HEADER STRUCTURAL PROTEIN/IMMUNE SYSTEM 04-FEB-25 9LSJ TITLE CRYO-EM STRUCTURE OF THE G15C-R66C AND T83C-T83C DIABODY COMPLEX TITLE 2 (CITS-DIABODY #7-TLR3) COMPND MOL_ID: 1; COMPND 2 MOLECULE: CITRATE/SODIUM SYMPORTER; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: CITRATE TRANSPORTER CITS,NA(+)-DEPENDENT CITRATE CARRIER, COMPND 5 SODIUM-DEPENDENT CITRATE TRANSPORT SYSTEM; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: TOLL-LIKE RECEPTOR 3; COMPND 9 CHAIN: C; COMPND 10 ENGINEERED: YES; COMPND 11 MOL_ID: 3; COMPND 12 MOLECULE: DIABODY (CITS VH-TLR3 VL); COMPND 13 CHAIN: D; COMPND 14 ENGINEERED: YES; COMPND 15 MOL_ID: 4; COMPND 16 MOLECULE: DIABODY (TLR3 VH-CITS VL); COMPND 17 CHAIN: E; COMPND 18 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: KLEBSIELLA PNEUMONIAE; SOURCE 3 ORGANISM_TAXID: 573; SOURCE 4 GENE: CITS; SOURCE 5 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 6 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 7 MOL_ID: 2; SOURCE 8 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 9 ORGANISM_COMMON: HUMAN; SOURCE 10 ORGANISM_TAXID: 9606; SOURCE 11 GENE: TLR3; SOURCE 12 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 13 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 14 MOL_ID: 3; SOURCE 15 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 16 ORGANISM_TAXID: 32630; SOURCE 17 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 18 EXPRESSION_SYSTEM_TAXID: 7111; SOURCE 19 MOL_ID: 4; SOURCE 20 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 21 ORGANISM_TAXID: 32630; SOURCE 22 EXPRESSION_SYSTEM: TRICHOPLUSIA NI; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7111 KEYWDS DISULFIDE-BRIDGED DIABODY, CRYO-ELECTRON MICROSCOPY (CRYO-EM), SMALL KEYWDS 2 PROTEIN IMAGING, STRUCTURAL MARKER, ANTIBODY ENGINEERING, PROTEIN KEYWDS 3 NANOTECHNOLOGY, STRUCTURAL PROTEIN, STRUCTURAL PROTEIN-IMMUNE SYSTEM KEYWDS 4 COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR S.KIM,J.W.KIM,J.G.PARK,S.S.LEE,S.H.CHOI,J.-O.LEE,M.S.JIN REVDAT 1 12-MAR-25 9LSJ 0 JRNL AUTH S.KIM,J.W.KIM,J.G.PARK,S.S.LEE,S.H.CHOI,J.-O.LEE,M.S.JIN JRNL TITL DISULFIDE-STABILIZED DIABODIES ENABLE NEAR-ATOMIC CRYO-EM JRNL TITL 2 IMAGING OF SMALL PROTEINS: A CASE STUDY OF THE BACTERIAL JRNL TITL 3 NA+/CITRATE SYMPORTER CITS JRNL REF TO BE PUBLISHED JRNL REFN REMARK 2 REMARK 2 RESOLUTION. 3.10 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : PHENIX 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) : 3.100 REMARK 3 NUMBER OF PARTICLES : 259962 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 9LSJ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 05-FEB-25. REMARK 100 THE DEPOSITION ID IS D_1300056363. 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 : CITS-DIABODY #1-TLR3 COMPLEX; REMARK 245 CITS; TLR3; DIABODY 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 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 800.00 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) : 6000.00 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: PENTAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D, E, H, F, G, I 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 1 REMARK 465 THR A 2 REMARK 465 ASN A 3 REMARK 465 MET A 4 REMARK 465 SER A 5 REMARK 465 GLN A 6 REMARK 465 PRO A 7 REMARK 465 PRO A 8 REMARK 465 ALA A 9 REMARK 465 THR A 10 REMARK 465 GLU A 11 REMARK 465 LYS A 12 REMARK 465 LYS A 13 REMARK 465 GLY A 14 REMARK 465 VAL A 15 REMARK 465 MET B 1 REMARK 465 THR B 2 REMARK 465 ASN B 3 REMARK 465 MET B 4 REMARK 465 SER B 5 REMARK 465 GLN B 6 REMARK 465 PRO B 7 REMARK 465 PRO B 8 REMARK 465 ALA B 9 REMARK 465 THR B 10 REMARK 465 GLU B 11 REMARK 465 LYS B 12 REMARK 465 LYS B 13 REMARK 465 GLY B 14 REMARK 465 VAL B 15 REMARK 465 MET C 1 REMARK 465 ARG C 2 REMARK 465 GLN C 3 REMARK 465 THR C 4 REMARK 465 LEU C 5 REMARK 465 PRO C 6 REMARK 465 CYS C 7 REMARK 465 ILE C 8 REMARK 465 TYR C 9 REMARK 465 PHE C 10 REMARK 465 TRP C 11 REMARK 465 GLY C 12 REMARK 465 GLY C 13 REMARK 465 LEU C 14 REMARK 465 LEU C 15 REMARK 465 PRO C 16 REMARK 465 PHE C 17 REMARK 465 GLY C 18 