HEADER TRANSPORT PROTEIN 31-MAY-24 9FJF TITLE LYSOSOMAL TRANSPORTING COMPLEX OF BETA-GLUCOCEREBROSIDASE (GCASE) AND TITLE 2 LYSOSOMAL INTEGRAL MEMBRANE PROTEIN 2 (LIMP-2) WITH BOUND PRO- TITLE 3 MACROBODIES (COMBINED FOCUS MAP) COMPND MOL_ID: 1; COMPND 2 MOLECULE: LYSOSOME MEMBRANE PROTEIN 2; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: 85 KDA LYSOSOMAL MEMBRANE SIALOGLYCOPROTEIN,LGP85,CD36 COMPND 5 ANTIGEN-LIKE 2,LYSOSOME MEMBRANE PROTEIN II,LIMP II,SCAVENGER COMPND 6 RECEPTOR CLASS B MEMBER 2; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: LYSOSOMAL ACID GLUCOSYLCERAMIDASE; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: LYSOSOMAL ACID GCASE,ACID BETA-GLUCOSIDASE,ALGLUCERASE,BETA- COMPND 13 GLUCOCEREBROSIDASE,BETA-GC,CHOLESTEROL GLUCOSYLTRANSFERASE,SGTASE, COMPND 14 CHOLESTERYL-BETA-GLUCOSIDASE,D-GLUCOSYL-N-ACYLSPHINGOSINE COMPND 15 GLUCOHYDROLASE,IMIGLUCERASE; COMPND 16 EC: 3.2.1.45,2.4.1.-,3.2.1.104; COMPND 17 ENGINEERED: YES; COMPND 18 MUTATION: YES; COMPND 19 MOL_ID: 3; COMPND 20 MOLECULE: NANOBODY NB1; COMPND 21 CHAIN: C; COMPND 22 ENGINEERED: YES; COMPND 23 OTHER_DETAILS: PRO-MACROBODY; NANOBODY FUSED TO MALTOSE-BINDING COMPND 24 PROTEIN (MBP) VIA PRO-PRO LINKER; MBP NOT RESOLVED AND NOT MODELED.; COMPND 25 MOL_ID: 4; COMPND 26 MOLECULE: NANOBODY NB6; COMPND 27 CHAIN: D; COMPND 28 ENGINEERED: YES; COMPND 29 OTHER_DETAILS: PRO-MACROBODY; NANOBODY FUSED TO MALTOSE-BINDING COMPND 30 PROTEIN (MBP) VIA PRO-PRO LINKER; MBP NOT RESOLVED AND NOT MODELED. SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: SCARB2, CD36L2, LIMP2, LIMPII; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F; SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PCMV3_IGK-SLIMP-2-10XHIS; SOURCE 11 MOL_ID: 2; SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 13 ORGANISM_COMMON: HUMAN; SOURCE 14 ORGANISM_TAXID: 9606; SOURCE 15 GENE: GBA, GC, GLUC; SOURCE 16 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 17 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 18 EXPRESSION_SYSTEM_CELL_LINE: HEK 293F; SOURCE 19 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID; SOURCE 20 EXPRESSION_SYSTEM_PLASMID: PCMV3_GBA1; SOURCE 21 MOL_ID: 3; SOURCE 22 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 23 ORGANISM_TAXID: 32630; SOURCE 24 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 25 EXPRESSION_SYSTEM_TAXID: 1211845; SOURCE 26 MOL_ID: 4; SOURCE 27 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 28 ORGANISM_TAXID: 32630; SOURCE 29 EXPRESSION_SYSTEM: ESCHERICHIA COLI