK 470 LYS A -24 CG CD CE NZ REMARK 470 GLN A -15 CG CD OE1 NE2 REMARK 470 ARG A -6 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 42 CG CD CE NZ REMARK 470 ARG A 47 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 48 CG CD CE NZ REMARK 470 GLU A 56 CG CD OE1 OE2 REMARK 470 LYS A 57 CG CD CE NZ REMARK 470 ARG A 62 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 98 CG CD NE CZ NH1 NH2 REMARK 470 ARG A 122 CG CD NE CZ NH1 NH2 REMARK 470 LYS A 123 CG CD CE NZ REMARK 470 ASP A 131 CG OD1 OD2 REMARK 470 LYS H 43 CG CD CE NZ REMARK 470 LYS H 54 CG CD CE NZ REMARK 470 LYS H 64 CG CD CE NZ REMARK 470 ARG H 66 CG CD NE CZ NH1 NH2 REMARK 470 LYS H 75 CG CD CE NZ REMARK 470 LYS H 81 CG CD CE NZ REMARK 470 GLN H 115 CG CD OE1 NE2 REMARK 470 LYS H 127 CG CD CE NZ REMARK 470 LYS H 139 CG CD CE NZ REMARK 470 THR H 141 OG1 CG2 REMARK 470 LYS H 211 CG CD CE NZ REMARK 470 LYS H 216 CG CD CE NZ REMARK 470 ARG L 24 CG CD NE CZ NH1 NH2 REMARK 470 LYS L 45 CG CD CE NZ REMARK 470 LYS L 145 CG CD CE NZ REMARK 470 LYS L 149 CG CD CE NZ REMARK 470 LYS L 169 CG CD CE NZ REMARK 470 LYS L 183 CG CD CE NZ REMARK 470 GLU L 187 CG CD OE1 OE2 REMARK 470 LYS L 188 CG CD CE NZ REMARK 470 LYS L 190 CG CD CE NZ REMARK 470 GLU L 213 CG CD OE1 OE2 REMARK 470 CYS L 214 SG 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 ASP A-295 32.08 -89.42 REMARK 500 ASP A-186 36.82 -98.91 REMARK 500 ALA A-182 -70.50 -85.63 REMARK 500 TYR A -67 -36.09 -131.69 REMARK 500 HIS A 103 -17.38 80.63 REMARK 500 LEU A 107 71.30 42.39 REMARK 500 ARG A 122 112.09 -161.75 REMARK 500 SER H 15 -6.98 74.83 REMARK 500 ASN H 76 49.70 38.81 REMARK 500 SER H 83 -71.93 -71.89 REMARK 500 TYR H 101 90.90 40.51 REMARK 500 PRO H 110 108.72 -52.94 REMARK 500 ASP H 154 70.71 57.07 REMARK 500 SER L 30 -123.41 58.82 REMARK 500 TYR L 32 66.72 -113.91 REMARK 500 ALA L 51 -37.25 68.56 REMARK 500 ALA L 84 -165.40 -168.52 REMARK 500 ASN L 138 77.81 56.96 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: 9PWN RELATED DB: PDB DBREF 9PX5 A -349 16 UNP P0AEX9 MALE_ECOLI 27 392 DBREF 9PX5 A 18 135 UNP Q9NZC2 TREM2_HUMAN 18 135 DBREF 9PX5 H 1 226 PDB 9PX5 9PX5 1 226 DBREF 9PX5 L 1 214 PDB 9PX5 9PX5 1 214 SEQADV 9PX5 THR A -348 UNP P0AEX9 ILE 28 CONFLICT