HEADER SIGNALING PROTEIN 19-MAY-16 5G53
TITLE STRUCTURE OF THE ADENOSINE A2A RECEPTOR BOUND TO AN ENGINEERED G
TITLE 2 PROTEIN
CAVEAT 5G53 ASN C 239 HAS WRONG CHIRALITY AT ATOM CA
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: ADENOSINE RECEPTOR A2A;
COMPND 3 CHAIN: A, B;
COMPND 4 ENGINEERED: YES;
COMPND 5 MUTATION: YES;
COMPND 6 OTHER_DETAILS: THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE 308 OF THE
COMPND 7 A2A SEQUENCE, BUT HAS A 6 RESIDUE SEQUENCE THAT INCLUDES THE TEV
COMPND 8 CLEAVAGE SEQUENCE (ENLYFQ) AT THE C- TERMINUS;
COMPND 9 MOL_ID: 2;
COMPND 10 MOLECULE: ENGINEERED DOMAIN OF HUMAN G ALPHA S LONG ISOFORM;
COMPND 11 CHAIN: C, D;
COMPND 12 FRAGMENT: RAS DOMAIN, RESIDUES 26-60 AND 847-1037;
COMPND 13 ENGINEERED: YES;
COMPND 14 MUTATION: YES;
COMPND 15 OTHER_DETAILS: DELETIONS 1-25,65-203,255-264 INSERTION GGSGGSGG
COMPND 16 LINKING RESIDUES 64 AND 204
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606;
SOURCE 5 TISSUE: BRAIN;
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: BACULOVIRUS FLASHBAC ULTRA;
SOURCE 10 EXPRESSION_SYSTEM_PLASMID: PBACPAK8;
SOURCE 11 MOL_ID: 2;
SOURCE 12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;
SOURCE 13 ORGANISM_COMMON: HUMAN;
SOURCE 14 ORGANISM_TAXID: 9606;
SOURCE 15 TISSUE: BRAIN;
SOURCE 16 EXPRESSION_SYSTEM: ESCHERICHIA COLI;
SOURCE 17 EXPRESSION_SYSTEM_TAXID: 469008;
SOURCE 18 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);
SOURCE 19 EXPRESSION_SYSTEM_VARIANT: CODONPLUS-RIL;
SOURCE 20 EXPRESSION_SYSTEM_VECTOR_TYPE: MULTI-COPY PLASMID;
SOURCE 21 EXPRESSION_SYSTEM_VECTOR: PET15B
KEYWDS SIGNALING PROTEIN, G PROTEIN COUPLED RECEPTOR, ADENOSINE RECEPTOR,
KEYWDS 2 SEVEN-HELIX RECEPTOR, INTEGRAL MEMBRANE PROTEIN, GPCR, ENGINEERED G
KEYWDS 3 PROTEIN, GPCR-G PROTEIN COMPLEX, MINI-GS
EXPDTA X-RAY DIFFRACTION
AUTHOR B.CARPENTER,R.NEHME,T.WARNE,A.G.W.LESLIE,C.G.TATE
REVDAT 6 10-JAN-24 5G53 1 HETSYN
REVDAT 5 29-JUL-20 5G53 1 CAVEAT COMPND REMARK HETNAM
REVDAT 5 2 1 SITE
REVDAT 4 08-MAR-17 5G53 1 JRNL
REVDAT 3 24-AUG-16 5G53 1 JRNL
REVDAT 2 10-AUG-16 5G53 1 JRNL
REVDAT 1 03-AUG-16 5G53 0
JRNL AUTH B.CARPENTER,R.NEHME,T.WARNE,A.G.W.LESLIE,C.G.TATE
JRNL TITL STRUCTURE OF THE ADENOSINE A2A RECEPTOR BOUND TO AN
JRNL TITL 2 ENGINEERED G PROTEIN
JRNL REF NATURE V. 536 104 2016
JRNL REFN ISSN 0028-0836
JRNL PMID 27462812
JRNL DOI 10.1038/NATURE18966
REMARK 1
REMARK 1 REFERENCE 1
REMARK 1 AUTH G.LEBON,T.WARNE,P.C.EDWARDS,K.BENNETT,C.J.LANGMEAD,
REMARK 1 AUTH 2 A.G.W.LESLIE,C.G.TATE
REMARK 1 TITL AGONIST-BOUND ADENOSINE A2A RECEPTOR STRUCTURES REVEAL
REMARK 1 TITL 2 COMMON FEATURES OF GPCR ACTIVATION
REMARK 1 REF NATURE V. 474 521 2011
REMARK 1 REFN ISSN 0028-0836
REMARK 1 PMID 21593763
REMARK 1 DOI 10.1038/NATURE10136
REMARK 1 REFERENCE 2
REMARK 1 AUTH B.CARPENTER,C.G.TATE
REMARK 1 TITL ENGINEERING A MINIMAL G PROTEIN TO FACILITATE
REMARK 1 TITL 2 CRYSTALLISATION OF G PROTEIN-COUPLED RECEPTORS IN THEIR
REMARK 1 TITL 3 ACTIVE CONFORMATION.
REMARK 1 REF PROTEIN ENG. DES. SEL. V. 29 583 2016
REMARK 1 REFN ESSN 1741-0134
REMARK 1 PMID 27672048
REMARK 1 DOI 10.1093/PROTEIN/GZW049
REMARK 2
REMARK 2 RESOLUTION. 3.40 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : REFMAC 5.8.0144
REMARK 3 AUTHORS : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,
REMARK 3 : NICHOLLS,WINN,LONG,VAGIN
REMARK 3
REMARK 3 REFINEMENT TARGET : MAXIMUM LIKELIHOOD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.40
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 91.89
REMARK 3 DATA CUTOFF (SIGMA(F)) : NULL
REMARK 3 COMPLETENESS FOR RANGE (%) : 89.9
REMARK 3 NUMBER OF REFLECTIONS : 19788
REMARK 3
REMARK 3 FIT TO DATA USED IN REFINEMENT.
