HEADER MEMBRANE PROTEIN 14-MAY-24 8ZJG TITLE CRYO-EM STRUCTURE OF HUMAN CMKLR1-GI COMPLEX BOUND TO CHEMERIN COMPND MOL_ID: 1; COMPND 2 MOLECULE: CHEMERIN-LIKE RECEPTOR 1; COMPND 3 CHAIN: A; COMPND 4 SYNONYM: CHEMOKINE-LIKE RECEPTOR 1,G-PROTEIN COUPLED RECEPTOR COMPND 5 CHEMR23,G-PROTEIN COUPLED RECEPTOR DEZ; COMPND 6 ENGINEERED: YES; COMPND 7 MUTATION: YES; COMPND 8 MOL_ID: 2; COMPND 9 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 10 BETA-1; COMPND 11 CHAIN: B; COMPND 12 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 13 ENGINEERED: YES; COMPND 14 MOL_ID: 3; COMPND 15 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I) SUBUNIT ALPHA-1; COMPND 16 CHAIN: C; COMPND 17 SYNONYM: ADENYLATE CYCLASE-INHIBITING G ALPHA PROTEIN; COMPND 18 ENGINEERED: YES; COMPND 19 MUTATION: YES; COMPND 20 MOL_ID: 4; COMPND 21 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 22 GAMMA-2; COMPND 23 CHAIN: G; COMPND 24 SYNONYM: G GAMMA-I; COMPND 25 ENGINEERED: YES; COMPND 26 MOL_ID: 5; COMPND 27 MOLECULE: SCFV16; COMPND 28 CHAIN: S; COMPND 29 ENGINEERED: YES; COMPND 30 MOL_ID: 6; COMPND 31 MOLECULE: RETINOIC ACID RECEPTOR RESPONDER PROTEIN 2 CHEMERINV; COMPND 32 CHAIN: L; COMPND 33 SYNONYM: CHEMERIN; COMPND 34 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: CMKLR1, CHEMR23, DEZ; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 10 ORGANISM_COMMON: HUMAN; SOURCE 11 ORGANISM_TAXID: 9606; SOURCE 12 GENE: GNB1; SOURCE 13 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 14 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 15 MOL_ID: 3; SOURCE 16 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 17 ORGANISM_COMMON: HUMAN; SOURCE 18 ORGANISM_TAXID: 9606; SOURCE 19 GENE: GNAI1; SOURCE 20 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 21 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 22 MOL_ID: 4; SOURCE 23 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 24 ORGANISM_COMMON: HUMAN; SOURCE 25 ORGANISM_TAXID: 9606; SOURCE 26 GENE: GNG2; SOURCE 27 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 28 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 29 MOL_ID: 5; SOURCE 30 ORGANISM_SCIENTIFIC: VICUGNA PACOS; SOURCE 31 ORGANISM_TAXID: 30538; SOURCE 32 EXPRESSION_SYSTEM: ESCHERICHIA COLI; SOURCE 33 EXPRESSION_SYSTEM_TAXID: 562; SOURCE 34 MOL_ID: 6; SOURCE 35 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 36 ORGANISM_COMMON: HUMAN; SOURCE 37 ORGANISM_TAXID: 9606; SOURCE 38 GENE: RARRES2; SOURCE 39 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 40 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS CHEMERIN RECEPTOR, MEMBRANE PROTEIN EXPDTA ELECTRON MICROSCOPY AUTHOR A.J.LIU,Y.Z.LIU,R.D.YE REVDAT 2 29-JAN-25 8ZJG 1 COMPND REVDAT 1 22-JAN-25 8ZJG 0 JRNL AUTH A.LIU,Y.LIU,J.WANG,R.D.YE JRNL TITL STRUCTURAL BASIS FOR FULL-LENGTH CHEMERIN RECOGNITION AND JRNL TITL 2 SIGNALING THROUGH CHEMERIN RECEPTOR 1. JRNL REF COMMUN BIOL V. 7 1598 2024 JRNL REFN ESSN 2399-3642 JRNL PMID 39616240 JRNL DOI 10.1038/S42003-024-07228-9 REMARK 2 REMARK 2 RESOLUTION. 