HEADER MEMBRANE PROTEIN 27-JUL-17 5OLG
TITLE STRUCTURE OF THE A2A-STAR2-BRIL562-ZM241385 COMPLEX AT 1.86A OBTAINED
TITLE 2 FROM IN MESO SOAKING EXPERIMENTS.
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A,SOLUBLE CYTOCHROME B562,ADENOSINE
COMPND 3 RECEPTOR A2A;
COMPND 4 CHAIN: A;
COMPND 5 SYNONYM: CYTOCHROME B-562;
COMPND 6 ENGINEERED: YES;
COMPND 7 MUTATION: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ESCHERICHIA COLI;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 562;
SOURCE 5 GENE: ADORA2A, ADORA2, CYBC;
SOURCE 6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7111;
SOURCE 9 EXPRESSION_SYSTEM_VECTOR_TYPE: VIRUS
KEYWDS G-PROTEIN COUPLED RECEPTOR, ADENOSINE 2A RECEPTOR, 7 TM INTEGRAL
KEYWDS 2 MEMBRANE PROTEIN, THERMOSTABILIZING MUTATIONS, MEMBRANE PROTEINS,
KEYWDS 3 MEMBRANE PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN,R.COOKE,
AUTHOR 2 F.H.MARSHALL,A.S.DORE
REVDAT 2 07-FEB-24 5OLG 1 REMARK
REVDAT 1 17-JAN-18 5OLG 0
JRNL AUTH P.RUCKTOOA,R.K.Y.CHENG,E.SEGALA,T.GENG,J.C.ERREY,G.A.BROWN,
JRNL AUTH 2 R.M.COOKE,F.H.MARSHALL,A.S.DORE
JRNL TITL TOWARDS HIGH THROUGHPUT GPCR CRYSTALLOGRAPHY: IN MESO
JRNL TITL 2 SOAKING OF ADENOSINE A2A RECEPTOR CRYSTALS.
JRNL REF SCI REP V. 8 41 2018
JRNL REFN ESSN 2045-2322
JRNL PMID 29311713
JRNL DOI 10.1038/S41598-017-18570-W
REMARK 2
REMARK 2 RESOLUTION. 1.87 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (1.12RC2_2821)
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 : NULL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 1.87
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 41.31
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 97.7
REMARK 3 NUMBER OF REFLECTIONS : 41376
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.191
REMARK 3 R VALUE (WORKING SET) : 0.189
REMARK 3 FREE R VALUE : 0.224
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.000
REMARK 3 FREE R VALUE TEST SET COUNT : 3894
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 1.9320 - 1.8650 1.00 3701 200 0.4834 0.5144
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : NULL
REMARK 3 SOLVENT RADIUS : 1.11
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) : 0.250
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 23.670
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 24.36
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 38.73
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 : 0.012 3703
REMARK 3 ANGLE : 1.447 4946
REMARK 3 CHIRALITY : 0.070 551
REMARK 3 PLANARITY : 0.006 590
REMARK 3 DIHEDRAL : 16.617 2276
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): -22.1678 -7.0563 17.6583
REMARK 3 T TENSOR
REMARK 3 T11: 0.1778 T22: 0.1859
REMARK 3 T33: 0.1615 T12: -0.0024
REMARK 3 T13: 0.0031 T23: 0.0064
REMARK 3 L TENSOR
REMARK 3 L11: 0.6759 L22: 0.6691
REMARK 3 L33: 0.8208 L12: 0.0955
REMARK 3 L13: 0.1973 L23: 0.0123
REMARK 3 S TENSOR
REMARK 3 S11: 0.0198 S12: -0.0048 S13: -0.0381
REMARK 3 S21: -0.0743 S22: -0.0088 S23: -0.0320
REMARK 3 S31: 0.0917 S32: -0.0559 S33: -0.0000
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): 0.1168 -54.5611 19.9519
REMARK 3 T TENSOR
REMARK 3 T11: 0.4054 T22: 0.3022
REMARK 3 T33: 0.6749 T12: 0.0712
REMARK 3 T13: -0.0124 T23: -0.0261
REMARK 3 L TENSOR
REMARK 3 L11: 0.0770 L22: 0.1943
REMARK 3 L33: 0.2107 L12: -0.0034
REMARK 3 L13: -0.0721 L23: -0.0953
REMARK 3 S TENSOR
REMARK 3 S11: 0.0456 S12: -0.2658 S13: 0.3529
REMARK 3 S21: -0.2942 S22: 0.0507 S23: -0.1541
REMARK 3 S31: 0.1564 S32: 0.1043 S33: 0.0007
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 5OLG COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 27-JUL-17.