REMARK 3 CROSS-VALIDATION METHOD : THROUGHOUT
REMARK 3 FREE R VALUE TEST SET SELECTION : RANDOM
REMARK 3 R VALUE (WORKING + TEST SET) : 0.285
REMARK 3 R VALUE (WORKING SET) : 0.284
REMARK 3 FREE R VALUE : 0.315
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 5.200
REMARK 3 FREE R VALUE TEST SET COUNT : 1089
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 20
REMARK 3 BIN RESOLUTION RANGE HIGH (A) : 3.40
REMARK 3 BIN RESOLUTION RANGE LOW (A) : 3.49
REMARK 3 REFLECTION IN BIN (WORKING SET) : 903
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 56.48
REMARK 3 BIN R VALUE (WORKING SET) : 0.4080
REMARK 3 BIN FREE R VALUE SET COUNT : 64
REMARK 3 BIN FREE R VALUE : 0.3820
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 7247
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 112
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : NULL
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 76.30
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : -1.78000
REMARK 3 B22 (A**2) : -3.88000
REMARK 3 B33 (A**2) : 5.66000
REMARK 3 B12 (A**2) : 0.00000
REMARK 3 B13 (A**2) : 0.00000
REMARK 3 B23 (A**2) : 0.00000
REMARK 3
REMARK 3 ESTIMATED OVERALL COORDINATE ERROR.
REMARK 3 ESU BASED ON R VALUE (A): NULL
REMARK 3 ESU BASED ON FREE R VALUE (A): 0.690
REMARK 3 ESU BASED ON MAXIMUM LIKELIHOOD (A): 0.697
REMARK 3 ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 46.428
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.828
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.811
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES COUNT RMS WEIGHT
REMARK 3 BOND LENGTHS REFINED ATOMS (A): 7546 ; 0.008 ; 0.019
REMARK 3 BOND LENGTHS OTHERS (A): 7116 ; 0.001 ; 0.020
REMARK 3 BOND ANGLES REFINED ATOMS (DEGREES): 10315 ; 1.149 ; 1.958
REMARK 3 BOND ANGLES OTHERS (DEGREES): 16166 ; 0.923 ; 3.000
REMARK 3 TORSION ANGLES, PERIOD 1 (DEGREES): 937 ; 5.295 ; 5.000
REMARK 3 TORSION ANGLES, PERIOD 2 (DEGREES): 291 ;35.502 ;23.024
REMARK 3 TORSION ANGLES, PERIOD 3 (DEGREES): 1092 ;16.014 ;15.000
REMARK 3 TORSION ANGLES, PERIOD 4 (DEGREES): 33 ;13.261 ;15.000
REMARK 3 CHIRAL-CENTER RESTRAINTS (A**3): 1234 ; 0.115 ; 0.200
REMARK 3 GENERAL PLANES REFINED ATOMS (A): 8458 ; 0.004 ; 0.020
REMARK 3 GENERAL PLANES OTHERS (A): 1845 ; 0.001 ; 0.020
REMARK 3 NON-BONDED CONTACTS REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED CONTACTS OTHERS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 NON-BONDED TORSION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 H-BOND (X...Y) OTHERS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 POTENTIAL METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY VDW OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY H-BOND OTHERS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION REFINED ATOMS (A): NULL ; NULL ; NULL
REMARK 3 SYMMETRY METAL-ION OTHERS (A): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 MAIN-CHAIN BOND REFINED ATOMS (A**2): 3781 ; 3.020 ; 7.920
REMARK 3 MAIN-CHAIN BOND OTHER ATOMS (A**2): 3780 ; 3.021 ; 7.919
REMARK 3 MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 4707 ; 5.207 ;11.876
REMARK 3 MAIN-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN BOND REFINED ATOMS (A**2): 3765 ; 2.219 ; 8.045
REMARK 3 SIDE-CHAIN BOND OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 5608 ; 3.942 ;12.013
REMARK 3 SIDE-CHAIN ANGLE OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B REFINED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 LONG RANGE B OTHER ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 ANISOTROPIC THERMAL FACTOR RESTRAINTS. COUNT RMS WEIGHT
REMARK 3 RIGID-BOND RESTRAINTS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; FREE ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3 SPHERICITY; BONDED ATOMS (A**2): NULL ; NULL ; NULL
REMARK 3
REMARK 3 NCS RESTRAINTS STATISTICS
REMARK 3 NUMBER OF DIFFERENT NCS GROUPS : NULL
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : NULL
REMARK 3
REMARK 3 BULK SOLVENT MODELLING.
REMARK 3 METHOD USED : MASK
REMARK 3 PARAMETERS FOR MASK CALCULATION
REMARK 3 VDW PROBE RADIUS : 1.20
REMARK 3 ION PROBE RADIUS : 0.80
REMARK 3 SHRINKAGE RADIUS : 0.80
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING
REMARK 3 POSITIONS. U VALUES REFINED INDIVIDUALLY SIDE CHAINS WITHOUT
REMARK 3 CLEAR ELECTRON DENSITY HAVE BEEN TRUNCATED BACK TO CBETA.
REMARK 4
REMARK 4 5G53 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 19-MAY-16.
