HEADER TRANSFERASE/IMMUNE SYSTEM 15-OCT-25 9YQ4 TITLE CHLORELLA VIRUS HYALURONAN SYNTHASE BOUND TO A PROOFREADING UDP-GLCA COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYALURONAN SYNTHASE; COMPND 3 CHAIN: A; COMPND 4 EC: 2.4.1.212; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: NANOBODY NB872; COMPND 8 CHAIN: B; COMPND 9 ENGINEERED: YES; COMPND 10 MOL_ID: 3; COMPND 11 MOLECULE: NANOBODY NB881; COMPND 12 CHAIN: C; COMPND 13 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: PARAMECIUM BURSARIA CHLORELLA VIRUS CZ-2; SOURCE 3 ORGANISM_TAXID: 1278251; SOURCE 4 GENE: CZ-2_118R; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 6 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 9 ORGANISM_COMMON: LLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 12 EXPRESSION_SYSTEM_TAXID: 469008; SOURCE 13 MOL_ID: 3; SOURCE 14 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 15 ORGANISM_COMMON: LLAMA; SOURCE 16 ORGANISM_TAXID: 9844; SOURCE 17 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3); SOURCE 18 EXPRESSION_SYSTEM_TAXID: 469008 KEYWDS GLYCOSYLTRANSFERASE, MEMBRANE PROTEIN, HYALURONAN SYNTHASE, KEYWDS 2 SUBSTRATE, TRANSFERASE-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Z.STEPHENS,J.ZIMMER REVDAT 1 10-DEC-25 9YQ4 0 JRNL AUTH Z.STEPHENS,J.KARASINSKA,J.ZIMMER JRNL TITL INSIGHTS INTO SUBSTRATE BINDING AND UTILIZATION BY JRNL TITL 2 HYALURONAN SYNTHASE. JRNL REF BIORXIV 2025 JRNL REFN ISSN 2692-8205 JRNL PMID 41280022 JRNL DOI 10.1101/2025.10.17.683186 REMARK 2 REMARK 2 RESOLUTION. 3.30 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : CRYOSPARC, PHENIX, CRYOSPARC REMARK 3 RECONSTRUCTION SCHEMA : NULL REMARK 3 REMARK 3 EM MAP-MODEL FITTING AND REFINEMENT REMARK 3 PDB ENTRY : NULL REMARK 3 REFINEMENT SPACE : NULL REMARK 3 REFINEMENT PROTOCOL : NULL REMARK 3 REFINEMENT TARGET : NULL REMARK 3 OVERALL ANISOTROPIC B VALUE : NULL REMARK 3 REMARK 3 FITTING PROCEDURE : NULL 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) : 3.300 REMARK 3 NUMBER OF PARTICLES : 64146 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 9YQ4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 16-OCT-25. REMARK 100 THE DEPOSITION ID IS D_1000301077. 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 : TERNARY COMPLEX OF CVHAS, NB872 REMARK 245 AND NB881 REMARK 245 SAMPLE CONCENTRATION (MG ML-1) : NULL REMARK 245 SAMPLE SUPPORT DETAILS : NULL REMARK 245 SAMPLE VITRIFICATION DETAILS : NULL REMARK 245 SAMPLE BUFFER : NULL REMARK 245 PH : 7.50 REMARK 245 SAMPLE DETAILS : NULL REMARK 245 REMARK 245 DATA ACQUISITION REMARK 245 DATE OF EXPERIMENT : NULL REMARK 245 NUMBER OF MICROGRAPHS-IMAGES : NULL REMARK 245 TEMPERATURE (KELVIN) : NULL