HEADER MEMBRANE PROTEIN/IMMUNE SYSTEM 27-MAR-24 8YUT TITLE CRYO-EM STRUCTURE OF THE AMTHAMINE-BOUND H2R-GS COMPLEX COMPND MOL_ID: 1; COMPND 2 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(S) SUBUNIT ALPHA COMPND 3 ISOFORMS SHORT; COMPND 4 CHAIN: A; COMPND 5 ENGINEERED: YES; COMPND 6 MOL_ID: 2; COMPND 7 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(T) SUBUNIT COMPND 8 BETA-1; COMPND 9 CHAIN: B; COMPND 10 SYNONYM: TRANSDUCIN BETA CHAIN 1; COMPND 11 ENGINEERED: YES; COMPND 12 MOL_ID: 3; COMPND 13 MOLECULE: GUANINE NUCLEOTIDE-BINDING PROTEIN G(I)/G(S)/G(O) SUBUNIT COMPND 14 GAMMA-2; COMPND 15 CHAIN: G; COMPND 16 SYNONYM: G GAMMA-I; COMPND 17 ENGINEERED: YES; COMPND 18 MOL_ID: 4; COMPND 19 MOLECULE: NANOBODY-35; COMPND 20 CHAIN: N; COMPND 21 ENGINEERED: YES; COMPND 22 MOL_ID: 5; COMPND 23 MOLECULE: HISTAMINE H2 RECEPTOR; COMPND 24 CHAIN: R; COMPND 25 SYNONYM: H2R,HH2R,GASTRIC RECEPTOR I; COMPND 26 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: GNAS; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 9 MOL_ID: 2; SOURCE 10 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 11 ORGANISM_COMMON: HUMAN; SOURCE 12 ORGANISM_TAXID: 9606; SOURCE 13 GENE: GNB1; SOURCE 14 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 15 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 16 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 17 MOL_ID: 3; SOURCE 18 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 19 ORGANISM_COMMON: HUMAN; SOURCE 20 ORGANISM_TAXID: 9606; SOURCE 21 GENE: GNG2; SOURCE 22 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 23 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 24 EXPRESSION_SYSTEM_CELL: SF9; SOURCE 25 MOL_ID: 4; SOURCE 26 ORGANISM_SCIENTIFIC: SYNTHETIC CONSTRUCT; SOURCE 27 ORGANISM_TAXID: 32630; SOURCE 28 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 29 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 30 MOL_ID: 5; SOURCE 31 ORGANISM_SCIENTIFIC: HOMO SAPIENS; SOURCE 32 ORGANISM_COMMON: HUMAN; SOURCE 33 ORGANISM_TAXID: 9606; SOURCE 34 GENE: HRH2; SOURCE 35 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 36 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 37 EXPRESSION_SYSTEM_CELL: SF9 KEYWDS GPCR, H2R, HISTAMINE RECEPTOR, MEMBRANE PROTEIN/IMMUNE SYSTEM, KEYWDS 2 MEMBRANE PROTEIN-IMMUNE SYSTEM COMPLEX EXPDTA ELECTRON MICROSCOPY AUTHOR Q.SHEN,X.TANG,X.WEN,S.CHENG,P.XIAO,S.ZANG,D.SHEN,L.JIANG,Y.ZHENG, AUTHOR 2 H.ZHANG,H.XU,C.MAO,M.ZHANG,W.HU,J.SUN,Z.CHEN,Y.ZHANG JRNL AUTH Q.SHEN,X.TANG,X.WEN,S.CHENG,P.XIAO,S.K.ZANG,D.D.SHEN, JRNL AUTH 2 L.JIANG,Y.ZHENG,H.ZHANG,H.XU,C.MAO,M.ZHANG,W.HU,J.P.SUN, JRNL AUTH 3 Y.ZHANG,Z.CHEN JRNL TITL MOLECULAR DETERMINANT UNDERLYING SELECTIVE COUPLING OF JRNL TITL 2 PRIMARY G-PROTEIN BY CLASS A GPCRS. JRNL REF ADV SCI 10120 2024 JRNL REFN ISSN 2198-3844 JRNL PMID 38647423 JRNL DOI 10.1002/ADVS.202310120 REMARK 2 REMARK 2 RESOLUTION. 