REMARK 100 THE DEPOSITION ID IS D_1290066872.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 09-APR-15
REMARK 200 TEMPERATURE (KELVIN) : 100
REMARK 200 PH : 5.5
REMARK 200 NUMBER OF CRYSTALS USED : 2
REMARK 200
REMARK 200 SYNCHROTRON (Y/N) : Y
REMARK 200 RADIATION SOURCE : ESRF
REMARK 200 BEAMLINE : ID23-2
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 0.872900
REMARK 200 MONOCHROMATOR : SI(111)
REMARK 200 OPTICS : KB MIRRORS
REMARK 200
REMARK 200 DETECTOR TYPE : PIXEL
REMARK 200 DETECTOR MANUFACTURER : DECTRIS PILATUS 2M
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : MOSFLM
REMARK 200 DATA SCALING SOFTWARE : AIMLESS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 20898
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.400
REMARK 200 RESOLUTION RANGE LOW (A) : 40.300
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : 0.000
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 90.6
REMARK 200 DATA REDUNDANCY : 2.600
REMARK 200 R MERGE (I) : 0.17000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 3.6000
REMARK 200
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.40
REMARK 200 HIGHEST RESOLUTION SHELL, RANGE LOW (A) : 3.49
REMARK 200 COMPLETENESS FOR SHELL (%) : 78.5
REMARK 200 DATA REDUNDANCY IN SHELL : 2.40
REMARK 200 R MERGE FOR SHELL (I) : 0.75000
REMARK 200 R SYM FOR SHELL (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR SHELL : 1.200
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 ENTRIES 2YDV, 3SN6
REMARK 200
REMARK 200 REMARK: THE RAS DOMAIN FROM ENTRY 3SN6 WAS USED FOR MOLECULAR
REMARK 200 REPLACEMENT
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 58.00
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.90
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M NAOAC PH 5.5, 10% PEG 2000 (IN
REMARK 280 THE PRESENCE OF CHS); OR 0.1 M NAOAC PH 5.7, 9.5% PEG 2000 MME
REMARK 280 (IN THE ABSENCE OF CHS)
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,Z
REMARK 290 2555 -X+1/2,-Y,Z+1/2
REMARK 290 3555 -X,Y+1/2,-Z+1/2
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 45.31600
REMARK 290 SMTRY2 2 0.000000 -1.000000 0.000000 0.00000
REMARK 290 SMTRY3 2 0.000000 0.000000 1.000000 80.65200
REMARK 290 SMTRY1 3 -1.000000 0.000000 0.000000 0.00000
REMARK 290 SMTRY2 3 0.000000 1.000000 0.000000 55.90700
REMARK 290 SMTRY3 3 0.000000 0.000000 -1.000000 80.65200
REMARK 290 SMTRY1 4 1.000000 0.000000 0.000000 45.31600
REMARK 290 SMTRY2 4 0.000000 -1.000000 0.000000 55.90700
REMARK 290 SMTRY3 4 0.000000 0.000000 -1.000000 0.00000
REMARK 290
REMARK 290 REMARK: NULL
REMARK 300
REMARK 300 BIOMOLECULE: 1, 2
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: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 4140 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 23700 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 TOTAL BURIED SURFACE AREA: 2410 ANGSTROM**2
REMARK 350 SURFACE AREA OF THE COMPLEX: 22500 ANGSTROM**2
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.2 KCAL/MOL
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D
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 PRO A 2
REMARK 465 ILE A 3
REMARK 465 MET A 4
REMARK 465 GLY A 5
REMARK 465 GLY A 147
REMARK 465 GLN A 148
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 ALA A 154
REMARK 465 HIS A 155
REMARK 465 SER A 156
REMARK 465 GLN A 157
REMARK 465 GLY A 158
REMARK 465 GLU A 212
REMARK 465 SER A 213
REMARK 465 GLN A 214
REMARK 465 PRO A 215
REMARK 465 LEU A 216
REMARK 465 PRO A 217
REMARK 465 GLY A 218
REMARK 465 GLU A 219
REMARK 465 ARG A 220
REMARK 465 ALA A 221
REMARK 465 ARG A 222
REMARK 465 SER A 223
REMARK 465 PHE A 313
REMARK 465 GLN A 314
REMARK 465 MET B 1
REMARK 465 PRO B 2
REMARK 465 ILE B 3
REMARK 465 MET B 4
REMARK 465 GLY B 5
REMARK 465 LEU B 208
REMARK 465 LYS B 209
REMARK 465 GLN B 210
REMARK 465 MET B 211
REMARK 465 GLU B 212
REMARK 465 SER B 213
REMARK 465 GLN B 214