SEQADV 9PX5 ALA A -268 UNP P0AEX9 ASP 108 CONFLICT SEQADV 9PX5 ALA A -267 UNP P0AEX9 LYS 109 CONFLICT SEQADV 9PX5 ALA A -178 UNP P0AEX9 GLU 198 CONFLICT SEQADV 9PX5 ALA A -177 UNP P0AEX9 ASN 199 CONFLICT SEQADV 9PX5 HIS A -135 UNP P0AEX9 ALA 241 CONFLICT SEQADV 9PX5 HIS A -131 UNP P0AEX9 LYS 245 CONFLICT SEQADV 9PX5 ALA A -111 UNP P0AEX9 LYS 265 CONFLICT SEQADV 9PX5 VAL A -38 UNP P0AEX9 ALA 338 CONFLICT SEQADV 9PX5 VAL A -33 UNP P0AEX9 ILE 343 CONFLICT SEQADV 9PX5 ALA A 9 UNP P0AEX9 GLU 385 CONFLICT SEQADV 9PX5 ALA A 12 UNP P0AEX9 LYS 388 CONFLICT SEQADV 9PX5 ALA A 13 UNP P0AEX9 ASP 389 CONFLICT SEQADV 9PX5 ASN A 17 UNP P0AEX9 LINKER SEQADV 9PX5 ASP A 20 UNP Q9NZC2 ASN 20 CONFLICT SEQADV 9PX5 HIS A 136 UNP Q9NZC2 EXPRESSION TAG SEQADV 9PX5 HIS A 137 UNP Q9NZC2 EXPRESSION TAG SEQADV 9PX5 HIS A 138 UNP Q9NZC2 EXPRESSION TAG SEQADV 9PX5 HIS A 139 UNP Q9NZC2 EXPRESSION TAG SEQADV 9PX5 HIS A 140 UNP Q9NZC2 EXPRESSION TAG SEQADV 9PX5 HIS A 141 UNP Q9NZC2 EXPRESSION TAG SEQADV 9PX5 HIS A 142 UNP Q9NZC2 EXPRESSION TAG SEQRES 1 A 492 LYS THR GLU GLU GLY LYS LEU VAL ILE TRP ILE ASN GLY SEQRES 2 A 492 ASP LYS GLY TYR ASN GLY LEU ALA GLU VAL GLY LYS LYS SEQRES 3 A 492 PHE GLU LYS ASP THR GLY ILE LYS VAL THR VAL GLU HIS SEQRES 4 A 492 PRO ASP LYS LEU GLU GLU LYS PHE PRO GLN VAL ALA ALA SEQRES 5 A 492 THR GLY ASP GLY PRO ASP ILE ILE PHE TRP ALA HIS ASP SEQRES 6 A 492 ARG PHE GLY GLY TYR ALA GLN SER GLY LEU LEU ALA GLU SEQRES 7 A 492 ILE THR PRO ALA ALA ALA PHE GLN ASP LYS LEU TYR PRO SEQRES 8 A 492 PHE THR TRP ASP ALA VAL ARG TYR ASN GLY LYS LEU ILE SEQRES 9 A 492 ALA TYR PRO ILE ALA VAL GLU ALA LEU SER LEU ILE TYR SEQRES 10 A 492 ASN LYS ASP LEU LEU PRO ASN PRO PRO LYS THR TRP GLU SEQRES 11 A 492 GLU ILE PRO ALA LEU ASP LYS GLU LEU LYS ALA LYS GLY SEQRES 12 A 492 LYS SER ALA LEU MET PHE ASN LEU GLN GLU PRO TYR PHE SEQRES 13 A 492 THR TRP PRO LEU ILE ALA ALA ASP GLY GLY TYR ALA PHE SEQRES 14 A 492 LYS TYR ALA ALA GLY LYS TYR ASP ILE LYS ASP VAL GLY SEQRES 15 A 492 VAL ASP ASN ALA GLY ALA LYS ALA GLY LEU THR PHE LEU SEQRES 16 A 492 VAL ASP LEU ILE LYS ASN LYS HIS MET ASN ALA ASP THR SEQRES 17 A 492 ASP TYR SER ILE ALA GLU HIS ALA PHE ASN HIS GLY GLU SEQRES 18 A 492 THR ALA MET THR ILE ASN GLY PRO TRP ALA TRP