2.70 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 SOFTWARE PACKAGES : COOT, 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 : REAL REMARK 3 REFINEMENT PROTOCOL : FLEXIBLE FIT 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) : 2.700 REMARK 3 NUMBER OF PARTICLES : 368447 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 8YUT COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBC. REMARK 100 THE DEPOSITION ID IS D_1300040573. 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 : AMTHAMINE-BOUND H2R-GS COMPLEX 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 : FEI TITAN KRIOS REMARK 245 DETECTOR TYPE : GATAN K2 SUMMIT (4K X 4K) REMARK 245 MINIMUM DEFOCUS (NM) : 500.00 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) : 62.00 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, G, N, R 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 GLY A 2 REMARK 465 CYS A 3 REMARK 465 LEU A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 SER A 7 REMARK 465 LYS A 8 REMARK 465 THR A 9 REMARK 465 GLU A 10 REMARK 465 ARG A 77 REMARK 465 ILE A 78 REMARK 465 LEU A 79 REMARK 465 HIS A 80 REMARK 465 VAL A 81 REMARK 465 ASN A 82 REMARK 465 GLY A 83 REMARK 465 TYR A 84 REMARK 465 SER A 85 REMARK 465 GLU A 86 REMARK 465 GLU A 87 REMARK 465 GLU A 88 REMARK 465 CYS A 89 REMARK 465 LYS A 90 REMARK 465 GLN A 91 REMARK 465 TYR A 92 REMARK 465 LYS A 93 REMARK 465 ALA A 94 REMARK 465 VAL A 95 REMARK 465 VAL A 96 REMARK 465 TYR A 97 REMARK 465 SER A 98 REMARK 465 ASN A 99 REMARK 465 THR A 100 REMARK 465 ILE A 101 REMARK 465 GLN A 102 REMARK 465 SER A 103 REMARK 465 ILE A 104 REMARK 465 ILE A 105 REMARK 465 ALA A 106 REMARK 465 ILE A 107 REMARK 465 ILE A 108 REMARK 465 ARG A 109 REMARK 465 ALA A 110 REMARK 465 MET A 111 REMARK 465 GLY A 112 REMARK 465 ARG A 113 REMARK 465 LEU A 114 REMARK 465 LYS A 115 REMARK 465 ILE A 116 REMARK 465 ASP A 117 REMARK 465 PHE A 118 REMARK 465 GLY A 119 REMARK 465 ASP A 120 REMARK 465 SER A 121 REMARK 465 ALA A 122 REMARK 465 ARG A 123 REMARK 465 ALA A 124 REMARK 465 ASP A 125 REMARK 465 ASP A 126 REMARK 465 ALA A 127 REMARK 465 ARG A 128 REMARK 465 GLN A 129 REMARK 465 LEU A 130 REMARK 465 PHE A 131 REMARK 465 VAL A 132 REMARK 465 LEU A 133 REMARK 465 ALA A 134 REMARK 465 GLY A 135 REMARK 465 ALA A 136 REMARK 465 ALA A 137 REMARK 465 GLU A 138 REMARK 465 GLU A 139 REMARK 465 GLY A 140 REMARK 465 PHE A 141 REMARK 465 MET A 142 REMARK 465 THR A 143 REMARK 465 ALA A 144 REMARK 465 GLU A 145 REMARK 465 LEU A 146 REMARK 465 ALA A 147 REMARK 465 GLY A 148 REMARK 465 VAL A 149 REMARK 465 ILE A 150 REMARK 465 LYS A 151 REMARK 465 ARG A 152 REMARK 465 LEU A 153 REMARK 465 TRP A 154 REMARK 465 LYS A 155 REMARK 465 ASP A 156 REMARK 465 SER A 157 REMARK 465 GLY A 158 REMARK 465 VAL A 159 REMARK 465 GLN A 160 REMARK 465 ALA A 161 REMARK 465 CYS A 162 REMARK 465 PHE A 163 REMARK 465 ASN A 164 REMARK 465 ARG A 165 REMARK 465 SER A 166 REMARK 465 ARG A 167 REMARK 465 GLU A 168 REMARK 465 TYR A 169 REMARK 465 GLN A 170 REMARK 465 LEU A 171 REMARK 465 ASN A 172 REMARK 465 ASP A 173 REMARK 465 SER A 174 REMARK 465 ALA A 175 REMARK 465 ALA A 176 REMARK 465 TYR A 177 REMARK 465 TYR A 178 REMARK 465 LEU A 179 REMARK 465 