REMARK 465 PRO B 215
REMARK 465 LEU B 216
REMARK 465 PRO B 217
REMARK 465 GLY B 218
REMARK 465 GLU B 219
REMARK 465 ARG B 220
REMARK 465 ALA B 221
REMARK 465 ARG B 222
REMARK 465 SER B 223
REMARK 465 HIS B 306
REMARK 465 VAL B 307
REMARK 465 LEU B 308
REMARK 465 GLU B 309
REMARK 465 ASN B 310
REMARK 465 LEU B 311
REMARK 465 TYR B 312
REMARK 465 PHE B 313
REMARK 465 GLN B 314
REMARK 465 GLY C 25
REMARK 465 ILE C 26
REMARK 465 GLU C 27
REMARK 465 LYS C 28
REMARK 465 GLN C 29
REMARK 465 LEU C 30
REMARK 465 GLN C 31
REMARK 465 LYS C 32
REMARK 465 ASP C 33
REMARK 465 LYS C 34
REMARK 465 GLN C 35
REMARK 465 VAL C 36
REMARK 465 TYR C 37
REMARK 465 ARG C 38
REMARK 465 ALA C 39
REMARK 465 ILE C 193
REMARK 465 TYR C 194
REMARK 465 HIS C 195
REMARK 465 GLY C 196
REMARK 465 GLY C 197
REMARK 465 SER C 198
REMARK 465 GLY C 199
REMARK 465 GLY C 200
REMARK 465 SER C 201
REMARK 465 GLY C 202
REMARK 465 GLY C 203
REMARK 465 THR C 204
REMARK 465 SER C 205
REMARK 465 GLY C 206
REMARK 465 ILE C 207
REMARK 465 ALA C 366
REMARK 465 VAL C 367
REMARK 465 ASP C 368
REMARK 465 GLY D 25
REMARK 465 ILE D 26
REMARK 465 GLU D 27
REMARK 465 LYS D 28
REMARK 465 GLN D 29
REMARK 465 LEU D 30
REMARK 465 GLN D 31
REMARK 465 LYS D 32
REMARK 465 ASP D 33
REMARK 465 LYS D 34
REMARK 465 GLN D 35
REMARK 465 VAL D 36
REMARK 465 TYR D 37
REMARK 465 ARG D 38
REMARK 465 ILE D 193
REMARK 465 TYR D 194
REMARK 465 HIS D 195
REMARK 465 GLY D 196
REMARK 465 GLY D 197
REMARK 465 SER D 198
REMARK 465 GLY D 199
REMARK 465 GLY D 200
REMARK 465 SER D 201
REMARK 465 GLY D 202
REMARK 465 GLY D 203
REMARK 465 THR D 204
REMARK 465 SER D 205
REMARK 465 GLY D 206
REMARK 465 ILE D 207
REMARK 465 GLY D 225
REMARK 465 GLY D 226
REMARK 465 GLN D 227
REMARK 465 ARG D 228
REMARK 465 ASP D 229
REMARK 465 GLU D 230
REMARK 465 ARG D 231
REMARK 465 ARG D 232
REMARK 465 LYS D 233
REMARK 465 TRP D 234
REMARK 465 ILE D 235
REMARK 465 GLN D 236
REMARK 465 CYS D 237
REMARK 465 PHE D 238
REMARK 465 LEU D 394
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 107 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 161 CG CD OE1 OE2
REMARK 470 ARG A 199 CG CD NE CZ NH1 NH2
REMARK 470 LYS A 209 CG CD CE NZ
REMARK 470 GLU A 228 CG CD OE1 OE2
REMARK 470 ARG A 293 CG CD NE CZ NH1 NH2
REMARK 470 GLU A 294 CG CD OE1 OE2
REMARK 470 GLN B 38 CG CD OE1 NE2
REMARK 470 ARG B 102 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 107 CG CD NE CZ NH1 NH2
REMARK 470 LYS B 122 CG CD CE NZ
REMARK 470 GLU B 151 CG CD OE1 OE2
REMARK 470 GLU B 161 CG CD OE1 OE2
REMARK 470 ARG B 199 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 206 CG CD NE CZ NH1 NH2
REMARK 470 GLN B 226 CG CD OE1 NE2
REMARK 470 LYS B 227 CG CD CE NZ
REMARK 470 GLU B 228 CG CD OE1 OE2
REMARK 470 ASP B 261 CG OD1 OD2
REMARK 470 ARG B 291 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 293 CG CD NE CZ NH1 NH2
REMARK 470 LYS C 58 CG CD CE NZ
REMARK 470 GLN C 59 CG CD OE1 NE2
REMARK 470 MET C 60 CG SD CE
REMARK 470 ARG C 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 209 CG CD OE1 OE2
REMARK 470 ASP C 215 CG OD1 OD2
REMARK 470 LYS C 216 CG CD CE NZ
REMARK 470 ARG C 228 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 229 CG OD1 OD2
REMARK 470 LYS C 233 CG CD CE NZ
REMARK 470 GLU C 268 CG CD OE1 OE2
REMARK 470 ARG C 280 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 283 CG CD NE CZ NH1 NH2
REMARK 470 GLU C 299 CG CD OE1 OE2
REMARK 470 LEU C 302 CG CD1 CD2
REMARK 470 LYS C 305 CG CD CE NZ
REMARK 470 LYS C 307 CG CD CE NZ
REMARK 470 GLU C 322 CG CD OE1 OE2
REMARK 470 GLU C 330 CG CD OE1 OE2
REMARK 470 ARG C 333 CG CD NE CZ NH1 NH2
REMARK 470 ASP C 354 CG OD1 OD2
REMARK 470 ARG C 356 CG CD NE CZ NH1 NH2
REMARK 470 CYS C 365 SG
REMARK 470 THR C 369 OG1 CG2
REMARK 470 GLU C 370 CG CD OE1 OE2
REMARK 470 ARG C 373 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 385 CG CD NE CZ NH1 NH2
REMARK 470 ARG C 389 CG CD NE CZ NH1 NH2
