HEADER MEMBRANE PROTEIN 10-JAN-24 8XT9 TITLE STRUCTURE OF LGR4 COMPND MOL_ID: 1; COMPND 2 MOLECULE: LEUCINE-RICH REPEAT-CONTAINING G-PROTEIN COUPLED RECEPTOR COMPND 3 4; COMPND 4 CHAIN: C; COMPND 5 SYNONYM: G-PROTEIN COUPLED RECEPTOR 48; COMPND 6 ENGINEERED: YES; COMPND 7 MOL_ID: 2; COMPND 8 MOLECULE: MB52; COMPND 9 CHAIN: A; COMPND 10 ENGINEERED: YES SOURCE MOL_ID: 1; SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 3 ORGANISM_COMMON: HUMAN; SOURCE 4 ORGANISM_TAXID: 9606; SOURCE 5 GENE: LGR4, GPR48; SOURCE 6 EXPRESSION_SYSTEM: HOMO SAPIENS; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 9606; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: CAMELUS BACTRIANUS; SOURCE 10 ORGANISM_TAXID: 9837; SOURCE 11 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 562 KEYWDS LGR4, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR L.WANG,Y.GENG REVDAT 1 15-JAN-25 8XT9 0 JRNL AUTH L.WANG,Y.GENG JRNL TITL STRUCTURE OF LGR4 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 : 177214 REMARK 3 CTF CORRECTION METHOD : NONE REMARK 3 REMARK 3 EM RECONSTRUCTION MAGNIFICATION CALIBRATION: NULL REMARK 3 REMARK 3 OTHER DETAILS: NULL REMARK 4 REMARK 4 8XT9 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 15-JAN-24. REMARK 100 THE DEPOSITION ID IS D_1300044145. 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 : STRUCTURE OF LGR4 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 : 7.40 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 TITAN REMARK 245 DETECTOR TYPE : GATAN K3 (6K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1500.00 REMARK 245 MAXIMUM DEFOCUS (NM) : 2500.00 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) : 194.40 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: C, A 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 C 1 REMARK 465 PRO C 2 REMARK 465 GLY C 3 REMARK 465 PRO C 4 REMARK 465 LEU C 5 REMARK 465 GLY C 6 REMARK 465 LEU C 7 REMARK 465 LEU C 8 REMARK 465 CYS C 9 REMARK 465 PHE C 10 REMARK 465 LEU C 11 REMARK 465 ALA C 12 REMARK 465 LEU C 13 REMARK 465 GLY C 14 REMARK 465 LEU C 15 REMARK 465 LEU C 16 REMARK 465 GLY C 17 REMARK 465 SER C 18 REMARK 465 ALA C 19 REMARK 465 GLY C 20 REMARK 465 PRO C 21 REMARK 465 SER C 22 REMARK 465 GLY C 23 REMARK 465 ALA C 24 REMARK 465 ALA C 25 REMARK 465 PRO C 26 REMARK 465 PRO C 27 REMARK 465 LEU C 28 REMARK 465 GLY C 475 REMARK 465 CYS C 476 REMARK 465 ASP C 477 REMARK 465 SER C 478 REMARK 465 TYR C 479 REMARK 465 ALA C 480 REMARK 465 ASN C 481 REMARK 465 LEU C 482 REMARK 465 ASN C 483 REMARK 465 THR C 484 REMARK 465 GLU C 485 REMARK 465 ASP C 486 REMARK 465 ASN C 487 REMARK 465 SER C 488 REMARK 465 LEU C 489 REMARK 465 