HEADER SIGNALING PROTEIN 04-AUG-11 3VGA
TITLE CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN ALLOSTERIC
TITLE 2 INVERSE-AGONIST ANTIBODY AT 3.1 A RESOLUTION
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A;
COMPND 3 CHAIN: A;
COMPND 4 FRAGMENT: UNP RESIDUES 1-316;
COMPND 5 ENGINEERED: YES;
COMPND 6 MUTATION: YES;
COMPND 7 MOL_ID: 2;
COMPND 8 MOLECULE: ANTIBODY FAB FRAGMENT LIGHT CHAIN;
COMPND 9 CHAIN: B;
COMPND 10 MOL_ID: 3;
COMPND 11 MOLECULE: ANTIBODY FAB FRAGMENT HEAVY CHAIN;
COMPND 12 CHAIN: C
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 GENE: ADORA2A, ADORA2;
SOURCE 6 EXPRESSION_SYSTEM: PICHIA PASTORIS;
SOURCE 7 EXPRESSION_SYSTEM_TAXID: 4922;
SOURCE 8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;
SOURCE 9 EXPRESSION_SYSTEM_PLASMID: PPIC9K;
SOURCE 10 MOL_ID: 2;
SOURCE 11 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 12 ORGANISM_COMMON: MOUSE;
SOURCE 13 ORGANISM_TAXID: 10090;
SOURCE 14 MOL_ID: 3;
SOURCE 15 ORGANISM_SCIENTIFIC: MUS MUSCULUS;
SOURCE 16 ORGANISM_COMMON: MOUSE;
SOURCE 17 ORGANISM_TAXID: 10090
KEYWDS 7 TRANSMEMBRANE RECEPTOR, SIGNAL TRANSDUCTION, SIGNALING PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR T.HINO,T.ARAKAWA,H.IWANARI,T.YURUGI-KOBAYASHI,C.IKEDA-SUNO,Y.NAKADA-
AUTHOR 2 NAKURA,O.KUSANO-ARAI,S.WEYAND,T.SHIMAMURA,N.NOMURA,A.D.CAMERON,
AUTHOR 3 T.KOBAYASHI,T.HAMAKUBO,S.IWATA,T.MURATA
REVDAT 4 30-OCT-24 3VGA 1 REMARK
REVDAT 3 08-NOV-23 3VGA 1 REMARK SEQADV
REVDAT 2 15-FEB-12 3VGA 1 JRNL
REVDAT 1 01-FEB-12 3VGA 0
JRNL AUTH T.HINO,T.ARAKAWA,H.IWANARI,T.YURUGI-KOBAYASHI,C.IKEDA-SUNO,
JRNL AUTH 2 Y.NAKADA-NAKURA,O.KUSANO-ARAI,S.WEYAND,T.SHIMAMURA,N.NOMURA,
JRNL AUTH 3 A.D.CAMERON,T.KOBAYASHI,T.HAMAKUBO,S.IWATA,T.MURATA
JRNL TITL G-PROTEIN-COUPLED RECEPTOR INACTIVATION BY AN ALLOSTERIC
JRNL TITL 2 INVERSE-AGONIST ANTIBODY
JRNL REF NATURE V. 482 237 2012
JRNL REFN ISSN 0028-0836
JRNL PMID 22286059
JRNL DOI 10.1038/NATURE10750
REMARK 2
REMARK 2 RESOLUTION. 3.10 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : PHENIX (PHENIX.REFINE: 1.7.1_743)
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 : MLHL
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.10
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 20.00
REMARK 3 MIN(FOBS/SIGMA_FOBS) : 1.340
REMARK 3 COMPLETENESS FOR RANGE (%) : 88.4
REMARK 3 NUMBER OF REFLECTIONS : 17901
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 R VALUE (WORKING + TEST SET) : 0.199
REMARK 3 R VALUE (WORKING SET) : 0.196
REMARK 3 FREE R VALUE : 0.263
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.130
REMARK 3 FREE R VALUE TEST SET COUNT : 968
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 19.9969 - 5.8866 0.85 2518 151 0.2252 0.2838
REMARK 3 2 5.8866 - 4.6922 0.90 2612 135 0.1722 0.2451
REMARK 3 3 4.6922 - 4.1049 0.86 2498 132 0.1564 0.2259
REMARK 3 4 4.1049 - 3.7323 0.90 2584 158 0.1779 0.2710
REMARK 3 5 3.7323 - 3.4662 0.88 2523 137 0.2033 0.2460
REMARK 3 6 3.4662 - 3.2628 0.89 2575 114 0.2224 0.2869
REMARK 3 7 3.2628 - 3.1000 0.90 2591 141 0.2614 0.3167
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : FLAT BULK SOLVENT MODEL
REMARK 3 SOLVENT RADIUS : 0.60
REMARK 3 SHRINKAGE RADIUS : 0.27
REMARK 3 K_SOL : 0.30
REMARK 3 B_SOL : 58.17
REMARK 3
REMARK 3 ERROR ESTIMATES.
