HEADER SIGNALING PROTEIN 05-APR-17 5VEX
TITLE STRUCTURE OF THE HUMAN GLP-1 RECEPTOR COMPLEX WITH NNC0640
COMPND MOL_ID: 1;
COMPND 2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR, ENDOLYSIN CHIMERA;
COMPND 3 CHAIN: A, B;
COMPND 4 SYNONYM: GLP-1R,LYSIS PROTEIN,LYSOZYME,MURAMIDASE;
COMPND 5 EC: 3.2.1.17;
COMPND 6 ENGINEERED: YES
SOURCE MOL_ID: 1;
SOURCE 2 ORGANISM_SCIENTIFIC: HOMO SAPIENS, ENTEROBACTERIA PHAGE T4;
SOURCE 3 ORGANISM_COMMON: HUMAN;
SOURCE 4 ORGANISM_TAXID: 9606, 10665;
SOURCE 5 GENE: GLP1R;
SOURCE 6 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;
SOURCE 7 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;
SOURCE 8 EXPRESSION_SYSTEM_TAXID: 7108
KEYWDS GPCR, CLASS B, 7TM DOMAIN, TREATMENT OF TYPE 2 DIABETES, SIGNALING
KEYWDS 2 PROTEIN
EXPDTA X-RAY DIFFRACTION
AUTHOR G.SONG,D.YANG,Y.WANG,C.D.GRAAF,Q.ZHOU,S.JIANG,K.LIU,X.CAI,A.DAI,
AUTHOR 2 G.LIN,D.LIU,F.WU,Y.WU,S.ZHAO,L.YE,G.W.HAN,J.LAU,B.WU,M.A.HANSON,Z.-
AUTHOR 3 J.LIU,M.-W.WANG,R.C.STEVENS
REVDAT 4 04-OCT-23 5VEX 1 REMARK
REVDAT 3 14-JUN-17 5VEX 1 JRNL
REVDAT 2 31-MAY-17 5VEX 1 JRNL
REVDAT 1 17-MAY-17 5VEX 0
JRNL AUTH G.SONG,D.YANG,Y.WANG,C.DE GRAAF,Q.ZHOU,S.JIANG,K.LIU,X.CAI,
JRNL AUTH 2 A.DAI,G.LIN,D.LIU,F.WU,Y.WU,S.ZHAO,L.YE,G.W.HAN,J.LAU,B.WU,
JRNL AUTH 3 M.A.HANSON,Z.J.LIU,M.W.WANG,R.C.STEVENS
JRNL TITL HUMAN GLP-1 RECEPTOR TRANSMEMBRANE DOMAIN STRUCTURE IN
JRNL TITL 2 COMPLEX WITH ALLOSTERIC MODULATORS.
JRNL REF NATURE V. 546 312 2017
JRNL REFN ISSN 0028-0836
JRNL PMID 28514449
JRNL DOI 10.1038/NATURE22378
REMARK 2
REMARK 2 RESOLUTION. 3.00 ANGSTROMS.
REMARK 3
REMARK 3 REFINEMENT.
REMARK 3 PROGRAM : BUSTER 2.10.2
REMARK 3 AUTHORS : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,
REMARK 3 : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,
REMARK 3 : WOMACK,MATTHEWS,TEN EYCK,TRONRUD
REMARK 3
REMARK 3 DATA USED IN REFINEMENT.
REMARK 3 RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 RESOLUTION RANGE LOW (ANGSTROMS) : 30.00
REMARK 3 DATA CUTOFF (SIGMA(F)) : 0.000
REMARK 3 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 3 NUMBER OF REFLECTIONS : 24728
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) : 0.234
REMARK 3 R VALUE (WORKING SET) : 0.233
REMARK 3 FREE R VALUE : 0.256
REMARK 3 FREE R VALUE TEST SET SIZE (%) : 4.290
REMARK 3 FREE R VALUE TEST SET COUNT : 1060
REMARK 3 ESTIMATED ERROR OF FREE R VALUE : 0.000
REMARK 3
REMARK 3 FIT IN THE HIGHEST RESOLUTION BIN.
REMARK 3 TOTAL NUMBER OF BINS USED : 12
REMARK 3 BIN RESOLUTION RANGE HIGH (ANGSTROMS) : 3.00
REMARK 3 BIN RESOLUTION RANGE LOW (ANGSTROMS) : 3.13
REMARK 3 BIN COMPLETENESS (WORKING+TEST) (%) : 87.76
REMARK 3 REFLECTIONS IN BIN (WORKING + TEST SET) : 2936
REMARK 3 BIN R VALUE (WORKING + TEST SET) : 0.2450
REMARK 3 REFLECTIONS IN BIN (WORKING SET) : 2801
REMARK 3 BIN R VALUE (WORKING SET) : 0.2430
REMARK 3 BIN FREE R VALUE : 0.2890
REMARK 3 BIN FREE R VALUE TEST SET SIZE (%) : 4.60
REMARK 3 BIN FREE R VALUE TEST SET COUNT : 135
REMARK 3 ESTIMATED ERROR OF BIN FREE R VALUE : 0.000
REMARK 3
REMARK 3 NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.
REMARK 3 PROTEIN ATOMS : 6625
REMARK 3 NUCLEIC ACID ATOMS : 0
REMARK 3 HETEROGEN ATOMS : 82
REMARK 3 SOLVENT ATOMS : 0
REMARK 3
REMARK 3 B VALUES.
REMARK 3 FROM WILSON PLOT (A**2) : 92.82
REMARK 3 MEAN B VALUE (OVERALL, A**2) : 111.7
REMARK 3 OVERALL ANISOTROPIC B VALUE.