ASN A 180 REMARK 465 ASP A 181 REMARK 465 LEU A 182 REMARK 465 ASP A 183 REMARK 465 ARG A 184 REMARK 465 ILE A 185 REMARK 465 ALA A 186 REMARK 465 GLN A 187 REMARK 465 PRO A 188 REMARK 465 ASN A 189 REMARK 465 TYR A 190 REMARK 465 ILE A 191 REMARK 465 PRO A 192 REMARK 465 THR A 193 REMARK 465 GLN A 194 REMARK 465 GLN A 195 REMARK 465 ASP A 196 REMARK 465 VAL A 197 REMARK 465 LEU A 198 REMARK 465 ARG A 199 REMARK 465 THR A 200 REMARK 465 ARG A 201 REMARK 465 VAL A 202 REMARK 465 LYS A 203 REMARK 465 THR A 204 REMARK 465 SER A 252 REMARK 465 TYR A 253 REMARK 465 ASN A 254 REMARK 465 MET A 255 REMARK 465 VAL A 256 REMARK 465 ILE A 257 REMARK 465 ARG A 258 REMARK 465 GLU A 259 REMARK 465 ASP A 260 REMARK 465 ASN A 261 REMARK 465 GLY A 304 REMARK 465 LYS A 305 REMARK 465 SER A 306 REMARK 465 MET B -15 REMARK 465 HIS B -14 REMARK 465 HIS B -13 REMARK 465 HIS B -12 REMARK 465 HIS B -11 REMARK 465 LEU B -10 REMARK 465 GLU B -9 REMARK 465 VAL B -8 REMARK 465 LEU B -7 REMARK 465 PHE B -6 REMARK 465 GLN B -5 REMARK 465 GLY B -4 REMARK 465 PRO B -3 REMARK 465 GLY B -2 REMARK 465 SER B -1 REMARK 465 SER B 0 REMARK 465 GLY B 1 REMARK 465 SER B 2 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 GLU G 63 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 SER N 127 REMARK 465 SER N 128 REMARK 465 MET R -32 REMARK 465 LYS R -31 REMARK 465 THR R -30 REMARK 465 ILE R -29 REMARK 465 ILE R -28 REMARK 465 ALA R -27 REMARK 465 LEU R -26 REMARK 465 SER R -25 REMARK 465 TYR R -24 REMARK 465 ILE R -23 REMARK 465 PHE R -22 REMARK 465 CYS R -21 REMARK 465 LEU R -20 REMARK 465 VAL R -19 REMARK 465 PHE R -18 REMARK 465 ALA R -17 REMARK 465 ASP R -16 REMARK 465 TYR R -15 REMARK 465 LYS R -14 REMARK 465 ASP R -13 REMARK 465 ASP R -12 REMARK 465 ASP R -11 REMARK 465 ASP R -10 REMARK 465 LYS R -9 REMARK 465 GLU R -8 REMARK 465 PHE R -7 REMARK 465 LEU R -6 REMARK 465 GLU R -5 REMARK 465 VAL R -4 REMARK 465 LEU R -3 REMARK 465 PHE R -2 REMARK 465 GLN R -1 REMARK 465 GLY R 0 REMARK 465 PRO R 1 REMARK 465 ALA R 2 REMARK 465 PRO R 3 REMARK 465 ASN R 4 REMARK 465 GLY R 5 REMARK 465 THR R 6 REMARK 465 ALA R 7 REMARK 465 SER R 8 REMARK 465 SER R 9 REMARK 465 PHE R 10 REMARK 465 CYS R 11 REMARK 465 LEU R 12 REMARK 465 ARG R 306 REMARK 465 LEU R 307 REMARK 465 ALA R 308 REMARK 465 ASN R 309 REMARK 465 ARG R 310 REMARK 465 ASN R 311 REMARK 465 SER R 312 REMARK 465 HIS R 313 REMARK 465 LYS R 314 REMARK 465 THR R 315 REMARK 465 SER R 316 REMARK 465 LEU R 317 REMARK 465 ARG R 318 REMARK 465 SER R 319 REMARK 465 ASN R 320 REMARK 465 ALA R 321 REMARK 465 SER R 322 REMARK 465 GLN R 323 REMARK 465 LEU R 324 REMARK 465 SER R 325 REMARK 465 ARG R 326 REMARK 465 THR R 327 REMARK 465 GLN R 328 REMARK 465 SER R 329 REMARK 465 ARG R 330 REMARK 465 GLU R 331 REMARK 465 PRO R 332 REMARK 465 ARG R 333 REMARK 465 GLN R 334 REMARK 465 GLN R 335 REMARK 465 GLU R 336 REMARK 465 GLU R 337 REMARK 465 LYS R 338 REMARK 465 PRO R 339 REMARK 465 LEU R 340 REMARK 465 LYS R 341 REMARK 465 LEU R 342 REMARK 465 GLN R 343 REMARK 465 VAL R 344 REMARK 465 TRP R 