HEADER MEMBRANE PROTEIN 19-FEB-24 8W1V TITLE THE BETA2 ADRENERGIC RECEPTOR BOUND TO A BITOPIC LIGAND COMPND MOL_ID: 1; COMPND 2 MOLECULE: BETA-2 ADRENERGIC RECEPTOR,ENDOLYSIN; COMPND 3 CHAIN: A, B; COMPND 4 SYNONYM: BETA-2 ADRENORECEPTOR,BETA-2 ADRENOCEPTOR,LYSIS PROTEIN, COMPND 5 LYSOZYME,MURAMIDASE; COMPND 6 EC: 3.2.1.17; COMPND 7 ENGINEERED: YES; COMPND 8 MUTATION: YES; COMPND 9 MOL_ID: 2; COMPND 10 MOLECULE: NANOBODY60; COMPND 11 CHAIN: D, F; COMPND 12 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: ADRB2, ADRB2R, B2AR; SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 7 EXPRESSION_SYSTEM_TAXID: 7108; SOURCE 8 MOL_ID: 2; SOURCE 9 ORGANISM_SCIENTIFIC: LAMA GLAMA; SOURCE 10 ORGANISM_TAXID: 9844; SOURCE 11 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA; SOURCE 12 EXPRESSION_SYSTEM_TAXID: 7108 KEYWDS SIGNAL TRANSDUCTION, BITOPIC LIGAND, , SIGNALING PROTEIN, GPCR, KEYWDS 2 MEMBRANE PROTEIN EXPDTA X-RAY DIFFRACTION AUTHOR B.GAISER,M.DANIELSEN,X.XU,K.JORGENSEN,P.FRONIK,E.MARCHER-RORSTED, AUTHOR 2 T.WROBE,K.HIRATA,X.LIU,J.MATHIESEN,D.PEDERSEN JRNL AUTH B.I.GAISER,M.DANIELSEN,X.XU,K.ROPKE JORGENSEN,P.FRONIK, JRNL AUTH 2 E.MARCHER-RORSTED,T.M.WROBEL,X.LIU,J.MOSOLFF MATHIESEN, JRNL AUTH 3 D.SEJER PEDERSEN JRNL TITL BITOPIC LIGANDS SUPPORT THE PRESENCE OF A METASTABLE BINDING JRNL TITL 2 SITE AT THE BETA 2 ADRENERGIC RECEPTOR. JRNL REF J.MED.CHEM. 2024 JRNL REFN ISSN 0022-2623 JRNL PMID 38952152 JRNL DOI 10.1021/ACS.JMEDCHEM.4C00578 REMARK 2 REMARK 2 RESOLUTION. 3.00 ANGSTROMS. REMARK 3 REMARK 3 REFINEMENT. REMARK 3 PROGRAM : PHENIX 1.20.1_4487 REMARK 3 AUTHORS : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN REMARK 3 : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE, REMARK 3 : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER, REMARK 3 : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY, REMARK 3 : REETAL PAI,RANDY READ,JANE RICHARDSON, REMARK 3 : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI, REMARK 3 : NICHOLAS SAUTER,JACOB SMITH,LAURENT REMARK 3 : STORONI,TOM TERWILLIGER,PETER ZWART REMARK 3 REMARK 3 REFINEMENT TARGET : GEOSTD + MONOMER LIBRARY + CDL V1.2 REMARK 3 REMARK 3 DATA USED IN REFINEMENT. REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00 REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 48.44 REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.360 REMARK 3 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 3 NUMBER OF REFLECTIONS : 37359 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT. REMARK 3 R VALUE (WORKING + TEST SET) : 0.250 REMARK 3 R VALUE (WORKING SET) : 0.248 REMARK 3 FREE R VALUE : 0.292 REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.540 REMARK 3 FREE R VALUE TEST SET COUNT : 2068 REMARK 3 REMARK 3 FIT TO DATA USED IN REFINEMENT (IN BINS). REMARK 3 BIN RESOLUTION RANGE COMPL. NWORK NFREE RWORK RFREE REMARK 3 1 48.4400 - 7.3900 0.99 2383 142 0.2162 0.2513 REMARK 3 2 7.3900 - 5.8700 1.00 2377 136 0.2668 0.2785 REMARK 3 3 5.8700 - 5.1300 1.00 2358 140 0.2665 0.3246 REMARK 3 4 5.1300 - 4.6600 1.00 2355 142 0.2324 0.2731 REMARK 3 5 4.6600 - 4.3300 1.00 2330 138 0.2201 0.2833 REMARK 3 6 4.3300 - 4.0700 1.00 2374 142 0.2121 0.2586 REMARK 3 7 4.0700 - 3.8700 1.00 2350 128 0.2224 0.2359 REMARK 3 8 3.8700 - 3.7000 1.00 2330 145 0.2332 0.2870 REMARK 3 9 3.7000 - 3.5600 1.00 2369 137 0.2427 0.3100 REMARK 3 10 3.5600 - 3.4300 1.00 2329 139 0.2582 0.2889 REMARK 3 11 3.4300 - 3.3300 1.00 2337 140 0.2665 0.3057 REMARK 3 12 3.3300 - 3.2300 1.00 2356 135 0.2777 0.3299 REMARK 3 13 3.2300 - 3.1500 1.00 2347 137 0.3110 0.3531 REMARK 3 14 3.1500 - 3.0700 1.00 2345 134 0.3270 0.3752 REMARK 3 15 3.0700 - 3.0000 1.00 2351 133 0.3606 0.4421 REMARK 3 