REMARK 3 COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED) : 0.830
REMARK 3 PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 26.760
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 79.00
REMARK 3 MEAN B VALUE (OVERALL, A**2) : NULL
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -15.73960
REMARK 3 B22 (A**2) : 6.80060
REMARK 3 B33 (A**2) : 8.93910
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : -9.55300
REMARK 3 B23 (A**2) : 0.00000
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 : 0.008 5768
REMARK 3 ANGLE : 1.278 7850
REMARK 3 CHIRALITY : 0.084 902
REMARK 3 PLANARITY : 0.006 980
REMARK 3 DIHEDRAL : 17.053 2007
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: CHAIN 'A'
REMARK 3 ORIGIN FOR THE GROUP (A): 62.7650 -8.8708 36.3356
REMARK 3 T TENSOR
REMARK 3 T11: -0.4586 T22: 0.8223
REMARK 3 T33: -0.0638 T12: 0.0402
REMARK 3 T13: -0.2764 T23: -0.1037
REMARK 3 L TENSOR
REMARK 3 L11: 0.9795 L22: 1.4776
REMARK 3 L33: 1.7749 L12: 0.0699
REMARK 3 L13: -0.6019 L23: 0.3411
REMARK 3 S TENSOR
REMARK 3 S11: 0.0755 S12: -0.6853 S13: -0.0693
REMARK 3 S21: 0.5246 S22: 0.1228 S23: -0.6416
REMARK 3 S31: -0.0417 S32: 0.8520 S33: 0.0461
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: CHAIN 'C'
REMARK 3 ORIGIN FOR THE GROUP (A): 19.7508 1.4067 0.0609
REMARK 3 T TENSOR
REMARK 3 T11: 0.3953 T22: 0.2013
REMARK 3 T33: 0.4645 T12: -0.0364
REMARK 3 T13: 0.0060 T23: 0.0775
REMARK 3 L TENSOR
REMARK 3 L11: 4.9038 L22: 0.8705
REMARK 3 L33: 1.1396 L12: 0.7196
REMARK 3 L13: 1.6861 L23: 0.2871
REMARK 3 S TENSOR
REMARK 3 S11: -0.2429 S12: 0.1178 S13: 0.6495
REMARK 3 S21: -0.0755 S22: -0.0260 S23: 0.0882
REMARK 3 S31: -0.2084 S32: 0.0898 S33: 0.2253
REMARK 3 TLS GROUP : 3
REMARK 3 SELECTION: CHAIN 'B'
REMARK 3 ORIGIN FOR THE GROUP (A): 20.4190 -15.9471 -4.7868
REMARK 3 T TENSOR
REMARK 3 T11: 0.3184 T22: 0.3262
REMARK 3 T33: 0.3417 T12: 0.0975
REMARK 3 T13: 0.0384 T23: -0.0099
REMARK 3 L TENSOR
REMARK 3 L11: 3.9493 L22: 1.3228
REMARK 3 L33: 2.8884 L12: 0.2629
REMARK 3 L13: 2.6339 L23: 0.5871
REMARK 3 S TENSOR
REMARK 3 S11: 0.1956 S12: 0.7483 S13: -0.0005
REMARK 3 S21: -0.2767 S22: -0.0522 S23: 0.0071
REMARK 3 S31: 0.0717 S32: 0.4044 S33: -0.1589
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 3VGA COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-AUG-11.