REMARK 100 THE DEPOSITION ID IS D_1200005995.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 17-MAY-17
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.3-5.4
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : SLS
REMARK 200 BEAMLINE : X06SA
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS EIGER X 16M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 42870
REMARK 200 RESOLUTION RANGE HIGH (A) : 1.850
REMARK 200 RESOLUTION RANGE LOW (A) : 46.530
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 98.6
REMARK 200 DATA REDUNDANCY : 6.200
REMARK 200 R MERGE (I) : 0.15700
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 7.7000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.85
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 1.89
REMARK 200 COMPLETENESS FOR SHELL (%) : 100.0
REMARK 200 DATA REDUNDANCY IN SHELL : 6.40
REMARK 200 R MERGE FOR SHELL (I) : 2.19700
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> 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: PHASER
REMARK 200 STARTING MODEL: 5MZJ
REMARK 200
REMARK 200 REMARK: 0.060-0.080 MM LONG PLATE-SHAPED CRYSTALS
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 41.75
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.11
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: CRYSTAL GROWTH: 0.L M TRI-SODIUM
REMARK 280 CITRATE PH 5.3-5.4, 0.05 M SODIUM THIOCYANATE, 29-32% PEG400, 2%
REMARK 280 (V/V) 2,5-HEXANEDIOL, 0.5 MM THEOPHYLLINE. ZM241385 WAS
REMARK 280 SUBSEQUENTLY ADDED TO MOTHERLIQUOR FOR THE SOAKING EXPERIMENT AT
REMARK 280 A FINAL CONCENTRATION OF 0.005 MM., LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293.15K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,-Y,Z+1/2
REMARK 290 3555 -X,Y,-Z+1/2
REMARK 290 4555 X,-Y,-Z
REMARK 290 5555 X+1/2,Y+1/2,Z
REMARK 290 6555 -X+1/2,-Y+1/2,Z+1/2
REMARK 290 7555 -X+1/2,Y+1/2,-Z+1/2
REMARK 290 8555 X+1/2,-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 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 69.80000
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 0.00000
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 69.80000
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290 SMTRY1 5 1.000000 0.000000 0.000000 19.72500
REMARK 290 SMTRY2 5 0.000000 1.000000 0.000000 89.69650
REMARK 290 SMTRY3 5 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 6 -1.000000 0.000000 0.000000 19.72500
REMARK 290 SMTRY2 6 0.000000 -1.000000 0.000000 89.69650
REMARK 290 SMTRY3 6 0.000000 0.000000 1.000000 69.80000
REMARK 290 SMTRY1 7 -1.000000 0.000000 0.000000 19.72500
REMARK 290 SMTRY2 7 0.000000 1.000000 0.000000 89.69650
REMARK 290 SMTRY3 7 0.000000 0.000000 -1.000000 69.80000
REMARK 290 SMTRY1 8 1.000000 0.000000 0.000000 19.72500
REMARK 290 SMTRY2 8 0.000000 -1.000000 0.000000 89.69650
REMARK 290 SMTRY3 8 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: MONOMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 12190 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 21210 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 ALA A -9
REMARK 465 ASP A -8
REMARK 465 TYR A -7
REMARK 465 LYS A -6
REMARK 465 ASP A -5
REMARK 465 ASP A -4
REMARK 465 ASP A -3
REMARK 465 ASP A -2
REMARK 465 ALA A 1043
REMARK 465 THR A 1044