GLN C 490 REMARK 465 ASP C 491 REMARK 465 HIS C 492 REMARK 465 SER C 493 REMARK 465 VAL C 494 REMARK 465 ALA C 495 REMARK 465 GLN C 496 REMARK 465 GLU C 497 REMARK 465 LYS C 498 REMARK 465 GLY C 499 REMARK 465 THR C 500 REMARK 465 ALA C 501 REMARK 465 ASP C 502 REMARK 465 ALA C 503 REMARK 465 ALA C 504 REMARK 465 ASN C 505 REMARK 465 VAL C 506 REMARK 465 THR C 507 REMARK 465 SER C 508 REMARK 465 THR C 509 REMARK 465 LEU C 510 REMARK 465 GLU C 511 REMARK 465 ASN C 512 REMARK 465 GLU C 513 REMARK 465 GLU C 514 REMARK 465 HIS C 515 REMARK 465 SER C 516 REMARK 465 GLN C 517 REMARK 465 ILE C 650 REMARK 465 MET C 651 REMARK 465 LYS C 652 REMARK 465 ASN C 653 REMARK 465 GLY C 654 REMARK 465 GLU C 733 REMARK 465 LYS C 734 REMARK 465 GLU C 735 REMARK 465 ASP C 736 REMARK 465 LEU C 737 REMARK 465 SER C 738 REMARK 465 GLU C 739 REMARK 465 ASN C 740 REMARK 465 LYS C 822 REMARK 465 SER C 823 REMARK 465 GLY C 824 REMARK 465 SER C 825 REMARK 465 VAL C 826 REMARK 465 SER C 827 REMARK 465 VAL C 828 REMARK 465 SER C 829 REMARK 465 ILE C 830 REMARK 465 SER C 831 REMARK 465 SER C 832 REMARK 465 GLN C 833 REMARK 465 GLY C 834 REMARK 465 GLY C 835 REMARK 465 CYS C 836 REMARK 465 LEU C 837 REMARK 465 GLU C 838 REMARK 465 GLN C 839 REMARK 465 ASP C 840 REMARK 465 PHE C 841 REMARK 465 TYR C 842 REMARK 465 TYR C 843 REMARK 465 ASP C 844 REMARK 465 CYS C 845 REMARK 465 GLY C 846 REMARK 465 MET C 847 REMARK 465 TYR C 848 REMARK 465 SER C 849 REMARK 465 HIS C 850 REMARK 465 LEU C 851 REMARK 465 GLN C 852 REMARK 465 GLY C 853 REMARK 465 ASN C 854 REMARK 465 LEU C 855 REMARK 465 THR C 856 REMARK 465 VAL C 857 REMARK 465 CYS C 858 REMARK 465 ASP C 859 REMARK 465 CYS C 860 REMARK 465 CYS C 861 REMARK 465 GLU C 862 REMARK 465 SER C 863 REMARK 465 PHE C 864 REMARK 465 LEU C 865 REMARK 465 LEU C 866 REMARK 465 THR C 867 REMARK 465 LYS C 868 REMARK 465 PRO C 869 REMARK 465 VAL C 870 REMARK 465 SER C 871 REMARK 465 CYS C 872 REMARK 465 LYS C 873 REMARK 465 HIS C 874 REMARK 465 LEU C 875 REMARK 465 ILE C 876 REMARK 465 LYS C 877 REMARK 465 SER C 878 REMARK 465 HIS C 879 REMARK 465 SER C 880 REMARK 465 CYS C 881 REMARK 465 PRO C 882 REMARK 465 ALA C 883 REMARK 465 LEU C 884 REMARK 465 ALA C 885 REMARK 465 VAL C 886 REMARK 465 ALA C 887 REMARK 465 SER C 888 REMARK 465 CYS C 889 REMARK 465 GLN C 890 REMARK 465 ARG C 891 REMARK 465 PRO C 892 REMARK 465 GLU C 893 REMARK 465 GLY C 894 REMARK 465 TYR C 895 REMARK 465 TRP C 896 REMARK 465 SER C 897 REMARK 465 ASP C 898 REMARK 465 CYS C 899 REMARK 465 GLY C 900 REMARK 465 THR C 901 REMARK 465 GLN C 902 REMARK 465 SER C 903 REMARK 465 ALA C 904 REMARK 465 HIS C 905 REMARK 465 SER C 906 REMARK 465 ASP C 907 REMARK 