HEADER TRANSFERASE 25-NOV-24 9KQC TITLE CHLORELLA VIRUS HYALURONAN SYNTHASE BOUND TO VNAR COMPND MOL_ID: 1; COMPND 2 MOLECULE: HYALURONAN SYNTHASE; COMPND 3 CHAIN: A; COMPND 4 ENGINEERED: YES; COMPND 5 MOL_ID: 2; COMPND 6 MOLECULE: VNAR; COMPND 7 CHAIN: B; COMPND 8 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: CHLORELLA VIRUS; SOURCE 3 ORGANISM_TAXID: 10507; SOURCE 4 GENE: CZ-2_118R, PBCVCZ2_118R; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: CHILOSCYLLIUM PLAGIOSUM; SOURCE 9 ORGANISM_TAXID: 36176; SOURCE 10 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 11 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS CHLORELLA VIRUS HYALURONAN SYNTHASE, MEMBRANE-INTEGRATED KEYWDS 2 GLYCOSYLTRANSFERASE, TRANSFERASE EXPDTA ELECTRON MICROSCOPY AUTHOR P.DENG,X.ZHANG,M.XU,J.WEN,P.LI,Y.BI,H.WANG REVDAT 2 18-JUN-25 9KQC 1 JRNL REVDAT 1 14-MAY-25 9KQC 0 JRNL AUTH P.DENG,X.ZHANG,J.WEN,M.XU,P.LI,H.WANG,Y.BI JRNL TITL GENERATION OF SHARK SINGLE-DOMAIN ANTIBODIES AS AN AID FOR JRNL TITL 2 CRYO-EM STRUCTURE DETERMINATION OF MEMBRANE PROTEINS: USE JRNL TITL 3 HYALURONAN SYNTHASE AS AN EXAMPLE. JRNL REF J STRUCT BIOL X V. 11 00126 2025 JRNL REFN ESSN 2590-1524 JRNL PMID 40475323 JRNL DOI 10.1016/J.YJSBX.2025.100126 REMARK 2 REMARK 2 RESOLUTION. 3.36 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : NULL 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) : 3.360 REMARK 3 NUMBER OF PARTICLES : 263915 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 9KQC COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 26-NOV-24. REMARK 100 THE DEPOSITION ID IS D_1300054066. 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 : CHLORELLA VIRUS HYALURONAN REMARK 245 SYNTHASE BOUND TO VNAR. 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 : 6.50 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 : FEI MORGAGNI REMARK 245 DETECTOR TYPE : FEI FALCON IV (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 1800.00 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: DIMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 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 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 B -24 REMARK 465 HIS B -23 REMARK 465 HIS B -22 REMARK 465 HIS B -21 REMARK 465 HIS B -20 REMARK 465 HIS B -19 REMARK 465 SER B -18 REMARK 465 SER B -17 REMARK 465 GLY B -16 REMARK 465 LEU B -15 REMARK 465 VAL B -14 REMARK 465 PRO B -13 REMARK 465 ARG B -12 REMARK 465 GLY B -11 REMARK 465 SER B -10 REMARK 465 GLY B -9 REMARK 465 MET B -8 REMARK 465 LEU B -7 REMARK 465 GLU B -6 REMARK 465 VAL B -5 REMARK 465 