REMARK 3 BULK SOLVENT MODELLING. REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL REMARK 3 SOLVENT RADIUS : 1.10 REMARK 3 SHRINKAGE RADIUS : 0.90 REMARK 3 K_SOL : NULL REMARK 3 B_SOL : NULL REMARK 3 REMARK 3 ERROR ESTIMATES. REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.490 REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.556 REMARK 3 REMARK 3 B VALUES. REMARK 3 FROM WILSON PLOT (A**2) : 54.78 REMARK 3 MEAN B VALUE (OVERALL, A**2) : 60.43 REMARK 3 OVERALL ANISOTROPIC B VALUE. REMARK 3 B11 (A**2) : NULL REMARK 3 B22 (A**2) : NULL REMARK 3 B33 (A**2) : NULL REMARK 3 B12 (A**2) : NULL REMARK 3 B13 (A**2) : NULL REMARK 3 B23 (A**2) : NULL REMARK 3 REMARK 3 TWINNING INFORMATION. REMARK 3 FRACTION: NULL REMARK 3 OPERATOR: NULL REMARK 3 REMARK 3 DEVIATIONS FROM IDEAL VALUES. REMARK 3 RMSD COUNT REMARK 3 BOND : 0.007 9106 REMARK 3 ANGLE : 0.705 12348 REMARK 3 CHIRALITY : 0.043 1429 REMARK 3 PLANARITY : 0.004 1509 REMARK 3 DIHEDRAL : 14.879 3188 REMARK 3 REMARK 3 TLS DETAILS REMARK 3 NUMBER OF TLS GROUPS : NULL REMARK 3 REMARK 3 NCS DETAILS REMARK 3 NUMBER OF NCS GROUPS : NULL REMARK 3 REMARK 3 OTHER REFINEMENT REMARKS: NULL REMARK 4 REMARK 4 8W1V COMPLIES WITH FORMAT V. 3.30, 13-JUL-11 REMARK 100 REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB. REMARK 100 THE DEPOSITION ID IS D_1000281248. REMARK 200 REMARK 200 EXPERIMENTAL DETAILS REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION REMARK 200 DATE OF DATA COLLECTION : 15-JUL-20 REMARK 200 TEMPERATURE (KELVIN) : 80 REMARK 200 PH : NULL REMARK 200 NUMBER OF CRYSTALS USED : 1 REMARK 200 REMARK 200 SYNCHROTRON (Y/N) : Y REMARK 200 RADIATION SOURCE : SPRING-8 REMARK 200 BEAMLINE : BL32XU REMARK 200 X-RAY GENERATOR MODEL : NULL REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M REMARK 200 WAVELENGTH OR RANGE (A) : 1.000 REMARK 200 MONOCHROMATOR : NULL REMARK 200 OPTICS : NULL REMARK 200 REMARK 200 DETECTOR TYPE : PIXEL REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 9M REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS REMARK 200 DATA SCALING SOFTWARE : XSCALE REMARK 200 REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 40547 REMARK 200 RESOLUTION RANGE HIGH (A) : 2.920 REMARK 200 RESOLUTION RANGE LOW (A) : 48.440 REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL REMARK 200 REMARK 200 OVERALL. REMARK 200 COMPLETENESS FOR RANGE (%) : 99.9 REMARK 200 DATA REDUNDANCY : 55.50 REMARK 200 R MERGE (I) : NULL REMARK 200 R SYM (I) : NULL REMARK 200 FOR THE DATA SET : 8.2500 REMARK 200 REMARK 200 IN THE HIGHEST RESOLUTION SHELL. REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00 REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.10 REMARK 200 COMPLETENESS FOR SHELL (%) : NULL REMARK 200 DATA REDUNDANCY IN SHELL : NULL REMARK 200 R MERGE FOR SHELL (I) : NULL REMARK 200 R SYM FOR SHELL (I) : NULL REMARK 200 FOR SHELL : NULL REMARK 200 REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT REMARK 200 SOFTWARE USED: PHENIX REMARK 200 STARTING MODEL: NULL REMARK 200 REMARK 200 REMARK: NULL REMARK 280 REMARK 280 CRYSTAL REMARK 280 SOLVENT CONTENT, VS (%): 62.57 REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.29 REMARK 280 REMARK 280 CRYSTALLIZATION CONDITIONS: 100 MM TRIS BUFFER (PH 8.0), 100 TO REMARK 280 175 MM LITHIUM SULFATE, 38% TO 42% PEG400, AND 10 MM EDTA, REMARK 280 LIPIDIC CUBIC PHASE, TEMPERATURE 293K REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1 REMARK 290 REMARK 290 SYMOP SYMMETRY REMARK 290 NNNMMM OPERATOR REMARK 290 1555 X,Y,Z REMARK 290 2555 -X,Y+1/2,-Z REMARK 290 REMARK 290 WHERE NNN -> OPERATOR NUMBER REMARK 290 MMM -> TRANSLATION VECTOR REMARK 290 REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY REMARK 290 RELATED MOLECULES. REMARK 290 SMTRY1 1 1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 1 0.000000 1.000000 0.000000 0.00000 REMARK 290 SMTRY3 1 0.000000 0.000000 1.000000 0.00000 REMARK 290 SMTRY1 2 -1.000000 0.000000 0.000000 0.00000 REMARK 290 SMTRY2 2 0.000000 1.000000 0.000000 73.38500 REMARK 290 SMTRY3 2 0.000000 0.000000 -1.000000 0.00000 REMARK 290 REMARK 290 REMARK: NULL 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: TETRAMERIC REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, D, F 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 -23 REMARK 465 LYS A -22 REMARK 465 THR A -21 REMARK 465 ILE A -20 REMARK 465 ILE A -19 REMARK 465 ALA A -18 REMARK 465 LEU A -17 REMARK 465 SER A -16 REMARK 465 TYR A -15 REMARK 465 ILE A -14 REMARK 465 PHE A -13 REMARK 465 CYS A -12 REMARK 465 LEU A -11 REMARK 465 VAL A -10 REMARK 465 PHE A -9 REMARK 465 ALA A -8 REMARK 465 ASP A -7 REMARK 465 TYR A -6 REMARK 465 LYS A -5 REMARK 465 ASP A -4 REMARK 465 ASP A -3 REMARK 465 ASP A -2 REMARK 465 ASP A -1 REMARK 465 ALA A 0 REMARK 465 MET A 1 REMARK 465 GLY A 2 REMARK 465 GLN A 3 REMARK 465 PRO A 4 REMARK 465 GLY A 5 REMARK 465 ASN A 6 REMARK 465 GLY A 7 REMARK 465 SER A 8 REMARK 465 ALA A 9 REMARK 465 PHE A 10 REMARK 465 LEU A 11 REMARK 465 LEU A 12 REMARK 465 ALA A 13 REMARK 465 PRO A 14 REMARK 465 ASN A 15 REMARK 465 ARG A 16 REMARK 465 SER A 17 REMARK 465 HIS A 18 REMARK 465 ALA A 19 REMARK 465 PRO A 20 REMARK 465 ASP A 21 REMARK 465 HIS A 22 REMARK 465 ASP A 23 REMARK 465 VAL A 24 REMARK 465 THR A 25 REMARK 465 GLN A 26 REMARK 465 GLN A 27 REMARK 465 ARG A 28 REMARK 465 TYR A 231 REMARK 465 LYS A 232 REMARK 465 ILE A 233 REMARK 465 ASP A 234 REMARK 465 LYS A 235 REMARK 465 SER A 236 REMARK 465 GLU A 237 REMARK 465 GLY A 238 REMARK 465 ARG A 239 REMARK 465 PHE A 240 REMARK 465 HIS A 241 REMARK 465 VAL A 242 REMARK 465 GLN A 243 REMARK 465 ASN A 244 REMARK 465 LEU A 245 REMARK 465 SER A 246 REMARK 465 GLN A 247 REMARK 465 VAL A 248 REMARK 465 GLU A 249 REMARK 465 GLN A 250 REMARK 465 ASP A 251 REMARK 465 GLY A 252 REMARK 465 ARG A 253 REMARK 465 THR A 254 REMARK 465 GLY A 255 REMARK 465 HIS A 256 REMARK 465 GLY A 257 REMARK 465 LEU A 258 REMARK 465 ARG A 259 REMARK 465 ARG A 260 REMARK 465 SER A 261 REMARK 465 SER A 262 REMARK 465 ARG A 979 REMARK 465 ARG A 980 REMARK 465 SER A 981 REMARK 465 SER A 982 REMARK 465 LEU A 983 REMARK 465 LYS A 984 REMARK 465 ALA A 985 REMARK 465 TYR A 986 REMARK 465 GLY A 987 REMARK 465 ASN A 988 REMARK 465 GLY A 989 REMARK 465 TYR A 990 REMARK 465 SER A 991 REMARK 465 SER A 992 REMARK 465 ASN A 993 REMARK 465 GLY A 994 REMARK 465 ASN A 995 REMARK 465 THR A 996 REMARK 465 GLY A 997 REMARK 465 GLU A 998 REMARK 465 GLN A 999 REMARK 465 SER A 1000 REMARK 465 GLY A 1001 REMARK 465 ASN A 1002 REMARK 465 MET B -23 REMARK 465 LYS B -22 REMARK 465 THR B -21 REMARK 465 ILE B -20 REMARK 465 ILE B -19 REMARK 465 ALA B -18 REMARK 465 LEU B -17 REMARK 465 SER B -16 REMARK 465 TYR B -15 REMARK 465 ILE B -14 REMARK 465 PHE B -13 REMARK 465 CYS B -12 REMARK 465 LEU B -11 REMARK 465 VAL B -10 REMARK 465 PHE B -9 REMARK 465 ALA B -8 REMARK 465 ASP B -7 REMARK 465 TYR B -6 REMARK 465 LYS B -5 REMARK 465 ASP B -4 REMARK 465 ASP B -3 REMARK 465 ASP B -2 REMARK 465 ASP B -1 REMARK 465 ALA B 0 REMARK 465 MET B 1 REMARK 465 GLY B 2 REMARK 465 GLN B 3 REMARK 465 PRO B 4 REMARK 465 GLY B 5 REMARK 465 ASN B 6 REMARK 465 GLY B 7 REMARK 465 SER B 8 REMARK 465 ALA B 9 REMARK 465 PHE B 10 REMARK 465 LEU B 11 REMARK 465 LEU B 12 REMARK 465 ALA B 13 REMARK 465 PRO B 14 REMARK 465 ASN B 15 REMARK 465 ARG B 16 REMARK 465 SER B 17 REMARK 465 HIS B 18 REMARK 465 ALA B 19 REMARK 465 PRO B 20 