REMARK 100 THE DEPOSITION ID IS D_1000095008.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 07-MAR-10
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 6.5
REMARK 200 NUMBER OF CRYSTALS USED : 1
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : DIAMOND
REMARK 200 BEAMLINE : I24
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.9795
REMARK 200 MONOCHROMATOR : ACCEL FIXED EXIT DOUBLE CRYSTAL
REMARK 200 SI(111)
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 6M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : SCALA
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 18451
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.100
REMARK 200 RESOLUTION RANGE LOW (A) : 71.200
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 88.8
REMARK 200 DATA REDUNDANCY : 2.300
REMARK 200 R MERGE (I) : 0.10900
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.3000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.10
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.27
REMARK 200 COMPLETENESS FOR SHELL (%) : 90.4
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.63600
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.500
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: PDB ENTRY 1VGA
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 65.12
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.53
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG 400, 0.1M MES, 0.2M MAGNESIUM
REMARK 280 CHLORIDE, 0.5% OCTHYL THIOGLUCOSIDE , PH 6.5, VAPOR DIFFUSION,
REMARK 280 HANGING DROP, TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X,Y,-Z
REMARK 290 3555 X+1/2,Y+1/2,Z
REMARK 290 4555 -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 0.00000
REMARK 290 SMTRY1 3 1.000000 0.000000 0.000000 60.15650
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 44.88300
REMARK 290 SMTRY3 3 0.000000 0.000000 1.000000 0.00000
REMARK 290 SMTRY1 4 -1.000000 0.000000 0.000000 60.15650
REMARK 290 SMTRY2 4 0.000000 1.000000 0.000000 44.88300
REMARK 290 SMTRY3 4 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: TRIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 6170 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 32820 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C
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 375
REMARK 375 SPECIAL POSITION
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL
REMARK 375 POSITIONS.
REMARK 375
REMARK 375 ATOM RES CSSEQI
REMARK 375 HOH C 231 LIES ON A SPECIAL POSITION.
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 PRO A 2
REMARK 465 ILE A 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 PRO A 149
REMARK 465 LYS A 150
REMARK 465 GLU A 151
REMARK 465 GLY A 152
REMARK 465 LYS A 153
REMARK 465 GLN A 154
REMARK 465 HIS A 155
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 HIS A 317
REMARK 465 HIS 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 GLU B 213
REMARK 465 CYS B 214
REMARK 465 CYS C 139
REMARK 465 GLY C 140
REMARK 465 ASP C 141
REMARK 465 THR C 142
REMARK 465 SER C 143
REMARK 465 PRO C 226
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 ARG A 220 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 222 CG CD NE CZ NH1 NH2
REMARK 470 ASN B 212 O CG OD1 ND2
REMARK 470 LYS C 43 CG CD CE NZ
REMARK 470 GLY C 225 O
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 CB CYS A 259 SG CYS A 262 1.74
REMARK 500 O ILE B 29 O SER B 31 2.16