345 REMARK 465 SER R 346 REMARK 465 GLY R 347 REMARK 465 THR R 348 REMARK 465 GLU R 349 REMARK 465 VAL R 350 REMARK 465 THR R 351 REMARK 465 ALA R 352 REMARK 465 PRO R 353 REMARK 465 GLN R 354 REMARK 465 GLY R 355 REMARK 465 ALA R 356 REMARK 465 THR R 357 REMARK 465 ASP R 358 REMARK 465 ARG R 359 REMARK 465 LEU R 360 REMARK 465 GLU R 361 REMARK 465 GLU R 362 REMARK 465 ASN R 363 REMARK 465 LEU R 364 REMARK 465 TYR R 365 REMARK 465 PHE R 366 REMARK 465 GLN R 367 REMARK 465 GLY R 368 REMARK 465 HIS R 369 REMARK 465 HIS R 370 REMARK 465 HIS R 371 REMARK 465 HIS R 372 REMARK 465 HIS R 373 REMARK 465 HIS R 374 REMARK 465 HIS R 375 REMARK 465 HIS R 376 REMARK 465 HIS R 377 REMARK 465 HIS R 378 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 R 173 CG CD CE NZ 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 A 283 48.87 -82.99 REMARK 500 THR A 284 -0.21 -140.47 REMARK 500 CYS B 148 134.94 -38.26 REMARK 500 THR B 164 -1.45 81.35 REMARK 500 VAL N 48 -62.72 -99.38 REMARK 500 ASN N 77 62.01 60.67 REMARK 500 ARG R 50 96.92 -64.29 REMARK 500 THR R 170 -157.62 -127.73 REMARK 500 PHE R 191 -50.22 -120.88 REMARK 500 REMARK 500 REMARK: NULL REMARK 900 REMARK 900 RELATED ENTRIES REMARK 900 RELATED ID: EMD-39582 RELATED DB: EMDB REMARK 900 CRYO-EM STRUCTURE OF THE AMTHAMINE-BOUND H2R-GS COMPLEX DBREF 8YUT A 1 394 PDB 8YUT 8YUT 1 394 DBREF 8YUT B 2 340 UNP P62873 GBB1_HUMAN 2 340 DBREF 8YUT G 1 71 UNP P59768 GBG2_HUMAN 1 71 DBREF 8YUT N 1 128 PDB 8YUT 8YUT 1 128 DBREF 8YUT R 2 359 UNP P25021 HRH2_HUMAN 2 359 SEQADV 8YUT MET B -15 UNP P62873 INITIATING METHIONINE SEQADV 8YUT HIS B -14 UNP P62873 EXPRESSION TAG SEQADV 8YUT HIS B -13 UNP P62873 EXPRESSION TAG SEQADV 8YUT HIS B -12 UNP P62873 EXPRESSION TAG SEQADV 8YUT HIS B -11 UNP P62873 EXPRESSION TAG SEQADV 8YUT LEU B -10 UNP P62873 EXPRESSION TAG SEQADV 8YUT GLU B -9 UNP P62873 EXPRESSION TAG SEQADV 8YUT VAL B -8 UNP P62873 EXPRESSION TAG SEQADV 8YUT LEU B -7 UNP P62873 EXPRESSION TAG SEQADV 8YUT PHE B -6 UNP P62873 EXPRESSION TAG SEQADV 8YUT GLN B -5 UNP P62873 EXPRESSION TAG SEQADV 8YUT GLY B -4 UNP P62873 EXPRESSION TAG SEQADV 8YUT PRO B -3 UNP P62873 EXPRESSION TAG SEQADV 8YUT GLY B -2 UNP P62873 EXPRESSION TAG SEQADV 8YUT SER B -1 UNP P62873 EXPRESSION TAG SEQADV 8YUT SER B 0 UNP P62873 EXPRESSION TAG SEQADV 8YUT GLY B 1 UNP P62873 EXPRESSION TAG SEQADV 8YUT MET R -32 UNP P25021 INITIATING METHIONINE SEQADV 8YUT LYS R -31 UNP P25021 EXPRESSION TAG SEQADV 8YUT THR R -30 UNP P25021 EXPRESSION TAG SEQADV 8YUT ILE R -29 UNP P25021 EXPRESSION TAG SEQADV 8YUT ILE R -28 UNP P25021 EXPRESSION TAG SEQADV 8YUT ALA R -27 UNP P25021 EXPRESSION TAG SEQADV 8YUT LEU R -26 UNP P25021 EXPRESSION TAG SEQADV 8YUT SER R -25 UNP P25021 EXPRESSION TAG SEQADV 8YUT TYR R -24 UNP P25021 EXPRESSION TAG SEQADV 8YUT ILE R -23 UNP P25021 EXPRESSION TAG SEQADV 8YUT PHE R -22 UNP P25021 EXPRESSION TAG SEQADV 8YUT CYS R -21 UNP P25021 EXPRESSION TAG SEQADV 8YUT LEU R -20 UNP P25021 EXPRESSION TAG SEQADV 8YUT VAL R -19 UNP P25021 EXPRESSION TAG SEQADV 8YUT PHE R -18 UNP P25021 