SER ASN SEQRES 19 A 492 ILE ASP THR SER ALA VAL ASN TYR GLY VAL THR VAL LEU SEQRES 20 A 492 PRO THR PHE LYS GLY GLN PRO SER LYS PRO PHE VAL GLY SEQRES 21 A 492 VAL LEU SER ALA GLY ILE ASN ALA ALA SER PRO ASN LYS SEQRES 22 A 492 GLU LEU ALA LYS GLU PHE LEU GLU ASN TYR LEU LEU THR SEQRES 23 A 492 ASP GLU GLY LEU GLU ALA VAL ASN LYS ASP LYS PRO LEU SEQRES 24 A 492 GLY ALA VAL ALA LEU LYS SER TYR GLU GLU GLU LEU VAL SEQRES 25 A 492 LYS ASP PRO ARG VAL ALA ALA THR MET GLU ASN ALA GLN SEQRES 26 A 492 LYS GLY GLU ILE MET PRO ASN ILE PRO GLN MET SER ALA SEQRES 27 A 492 PHE TRP TYR ALA VAL ARG THR ALA VAL ILE ASN ALA ALA SEQRES 28 A 492 SER GLY ARG GLN THR VAL ASP ALA ALA LEU ALA ALA ALA SEQRES 29 A 492 GLN THR ASN ALA HIS ASP THR THR VAL PHE GLN GLY VAL SEQRES 30 A 492 ALA GLY GLN SER LEU GLN VAL SER CYS PRO TYR ASP SER SEQRES 31 A 492 MET LYS HIS TRP GLY ARG ARG LYS ALA TRP CYS ARG GLN SEQRES 32 A 492 LEU GLY GLU LYS GLY PRO CYS GLN ARG VAL VAL SER THR SEQRES 33 A 492 HIS ASN LEU TRP LEU LEU SER PHE LEU ARG ARG TRP ASN SEQRES 34 A 492 GLY SER THR ALA ILE THR ASP ASP THR LEU GLY GLY THR SEQRES 35 A 492 LEU THR ILE THR LEU ARG ASN LEU GLN PRO HIS ASP ALA SEQRES 36 A 492 GLY LEU TYR GLN CYS GLN SER LEU HIS GLY SER GLU ALA SEQRES 37 A 492 ASP THR LEU ARG LYS VAL LEU VAL GLU VAL LEU ALA ASP SEQRES 38 A 492 PRO LEU ASP HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 1 H 226 GLN VAL GLN LEU GLN GLN TRP GLY ALA GLY LEU LEU LYS SEQRES 2 H 226 PRO SER GLU THR LEU SER LEU THR CYS ALA VAL TYR GLY SEQRES 3 H 226 VAL SER PHE SER GLY TYR HIS TRP TYR TRP ILE ARG GLN SEQRES 4 H 226 PRO PRO GLY LYS GLY LEU GLU TRP ILE GLY GLU ILE ASP SEQRES 5 H 226 ASN LYS GLY GLN THR ASN TYR ASN PRO SER LEU LYS SER SEQRES 6 H 226 ARG VAL THR ILE SER VAL ASP THR SER LYS ASN GLN PHE SEQRES 7 H 226 SER LEU LYS LEU SER SER VAL THR ALA ALA ASP THR ALA SEQRES 8 H 226 VAL TYR TYR CYS ALA ARG GLY GLY SER TYR TYR GLY HIS SEQRES 9 H 226 PRO TYR LEU ALA ALA PRO ASP ILE TRP GLY GLN GLY THR SEQRES 10 H 226 MET VAL THR VAL SER SER ALA SER THR LYS GLY PRO SER SEQRES 11 H 226 VAL PHE PRO LEU ALA PRO SER SER LYS SER THR SER GLY SEQRES 12 H 226 GLY THR ALA ALA LEU GLY CYS LEU VAL LYS ASP TYR PHE SEQRES 13 H 226 PRO GLU PRO VAL THR VAL SER TRP