MC1061; SOURCE 30 EXPRESSION_SYSTEM_TAXID: 1211845 KEYWDS PARKINSON, LYSOSOME, GAUCHER, GCASE, SCARB2, PRO-MACROBODY, KEYWDS 2 GLUCOSYLCERAMIDE, COMPLEX, TRANSPORT PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR J.P.DOBERT,J.H.S.SCHAEFER,T.DAL MASO,E.SOCHER,W.VERSEES,A.MOELLER, AUTHOR 2 F.ZUNKE,P.ARNOLD REVDAT 1 09-APR-25 9FJF 0 JRNL AUTH J.P.DOBERT,J.H.SCHAFER,T.DAL MASO,P.RAVINDRAN,D.J.E.HUARD, JRNL AUTH 2 E.SOCHER,L.A.SCHILDMEYER,R.L.LIEBERMAN,W.VERSEES,A.MOELLER, JRNL AUTH 3 F.ZUNKE,P.ARNOLD JRNL TITL CRYO-TEM STRUCTURE OF BETA-GLUCOCEREBROSIDASE IN COMPLEX JRNL TITL 2 WITH ITS TRANSPORTER LIMP-2. JRNL REF NAT COMMUN V. 16 3074 2025 JRNL REFN ESSN 2041-1723 JRNL PMID 40159502 JRNL DOI 10.1038/S41467-025-58340-1 REMARK 2 REMARK 2 RESOLUTION. 3.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, EPU, UCSF CHIMERAX, REMARK 3 CRYOSPARC, CRYOSPARC, COOT, UCSF REMARK 3 CHIMERAX, PHENIX, MODELLER, CRYOSPARC, REMARK 3 CRYOSPARC, PHENIX, COOT, UCSF CHIMERAX, REMARK 3 PHENIX, COOT, UCSF CHIMERAX, PHENIX, REMARK 3 PHENIX REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : 6TN1 REMARK 3 REFINEMENT SPACE : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : INITIAL FITTING WITH CHIMERAX, MANUAL FLEXIBLE REMARK 3 FITTING WITH COOT, REFINEMENT WITH PHENIX REMARK 3 REMARK 3 EM IMAGE RECONSTRUCTION STATISTICS REMARK 3 NOMINAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 ACTUAL PIXEL SIZE (ANGSTROMS) : NULL REMARK 3 EFFECTIVE RESOLUTION (ANGSTROMS) : 3.700 REMARK 3 NUMBER OF PARTICLES : 397385 REMARK 3 CTF CORRECTION METHOD : PHASE FLIPPING AND AMPLITUDE REMARK 3 CORRECTION REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 9FJF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 31-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1292138895. REMARK 245 REMARK 245 EXPERIMENTAL DETAILS REMARK 245 RECONSTRUCTION METHOD : SINGLE PARTICLE REMARK 245 SPECIMEN TYPE : NULL REMARK 245 REMARK 245 ELECTRON MICROSCOPE SAMPLE REMARK 245 SAMPLE TYPE : PARTICLE REMARK 245 PARTICLE TYPE : POINT REMARK 245 NAME OF SAMPLE : LYSOSOMAL TRANSPORTING COMPLEX REMARK 245 OF BETA-GLUCOCEREBROSIDASE AND REMARK 245 LYSOSOMAL INTEGRAL MEMBRANE REMARK 245 PROTEIN 2 (LIMP-2) WITH TWO REMARK 245 BOUND PRO-MACROBODIES. REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : 0.60 REMARK 245 SAMPLE SUPPORT DETAILS : PROTOCHIPS; CF-1.2/1.3-3CU-50 REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.40 REMARK 245 SAMPLE DETAILS : MALTOSE-BINDING PROTEIN (MBP) REMARK 245 DOMAINS OF PRO-MACROBODIES WERE NOT RESOLVED, ONLY NANOBODY REMARK 245 DOMAINS ARE INCLUDED IN THE MODEL. REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : 10550 REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS GLACIOS REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 600.