REMARK 245 MICROSCOPE MODEL : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1000.00 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 : NULL REMARK 245 CALIBRATED MAGNIFICATION : NULL REMARK 245 SOURCE : FIELD EMISSION GUN REMARK 245 ACCELERATION VOLTAGE (KV) : 300 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: TRIMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C 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 MET A 0 REMARK 465 GLY A 1 REMARK 465 THR A 2 REMARK 465 SER A 3 REMARK 465 TRP A 4 REMARK 465 ARG A 5 REMARK 465 THR A 6 REMARK 465 ILE A 7 REMARK 465 VAL A 8 REMARK 465 SER A 9 REMARK 465 ALA A 10 REMARK 465 ASN A 11 REMARK 465 LEU A 12 REMARK 465 PHE A 13 REMARK 465 ALA A 14 REMARK 465 VAL A 15 REMARK 465 GLY A 16 REMARK 465 GLY A 17 REMARK 465 ALA A 18 REMARK 465 LEU A 19 REMARK 465 LEU A 20 REMARK 465 MET A 21 REMARK 465 LEU A 22 REMARK 465 ALA A 23 REMARK 465 PRO A 24 REMARK 465 ALA A 25 REMARK 465 ILE A 26 REMARK 465 VAL A 27 REMARK 465 GLY A 28 REMARK 465 TYR A 29 REMARK 465 VAL A 30 REMARK 465 PHE A 31 REMARK 465 GLN A 32 REMARK 465 TRP A 33 REMARK 465 ASN A 34 REMARK 465 ILE A 35 REMARK 465 GLY A 36 REMARK 465 VAL A 37 REMARK 465 ASP A 451 REMARK 465 ILE A 452 REMARK 465 ALA A 453 REMARK 465 TRP A 454 REMARK 465 GLY A 455 REMARK 465 THR A 456 REMARK 465 ARG A 457 REMARK 465 GLY A 458 REMARK 465 GLY A 459 REMARK 465 ASN A 460 REMARK 465 ALA A 461 REMARK 465 LYS A 462 REMARK 465 MET A 463 REMARK 465 THR A 464 REMARK 465 ILE A 465 REMARK 465 GLY A 466 REMARK 465 ALA A 467 REMARK 465 ARG A 468 REMARK 465 VAL A 469 REMARK 465 TRP A 470 REMARK 465 LEU A 471 REMARK 465 ASN A 553 REMARK 465 ALA A 554 REMARK 465 SER A 555 REMARK 465 GLU A 556 REMARK 465 ASN A 557 REMARK 465 ALA A 558 REMARK 465 PRO A 559 REMARK 465 GLU A 560 REMARK 465 VAL A 561 REMARK 465 LEU A 562 REMARK 465 GLU A 563 REMARK 465 HIS A 564 REMARK 465 HIS A 565 REMARK 465 HIS A 566 REMARK 465 HIS A 567 REMARK 465 HIS A 568 REMARK 465 HIS A 569 REMARK 465 HIS A 570 REMARK 465 HIS A 571 REMARK 465 HIS A 572 REMARK 465 HIS A 573 REMARK 465 HIS B 125 REMARK 465 HIS B 126 REMARK 465 HIS B 127 REMARK 465 HIS B 128 REMARK 465 HIS B 129 REMARK 465 HIS B 130 REMARK 465 GLU B 131 REMARK 465 PRO B 132 REMARK 465 GLU B 133 REMARK 465 ALA B 134 REMARK 465 ALA C 60A REMARK 465 SER C 122 REMARK 465 SER C 123 REMARK 465 HIS C 124 REMARK 465 HIS C 125 REMARK 465 HIS C 126 REMARK 465 HIS C 127 REMARK 465 HIS C 128 REMARK 465 HIS C 129 REMARK 465 GLU C 130 REMARK 465 PRO C 131 REMARK 465 GLU C 132 REMARK 465 ALA C 133 REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT REMARK 500 REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT. REMARK 500 REMARK 500 ATM1 RES