REMARK 470 GLN C 390 CG CD OE1 NE2
REMARK 470 GLN D 59 CG CD OE1 NE2
REMARK 470 ARG D 61 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 209 CG CD OE1 OE2
REMARK 470 LYS D 211 CG CD CE NZ
REMARK 470 LYS D 216 CG CD CE NZ
REMARK 470 HIS D 220 CG ND1 CD2 CE1 NE2
REMARK 470 ASP D 240 CG OD1 OD2
REMARK 470 LYS D 274 CG CD CE NZ
REMARK 470 ARG D 280 CG CD NE CZ NH1 NH2
REMARK 470 TRP D 281 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP D 281 CZ3 CH2
REMARK 470 LYS D 300 CG CD CE NZ
REMARK 470 LYS D 305 CG CD CE NZ
REMARK 470 LYS D 307 CG CD CE NZ
REMARK 470 GLU D 309 CG CD OE1 OE2
REMARK 470 ASP D 310 CG OD1 OD2
REMARK 470 ARG D 317 CG CD NE CZ NH1 NH2
REMARK 470 GLU D 322 CG CD OE1 OE2
REMARK 470 ASP D 323 CG OD1 OD2
REMARK 470 ARG D 333 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 336 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 347 CG CD NE CZ NH1 NH2
REMARK 470 ARG D 356 CG CD NE CZ NH1 NH2
REMARK 470 CYS D 365 SG
REMARK 470 VAL D 367 CG1 CG2
REMARK 470 ASP D 368 CG OD1 OD2
REMARK 470 THR D 369 OG1 CG2
REMARK 470 GLU D 370 CG CD OE1 OE2
REMARK 470 ARG D 385 CG CD NE CZ NH1 NH2
REMARK 470 GLN D 390 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 PHE A 180 -60.53 -105.08
REMARK 500 GLN B 148 69.79 -119.98
REMARK 500 PHE B 180 -60.63 -105.21
REMARK 500 VAL C 224 53.92 -155.08
REMARK 500 GLN C 227 -13.07 91.10
REMARK 500 GLU C 230 -3.57 78.44
REMARK 500 PHE C 238 -90.22 114.97
REMARK 500 ASN C 239 -39.77 74.27
REMARK 500 ASP C 240 38.03 -98.05
REMARK 500 THR C 325 73.69 -118.44
REMARK 500 ASP D 240 41.96 -96.36
REMARK 500 THR D 325 73.02 -118.81
REMARK 500 ALA D 366 -54.04 66.70
REMARK 500 ASP D 368 126.44 -38.46
REMARK 500
REMARK 500 REMARK: NULL
REMARK 999
REMARK 999 SEQUENCE
REMARK 999 A2A RECEPTOR. THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE
REMARK 999 308 OF THE A2A SEQUENCE. REMOVAL OF GLYCOSYLATION SITE BY
REMARK 999 MUTATION N154A. AT C-TERMINUS,THERE IS A TEV CLEAVAGE
REMARK 999 SEQUENCE ENLYFQ
REMARK 999 ENGINEERED G ALPHA S. DELETIONS 1-25, 65-203, 255-264.
REMARK 999 MUTATIONS G49D, E50N, L63Y, A249D, S252D, L272D, I372A,
REMARK 999 V375I. INSERTION GGSGGSGG LINKING RESIDUES 64 AND 204.
REMARK 999 ADDITIONAL G RESIDUE AT N TERMINUS FROM TEV CLEAVAGE SITE.
DBREF 5G53 A 1 308 UNP P29274 AA2AR_HUMAN 1 308
DBREF 5G53 B 1 308 UNP P29274 AA2AR_HUMAN 1 308
DBREF 5G53 C 26 60 UNP P63092 GNAS2_HUMAN 26 60
DBREF 5G53 C 204 394 UNP Q5JWF2 GNAS1_HUMAN 847 1037
DBREF 5G53 D 26 60 UNP P63092 GNAS2_HUMAN 26 60
DBREF 5G53 D 204 394 UNP Q5JWF2 GNAS1_HUMAN 847 1037
SEQADV 5G53 ALA A 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 5G53 GLU A 309 UNP P29274 EXPRESSION TAG
SEQADV 5G53 ASN A 310 UNP P29274 EXPRESSION TAG
SEQADV 5G53 LEU A 311 UNP P29274 EXPRESSION TAG
SEQADV 5G53 TYR A 312 UNP P29274 EXPRESSION TAG
SEQADV 5G53 PHE A 313 UNP P29274 EXPRESSION TAG
SEQADV 5G53 GLN A 314 UNP P29274 EXPRESSION TAG
SEQADV 5G53 ALA B 154 UNP P29274 ASN 154 ENGINEERED MUTATION
SEQADV 5G53 GLU B 309 UNP P29274 EXPRESSION TAG
SEQADV 5G53 ASN B 310 UNP P29274 EXPRESSION TAG
SEQADV 5G53 LEU B 311 UNP P29274 EXPRESSION TAG
SEQADV 5G53 TYR B 312 UNP P29274 EXPRESSION TAG
SEQADV 5G53 PHE B 313 UNP P29274 EXPRESSION TAG
SEQADV 5G53 GLN B 314 UNP P29274 EXPRESSION TAG
SEQADV 5G53 GLY C 25 UNP P63092 EXPRESSION TAG
SEQADV 5G53 ASP C 49 UNP P63092 GLY 49 ENGINEERED MUTATION
SEQADV 5G53 ASN C 50 UNP P63092 GLU 50 ENGINEERED MUTATION
SEQADV 5G53 ARG C 61 UNP P63092 LINKER
SEQADV 5G53 ILE C 193 UNP P63092 LINKER
SEQADV 5G53 TYR C 194 UNP P63092 LINKER
SEQADV 5G53 HIS C 195 UNP P63092 LINKER
SEQADV 5G53 GLY C 196 UNP P63092 LINKER
SEQADV 5G53 GLY C 197 UNP P63092 LINKER
SEQADV 5G53 SER C 198 UNP P63092 LINKER
SEQADV 5G53 GLY C 199 UNP P63092 LINKER
SEQADV 5G53 GLY C 200 UNP P63092 LINKER
SEQADV 5G53 SER C 201 UNP P63092 LINKER
SEQADV 5G53 GLY C 202 UNP P63092 LINKER
SEQADV 5G53 GLY C 203 UNP P63092 LINKER