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2000.00 REMARK 245 MINIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 MAXIMUM TILT ANGLE (DEGREES) : NULL REMARK 245 NOMINAL CS : NULL REMARK 245 IMAGING MODE : BRIGHT FIELD REMARK 245 ELECTRON DOSE (ELECTRONS NM**-2) : 5000.00 REMARK 245 ILLUMINATION MODE : FLOOD BEAM REMARK 245 NOMINAL MAGNIFICATION : 130000 REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 200 REMARK 245 IMAGING DETAILS : NULL REMARK 247 REMARK 247 ELECTRON MICROSCOPY REMARK 247 THE COORDINATES IN THIS ENTRY WERE GENERATED FROM ELECTRON REMARK 247 MICROSCOPY DATA. PROTEIN DATA BANK CONVENTIONS REQUIRE REMARK 247 THAT CRYST1 AND SCALE RECORDS BE INCLUDED, BUT THE VALUES REMARK 247 ON THESE RECORDS ARE MEANINGLESS EXCEPT FOR THE CALCULATION REMARK 247 OF THE STRUCTURE FACTORS. 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: TETRAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, F, G, H, I, 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 LEU B 241 REMARK 465 SER B 242 REMARK 465 GLY B 243 REMARK 465 TYR B 244 REMARK 465 PRO B 245 REMARK 465 PHE B 246 REMARK 465 GLN B 247 REMARK 465 CYS B 248 REMARK 465 LEU B 249 REMARK 465 GLY B 250 REMARK 465 PRO D 101 REMARK 465 THR D 102 REMARK 465 ASP D 103 REMARK 465 SER D 104 REMARK 465 SER D 105 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 PRO B 6 O 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 GLN A 101 141.27 -173.74 REMARK 500 ASP A 210 -63.93 -91.78 REMARK 500 ASN A 331 61.57 61.33 REMARK 500 ALA A 352 -79.19 -85.26 REMARK 500 VAL A 408 -64.86 -129.72 REMARK 500 TYR B 11 -169.62 -127.42 REMARK 500 PHE B 75 -132.41 59.01 REMARK 500 THR B 86 -168.91 -128.42 REMARK 500 ALA B 95 58.87 -95.27 REMARK 500 LYS B 157 -51.19 -123.60 REMARK 500 ASP B 283 -167.82 -162.15 REMARK 500 ASP B 380 -166.67 -101.33 REMARK 500 ALA C 97 -151.28 -115.77 REMARK 500 SER C 107 56.53 -141.06 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-50502 RELATED DB: EMDB REMARK 900 LYSOSOMAL TRANSPORTING COMPLEX OF BETA-GLUCOCEREBROSIDASE (GCASE) REMARK 900 AND LYSOSOMAL INTEGRAL MEMBRANE PROTEIN 2 (LIMP-2) WITH BOUND PRO- REMARK 900 MACROBODIES REMARK 900 RELATED ID: EMD-50936 RELATED DB: EMDB REMARK 900 CONSENSUS MAP OF COMPLEX REMARK 900 RELATED ID: EMD-50937 