REMARK 465 PRO A 1045
REMARK 465 PRO A 1046
REMARK 465 LYS A 1047
REMARK 465 LEU A 1048
REMARK 465 GLU A 1049
REMARK 465 ASP A 1050
REMARK 465 LYS A 1051
REMARK 465 SER A 1052
REMARK 465 PRO A 1053
REMARK 465 ASP A 1054
REMARK 465 SER A 1055
REMARK 465 HIS A 306
REMARK 465 VAL A 307
REMARK 465 LEU A 308
REMARK 465 ARG A 309
REMARK 465 GLN A 310
REMARK 465 GLN A 311
REMARK 465 GLU A 312
REMARK 465 PRO A 313
REMARK 465 PHE A 314
REMARK 465 LYS A 315
REMARK 465 ALA A 316
REMARK 465 ALA A 317
REMARK 465 ALA A 318
REMARK 465 HIS A 319
REMARK 465 HIS A 320
REMARK 465 HIS A 321
REMARK 465 HIS A 322
REMARK 465 HIS A 323
REMARK 465 HIS A 324
REMARK 465 HIS A 325
REMARK 465 HIS A 326
REMARK 465 HIS A 327
REMARK 465 HIS A 328
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 CG ARG A 293 C14 OLA A 1221 1.84
REMARK 500 O2 OLA A 1221 O HOH A 1301 2.06
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 LEU A 58 -53.67 -120.22
REMARK 500 TYR A1101 -54.01 -129.07
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 LEU A 208 -10.14
REMARK 500
REMARK 500 REMARK: NULL
REMARK 610
REMARK 610 MISSING HETEROATOM
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;
REMARK 610 I=INSERTION CODE):
REMARK 610 M RES C SSEQI
REMARK 610 OLA A 1214
REMARK 610 OLA A 1218
REMARK 610 OLA A 1222
REMARK 610 OLC A 1228
REMARK 620
REMARK 620 METAL COORDINATION
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):
REMARK 620
REMARK 620 COORDINATION ANGLES FOR: M RES CSSEQI METAL
REMARK 620 NA A1231 NA
REMARK 620 N RES CSSEQI ATOM
REMARK 620 1 ASP A 52 OD1
REMARK 620 2 SER A 91 OG 123.1
REMARK 620 3 HOH A1349 O 99.2 119.1
REMARK 620 4 HOH A1375 O 79.1 65.4 85.0
REMARK 620 N 1 2 3
REMARK 800
REMARK 800 SITE
REMARK 800 SITE_IDENTIFIER: AC1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue ZMA A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1202
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1203
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1204
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CLR A 1205
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1206
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1207
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1208
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1209
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1210
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1211
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1212
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1213
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1214
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1215
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1216
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1217
REMARK 800
REMARK 800 SITE_IDENTIFIER: AD9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1218
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1219
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1220
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1221
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLA A 1222
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE5
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1223
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE6