C SSEQI ATM2 RES C SSEQI DISTANCE REMARK 500 OH TYR A 432 OH TYR A 517 2.12 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 RES CSSEQI ATM2 DEVIATION REMARK 500 PRO A 286 CB PRO A 286 CG 0.471 REMARK 500 PRO A 286 CG PRO A 286 CD -1.007 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: COVALENT BOND ANGLES REMARK 500 REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 STANDARD TABLE: REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1) REMARK 500 REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999 REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996 REMARK 500 REMARK 500 M RES CSSEQI ATM1 ATM2 ATM3 REMARK 500 PRO A 286 N - CA - CB ANGL. DEV. = -9.3 DEGREES REMARK 500 PRO A 286 CA - CB - CG ANGL. DEV. = -30.4 DEGREES REMARK 500 PRO A 286 N - CD - CG ANGL. DEV. = -61.3 DEGREES REMARK 500 ASP B 104 CB - CG - OD2 ANGL. DEV. = 5.7 DEGREES REMARK 500 REMARK 500 REMARK: NULL 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 A 81 -38.97 -130.58 REMARK 500 GLU A 93 75.01 -100.91 REMARK 500 ASP A 94 80.94 51.84 REMARK 500 PRO A 95 -38.23 -36.31 REMARK 500 LYS A 129 43.42 -86.43 REMARK 500 ASN A 139 -175.07 -173.53 REMARK 500 ASN A 141 58.79 -95.34 REMARK 500 LYS A 144 73.68 -161.03 REMARK 500 SER A 165 52.77 -95.93 REMARK 500 ALA A 188 46.47 -90.35 REMARK 500 SER A 189 -39.72 -130.82 REMARK 500 ASP A 203 57.81 -98.88 REMARK 500 ASN A 209 58.61 -96.54 REMARK 500 PHE A 252 -67.67 -93.81 REMARK 500 PHE A 292 -61.28 -93.09 REMARK 500 LEU A 422 -6.47 68.55 REMARK 500 ASN A 497 58.23 -97.69 REMARK 500 LYS B 43 -2.47 69.73 REMARK 500 VAL B 48 -59.43 -122.25 REMARK 500 GLU B 55 -3.62 69.72 REMARK 500 THR B 90 99.66 -69.26 REMARK 500 ALA C 14 -144.94 55.05 REMARK 500 SER C 62 -4.34 68.88 REMARK 500 ASN C 73 -0.71 63.81 REMARK 500 TYR C 104 31.06 -94.74 REMARK 500 REMARK 500 REMARK: NULL REMARK 620 REMARK 620 METAL COORDINATION REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE): REMARK 620 REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL REMARK 620 MN A 602 MN REMARK 620 N RES CSSEQI ATOM REMARK 620 1 GLU A 93 OE1 REMARK 620 2 ASP A 203 OD2 82.2 REMARK 620 N 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-73323 RELATED DB: EMDB REMARK 900 CHLORELLA VIRUS HYALURONAN SYNTHASE BOUND TO A PROOFREADING UDP-GLCA DBREF 9YQ4 A 2 561 UNP M1H2Q1 M1H2Q1_9PHYC 2 561 DBREF 9YQ4 B 1 134 PDB 9YQ4 9YQ4 1 134 DBREF 9YQ4 C 1 133 PDB 9YQ4 9YQ4 1 133 SEQADV 9YQ4 MET A 0 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 GLY A 1 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 ASN A 302 UNP M1H2Q1 ASP 302 CONFLICT SEQADV 9YQ4 LEU A 562 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 GLU A 563 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 