REMARK 465 MET C 19 REMARK 465 LEU C 20 REMARK 465 CYS C 21 REMARK 465 ALA C 22 REMARK 465 SER C 23 REMARK 465 SER C 24 REMARK 465 THR C 25 REMARK 465 THR C 26 REMARK 465 ASP C 692 REMARK 465 THR C 693 REMARK 465 SER C 694 REMARK 465 SER C 695 REMARK 465 CYS C 696 REMARK 465 LYS C 697 REMARK 465 ASP C 698 REMARK 465 SER C 699 REMARK 465 ALA C 700 REMARK 465 PRO C 701 REMARK 465 PHE C 702 REMARK 465 GLU C 703 REMARK 465 LEU C 704 REMARK 465 PHE C 705 REMARK 465 PHE C 706 REMARK 465 MET C 707 REMARK 465 ILE C 708 REMARK 465 ASN C 709 REMARK 465 THR C 710 REMARK 465 SER C 711 REMARK 465 ILE C 712 REMARK 465 LEU C 713 REMARK 465 LEU C 714 REMARK 465 ILE C 715 REMARK 465 PHE C 716 REMARK 465 ILE C 717 REMARK 465 PHE C 718 REMARK 465 ILE C 719 REMARK 465 VAL C 720 REMARK 465 LEU C 721 REMARK 465 LEU C 722 REMARK 465 ILE C 723 REMARK 465 HIS C 724 REMARK 465 PHE C 725 REMARK 465 GLU C 726 REMARK 465 GLY C 727 REMARK 465 TRP C 728 REMARK 465 ARG C 729 REMARK 465 ILE C 730 REMARK 465 SER C 731 REMARK 465 PHE C 732 REMARK 465 TYR C 733 REMARK 465 TRP C 734 REMARK 465 ASN C 735 REMARK 465 VAL C 736 REMARK 465 SER C 737 REMARK 465 VAL C 738 REMARK 465 HIS C 739 REMARK 465 ARG C 740 REMARK 465 VAL C 741 REMARK 465 LEU C 742 REMARK 465 GLY C 743 REMARK 465 PHE C 744 REMARK 465 LYS C 745 REMARK 465 GLU C 746 REMARK 465 ILE C 747 REMARK 465 ASP C 748 REMARK 465 ARG C 749 REMARK 465 GLN C 750 REMARK 465 THR C 751 REMARK 465 GLU C 752 REMARK 465 GLN C 753 REMARK 465 PHE C 754 REMARK 465 GLU C 755 REMARK 465 TYR C 756 REMARK 465 ALA C 757 REMARK 465 ALA C 758 REMARK 465 TYR C 759 REMARK 465 ILE C 760 REMARK 465 ILE C 761 REMARK 465 HIS C 762 REMARK 465 ALA C 763 REMARK 465 TYR C 764 REMARK 465 LYS C 765 REMARK 465 ASP C 766 REMARK 465 LYS C 767 REMARK 465 ASP C 768 REMARK 465 TRP C 769 REMARK 465 VAL C 770 REMARK 465 TRP C 771 REMARK 465 GLU C 772 REMARK 465 HIS C 773 REMARK 465 PHE C 774 REMARK 465 SER C 775 REMARK 465 SER C 776 REMARK 465 MET C 777 REMARK 465 GLU C 778 REMARK 465 LYS C 779 REMARK 465 GLU C 780 REMARK 465 ASP C 781 REMARK 465 GLN C 782 REMARK 465 SER C 783 REMARK 465 LEU C 784 REMARK 465 LYS C 785 REMARK 465 PHE C 786 REMARK 465 CYS C 787 REMARK 465 LEU C 788 REMARK 465 GLU C 789 REMARK 465 GLU C 790 REMARK 465 ARG C 791 REMARK 465 ASP C 792 REMARK 465 PHE C 793 REMARK 465 GLU C 794 REMARK 465 ALA C 795 REMARK 465 GLY C 796 REMARK 465 VAL C 797 REMARK 465 PHE C 798 REMARK 465 GLU C 799 REMARK 465 LEU C 800 REMARK 465 GLU C 801 REMARK 465 ALA C 802 REMARK 465 ILE C 803 REMARK 465 VAL C 804 REMARK 465 ASN C 805 REMARK 465 SER C 806 REMARK 465 ILE C 807 REMARK 465 LYS C 808 REMARK 465 ARG C 809 REMARK 465 SER C 810 REMARK 465 ARG C 811 REMARK 465 LYS C 812 REMARK 465 ILE C 813 REMARK 465 ILE C 814 REMARK 465 PHE C 815 REMARK 465 VAL C 816 REMARK 465 ILE C 817 REMARK 465 THR C 818 REMARK 465 HIS C 819 REMARK 465 HIS C 820 REMARK 465 LEU C 821 REMARK 465 LEU C 822 REMARK 465 LYS C 823 REMARK 465 ASP C 824 REMARK 465 PRO C 825 REMARK 465 LEU C 826 REMARK 465 CYS C 827 REMARK 465 LYS C 828 REMARK 465 ARG C 829 REMARK 465 PHE C 830 REMARK 465 LYS C 831 REMARK 465 VAL C 832 REMARK 465 HIS C 833 REMARK 465 HIS C 834 REMARK 465 ALA C 835 REMARK 465 VAL C 836 REMARK 465 GLN C 837 REMARK 465 GLN C 838 REMARK 465 ALA C 839 REMARK 465 ILE C 840 REMARK 465 GLU C 841 REMARK 465 GLN C 842 REMARK 465 ASN C 843 REMARK 465 LEU C 844 REMARK 465 ASP C 845 REMARK 465 SER C 846 REMARK 465 ILE C 847 REMARK 465 ILE C 848 REMARK 465 LEU C 849 REMARK 465 VAL C 850 REMARK 465 PHE C 851 REMARK 465 LEU C 852 REMARK 465 GLU C 853 REMARK 465 GLU C 854 REMARK 465 ILE C 855 REMARK 465 PRO C 856 REMARK 465 ASP C 857 REMARK 465 TYR C 858 REMARK 465 LYS C 859 REMARK 465 LEU C 860 REMARK 465 ASN C 861 REMARK 465 HIS C 862 REMARK 465 ALA C 863 REMARK 465 LEU C 864 REMARK 465 CYS C 865 REMARK 465 LEU C 866 REMARK 465 ARG C 867 REMARK 465 ARG C 868 REMARK 465 GLY C 869 REMARK 465 MET C 870 REMARK 465 PHE C 871 REMARK 465 LYS C 872 REMARK 465 SER C 873 REMARK 465 HIS C 874 REMARK 465 CYS C 875 REMARK 465 ILE C 876 REMARK 465 LEU C 877 REMARK 465 ASN C 