3.18 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) : 3.180 REMARK 3 NUMBER OF PARTICLES : 268231 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 8ZJG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-24. REMARK 100 THE DEPOSITION ID IS D_1300047906. 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 : HUMAN CHEMERIN RECEPTOR 1-GI REMARK 245 COMPLEX BOUND TO CHEMERIN 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 : TFS KRIOS REMARK 245 DETECTOR TYPE : GATAN K3 BIOQUANTUM (6K X REMARK 245 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 1200.00 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) : 5200.00 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: HEXAMERIC REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: HEXAMERIC REMARK 350 SOFTWARE USED: PISA REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, G, S, L 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 ARG A 2 REMARK 465 MET A 3 REMARK 465 GLU A 4 REMARK 465 ASP A 5 REMARK 465 GLU A 6 REMARK 465 ASP A 7 REMARK 465 TYR A 8 REMARK 465 ASN A 9 REMARK 465 THR A 10 REMARK 465 SER A 11 REMARK 465 ILE A 12 REMARK 465 SER A 13 REMARK 465 TYR A 14 REMARK 465 GLY A 15 REMARK 465 ASP A 16 REMARK 465 GLU A 17 REMARK 465 TYR A 18 REMARK 465 PRO A 19 REMARK 465 GLU A 340 REMARK 465 ASP A 341 REMARK 465 THR A 342 REMARK 465 GLY A 343 REMARK 465 HIS A 344 REMARK 465 SER A 345 REMARK 465 SER A 346 REMARK 465 TYR A 347 REMARK 465 PRO A 348 REMARK 465 SER A 349 REMARK 465 HIS A 350 REMARK 465 ARG A 351 REMARK 465 SER A 352 REMARK 465 PHE A 353 REMARK 465 THR A 354 REMARK 465 LYS A 355 REMARK 465 MET A 356 REMARK 465 SER A 357 REMARK 465 SER A 358 REMARK 465 MET A 359 REMARK 465 ASN A 360 REMARK 465 GLU A 361 REMARK 465 ARG A 362 REMARK 465 THR A 363 REMARK 465 SER A 364 REMARK 465 MET A 365 REMARK 465 ASN A 366 REMARK 465 GLU A 367 REMARK 465 ARG A 368 REMARK 465 GLU A 369 REMARK 465 THR A 370 REMARK 465 GLY A 371 REMARK 465 MET A 372 REMARK 465 LEU A 373 REMARK 465 MET B 1 REMARK 465 SER B 2 REMARK 465 GLU B 3 REMARK 465 LYS C 54 REMARK 465 ILE C 55 REMARK 465 ILE C 56 REMARK 465 HIS C 57 REMARK 465 GLU C 58 REMARK 465 ALA C 59 REMARK 465 GLY C 60 REMARK 465 TYR C 61 REMARK 465 SER C 62 REMARK 465 GLU C 63 REMARK 465 GLU C 64 REMARK 465 GLU C 65 REMARK 465 CYS C 66 REMARK 465 LYS C 67 REMARK 465 GLN C 68 REMARK 465 TYR C 69 REMARK 465 LYS C 70 REMARK 465 ALA C 71 REMARK 465 VAL C 72 REMARK 465 VAL C 73 REMARK 465 TYR C 74 REMARK 465 SER C 75 REMARK 465 ASN C 76 REMARK 465 THR C 77 REMARK 465 ILE C 78 REMARK 465 GLN C 79 REMARK 465 SER C 80 REMARK 465 ILE C 81 REMARK 465 ILE C 82 REMARK 465 ALA C 83 REMARK 465 ILE C 84 REMARK 465 ILE C 85 REMARK 465 ARG C 86 REMARK 465 ALA C 87 REMARK 465 MET C 88 REMARK 465 GLY C 89 REMARK 465 ARG C 90 REMARK 465 LEU C 91 REMARK 465 LYS C 92 REMARK 465 ILE C 93 REMARK 465 ASP C 94 REMARK 465 PHE C 95 REMARK 465 GLY