465 TYR C 908 REMARK 465 ALA C 909 REMARK 465 ASP C 910 REMARK 465 GLU C 911 REMARK 465 GLU C 912 REMARK 465 ASP C 913 REMARK 465 SER C 914 REMARK 465 PHE C 915 REMARK 465 VAL C 916 REMARK 465 SER C 917 REMARK 465 ASP C 918 REMARK 465 SER C 919 REMARK 465 SER C 920 REMARK 465 ASP C 921 REMARK 465 GLN C 922 REMARK 465 VAL C 923 REMARK 465 GLN C 924 REMARK 465 ALA C 925 REMARK 465 CYS C 926 REMARK 465 GLY C 927 REMARK 465 ARG C 928 REMARK 465 ALA C 929 REMARK 465 CYS C 930 REMARK 465 PHE C 931 REMARK 465 TYR C 932 REMARK 465 GLN C 933 REMARK 465 SER C 934 REMARK 465 ARG C 935 REMARK 465 GLY C 936 REMARK 465 PHE C 937 REMARK 465 PRO C 938 REMARK 465 LEU C 939 REMARK 465 VAL C 940 REMARK 465 ARG C 941 REMARK 465 TYR C 942 REMARK 465 ALA C 943 REMARK 465 TYR C 944 REMARK 465 ASN C 945 REMARK 465 LEU C 946 REMARK 465 PRO C 947 REMARK 465 ARG C 948 REMARK 465 VAL C 949 REMARK 465 LYS C 950 REMARK 465 ASP C 951 REMARK 465 GLY A 422 REMARK 465 SER A 423 REMARK 465 VAL A 529 REMARK 465 SER A 530 REMARK 465 SER A 531 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 C 78 CG CD CE NZ REMARK 470 THR C 698 OG1 CG2 REMARK 470 PHE C 766 CG CD1 CD2 CE1 CE2 CZ REMARK 470 LEU A 424 CG CD1 CD2 REMARK 470 ARG A 425 CG CD NE CZ NH1 NH2 REMARK 470 TYR A 433 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 TYR A 438 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 VAL A 454 CG1 CG2 REMARK 470 VAL A 469 CG1 CG2 REMARK 470 ARG A 472 CG CD NE CZ NH1 NH2 REMARK 470 PHE A 473 CG CD1 CD2 CE1 CE2 CZ REMARK 470 ASP A 478 CG OD1 OD2 REMARK 470 MET A 488 CG SD CE REMARK 470 SER A 490 OG REMARK 470 LEU A 491 CG CD1 CD2 REMARK 470 LYS A 492 CG CD CE NZ REMARK 470 GLU A 494 CG CD OE1 OE2 REMARK 470 TYR A 499 CG CD1 CD2 CE1 CE2 CZ OH REMARK 470 ARG A 504 CG CD NE CZ NH1 NH2 REMARK 470 VAL A 527 CG1 CG2 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 C 177 CD PRO C 177 N -0.107 REMARK 500 PRO C 193 CD PRO C 193 N -0.181 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 ASP C 147 CB - CA - C ANGL. DEV. = -15.9 DEGREES REMARK 500 SER C 148 N - CA - CB ANGL. DEV. = 10.2 DEGREES REMARK 500 SER C 148 N - CA - C ANGL. DEV. = -20.0 DEGREES REMARK 500 PRO C 193 C - N - CD ANGL. DEV. = -13.6 DEGREES REMARK 500 PRO C 193 CA - N - CD ANGL. DEV. = 13.2 DEGREES REMARK 500 PRO C 193 N - CA - CB ANGL. DEV. = -7.3 DEGREES REMARK 500 LEU C 713 CA - CB - CG ANGL. DEV. = 14.6 DEGREES REMARK 500 CYS C 761 CA - CB - SG ANGL. DEV. = 6.8 DEGREES REMARK 500 ASN A 489 N - CA - C ANGL. DEV. = 16.9 DEGREES REMARK 500 SER A 490 N - CA - CB ANGL. DEV. = -9.4 DEGREES REMARK 500 ASP A 495 N - CA - CB ANGL. DEV. = -12.6 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 