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1224
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE7
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1225
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE8
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue SCN A 1226
REMARK 800
REMARK 800 SITE_IDENTIFIER: AE9
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1227
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF1
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1228
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue OLC A 1229
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF3
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue CIT A 1230
REMARK 800
REMARK 800 SITE_IDENTIFIER: AF4
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 1231
DBREF 5OLG A 2 208 UNP P29274 AA2AR_HUMAN 2 208
DBREF 5OLG A 1001 1105 UNP P0ABE7 C562_ECOLX 23 127
DBREF 5OLG A 219 317 UNP P29274 AA2AR_HUMAN 219 317
SEQADV 5OLG ALA A -9 UNP P29274 EXPRESSION TAG
SEQADV 5OLG ASP A -8 UNP P29274 EXPRESSION TAG
SEQADV 5OLG TYR A -7 UNP P29274 EXPRESSION TAG
SEQADV 5OLG LYS A -6 UNP P29274 EXPRESSION TAG
SEQADV 5OLG ASP A -5 UNP P29274 EXPRESSION TAG
SEQADV 5OLG ASP A -4 UNP P29274 EXPRESSION TAG
SEQADV 5OLG ASP A -3 UNP P29274 EXPRESSION TAG
SEQADV 5OLG ASP A -2 UNP P29274 EXPRESSION TAG
SEQADV 5OLG GLY A -1 UNP P29274 EXPRESSION TAG
SEQADV 5OLG ALA A 0 UNP P29274 EXPRESSION TAG
SEQADV 5OLG PRO A 1 UNP P29274 EXPRESSION TAG
SEQADV 5OLG LEU A 54 UNP P29274 ALA 54 ENGINEERED MUTATION
SEQADV 5OLG ALA A 88 UNP P29274 THR 88 ENGINEERED MUTATION
SEQADV 5OLG ALA A 107 UNP P29274 ARG 107 ENGINEERED MUTATION
SEQADV 5OLG ALA A 122 UNP P29274 LYS 122 ENGINEERED MUTATION
SEQADV 5OLG ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 5OLG ALA A 202 UNP P29274 LEU 202 ENGINEERED MUTATION
SEQADV 5OLG TRP A 1007 UNP P0ABE7 MET 29 ENGINEERED MUTATION
SEQADV 5OLG ILE A 1102 UNP P0ABE7 HIS 124 CONFLICT
SEQADV 5OLG LEU A 1106 UNP P0ABE7 LINKER
SEQADV 5OLG ALA A 235 UNP P29274 LEU 235 ENGINEERED MUTATION
SEQADV 5OLG ALA A 239 UNP P29274 VAL 239 ENGINEERED MUTATION
SEQADV 5OLG ALA A 277 UNP P29274 SER 277 ENGINEERED MUTATION
SEQADV 5OLG ALA A 318 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 326 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 327 UNP P29274 EXPRESSION TAG
SEQADV 5OLG HIS A 328 UNP P29274 EXPRESSION TAG
SEQRES 1 A 434 ALA ASP TYR LYS ASP ASP ASP ASP GLY ALA PRO PRO ILE
SEQRES 2 A 434 MET GLY SER SER VAL TYR ILE THR VAL GLU LEU ALA ILE
SEQRES 3 A 434 ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU VAL CYS TRP
SEQRES 4 A 434 ALA VAL TRP LEU ASN SER ASN LEU GLN ASN VAL THR ASN
SEQRES 5 A 434 TYR PHE VAL VAL SER LEU ALA ALA ALA ASP ILE LEU VAL
SEQRES 6 A 434 GLY VAL LEU ALA ILE PRO PHE ALA ILE THR ILE SER THR
SEQRES 7 A 434 GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU PHE ILE ALA
SEQRES 8 A 434 CYS PHE VAL LEU VAL LEU ALA GLN SER SER ILE PHE SER
SEQRES 9 A 434 LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE ALA ILE ALA
SEQRES 10 A 434 ILE PRO LEU ARG TYR ASN GLY LEU VAL THR GLY THR ARG
SEQRES 11 A 434 ALA ALA GLY ILE ILE ALA ILE CYS TRP VAL LEU SER PHE
SEQRES 12 A 434 ALA ILE GLY LEU THR PRO MET LEU GLY TRP ASN ASN CYS
SEQRES 13 A 434 GLY GLN PRO LYS GLU GLY LYS ALA HIS SER GLN GLY CYS