C 96 REMARK 465 ASP C 97 REMARK 465 SER C 98 REMARK 465 ALA C 99 REMARK 465 ARG C 100 REMARK 465 ALA C 101 REMARK 465 ASP C 102 REMARK 465 ASP C 103 REMARK 465 ALA C 104 REMARK 465 ARG C 105 REMARK 465 GLN C 106 REMARK 465 LEU C 107 REMARK 465 PHE C 108 REMARK 465 VAL C 109 REMARK 465 LEU C 110 REMARK 465 ALA C 111 REMARK 465 GLY C 112 REMARK 465 ALA C 113 REMARK 465 ALA C 114 REMARK 465 GLU C 115 REMARK 465 GLU C 116 REMARK 465 GLY C 117 REMARK 465 PHE C 118 REMARK 465 MET C 119 REMARK 465 THR C 120 REMARK 465 ALA C 121 REMARK 465 GLU C 122 REMARK 465 LEU C 123 REMARK 465 ALA C 124 REMARK 465 GLY C 125 REMARK 465 VAL C 126 REMARK 465 ILE C 127 REMARK 465 LYS C 128 REMARK 465 ARG C 129 REMARK 465 LEU C 130 REMARK 465 TRP C 131 REMARK 465 LYS C 132 REMARK 465 ASP C 133 REMARK 465 SER C 134 REMARK 465 GLY C 135 REMARK 465 VAL C 136 REMARK 465 GLN C 137 REMARK 465 ALA C 138 REMARK 465 CYS C 139 REMARK 465 PHE C 140 REMARK 465 ASN C 141 REMARK 465 ARG C 142 REMARK 465 SER C 143 REMARK 465 ARG C 144 REMARK 465 GLU C 145 REMARK 465 TYR C 146 REMARK 465 GLN C 147 REMARK 465 LEU C 148 REMARK 465 ASN C 149 REMARK 465 ASP C 150 REMARK 465 SER C 151 REMARK 465 ALA C 152 REMARK 465 ALA C 153 REMARK 465 TYR C 154 REMARK 465 TYR C 155 REMARK 465 LEU C 156 REMARK 465 ASN C 157 REMARK 465 ASP C 158 REMARK 465 LEU C 159 REMARK 465 ASP C 160 REMARK 465 ARG C 161 REMARK 465 ILE C 162 REMARK 465 ALA C 163 REMARK 465 GLN C 164 REMARK 465 PRO C 165 REMARK 465 ASN C 166 REMARK 465 TYR C 167 REMARK 465 ILE C 168 REMARK 465 PRO C 169 REMARK 465 THR C 170 REMARK 465 GLN C 171 REMARK 465 GLN C 172 REMARK 465 ASP C 173 REMARK 465 VAL C 174 REMARK 465 LEU C 175 REMARK 465 ARG C 176 REMARK 465 THR C 177 REMARK 465 ARG C 178 REMARK 465 VAL C 179 REMARK 465 LYS C 180 REMARK 465 THR C 181 REMARK 465 MET G 1 REMARK 465 ALA G 2 REMARK 465 SER G 3 REMARK 465 ASN G 4 REMARK 465 ASN G 5 REMARK 465 THR G 6 REMARK 465 ALA G 7 REMARK 465 LYS G 64 REMARK 465 LYS G 65 REMARK 465 PHE G 66 REMARK 465 PHE G 67 REMARK 465 CYS G 68 REMARK 465 ALA G 69 REMARK 465 ILE G 70 REMARK 465 LEU G 71 REMARK 465 GLY S 122 REMARK 465 GLY S 123 REMARK 465 GLY S 124 REMARK 465 GLY S 125 REMARK 465 SER S 126 REMARK 465 GLY S 127 REMARK 465 GLY S 128 REMARK 465 GLY S 129 REMARK 465 GLY S 130 REMARK 465 SER S 131 REMARK 465 GLY S 132 REMARK 465 GLY S 133 REMARK 465 GLY S 134 REMARK 465 GLY S 135 REMARK 465 PRO L 21 REMARK 465 PRO L 22 REMARK 465 VAL L 23 REMARK 465 GLN L 24 REMARK 465 TRP L 25 REMARK 465 ALA L 26 REMARK 465 PHE L 27 REMARK 465 GLN L 28 REMARK 465 GLU L 29 REMARK 465 THR L 30 REMARK 465 SER L 31 REMARK 465 VAL L 32 REMARK 465 GLU L 33 REMARK 465 GLU L 66 REMARK 465 CYS L 67 REMARK 465 LYS L 68 REMARK 465 VAL L 69 REMARK 465 ARG L 70 REMARK 465 PRO L 71 REMARK 465 ASN L 72 REMARK 465 GLY L 73 REMARK 465 ARG L 74 REMARK 465 LYS L 75 REMARK 465 GLU L 100 REMARK 465 THR L 101 REMARK 465 GLN L 102 REMARK 465 VAL L 103 REMARK 465 LEU L 104 REMARK 465 ARG L 105 REMARK 465 