878 REMARK 465 TRP C 879 REMARK 465 PRO C 880 REMARK 465 VAL C 881 REMARK 465 GLN C 882 REMARK 465 LYS C 883 REMARK 465 GLU C 884 REMARK 465 ARG C 885 REMARK 465 ILE C 886 REMARK 465 GLY C 887 REMARK 465 ALA C 888 REMARK 465 PHE C 889 REMARK 465 ARG C 890 REMARK 465 HIS C 891 REMARK 465 LYS C 892 REMARK 465 LEU C 893 REMARK 465 GLN C 894 REMARK 465 VAL C 895 REMARK 465 ALA C 896 REMARK 465 LEU C 897 REMARK 465 GLY C 898 REMARK 465 SER C 899 REMARK 465 LYS C 900 REMARK 465 ASN C 901 REMARK 465 SER C 902 REMARK 465 VAL C 903 REMARK 465 HIS C 904 REMARK 465 ILE D 230 REMARK 465 LYS D 231 REMARK 465 PRO D 232 REMARK 465 TRP D 233 REMARK 465 LEU D 234 REMARK 465 VAL D 235 REMARK 465 PRO D 236 REMARK 465 ARG D 237 REMARK 465 GLY D 238 REMARK 465 SER D 239 REMARK 465 HIS D 240 REMARK 465 HIS D 241 REMARK 465 HIS D 242 REMARK 465 HIS D 243 REMARK 465 HIS D 244 REMARK 465 HIS D 245 REMARK 465 SER D 246 REMARK 465 GLY D 247 REMARK 465 GLY D 248 REMARK 465 GLY D 249 REMARK 465 GLY D 250 REMARK 465 SER D 251 REMARK 465 GLY D 252 REMARK 465 GLY D 253 REMARK 465 GLY D 254 REMARK 465 GLY D 255 REMARK 465 SER D 256 REMARK 465 GLY E 257 REMARK 465 GLY E 258 REMARK 465 GLY E 259 REMARK 465 GLY E 260 REMARK 465 SER E 261 REMARK 465 GLY E 262 REMARK 465 GLY E 263 REMARK 465 GLY E 264 REMARK 465 GLY E 265 REMARK 465 LEU E 266 REMARK 465 VAL E 267 REMARK 465 PRO E 268 REMARK 465 ARG E 269 REMARK 465 GLY E 270 REMARK 465 SER E 271 REMARK 465 PRO E 272 REMARK 465 GLY E 273 REMARK 465 LYS E 507 REMARK 465 SER E 508 REMARK 465 GLY E 509 REMARK 465 ARG E 510 REMARK 465 LEU E 511 REMARK 465 VAL E 512 REMARK 465 PRO E 513 REMARK 465 ARG E 514 REMARK 465 GLY E 515 REMARK 465 SER E 516 REMARK 465 HIS E 517 REMARK 465 HIS E 518 REMARK 465 HIS E 519 REMARK 465 HIS E 520 REMARK 465 HIS E 521 REMARK 465 HIS E 522 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 LYS A 249 CG CD CE NZ REMARK 470 PHE A 252 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS A 253 CG CD CE NZ REMARK 470 GLU A 255 CG CD OE1 OE2 REMARK 470 GLU A 256 CG CD OE1 OE2 REMARK 470 ASP A 257 CG OD1 OD2 REMARK 470 LYS A 259 CG CD CE NZ REMARK 470 PHE B 252 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LYS B 253 CG CD CE NZ REMARK 470 GLU B 255 CG CD OE1 OE2 REMARK 470 GLU B 256 CG CD OE1 OE2 REMARK 470 ASP B 257 CG OD1 OD2 REMARK 470 GLU B 258 CG CD OE1 OE2 REMARK 470 LYS B 259 CG CD CE NZ REMARK 470 ARG C 689 CG CD NE CZ NH1 NH2 REMARK 470 GLU E 505 CG CD OE1 OE2 REMARK 470 ILE E 506 CG1 CG2 CD1 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 395 -10.82 71.44 REMARK 500 ARG B 71 52.79 -93.36 REMARK 500 LYS B 249 24.52 46.99 REMARK 500 ARG B 402 52.80 -92.37 REMARK 500 ASN B 415 51.59 -93.96 REMARK 500 ARG C 64 -61.37 -95.19 REMARK 500 TYR C 74 66.69 -101.57 REMARK 500 GLN C 169 -169.03 -168.03 REMARK 500 TYR C 283 11.63 59.35 REMARK 500 ASN C 285 42.86 38.17 REMARK 500 LEU C 343 71.74 48.56 REMARK 500 PHE C 349 12.98 59.73 REMARK 500 LYS C 418 58.37 38.01 REMARK 500 GLU C 442 77.87 -116.32 REMARK 500 TYR C 465 64.33 60.28 REMARK 500 ASN C 474 56.57 -98.82 REMARK 500 PHE C 630 49.31 -95.72 REMARK 500 SER C 672 -74.01 -90.08 REMARK 500 TYR C 675 99.92 -66.90 REMARK 500 ASN C 678 -31.23 -144.12 REMARK 500 ASN D 31 -3.56 74.52 REMARK 500 LYS D 169 11.48 51.10 REMARK 500 ARG D 185 13.07 56.04 REMARK 500 PHE E 302 -5.54 69.01 REMARK 500 ASN E 304 -30.11 -130.89 REMARK 500 ASP E 328 22.36 -140.92 REMARK 500 SER E 362 -2.60 69.31 REMARK 500 SER E 452 -30.66 -130.07 REMARK 500 SER E 463 114.72 -161.53 REMARK 500 TYR E 491 31.24 -140.13 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-63357 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE G15C-R66C AND T83C-T83C DIABODY COMPLEX REMARK 900 (CITS-DIABODY #7-TLR3) DBREF 9LSJ A 1 446 UNP P31602 CITN_KLEPN 1 446 DBREF 9LSJ B 1 446 UNP P31602 CITN_KLEPN 1 446 DBREF 9LSJ C 1 904 UNP O15455 TLR3_HUMAN 1 904 DBREF 9LSJ D 1 256 PDB 9LSJ 9LSJ 1 256 DBREF 9LSJ E 257 522 PDB 9LSJ 9LSJ 257 522 SEQRES 1 A 446 MET THR ASN MET SER GLN PRO PRO ALA THR GLU LYS LYS SEQRES 2 A 446 GLY VAL SER ASP LEU LEU GLY PHE LYS ILE