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 -66.94 -107.33
REMARK 500 CYS A 146 -75.80 -91.82
REMARK 500 GLU A 161 66.70 39.13
REMARK 500 PHE A 182 -74.28 -97.37
REMARK 500 VAL A 186 -62.49 -128.54
REMARK 500 LEU A 216 149.82 72.33
REMARK 500 PRO A 260 43.66 -76.92
REMARK 500 ASP A 261 -61.07 -134.66
REMARK 500 PRO A 266 -172.50 -66.33
REMARK 500 SER A 305 -71.71 -117.90
REMARK 500 TYR B 30 -124.64 62.87
REMARK 500 SER B 32 9.31 98.46
REMARK 500 LEU B 47 -64.15 -108.49
REMARK 500 ALA B 51 -26.10 77.37
REMARK 500 SER B 67 166.32 179.98
REMARK 500 ARG B 77 73.91 45.00
REMARK 500 LYS B 169 -70.14 -99.03
REMARK 500 ASN B 190 -61.17 -90.48
REMARK 500 LYS C 43 -73.96 -130.27
REMARK 500 ALA C 92 -177.43 -173.36
REMARK 500 PRO C 137 -166.29 -68.26
REMARK 500 SER C 171 -70.30 -100.31
REMARK 500 SER C 183 -115.27 51.57
REMARK 500
REMARK 500 REMARK: NULL
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 401
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 3VG9 RELATED DB: PDB
REMARK 900 CRYSTAL STRUCTURE OF HUMAN ADENOSINE A2A RECEPTOR WITH AN
REMARK 900 ALLOSTERIC INVERSE-AGONIST ANTIBODY AT 2.7 A RESOLUTION
DBREF 3VGA A 1 316 UNP P29274 AA2AR_HUMAN 1 316
DBREF 3VGA B 1 214 PDB 3VGA 3VGA 1 214
DBREF 3VGA C 1 226 PDB 3VGA 3VGA 1 226
SEQADV 3VGA GLN A 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 3VGA HIS A 317 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 318 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 319 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 320 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 321 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 322 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 323 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 324 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 325 UNP P29274 EXPRESSION TAG
SEQADV 3VGA HIS A 326 UNP P29274 EXPRESSION TAG
SEQRES 1 A 326 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU
SEQRES 2 A 326 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU
SEQRES 3 A 326 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN
SEQRES 4 A 326 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP
SEQRES 5 A 326 ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR
SEQRES 6 A 326 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU
SEQRES 7 A 326 PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER
SEQRES 8 A 326 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE
SEQRES 9 A 326 ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR
SEQRES 10 A 326 GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL
SEQRES 11 A 326 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP
SEQRES 12 A 326 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS GLN HIS SER
SEQRES 13 A 326 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU
SEQRES 14 A 326 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE
SEQRES 15 A 326 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY
SEQRES 16 A 326 VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU
SEQRES 17 A 326 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA
SEQRES 18 A 326 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER
SEQRES 19 A 326 LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU
SEQRES 20 A 326 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO
SEQRES 21 A 326 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA
SEQRES 22 A 326 ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE
SEQRES 23 A 326 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE
SEQRES 24 A 326 ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU
SEQRES 25 A 326 PRO PHE LYS ALA HIS HIS HIS HIS HIS HIS HIS HIS HIS
SEQRES 26 A 326 HIS
SEQRES 1 B 214 ASP ILE VAL MET THR GLN SER PRO ALA SER LEU SER ALA
SEQRES 2 B 214 SER VAL GLY ASP THR VAL THR ILE THR CYS ARG ALA SER
SEQRES 3 B 214 GLU PHE ILE TYR SER SER LEU THR TRP TYR GLN GLN LYS
SEQRES 4 B 214 GLN GLY GLY SER PRO GLN LEU LEU VAL TYR ALA ALA THR
SEQRES 5 B 214 ASN LEU ALA ASP ALA VAL PRO SER ARG PHE SER GLY SER
SEQRES 6 B 214 GLY SER GLY THR GLN PHE SER LEU LYS ILE ASN ARG LEU
SEQRES 7 B 214 GLN PRO GLU ASP PHE GLY THR TYR TYR CYS GLN HIS PHE
SEQRES 8 B 214 TYR GLY SER THR TRP ALA PHE GLY GLY GLY THR LYS LEU
SEQRES 9 B 214 GLU ILE LYS ARG ALA ASP ALA ALA PRO THR VAL SER ILE
SEQRES 10 B 214 PHE PRO PRO SER SER GLU GLN LEU THR SER GLY GLY ALA
SEQRES 11 B 214 SER VAL VAL CYS PHE LEU ASN ASN PHE TYR PRO LYS ASP
SEQRES 12 B 214 ILE ASN VAL LYS TRP LYS ILE ASP GLY SER GLU ARG GLN
SEQRES 13 B 214 ASN GLY VAL LEU ASN SER TRP THR ASP GLN ASP SER LYS
SEQRES 14 B 214 ASP SER THR TYR SER MET SER SER THR LEU THR LEU THR
SEQRES 15 B 214 LYS ASP GLU TYR GLU ARG HIS ASN SER TYR THR CYS GLU
SEQRES 16 B 214 ALA THR HIS LYS THR SER THR SER PRO ILE VAL LYS SER
SEQRES 17 B 214 PHE ASN ARG ASN GLU CYS
SEQRES 1 C 226 GLU VAL GLN LEU GLN GLN SER GLY ALA GLU LEU VAL LYS
SEQRES 2 C 226 PRO GLY SER SER VAL LYS ILE SER CYS LYS THR SER GLY
SEQRES 3 C 226 ASP SER PHE THR ALA TYR ASN MET ASN TRP VAL LYS GLN
SEQRES 4 C 226 SER HIS GLY LYS SER LEU GLU TRP ILE GLY ASN ILE ASN
SEQRES 5 C 226 PRO TYR TYR GLY SER THR ARG TYR ASN GLN LYS PHE LYS
SEQRES 6 C 226 GLY LYS ALA THR LEU THR VAL ASP LYS SER SER SER THR
SEQRES 7 C 226 ALA TYR ILE GLN LEU ASN SER LEU THR SER GLU ASP SER
SEQRES 8 C 226 ALA VAL TYR TYR CYS ALA ARG GLU GLY ASN TYR TYR ASP
SEQRES 9 C 226 GLY GLY SER VAL ARG TYR PHE ASP TYR TRP GLY GLN GLY
SEQRES 10 C 226 THR THR LEU THR VAL SER SER ALA LYS THR THR ALA PRO
SEQRES 11 C 226 SER VAL TYR PRO LEU ALA PRO VAL CYS GLY ASP THR SER
SEQRES 12 C 226 GLY SER SER VAL THR LEU GLY CYS LEU VAL LYS GLY TYR
SEQRES 13 C 226 PHE PRO GLU PRO VAL THR LEU THR TRP ASN SER GLY SER
SEQRES 14 C 226 LEU SER SER GLY VAL HIS THR PHE PRO ALA VAL LEU GLN
SEQRES 15 C 226 SER ASP LEU TYR THR LEU SER SER SER VAL THR VAL THR
SEQRES 16 C 226 SER SER THR TRP PRO SER GLN SER ILE THR CYS ASN VAL
SEQRES 17 C 226 ALA HIS PRO ALA SER SER THR LYS VAL ASP LYS LYS ILE
SEQRES 18 C 226 GLU PRO ARG GLY PRO
HET ZMA A 401 25
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
FORMUL 4 ZMA C16 H15 N7 O2
FORMUL 5 HOH *14(H2 O)
HELIX 1 1 SER A 6 ASN A 34 1 29
HELIX 2 2 SER A 35 GLN A 38 5 4
HELIX 3 3 ASN A 39 LEU A 58 1 20
HELIX 4 4 LEU A 58 ILE A 66 1 9
HELIX 5 5 ALA A 73 CYS A 82 1 10
HELIX 6 6 CYS A 82 ILE A 108 1 27
HELIX 7 7 ILE A 108 VAL A 116 1 9
HELIX 8 8 THR A 117 LEU A 137 1 21
HELIX 9 9 THR A 138 LEU A 141 5 4
HELIX 10 10 LEU A 167 VAL A 172 1 6
HELIX 11 11 PRO A 173 TYR A 179 1 7
HELIX 12 12 VAL A 186 SER A 213 1 28
HELIX 13 13 ALA A 221 PHE A 258 1 38
HELIX 14 14 PRO A 266 THR A 279 1 14
HELIX 15 15 VAL A 282 ILE A 292 1 11
HELIX 16 16 ILE A 292 VAL A 307 1 16
HELIX 17 17 GLN B 79 PHE B 83 5 5
HELIX 18 18 SER B 121 THR B 126 1 6
HELIX 19 19 LYS B 183 GLU B 187 1 5
HELIX 20 20 SER C 28 TYR C 32 5 5
HELIX 21 21 GLN C 62 LYS C 65 5 4
HELIX 22 22 THR C 87 SER C 91 5 5
HELIX 23 23 SER C 167 SER C 169 5 3
HELIX 24 24 PRO C 211 SER C 214 5 4