SEQRES 14 A 434 GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU ASP VAL VAL
SEQRES 15 A 434 PRO MET ASN TYR MET VAL TYR PHE ASN PHE PHE ALA CYS
SEQRES 16 A 434 VAL LEU VAL PRO LEU LEU LEU MET LEU GLY VAL TYR LEU
SEQRES 17 A 434 ARG ILE PHE ALA ALA ALA ARG ARG GLN LEU ALA ASP LEU
SEQRES 18 A 434 GLU ASP ASN TRP GLU THR LEU ASN ASP ASN LEU LYS VAL
SEQRES 19 A 434 ILE GLU LYS ALA ASP ASN ALA ALA GLN VAL LYS ASP ALA
SEQRES 20 A 434 LEU THR LYS MET ARG ALA ALA ALA LEU ASP ALA GLN LYS
SEQRES 21 A 434 ALA THR PRO PRO LYS LEU GLU ASP LYS SER PRO ASP SER
SEQRES 22 A 434 PRO GLU MET LYS ASP PHE ARG HIS GLY PHE ASP ILE LEU
SEQRES 23 A 434 VAL GLY GLN ILE ASP ASP ALA LEU LYS LEU ALA ASN GLU
SEQRES 24 A 434 GLY LYS VAL LYS GLU ALA GLN ALA ALA ALA GLU GLN LEU
SEQRES 25 A 434 LYS THR THR ARG ASN ALA TYR ILE GLN LYS TYR LEU GLU
SEQRES 26 A 434 ARG ALA ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA
SEQRES 27 A 434 LYS SER ALA ALA ILE ILE ALA GLY LEU PHE ALA LEU CYS
SEQRES 28 A 434 TRP LEU PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE
SEQRES 29 A 434 CYS PRO ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR
SEQRES 30 A 434 LEU ALA ILE VAL LEU ALA HIS THR ASN SER VAL VAL ASN
SEQRES 31 A 434 PRO PHE ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN
SEQRES 32 A 434 THR PHE ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN
SEQRES 33 A 434 GLN GLU PRO PHE LYS ALA ALA ALA HIS HIS HIS HIS HIS
SEQRES 34 A 434 HIS HIS HIS HIS HIS
HET ZMA A1201 25
HET CLR A1202 28
HET CLR A1203 28
HET CLR A1204 28
HET CLR A1205 28
HET OLA A1206 20
HET OLA A1207 20
HET OLA A1208 20
HET OLA A1209 20
HET OLA A1210 20
HET OLA A1211 20
HET OLA A1212 20
HET OLA A1213 20
HET OLA A1214 11
HET OLA A1215 20
HET OLA A1216 20
HET OLA A1217 20
HET OLA A1218 15
HET OLA A1219 20
HET OLA A1220 20
HET OLA A1221 20
HET OLA A1222 6
HET SCN A1223 3
HET SCN A1224 3
HET SCN A1225 3
HET SCN A1226 3
HET OLC A1227 25
HET OLC A1228 9
HET OLC A1229 25
HET CIT A1230 13
HET NA A1231 1
HETNAM ZMA 4-{2-[(7-AMINO-2-FURAN-2-YL[1,2,4]TRIAZOLO[1,5-A][1,3,
HETNAM 2 ZMA 5]TRIAZIN-5-YL)AMINO]ETHYL}PHENOL
HETNAM CLR CHOLESTEROL
HETNAM OLA OLEIC ACID
HETNAM SCN THIOCYANATE ION
HETNAM OLC (2R)-2,3-DIHYDROXYPROPYL (9Z)-OCTADEC-9-ENOATE
HETNAM CIT CITRIC ACID
HETNAM NA SODIUM ION
HETSYN OLC 1-OLEOYL-R-GLYCEROL
FORMUL 2 ZMA C16 H15 N7 O2
FORMUL 3 CLR 4(C27 H46 O)
FORMUL 7 OLA 17(C18 H34 O2)
FORMUL 24 SCN 4(C N S 1-)
FORMUL 28 OLC 3(C21 H40 O4)
FORMUL 31 CIT C6 H8 O7
FORMUL 32 NA NA 1+
FORMUL 33 HOH *88(H2 O)
HELIX 1 AA1 PRO A 1 ASN A 34 1 34
HELIX 2 AA2 SER A 35 GLN A 38 5 4
HELIX 3 AA3 ASN A 39 LEU A 58 1 20
HELIX 4 AA4 LEU A 58 THR A 68 1 11
HELIX 5 AA5 CYS A 74 ILE A 108 1 35
HELIX 6 AA6 ILE A 108 VAL A 116 1 9
HELIX 7 AA7 THR A 117 LEU A 137 1 21
HELIX 8 AA8 THR A 138 GLY A 142 5 5
HELIX 9 AA9 LYS A 150 GLN A 157 1 8
HELIX 10 AB1 LEU A 167 VAL A 172 1 6
HELIX 11 AB2 PRO A 173 PHE A 180 1 8
HELIX 12 AB3 VAL A 186 LYS A 1019 1 42
HELIX 13 AB4 ASN A 1022 GLN A 1041 1 20
HELIX 14 AB5 GLU A 1057 GLU A 1081 1 25
HELIX 15 AB6 LYS A 1083 GLN A 1093 1 11
HELIX 16 AB7 GLN A 1093 TYR A 1101 1 9
HELIX 17 AB8 TYR A 1101 CYS A 259 1 47
HELIX 18 AB9 PRO A 266 ILE A 292 1 27
HELIX 19 AC1 ILE A 292 SER A 305 1 14
SHEET 1 AA1 2 CYS A 71 ALA A 73 0