EXPRESSION TAG SEQADV 8YUT ALA R -17 UNP P25021 EXPRESSION TAG SEQADV 8YUT ASP R -16 UNP P25021 EXPRESSION TAG SEQADV 8YUT TYR R -15 UNP P25021 EXPRESSION TAG SEQADV 8YUT LYS R -14 UNP P25021 EXPRESSION TAG SEQADV 8YUT ASP R -13 UNP P25021 EXPRESSION TAG SEQADV 8YUT ASP R -12 UNP P25021 EXPRESSION TAG SEQADV 8YUT ASP R -11 UNP P25021 EXPRESSION TAG SEQADV 8YUT ASP R -10 UNP P25021 EXPRESSION TAG SEQADV 8YUT LYS R -9 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLU R -8 UNP P25021 EXPRESSION TAG SEQADV 8YUT PHE R -7 UNP P25021 EXPRESSION TAG SEQADV 8YUT LEU R -6 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLU R -5 UNP P25021 EXPRESSION TAG SEQADV 8YUT VAL R -4 UNP P25021 EXPRESSION TAG SEQADV 8YUT LEU R -3 UNP P25021 EXPRESSION TAG SEQADV 8YUT PHE R -2 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLN R -1 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLY R 0 UNP P25021 EXPRESSION TAG SEQADV 8YUT PRO R 1 UNP P25021 EXPRESSION TAG SEQADV 8YUT LEU R 360 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLU R 361 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLU R 362 UNP P25021 EXPRESSION TAG SEQADV 8YUT ASN R 363 UNP P25021 EXPRESSION TAG SEQADV 8YUT LEU R 364 UNP P25021 EXPRESSION TAG SEQADV 8YUT TYR R 365 UNP P25021 EXPRESSION TAG SEQADV 8YUT PHE R 366 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLN R 367 UNP P25021 EXPRESSION TAG SEQADV 8YUT GLY R 368 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 369 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 370 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 371 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 372 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 373 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 374 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 375 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 376 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 377 UNP P25021 EXPRESSION TAG SEQADV 8YUT HIS R 378 UNP P25021 EXPRESSION TAG SEQRES 1 A 378 MET GLY CYS LEU GLY ASN SER LYS THR GLU ASP GLN ARG SEQRES 2 A 378 ASN GLU GLU LYS ALA GLN ARG GLU ALA ASN LYS LYS ILE SEQRES 3 A 378 GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR ARG ALA SEQRES 4 A 378 THR HIS ARG LEU LEU LEU LEU GLY ALA GLY GLU SER GLY SEQRES 5 A 378 LYS SER THR ILE VAL LYS GLN MET ARG ILE LEU HIS VAL SEQRES 6 A 378 ASN GLY TYR SER GLU GLU GLU CYS LYS GLN TYR LYS ALA SEQRES 7 A 378 VAL VAL TYR SER ASN THR ILE GLN SER ILE ILE ALA ILE SEQRES 8 A 378 ILE ARG ALA MET GLY ARG LEU LYS ILE ASP PHE GLY ASP SEQRES 9 A 378 SER ALA ARG ALA ASP ASP ALA ARG GLN LEU PHE VAL LEU SEQRES 10 A 378 ALA GLY ALA ALA GLU GLU GLY PHE MET THR ALA GLU LEU SEQRES 11 A 378 ALA GLY VAL ILE LYS ARG LEU TRP LYS ASP SER GLY VAL SEQRES 12 A 378 GLN ALA CYS PHE ASN ARG SER ARG GLU TYR GLN LEU ASN SEQRES 13 A 378 ASP SER ALA ALA TYR TYR LEU ASN ASP LEU ASP ARG ILE SEQRES 14 A 378 ALA GLN PRO ASN TYR ILE PRO THR GLN GLN ASP VAL LEU SEQRES 15 A 378 ARG THR ARG VAL LYS THR SER GLY ILE PHE GLU THR LYS SEQRES 16 A 378 