PHE GLY MET SEQRES 3 A 446 PRO LEU PRO LEU TYR ALA PHE ALA LEU ILE THR LEU LEU SEQRES 4 A 446 LEU SER HIS PHE TYR ASN ALA LEU PRO THR ASP ILE VAL SEQRES 5 A 446 GLY GLY PHE ALA ILE MET PHE ILE ILE GLY ALA ILE PHE SEQRES 6 A 446 GLY GLU ILE GLY LYS ARG LEU PRO ILE PHE ASN LYS TYR SEQRES 7 A 446 ILE GLY GLY ALA PRO VAL MET ILE PHE LEU VAL ALA ALA SEQRES 8 A 446 TYR PHE VAL TYR ALA GLY ILE PHE THR GLN LYS GLU ILE SEQRES 9 A 446 ASP ALA ILE SER ASN VAL MET ASP LYS SER ASN PHE LEU SEQRES 10 A 446 ASN LEU PHE ILE ALA VAL LEU ILE THR GLY ALA ILE LEU SEQRES 11 A 446 SER VAL ASN ARG ARG LEU LEU LEU LYS SER LEU LEU GLY SEQRES 12 A 446 TYR ILE PRO THR ILE LEU MET GLY ILE VAL GLY ALA SER SEQRES 13 A 446 ILE PHE GLY ILE ALA ILE GLY LEU VAL PHE GLY ILE PRO SEQRES 14 A 446 VAL ASP ARG ILE MET MET LEU TYR VAL LEU PRO ILE MET SEQRES 15 A 446 GLY GLY GLY ASN GLY ALA GLY ALA VAL PRO LEU SER GLU SEQRES 16 A 446 ILE TYR HIS SER VAL THR GLY ARG SER ARG GLU GLU TYR SEQRES 17 A 446 TYR SER THR ALA ILE ALA ILE LEU THR ILE ALA ASN ILE SEQRES 18 A 446 PHE ALA ILE VAL PHE ALA ALA VAL LEU ASP ILE ILE GLY SEQRES 19 A 446 LYS LYS HIS THR TRP LEU SER GLY GLU GLY GLU LEU VAL SEQRES 20 A 446 ARG LYS ALA SER PHE LYS VAL GLU GLU ASP GLU LYS THR SEQRES 21 A 446 GLY GLN ILE THR HIS ARG GLU THR ALA VAL GLY LEU VAL SEQRES 22 A 446 LEU SER THR THR CYS PHE LEU LEU ALA TYR VAL VAL ALA SEQRES 23 A 446 LYS LYS ILE LEU PRO SER ILE GLY GLY VAL ALA ILE HIS SEQRES 24 A 446 TYR PHE ALA TRP MET VAL LEU ILE VAL ALA ALA LEU ASN SEQRES 25 A 446 ALA SER GLY LEU CYS SER PRO GLU ILE LYS ALA GLY ALA SEQRES 26 A 446 LYS ARG LEU SER ASP PHE PHE SER LYS GLN LEU LEU TRP SEQRES 27 A 446 VAL LEU MET VAL GLY VAL GLY VAL CYS TYR THR ASP LEU SEQRES 28 A 446 GLN GLU ILE ILE ASN ALA ILE THR PHE ALA ASN VAL VAL SEQRES 29 A 446 ILE ALA ALA ILE ILE VAL ILE GLY ALA VAL LEU GLY ALA SEQRES 30 A 446 ALA ILE GLY GLY TRP LEU MET GLY PHE PHE PRO ILE GLU SEQRES 31 A 446 SER ALA ILE THR ALA GLY LEU CYS MET ALA ASN ARG GLY SEQRES 32 A 446 GLY SER GLY ASP LEU GLU VAL LEU SER ALA CYS ASN ARG SEQRES 33 A 446 MET ASN LEU ILE SER TYR ALA GLN ILE SER SER ARG LEU SEQRES 34 A 446 GLY GLY GLY ILE VAL LEU VAL ILE ALA SER ILE VAL PHE SEQRES 35 A 446 GLY MET MET ILE SEQRES 1 B 446 MET THR ASN MET SER GLN PRO PRO ALA THR GLU LYS LYS SEQRES 2 B 446 GLY VAL SER ASP LEU LEU GLY PHE LYS ILE PHE GLY MET SEQRES 3 B 446 PRO LEU PRO LEU TYR ALA PHE ALA LEU ILE THR LEU LEU SEQRES 4 B 446 LEU SER HIS PHE TYR ASN ALA LEU PRO THR ASP ILE VAL SEQRES 5 B 446 GLY GLY PHE ALA ILE MET PHE ILE ILE GLY ALA ILE PHE SEQRES 6 B 446 GLY GLU ILE GLY LYS ARG LEU PRO ILE PHE ASN LYS TYR SEQRES 7 B 446 ILE GLY GLY ALA PRO VAL MET ILE PHE LEU VAL ALA ALA SEQRES 8 B 446 TYR PHE VAL TYR ALA GLY ILE PHE THR GLN LYS GLU ILE SEQRES 9 B 446 ASP ALA ILE SER ASN VAL MET ASP LYS SER ASN PHE LEU SEQRES 10 B 446 ASN LEU PHE ILE ALA VAL LEU ILE THR GLY ALA ILE LEU SEQRES 11 B 446 SER VAL ASN ARG ARG LEU LEU LEU LYS SER LEU LEU GLY SEQRES 12 B 446 TYR ILE PRO THR ILE LEU MET GLY ILE VAL GLY ALA SER SEQRES 13 B 446 ILE PHE GLY ILE ALA ILE GLY LEU VAL PHE GLY ILE PRO SEQRES 14 B 446 VAL ASP ARG ILE MET MET LEU TYR VAL LEU PRO ILE MET SEQRES 15 B 446 GLY GLY GLY ASN GLY ALA GLY ALA VAL PRO LEU SER GLU SEQRES 16 B 446 ILE TYR HIS SER VAL THR GLY ARG SER ARG GLU GLU TYR SEQRES 17 B 446 TYR SER THR ALA ILE ALA ILE LEU THR ILE ALA ASN ILE SEQRES 18 B 446 PHE ALA ILE VAL PHE ALA ALA VAL LEU ASP ILE ILE GLY SEQRES 19 B 446 LYS LYS HIS THR TRP LEU SER GLY GLU GLY GLU LEU VAL SEQRES 20 B 446 ARG LYS ALA SER PHE LYS VAL GLU GLU ASP GLU LYS THR SEQRES 21 B 446 GLY GLN ILE THR HIS ARG GLU THR ALA VAL GLY LEU VAL SEQRES 22 B 446 LEU SER THR THR CYS PHE LEU LEU ALA TYR VAL VAL ALA SEQRES 23 B 446 LYS LYS ILE LEU PRO SER ILE GLY GLY VAL ALA ILE HIS SEQRES 24 B 446 TYR PHE ALA TRP MET VAL LEU ILE VAL ALA ALA LEU ASN SEQRES 25 B 446 ALA SER GLY LEU CYS SER PRO GLU ILE LYS ALA GLY ALA SEQRES 26 B 446 LYS ARG LEU SER ASP PHE PHE SER LYS GLN LEU LEU TRP SEQRES 27 B 446 VAL LEU MET VAL GLY VAL GLY VAL CYS TYR THR ASP LEU SEQRES 28 B 446 GLN GLU ILE ILE ASN ALA ILE