ASN SER GLY ALA LEU SEQRES 14 H 226 THR SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN SER SEQRES 15 H 226 SER GLY LEU TYR SER LEU SER SER VAL VAL THR VAL PRO SEQRES 16 H 226 SER SER SER LEU GLY THR GLN THR TYR ILE CYS ASN VAL SEQRES 17 H 226 ASN HIS LYS PRO SER ASN THR LYS VAL ASP LYS LYS VAL SEQRES 18 H 226 GLU PRO LYS SER CYS SEQRES 1 L 214 ASP ILE GLN MET THR GLN SER PRO SER SER LEU SER ALA SEQRES 2 L 214 SER VAL GLY ASP ARG VAL THR ILE THR CYS ARG ALA SER SEQRES 3 L 214 GLN SER ILE SER SER TYR LEU ASN TRP TYR GLN GLN LYS SEQRES 4 L 214 PRO GLY LYS ALA PRO LYS LEU LEU ILE TYR ALA ALA SER SEQRES 5 L 214 SER LEU GLN SER GLY VAL PRO SER ARG PHE SER GLY SER SEQRES 6 L 214 GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER LEU SEQRES 7 L 214 GLN PRO GLU ASP PHE ALA THR TYR TYR CYS GLN GLN SER SEQRES 8 L 214 TYR SER THR PRO TYR THR PHE GLY GLN GLY THR LYS LEU SEQRES 9 L 214 GLU ILE LYS ARG THR VAL ALA ALA PRO SER VAL PHE ILE SEQRES 10 L 214 PHE PRO PRO SER ASP GLU GLN LEU LYS SER GLY THR ALA SEQRES 11 L 214 SER VAL VAL CYS LEU LEU ASN ASN PHE TYR PRO ARG GLU SEQRES 12 L 214 ALA LYS VAL GLN TRP LYS VAL ASP ASN ALA LEU GLN SER SEQRES 13 L 214 GLY ASN SER GLN GLU SER VAL THR GLU GLN ASP SER LYS SEQRES 14 L 214 ASP SER THR TYR SER LEU SER SER THR LEU THR LEU SER SEQRES 15 L 214 LYS ALA ASP TYR GLU LYS HIS LYS VAL TYR ALA CYS GLU SEQRES 16 L 214 VAL THR HIS GLN GLY LEU SER SER PRO VAL THR LYS SER SEQRES 17 L 214 PHE ASN ARG GLY GLU CYS HET BGC B 1 12 HET GLC B 2 11 HET SO4 A 201 5 HET SO4 A 202 5 HETNAM BGC BETA-D-GLUCOPYRANOSE HETNAM GLC ALPHA-D-GLUCOPYRANOSE HETNAM SO4 SULFATE ION HETSYN BGC BETA-D-GLUCOSE; D-GLUCOSE; GLUCOSE HETSYN GLC ALPHA-D-GLUCOSE; D-GLUCOSE; GLUCOSE FORMUL 4 BGC C6 H12 O6 FORMUL 4 GLC C6 H12 O6 FORMUL 5 SO4 2(O4 S 2-) HELIX 1 AA1 TYR A -333 GLY A -318 1 16 HELIX 2 AA2 LYS A -308 ALA A -298 1 11 HELIX 3 AA3 ARG A -284 SER A -277 1 8 HELIX 4 AA4 ALA A -268 ASP A -263 1 6 HELIX 5 AA5 TYR A -260 VAL A -253 1 8 HELIX 6 AA6 GLU A -219 LYS A -210 1 10 HELIX 7 AA7 GLU A -197 ALA A -187 1 11 HELIX 8 AA8 ASN A -165 ASN A -149 1 17 HELIX 9 AA9 ASP A -141 HIS A -131 1 11 HELIX 10 AB1 GLY A -122 TRP A -120 5 3 HELIX 11 AB2 ALA A -119 SER A -112 1 8 HELIX 12 AB3 ASN A -78 TYR