GLU L 106 REMARK 465 ALA L 107 REMARK 465 GLU L 108 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 OG1 THR B 128 O ASN B 132 2.18 REMARK 500 NH2 ARG A 40 O ALA A 100 2.19 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 ASP A 23 -137.68 -93.14 REMARK 500 LEU A 28 -9.52 78.40 REMARK 500 GLU A 35 -147.93 42.99 REMARK 500 ALA A 36 -108.66 51.37 REMARK 500 MET A 101 51.75 -95.77 REMARK 500 SER A 174 -177.54 -69.52 REMARK 500 LEU A 175 -64.52 68.98 REMARK 500 ASN A 182 41.82 -97.04 REMARK 500 SER A 200 33.07 70.02 REMARK 500 THR A 205 -4.72 76.38 REMARK 500 LYS A 254 -4.96 64.48 REMARK 500 ILE A 306 4.93 -63.33 REMARK 500 CYS A 310 -4.97 -143.37 REMARK 500 ASN B 35 48.84 -82.73 REMARK 500 THR B 87 11.14 59.14 REMARK 500 CYS B 204 49.16 -86.11 REMARK 500 ASP B 205 23.99 -141.32 REMARK 500 SER B 227 -169.25 -160.73 REMARK 500 GLU C 43 57.70 -91.35 REMARK 500 MET C 240 116.90 -162.44 REMARK 500 LEU C 266 123.63 -38.27 REMARK 500 PRO C 288 44.28 -82.25 REMARK 500 HIS G 44 52.61 -94.09 REMARK 500 PRO G 49 42.62 -84.75 REMARK 500 VAL S 48 -54.03 -120.30 REMARK 500 ASN S 77 58.18 36.72 REMARK 500 ALA S 92 -168.95 -166.57 REMARK 500 MET S 192 -9.91 72.87 REMARK 500 THR S 210 -5.50 76.34 REMARK 500 ASP S 223 7.40 -69.19 REMARK 500 ARG L 7 -8.09 72.53 REMARK 500 GLN L 53 -0.25 72.08 REMARK 500 GLU L 87 -125.28 58.55 REMARK 500 HIS L 126 -7.96 77.78 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-60144 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF HUMAN CMKLR1-GI COMPLEX BOUND TO CHEMERIN DBREF 8ZJG A 1 373 UNP Q99788 CML1_HUMAN 1 373 DBREF 8ZJG B 1 340 UNP P62873 GBB1_HUMAN 1 340 DBREF 8ZJG C 4 354 UNP P63096 GNAI1_HUMAN 4 354 DBREF 8ZJG G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8ZJG S 1 247 PDB 8ZJG 8ZJG 1 247 DBREF 8ZJG L 1 137 UNP Q99969 RARR2_HUMAN 21 157 SEQADV 8ZJG ALA C 203 UNP P63096 GLY 203 ENGINEERED MUTATION SEQADV 8ZJG SER C 326 UNP P63096 ALA 326 ENGINEERED MUTATION SEQRES 1 A 373 MET ARG MET GLU ASP GLU ASP TYR ASN THR SER ILE SER SEQRES 2 A 373 TYR GLY ASP GLU TYR PRO ASP TYR LEU ASP SER ILE VAL SEQRES 3 A 373 VAL LEU GLU ASP LEU SER PRO LEU GLU ALA ARG VAL THR SEQRES 4 A 373 ARG ILE PHE LEU VAL VAL VAL TYR SER ILE VAL CYS PHE SEQRES 5 A 373 LEU GLY ILE LEU GLY ASN GLY LEU VAL ILE ILE ILE ALA SEQRES 6 A 373 THR PHE LYS MET LYS LYS THR VAL ASN MET VAL TRP PHE SEQRES 7 A 373 LEU ASN LEU ALA VAL ALA ASP PHE LEU PHE ASN VAL PHE SEQRES 8 A 373 LEU PRO ILE HIS ILE THR TYR ALA ALA MET ASP TYR HIS SEQRES 9 A 373 TRP VAL PHE GLY THR ALA MET CYS LYS ILE SER ASN PHE SEQRES 10 A 373 LEU LEU ILE HIS ASN MET PHE THR SER VAL PHE LEU LEU SEQRES 11 A 373 THR ILE ILE SER SER ASP ARG CYS ILE SER VAL LEU LEU SEQRES 12 A 373 PRO VAL TRP SER GLN ASN HIS ARG SER VAL ARG LEU ALA SEQRES 13 A 373 TYR MET ALA CYS MET VAL ILE TRP VAL LEU ALA PHE PHE SEQRES 14 A 373 LEU SER SER PRO SER LEU VAL PHE ARG ASP THR ALA ASN SEQRES 15 A 373 LEU HIS GLY LYS ILE SER CYS PHE ASN ASN PHE SER LEU SEQRES 16 A 373 SER