564 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 565 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 566 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 567 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 568 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 569 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 570 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 571 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 572 UNP M1H2Q1 EXPRESSION TAG SEQADV 9YQ4 HIS A 573 UNP M1H2Q1 EXPRESSION TAG SEQRES 1 A 574 MET GLY THR SER TRP ARG THR ILE VAL SER ALA ASN LEU SEQRES 2 A 574 PHE ALA VAL GLY GLY ALA LEU LEU MET LEU ALA PRO ALA SEQRES 3 A 574 ILE VAL GLY TYR VAL PHE GLN TRP ASN ILE GLY VAL SER SEQRES 4 A 574 ALA VAL TRP GLY ILE SER VAL TYR GLY VAL PHE VAL LEU SEQRES 5 A 574 GLY PHE TYR ILE ALA GLN ILE VAL PHE SER GLU PHE ASN SEQRES 6 A 574 ARG MET ARG LEU SER ASP TRP ILE SER LEU ARG PRO ASP SEQRES 7 A 574 ASN TRP ASN ALA THR ARG VAL ALA VAL ILE ILE ALA GLY SEQRES 8 A 574 TYR ARG GLU ASP PRO PHE MET PHE LYS LYS CYS LEU GLU SEQRES 9 A 574 SER VAL ARG ASP SER GLU TYR GLY ASN VAL ALA ARG LEU SEQRES 10 A 574 ILE CYS VAL ILE ASP GLY ASP GLU GLU GLU ASP LEU LYS SEQRES 11 A 574 MET ALA GLU ILE TYR LYS GLN VAL TYR ASN ASP ASN VAL SEQRES 12 A 574 LYS LYS PRO GLY VAL VAL LEU CYS GLU SER GLU ASN LYS SEQRES 13 A 574 ASN GLY SER THR ILE ASP SER ASP VAL SER LYS ASN ILE SEQRES 14 A 574 CYS ILE LEU GLN PRO HIS ARG GLY LYS ARG GLU SER LEU SEQRES 15 A 574 TYR THR GLY PHE GLN LEU ALA SER MET ASP PRO SER VAL SEQRES 16 A 574 HIS ALA VAL VAL LEU ILE ASP SER ASP THR VAL LEU GLU SEQRES 17 A 574 LYS ASN ALA ILE LEU GLU VAL VAL TYR PRO LEU SER CYS SEQRES 18 A 574 ASP PRO ASN ILE LYS ALA VAL ALA GLY GLU CYS LYS ILE SEQRES 19 A 574 TRP ASN THR ASP THR ILE LEU SER MET LEU VAL SER TRP SEQRES 20 A 574 ARG TYR PHE SER ALA PHE ASN VAL GLU ARG GLY ALA GLN SEQRES 21 A 574 SER LEU TRP LYS THR VAL GLN CYS VAL GLY GLY PRO LEU SEQRES 22 A 574 GLY ALA TYR THR ILE ASP ILE ILE ASN GLU ILE LYS ASP SEQRES 23 A 574 PRO TRP ILE THR GLN THR PHE LEU GLY ASN LYS CYS THR SEQRES 24 A 574 TYR GLY ASP ASN ARG ARG LEU THR ASN GLU VAL LEU MET SEQRES 25 A 574 ARG GLY LYS LYS ILE VAL TYR THR PRO PHE ALA VAL GLY SEQRES 26 A 574 TRP SER ASP SER PRO THR ASN VAL MET ARG TYR ILE VAL SEQRES 27 A 574 GLN GLN THR ARG TRP SER LYS SER TRP CYS ARG GLU ILE SEQRES 28 A 574 TRP TYR THR LEU GLY SER ALA TRP LYS HIS GLY PHE SER SEQRES 29 A 574 GLY ILE TYR LEU ALA PHE GLU CYS MET TYR GLN ILE MET SEQRES 30 A 574 TYR PHE PHE LEU VAL MET TYR LEU PHE SER TYR ILE ALA SEQRES 31 A 574 ILE LYS ALA ASP ILE ARG ALA GLN THR ALA THR VAL LEU SEQRES 32 A 574 VAL SER THR LEU VAL THR