SEQADV 5G53 ASP C 249 UNP Q5JWF2 ALA 892 ENGINEERED MUTATION
SEQADV 5G53 ASP C 252 UNP Q5JWF2 SER 895 ENGINEERED MUTATION
SEQADV 5G53 C UNP Q5JWF2 ASN 897 DELETION
SEQADV 5G53 C UNP Q5JWF2 MET 898 DELETION
SEQADV 5G53 C UNP Q5JWF2 VAL 899 DELETION
SEQADV 5G53 C UNP Q5JWF2 ILE 900 DELETION
SEQADV 5G53 C UNP Q5JWF2 ARG 901 DELETION
SEQADV 5G53 C UNP Q5JWF2 GLU 902 DELETION
SEQADV 5G53 C UNP Q5JWF2 ASP 903 DELETION
SEQADV 5G53 C UNP Q5JWF2 ASN 904 DELETION
SEQADV 5G53 C UNP Q5JWF2 GLN 905 DELETION
SEQADV 5G53 C UNP Q5JWF2 THR 906 DELETION
SEQADV 5G53 ASP C 272 UNP Q5JWF2 LEU 915 ENGINEERED MUTATION
SEQADV 5G53 ALA C 372 UNP Q5JWF2 ILE 1015 ENGINEERED MUTATION
SEQADV 5G53 ILE C 375 UNP Q5JWF2 VAL 1018 ENGINEERED MUTATION
SEQADV 5G53 GLY D 25 UNP P63092 EXPRESSION TAG
SEQADV 5G53 ASP D 49 UNP P63092 GLY 49 ENGINEERED MUTATION
SEQADV 5G53 ASN D 50 UNP P63092 GLU 50 ENGINEERED MUTATION
SEQADV 5G53 ARG D 61 UNP P63092 LINKER
SEQADV 5G53 ILE D 193 UNP P63092 LINKER
SEQADV 5G53 TYR D 194 UNP P63092 LINKER
SEQADV 5G53 HIS D 195 UNP P63092 LINKER
SEQADV 5G53 GLY D 196 UNP P63092 LINKER
SEQADV 5G53 GLY D 197 UNP P63092 LINKER
SEQADV 5G53 SER D 198 UNP P63092 LINKER
SEQADV 5G53 GLY D 199 UNP P63092 LINKER
SEQADV 5G53 GLY D 200 UNP P63092 LINKER
SEQADV 5G53 SER D 201 UNP P63092 LINKER
SEQADV 5G53 GLY D 202 UNP P63092 LINKER
SEQADV 5G53 GLY D 203 UNP P63092 LINKER
SEQADV 5G53 ASP D 249 UNP Q5JWF2 ALA 892 ENGINEERED MUTATION
SEQADV 5G53 ASP D 252 UNP Q5JWF2 SER 895 ENGINEERED MUTATION
SEQADV 5G53 D UNP Q5JWF2 ASN 897 DELETION
SEQADV 5G53 D UNP Q5JWF2 MET 898 DELETION
SEQADV 5G53 D UNP Q5JWF2 VAL 899 DELETION
SEQADV 5G53 D UNP Q5JWF2 ILE 900 DELETION
SEQADV 5G53 D UNP Q5JWF2 ARG 901 DELETION
SEQADV 5G53 D UNP Q5JWF2 GLU 902 DELETION
SEQADV 5G53 D UNP Q5JWF2 ASP 903 DELETION
SEQADV 5G53 D UNP Q5JWF2 ASN 904 DELETION
SEQADV 5G53 D UNP Q5JWF2 GLN 905 DELETION
SEQADV 5G53 D UNP Q5JWF2 THR 906 DELETION
SEQADV 5G53 ASP D 272 UNP Q5JWF2 LEU 915 ENGINEERED MUTATION
SEQADV 5G53 ALA D 372 UNP Q5JWF2 ILE 1015 ENGINEERED MUTATION
SEQADV 5G53 ILE D 375 UNP Q5JWF2 VAL 1018 ENGINEERED MUTATION
SEQRES 1 A 314 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU
SEQRES 2 A 314 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU
SEQRES 3 A 314 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN
SEQRES 4 A 314 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP
SEQRES 5 A 314 ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR
SEQRES 6 A 314 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU
SEQRES 7 A 314 PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER
SEQRES 8 A 314 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE
SEQRES 9 A 314 ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR
SEQRES 10 A 314 GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL
SEQRES 11 A 314 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP
SEQRES 12 A 314 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER
SEQRES 13 A 314 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU
SEQRES 14 A 314 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE
SEQRES 15 A 314 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY
SEQRES 16 A 314 VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU
SEQRES 17 A 314 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA
SEQRES 18 A 314 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER
SEQRES 19 A 314 LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU
SEQRES 20 A 314 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO
SEQRES 21 A 314 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA
SEQRES 22 A 314 ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE
SEQRES 23 A 314 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE
SEQRES 24 A 314 ARG LYS ILE ILE ARG SER HIS VAL LEU GLU ASN LEU TYR
SEQRES 25 A 314 PHE GLN
SEQRES 1 B 314 MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU
SEQRES 2 B 314 LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU
SEQRES 3 B 314 VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN
SEQRES 4 B 314 VAL THR ASN TYR PHE VAL VAL SER LEU ALA ALA ALA ASP
SEQRES 5 B 314 ILE ALA VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE THR
SEQRES 6 B 314 ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU
SEQRES 7 B 314 PHE ILE ALA CYS PHE VAL LEU VAL LEU THR GLN SER SER
SEQRES 8 B 314 ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE
SEQRES 9 B 314 ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR
SEQRES 10 B 314 GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL
SEQRES 11 B 314 LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP
SEQRES 12 B 314 ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER
SEQRES 13 B 314 GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU
SEQRES 14 B 314 ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE
SEQRES 15 B 314 PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY
SEQRES 16 B 314 VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU
SEQRES 17 B 314 LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA
SEQRES 18 B 314 ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER
SEQRES 19 B 314 LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU
SEQRES 20 B 314 PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO
SEQRES 21 B 314 ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA
SEQRES 22 B 314 ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE
SEQRES 23 B 314 ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE
SEQRES 24 B 314 ARG LYS ILE ILE ARG SER HIS VAL LEU GLU ASN LEU TYR
SEQRES 25 B 314 PHE GLN
SEQRES 1 C 229 GLY ILE GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR
SEQRES 2 C 229 ARG ALA THR HIS ARG LEU LEU LEU LEU GLY ALA ASP ASN
SEQRES 3 C 229 SER GLY LYS SER THR ILE VAL LYS GLN MET ARG ILE TYR
SEQRES 4 C 229 HIS GLY GLY SER GLY GLY SER GLY GLY THR SER GLY ILE
SEQRES 5 C 229 PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS
SEQRES 6 C 229 MET PHE ASP VAL GLY GLY GLN ARG ASP GLU ARG ARG LYS
SEQRES 7 C 229 TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE
SEQRES 8 C 229 VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN GLU ALA
SEQRES 9 C 229 LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG TRP LEU
SEQRES 10 C 229 ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS GLN ASP
SEQRES 11 C 229 LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER LYS ILE
SEQRES 12 C 229 GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR THR PRO
SEQRES 13 C 229 GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO ARG VAL
SEQRES 14 C 229 THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE LEU ARG
SEQRES 15 C 229 ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR CYS TYR
SEQRES 16 C 229 PRO HIS PHE THR CYS ALA VAL ASP THR GLU ASN ALA ARG
SEQRES 17 C 229 ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN ARG MET
SEQRES 18 C 229 HIS LEU ARG GLN TYR GLU LEU LEU
SEQRES 1 D 229 GLY ILE GLU LYS GLN LEU GLN LYS ASP LYS GLN VAL TYR
SEQRES 2 D 229 ARG ALA THR HIS ARG LEU LEU LEU LEU GLY ALA ASP ASN
SEQRES 3 D 229 SER GLY LYS SER THR ILE VAL LYS GLN MET ARG ILE TYR
SEQRES 4 D 229 HIS GLY GLY SER GLY GLY SER GLY GLY THR SER GLY ILE
SEQRES 5 D 229 PHE GLU THR LYS PHE GLN VAL ASP LYS VAL ASN PHE HIS
SEQRES 6 D 229 MET PHE ASP VAL GLY GLY GLN ARG ASP GLU ARG ARG LYS
SEQRES 7 D 229 TRP ILE GLN CYS PHE ASN ASP VAL THR ALA ILE ILE PHE
SEQRES 8 D 229 VAL VAL ASP SER SER ASP TYR ASN ARG LEU GLN GLU ALA
SEQRES 9 D 229 LEU ASN ASP PHE LYS SER ILE TRP ASN ASN ARG TRP LEU
SEQRES 10 D 229 ARG THR ILE SER VAL ILE LEU PHE LEU ASN LYS GLN ASP
SEQRES 11 D 229 LEU LEU ALA GLU LYS VAL LEU ALA GLY LYS SER LYS ILE
SEQRES 12 D 229 GLU ASP TYR PHE PRO GLU PHE ALA ARG TYR THR THR PRO
SEQRES 13 D 229 GLU ASP ALA THR PRO GLU PRO GLY GLU ASP PRO ARG VAL
SEQRES 14 D 229 THR ARG ALA LYS TYR PHE ILE ARG ASP GLU PHE LEU ARG