PHE GLN VAL ASP LYS VAL ASN PHE HIS MET PHE ASP VAL SEQRES 17 A 378 GLY ALA GLN ARG ASP GLU ARG ARG LYS TRP ILE GLN CYS SEQRES 18 A 378 PHE ASN ASP VAL THR ALA ILE ILE PHE VAL VAL ALA SER SEQRES 19 A 378 SER SER TYR ASN MET VAL ILE ARG GLU ASP ASN GLN THR SEQRES 20 A 378 ASN ARG LEU GLN GLU ALA LEU ASN LEU PHE LYS SER ILE SEQRES 21 A 378 TRP ASN ASN ARG TRP LEU ARG THR ILE SER VAL ILE LEU SEQRES 22 A 378 PHE LEU ASN LYS GLN ASP LEU LEU ALA GLU LYS VAL LEU SEQRES 23 A 378 ALA GLY LYS SER LYS ILE GLU ASP TYR PHE PRO GLU PHE SEQRES 24 A 378 ALA ARG TYR THR THR PRO GLU ASP ALA THR PRO GLU PRO SEQRES 25 A 378 GLY GLU ASP PRO ARG VAL THR ARG ALA LYS TYR PHE ILE SEQRES 26 A 378 ARG ASP GLU PHE LEU ARG ILE SER THR ALA SER GLY ASP SEQRES 27 A 378 GLY ARG HIS TYR CYS TYR PRO HIS PHE THR CYS SER VAL SEQRES 28 A 378 ASP THR GLU ASN ILE ARG ARG VAL PHE ASN ASP CYS ARG SEQRES 29 A 378 ASP ILE ILE GLN ARG MET HIS LEU ARG GLN TYR GLU LEU SEQRES 30 A 378 LEU SEQRES 1 B 356 MET HIS HIS HIS HIS LEU GLU VAL LEU PHE GLN GLY PRO SEQRES 2 B 356 GLY SER SER GLY SER GLU LEU ASP GLN LEU ARG GLN GLU SEQRES 3 B 356 ALA GLU GLN LEU LYS ASN GLN ILE ARG ASP ALA ARG LYS SEQRES 4 B 356 ALA CYS ALA ASP ALA THR LEU SER GLN ILE THR ASN ASN SEQRES 5 B 356 ILE ASP PRO VAL GLY ARG ILE GLN MET ARG THR ARG ARG SEQRES 6 B 356 THR LEU ARG GLY HIS LEU ALA LYS ILE TYR ALA MET HIS SEQRES 7 B 356 TRP GLY THR ASP SER ARG LEU LEU VAL SER ALA SER GLN SEQRES 8 B 356 ASP GLY LYS LEU ILE ILE TRP ASP SER TYR THR THR ASN SEQRES 9 B 356 LYS VAL HIS ALA ILE PRO LEU ARG SER SER TRP VAL MET SEQRES 10 B 356 THR CYS ALA TYR ALA PRO SER GLY ASN TYR VAL ALA CYS SEQRES 11 B 356 GLY GLY LEU ASP ASN ILE CYS SER ILE TYR ASN LEU LYS SEQRES 12 B 356 THR ARG GLU GLY ASN VAL ARG VAL SER ARG GLU LEU ALA SEQRES 13 B 356 GLY HIS THR GLY TYR LEU SER CYS CYS ARG PHE LEU ASP SEQRES 14 B 356 ASP ASN GLN ILE VAL THR SER SER GLY ASP THR THR CYS SEQRES 15 B 356 ALA LEU TRP ASP ILE GLU THR GLY GLN GLN THR THR THR SEQRES 16 B 356 PHE THR GLY HIS THR GLY ASP VAL MET SER LEU SER LEU SEQRES 17 B 356 ALA PRO ASP THR ARG LEU PHE VAL SER GLY ALA CYS ASP SEQRES 18 B 356 ALA SER ALA LYS LEU TRP ASP VAL ARG GLU GLY MET CYS SEQRES 19 B 356 ARG GLN THR PHE THR GLY HIS GLU SER ASP ILE ASN ALA SEQRES 20 B 356 ILE CYS PHE PHE PRO ASN GLY ASN ALA PHE ALA THR GLY SEQRES 21 B 356 SER ASP ASP ALA THR CYS ARG LEU PHE ASP LEU ARG ALA SEQRES 22 B 356 ASP GLN GLU LEU MET THR TYR SER HIS ASP ASN ILE ILE SEQRES 23 B 356 CYS GLY ILE THR SER VAL SER PHE SER LYS SER GLY ARG SEQRES 24 B 356 LEU LEU LEU ALA GLY TYR ASP ASP PHE ASN CYS ASN VAL SEQRES 25 B 356 TRP ASP ALA LEU LYS ALA ASP ARG ALA GLY VAL LEU ALA SEQRES 26 B 356 GLY HIS ASP ASN ARG VAL SER CYS LEU GLY VAL THR ASP SEQRES 27 B 356 ASP GLY MET ALA VAL ALA THR GLY SER TRP ASP SER PHE SEQRES 28 B 356 LEU LYS ILE TRP ASN 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 N 128 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 N 128 PRO GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 N 128 PHE THR PHE SER ASN TYR LYS MET ASN TRP VAL