ILE ILE LYS SER SER TYR LEU SEQRES 33 A 574 ALA LEU ARG ALA LYS ASN LEU LYS ALA PHE TYR PHE VAL SEQRES 34 A 574 LEU TYR THR TYR VAL TYR PHE PHE CYS MET ILE PRO ALA SEQRES 35 A 574 ARG ILE THR ALA MET PHE THR MET PHE ASP ILE ALA TRP SEQRES 36 A 574 GLY THR ARG GLY GLY ASN ALA LYS MET THR ILE GLY ALA SEQRES 37 A 574 ARG VAL TRP LEU TRP ALA LYS GLN PHE LEU ILE THR TYR SEQRES 38 A 574 MET TRP TRP ALA GLY VAL LEU ALA ALA GLY VAL TYR SER SEQRES 39 A 574 ILE VAL ASP ASN TRP TYR PHE ASP TRP ALA ASP ILE GLN SEQRES 40 A 574 TYR ARG PHE ALA LEU VAL GLY ILE CYS SER TYR LEU VAL SEQRES 41 A 574 PHE VAL SER ILE VAL LEU VAL ILE TYR LEU ILE GLY LYS SEQRES 42 A 574 ILE THR THR TRP ASN TYR THR PRO LEU GLN LYS GLU LEU SEQRES 43 A 574 ILE GLU GLU ARG TYR LEU HIS ASN ALA SER GLU ASN ALA SEQRES 44 A 574 PRO GLU VAL LEU GLU HIS HIS HIS HIS HIS HIS HIS HIS SEQRES 45 A 574 HIS HIS SEQRES 1 B 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 B 134 ALA GLY GLY SER LEU LYS VAL SER CYS ALA ALA SER GLY SEQRES 3 B 134 ARG ALA PHE LYS THR TYR ARG MET ALA TRP PHE ARG GLN SEQRES 4 B 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL SER GLY ILE SER SEQRES 5 B 134 ALA LEU GLU THR THR TYR TYR ALA ASP SER VAL LYS GLY SEQRES 6 B 134 ARG PHE THR ILE SER ARG ASP ASN THR LYS ASN THR VAL SEQRES 7 B 134 SER LEU GLN MET ASP SER LEU LYS PRO GLU ASP THR ALA SEQRES 8 B 134 VAL TYR TYR CYS ALA ALA ARG ARG TYR GLY GLY THR ASP SEQRES 9 B 134 TYR THR THR THR GLY SER TYR ASP TYR TRP GLY GLN GLY SEQRES 10 B 134 THR GLN VAL THR VAL SER SER HIS HIS HIS HIS HIS HIS SEQRES 11 B 134 GLU PRO GLU ALA SEQRES 1 C 134 GLN VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 C 134 ALA GLY GLY SER LEU ARG LEU ALA CYS ALA ALA SER GLY SEQRES 3 C 134 ARG ILE PHE SER SER ASP THR LEU ALA TRP PHE ARG ARG SEQRES 4 C 134 ALA PRO GLY LYS GLU ARG GLU PHE VAL ALA ALA SER ARG SEQRES 5 C 134 TRP SER GLY GLY GLY THR ASP TYR ALA ASP SER VAL LYS SEQRES 6 C 134 GLY ARG PHE THR PHE SER ARG ASP ASN THR PHE ASN THR SEQRES 7 C 134 MET CYS LEU GLU MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 C 134 ALA VAL TYR TYR CYS ALA LEU ARG THR ALA ARG ASP SER SEQRES 9 C 134 TYR TYR TYR THR ARG ASN PRO THR GLY TYR ASP TYR TRP SEQRES 10 C 134 GLY GLN GLY THR GLN SER SER HIS HIS HIS HIS HIS HIS SEQRES 11 C 134 GLU PRO GLU ALA HET UGA A 601 37 HET MN A 602 1 HET Y01 A 603 35 HETNAM UGA URIDINE-5'-DIPHOSPHATE-GLUCURONIC ACID HETNAM MN MANGANESE (II) ION HETNAM Y01 CHOLESTEROL HEMISUCCINATE HETSYN UGA UDP-GLUCURONIC ACID FORMUL 4 UGA C15 H22 N2 O18 P2 FORMUL 5 MN MN 2+ FORMUL 6 Y01 C31 H50 O4 HELIX 1 AA1 ALA A 39 LEU A 74 1 36 HELIX 2 AA2 ASP A 94 SER A 108 1 15 HELIX 3 AA3 ASP A 127 GLN A 136 1 10 HELIX 4 AA4 GLY A 176 ALA A 188 1 13 