REMARK 465 ASP B 21 REMARK 465 HIS B 22 REMARK 465 ASP B 23 REMARK 465 VAL B 24 REMARK 465 THR B 25 REMARK 465 GLN B 26 REMARK 465 GLN B 27 REMARK 465 ARG B 28 REMARK 465 LEU B 230 REMARK 465 TYR B 231 REMARK 465 LYS B 232 REMARK 465 ILE B 233 REMARK 465 ASP B 234 REMARK 465 LYS B 235 REMARK 465 SER B 236 REMARK 465 GLU B 237 REMARK 465 GLY B 238 REMARK 465 ARG B 239 REMARK 465 PHE B 240 REMARK 465 HIS B 241 REMARK 465 VAL B 242 REMARK 465 GLN B 243 REMARK 465 ASN B 244 REMARK 465 LEU B 245 REMARK 465 SER B 246 REMARK 465 GLN B 247 REMARK 465 VAL B 248 REMARK 465 GLU B 249 REMARK 465 GLN B 250 REMARK 465 ASP B 251 REMARK 465 GLY B 252 REMARK 465 ARG B 253 REMARK 465 THR B 254 REMARK 465 GLY B 255 REMARK 465 HIS B 256 REMARK 465 GLY B 257 REMARK 465 LEU B 258 REMARK 465 ARG B 259 REMARK 465 ARG B 260 REMARK 465 SER B 261 REMARK 465 SER B 262 REMARK 465 ARG B 979 REMARK 465 ARG B 980 REMARK 465 SER B 981 REMARK 465 SER B 982 REMARK 465 LEU B 983 REMARK 465 LYS B 984 REMARK 465 ALA B 985 REMARK 465 TYR B 986 REMARK 465 GLY B 987 REMARK 465 ASN B 988 REMARK 465 GLY B 989 REMARK 465 TYR B 990 REMARK 465 SER B 991 REMARK 465 SER B 992 REMARK 465 ASN B 993 REMARK 465 GLY B 994 REMARK 465 ASN B 995 REMARK 465 THR B 996 REMARK 465 GLY B 997 REMARK 465 GLU B 998 REMARK 465 GLN B 999 REMARK 465 SER B 1000 REMARK 465 GLY B 1001 REMARK 465 GLY B 1056 REMARK 465 VAL B 1057 REMARK 465 GLN D 1 REMARK 465 HIS D 121 REMARK 465 HIS D 122 REMARK 465 HIS D 123 REMARK 465 HIS D 124 REMARK 465 HIS D 125 REMARK 465 HIS F 120 REMARK 465 HIS F 121 REMARK 465 HIS F 122 REMARK 465 HIS F 123 REMARK 465 HIS F 124 REMARK 465 HIS F 125 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 ASP A 29 CG OD1 OD2 REMARK 470 GLN A 299 CG CD OE1 NE2 REMARK 470 ASP A 300 CG OD1 OD2 REMARK 470 GLN A1122 CG CD OE1 NE2 REMARK 470 GLN A1123 CG CD OE1 NE2 REMARK 470 ARG A1125 CG CD NE CZ NH1 NH2 REMARK 470 ILE B1027 CG1 CG2 CD1 REMARK 470 LEU B1032 CG CD1 CD2 REMARK 470 ARG B1080 CG CD NE CZ NH1 NH2 REMARK 470 GLN D 13 CG CD OE1 NE2 REMARK 470 LYS D 43 CG CD CE NZ REMARK 470 LYS D 58 CG CD CE NZ REMARK 470 LYS D 64 CG CD CE NZ REMARK 470 LYS D 75 CG CD CE NZ REMARK 470 GLN F 1 CG CD OE1 NE2 REMARK 470 GLN F 3 CG CD OE1 NE2 REMARK 470 GLN F 5 CG CD OE1 NE2 REMARK 470 GLN F 13 CG CD OE1 NE2 REMARK 470 LYS F 58 CG CD CE NZ REMARK 470 LYS F 64 CG CD CE NZ REMARK 470 LYS F 75 CG CD CE NZ REMARK 470 GLN F 111 CG CD OE1 NE2 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 GLN A 65 49.10 -82.56 REMARK 500 VAL A 86 -67.44 -107.96 REMARK 500 SER A 165 -56.52 -133.51 REMARK 500 PHE A 193 62.26 -102.68 REMARK 500 PHE A 208 -65.16 -124.32 REMARK 500 PHE A 264 68.55 63.87 REMARK 500 GLN A 299 -97.83 -84.75 REMARK 500 ALA A1082 -136.11 45.61 REMARK 500 LYS A1124 15.27 58.39 REMARK 500 VAL B 86 -67.66 -124.61 REMARK 500 TYR B 141 0.00 87.37 REMARK 500 PHE B 208 -63.39 -129.37 REMARK 500 CYS B 327 2.61 -69.15 REMARK 500 LYS B1016 -153.87 -116.95 REMARK 500 ILE B1029 58.87 -94.31 REMARK 500 MET B1106 -38.50 -133.69 REMARK 500 SER D 7 146.30 -171.37 REMARK 500 THR D 102 -72.98 -70.58 REMARK 500 VAL F 12 148.31 -171.51 REMARK 500 THR F 102 -74.08 -75.53 REMARK 500 REMARK 500 REMARK: NULL DBREF 8W1V A 1 1001 UNP P07550 ADRB2_HUMAN 1 365 DBREF 8W1V A 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 8W1V B 1 1001 UNP P07550 ADRB2_HUMAN 1 365 DBREF 8W1V B 1002 1161 UNP P00720 ENLYS_BPT4 2 161 DBREF 8W1V D 1 125 PDB 8W1V 8W1V 1 125 DBREF 8W1V F 1 125 PDB 8W1V 8W1V 1 125 SEQADV 8W1V MET A -23 UNP P07550 INITIATING METHIONINE SEQADV 8W1V LYS A -22 UNP P07550 EXPRESSION TAG SEQADV 8W1V THR A -21 UNP P07550 EXPRESSION TAG SEQADV 8W1V ILE A -20 UNP P07550 EXPRESSION TAG SEQADV 8W1V ILE A -19 UNP P07550 EXPRESSION TAG SEQADV 8W1V ALA A -18 UNP P07550 EXPRESSION TAG SEQADV 8W1V LEU A -17 UNP P07550 EXPRESSION TAG SEQADV 8W1V SER A -16 UNP P07550 EXPRESSION TAG SEQADV 8W1V TYR A -15 UNP P07550 EXPRESSION TAG SEQADV 8W1V ILE A -14 UNP P07550 EXPRESSION TAG SEQADV 8W1V PHE A -13 UNP P07550 EXPRESSION TAG SEQADV 8W1V CYS A -12 UNP P07550 EXPRESSION TAG SEQADV 8W1V LEU A -11 UNP P07550 EXPRESSION TAG SEQADV 8W1V VAL A -10 UNP P07550 EXPRESSION TAG SEQADV 8W1V PHE A -9 UNP P07550 EXPRESSION TAG SEQADV 8W1V ALA A -8 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP A -7 UNP P07550 EXPRESSION TAG SEQADV 8W1V TYR A -6 UNP P07550 EXPRESSION TAG SEQADV 8W1V LYS A -5 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP A -4 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP A -3 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP A -2 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP A -1 UNP P07550 EXPRESSION TAG SEQADV 8W1V ALA A 0 UNP P07550 EXPRESSION TAG SEQADV 8W1V ARG A 16 UNP P07550 GLY 16 CONFLICT SEQADV 8W1V GLN A 27 UNP P07550 GLU 27 CONFLICT SEQADV 8W1V GLU A 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 8W1V TYR A 231 UNP P07550 GLN 231 CONFLICT SEQADV 8W1V GLY A 1012 UNP P00720 ARG 12 CONFLICT SEQADV 8W1V THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 8W1V ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 8W1V ARG A 1137 UNP P00720 ILE 137 CONFLICT SEQADV 8W1V MET B -23 UNP P07550 INITIATING METHIONINE SEQADV 8W1V LYS B -22 UNP P07550 EXPRESSION TAG SEQADV 8W1V THR B -21 UNP P07550 EXPRESSION TAG SEQADV 8W1V ILE B -20 UNP P07550 EXPRESSION TAG SEQADV 8W1V ILE B -19 UNP P07550 EXPRESSION TAG SEQADV 8W1V ALA B -18 UNP P07550 EXPRESSION TAG SEQADV 8W1V LEU B -17 UNP P07550 EXPRESSION TAG SEQADV 8W1V SER B -16 UNP P07550 EXPRESSION TAG SEQADV 8W1V TYR B -15 UNP P07550 EXPRESSION TAG SEQADV 8W1V ILE B -14 UNP P07550 EXPRESSION TAG SEQADV 8W1V PHE B -13 UNP P07550 EXPRESSION TAG SEQADV 8W1V CYS B -12 UNP P07550 EXPRESSION TAG SEQADV 8W1V LEU B -11 UNP P07550 EXPRESSION TAG SEQADV 8W1V VAL B -10 UNP P07550 EXPRESSION TAG SEQADV 8W1V PHE B -9 UNP P07550 EXPRESSION TAG SEQADV 8W1V ALA B -8 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP B -7 UNP P07550 EXPRESSION TAG SEQADV 8W1V TYR B -6 UNP P07550 EXPRESSION TAG SEQADV 8W1V LYS B -5 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP B -4 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP B -3 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP B -2 UNP P07550 EXPRESSION TAG SEQADV 8W1V ASP B -1 UNP P07550 EXPRESSION TAG SEQADV 8W1V ALA B 0 UNP P07550 EXPRESSION TAG SEQADV 8W1V ARG B 16 UNP P07550 GLY 16 CONFLICT SEQADV 8W1V GLN B 27 UNP P07550 GLU 27 CONFLICT SEQADV 8W1V GLU B 187 UNP P07550 ASN 187 ENGINEERED MUTATION SEQADV 8W1V TYR B 231 UNP P07550 GLN 231 CONFLICT SEQADV 8W1V GLY B 1012 UNP P00720 ARG 12 CONFLICT SEQADV 8W1V THR B 1054 UNP P00720 CYS 54 ENGINEERED MUTATION SEQADV 8W1V ALA B 1097 UNP P00720 CYS 97 ENGINEERED MUTATION SEQADV 8W1V ARG B 1137 UNP P00720 ILE 137 CONFLICT SEQRES 1 A 549 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 A 549 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLY SEQRES 3 A 549 GLN PRO GLY ASN GLY SER ALA PHE LEU LEU ALA PRO ASN SEQRES 4 A 549 ARG SER HIS ALA PRO ASP HIS ASP VAL THR GLN GLN ARG SEQRES 5 A 549 ASP GLU VAL TRP VAL VAL GLY MET GLY ILE VAL MET SER SEQRES 6 A 549 LEU ILE VAL LEU ALA ILE VAL PHE GLY ASN VAL LEU VAL SEQRES 7 A 549 ILE THR ALA ILE ALA LYS PHE GLU ARG LEU GLN THR VAL SEQRES 8 A 549 THR ASN TYR PHE ILE THR SER LEU ALA CYS ALA ASP LEU SEQRES 9 A 549 VAL MET GLY LEU ALA VAL VAL PRO PHE GLY ALA ALA HIS SEQRES 10 A 549 ILE LEU MET LYS MET