ARG GLN SEQRES 4 N 128 ALA PRO GLY LYS GLY LEU GLU TRP VAL SER ASP ILE SER SEQRES 5 N 128 GLN SER GLY ALA SER ILE SER TYR THR GLY SER VAL LYS SEQRES 6 N 128 GLY ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR SEQRES 7 N 128 LEU TYR LEU GLN MET ASN SER LEU LYS PRO GLU ASP THR SEQRES 8 N 128 ALA VAL TYR TYR CYS ALA ARG CYS PRO ALA PRO PHE THR SEQRES 9 N 128 ARG ASP CYS PHE ASP VAL THR SER THR THR TYR ALA TYR SEQRES 10 N 128 ARG GLY GLN GLY THR GLN VAL THR VAL SER SER SEQRES 1 R 411 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 R 411 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP LYS GLU PHE SEQRES 3 R 411 LEU GLU VAL LEU PHE GLN GLY PRO ALA PRO ASN GLY THR SEQRES 4 R 411 ALA SER SER PHE CYS LEU ASP SER THR ALA CYS LYS ILE SEQRES 5 R 411 THR ILE THR VAL VAL LEU ALA VAL LEU ILE LEU ILE THR SEQRES 6 R 411 VAL ALA GLY ASN VAL VAL VAL CYS LEU ALA VAL GLY LEU SEQRES 7 R 411 ASN ARG ARG LEU ARG ASN LEU THR ASN CYS PHE ILE VAL SEQRES 8 R 411 SER LEU ALA ILE THR ASP LEU LEU LEU GLY LEU LEU VAL SEQRES 9 R 411 LEU PRO PHE SER ALA ILE TYR GLN LEU SER CYS LYS TRP SEQRES 10 R 411 SER PHE GLY LYS VAL PHE CYS ASN ILE TYR THR SER LEU SEQRES 11 R 411 ASP VAL MET LEU CYS THR ALA SER ILE LEU ASN LEU PHE SEQRES 12 R 411 MET ILE SER LEU ASP ARG TYR CYS ALA VAL MET ASP PRO SEQRES 13 R 411 LEU ARG TYR PRO VAL LEU VAL THR PRO VAL ARG VAL ALA SEQRES 14 R 411 ILE SER LEU VAL LEU ILE TRP VAL ILE SER ILE THR LEU SEQRES 15 R 411 SER PHE LEU SER ILE HIS LEU GLY TRP ASN SER ARG ASN SEQRES 16 R 411 GLU THR SER LYS GLY ASN HIS THR THR SER LYS CYS LYS SEQRES 17 R 411 VAL GLN VAL ASN GLU VAL TYR GLY LEU VAL ASP GLY LEU SEQRES 18 R 411 VAL THR PHE TYR LEU PRO LEU LEU ILE MET CYS ILE THR SEQRES 19 R 411 TYR TYR ARG ILE PHE LYS VAL ALA ARG ASP GLN ALA LYS SEQRES 20 R 411 ARG ILE ASN HIS ILE SER SER TRP LYS ALA ALA THR ILE SEQRES 21 R 411 ARG GLU HIS LYS ALA THR VAL THR LEU ALA ALA VAL MET SEQRES 22 R 411 GLY ALA PHE ILE ILE CYS TRP PHE PRO TYR PHE THR ALA SEQRES 23 R 411 PHE VAL TYR ARG GLY LEU ARG GLY ASP ASP ALA ILE ASN SEQRES 24 R 411 GLU VAL LEU GLU ALA ILE VAL LEU TRP LEU GLY TYR ALA SEQRES 25 R 411 ASN SER ALA LEU ASN PRO ILE LEU TYR ALA ALA LEU ASN SEQRES 26 R 411 ARG ASP PHE ARG THR GLY TYR GLN GLN LEU PHE CYS CYS SEQRES 27 R 411 ARG LEU ALA ASN ARG ASN SER HIS LYS THR SER LEU ARG SEQRES 28 R 411 SER ASN ALA SER GLN LEU SER ARG THR GLN SER ARG GLU SEQRES 29 R 411 PRO ARG GLN GLN GLU GLU LYS PRO LEU LYS LEU GLN VAL SEQRES 30 R 411 TRP SER GLY THR GLU VAL THR ALA PRO GLN GLY ALA THR SEQRES 31 R 411 ASP ARG LEU GLU GLU ASN LEU TYR PHE GLN GLY HIS HIS SEQRES 32 R 411 HIS HIS HIS HIS HIS HIS HIS HIS HET D67 R 401 10 HET CLR R 402 28 HETNAM CLR CHOLESTEROL FORMUL 6 D67 FORMUL 7 CLR C27 H46 O HELIX 1 AA1 ASP A 11 ALA A 39 1 29 HELIX 2 AA2 GLY A 52 MET A 60 1 9 HELIX 3 AA3 LYS A 233 ASN A 239 5 7 HELIX 4 AA4 ASN A 264 ASN A 278 1 15 HELIX 5 AA5 LYS A 293 LEU A 302 1 10 HELIX 6 AA6 LYS A 307 TYR A 311 5 5 HELIX 7 AA7 PHE A 312 TYR A 318 5 7 HELIX 8 AA8 ASP A 331 THR A 350 1 20 HELIX 9 AA9 GLU A 370 TYR A 391 1 22 