THR PHE ALA ASN VAL VAL SEQRES 29 B 446 ILE ALA ALA ILE ILE VAL ILE GLY ALA VAL LEU GLY ALA SEQRES 30 B 446 ALA ILE GLY GLY TRP LEU MET GLY PHE PHE PRO ILE GLU SEQRES 31 B 446 SER ALA ILE THR ALA GLY LEU CYS MET ALA ASN ARG GLY SEQRES 32 B 446 GLY SER GLY ASP LEU GLU VAL LEU SER ALA CYS ASN ARG SEQRES 33 B 446 MET ASN LEU ILE SER TYR ALA GLN ILE SER SER ARG LEU SEQRES 34 B 446 GLY GLY GLY ILE VAL LEU VAL ILE ALA SER ILE VAL PHE SEQRES 35 B 446 GLY MET MET ILE SEQRES 1 C 904 MET ARG GLN THR LEU PRO CYS ILE TYR PHE TRP GLY GLY SEQRES 2 C 904 LEU LEU PRO PHE GLY MET LEU CYS ALA SER SER THR THR SEQRES 3 C 904 LYS CYS THR VAL SER HIS GLU VAL ALA ASP CYS SER HIS SEQRES 4 C 904 LEU LYS LEU THR GLN VAL PRO ASP ASP LEU PRO THR ASN SEQRES 5 C 904 ILE THR VAL LEU ASN LEU THR HIS ASN GLN LEU ARG ARG SEQRES 6 C 904 LEU PRO ALA ALA ASN PHE THR ARG TYR SER GLN LEU THR SEQRES 7 C 904 SER LEU ASP VAL GLY PHE ASN THR ILE SER LYS LEU GLU SEQRES 8 C 904 PRO GLU LEU CYS GLN LYS LEU PRO MET LEU LYS VAL LEU SEQRES 9 C 904 ASN LEU GLN HIS ASN GLU LEU SER GLN LEU SER ASP LYS SEQRES 10 C 904 THR PHE ALA PHE CYS THR ASN LEU THR GLU LEU HIS LEU SEQRES 11 C 904 MET SER ASN SER ILE GLN LYS ILE LYS ASN ASN PRO PHE SEQRES 12 C 904 VAL LYS GLN LYS ASN LEU ILE THR LEU ASP LEU SER HIS SEQRES 13 C 904 ASN GLY LEU SER SER THR LYS LEU GLY THR GLN VAL GLN SEQRES 14 C 904 LEU GLU ASN LEU GLN GLU LEU LEU LEU SER ASN ASN LYS SEQRES 15 C 904 ILE GLN ALA LEU LYS SER GLU GLU LEU ASP ILE PHE ALA SEQRES 16 C 904 ASN SER SER LEU LYS LYS LEU GLU LEU SER SER ASN GLN SEQRES 17 C 904 ILE LYS GLU PHE SER PRO GLY CYS PHE HIS ALA ILE GLY SEQRES 18 C 904 ARG LEU PHE GLY LEU PHE LEU ASN ASN VAL GLN LEU GLY SEQRES 19 C 904 PRO SER LEU THR GLU LYS LEU CYS LEU GLU LEU ALA ASN SEQRES 20 C 904 THR SER ILE ARG ASN LEU SER LEU SER ASN SER GLN LEU SEQRES 21 C 904 SER THR THR SER ASN THR THR PHE LEU GLY LEU LYS TRP SEQRES 22 C 904 THR ASN LEU THR MET LEU ASP LEU SER TYR ASN ASN LEU SEQRES 23 C 904 ASN VAL VAL GLY ASN ASP SER PHE ALA TRP LEU PRO GLN SEQRES 24 C 904 LEU GLU TYR PHE PHE LEU GLU TYR ASN ASN ILE GLN HIS SEQRES 25 C 904 LEU PHE SER HIS SER LEU HIS GLY LEU PHE ASN VAL ARG SEQRES 26 C 904 TYR LEU ASN LEU LYS ARG SER PHE THR LYS GLN SER ILE SEQRES 27 C 904 SER LEU ALA SER LEU PRO LYS ILE ASP ASP PHE SER PHE SEQRES 28 C 904 GLN TRP LEU LYS CYS LEU GLU HIS LEU ASN MET GLU ASP SEQRES 29 C 904 ASN ASP ILE PRO GLY ILE LYS SER ASN MET PHE THR GLY SEQRES 30 C 904 LEU ILE ASN LEU LYS TYR LEU SER LEU SER ASN SER PHE SEQRES 31 C 904 THR SER LEU ARG THR LEU THR ASN GLU THR PHE VAL SER SEQRES 32 C 904 LEU ALA HIS SER PRO LEU HIS ILE LEU ASN LEU THR LYS SEQRES 33 C 904 ASN LYS ILE SER LYS ILE GLU SER ASP ALA PHE SER TRP SEQRES 34 C 904 LEU GLY HIS LEU GLU VAL LEU ASP LEU GLY LEU ASN GLU SEQRES 35 C 904 ILE GLY GLN GLU LEU THR GLY GLN GLU TRP ARG GLY LEU SEQRES 36 C 904 GLU ASN ILE PHE GLU ILE TYR LEU SER TYR ASN LYS TYR SEQRES 37 C 904 LEU GLN LEU THR ARG ASN SER PHE ALA LEU VAL PRO SER SEQRES 38 C 904 LEU GLN ARG LEU MET LEU ARG ARG VAL ALA LEU LYS ASN SEQRES 39 C 904 VAL ASP SER SER PRO SER PRO PHE GLN PRO LEU ARG ASN SEQRES 40 C 904 LEU THR ILE LEU ASP LEU SER ASN ASN ASN ILE ALA ASN SEQRES 41 C 904 ILE ASN ASP ASP MET LEU GLU GLY LEU GLU LYS LEU GLU SEQRES 42 C 904 ILE LEU ASP LEU GLN HIS ASN ASN LEU ALA ARG LEU TRP SEQRES 43 C 904 LYS HIS ALA ASN PRO GLY GLY PRO ILE TYR PHE LEU LYS SEQRES 44 C 904 GLY LEU SER HIS LEU HIS ILE LEU ASN LEU GLU SER ASN SEQRES 45 C 904 GLY PHE ASP GLU ILE PRO VAL GLU VAL PHE LYS ASP LEU SEQRES 46 C 904 PHE GLU LEU LYS ILE ILE ASP LEU GLY LEU ASN ASN LEU SEQRES 47 C 904 ASN THR LEU PRO ALA SER VAL PHE ASN ASN GLN VAL SER SEQRES 48 C 904 LEU LYS SER LEU ASN LEU GLN LYS ASN LEU ILE THR SER SEQRES 49 C 904 VAL GLU LYS LYS VAL PHE GLY PRO ALA PHE ARG ASN LEU SEQRES 50 C 904 THR GLU LEU ASP MET ARG PHE ASN PRO PHE ASP CYS THR SEQRES 51 C 904 CYS GLU SER ILE ALA TRP PHE VAL ASN TRP ILE ASN GLU SEQRES 52 C 904 THR HIS THR ASN ILE PRO GLU LEU SER SER HIS TYR LEU SEQRES 53 C 904 CYS ASN THR PRO PRO HIS TYR HIS GLY PHE PRO VAL ARG SEQRES 54 C 904 LEU