SHEET 2 AA1 2 GLN A 163 ALA A 165 -1 O VAL A 164 N ALA A 72
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.05
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.01
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.04
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
LINK OD1 ASP A 52 NA NA A1231 1555 1555 2.42
LINK OG SER A 91 NA NA A1231 1555 1555 2.57
LINK NA NA A1231 O HOH A1349 1555 1555 2.75
LINK NA NA A1231 O HOH A1375 1555 1555 2.93
SITE 1 AC1 14 LEU A 85 PHE A 168 GLU A 169 MET A 177
SITE 2 AC1 14 TRP A 246 LEU A 249 HIS A 250 ASN A 253
SITE 3 AC1 14 MET A 270 ILE A 274 HOH A1322 HOH A1356
SITE 4 AC1 14 HOH A1357 HOH A1373
SITE 1 AC2 9 ALA A 72 ALA A 73 GLY A 76 ILE A 80
SITE 2 AC2 9 CLR A1204 OLA A1207 OLA A1209 OLA A1211
SITE 3 AC2 9 HOH A1313
SITE 1 AC3 6 LEU A 247 CYS A 262 SER A 263 OLA A1208
SITE 2 AC3 6 OLA A1218 OLA A1219
SITE 1 AC4 7 PHE A 255 PHE A 258 CLR A1202 OLA A1207
SITE 2 AC4 7 OLA A1208 OLA A1209 HOH A1354
SITE 1 AC5 4 TRP A 268 OLA A1215 OLA A1218 OLC A1229
SITE 1 AC6 6 THR A 65 PHE A 70 CYS A 71 OLA A1207
SITE 2 AC6 6 OLA A1208 OLA A1220
SITE 1 AC7 12 LEU A 58 PRO A 61 THR A 65 PHE A 70
SITE 2 AC7 12 CYS A 71 GLN A 163 ASP A 261 CLR A1202
SITE 3 AC7 12 CLR A1204 OLA A1206 OLA A1208 HOH A1313
SITE 1 AC8 9 PHE A 255 ASP A 261 CYS A 262 CLR A1203
SITE 2 AC8 9 CLR A1204 OLA A1206 OLA A1207 OLA A1219
SITE 3 AC8 9 HOH A1377
SITE 1 AC9 6 PHE A 258 CLR A1202 CLR A1204 OLA A1210
SITE 2 AC9 6 OLA A1216 HOH A1313
SITE 1 AD1 4 VAL A 31 TRP A 32 ALA A 50 OLA A1209
SITE 1 AD2 6 TYR A 43 LEU A 54 LEU A 58 TRP A 129
SITE 2 AD2 6 CLR A1202 OLC A1227
SITE 1 AD3 7 MET A 140 LEU A 141 TYR A 179 ALA A 184
SITE 2 AD3 7 OLA A1216 OLC A1227 HOH A1320
SITE 1 AD4 5 TRP A 29 TRP A 32 LEU A 194 LYS A 233
SITE 2 AD4 5 ALA A 236
SITE 1 AD5 6 VAL A 40 PHE A 44 PHE A 93 LEU A 96
SITE 2 AD5 6 ASP A 101 VAL A 116
SITE 1 AD6 8 GLY A 5 SER A 6 LEU A 267 TYR A 271
SITE 2 AD6 8 VAL A 275 CLR A1205 OLC A1229 HOH A1306
SITE 1 AD7 6 TYR A 179 VAL A 188 LEU A 191 OLA A1209
SITE 2 AD7 6 OLA A1212 OLC A1228
SITE 1 AD8 4 SER A 7 LEU A 14 OLA A1220 HOH A1305
SITE 1 AD9 3 PRO A 266 CLR A1203 CLR A1205
SITE 1 AE1 3 CLR A1203 OLA A1208 OLA A1220
SITE 1 AE2 6 ILE A 10 LEU A 14 OLA A1206 OLA A1217
SITE 2 AE2 6 OLA A1219 HOH A1305
SITE 1 AE3 10 VAL A 45 ILE A 98 HIS A 230 ALA A 231
SITE 2 AE3 10 ALA A 235 TYR A 288 ARG A 291 ILE A 292
SITE 3 AE3 10 ARG A 293 HOH A1301
SITE 1 AE4 3 MET A 4 LEU A 19 PHE A 286
SITE 1 AE5 7 MET A 174 ASN A 175 LYS A1083 HOH A1348
SITE 2 AE5 7 HOH A1365 HOH A1379 HOH A1384
SITE 1 AE6 4 THR A 256 PHE A 257 HOH A1348 HOH A1384
SITE 1 AE7 4 PRO A 1 PRO A 2 ILE A 3 ARG A 300
SITE 1 AE8 4 GLY A 142 TRP A 143 ASN A 144 ASN A 175
SITE 1 AE9 5 ILE A 125 TRP A 129 PHE A 133 OLA A1211
SITE 2 AE9 5 OLA A1212
SITE 1 AF1 1 OLA A1216
SITE 1 AF2 8 VAL A 12 ILE A 16 THR A 279 VAL A 282
SITE 2 AF2 8 VAL A 283 PHE A 286 CLR A1205 OLA A1215
SITE 1 AF3 3 THR A 119 GLY A 123 ILE A 127
SITE 1 AF4 4 ASP A 52 SER A 91 HOH A1349 HOH A1375
CRYST1 39.450 179.393 139.600 90.00 90.00 90.00 C 2 2 21 8
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 0.025349 0.000000 0.000000 0.00000
SCALE2 0.000000 0.005574 0.000000 0.00000
SCALE3 0.000000 0.000000 0.007163 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