HELIX 10 AB1 LEU B 4 CYS B 25 1 22 HELIX 11 AB2 THR B 29 THR B 34 1 6 HELIX 12 AB3 ASN B 35 ILE B 37 5 3 HELIX 13 AB4 ALA G 7 ASN G 24 1 18 HELIX 14 AB5 LYS G 29 HIS G 44 1 16 HELIX 15 AB6 ALA G 45 ASP G 48 5 4 HELIX 16 AB7 THR N 28 TYR N 32 5 5 HELIX 17 AB8 LYS N 87 THR N 91 5 5 HELIX 18 AB9 SER R 14 ASN R 46 1 33 HELIX 19 AC1 ARG R 47 ARG R 50 5 4 HELIX 20 AC2 ASN R 54 VAL R 71 1 18 HELIX 21 AC3 VAL R 71 CYS R 82 1 12 HELIX 22 AC4 GLY R 87 ASP R 122 1 36 HELIX 23 AC5 ARG R 125 VAL R 130 1 6 HELIX 24 AC6 THR R 131 PHE R 151 1 21 HELIX 25 AC7 PHE R 151 LEU R 156 1 6 HELIX 26 AC8 ASN R 179 PHE R 191 1 13 HELIX 27 AC9 PHE R 191 SER R 220 1 30 HELIX 28 AD1 ARG R 228 GLY R 261 1 34 HELIX 29 AD2 ASP R 262 ILE R 265 5 4 HELIX 30 AD3 ASN R 266 ASN R 280 1 15 HELIX 31 AD4 LEU R 283 TYR R 288 1 6 HELIX 32 AD5 ASN R 292 CYS R 305 1 14 SHEET 1 AA1 6 ILE A 207 VAL A 214 0 SHEET 2 AA1 6 VAL A 217 VAL A 224 -1 O PHE A 219 N PHE A 212 SHEET 3 AA1 6 THR A 40 LEU A 46 1 N LEU A 43 O HIS A 220 SHEET 4 AA1 6 ALA A 243 ALA A 249 1 O ILE A 245 N LEU A 44 SHEET 5 AA1 6 SER A 286 ASN A 292 1 O PHE A 290 N VAL A 248 SHEET 6 AA1 6 CYS A 359 PHE A 363 1 O HIS A 362 N LEU A 291 SHEET 1 AA2 4 THR B 47 LEU B 51 0 SHEET 2 AA2 4 LEU B 336 TRP B 339 -1 O ILE B 338 N ARG B 48 SHEET 3 AA2 4 VAL B 327 GLY B 330 -1 N VAL B 327 O TRP B 339 SHEET 4 AA2 4 CYS B 317 VAL B 320 -1 N GLY B 319 O ALA B 328 SHEET 1 AA3 4 ILE B 58 TRP B 63 0 SHEET 2 AA3 4 LEU B 69 SER B 74 -1 O VAL B 71 N HIS B 62 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 ALA B 113 N ALA B 104 SHEET 3 AA4 4 CYS B 121 ASN B 125 -1 O TYR B 124 N VAL B 112 SHEET 4 AA4 4 ARG B 134 LEU B 139 -1 O ARG B 137 N ILE B 123 SHEET 1 AA5 4 LEU B 146 ASP B 153 0 SHEET 2 AA5 4 GLN B 156 SER B 161 -1 O SER B 160 N SER B 147 SHEET 3 AA5 4 CYS B 166 ASP B 170 -1 O TRP B 169 N ILE B 157 SHEET 4 AA5 4 GLN B 175 PHE B 180 -1 O THR B 177 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 VAL B 200 N SER B 191 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 THR B 223 -1 O PHE B 222 N ALA B 208 SHEET 1 AA7 4 ILE B 229 PHE B 234 0 SHEET 2 AA7 4 ALA B 240 SER B 245 -1 O GLY B 244 N ALA B 231 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 LEU B 286 N SER B 277 SHEET 3 AA8 4 CYS B 294 ASP B 298 -1 O TRP B 297 N LEU B 285 SHEET 4 AA8 4 ARG B 304 LEU B 308 -1 O LEU B 308 N CYS B 294 SHEET 1 AA9 4 GLN N 3 SER N 7 0 SHEET 2 AA9 4 LEU N 18 SER N 25 -1 O ALA N 23 N GLN N 5 SHEET 3 AA9 4 THR N 78 MET N 83 -1 O LEU N 81 N LEU N 20 SHEET 4 AA9 4 PHE N 68 ASP N 73 -1 N ASP N 73 O THR N 78 SHEET 1 AB1 6 GLY N 10 LEU N 11 0 SHEET 2 AB1 6 THR N 122 THR N 125 1 O GLN N 123 N GLY N 10 SHEET 3 AB1 6 ALA N 92 ARG N 98 -1 N TYR N 94 O THR N 122 SHEET 4 AB1 6 MET N 34 GLN N 39 -1 N GLN N 39 O VAL N 93 SHEET 5 AB1 6 LEU N 45 ILE N 51 -1 O GLU N 46 N ARG N 38 SHEET 6 AB1 6 ILE N 58 TYR N 60 -1 O SER N 59 N ASP N 50 SSBOND 1 CYS N 22 CYS N 96 1555 1555 2.03 SSBOND 2 CYS N 99 CYS N 107 1555 1555 2.03 SSBOND 3 CYS R 91 CYS R 174 1555 1555 2.04 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