LEU B -4 REMARK 465 PHE B -3 REMARK 465 GLN B -2 REMARK 465 GLY B -1 REMARK 465 PRO B 0 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 A 138 -169.73 -121.52 REMARK 500 LYS A 177 -94.32 -114.30 REMARK 500 ARG A 178 -66.30 -20.69 REMARK 500 TYR A 216 -44.67 -168.82 REMARK 500 ALA A 251 -71.46 -36.94 REMARK 500 VAL A 254 -78.32 -125.26 REMARK 500 THR A 264 50.90 -155.61 REMARK 500 PHE A 292 -96.07 -68.68 REMARK 500 ARG A 303 -48.52 105.42 REMARK 500 CYS A 437 -51.88 -120.41 REMARK 500 THR B 6 -70.09 -23.18 REMARK 500 THR B 10 146.84 -172.92 REMARK 500 ASP B 32 -61.23 -92.73 REMARK 500 REMARK 500 REMARK: NULL REMARK 610 REMARK 610 MISSING HETEROATOM REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER; REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 610 I=INSERTION CODE): REMARK 610 M RES C SSEQI REMARK 610 UD1 A 601 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 OE2 REMARK 620 2 ASP A 203 OD2 105.8 REMARK 620 N 1 REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-62500 RELATED DB: EMDB REMARK 900 CHLORELLA VIRUS HYALURONAN SYNTHASE BOUND TO VNAR DBREF 9KQC A 2 561 UNP M1H2Q1 M1H2Q1_9PHYC 2 561 DBREF 9KQC B -24 107 PDB 9KQC 9KQC -24 107 SEQADV 9KQC MET A 0 UNP M1H2Q1 INITIATING METHIONINE SEQADV 9KQC GLY A 1 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC LEU A 562 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC GLU A 563 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC HIS A 564 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC HIS A 565 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC HIS A 566 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC HIS A 567 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC HIS A 568 UNP M1H2Q1 EXPRESSION TAG SEQADV 9KQC HIS A 569 UNP M1H2Q1 EXPRESSION TAG SEQRES 1 A 570 MET GLY THR SER TRP ARG THR ILE VAL SER ALA ASN LEU SEQRES 2 A 570 PHE ALA VAL GLY GLY ALA LEU LEU MET LEU ALA PRO ALA SEQRES 3 A 570 ILE VAL GLY TYR VAL PHE GLN TRP ASN ILE GLY VAL SER SEQRES 4 A 570 ALA VAL TRP GLY ILE SER VAL TYR GLY VAL PHE VAL LEU SEQRES 5 A 570 GLY PHE TYR ILE ALA GLN ILE VAL PHE SER GLU PHE ASN SEQRES 6 A 570 ARG MET ARG LEU SER ASP TRP ILE SER LEU ARG PRO ASP SEQRES 7 A 570 ASN TRP ASN ALA THR ARG VAL ALA VAL ILE ILE ALA GLY SEQRES 8 A 570 TYR ARG GLU ASP PRO PHE MET PHE LYS LYS CYS LEU GLU SEQRES 9 A 570 SER VAL ARG ASP SER GLU TYR GLY ASN VAL ALA ARG LEU SEQRES 10 A 570 ILE CYS VAL ILE ASP GLY ASP GLU GLU GLU ASP LEU LYS SEQRES 11 A 570 MET ALA GLU ILE TYR LYS GLN VAL TYR ASN ASP ASN VAL SEQRES 12 A 570 LYS LYS PRO GLY VAL VAL LEU CYS GLU SER GLU