TRP THR PHE GLY ASN PHE TRP CYS SEQRES 11 A 549 GLU PHE TRP THR SER ILE ASP VAL LEU CYS VAL THR ALA SEQRES 12 A 549 SER ILE GLU THR LEU CYS VAL ILE ALA VAL ASP ARG TYR SEQRES 13 A 549 PHE ALA ILE THR SER PRO PHE LYS TYR GLN SER LEU LEU SEQRES 14 A 549 THR LYS ASN LYS ALA ARG VAL ILE ILE LEU MET VAL TRP SEQRES 15 A 549 ILE VAL SER GLY LEU THR SER PHE LEU PRO ILE GLN MET SEQRES 16 A 549 HIS TRP TYR ARG ALA THR HIS GLN GLU ALA ILE ASN CYS SEQRES 17 A 549 TYR ALA GLU GLU THR CYS CYS ASP PHE PHE THR ASN GLN SEQRES 18 A 549 ALA TYR ALA ILE ALA SER SER ILE VAL SER PHE TYR VAL SEQRES 19 A 549 PRO LEU VAL ILE MET VAL PHE VAL TYR SER ARG VAL PHE SEQRES 20 A 549 GLN GLU ALA LYS ARG GLN LEU TYR LYS ILE ASP LYS SER SEQRES 21 A 549 GLU GLY ARG PHE HIS VAL GLN ASN LEU SER GLN VAL GLU SEQRES 22 A 549 GLN ASP GLY ARG THR GLY HIS GLY LEU ARG ARG SER SER SEQRES 23 A 549 LYS PHE CYS LEU LYS GLU HIS LYS ALA LEU LYS THR LEU SEQRES 24 A 549 GLY ILE ILE MET GLY THR PHE THR LEU CYS TRP LEU PRO SEQRES 25 A 549 PHE PHE ILE VAL ASN ILE VAL HIS VAL ILE GLN ASP ASN SEQRES 26 A 549 LEU ILE ARG LYS GLU VAL TYR ILE LEU LEU ASN TRP ILE SEQRES 27 A 549 GLY TYR VAL ASN SER GLY PHE ASN PRO LEU ILE TYR CYS SEQRES 28 A 549 ARG SER PRO ASP PHE ARG ILE ALA PHE GLN GLU LEU LEU SEQRES 29 A 549 CYS LEU ARG ARG SER SER LEU LYS ALA TYR GLY ASN GLY SEQRES 30 A 549 TYR SER SER ASN GLY ASN THR GLY GLU GLN SER GLY ASN SEQRES 31 A 549 ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG LEU SEQRES 32 A 549 LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE GLY SEQRES 33 A 549 ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN ALA SEQRES 34 A 549 ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN THR SEQRES 35 A 549 ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU PHE SEQRES 36 A 549 ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG SEQRES 37 A 549 ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP ALA SEQRES 38 A 549 VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN MET SEQRES 39 A 549 GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU ARG SEQRES 40 A 549 MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN SEQRES 41 A 549 LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN ARG SEQRES 42 A 549 ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR TRP SEQRES 43 A 549 ASP ALA TYR SEQRES 1 B 549 MET LYS THR ILE ILE ALA LEU SER TYR ILE PHE CYS LEU SEQRES 2 B 549 VAL PHE ALA ASP TYR LYS ASP ASP ASP ASP ALA MET GLY SEQRES 3 B 549 GLN PRO GLY ASN GLY SER ALA PHE LEU LEU ALA PRO ASN SEQRES 4 B 549 ARG SER HIS ALA PRO ASP HIS ASP VAL THR GLN GLN ARG SEQRES 5 B 549 ASP GLU VAL TRP VAL VAL GLY MET GLY ILE VAL MET SER SEQRES 6 B 549 LEU ILE VAL LEU ALA ILE VAL PHE GLY ASN VAL LEU VAL SEQRES 7 B 549 ILE THR ALA ILE ALA LYS PHE GLU ARG LEU GLN THR VAL SEQRES 8 B 549 THR ASN TYR PHE ILE THR SER LEU ALA CYS ALA ASP LEU SEQRES 9 B 549 VAL MET GLY LEU ALA VAL VAL PRO PHE GLY ALA ALA HIS SEQRES 10 B 549 ILE LEU MET LYS MET TRP THR PHE GLY ASN PHE TRP CYS SEQRES 11 B 549 GLU PHE TRP THR SER ILE ASP VAL LEU CYS VAL THR ALA SEQRES 12 B 549 SER ILE GLU THR LEU CYS VAL ILE ALA VAL ASP ARG TYR SEQRES 13 B 549 PHE ALA ILE THR SER PRO PHE LYS TYR GLN SER LEU LEU SEQRES 14 B 549 THR LYS ASN LYS ALA ARG VAL ILE ILE LEU MET VAL TRP SEQRES 15 B 549 ILE VAL SER GLY LEU THR SER PHE LEU PRO ILE GLN MET SEQRES 16 B 549 HIS TRP TYR ARG ALA THR HIS GLN GLU ALA ILE ASN CYS SEQRES 17 B 549 TYR ALA GLU GLU THR CYS CYS ASP PHE PHE THR ASN GLN SEQRES 18 B 549 ALA TYR ALA ILE ALA SER SER ILE VAL SER PHE TYR VAL SEQRES 19 B 549 PRO LEU VAL ILE MET VAL PHE VAL TYR SER ARG VAL PHE SEQRES 20 B 549 GLN GLU ALA LYS ARG GLN LEU TYR LYS ILE ASP LYS SER SEQRES 21 B 549 GLU GLY ARG