PHE ASP THR SER SER CYS LYS ASP SER ALA PRO PHE SEQRES 55 C 904 GLU LEU PHE PHE MET ILE ASN THR SER ILE LEU LEU ILE SEQRES 56 C 904 PHE ILE PHE ILE VAL LEU LEU ILE HIS PHE GLU GLY TRP SEQRES 57 C 904 ARG ILE SER PHE TYR TRP ASN VAL SER VAL HIS ARG VAL SEQRES 58 C 904 LEU GLY PHE LYS GLU ILE ASP ARG GLN THR GLU GLN PHE SEQRES 59 C 904 GLU TYR ALA ALA TYR ILE ILE HIS ALA TYR LYS ASP LYS SEQRES 60 C 904 ASP TRP VAL TRP GLU HIS PHE SER SER MET GLU LYS GLU SEQRES 61 C 904 ASP GLN SER LEU LYS PHE CYS LEU GLU GLU ARG ASP PHE SEQRES 62 C 904 GLU ALA GLY VAL PHE GLU LEU GLU ALA ILE VAL ASN SER SEQRES 63 C 904 ILE LYS ARG SER ARG LYS ILE ILE PHE VAL ILE THR HIS SEQRES 64 C 904 HIS LEU LEU LYS ASP PRO LEU CYS LYS ARG PHE LYS VAL SEQRES 65 C 904 HIS HIS ALA VAL GLN GLN ALA ILE GLU GLN ASN LEU ASP SEQRES 66 C 904 SER ILE ILE LEU VAL PHE LEU GLU GLU ILE PRO ASP TYR SEQRES 67 C 904 LYS LEU ASN HIS ALA LEU CYS LEU ARG ARG GLY MET PHE SEQRES 68 C 904 LYS SER HIS CYS ILE LEU ASN TRP PRO VAL GLN LYS GLU SEQRES 69 C 904 ARG ILE GLY ALA PHE ARG HIS LYS LEU GLN VAL ALA LEU SEQRES 70 C 904 GLY SER LYS ASN SER VAL HIS SEQRES 1 D 256 GLU VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 256 PRO CYS GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 256 PHE THR PHE ARG ASN SER ALA MET HIS TRP VAL ARG GLN SEQRES 4 D 256 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER SER ILE TRP SEQRES 5 D 256 TYR SER GLY SER ASN THR TYR TYR ALA ASP SER VAL LYS SEQRES 6 D 256 GLY ARG PHE THR ILE SER ARG ASP ASN SER LYS ASN THR SEQRES 7 D 256 LEU TYR LEU GLN MET ASN SER LEU CYS ALA GLU ASP THR SEQRES 8 D 256 ALA VAL TYR TYR CYS ALA ARG PHE ALA GLY GLY TRP GLY SEQRES 9 D 256 ALA TYR ASP VAL TRP GLY GLN GLY THR LEU VAL THR VAL SEQRES 10 D 256 SER SER GLY GLY GLY GLY SER ASP ILE GLN MET THR GLN SEQRES 11 D 256 SER PRO SER SER LEU SER ALA SER VAL GLY ASP ARG VAL SEQRES 12 D 256 THR ILE THR CYS ARG ALA SER GLN SER ILE GLY LEU TYR SEQRES 13 D 256 LEU ALA TRP TYR GLN GLN LYS PRO GLY LYS ALA PRO LYS SEQRES 14 D 256 LEU LEU ILE TYR ALA ALA SER SER LEU GLN SER GLY VAL SEQRES 15 D 256 PRO SER ARG PHE SER GLY SER GLY SER GLY THR ASP PHE SEQRES 16 D 256 THR LEU THR ILE SER SER LEU GLN PRO GLU ASP PHE ALA SEQRES 17 D 256 THR TYR TYR CYS GLN GLN GLY ASN THR LEU SER TYR THR SEQRES 18 D 256 PHE GLY GLN GLY THR LYS VAL GLU ILE LYS PRO TRP LEU SEQRES 19 D 256 VAL PRO ARG GLY SER HIS HIS HIS HIS HIS HIS SER GLY SEQRES 20 D 256 GLY GLY GLY SER GLY GLY GLY GLY SER SEQRES 1 E 266 GLY GLY GLY GLY SER GLY GLY GLY GLY LEU VAL PRO ARG SEQRES 2 E 266 GLY SER PRO GLY GLU VAL GLN LEU VAL GLN SER GLY ALA SEQRES 3 E 266 GLU VAL LYS LYS PRO GLY GLU SER LEU LYS ILE SER CYS SEQRES 4 E 266 LYS GLY SER GLY TYR SER PHE THR ASN TYR TRP VAL GLY SEQRES 5 E 266 TRP VAL ARG GLN MET PRO GLY LYS GLY LEU GLU TRP MET SEQRES 6 E 266 GLY PHE ILE ASP PRO SER ASP SER TYR THR ASN TYR ALA SEQRES 7 E 266 ASP SER VAL LYS GLY CYS PHE THR ILE SER ALA ASP LYS SEQRES 8 E 266 SER ILE SER THR ALA TYR LEU GLN MET ASN SER LEU CYS SEQRES 9 E 266 ALA SER ASP THR ALA MET TYR TYR CYS ALA ARG GLU LEU SEQRES 10 E 266 TYR GLN GLY TYR MET ASP THR PHE ASP SER TRP GLY GLN SEQRES 11 E 266 GLY THR LEU VAL THR VAL SER SER GLY GLY GLY GLY SER SEQRES 12 E 266 ASP ILE VAL LEU THR GLN SER PRO ALA THR LEU SER LEU SEQRES 13 E 266 SER PRO GLY GLU ARG ALA THR LEU SER CYS ARG ALA SER SEQRES 14 E 266 GLN SER VAL SER SER ASN TYR LEU ALA TRP TYR GLN GLN SEQRES 15 E 266 LYS PRO GLY GLN ALA PRO ARG LEU LEU ILE TYR ASP SER SEQRES 16 E 266 SER SER ARG ALA THR GLY VAL PRO ALA ARG PHE SER GLY SEQRES 17 E 266 SER GLY SER GLY THR ASP PHE THR LEU THR ILE SER SER SEQRES 18 E 266 LEU GLU PRO GLU ASP PHE ALA VAL TYR TYR CYS HIS GLN SEQRES 19 E 266 TYR SER ASP ILE SER PRO THR PHE GLY GLN GLY THR LYS SEQRES 20 E 266 VAL GLU ILE LYS SER GLY ARG LEU VAL PRO ARG GLY SER SEQRES 21 E 266 HIS HIS HIS HIS HIS HIS HET NAG H 1 14 HET NAG H 2 14 HET NAG F 1 14 HET NAG F 2 14 HET NAG G 1 14 HET NAG G 2 14 HET BMA G 3 11 HET NAG I 1 14 HET NAG I 2 14 HET CIT A 501 13 HET PLM A 502 18 HET NAG C1001 14 HET NAG C1002 14 HET NAG C1003 14 HET NAG C1004 