THR PRO GLY SER SER SER TRP PRO THR HIS SER GLN SEQRES 17 A 373 MET ASP PRO VAL GLY TYR SER ARG HIS MET VAL VAL THR SEQRES 18 A 373 VAL THR ARG PHE LEU CYS GLY PHE LEU VAL PRO VAL LEU SEQRES 19 A 373 ILE ILE THR ALA CYS TYR LEU THR ILE VAL CYS LYS LEU SEQRES 20 A 373 GLN ARG ASN ARG LEU ALA LYS THR LYS LYS PRO PHE LYS SEQRES 21 A 373 ILE ILE VAL THR ILE ILE ILE THR PHE PHE LEU CYS TRP SEQRES 22 A 373 CYS PRO TYR HIS THR LEU ASN LEU LEU GLU LEU HIS HIS SEQRES 23 A 373 THR ALA MET PRO GLY SER VAL PHE SER LEU GLY LEU PRO SEQRES 24 A 373 LEU ALA THR ALA LEU ALA ILE ALA ASN SER CYS MET ASN SEQRES 25 A 373 PRO ILE LEU TYR VAL PHE MET GLY GLN ASP PHE LYS LYS SEQRES 26 A 373 PHE LYS VAL ALA LEU PHE SER ARG LEU VAL ASN ALA LEU SEQRES 27 A 373 SER GLU ASP THR GLY HIS SER SER TYR PRO SER HIS ARG SEQRES 28 A 373 SER PHE THR LYS MET SER SER MET ASN GLU ARG THR SER SEQRES 29 A 373 MET ASN GLU ARG GLU THR GLY MET LEU SEQRES 1 B 340 MET SER GLU LEU ASP GLN LEU ARG GLN GLU ALA GLU GLN SEQRES 2 B 340 LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS ALA CYS ALA SEQRES 3 B 340 ASP ALA THR LEU SER GLN ILE THR ASN ASN ILE ASP PRO SEQRES 4 B 340 VAL GLY ARG ILE GLN MET ARG THR ARG ARG THR LEU ARG SEQRES 5 B 340 GLY HIS LEU ALA LYS ILE TYR ALA MET HIS TRP GLY THR SEQRES 6 B 340 ASP SER ARG LEU LEU VAL SER ALA SER GLN ASP GLY LYS SEQRES 7 B 340 LEU ILE ILE TRP ASP SER TYR THR THR ASN LYS VAL HIS SEQRES 8 B 340 ALA ILE PRO LEU ARG SER SER TRP VAL MET THR CYS ALA SEQRES 9 B 340 TYR ALA PRO SER GLY ASN TYR VAL ALA CYS GLY GLY LEU SEQRES 10 B 340 ASP ASN ILE CYS SER ILE TYR ASN LEU LYS THR ARG GLU SEQRES 11 B 340 GLY ASN VAL ARG VAL SER ARG GLU LEU ALA GLY HIS THR SEQRES 12 B 340 GLY TYR LEU SER CYS CYS ARG PHE LEU ASP ASP ASN GLN SEQRES 13 B 340 ILE VAL THR SER SER GLY ASP THR THR CYS ALA LEU TRP SEQRES 14 B 340 ASP ILE GLU THR GLY GLN GLN THR THR THR PHE THR GLY SEQRES 15 B 340 HIS THR GLY ASP VAL MET SER LEU SER LEU ALA PRO ASP SEQRES 16 B 340 THR ARG LEU PHE VAL SER GLY ALA CYS ASP ALA SER ALA SEQRES 17 B 340 LYS LEU TRP ASP VAL ARG GLU GLY MET CYS ARG GLN THR SEQRES 18 B 340 PHE THR GLY HIS GLU SER ASP ILE ASN ALA ILE CYS PHE SEQRES 19 B 340 PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SER ASP ASP SEQRES 20 B 340 ALA THR CYS ARG LEU PHE ASP LEU ARG ALA ASP GLN GLU SEQRES 21 B 340 LEU MET THR TYR SER HIS ASP ASN ILE ILE CYS GLY ILE SEQRES 22 B 340 THR SER VAL SER PHE SER LYS SER GLY ARG LEU LEU LEU SEQRES 23 B 340 ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL TRP ASP ALA SEQRES 24 B 340 LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA GLY HIS ASP SEQRES 25 B 340 ASN ARG VAL SER CYS LEU GLY VAL THR ASP ASP GLY MET SEQRES 26 B 340 ALA VAL ALA THR GLY SER TRP ASP SER PHE LEU LYS ILE SEQRES 27 B 340 TRP ASN SEQRES 1 C 351 THR LEU SER ALA GLU ASP LYS ALA ALA VAL GLU ARG SER SEQRES 2 C 351 LYS MET ILE ASP ARG ASN LEU ARG GLU ASP GLY GLU LYS SEQRES 3 C 351 ALA ALA ARG GLU VAL LYS LEU LEU LEU LEU GLY ALA GLY SEQRES 