ARG C 39 49.59 38.52 REMARK 500 ASP C 75 50.46 26.86 REMARK 500 LYS C 108 -38.90 -131.10 REMARK 500 ASP C 147 34.35 -97.40 REMARK 500 ASP C 162 66.26 28.93 REMARK 500 LEU C 186 16.84 59.88 REMARK 500 ASP C 281 -2.16 67.35 REMARK 500 THR C 329 -167.13 -79.37 REMARK 500 ASN C 353 -168.21 -78.28 REMARK 500 PRO C 414 48.54 -88.59 REMARK 500 GLU C 431 112.60 -160.18 REMARK 500 LEU C 459 115.51 -163.03 REMARK 500 ALA C 528 -5.48 66.61 REMARK 500 ILE C 610 -74.40 -47.71 REMARK 500 MET C 745 -7.64 67.45 REMARK 500 PRO A 437 3.96 -65.00 REMARK 500 SER A 468 36.13 -99.60 REMARK 500 SER A 490 93.15 38.33 REMARK 500 GLU A 494 -63.28 -21.81 REMARK 500 ASP A 495 52.12 -63.33 REMARK 500 ALA A 507 75.42 46.34 REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: PLANAR GROUPS REMARK 500 REMARK 500 PLANAR GROUPS IN THE FOLLOWING RESIDUES HAVE A TOTAL REMARK 500 RMS DISTANCE OF ALL ATOMS FROM THE BEST-FIT PLANE REMARK 500 BY MORE THAN AN EXPECTED VALUE OF 6*RMSD, WITH AN REMARK 500 RMSD 0.02 ANGSTROMS, OR AT LEAST ONE ATOM HAS REMARK 500 AN RMSD GREATER THAN THIS VALUE REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI RMS TYPE REMARK 500 ARG C 275 0.27 SIDE CHAIN REMARK 500 REMARK 500 REMARK: NULL REMARK 500 REMARK 500 GEOMETRY AND STEREOCHEMISTRY REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY REMARK 500 REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME; REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; REMARK 500 I=INSERTION CODE). REMARK 500 REMARK 500 M RES CSSEQI ANGLE REMARK 500 PRO A 493 10.03 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-38641 RELATED DB: EMDB REMARK 900 STRUCTURE OF LGR4 DBREF 8XT9 C 1 951 UNP Q9BXB1 LGR4_HUMAN 1 951 DBREF 8XT9 A 422 531 PDB 8XT9 8XT9 422 531 SEQRES 1 C 951 MET PRO GLY PRO LEU GLY LEU LEU CYS PHE LEU ALA LEU SEQRES 2 C 951 GLY LEU LEU GLY SER ALA GLY PRO SER GLY ALA ALA PRO SEQRES 3 C 951 PRO LEU CYS ALA ALA PRO CYS SER CYS ASP GLY ASP ARG SEQRES 4 C 951 ARG VAL ASP CYS SER GLY LYS GLY LEU THR ALA VAL PRO SEQRES 5 C 951 GLU GLY LEU SER ALA PHE THR GLN ALA LEU ASP ILE SER SEQRES 6 C 951 MET ASN ASN ILE THR GLN LEU PRO GLU ASP ALA PHE LYS SEQRES 7 C 951 ASN PHE PRO PHE LEU GLU GLU LEU GLN LEU ALA GLY ASN SEQRES 8 C 951 ASP LEU SER PHE ILE HIS PRO LYS ALA LEU SER GLY LEU SEQRES 9 C 951 LYS GLU LEU LYS VAL LEU THR LEU GLN ASN ASN GLN LEU SEQRES 10 C 951 LYS THR VAL PRO SER GLU ALA ILE ARG GLY LEU SER ALA SEQRES 11 C 951 LEU GLN SER LEU ARG LEU ASP ALA ASN HIS ILE THR SER SEQRES 12 C 951 VAL PRO GLU ASP SER PHE GLU GLY LEU VAL GLN LEU ARG SEQRES 13 C 951 HIS LEU TRP LEU ASP ASP ASN SER LEU THR GLU VAL PRO SEQRES 14 C 951 VAL HIS PRO LEU