RELATED DB: EMDB REMARK 900 CONSTITUENT EM MAP: GCASE-FOCUSED LOCAL REFINEMENT MAP REMARK 900 RELATED ID: EMD-50938 RELATED DB: EMDB REMARK 900 CONSTITUENT EM MAP: LIMP-2-FOCUSED LOCAL REFINEMENT MAP DBREF 9FJF A 39 429 UNP Q14108 SCRB2_HUMAN 39 429 DBREF 9FJF B 1 497 UNP P04062 GLCM_HUMAN 40 536 DBREF 9FJF C 1 130 PDB 9FJF 9FJF 1 130 DBREF 9FJF D 1 121 PDB 9FJF 9FJF 1 121 SEQRES 1 A 391 LYS LYS ILE VAL LEU ARG ASN GLY THR GLU ALA PHE ASP SEQRES 2 A 391 SER TRP GLU LYS PRO PRO LEU PRO VAL TYR THR GLN PHE SEQRES 3 A 391 TYR PHE PHE ASN VAL THR ASN PRO GLU GLU ILE LEU ARG SEQRES 4 A 391 GLY GLU THR PRO ARG VAL GLU GLU VAL GLY PRO TYR THR SEQRES 5 A 391 TYR ARG GLU LEU ARG ASN LYS ALA ASN ILE GLN PHE GLY SEQRES 6 A 391 ASP ASN GLY THR THR ILE SER ALA VAL SER ASN LYS ALA SEQRES 7 A 391 TYR VAL PHE GLU ARG ASP GLN SER VAL GLY ASP PRO LYS SEQRES 8 A 391 ILE ASP LEU ILE ARG THR LEU ASN ILE PRO VAL LEU THR SEQRES 9 A 391 VAL ILE GLU TRP SER GLN VAL HIS PHE LEU ARG GLU ILE SEQRES 10 A 391 ILE GLU ALA MET LEU LYS ALA TYR GLN GLN LYS LEU PHE SEQRES 11 A 391 VAL THR HIS THR VAL ASP GLU LEU LEU TRP GLY TYR LYS SEQRES 12 A 391 ASP GLU ILE LEU SER LEU ILE HIS VAL PHE ARG PRO ASP SEQRES 13 A 391 ILE SER PRO TYR PHE GLY LEU PHE TYR GLU LYS ASN GLY SEQRES 14 A 391 THR ASN ASP GLY ASP TYR VAL PHE LEU THR GLY GLU ASP SEQRES 15 A 391 SER TYR LEU ASN PHE THR LYS ILE VAL GLU TRP ASN GLY SEQRES 16 A 391 LYS THR SER LEU ASP TRP TRP ILE THR ASP LYS CYS ASN SEQRES 17 A 391 MET ILE ASN GLY THR ASP GLY ASP SER PHE HIS PRO LEU SEQRES 18 A 391 ILE THR LYS ASP GLU VAL LEU TYR VAL PHE PRO SER ASP SEQRES 19 A 391 PHE CYS ARG SER VAL TYR ILE THR PHE SER ASP TYR GLU SEQRES 20 A 391 SER VAL GLN GLY LEU PRO ALA PHE ARG TYR LYS VAL PRO SEQRES 21 A 391 ALA GLU ILE LEU ALA ASN THR SER ASP ASN ALA GLY PHE SEQRES 22 A 391 CYS ILE PRO GLU GLY ASN CYS LEU GLY SER GLY VAL LEU SEQRES 23 A 391 ASN VAL SER ILE CYS LYS ASN GLY ALA PRO ILE ILE MET SEQRES 24 A 391 SER PHE PRO HIS PHE TYR GLN ALA ASP GLU ARG PHE VAL SEQRES 25 A 391 SER ALA ILE GLU GLY MET HIS PRO ASN GLN GLU ASP HIS SEQRES 26 A 391 GLU THR PHE VAL ASP ILE ASN PRO LEU THR GLY ILE ILE SEQRES 27 A 391 LEU LYS ALA ALA LYS ARG PHE GLN ILE ASN ILE TYR VAL SEQRES 28 A 391 LYS LYS LEU ASP ASP PHE VAL GLU THR GLY ASP ILE ARG SEQRES 29 A 391 THR MET VAL PHE PRO VAL MET TYR LEU ASN GLU SER VAL SEQRES 30 A 391 HIS ILE ASP LYS GLU THR ALA SER ARG LEU LYS SER MET SEQRES 31 A 391 ILE SEQRES 1 B 497 ALA ARG PRO CYS ILE PRO LYS SER PHE GLY TYR SER SER SEQRES 2 B 497 VAL VAL CYS VAL CYS ASN ALA