4 C 351 GLU SER GLY LYS SER THR ILE VAL LYS GLN MET LYS ILE SEQRES 5 C 351 ILE HIS GLU ALA GLY TYR SER GLU GLU GLU CYS LYS GLN SEQRES 6 C 351 TYR LYS ALA VAL VAL TYR SER ASN THR ILE GLN SER ILE SEQRES 7 C 351 ILE ALA ILE ILE ARG ALA MET GLY ARG LEU LYS ILE ASP SEQRES 8 C 351 PHE GLY ASP SER ALA ARG ALA ASP ASP ALA ARG GLN LEU SEQRES 9 C 351 PHE VAL LEU ALA GLY ALA ALA GLU GLU GLY PHE MET THR SEQRES 10 C 351 ALA GLU LEU ALA GLY VAL ILE LYS ARG LEU TRP LYS ASP SEQRES 11 C 351 SER GLY VAL GLN ALA CYS PHE ASN ARG SER ARG GLU TYR SEQRES 12 C 351 GLN LEU ASN ASP SER ALA ALA TYR TYR LEU ASN ASP LEU SEQRES 13 C 351 ASP ARG ILE ALA GLN PRO ASN TYR ILE PRO THR GLN GLN SEQRES 14 C 351 ASP VAL LEU ARG THR ARG VAL LYS THR THR GLY ILE VAL SEQRES 15 C 351 GLU THR HIS PHE THR PHE LYS ASP LEU HIS PHE LYS MET SEQRES 16 C 351 PHE ASP VAL GLY ALA GLN ARG SER GLU ARG LYS LYS TRP SEQRES 17 C 351 ILE HIS CYS PHE GLU GLY VAL THR ALA ILE ILE PHE CYS SEQRES 18 C 351 VAL ALA LEU SER ASP TYR ASP LEU VAL LEU ALA GLU ASP SEQRES 19 C 351 GLU GLU MET ASN ARG MET HIS GLU SER MET LYS LEU PHE SEQRES 20 C 351 ASP SER ILE CYS ASN ASN LYS TRP PHE THR ASP THR SER SEQRES 21 C 351 ILE ILE LEU PHE LEU ASN LYS LYS ASP LEU PHE GLU GLU SEQRES 22 C 351 LYS ILE LYS LYS SER PRO LEU THR ILE CYS TYR PRO GLU SEQRES 23 C 351 TYR ALA GLY SER ASN THR TYR GLU GLU ALA ALA ALA TYR SEQRES 24 C 351 ILE GLN CYS GLN PHE GLU ASP LEU ASN LYS ARG LYS ASP SEQRES 25 C 351 THR LYS GLU ILE TYR THR HIS PHE THR CYS SER THR ASP SEQRES 26 C 351 THR LYS ASN VAL GLN PHE VAL PHE ASP ALA VAL THR ASP SEQRES 27 C 351 VAL ILE ILE LYS ASN ASN LEU LYS ASP CYS GLY LEU PHE SEQRES 1 G 71 MET ALA SER ASN ASN THR ALA SER ILE ALA GLN ALA ARG SEQRES 2 G 71 LYS LEU VAL GLU GLN LEU LYS MET GLU ALA ASN ILE ASP SEQRES 3 G 71 ARG ILE LYS VAL SER LYS ALA ALA ALA ASP LEU MET ALA SEQRES 4 G 71 TYR CYS GLU ALA HIS ALA LYS GLU ASP PRO LEU LEU THR SEQRES 5 G 71 PRO VAL PRO ALA SER GLU ASN PRO PHE ARG GLU LYS LYS SEQRES 6 G 71 PHE PHE CYS ALA ILE LEU SEQRES 1 S 247 ASP VAL GLN LEU VAL GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 S 247 PRO GLY GLY SER ARG LYS LEU SER CYS SER ALA SER GLY SEQRES 3 S 247 PHE ALA PHE SER SER PHE GLY MET HIS TRP VAL ARG GLN SEQRES 4 S 247 ALA PRO GLU LYS GLY LEU GLU TRP VAL ALA TYR ILE SER SEQRES 5 S 247 SER GLY SER GLY THR ILE TYR TYR ALA ASP THR VAL LYS SEQRES 6 S 247 GLY ARG PHE THR ILE SER ARG ASP ASP PRO LYS ASN THR SEQRES 7 S 247 LEU PHE LEU GLN MET THR SER LEU ARG SER GLU ASP THR SEQRES 8 S 247 ALA MET TYR TYR CYS VAL ARG SER ILE TYR TYR TYR GLY SEQRES 9 S 247 SER SER PRO PHE ASP PHE TRP GLY GLN GLY THR THR LEU SEQRES 10 S 247 THR VAL SER SER GLY GLY GLY GLY SER GLY GLY GLY GLY SEQRES 11 S 247 SER GLY GLY GLY GLY SER ASP ILE VAL MET THR GLN ALA SEQRES 12 S 247 THR SER SER VAL PRO VAL THR PRO GLY GLU SER VAL SER SEQRES 13 S 247 ILE SER CYS ARG SER SER LYS SER LEU LEU HIS SER ASN SEQRES 14 S 247 GLY ASN THR TYR LEU TYR TRP PHE LEU GLN ARG PRO GLY SEQRES 15 S 247 GLN SER