A -67 1 12 HELIX 13 AB4 THR A -64 LYS A -53 1 12 HELIX 14 AB5 LEU A -46 VAL A -38 1 9 HELIX 15 AB6 ASP A -36 GLY A -23 1 14 HELIX 16 AB7 GLN A -15 GLY A 3 1 19 HELIX 17 AB8 THR A 6 HIS A 19 1 14 HELIX 18 AB9 THR H 73 LYS H 75 5 3 HELIX 19 AC1 THR H 86 THR H 90 5 5 HELIX 20 AC2 SER H 137 LYS H 139 5 3 HELIX 21 AC3 SER H 166 ALA H 168 5 3 HELIX 22 AC4 SER H 197 LEU H 199 5 3 HELIX 23 AC5 GLN L 79 PHE L 83 5 5 HELIX 24 AC6 SER L 121A LYS L 126A 1 6 HELIX 25 AC7 LYS L 183 HIS L 189 1 7 SHEET 1 AA1 6 VAL A-315 GLU A-312 0 SHEET 2 AA1 6 LEU A-343 TRP A-340 1 N ILE A-341 O GLU A-312 SHEET 3 AA1 6 ILE A-291 ALA A-287 1 O ILE A-291 N TRP A-340 SHEET 4 AA1 6 GLY A -90 ILE A -84 -1 O GLY A -85 N ILE A-290 SHEET 5 AA1 6 TYR A-244 GLU A-239 -1 N GLU A-239 O GLY A -90 SHEET 6 AA1 6 ALA A -49 VAL A -48 -1 O ALA A -49 N VAL A-240 SHEET 1 AA2 3 MET A-126 ASN A-123 0 SHEET 2 AA2 3 SER A-236 ASN A-232 -1 N ILE A-234 O THR A-125 SHEET 3 AA2 3 TYR A-108 THR A-105 -1 O GLY A-107 N TYR A-233 SHEET 1 AA3 2 TYR A-183 ALA A-178 0 SHEET 2 AA3 2 LYS A-175 GLY A-168 -1 O ASP A-173 N LYS A-180 SHEET 1 AA4 5 VAL A 23 VAL A 27 0 SHEET 2 AA4 5 GLU A 117 LEU A 129 1 O GLU A 127 N PHE A 24 SHEET 3 AA4 5 TYR A 108 HIS A 114 -1 N CYS A 110 O LEU A 121 SHEET 4 AA4 5 ARG A 47 GLN A 53 -1 N ARG A 47 O LEU A 113 SHEET 5 AA4 5 CYS A 60 SER A 65 -1 O GLN A 61 N ARG A 52 SHEET 1 AA5 3 LEU A 32 PRO A 37 0 SHEET 2 AA5 3 THR A 92 LEU A 97 -1 O LEU A 93 N CYS A 36 SHEET 3 AA5 3 THR A 82 ASP A 87 -1 N ALA A 83 O THR A 96 SHEET 1 AA6 4 GLN H 3 GLY H 8 0 SHEET 2 AA6 4 LEU H 18 TYR H 25 -1 O ALA H 23 N GLN H 5 SHEET 3 AA6 4 GLN H 77 LEU H 82 -1 O LEU H 80 N LEU H 20 SHEET 4 AA6 4 VAL H 67 ASP H 72 -1 N ASP H 72 O GLN H 77 SHEET 1 AA7 6 LEU H 11 LEU H 12 0 SHEET 2 AA7 6 THR H 117 VAL H 121 1 O THR H 120 N LEU H 12 SHEET 3 AA7 6 ALA H 91 GLY H 98 -1 N ALA H 91 O VAL H 119 SHEET 4 AA7 6 TRP H 34 GLN H 39 -1 N ILE H 37 O TYR H 94 SHEET 5 AA7 6 GLU H 46 ILE H 51 -1 O GLU H 46 N ARG H 38 SHEET 6 AA7 6 THR H 57 TYR H 59 -1 O ASN H 58 N GLU H 50 SHEET 1 AA8 4 LEU H 11 LEU H 12 0 SHEET 2 AA8 4 THR H 117 VAL H 121 1 O THR H 120 N LEU H 12 SHEET 3 AA8 4 ALA H 91 GLY H 98 -1 N ALA H 91 O VAL H 119 SHEET 4 AA8 4 PRO H 110 TRP H 113 -1 O ILE H 112 N ARG H 