THR TYR CYS ASP SER PHE SEQRES 3 B 497 ASP PRO PRO THR PHE PRO ALA LEU GLY THR PHE SER ARG SEQRES 4 B 497 TYR GLU SER THR ARG SER GLY ARG ARG MET GLU LEU SER SEQRES 5 B 497 MET GLY PRO ILE GLN ALA ASN HIS THR GLY THR GLY LEU SEQRES 6 B 497 LEU LEU THR LEU GLN PRO GLU GLN LYS PHE GLN LYS VAL SEQRES 7 B 497 LYS GLY PHE GLY GLY ALA MET THR ASP ALA ALA ALA LEU SEQRES 8 B 497 ASN ILE LEU ALA LEU SER PRO PRO ALA GLN ASN LEU LEU SEQRES 9 B 497 LEU LYS SER TYR PHE SER GLU GLU GLY ILE GLY TYR ASN SEQRES 10 B 497 ILE ILE ARG VAL PRO MET ALA SER CYS ASP PHE SER ILE SEQRES 11 B 497 ARG THR TYR THR TYR ALA ASP THR PRO ASP ASP PHE GLN SEQRES 12 B 497 LEU HIS ASN PHE SER LEU PRO GLU GLU ASP THR LYS LEU SEQRES 13 B 497 LYS ILE PRO LEU ILE HIS ARG ALA LEU GLN LEU ALA GLN SEQRES 14 B 497 ARG PRO VAL SER LEU LEU ALA SER PRO TRP THR SER PRO SEQRES 15 B 497 THR TRP LEU LYS THR ASN GLY ALA VAL ASN GLY LYS GLY SEQRES 16 B 497 SER LEU LYS GLY GLN PRO GLY ASP ILE TYR HIS GLN THR SEQRES 17 B 497 TRP ALA ARG TYR PHE VAL LYS PHE LEU ASP ALA TYR ALA SEQRES 18 B 497 GLU HIS LYS LEU GLN PHE TRP ALA VAL THR ALA GLU ASN SEQRES 19 B 497 GLU PRO SER ALA GLY LEU LEU SER GLY TYR PRO PHE GLN SEQRES 20 B 497 CYS LEU GLY PHE THR PRO GLU HIS GLN ARG ASP PHE ILE SEQRES 21 B 497 ALA ARG ASP LEU GLY PRO THR LEU ALA ASN SER THR HIS SEQRES 22 B 497 HIS ASN VAL ARG LEU LEU MET LEU ASP ASP GLN ARG LEU SEQRES 23 B 497 LEU LEU PRO HIS TRP ALA LYS VAL VAL LEU THR ASP PRO SEQRES 24 B 497 GLU ALA ALA LYS TYR VAL HIS GLY ILE ALA VAL HIS TRP SEQRES 25 B 497 TYR LEU ASP PHE LEU ALA PRO ALA LYS ALA THR LEU GLY SEQRES 26 B 497 GLU THR HIS ARG LEU PHE PRO ASN THR MET LEU PHE ALA SEQRES 27 B 497 SER GLU ALA CYS VAL GLY SER LYS PHE TRP GLU GLN SER SEQRES 28 B 497 VAL ARG LEU GLY SER TRP ASP ARG GLY MET GLN TYR SER SEQRES 29 B 497 HIS SER ILE ILE THR ASN LEU LEU TYR HIS VAL VAL GLY SEQRES 30 B 497 TRP THR ASP TRP ASN LEU ALA LEU ASN PRO GLU GLY GLY SEQRES 31 B 497 PRO ASN TRP VAL ARG ASN PHE VAL ASP SER PRO ILE ILE SEQRES 32 B 497 VAL ASP ILE THR LYS ASP THR PHE TYR LYS GLN PRO MET SEQRES 33 B 497 PHE TYR HIS LEU GLY HIS PHE SER LYS PHE ILE PRO GLU SEQRES 34 B 497 GLY SER GLN ARG VAL GLY LEU VAL ALA SER GLN LYS ASN SEQRES 35 B 497 ASP LEU ASP ALA VAL ALA LEU MET HIS PRO ASP GLY SER SEQRES 36 B 497 ALA VAL VAL VAL VAL LEU ASN ARG SER SER LYS ASP VAL SEQRES 37 B 497 PRO LEU THR ILE LYS ASP PRO ALA VAL GLY PHE LEU GLU SEQRES 38 B 497 THR ILE SER PRO GLY TYR SER ILE HIS THR TYR LEU TRP SEQRES 39 B 497 ARG ARG GLN SEQRES 1 C 130 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 