ASN LYS SEQRES 13 A 570 ASN GLY SER THR ILE ASP SER ASP VAL SER LYS ASN ILE SEQRES 14 A 570 CYS ILE LEU GLN PRO HIS ARG GLY LYS ARG GLU SER LEU SEQRES 15 A 570 TYR THR GLY PHE GLN LEU ALA SER MET ASP PRO SER VAL SEQRES 16 A 570 HIS ALA VAL VAL LEU ILE ASP SER ASP THR VAL LEU GLU SEQRES 17 A 570 LYS ASN ALA ILE LEU GLU VAL VAL TYR PRO LEU SER CYS SEQRES 18 A 570 ASP PRO ASN ILE LYS ALA VAL ALA GLY GLU CYS LYS ILE SEQRES 19 A 570 TRP ASN THR ASP THR ILE LEU SER MET LEU VAL SER TRP SEQRES 20 A 570 ARG TYR PHE SER ALA PHE ASN VAL GLU ARG GLY ALA GLN SEQRES 21 A 570 SER LEU TRP LYS THR VAL GLN CYS VAL GLY GLY PRO LEU SEQRES 22 A 570 GLY ALA TYR THR ILE ASP ILE ILE ASN GLU ILE LYS ASP SEQRES 23 A 570 PRO TRP ILE THR GLN THR PHE LEU GLY ASN LYS CYS THR SEQRES 24 A 570 TYR GLY ASP ASP ARG ARG LEU THR ASN GLU VAL LEU MET SEQRES 25 A 570 ARG GLY LYS LYS ILE VAL TYR THR PRO PHE ALA VAL GLY SEQRES 26 A 570 TRP SER ASP SER PRO THR ASN VAL MET ARG TYR ILE VAL SEQRES 27 A 570 GLN GLN THR ARG TRP SER LYS SER TRP CYS ARG GLU ILE SEQRES 28 A 570 TRP TYR THR LEU GLY SER ALA TRP LYS HIS GLY PHE SER SEQRES 29 A 570 GLY ILE TYR LEU ALA PHE GLU CYS MET TYR GLN ILE MET SEQRES 30 A 570 TYR PHE PHE LEU VAL MET TYR LEU PHE SER TYR ILE ALA SEQRES 31 A 570 ILE LYS ALA ASP ILE ARG ALA GLN THR ALA THR VAL LEU SEQRES 32 A 570 VAL SER THR LEU VAL THR ILE ILE LYS SER SER TYR LEU SEQRES 33 A 570 ALA LEU ARG ALA LYS ASN LEU LYS ALA PHE TYR PHE VAL SEQRES 34 A 570 LEU TYR THR TYR VAL TYR PHE PHE CYS MET ILE PRO ALA SEQRES 35 A 570 ARG ILE THR ALA MET PHE THR MET PHE ASP ILE ALA TRP SEQRES 36 A 570 GLY THR ARG GLY GLY ASN ALA LYS MET THR ILE GLY ALA SEQRES 37 A 570 ARG VAL TRP LEU TRP ALA LYS GLN PHE LEU ILE THR TYR SEQRES 38 A 570 MET TRP TRP ALA GLY VAL LEU ALA ALA GLY VAL TYR SER SEQRES 39 A 570 ILE VAL ASP ASN TRP TYR PHE ASP TRP ALA ASP ILE GLN SEQRES 40 A 570 TYR ARG PHE ALA LEU VAL GLY ILE CYS SER TYR LEU VAL SEQRES 41 A 570 PHE VAL SER ILE VAL LEU VAL ILE TYR LEU ILE GLY LYS SEQRES 42 A 570 ILE THR THR TRP ASN TYR THR PRO LEU GLN LYS GLU LEU SEQRES 43 A 570 ILE GLU GLU ARG TYR LEU HIS ASN ALA SER GLU ASN ALA SEQRES 44 A 570 PRO GLU VAL LEU GLU HIS HIS HIS HIS HIS HIS SEQRES 1 B 132 HIS HIS HIS HIS HIS HIS SER SER GLY LEU VAL PRO ARG SEQRES 2 B 132 GLY SER GLY MET LEU GLU VAL LEU PHE GLN GLY PRO GLN SEQRES 3 B 132 ARG VAL GLU GLN THR PRO THR THR THR THR LYS GLU ALA SEQRES 4 B 132 GLY GLU SER LEU THR ILE ASN CYS VAL LEU ARG ASP SER SEQRES 5 B 132 ALA CYS ALA LEU ASP ASN THR TYR TRP TYR PHE THR LYS SEQRES 6 B 132 LYS GLY ALA THR LYS LYS GLU SER LEU SER ASN GLY GLY SEQRES 7 B 