PHE HIS VAL GLN ASN LEU SER GLN VAL GLU SEQRES 22 B 549 GLN ASP GLY ARG THR GLY HIS GLY LEU ARG ARG SER SER SEQRES 23 B 549 LYS PHE CYS LEU LYS GLU HIS LYS ALA LEU LYS THR LEU SEQRES 24 B 549 GLY ILE ILE MET GLY THR PHE THR LEU CYS TRP LEU PRO SEQRES 25 B 549 PHE PHE ILE VAL ASN ILE VAL HIS VAL ILE GLN ASP ASN SEQRES 26 B 549 LEU ILE ARG LYS GLU VAL TYR ILE LEU LEU ASN TRP ILE SEQRES 27 B 549 GLY TYR VAL ASN SER GLY PHE ASN PRO LEU ILE TYR CYS SEQRES 28 B 549 ARG SER PRO ASP PHE ARG ILE ALA PHE GLN GLU LEU LEU SEQRES 29 B 549 CYS LEU ARG ARG SER SER LEU LYS ALA TYR GLY ASN GLY SEQRES 30 B 549 TYR SER SER ASN GLY ASN THR GLY GLU GLN SER GLY ASN SEQRES 31 B 549 ILE PHE GLU MET LEU ARG ILE ASP GLU GLY LEU ARG LEU SEQRES 32 B 549 LYS ILE TYR LYS ASP THR GLU GLY TYR TYR THR ILE GLY SEQRES 33 B 549 ILE GLY HIS LEU LEU THR LYS SER PRO SER LEU ASN ALA SEQRES 34 B 549 ALA LYS SER GLU LEU ASP LYS ALA ILE GLY ARG ASN THR SEQRES 35 B 549 ASN GLY VAL ILE THR LYS ASP GLU ALA GLU LYS LEU PHE SEQRES 36 B 549 ASN GLN ASP VAL ASP ALA ALA VAL ARG GLY ILE LEU ARG SEQRES 37 B 549 ASN ALA LYS LEU LYS PRO VAL TYR ASP SER LEU ASP ALA SEQRES 38 B 549 VAL ARG ARG ALA ALA LEU ILE ASN MET VAL PHE GLN MET SEQRES 39 B 549 GLY GLU THR GLY VAL ALA GLY PHE THR ASN SER LEU ARG SEQRES 40 B 549 MET LEU GLN GLN LYS ARG TRP ASP GLU ALA ALA VAL ASN SEQRES 41 B 549 LEU ALA LYS SER ARG TRP TYR ASN GLN THR PRO ASN ARG SEQRES 42 B 549 ALA LYS ARG VAL ILE THR THR PHE ARG THR GLY THR TRP SEQRES 43 B 549 ASP ALA TYR SEQRES 1 D 125 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 D 125 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 D 125 SER ILE PHE SER LEU ASN ASP MET GLY TRP TYR ARG GLN SEQRES 4 D 125 ALA PRO GLY LYS LEU ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 D 125 SER GLY GLY SER THR LYS TYR ALA ASP SER VAL LYS GLY SEQRES 6 D 125 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 D 125 TYR LEU GLN MET ASN SER LEU LYS ALA GLU ASP THR ALA SEQRES 8 D 125 VAL TYR TYR CYS ASN ALA LYS VAL ALA GLY THR PHE SER SEQRES 9 D 125 ILE TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 10 D 125 SER SER HIS HIS HIS HIS HIS HIS SEQRES 1 F 125 GLN VAL GLN LEU GLN GLU SER GLY GLY GLY LEU VAL GLN SEQRES 2 F 125 ALA GLY GLY SER LEU ARG LEU SER CYS ALA ALA SER GLY SEQRES 3 F 125 SER ILE PHE SER LEU ASN ASP MET GLY TRP TYR ARG GLN SEQRES 4 F 125 ALA PRO GLY LYS LEU ARG GLU LEU VAL ALA ALA ILE THR SEQRES 5 F 125 SER GLY GLY SER THR LYS TYR ALA ASP SER VAL LYS GLY SEQRES 6 F 125 ARG PHE THR ILE SER ARG ASP ASN ALA LYS ASN THR VAL SEQRES 7 F 125 TYR LEU GLN MET ASN SER LEU LYS ALA GLU ASP THR ALA SEQRES 8 F 125 VAL TYR TYR CYS ASN ALA LYS VAL ALA GLY THR PHE SER SEQRES 9 F 125 ILE TYR ASP TYR TRP GLY GLN GLY THR GLN VAL THR VAL SEQRES 10 F 125 SER SER HIS HIS HIS HIS HIS HIS HET AE2 A1201 42 HET AE2 B1201 42 HET AV0 B1202 69 HETNAM AV0 2-DECYL-2-{[(4-O-ALPHA-D-GLUCOPYRANOSYL-BETA-D- HETNAM 2 AV0 GLUCOPYRANOSYL)OXY]METHYL}DODECYL 4-O-ALPHA-D- HETNAM 3 AV0 GLUCOPYRANOSYL-BETA-D-GLUCOPYRANOSIDE HETSYN AV0 2,2-DIDECYLPROPANE-1,3-BIS-B-D-MALTOPYRANOSIDE FORMUL 5 AE2 FORMUL 7 AV0 C47 H88 O22 HELIX 1 AA1 GLU A 30 PHE A 61 1 32 HELIX 2 AA2 GLU A 62 GLN A 65 5 4 HELIX 3 AA3 THR A 66 VAL A 86 1 21 HELIX 4 AA4 VAL A 86 LYS A 97 1 12 HELIX 5 AA5 PHE A 101 ILE A 135 1 35 HELIX 6 AA6 THR A 146 THR A 164 1 19 HELIX 7 AA7 SER A 165 MET A 171 1 7 HELIX 8 AA8 HIS A 178 GLU A 187 1 10 HELIX 9 AA9 ASN A 196 PHE A 208 1 13 HELIX 10 AB1 PHE A 208 GLN A 229 1 22 HELIX 11 AB2 LEU A 266 GLN A 299 1 34 HELIX 12 AB3 ARG A 304 ASN A 318 1 15 HELIX 13 AB4 PHE A 321 TYR A 326 1 6 HELIX 14 AB5 SER A 329 LEU A 340 1 12 HELIX 15 AB6 PHE A 1004 GLY A 1012 1 9 HELIX 16 AB7 SER A 1038 GLY A 1051 