SHEET 1 A 2 CYS A 71 ALA A 72 0
SHEET 2 A 2 VAL A 164 ALA A 165 -1 O VAL A 164 N ALA A 72
SHEET 1 B 4 MET B 4 SER B 7 0
SHEET 2 B 4 VAL B 19 ALA B 25 -1 O THR B 22 N SER B 7
SHEET 3 B 4 GLN B 70 ILE B 75 -1 O ILE B 75 N VAL B 19
SHEET 4 B 4 PHE B 62 SER B 67 -1 N SER B 63 O LYS B 74
SHEET 1 C 6 SER B 10 ALA B 13 0
SHEET 2 C 6 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11
SHEET 3 C 6 GLY B 84 HIS B 90 -1 N TYR B 86 O THR B 102
SHEET 4 C 6 LEU B 33 GLN B 38 -1 N TYR B 36 O TYR B 87
SHEET 5 C 6 GLN B 45 TYR B 49 -1 O LEU B 47 N TRP B 35
SHEET 6 C 6 ASN B 53 LEU B 54 -1 O ASN B 53 N TYR B 49
SHEET 1 D 4 SER B 10 ALA B 13 0
SHEET 2 D 4 THR B 102 ILE B 106 1 O GLU B 105 N LEU B 11
SHEET 3 D 4 GLY B 84 HIS B 90 -1 N TYR B 86 O THR B 102
SHEET 4 D 4 ALA B 97 PHE B 98 -1 O ALA B 97 N HIS B 90
SHEET 1 E 4 THR B 114 PHE B 118 0
SHEET 2 E 4 GLY B 129 PHE B 139 -1 O ASN B 137 N THR B 114
SHEET 3 E 4 TYR B 173 THR B 182 -1 O TYR B 173 N PHE B 139
SHEET 4 E 4 VAL B 159 TRP B 163 -1 N SER B 162 O SER B 176
SHEET 1 F 4 SER B 153 ARG B 155 0
SHEET 2 F 4 ASN B 145 ILE B 150 -1 N ILE B 150 O SER B 153
SHEET 3 F 4 SER B 191 HIS B 198 -1 O THR B 193 N LYS B 149
SHEET 4 F 4 SER B 201 ASN B 210 -1 O ILE B 205 N ALA B 196
SHEET 1 G 4 GLN C 3 GLN C 6 0
SHEET 2 G 4 VAL C 18 SER C 25 -1 O LYS C 23 N GLN C 5
SHEET 3 G 4 THR C 78 LEU C 83 -1 O ILE C 81 N ILE C 20
SHEET 4 G 4 ALA C 68 ASP C 73 -1 N THR C 71 O TYR C 80
SHEET 1 H 6 GLU C 10 VAL C 12 0
SHEET 2 H 6 THR C 118 VAL C 122 1 O THR C 119 N GLU C 10
SHEET 3 H 6 ALA C 92 TYR C 103 -1 N ALA C 92 O LEU C 120
SHEET 4 H 6 MET C 34 SER C 40 -1 N GLN C 39 O VAL C 93
SHEET 5 H 6 SER C 44 ILE C 51 -1 O ILE C 51 N MET C 34
SHEET 6 H 6 THR C 58 TYR C 60 -1 O ARG C 59 N ASN C 50
SHEET 1 I 4 GLU C 10 VAL C 12 0
SHEET 2 I 4 THR C 118 VAL C 122 1 O THR C 119 N GLU C 10
SHEET 3 I 4 ALA C 92 TYR C 103 -1 N ALA C 92 O LEU C 120
SHEET 4 I 4 SER C 107 TRP C 114 -1 O TYR C 113 N ARG C 98
SHEET 1 J 4 SER C 131 LEU C 135 0
SHEET 2 J 4 SER C 146 TYR C 156 -1 O GLY C 150 N LEU C 135
SHEET 3 J 4 LEU C 185 THR C 195 -1 O LEU C 188 N VAL C 153
SHEET 4 J 4 VAL C 174 THR C 176 -1 N HIS C 175 O SER C 191
SHEET 1 K 4 SER C 131 LEU C 135 0
SHEET 2 K 4 SER C 146 TYR C 156 -1 O GLY C 150 N LEU C 135
SHEET 3 K 4 LEU C 185 THR C 195 -1 O LEU C 188 N VAL C 153
SHEET 4 K 4 VAL C 180 GLN C 182 -1 N GLN C 182 O LEU C 185
SHEET 1 L 3 THR C 162 TRP C 165 0
SHEET 2 L 3 THR C 205 HIS C 210 -1 O ASN C 207 N THR C 164
SHEET 3 L 3 THR C 215 LYS C 220 -1 O LYS C 219 N CYS C 206
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.03
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.03
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.04
SSBOND 5 CYS B 23 CYS B 88 1555 1555 2.04
SSBOND 6 CYS B 134 CYS B 194 1555 1555 2.04
SSBOND 7 CYS C 22 CYS C 96 1555 1555 2.03
SSBOND 8 CYS C 151 CYS C 206 1555 1555 2.03
CISPEP 1 GLY A 218 GLU A 219 0 3.64
CISPEP 2 SER B 7 PRO B 8 0 -6.28
CISPEP 3 TYR B 140 PRO B 141 0 1.62
CISPEP 4 PHE C 157 PRO C 158 0 -7.32
CISPEP 5 GLU C 159 PRO C 160 0 -9.31
CISPEP 6 TRP C 199 PRO C 200 0 0.22
SITE 1 AC1 7 LEU A 85 PHE A 168 GLU A 169 MET A 177
SITE 2 AC1 7 LEU A 249 HIS A 250 MET A 270
CRYST1 120.313 89.766 110.682 90.00 96.14 90.00 C 1 2 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 0.008312 0.000000 0.000894 0.00000
SCALE2 0.000000 0.011140 0.000000 0.00000
SCALE3 0.000000 0.000000 0.009087 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