132 ARG TYR ALA GLU THR VAL ASN LYS ALA SER LYS SER SER SEQRES 8 B 132 SER LEU ARG ILE SER ASP LEU ARG VAL GLU ASP SER GLY SEQRES 9 B 132 THR TYR HIS CYS LYS ALA TYR THR ALA GLY ILE GLY CYS SEQRES 10 B 132 TRP ASN ILE PHE TYR GLU GLY GLY GLY THR ILE LEU THR SEQRES 11 B 132 VAL LYS HET UD1 A 601 25 HET MN A 602 1 HETNAM UD1 URIDINE-DIPHOSPHATE-N-ACETYLGLUCOSAMINE HETNAM MN MANGANESE (II) ION FORMUL 3 UD1 C17 H27 N3 O17 P2 FORMUL 4 MN MN 2+ HELIX 1 AA1 SER A 38 LEU A 74 1 37 HELIX 2 AA2 ASP A 94 SER A 108 1 15 HELIX 3 AA3 GLU A 124 GLU A 126 5 3 HELIX 4 AA4 ASP A 127 TYR A 138 1 12 HELIX 5 AA5 ASN A 156 ILE A 160 5 5 HELIX 6 AA6 LYS A 177 ASP A 191 1 15 HELIX 7 AA7 ASN A 209 VAL A 215 1 7 HELIX 8 AA8 TYR A 216 ASP A 221 1 6 HELIX 9 AA9 THR A 238 VAL A 254 1 17 HELIX 10 AB1 VAL A 254 TRP A 262 1 9 HELIX 11 AB2 THR A 276 THR A 289 1 14 HELIX 12 AB3 ARG A 303 ARG A 312 1 10 HELIX 13 AB4 ASN A 331 TRP A 358 1 28 HELIX 14 AB5 LYS A 359 GLY A 361 5 3 HELIX 15 AB6 GLY A 364 ALA A 392 1 29 HELIX 16 AB7 ASP A 393 LYS A 420 1 28 HELIX 17 AB8 ASN A 421 VAL A 428 5 8 HELIX 18 AB9 LEU A 429 PHE A 450 1 22 HELIX 19 AC1 ARG A 468 ASN A 497 1 30 HELIX 20 AC2 ASP A 504 THR A 534 1 31 HELIX 21 AC3 THR A 539 LEU A 551 1 13 HELIX 22 AC4 ARG B 74 ASP B 77 5 4 SHEET 1 AA1 4 ILE A 168 LEU A 171 0 SHEET 2 AA1 4 VAL A 113 ILE A 120 1 N CYS A 118 O ILE A 170 SHEET 3 AA1 4 VAL A 84 GLY A 90 1 N ILE A 88 O ILE A 117 SHEET 4 AA1 4 LEU A 199 ASP A 201 1 O ILE A 200 N ILE A 87 SHEET 1 AA2 4 VAL A 205 LEU A 206 0 SHEET 2 AA2 4 LYS A 315 SER A 326 -1 O TRP A 325 N VAL A 205 SHEET 3 AA2 4 ILE A 224 ILE A 233 1 N LYS A 232 O GLY A 324 SHEET 4 AA2 4 GLY A 273 TYR A 275 -1 O ALA A 274 N VAL A 227 SHEET 1 AA3 4 ARG B 2 GLU B 4 0 SHEET 2 AA3 4 LEU B 18 ARG B 25 -1 O ARG B 25 N ARG B 2 SHEET 3 AA3 4 SER B 65 ILE B 70 -1 O SER B 66 N CYS B 22 SHEET 4 AA3 4 TYR B 55 ASN B 60 -1 N ALA B 56 O ARG B 69 SHEET 1 AA4 5 THR B 9 GLU B 13 0 SHEET 2 AA4 5 THR B 102 LYS B 107 1 O THR B 105 N LYS B 12 SHEET 3 AA4 5 GLY B 79 THR B 87 -1 N TYR B 81 O THR B 102 SHEET 4 AA4 5 LEU B 31 LYS B 40 -1 N ASP B 32 O TYR B 86 SHEET 5 AA4 5 LYS B 46 SER B 48 -1 O GLU B 47 N PHE B 38 SHEET 1 AA5 4 THR B 9 GLU B 13 0 SHEET 2 AA5 4 THR B 102 LYS B 107 1 O THR B 105 N LYS B 12 SHEET 3 AA5 4 GLY B 79 THR B 87 -1 N TYR B 81 O THR B 102 SHEET 4 AA5 4 TYR B 97 GLU B 98 -1 O TYR B 97 N ALA B 85 SSBOND 1 CYS B 22 CYS B 83 1555 1555 2.03 SSBOND 2 CYS B 29 CYS B 92 1555 1555 2.03 LINK OE2 GLU A 93 MN MN A 602 1555 1555 2.17 LINK OD2 ASP A 203 MN MN A 602 1555 1555 2.35 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