SER ASN LEU PRO THR LEU GLN ALA LEU SEQRES 15 C 951 THR LEU ALA LEU ASN LYS ILE SER SER ILE PRO ASP PHE SEQRES 16 C 951 ALA PHE THR ASN LEU SER SER LEU VAL VAL LEU HIS LEU SEQRES 17 C 951 HIS ASN ASN LYS ILE ARG SER LEU SER GLN HIS CYS PHE SEQRES 18 C 951 ASP GLY LEU ASP ASN LEU GLU THR LEU ASP LEU ASN TYR SEQRES 19 C 951 ASN ASN LEU GLY GLU PHE PRO GLN ALA ILE LYS ALA LEU SEQRES 20 C 951 PRO SER LEU LYS GLU LEU GLY PHE HIS SER ASN SER ILE SEQRES 21 C 951 SER VAL ILE PRO ASP GLY ALA PHE ASP GLY ASN PRO LEU SEQRES 22 C 951 LEU ARG THR ILE HIS LEU TYR ASP ASN PRO LEU SER PHE SEQRES 23 C 951 VAL GLY ASN SER ALA PHE HIS ASN LEU SER ASP LEU HIS SEQRES 24 C 951 SER LEU VAL ILE ARG GLY ALA SER MET VAL GLN GLN PHE SEQRES 25 C 951 PRO ASN LEU THR GLY THR VAL HIS LEU GLU SER LEU THR SEQRES 26 C 951 LEU THR GLY THR LYS ILE SER SER ILE PRO ASN ASN LEU SEQRES 27 C 951 CYS GLN GLU GLN LYS MET LEU ARG THR LEU ASP LEU SER SEQRES 28 C 951 TYR ASN ASN ILE ARG ASP LEU PRO SER PHE ASN GLY CYS SEQRES 29 C 951 HIS ALA LEU GLU GLU ILE SER LEU GLN ARG ASN GLN ILE SEQRES 30 C 951 TYR GLN ILE LYS GLU GLY THR PHE GLN GLY LEU ILE SER SEQRES 31 C 951 LEU ARG ILE LEU ASP LEU SER ARG ASN LEU ILE HIS GLU SEQRES 32 C 951 ILE HIS SER ARG ALA PHE ALA THR LEU GLY PRO ILE THR SEQRES 33 C 951 ASN LEU ASP VAL SER PHE ASN GLU LEU THR SER PHE PRO SEQRES 34 C 951 THR GLU GLY LEU ASN GLY LEU ASN GLN LEU LYS LEU VAL SEQRES 35 C 951 GLY ASN PHE LYS LEU LYS GLU ALA LEU ALA ALA LYS ASP SEQRES 36 C 951 PHE VAL ASN LEU ARG SER LEU SER VAL PRO TYR ALA TYR SEQRES 37 C 951 GLN CYS CYS ALA PHE TRP GLY CYS ASP SER TYR ALA ASN SEQRES 38 C 951 LEU ASN THR GLU ASP ASN SER LEU GLN ASP HIS SER VAL SEQRES 39 C 951 ALA GLN GLU LYS GLY THR ALA ASP ALA ALA ASN VAL THR SEQRES 40 C 951 SER THR LEU GLU ASN GLU GLU HIS SER GLN ILE ILE ILE SEQRES 41 C 951 HIS CYS THR PRO SER THR GLY ALA PHE LYS PRO CYS GLU SEQRES 42 C 951 TYR LEU LEU GLY SER TRP MET ILE ARG LEU THR VAL TRP SEQRES 43 C 951 PHE ILE PHE LEU VAL ALA LEU PHE PHE ASN LEU LEU VAL SEQRES 44 C 951 ILE LEU THR THR PHE ALA SER CYS THR SER LEU PRO SER SEQRES 45 C 951 SER LYS LEU PHE ILE GLY LEU ILE SER VAL SER ASN LEU SEQRES 46 C 951 PHE MET GLY ILE TYR THR GLY ILE LEU THR PHE LEU ASP SEQRES 47 C 951 ALA VAL SER TRP GLY ARG PHE ALA GLU PHE GLY ILE TRP SEQRES 48 C 951 TRP GLU THR GLY SER GLY CYS LYS VAL ALA GLY PHE LEU SEQRES 49 C 951 ALA VAL PHE SER SER GLU SER ALA ILE PHE LEU LEU MET SEQRES 50 C 951 LEU ALA THR VAL GLU ARG SER LEU SER ALA LYS ASP ILE SEQRES 51 C 951 MET LYS ASN GLY LYS SER ASN HIS LEU LYS GLN PHE ARG SEQRES 52 C 951 VAL ALA ALA LEU LEU ALA PHE LEU GLY ALA THR VAL ALA SEQRES 53 C 951 GLY CYS PHE PRO LEU PHE HIS