14 HETNAM NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE HETNAM BMA BETA-D-MANNOPYRANOSE HETNAM CIT CITRIC ACID HETNAM PLM PALMITIC 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 FORMUL 6 NAG 12(C8 H15 N O6) FORMUL 8 BMA C6 H12 O6 FORMUL 10 CIT C6 H8 O7 FORMUL 11 PLM C16 H32 O2 HELIX 1 AA1 LEU A 28 ASN A 45 1 18 HELIX 2 AA2 ASP A 50 LYS A 70 1 21 HELIX 3 AA3 ILE A 74 ILE A 79 1 6 HELIX 4 AA4 GLY A 81 ALA A 96 1 16 HELIX 5 AA5 THR A 100 ASP A 112 1 13 HELIX 6 AA6 ASN A 115 LEU A 130 1 16 HELIX 7 AA7 SER A 131 VAL A 132 5 2 HELIX 8 AA8 ASN A 133 ARG A 135 5 3 HELIX 9 AA9 LEU A 136 GLY A 143 1 8 HELIX 10 AB1 GLY A 143 PHE A 166 1 24 HELIX 11 AB2 PRO A 169 TYR A 177 1 9 HELIX 12 AB3 TYR A 177 GLY A 183 1 7 HELIX 13 AB4 ALA A 190 GLY A 202 1 13 HELIX 14 AB5 SER A 204 HIS A 237 1 34 HELIX 15 AB6 THR A 264 ILE A 289 1 26 HELIX 16 AB7 HIS A 299 GLY A 315 1 17 HELIX 17 AB8 SER A 318 GLN A 335 1 18 HELIX 18 AB9 LEU A 336 TYR A 348 1 13 HELIX 19 AC1 ASP A 350 ALA A 357 1 8 HELIX 20 AC2 THR A 359 MET A 384 1 26 HELIX 21 AC3 ILE A 389 THR A 394 1 6 HELIX 22 AC4 ARG A 402 ASN A 415 1 14 HELIX 23 AC5 LEU A 419 ILE A 446 1 28 HELIX 24 AC6 LEU B 28 ASN B 45 1 18 HELIX 25 AC7 ASP B 50 ARG B 71 1 22 HELIX 26 AC8 LEU B 72 ILE B 79 1 8 HELIX 27 AC9 GLY B 81 ALA B 96 1 16 HELIX 28 AD1 THR B 100 ASP B 112 1 13 HELIX 29 AD2 ASN B 115 SER B 131 1 17 HELIX 30 AD3 ASN B 133 LEU B 141 1 9 HELIX 31 AD4 GLY B 143 GLY B 167 1 25 HELIX 32 AD5 PRO B 169 TYR B 177 1 9 HELIX 33 AD6 TYR B 177 MET B 182 1 6 HELIX 34 AD7 ALA B 190 THR B 201 1 12 HELIX 35 AD8 SER B 204 HIS B 237 1 34 HELIX 36 AD9 THR B 264 ILE B 289 1 26 HELIX 37 AE1 HIS B 299 GLY B 315 1 17 HELIX 38 AE2 SER B 318 GLN B 335 1 18 HELIX 39 AE3 LEU B 336 TYR B 348 1 13 HELIX 40 AE4 ASP B 350 ILE B 358 1 9 HELIX 41 AE5 THR B 359 MET B 384 1 26 HELIX 42 AE6 PHE B 387 GLY B 396 1 10 HELIX 43 AE7 GLY B 403 CYS B 414 1 12 HELIX 44 AE8 LEU B 419 ILE B 446 1 28 HELIX 45 AE9 PRO C 67 TYR C 74 1 8 HELIX 46 AF1 GLU C 91 LEU C 98 1 8 HELIX 47 AF2 SER C 115 CYS C 122 1 8 HELIX 48 AF3 SER C 188 ILE C 193 5 6 HELIX 49 AF4 LEU C 233 LEU C 245 1 13 HELIX 50 AF5 ASN C 265 THR C 274 5 10 HELIX 51 AF6 PHE C 314 HIS C 319 5 6 HELIX 52 AF7 PHE C 401 ALA C 405 5 5 HELIX 53 AF8 GLY C 449 ARG C 453 5 5 HELIX 54 AF9 ASN C 522 LEU C 526 5 5 HELIX 55 AG1 ALA C 543 LYS C 547 5 5 HELIX 56 AG2 SER C 653 THR C 664 1 12 HELIX 57 AG3 TYR D 53 SER D 56 5 4 HELIX 58 AG4 ASP D 62 LYS D 65 5 4 HELIX 59 AG5 ASN D 74 ASN D 77 5 4 HELIX 60 AG6 SER E 336 GLY E 339 5 4 HELIX 61 AG7 VAL E 428 ASN E 431 5 4 SHEET 1 AA1 2 LYS A 22 ILE A 23 0 SHEET 2 AA1 2 MET A 26 PRO A 27 -1 O MET A 26 N ILE A 23 SHEET 1 AA2 2 SER A 292 ILE A 293 0 SHEET 2 AA2 2 VAL A 296 ALA A 297 -1 O VAL A 296 N ILE A 293 SHEET 1 AA3 2 LYS B 22 ILE B 23 0 SHEET 2 AA3 2 MET B 26 PRO B 27 -1 O MET B 26 N ILE B 23 SHEET 1 AA424 VAL C 34 SER C 38 0 SHEET 2 AA424 VAL C 55 THR C 59 1 O VAL C 55 N ALA C 35 SHEET 3 AA424 SER C 79 VAL C 82 1 O ASP C 81 N LEU C 58 SHEET 4 AA424 VAL C 103 GLN C 107 1 O VAL C 103 N LEU C 80 SHEET 5 AA424 GLU C 127 MET C 131 1 O GLU C 127 N LEU C 104 SHEET 6 AA424 THR C 151 ASP C 153 1 O THR C 151 N LEU C 128 SHEET 7 AA424 GLU C 175 LEU C 177 1 O GLU C 175 N LEU C 152 SHEET 8 AA424 LYS C 201 GLU C 203 1 O GLU C 203 N LEU C 176 SHEET 9 AA424 GLY C 225 ASN C 229 1 O PHE C 227 N LEU C 202 SHEET 10 AA424 ASN C 252 SER C 256 1 O ASN C 252 N LEU C 226 SHEET 11 AA424 MET C 278 ASP C 280 1 O ASP C 280 N LEU C 255 SHEET 12 AA424 TYR C 302 PHE C 304 1 O PHE C 304 N LEU C 279 SHEET 13 AA424 TYR C 326 ASN C 328 1 O ASN C 328 N PHE C 303 SHEET 14 AA424 HIS C 359 ASN C 361 1 O HIS C 359 N LEU C 327 SHEET 15 AA424 TYR C 383 SER C 385 1 O SER C 385 N LEU C 360 SHEET 16 AA424 ILE C 411 ASN C 413 1 O ILE C 411 N LEU C 384 SHEET 17 AA424 VAL C 435 ASP C 437 1 O VAL C 435 N LEU C 412 SHEET 18 AA424 GLU C 460 TYR C 462 1 O TYR C 462 N LEU C 436 SHEET 19 AA424 ARG C 484 MET C 486 1 O ARG C 484 N ILE C 461 SHEET 20 AA424 ILE C 510 ASP C 512 1 O ILE C 510 N LEU C 485 SHEET 21 AA424 ILE C 534 ASP C 536 1 O ILE C 534 N LEU C 511 SHEET 22 AA424 