97 SHEET 1 AA9 4 SER H 130 LEU H 134 0 SHEET 2 AA9 4 THR H 145 TYR H 155 -1 O LEU H 151 N PHE H 132 SHEET 3 AA9 4 TYR H 186 PRO H 195 -1 O SER H 190 N CYS H 150 SHEET 4 AA9 4 VAL H 173 THR H 175 -1 N HIS H 174 O VAL H 191 SHEET 1 AB1 4 THR H 141 SER H 142 0 SHEET 2 AB1 4 THR H 145 TYR H 155 -1 O THR H 145 N SER H 142 SHEET 3 AB1 4 TYR H 186 PRO H 195 -1 O SER H 190 N CYS H 150 SHEET 4 AB1 4 VAL H 179 LEU H 180 -1 N VAL H 179 O SER H 187 SHEET 1 AB2 3 THR H 161 TRP H 164 0 SHEET 2 AB2 3 ILE H 205 HIS H 210 -1 O ASN H 207 N SER H 163 SHEET 3 AB2 3 THR H 215 LYS H 220 -1 O THR H 215 N HIS H 210 SHEET 1 AB3 4 MET L 4 SER L 7 0 SHEET 2 AB3 4 VAL L 19 ALA L 25 -1 O ARG L 24 N THR L 5 SHEET 3 AB3 4 ASP L 70 ILE L 75 -1 O LEU L 73 N ILE L 21 SHEET 4 AB3 4 PHE L 62 SER L 67 -1 N SER L 63 O THR L 74 SHEET 1 AB4 6 SER L 10 ALA L 13 0 SHEET 2 AB4 6 THR L 102 ILE L 106 1 O GLU L 105 N LEU L 11 SHEET 3 AB4 6 THR L 85 GLN L 90 -1 N TYR L 86 O THR L 102 SHEET 4 AB4 6 LEU L 33 GLN L 38 -1 N ASN L 34 O GLN L 89 SHEET 5 AB4 6 LYS L 45 TYR L 49 -1 O LEU L 47 N TRP L 35 SHEET 6 AB4 6 SER L 53 LEU L 54 -1 O SER L 53 N TYR L 49 SHEET 1 AB5 4 SER L 114A PHE L 118A 0 SHEET 2 AB5 4 THR L 129 PHE L 139 -1 O LEU L 135 N PHE L 116A SHEET 3 AB5 4 TYR L 173 SER L 182 -1 O LEU L 179 N VAL L 132 SHEET 4 AB5 4 SER L 159 VAL L 163 -1 N GLN L 160 O THR L 178 SHEET 1 AB6 4 ALA L 153 LEU L 154 0 SHEET 2 AB6 4 LYS L 145 VAL L 150 -1 N VAL L 150 O ALA L 153 SHEET 3 AB6 4 VAL L 191 THR L 197 -1 O GLU L 195 N GLN L 147 SHEET 4 AB6 4 VAL L 205 ASN L 210 -1 O LYS L 207 N CYS L 194 SSBOND 1 CYS A 36 CYS A 110 1555 1555 2.03 SSBOND 2 CYS A 51 CYS A 60 1555 1555 2.03 SSBOND 3 CYS H 22 CYS H 95 1555 1555 2.03 SSBOND 4 CYS H 150 CYS H 206 1555 1555 2.03 SSBOND 5 CYS L 23 CYS L 88 1555 1555 2.03 SSBOND 6 CYS L 134 CYS L 194 1555 1555 2.03 LINK O4 BGC B 1 C1 GLC B 2 1555 1555 1.43 CISPEP 1 PHE H 156 PRO H 157 0 -3.58 CISPEP 2 GLU H 158 PRO H 159 0 5.51 CISPEP 3 SER L 7 PRO L 8 0 -1.46 CISPEP 4 TYR L 140 PRO L 141 0 2.16 CRYST1 119.900 64.230 160.800 90.00 94.45 90.00 C 1 2 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 0.008340 0.000000 0.000649 0.00000 SCALE2 0.000000 0.015569 0.000000 0.00000 SCALE3 0.000000 0.000000 0.006238 0.00000