HELIX 5 AA5 ALA A 210 ASP A 221 1 12 HELIX 6 AA6 ILE A 239 ASN A 253 1 15 HELIX 7 AA7 VAL A 254 TRP A 262 1 9 HELIX 8 AA8 ILE A 277 ILE A 288 1 12 HELIX 9 AA9 GLY A 300 MET A 311 1 12 HELIX 10 AB1 ASN A 331 SER A 356 1 26 HELIX 11 AB2 ALA A 357 LYS A 359 5 3 HELIX 12 AB3 GLY A 364 LYS A 391 1 28 HELIX 13 AB4 ILE A 394 LYS A 420 1 27 HELIX 14 AB5 LYS A 423 VAL A 428 5 6 HELIX 15 AB6 LEU A 429 MET A 449 1 21 HELIX 16 AB7 PHE A 476 ASN A 497 1 22 HELIX 17 AB8 ASP A 504 THR A 534 1 31 HELIX 18 AB9 LEU A 541 ARG A 549 1 9 HELIX 19 AC1 ALA B 28 TYR B 32 5 5 HELIX 20 AC2 LYS B 86 THR B 90 5 5 HELIX 21 AC3 ASN C 109 TYR C 113 5 5 SHEET 1 AA1 9 VAL A 142 LYS A 143 0 SHEET 2 AA1 9 ILE A 168 GLN A 172 1 O CYS A 169 N LYS A 143 SHEET 3 AA1 9 VAL A 113 ASP A 121 1 N ILE A 120 O ILE A 170 SHEET 4 AA1 9 VAL A 84 GLY A 90 1 N ILE A 88 O VAL A 119 SHEET 5 AA1 9 ALA A 196 ASP A 201 1 O ILE A 200 N ILE A 87 SHEET 6 AA1 9 GLY A 273 THR A 276 -1 O TYR A 275 N VAL A 197 SHEET 7 AA1 9 ILE A 224 ILE A 233 -1 N VAL A 227 O ALA A 274 SHEET 8 AA1 9 LYS A 315 SER A 326 1 O GLY A 324 N LYS A 232 SHEET 9 AA1 9 VAL A 205 LEU A 206 -1 N VAL A 205 O TRP A 325 SHEET 1 AA2 2 PHE A 500 ASP A 501 0 SHEET 2 AA2 2 TYR B 100 GLY B 101 1 O GLY B 101 N PHE A 500 SHEET 1 AA3 2 GLN B 3 SER B 7 0 SHEET 2 AA3 2 SER B 21 SER B 25 -1 O ALA B 23 N VAL B 5 SHEET 1 AA4 6 LEU B 11 VAL B 12 0 SHEET 2 AA4 6 GLN B 119 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AA4 6 ALA B 91 ARG B 98 -1 N ALA B 91 O VAL B 120 SHEET 4 AA4 6 ARG B 33 GLN B 39 -1 N ALA B 35 O ALA B 96 SHEET 5 AA4 6 GLU B 46 ILE B 51 -1 O ILE B 51 N MET B 34 SHEET 6 AA4 6 THR B 57 TYR B 59 -1 O TYR B 58 N GLY B 50 SHEET 1 AA5 4 LEU B 11 VAL B 12 0 SHEET 2 AA5 4 GLN B 119 VAL B 122 1 O THR B 121 N VAL B 12 SHEET 3 AA5 4 ALA B 91 ARG B 98 -1 N ALA B 91 O VAL B 120 SHEET 4 AA5 4 TYR B 113 TRP B 114 -1 O TYR B 113 N ALA B 97 SHEET 1 AA6 2 PHE B 67 THR B 68 0 SHEET 2 AA6 2 GLN B 81 MET B 82 -1 O GLN B 81 N THR B 68 SHEET 1 AA7 4 GLN C 3 SER C 7 0 SHEET 2 AA7 4 LEU C 18 SER C 25 -1 O ALA C 23 N VAL C 5 SHEET 3 AA7 4 THR C 77 MET C 82 -1 O MET C 82 N LEU C 18 SHEET 4 AA7 4 PHE C 67 ARG C 71 -1 N SER C 70 O CYS C 79 SHEET 1 AA8 5 GLY C 56 GLY C 57 0 SHEET 2 AA8 5 ARG C 45 ARG C 52 -1 O ARG C 52 N GLY C 56 SHEET 3 AA8 5 THR C 33 ARG C 39 -1 N ARG C 38 O GLU C 46 SHEET 4 AA8 5 VAL C 92 ARG C 98 -1 O TYR C 94 N PHE C 37 SHEET 5 AA8 5 TYR C 115 TRP C 116 -1 O TYR C 115 N LEU C 97 SSBOND 1 CYS B 22 CYS B 95 1555 1555 2.03 SSBOND 2 CYS C 22 CYS C 95 1555 1555 2.04 LINK OE1 GLU A 93 MN MN A 602 1555 1555 2.11 LINK OD2 ASP A 203 MN MN A 602 1555 1555 2.26 CRYST1 1.000 1.000 1.000 90.00 90.00 90.00 P 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