130 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 C 130 PHE THR LEU ASP TYR TYR ALA ILE GLY TRP PHE ARG GLN SEQRES 4 C 130 ALA PRO GLY LYS GLU ARG GLU GLY VAL SER CYS ILE SER SEQRES 5 C 130 SER SER ASP GLY SER THR TYR TYR ALA ASP SER ALA LYS SEQRES 6 C 130 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 C 130 VAL TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 C 130 ALA VAL TYR TYR CYS ALA THR ASP ARG GLY GLN CYS THR SEQRES 9 C 130 TYR TYR SER SER GLY TYR TYR ARG ASP LEU ARG TRP TYR SEQRES 10 C 130 ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL PRO PRO SEQRES 1 D 121 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 121 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 121 SER ILE PHE SER ILE ASN THR MET GLY TRP TYR ARG GLN SEQRES 4 D 121 ALA PRO GLY LYS GLU ARG GLU MET VAL ALA TYR ILE ILE SEQRES 5 D 121 THR PHE GLY SER THR ASN TYR ALA ASP SER VAL LYS GLY SEQRES 6 D 121 ARG PHE THR ILE SER GLY ASP ASN ALA ASN ASN THR MET SEQRES 7 D 121 TRP LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 D 121 VAL TYR TYR CYS TYR ALA ALA ILE ARG PRO THR ASP SER SEQRES 9 D 121 SER THR TYR THR SER TYR TRP GLY GLN GLY THR GLN VAL SEQRES 10 D 121 THR VAL PRO PRO HET NAG E 1 14 HET NAG E 2 14 HET BMA E 3 11 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET NAG H 1 14 HET NAG H 2 14 HET NAG I 1 14 HET NAG I 2 14 HET BMA I 3 11 HET MAN I 4 11 HET MAN I 5 11 HET NAG J 1 14 HET NAG J 2 14 HET NAG A 501 14 HET NAG A 502 14 HET NAG A 503 14 HET NAG A 504 14 HET MES A 505 12 HET NAG B 501 14 HET NAG B 502 14 HET NAG B 503 14 HET MES B 504 12 HET MES B 505 12 HET MES B 506 12 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM MAN ALPHA-D-MANNOPYRANOSE HETNAM MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID 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 FORMUL 5 NAG 19(C8 H15 N O6) FORMUL 5 BMA 2(C6 H12 O6) FORMUL 9 MAN 2(C6 H12 O6) FORMUL 15 MES 4(C6 H13 N O4 S) FORMUL 22 HOH *27(H2 O) HELIX 1 AA1 THR A 47 LYS A 55 1 9 HELIX 2 AA2 PRO A 72 ARG A 77 1 6 HELIX 3 AA3 ASP A 127 ILE A 130 5 4 HELIX 4 AA4 ASN A 137 VAL A 149 1 13 HELIX 5 AA5 LEU A 152 TYR A 163 1 12 HELIX 6 AA6 VAL A 173 GLY A 179 1 7 HELIX 7 AA7 GLU A 183 VAL A 190 1 8 HELIX 8 AA8 SER A 327 ASN A 331 5 5 HELIX 9 AA9 PHE A 339 TYR A 343 5 5 HELIX 10 AB1 ASP A 346 ILE A 353 1 8 HELIX 11 AB2 ASP A 418 ILE A 429 1 12 HELIX 12 AB3 THR B 86 LEU B 94 1 9 HELIX 13 AB4 SER B 97 PHE B 109 1 13 HELIX 14 AB5 PRO B 150 LYS B 157 1 8 HELIX 15 AB6 LYS B 157 LEU B 165 1 9 HELIX 16 AB7 