ILE C 566 ASN C 568 1 O ILE C 566 N LEU C 535 SHEET 23 AA424 ILE C 590 ASP C 592 1 O ILE C 590 N LEU C 567 SHEET 24 AA424 SER C 614 ASN C 616 1 O SER C 614 N ILE C 591 SHEET 1 AA5 2 ALA C 185 LEU C 186 0 SHEET 2 AA5 2 GLU C 211 PHE C 212 1 O GLU C 211 N LEU C 186 SHEET 1 AA6 2 THR C 262 THR C 263 0 SHEET 2 AA6 2 VAL C 288 VAL C 289 1 O VAL C 288 N THR C 263 SHEET 1 AA7 2 HIS C 312 LEU C 313 0 SHEET 2 AA7 2 LYS C 345 ILE C 346 1 O LYS C 345 N LEU C 313 SHEET 1 AA8 2 THR C 395 LEU C 396 0 SHEET 2 AA8 2 LYS C 421 ILE C 422 1 O LYS C 421 N LEU C 396 SHEET 1 AA9 3 GLY C 444 GLU C 446 0 SHEET 2 AA9 3 TYR C 468 GLN C 470 1 O GLN C 470 N GLN C 445 SHEET 3 AA9 3 LEU C 492 LYS C 493 1 O LYS C 493 N LEU C 469 SHEET 1 AB1 2 LEU C 676 CYS C 677 0 SHEET 2 AB1 2 PHE C 686 PRO C 687 -1 O PHE C 686 N CYS C 677 SHEET 1 AB2 2 VAL D 2 LEU D 4 0 SHEET 2 AB2 2 ALA D 23 SER D 25 -1 O SER D 25 N VAL D 2 SHEET 1 AB3 6 GLY D 10 VAL D 12 0 SHEET 2 AB3 6 THR D 113 VAL D 117 1 O THR D 116 N GLY D 10 SHEET 3 AB3 6 ALA D 92 PHE D 99 -1 N TYR D 94 O THR D 113 SHEET 4 AB3 6 ALA D 33 GLN D 39 -1 N VAL D 37 O TYR D 95 SHEET 5 AB3 6 LEU D 45 ILE D 51 -1 O SER D 49 N TRP D 36 SHEET 6 AB3 6 THR D 58 TYR D 60 -1 O TYR D 59 N SER D 50 SHEET 1 AB4 4 GLY D 10 VAL D 12 0 SHEET 2 AB4 4 THR D 113 VAL D 117 1 O THR D 116 N GLY D 10 SHEET 3 AB4 4 ALA D 92 PHE D 99 -1 N TYR D 94 O THR D 113 SHEET 4 AB4 4 TYR D 106 TRP D 109 -1 O VAL D 108 N ARG D 98 SHEET 1 AB5 3 LEU D 18 LEU D 20 0 SHEET 2 AB5 3 THR D 78 MET D 83 -1 O MET D 83 N LEU D 18 SHEET 3 AB5 3 PHE D 68 ASP D 73 -1 N THR D 69 O GLN D 82 SHEET 1 AB6 4 MET D 128 GLN D 130 0 SHEET 2 AB6 4 VAL D 143 ALA D 149 -1 O ARG D 148 N THR D 129 SHEET 3 AB6 4 ASP D 194 ILE D 199 -1 O LEU D 197 N ILE D 145 SHEET 4 AB6 4 PHE D 186 SER D 191 -1 N SER D 187 O THR D 198 SHEET 1 AB7 2 LEU D 157 GLN D 162 0 SHEET 2 AB7 2 THR D 209 GLN D 214 -1 O TYR D 211 N TYR D 160 SHEET 1 AB8 4 GLN E 276 GLN E 279 0 SHEET 2 AB8 4 LEU E 291 SER E 298 -1 O SER E 298 N GLN E 276 SHEET 3 AB8 4 THR E 351 MET E 356 -1 O ALA E 352 N CYS E 295 SHEET 4 AB8 4 PHE E 341 ASP E 346 -1 N SER E 344 O TYR E 353 SHEET 1 AB9 6 GLU E 283 LYS E 285 0 SHEET 2 AB9 6 THR E 388 VAL E 392 1 O THR E 391 N GLU E 283 SHEET 3 AB9 6 ALA E 365 GLU E 372 -1 N TYR E 367 O THR E 388 SHEET 4 AB9 6 TRP E 306 GLN E 312 -1 N VAL E 310 O TYR E 368 SHEET 5 AB9 6 LEU E 318 ILE E 324 -1 O ILE E 324 N VAL E 307 SHEET 6 AB9 6 THR E 331 TYR E 333 -1 O ASN E 332 N PHE E 323 SHEET 1 AC1 4 GLU E 283 LYS E 285 0 SHEET 2 AC1 4 THR E 388 VAL E 392 1 O THR E 391 N GLU E 283 SHEET 3 AC1 4 ALA E 365 GLU E 372 -1 N TYR E 367 O THR E 388 SHEET 4 AC1 4 PHE E 381 TRP E 384 -1 O SER E 383 N ARG E 371 SHEET 1 AC2 5 THR E 409 SER E 411 0 SHEET 2 AC2 5 THR E 502 GLU E 505 1 O GLU E 505 N LEU E 410 SHEET 3 AC2 5 VAL E 485 GLN E 490 -1 N TYR E 486 O THR E 502 SHEET 4 AC2 5 LEU E 433 GLN E 438 -1 N ALA E 434 O HIS E 489 SHEET 5 AC2 5 ARG E 445 ILE E 448 -1 O ARG E 445 N GLN E 437 SHEET 1 AC3 3 LEU E 420 ARG E 423 0 SHEET 2 AC3 3 ASP E 470 ILE E 475 -1 O PHE E 471 N CYS E 422 SHEET 3 AC3 3 PHE E 462 SER E 465 -1 N SER E 463 O THR E 474 SSBOND 1 CYS C 95 CYS C 122 1555 1555 2.03 SSBOND 2 CYS C 649 CYS C 677 1555 1555 2.03 SSBOND 3 CYS D 15 CYS E 340 1555 1555 2.03 SSBOND 4 CYS D 22 CYS D 96 1555 1555 2.03 SSBOND 5 CYS D 87 CYS E 360 1555 1555 2.03 SSBOND 6 CYS D 147 CYS D 212 1555 1555 2.04 SSBOND 7 CYS E 295 CYS E 369 1555 1555 2.03 SSBOND 8 CYS E 422 CYS E 488 1555 1555 2.03 LINK ND2 ASN C 52 C1 NAG C1001 1555 1555 1.44 LINK ND2 ASN C 252 C1 NAG H 1 1555 1555 1.45 LINK ND2 ASN C 265 C1 NAG C1002 1555 1555 1.44 LINK ND2 ASN C 275 C1 NAG C1003 1555 1555 1.45 LINK ND2 ASN C 291 C1 NAG F 1 1555 1555 1.44 LINK ND2 ASN C 398 C1 NAG C1004 1555 1555 1.45 LINK ND2 ASN C 413 C1 NAG G 1 1555 1555 1.45 LINK ND2 ASN C 507 C1 NAG I 1 1555 1555 1.44 LINK O4 NAG H 1 C1 NAG H 2 1555 1555 1.44 LINK O4 NAG F 1 C1 NAG F 2 1555 1555 1.44 LINK O4 NAG G 1 C1 NAG G 2 1555 1555 1.39 LINK O3 NAG G 2 C1 BMA G 3 1555 1555 1.39 LINK O4 NAG I 1 C1 NAG I 2 1555 1555 1.44 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