PRO GLN LEU LEU ILE TYR ARG MET SER ASN LEU SEQRES 16 S 247 ALA SER GLY VAL PRO ASP ARG PHE SER GLY SER GLY SER SEQRES 17 S 247 GLY THR ALA PHE THR LEU THR ILE SER ARG LEU GLU ALA SEQRES 18 S 247 GLU ASP VAL GLY VAL TYR TYR CYS MET GLN HIS LEU GLU SEQRES 19 S 247 TYR PRO LEU THR PHE GLY ALA GLY THR LYS LEU GLU LEU SEQRES 1 L 137 GLU LEU THR GLU ALA GLN ARG ARG GLY LEU GLN VAL ALA SEQRES 2 L 137 LEU GLU GLU PHE HIS LYS HIS PRO PRO VAL GLN TRP ALA SEQRES 3 L 137 PHE GLN GLU THR SER VAL GLU SER ALA VAL ASP THR PRO SEQRES 4 L 137 PHE PRO ALA GLY ILE PHE VAL ARG LEU GLU PHE LYS LEU SEQRES 5 L 137 GLN GLN THR SER CYS ARG LYS ARG ASP TRP LYS LYS PRO SEQRES 6 L 137 GLU CYS LYS VAL ARG PRO ASN GLY ARG LYS ARG LYS CYS SEQRES 7 L 137 LEU ALA CYS ILE LYS LEU GLY SER GLU ASP LYS VAL LEU SEQRES 8 L 137 GLY ARG LEU VAL HIS CYS PRO ILE GLU THR GLN VAL LEU SEQRES 9 L 137 ARG GLU ALA GLU GLU HIS GLN GLU THR GLN CYS LEU ARG SEQRES 10 L 137 VAL GLN ARG ALA GLY GLU ASP PRO HIS SER PHE TYR PHE SEQRES 11 L 137 PRO GLY GLN PHE ALA PHE SER HET CLR A 401 28 HET CLR A 402 28 HET CLR A 403 28 HET CLR A 404 28 HETNAM CLR CHOLESTEROL FORMUL 7 CLR 4(C27 H46 O) FORMUL 11 HOH *(H2 O) HELIX 1 AA1 GLU A 35 LYS A 68 1 34 HELIX 2 AA2 THR A 72 MET A 101 1 30 HELIX 3 AA3 GLY A 108 LEU A 143 1 36 HELIX 4 AA4 LEU A 143 HIS A 150 1 8 HELIX 5 AA5 SER A 152 SER A 172 1 21 HELIX 6 AA6 ASN A 182 LYS A 186 5 5 HELIX 7 AA7 VAL A 212 ASN A 250 1 39 HELIX 8 AA8 LYS A 256 GLU A 283 1 28 HELIX 9 AA9 LEU A 284 HIS A 286 5 3 HELIX 10 AB1 GLY A 291 ILE A 306 1 16 HELIX 11 AB2 MET A 311 PHE A 318 1 8 HELIX 12 AB3 GLY A 320 SER A 339 1 20 HELIX 13 AB4 ASP B 5 ALA B 26 1 22 HELIX 14 AB5 THR B 29 ASN B 35 1 7 HELIX 15 AB6 SER C 6 ALA C 30 1 25 HELIX 16 AB7 GLY C 45 MET C 53 1 9 HELIX 17 AB8 GLU C 207 HIS C 213 1 7 HELIX 18 AB9 ASN C 241 ASN C 255 1 15 HELIX 19 AC1 LYS C 270 SER C 281 1 12 HELIX 20 AC2 PRO C 282 CYS C 286 5 5 HELIX 21 AC3 THR C 295 ASP C 309 1 15 HELIX 22 AC4 LYS C 330 CYS C 351 1 22 HELIX 23 AC5 ILE G 9 ALA G 23 1 15 HELIX 24 AC6 LYS G 29 HIS G 44 1 16 HELIX 25 AC7 ALA S 28 PHE S 32 5 5 HELIX 26 AC8 SER S 53 GLY S 56 5 4 HELIX 27 AC9 GLU S 220 VAL S 224 5 5 HELIX 28 AD1 GLY L 9 HIS L 20 1 12 HELIX 29 AD2 HIS L 110 ARG L 117 1 8 HELIX 30 AD3 VAL L 118 ARG L 120 5 3 SHEET 1 AA1 2 ARG A 178 ALA A 181 0 SHEET 2 AA1 2 SER A 188 ASN A 191 -1 O PHE A 190 N ASP A 179 SHEET 1 AA2 4 ARG B 46 LEU B 51 0 SHEET 2 AA2 4 PHE B 335 ASN B 340 -1 O LEU B 336 N LEU B 51 SHEET 3 AA2 4 VAL B 327 SER B 331 -1 N THR B 329 O LYS B 337 SHEET 4 AA2 4 VAL B 315 VAL B 320 -1 N CYS B 317 O GLY B 330 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O ALA B 73 N TYR B 59 SHEET 3 AA3 4 LYS B 78 ASP B 83 -1 O ILE B 80 N SER B 72 SHEET 4 AA3 4 LYS B 89 PRO B 94 -1 O VAL B 90 N ILE B 81 SHEET 1 AA4 4 VAL B 100 TYR B 105 0 SHEET 2 AA4 4 TYR B 111 GLY B 116 -1 O GLY B 115 N MET B 101 SHEET 3 AA4 4 ILE B 120 ASN B 125 -1 O SER B 122 N CYS B 114 SHEET 4 AA4 4 ARG B 134 ALA B 140 -1 O LEU B 