GLN B 166 ALA B 168 5 3 HELIX 17 AB8 ASP B 203 ALA B 210 1 8 HELIX 18 AB9 ARG B 211 ALA B 221 1 11 HELIX 19 AC1 GLU B 222 LYS B 224 5 3 HELIX 20 AC2 GLU B 254 ASP B 263 1 10 HELIX 21 AC3 ASP B 263 SER B 271 1 9 HELIX 22 AC4 LEU B 287 LEU B 296 1 10 HELIX 23 AC5 THR B 323 PHE B 331 1 9 HELIX 24 AC6 TRP B 357 LEU B 371 1 15 HELIX 25 AC7 LEU B 372 HIS B 374 5 3 HELIX 26 AC8 GLN B 414 ILE B 427 1 14 HELIX 27 AC9 THR C 28 TYR C 32 5 5 SHEET 1 AA1 8 VAL A 83 VAL A 86 0 SHEET 2 AA1 8 VAL A 60 VAL A 69 -1 N ASN A 68 O GLU A 84 SHEET 3 AA1 8 MET A 404 VAL A 415 -1 O TYR A 410 N TYR A 65 SHEET 4 AA1 8 ILE A 376 VAL A 389 -1 N ILE A 387 O PHE A 406 SHEET 5 AA1 8 PHE A 366 ILE A 369 -1 N ASP A 368 O LYS A 378 SHEET 6 AA1 8 LEU A 290 LYS A 296 -1 N TYR A 295 O VAL A 367 SHEET 7 AA1 8 VAL A 277 VAL A 287 -1 N VAL A 287 O LEU A 290 SHEET 8 AA1 8 LEU A 266 VAL A 268 -1 N LEU A 266 O ILE A 279 SHEET 1 AA2 8 TYR A 213 PHE A 215 0 SHEET 2 AA2 8 THR A 108 PHE A 119 -1 N ILE A 109 O PHE A 215 SHEET 3 AA2 8 TYR A 91 GLY A 103 -1 N ARG A 92 O VAL A 118 SHEET 4 AA2 8 VAL A 60 VAL A 69 -1 N THR A 62 O TYR A 91 SHEET 5 AA2 8 MET A 404 VAL A 415 -1 O TYR A 410 N TYR A 65 SHEET 6 AA2 8 ILE A 376 VAL A 389 -1 N ILE A 387 O PHE A 406 SHEET 7 AA2 8 ILE A 336 MET A 337 -1 N ILE A 336 O ASN A 386 SHEET 8 AA2 8 LEU A 324 ASN A 325 -1 N LEU A 324 O MET A 337 SHEET 1 AA3 2 LEU A 132 THR A 135 0 SHEET 2 AA3 2 VAL A 169 THR A 172 -1 O HIS A 171 N ILE A 133 SHEET 1 AA4 2 TYR A 180 LYS A 181 0 SHEET 2 AA4 2 TYR A 198 PHE A 199 -1 O PHE A 199 N TYR A 180 SHEET 1 AA5 4 VAL B 17 ASN B 19 0 SHEET 2 AA5 4 THR B 410 TYR B 412 -1 O PHE B 411 N CYS B 18 SHEET 3 AA5 4 ILE B 402 ASP B 405 -1 N ILE B 403 O TYR B 412 SHEET 4 AA5 4 ALA B 384 LEU B 385 1 N LEU B 385 O VAL B 404 SHEET 1 AA6 6 GLU B 50 PRO B 55 0 SHEET 2 AA6 6 THR B 36 THR B 43 -1 N ARG B 39 O SER B 52 SHEET 3 AA6 6 SER B 488 TRP B 494 -1 O ILE B 489 N SER B 42 SHEET 4 AA6 6 ALA B 456 LEU B 461 -1 N VAL B 458 O TYR B 492 SHEET 5 AA6 6 ASP B 445 MET B 450 -1 N ASP B 445 O LEU B 461 SHEET 6 AA6 6 GLN B 432 ARG B 433 -1 N GLN B 432 O MET B 450 SHEET 1 AA7 4 LEU B 436 VAL B 437 0 SHEET 2 AA7 4 LEU B 66 LEU B 69 -1 N THR B 68 O VAL B 437 SHEET 3 AA7 4 VAL B 468 ASP B 474 1 O THR B 471 N LEU B 67 SHEET 4 AA7 4 GLY B 478 SER B 484 -1 O GLY B 478 N ASP B 474 SHEET 1 AA8 4 SER B 173 SER B 177 0 SHEET 2 AA8 4 ILE B 118 PRO B 122 1 N ILE B 119 O SER B 173 SHEET 3 AA8 4 PHE B 81 ALA B 84 1 N GLY B 83 O ILE B 118 SHEET 4 AA8 4 TRP B 378 THR B 379 1 O TRP B 378 N GLY B 82 SHEET 1 AA9 2 ILE B 308 