SEQRES 15 D 229 ILE SER THR ALA SER GLY ASP GLY ARG HIS TYR CYS TYR
SEQRES 16 D 229 PRO HIS PHE THR CYS ALA VAL ASP THR GLU ASN ALA ARG
SEQRES 17 D 229 ARG ILE PHE ASN ASP CYS ARG ASP ILE ILE GLN ARG MET
SEQRES 18 D 229 HIS LEU ARG GLN TYR GLU LEU LEU
HET NEC A 400 22
HET SOG A 501 20
HET SOG A 502 20
HET NEC B 400 22
HET GDP C 400 28
HETNAM NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE
HETNAM SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE
HETNAM GDP GUANOSINE-5'-DIPHOSPHATE
HETSYN SOG 2-HYDROXYMETHYL-6-OCTYLSULFANYL-TETRAHYDRO-PYRAN-3,4,5-
HETSYN 2 SOG TRIOL; 1-S-OCTYL-BETA-D-THIOGLUCOSIDE; OCTYL 1-THIO-
HETSYN 3 SOG BETA-D-GLUCOSIDE; OCTYL 1-THIO-D-GLUCOSIDE; OCTYL 1-
HETSYN 4 SOG THIO-GLUCOSIDE
FORMUL 5 NEC 2(C12 H16 N6 O4)
FORMUL 6 SOG 2(C14 H28 O5 S)
FORMUL 9 GDP C10 H15 N5 O11 P2
HELIX 1 1 SER A 6 ASN A 34 1 29
HELIX 2 2 VAL A 40 LEU A 58 1 19
HELIX 3 3 LEU A 58 THR A 68 1 11
HELIX 4 4 ALA A 73 ILE A 108 1 36
HELIX 5 5 ARG A 111 VAL A 116 1 6
HELIX 6 6 THR A 117 LEU A 137 1 21
HELIX 7 7 THR A 138 GLY A 142 5 5
HELIX 8 8 LEU A 167 VAL A 172 1 6
HELIX 9 9 PRO A 173 PHE A 180 1 8
HELIX 10 10 PHE A 180 VAL A 186 1 7
HELIX 11 11 VAL A 186 MET A 211 1 26
HELIX 12 12 THR A 224 CYS A 259 1 36
HELIX 13 13 PRO A 266 THR A 279 1 14
HELIX 14 14 THR A 279 TYR A 290 1 12
HELIX 15 15 ILE A 292 LEU A 311 1 20
HELIX 16 16 SER B 6 ASN B 34 1 29
HELIX 17 17 VAL B 40 LEU B 58 1 19
HELIX 18 18 LEU B 58 THR B 68 1 11
HELIX 19 19 ALA B 73 ILE B 108 1 36
HELIX 20 20 ARG B 111 VAL B 116 1 6
HELIX 21 21 THR B 117 LEU B 137 1 21
HELIX 22 22 THR B 138 GLY B 142 5 5
HELIX 23 23 LYS B 150 GLN B 157 1 8
HELIX 24 24 LEU B 167 VAL B 172 1 6
HELIX 25 25 PRO B 173 PHE B 180 1 8
HELIX 26 26 PHE B 180 VAL B 186 1 7
HELIX 27 27 VAL B 186 GLN B 207 1 22
HELIX 28 28 THR B 224 CYS B 259 1 36
HELIX 29 29 PRO B 266 THR B 279 1 14
HELIX 30 30 THR B 279 TYR B 290 1 12
HELIX 31 31 ILE B 292 SER B 305 1 14
HELIX 32 32 GLY C 52 ARG C 61 1 10
HELIX 33 33 GLU C 230 GLN C 236 1 7
HELIX 34 34 ASN C 254 ASN C 279 1 16
HELIX 35 35 LYS C 293 GLY C 304 1 12
HELIX 36 36 LYS C 307 PHE C 312 1 6
HELIX 37 37 PRO C 313 TYR C 318 5 6
HELIX 38 38 ASP C 331 SER C 352 1 22
HELIX 39 39 GLU C 370 TYR C 391 1 22
HELIX 40 40 GLY D 52 ARG D 61 1 10
HELIX 41 41 ASN D 254 ASN D 279 1 16
HELIX 42 42 LYS D 293 GLY D 304 1 12
HELIX 43 43 LYS D 307 PHE D 312 1 6
HELIX 44 44 PRO D 313 TYR D 318 5 6
HELIX 45 45 ASP D 331 SER D 352 1 22
HELIX 46 46 GLU D 370 TYR D 391 1 22
SHEET 1 AA 2 CYS A 71 ALA A 72 0
SHEET 2 AA 2 VAL A 164 ALA A 165 -1 O VAL A 164 N ALA A 72
SHEET 1 BA 2 CYS B 71 ALA B 72 0
SHEET 2 BA 2 VAL B 164 ALA B 165 -1 O VAL B 164 N ALA B 72
SHEET 1 CA 6 GLU C 209 VAL C 214 0
SHEET 2 CA 6 VAL C 217 ASP C 223 -1 O VAL C 217 N VAL C 214
SHEET 3 CA 6 HIS C 41 GLY C 47 1 O HIS C 41 N HIS C 220
SHEET 4 CA 6 ALA C 243 ASP C 249 1 O ALA C 243 N LEU C 44
SHEET 5 CA 6 SER C 286 ASN C 292 1 O SER C 286 N ILE C 244
SHEET 6 CA 6 CYS C 359 PHE C 363 1 O TYR C 360 N LEU C 289
SHEET 1 DA 6 GLU D 209 VAL D 214 0
SHEET 2 DA 6 VAL D 217 ASP D 223 -1 O VAL D 217 N VAL D 214
SHEET 3 DA 6 HIS D 41 GLY D 47 1 O HIS D 41 N HIS D 220
SHEET 4 DA 6 ALA D 243 ASP D 249 1 O ALA D 243 N LEU D 44
SHEET 5 DA 6 VAL D 287 ASN D 292 1 O ILE D 288 N PHE D 246
SHEET 6 DA 6 CYS D 359 PHE D 363 1 O TYR D 360 N LEU D 289
SSBOND 1 CYS A 71 CYS A 159 1555 1555 2.04
SSBOND 2 CYS A 74 CYS A 146 1555 1555 2.04
SSBOND 3 CYS A 77 CYS A 166 1555 1555 2.03
SSBOND 4 CYS A 259 CYS A 262 1555 1555 2.03
SSBOND 5 CYS B 71 CYS B 159 1555 1555 2.05
SSBOND 6 CYS B 74 CYS B 146 1555 1555 2.04
SSBOND 7 CYS B 77 CYS B 166 1555 1555 2.03
SSBOND 8 CYS B 259 CYS B 262 1555 1555 2.02
CRYST1 90.632 111.814 161.304 90.00 90.00 90.00 P 21 21 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 0.011034 0.000000 0.000000 0.00000
SCALE2 0.000000 0.008943 0.000000 0.00000
SCALE3 0.000000 0.000000 0.006199 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