ARG GLY GLU TYR SER ALA SEQRES 54 C 951 SER PRO LEU CYS LEU PRO PHE PRO THR GLY GLU THR PRO SEQRES 55 C 951 SER LEU GLY PHE THR VAL THR LEU VAL LEU LEU ASN SER SEQRES 56 C 951 LEU ALA PHE LEU LEU MET ALA VAL ILE TYR THR LYS LEU SEQRES 57 C 951 TYR CYS ASN LEU GLU LYS GLU ASP LEU SER GLU ASN SER SEQRES 58 C 951 GLN SER SER MET ILE LYS HIS VAL ALA TRP LEU ILE PHE SEQRES 59 C 951 THR ASN CYS ILE PHE PHE CYS PRO VAL ALA PHE PHE SER SEQRES 60 C 951 PHE ALA PRO LEU ILE THR ALA ILE SER ILE SER PRO GLU SEQRES 61 C 951 ILE MET LYS SER VAL THR LEU ILE PHE PHE PRO LEU PRO SEQRES 62 C 951 ALA CYS LEU ASN PRO VAL LEU TYR VAL PHE PHE ASN PRO SEQRES 63 C 951 LYS PHE LYS GLU ASP TRP LYS LEU LEU LYS ARG ARG VAL SEQRES 64 C 951 THR LYS LYS SER GLY SER VAL SER VAL SER ILE SER SER SEQRES 65 C 951 GLN GLY GLY CYS LEU GLU GLN ASP PHE TYR TYR ASP CYS SEQRES 66 C 951 GLY MET TYR SER HIS LEU GLN GLY ASN LEU THR VAL CYS SEQRES 67 C 951 ASP CYS CYS GLU SER PHE LEU LEU THR LYS PRO VAL SER SEQRES 68 C 951 CYS LYS HIS LEU ILE LYS SER HIS SER CYS PRO ALA LEU SEQRES 69 C 951 ALA VAL ALA SER CYS GLN ARG PRO GLU GLY TYR TRP SER SEQRES 70 C 951 ASP CYS GLY THR GLN SER ALA HIS SER ASP TYR ALA ASP SEQRES 71 C 951 GLU GLU ASP SER PHE VAL SER ASP SER SER ASP GLN VAL SEQRES 72 C 951 GLN ALA CYS GLY ARG ALA CYS PHE TYR GLN SER ARG GLY SEQRES 73 C 951 PHE PRO LEU VAL ARG TYR ALA TYR ASN LEU PRO ARG VAL SEQRES 74 C 951 LYS ASP SEQRES 1 A 110 GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY TYR THR SEQRES 2 A 110 TYR SER PRO TYR CYS MET GLY TRP PHE ARG GLN ALA PRO SEQRES 3 A 110 GLY LYS ALA ARG GLU GLY VAL ALA THR VAL ASP LEU ASP SEQRES 4 A 110 GLY SER THR ILE TYR ALA ASP SER VAL LYS GLY ARG PHE SEQRES 5 A 110 THR ILE SER GLN ASP ASN ALA LYS ASN THR LEU TYR LEU SEQRES 6 A 110 GLN MET ASN SER LEU LYS PRO GLU ASP THR ALA MET TYR SEQRES 7 A 110 TYR CYS ALA SER ARG THR ARG ALA GLY VAL THR CYS GLY SEQRES 8 A 110 LEU ASN TRP ALA ILE PHE SER TYR TRP GLY GLN GLY THR SEQRES 9 A 110 GLN VAL THR VAL SER SER HELIX 1 AA1 PRO C 121 GLY C 127 1 7 HELIX 2 AA2 PRO C 169 LEU C 176 1 8 HELIX 3 AA3 ALA C 243 LEU C 247 5 5 HELIX 4 AA4 ASN C 289 PHE C 292 5 4 HELIX 5 AA5 ASN C 337 GLN C 342 1 6 HELIX 6 AA6 TYR C 466 CYS C 471 1 6 HELIX 7 AA7 SER C 538 SER C 566 1 29 HELIX 8 AA8 PRO C 571 SER C 601 1 31 HELIX 9 AA9 ARG C 604 THR C 614 1 11 HELIX 10 AB1 GLY C 615 ASP C 649 1 35 HELIX 11 AB2 ASN C 657 PHE C 679 1 23 HELIX 12 AB3 PRO C 680 PHE C 682 5 3 HELIX 13 AB4 SER C 703 LEU C 732 1 30 HELIX 14 AB5 MET C 745 ALA C 769 1 25 HELIX 15 AB6 PRO C 770 ILE C 772 5 3 HELIX 16 AB7 SER C 778 PHE C 790 1 13 HELIX 17 AB8 PRO C 791 PHE C 804 1 14 HELIX 18 AB9 ASN C 805 LYS C 821 1 17 