139 N CYS B 121 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O GLN B 156 N LEU B 152 SHEET 3 AA5 4 THR B 165 ASP B 170 -1 O ALA B 167 N THR B 159 SHEET 4 AA5 4 GLN B 175 THR B 181 -1 O THR B 178 N LEU B 168 SHEET 1 AA6 4 VAL B 187 LEU B 192 0 SHEET 2 AA6 4 LEU B 198 ALA B 203 -1 O GLY B 202 N MET B 188 SHEET 3 AA6 4 SER B 207 ASP B 212 -1 O TRP B 211 N PHE B 199 SHEET 4 AA6 4 CYS B 218 PHE B 222 -1 O GLN B 220 N LEU B 210 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O ALA B 242 N CYS B 233 SHEET 3 AA7 4 CYS B 250 ASP B 254 -1 O ARG B 251 N THR B 243 SHEET 4 AA7 4 GLN B 259 TYR B 264 -1 O LEU B 261 N LEU B 252 SHEET 1 AA8 4 ILE B 273 PHE B 278 0 SHEET 2 AA8 4 LEU B 284 TYR B 289 -1 O GLY B 288 N THR B 274 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O ASN B 295 N ALA B 287 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O LEU B 308 N CYS B 294 SHEET 1 AA9 5 VAL C 185 PHE C 191 0 SHEET 2 AA9 5 LEU C 194 ASP C 200 -1 O PHE C 196 N PHE C 189 SHEET 3 AA9 5 VAL C 34 LEU C 39 1 N VAL C 34 O LYS C 197 SHEET 4 AA9 5 ALA C 220 ALA C 226 1 O ILE C 222 N LEU C 37 SHEET 5 AA9 5 SER C 263 ILE C 264 1 O SER C 263 N ILE C 221 SHEET 1 AB1 6 VAL C 185 PHE C 191 0 SHEET 2 AB1 6 LEU C 194 ASP C 200 -1 O PHE C 196 N PHE C 189 SHEET 3 AB1 6 VAL C 34 LEU C 39 1 N VAL C 34 O LYS C 197 SHEET 4 AB1 6 ALA C 220 ALA C 226 1 O ILE C 222 N LEU C 37 SHEET 5 AB1 6 PHE C 267 ASN C 269 1 O ASN C 269 N VAL C 225 SHEET 6 AB1 6 HIS C 322 PHE C 323 1 O HIS C 322 N LEU C 268 SHEET 1 AB2 4 VAL S 5 SER S 7 0 SHEET 2 AB2 4 SER S 17 SER S 23 -1 O SER S 23 N VAL S 5 SHEET 3 AB2 4 THR S 78 THR S 84 -1 O MET S 83 N ARG S 18 SHEET 4 AB2 4 PHE S 68 ASP S 73 -1 N SER S 71 O PHE S 80 SHEET 1 AB3 6 LEU S 11 VAL S 12 0 SHEET 2 AB3 6 THR S 115 VAL S 119 1 O THR S 118 N VAL S 12 SHEET 3 AB3 6 ALA S 92 SER S 99 -1 N TYR S 94 O THR S 115 SHEET 4 AB3 6 GLY S 33 GLN S 39 -1 N HIS S 35 O VAL S 97 SHEET 5 AB3 6 LEU S 45 ILE S 51 -1 O GLU S 46 N ARG S 38 SHEET 6 AB3 6 ILE S 58 TYR S 60 -1 O TYR S 59 N TYR S 50 SHEET 1 AB4 6 SER S 146 PRO S 148 0 SHEET 2 AB4 6 THR S 243 GLU S 246 1 O LYS S 244 N VAL S 147 SHEET 3 AB4 6 GLY S 225 GLN S 231 -1 N TYR S 227 O THR S 243 SHEET 4 AB4 6 LEU S 174 GLN S 179 -1 N PHE S 177 O TYR S 228 SHEET 5 AB4 6 GLN S 186 TYR S 190 -1 O GLN S 186 N LEU S 178 SHEET 6 AB4 6 ASN S 194 LEU S 195 -1 O ASN S 194 N TYR S 190 SHEET 1 AB5 3 VAL S 155 ARG S 160 0 SHEET 2 AB5 3 ALA S 211 ILE S 216 -1 O PHE S 212 N CYS S 159 SHEET 3 AB5 3 PHE S 203 SER S 208 -1 N SER S 206 O THR S 213 SHEET 1 AB6 4 ALA L 35 PHE L 40 0 SHEET 2 AB6 4 GLY L 43 LEU L 48 -1 O ARG L 47 N VAL L 36 SHEET 3 AB6 4 ALA L 80 GLY L 85 -1 O ILE L 82 N VAL L 46 SHEET 4 AB6 4 GLY L 92 VAL L 95 -1 O LEU L 94 N CYS L 81 SSBOND 1 CYS A 112 CYS A 189 1555 1555 2.03 SSBOND 2 CYS S 22 CYS S 96 1555 1555 2.04 SSBOND 3 CYS S 159 CYS S 229 1555 1555 2.04 SSBOND 4 CYS L 78 CYS L 97 1555 1555 2.03 SSBOND 5 CYS L 81 CYS L 115 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