HIS B 311 0 SHEET 2 AA9 2 LEU B 336 GLU B 340 1 O PHE B 337 N VAL B 310 SHEET 1 AB1 4 GLN C 3 SER C 7 0 SHEET 2 AB1 4 SER C 21 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AB1 4 THR C 78 GLN C 82 -1 O VAL C 79 N CYS C 22 SHEET 4 AB1 4 THR C 69 ASP C 73 -1 N SER C 71 O TYR C 80 SHEET 1 AB2 4 GLU C 46 GLY C 47 0 SHEET 2 AB2 4 TRP C 36 GLN C 39 -1 N ARG C 38 O GLU C 46 SHEET 3 AB2 4 ALA C 92 CYS C 96 -1 O TYR C 95 N PHE C 37 SHEET 4 AB2 4 GLY C 123 VAL C 126 -1 O THR C 124 N TYR C 94 SHEET 1 AB3 2 SER C 49 CYS C 50 0 SHEET 2 AB3 2 TYR C 59 TYR C 60 -1 O TYR C 59 N CYS C 50 SHEET 1 AB4 3 LEU D 20 ALA D 23 0 SHEET 2 AB4 3 THR D 77 GLN D 81 -1 O MET D 78 N CYS D 22 SHEET 3 AB4 3 THR D 68 ASP D 72 -1 N SER D 70 O TRP D 79 SHEET 1 AB5 5 THR D 57 TYR D 59 0 SHEET 2 AB5 5 GLU D 46 ILE D 52 -1 N TYR D 50 O ASN D 58 SHEET 3 AB5 5 THR D 33 GLN D 39 -1 N ARG D 38 O GLU D 46 SHEET 4 AB5 5 VAL D 92 ALA D 97 -1 O VAL D 92 N GLN D 39 SHEET 5 AB5 5 THR D 115 GLN D 116 -1 O THR D 115 N TYR D 93 SSBOND 1 CYS A 274 CYS A 329 1555 1555 2.04 SSBOND 2 CYS A 312 CYS A 318 1555 1555 2.04 SSBOND 3 CYS C 22 CYS C 96 1555 1555 2.03 SSBOND 4 CYS C 50 CYS C 103 1555 1555 2.03 SSBOND 5 CYS D 22 CYS D 95 1555 1555 2.03 LINK ND2 ASN A 45 C1 NAG A 501 1555 1555 1.44 LINK ND2 ASN A 68 C1 NAG E 1 1555 1555 1.44 LINK ND2 ASN A 105 C1 NAG A 504 1555 1555 1.44 LINK ND2 ASN A 206 C1 NAG F 1 1555 1555 1.45 LINK ND2 ASN A 224 C1 NAG A 502 1555 1555 1.45 LINK ND2 ASN A 249 C1 NAG G 1 1555 1555 1.43 LINK ND2 ASN A 304 C1 NAG A 503 1555 1555 1.45 LINK ND2 ASN A 325 C1 NAG H 1 1555 1555 1.45 LINK ND2 ASN A 412 C1 NAG I 1 1555 1555 1.44 LINK ND2 ASN B 19 C1 NAG J 1 1555 1555 1.46 LINK ND2 ASN B 59 C1 NAG B 501 1555 1555 1.44 LINK ND2 ASN B 146 C1 NAG B 502 1555 1555 1.44 LINK ND2 ASN B 270 C1 NAG B 503 1555 1555 1.44 LINK O4 NAG E 1 C1 NAG E 2 1555 1555 1.44 LINK O4 NAG E 2 C1 BMA E 3 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.43 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.45 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.45 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.46 LINK O4 NAG I 2 C1 BMA I 3 1555 1555 1.45 LINK O3 BMA I 3 C1 MAN I 4 1555 1555 1.45 LINK O6 BMA I 3 C1 MAN I 5 1555 1555 1.44 LINK O4 NAG J 1 C1 NAG J 2 1555 1555 1.44 CISPEP 1 ILE A 313 PRO A 314 0 -4.98 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 1 1 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 1.000000 0.000000 0.000000 0.00000 SCALE2 0.000000 1.000000 0.000000 0.00000 SCALE3 0.000000 0.000000 1.000000 0.00000