HELIX 19 AC1 LEU A 459 GLY A 461 5 3 HELIX 20 AC2 ASP A 467 LYS A 470 5 4 HELIX 21 AC3 LYS A 492 THR A 496 5 5 HELIX 22 AC4 ASN A 514 PHE A 518 5 5 SHEET 1 AA112 CYS C 35 ASP C 36 0 SHEET 2 AA112 ARG C 40 SER C 44 -1 O ARG C 40 N ASP C 36 SHEET 3 AA112 ALA C 61 SER C 65 1 O ASP C 63 N CYS C 43 SHEET 4 AA112 GLU C 85 GLN C 87 1 O GLN C 87 N ILE C 64 SHEET 5 AA112 VAL C 109 THR C 111 1 O VAL C 109 N LEU C 86 SHEET 6 AA112 SER C 133 ARG C 135 1 O SER C 133 N LEU C 110 SHEET 7 AA112 HIS C 157 TRP C 159 1 O HIS C 157 N LEU C 134 SHEET 8 AA112 ALA C 181 THR C 183 1 O THR C 183 N LEU C 158 SHEET 9 AA112 VAL C 205 HIS C 207 1 O VAL C 205 N LEU C 182 SHEET 10 AA112 THR C 229 ASP C 231 1 O THR C 229 N LEU C 206 SHEET 11 AA112 GLU C 252 GLY C 254 1 O GLU C 252 N LEU C 230 SHEET 12 AA112 THR C 276 HIS C 278 1 O THR C 276 N LEU C 253 SHEET 1 AA2 2 GLN C 71 LEU C 72 0 SHEET 2 AA2 2 PHE C 95 ILE C 96 1 O PHE C 95 N LEU C 72 SHEET 1 AA3 2 SER C 191 ILE C 192 0 SHEET 2 AA3 2 SER C 215 LEU C 216 1 O SER C 215 N ILE C 192 SHEET 1 AA4 2 VAL C 262 ILE C 263 0 SHEET 2 AA4 2 PHE C 286 VAL C 287 1 O PHE C 286 N ILE C 263 SHEET 1 AA5 9 SER C 300 ARG C 304 0 SHEET 2 AA5 9 SER C 323 THR C 327 1 O THR C 327 N ILE C 303 SHEET 3 AA5 9 THR C 347 ASP C 349 1 O ASP C 349 N LEU C 326 SHEET 4 AA5 9 GLU C 369 SER C 371 1 O SER C 371 N LEU C 348 SHEET 5 AA5 9 ILE C 393 ASP C 395 1 O ILE C 393 N ILE C 370 SHEET 6 AA5 9 ASN C 417 ASP C 419 1 O ASN C 417 N LEU C 394 SHEET 7 AA5 9 GLN C 438 LYS C 440 1 O LYS C 440 N LEU C 418 SHEET 8 AA5 9 SER C 461 SER C 463 1 O SER C 461 N LEU C 439 SHEET 9 AA5 9 HIS C 521 CYS C 522 1 O HIS C 521 N LEU C 462 SHEET 1 AA6 3 ARG A 425 ALA A 429 0 SHEET 2 AA6 3 THR A 483 MET A 488 -1 O LEU A 484 N CYS A 428 SHEET 3 AA6 3 PHE A 473 GLN A 477 -1 N SER A 476 O TYR A 485 SHEET 1 AA7 5 THR A 463 TYR A 465 0 SHEET 2 AA7 5 GLU A 452 VAL A 457 -1 N THR A 456 O ILE A 464 SHEET 3 AA7 5 MET A 440 GLN A 445 -1 N MET A 440 O VAL A 457 SHEET 4 AA7 5 ALA A 497 SER A 503 -1 O TYR A 500 N PHE A 443 SHEET 5 AA7 5 TYR A 520 TRP A 521 -1 O TYR A 520 N SER A 503 SHEET 1 AA8 5 THR A 463 TYR A 465 0 SHEET 2 AA8 5 GLU A 452 VAL A 457 -1 N THR A 456 O ILE A 464 SHEET 3 AA8 5 MET A 440 GLN A 445 -1 N MET A 440 O VAL A 457 SHEET 4 AA8 5 ALA A 497 SER A 503 -1 O TYR A 500 N PHE A 443 SHEET 5 AA8 5 THR A 525 VAL A 527 -1 O VAL A 527 N ALA A 497 SSBOND 1 CYS C 29 CYS C 35 1555 1555 2.02 SSBOND 2 CYS C 33 CYS C 43 1555 1555 2.03 SSBOND 3 CYS C 339 CYS C 364 1555 1555 2.03 SSBOND 4 CYS C 618 CYS C 693 1555 1555 2.03 SSBOND 5 CYS C 757 CYS C 761 1555 1555 2.57 SSBOND 6 CYS A 428 CYS A 501 1555 1555 2.03 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