1 14 HELIX 17 AB8 THR A 1059 ARG A 1080 1 22 HELIX 18 AB9 ASN A 1081 LEU A 1084 5 4 HELIX 19 AC1 LYS A 1085 LEU A 1091 1 7 HELIX 20 AC2 ASP A 1092 VAL A 1111 1 20 HELIX 21 AC3 PHE A 1114 GLN A 1123 1 10 HELIX 22 AC4 ARG A 1125 LEU A 1133 1 9 HELIX 23 AC5 SER A 1136 THR A 1142 1 7 HELIX 24 AC6 THR A 1142 THR A 1155 1 14 HELIX 25 AC7 GLU B 30 PHE B 61 1 32 HELIX 26 AC8 GLU B 62 GLN B 65 5 4 HELIX 27 AC9 THR B 66 VAL B 86 1 21 HELIX 28 AD1 VAL B 86 MET B 96 1 11 HELIX 29 AD2 PHE B 101 THR B 136 1 36 HELIX 30 AD3 THR B 146 MET B 171 1 26 HELIX 31 AD4 HIS B 178 GLU B 187 1 10 HELIX 32 AD5 ASN B 196 SER B 207 1 12 HELIX 33 AD6 PHE B 208 GLN B 229 1 22 HELIX 34 AD7 LEU B 266 GLN B 299 1 34 HELIX 35 AD8 ARG B 304 ASN B 318 1 15 HELIX 36 AD9 GLY B 320 TYR B 326 1 7 HELIX 37 AE1 SER B 329 LEU B 340 1 12 HELIX 38 AE2 ILE B 1003 GLY B 1012 1 10 HELIX 39 AE3 SER B 1038 GLY B 1051 1 14 HELIX 40 AE4 THR B 1059 ARG B 1080 1 22 HELIX 41 AE5 LEU B 1084 LEU B 1091 1 8 HELIX 42 AE6 ASP B 1092 GLY B 1107 1 16 HELIX 43 AE7 GLY B 1107 ALA B 1112 1 6 HELIX 44 AE8 PHE B 1114 GLN B 1123 1 10 HELIX 45 AE9 ARG B 1125 ALA B 1134 1 10 HELIX 46 AF1 ARG B 1137 THR B 1142 1 6 HELIX 47 AF2 THR B 1142 GLY B 1156 1 15 HELIX 48 AF3 ILE D 28 ASN D 32 5 5 HELIX 49 AF4 ASP D 61 LYS D 64 5 4 HELIX 50 AF5 LYS D 86 THR D 90 5 5 HELIX 51 AF6 ILE F 28 ASN F 32 5 5 HELIX 52 AF7 ASP F 61 LYS F 64 5 4 HELIX 53 AF8 LYS F 86 THR F 90 5 5 SHEET 1 AA1 3 ARG A1014 LYS A1019 0 SHEET 2 AA1 3 TYR A1025 GLY A1028 -1 O THR A1026 N TYR A1018 SHEET 3 AA1 3 HIS A1031 THR A1034 -1 O LEU A1033 N TYR A1025 SHEET 1 AA2 3 TYR B1018 LYS B1019 0 SHEET 2 AA2 3 TYR B1025 ILE B1027 -1 O THR B1026 N TYR B1018 SHEET 3 AA2 3 HIS B1031 LEU B1032 -1 O HIS B1031 N ILE B1027 SHEET 1 AA3 4 GLN D 3 SER D 7 0 SHEET 2 AA3 4 SER D 17 SER D 25 -1 O SER D 21 N SER D 7 SHEET 3 AA3 4 THR D 77 ASN D 83 -1 O MET D 82 N LEU D 18 SHEET 4 AA3 4 PHE D 67 ASP D 72 -1 N SER D 70 O TYR D 79 SHEET 1 AA4 6 LEU D 11 GLN D 13 0 SHEET 2 AA4 6 THR D 113 SER D 118 1 O SER D 118 N VAL D 12 SHEET 3 AA4 6 ALA D 91 ALA D 100 -1 N TYR D 93 O THR D 113 SHEET 4 AA4 6 ASP D 33 GLN D 39 -1 N TYR D 37 O TYR D 94 SHEET 5 AA4 6 GLU D 46 ILE D 51 -1 O ILE D 51 N MET D 34 SHEET 6 AA4 6 THR D 57 TYR D 59 -1 O LYS D 58 N ALA D 50 SHEET 1 AA5 4 LEU D 11 GLN D 13 0 SHEET 2 AA5 4 THR D 113 SER D 118 1 O SER D 118 N VAL D 12 SHEET 3 AA5 4 ALA D 91 ALA D 100 -1 N TYR D 93 O THR D 113 SHEET 4 AA5 4 ILE D 105 TRP D 109 -1 O TYR D 108 N ALA D 97 SHEET 1 AA6 4 GLN F 3 SER F 7 0 SHEET 2 AA6 4 LEU F 18 SER F 25 -1 O SER F 25 N GLN F 3 SHEET 3 AA6 4 THR F 77 MET F 82 -1 O LEU F 80 N LEU F 20 SHEET 4 AA6 4 PHE F 67 ASP F 72 -1 N SER F 70 O TYR F 79 SHEET 1 AA7 6 GLY F 10 GLN F 13 0 SHEET 2 AA7 6 THR F 113 SER F 118 1 O THR F 116 N GLY F 10 SHEET 3 AA7 6 ALA F 91 ALA F 100 -1 N TYR F 93 O THR F 113 SHEET 4 AA7 6 ASP F 33 GLN F 39 -1 N TYR F 37 O TYR F 94 SHEET 5 AA7 6 GLU F 46 ILE F 51 -1 O ILE F 51 N MET F 34 SHEET 6 AA7 6 THR F 57 TYR F 59 -1 O LYS F 58 N ALA F 50 SHEET 1 AA8 4 GLY F 10 GLN F 13 0 SHEET 2 AA8 4 THR F 113 SER F 118 1 O THR F 116 N GLY F 10 SHEET 3 AA8 4 ALA F 91 ALA F 100 -1 N TYR F 93 O THR F 113 SHEET 4 AA8 4 ILE F 105 TRP F 109 -1 O TYR F 106 N VAL F 99 SSBOND 1 CYS A 106 CYS A 191 1555 1555 2.03 SSBOND 2 CYS A 184 CYS A 190 1555 1555 2.04 SSBOND 3 CYS B 106 CYS B 191 1555 1555 2.03 SSBOND 4 CYS B 184 CYS B 190 1555 1555 2.03 SSBOND 5 CYS D 22 CYS D 95 1555 1555 2.03 SSBOND 6 CYS F 22 CYS F 95 1555 1555 2.04 CRYST1 73.680 146.770 91.830 90.00 107.06 90.00 P 1 21 1 4 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 0.013572 0.000000 0.004165 0.00000 SCALE2 0.000000 0.006813 0.000000 0.00000 SCALE3 0.000000 0.000000 0.011391 0.00000