REMARK 3 B11 (A**2) : 11.72260
REMARK 3 B22 (A**2) : -27.32620
REMARK 3 B33 (A**2) : 15.60360
REMARK 3 B12 (A**2) : -1.96770
REMARK 3 B13 (A**2) : -0.61830
REMARK 3 B23 (A**2) : 3.13450
REMARK 3
REMARK 3 ESTIMATED COORDINATE ERROR.
REMARK 3 ESD FROM LUZZATI PLOT (A) : 0.560
REMARK 3 DPI (BLOW EQ-10) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (BLOW EQ-9) BASED ON FREE R VALUE (A) : 0.389
REMARK 3 DPI (CRUICKSHANK) BASED ON R VALUE (A) : NULL
REMARK 3 DPI (CRUICKSHANK) BASED ON FREE R VALUE (A) : NULL
REMARK 3
REMARK 3 REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797
REMARK 3 CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601
REMARK 3
REMARK 3 CORRELATION COEFFICIENTS.
REMARK 3 CORRELATION COEFFICIENT FO-FC : 0.915
REMARK 3 CORRELATION COEFFICIENT FO-FC FREE : 0.901
REMARK 3
REMARK 3 NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15
REMARK 3 TERM COUNT WEIGHT FUNCTION.
REMARK 3 BOND LENGTHS : 6877 ; 2.000 ; HARMONIC
REMARK 3 BOND ANGLES : 9372 ; 2.500 ; HARMONIC
REMARK 3 TORSION ANGLES : 3056 ; 15.000 ; SINUSOIDAL
REMARK 3 TRIGONAL CARBON PLANES : 111 ; 2.000 ; HARMONIC
REMARK 3 GENERAL PLANES : 1015 ; 5.000 ; HARMONIC
REMARK 3 ISOTROPIC THERMAL FACTORS : 6877 ; 20.000 ; HARMONIC
REMARK 3 BAD NON-BONDED CONTACTS : NULL ; NULL ; NULL
REMARK 3 IMPROPER TORSIONS : NULL ; NULL ; NULL
REMARK 3 PSEUDOROTATION ANGLES : NULL ; NULL ; NULL
REMARK 3 CHIRAL IMPROPER TORSION : 910 ; 5.000 ; SEMIHARMONIC
REMARK 3 SUM OF OCCUPANCIES : NULL ; NULL ; NULL
REMARK 3 UTILITY DISTANCES : NULL ; NULL ; NULL
REMARK 3 UTILITY ANGLES : NULL ; NULL ; NULL
REMARK 3 UTILITY TORSION : NULL ; NULL ; NULL
REMARK 3 IDEAL-DIST CONTACT TERM : 8120 ; 4.000 ; SEMIHARMONIC
REMARK 3
REMARK 3 RMS DEVIATIONS FROM IDEAL VALUES.
REMARK 3 BOND LENGTHS (A) : 0.010
REMARK 3 BOND ANGLES (DEGREES) : 0.86
REMARK 3 PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.25
REMARK 3 OTHER TORSION ANGLES (DEGREES) : 1.38
REMARK 3
REMARK 3 TLS DETAILS
REMARK 3 NUMBER OF TLS GROUPS : 2
REMARK 3
REMARK 3 TLS GROUP : 1
REMARK 3 SELECTION: { A|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 6.2031 -22.8618 -27.7299
REMARK 3 T TENSOR
REMARK 3 T11: -0.3862 T22: 0.1968
REMARK 3 T33: -0.3996 T12: -0.0781
REMARK 3 T13: -0.0165 T23: -0.0359
REMARK 3 L TENSOR
REMARK 3 L11: 1.4619 L22: 1.0720
REMARK 3 L33: 4.4936 L12: 0.1438
REMARK 3 L13: -0.3774 L23: 0.2166
REMARK 3 S TENSOR
REMARK 3 S11: 0.2313 S12: -0.2453 S13: -0.0392
REMARK 3 S21: 0.0761 S22: 0.0078 S23: 0.1200
REMARK 3 S31: 0.5438 S32: 0.0765 S33: -0.2391
REMARK 3
REMARK 3 TLS GROUP : 2
REMARK 3 SELECTION: { B|* }
REMARK 3 ORIGIN FOR THE GROUP (A): 38.5580 -10.2411 -58.0396
REMARK 3 T TENSOR
REMARK 3 T11: -0.4368 T22: 0.2280
REMARK 3 T33: -0.3828 T12: 0.0089
REMARK 3 T13: 0.0645 T23: -0.0246
REMARK 3 L TENSOR
REMARK 3 L11: 1.9858 L22: 1.2224
REMARK 3 L33: 4.0745 L12: -0.0305
REMARK 3 L13: 0.9891 L23: 0.2077
REMARK 3 S TENSOR
REMARK 3 S11: 0.1915 S12: 0.1855 S13: 0.2117
REMARK 3 S21: -0.0524 S22: -0.0660 S23: 0.1148
REMARK 3 S31: -0.4703 S32: 0.0496 S33: -0.1255
REMARK 3
REMARK 3 OTHER REFINEMENT REMARKS: NULL
REMARK 4
REMARK 4 5VEX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11
REMARK 100
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-APR-17.
REMARK 100 THE DEPOSITION ID IS D_1000227312.
REMARK 200
REMARK 200 EXPERIMENTAL DETAILS
REMARK 200 EXPERIMENT TYPE : X-RAY DIFFRACTION
REMARK 200 DATE OF DATA COLLECTION : 30-NOV-16
REMARK 200 TEMPERATURE (KELVIN) : 77
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 : BL41XU
REMARK 200 X-RAY GENERATOR MODEL : NULL
REMARK 200 MONOCHROMATIC OR LAUE (M/L) : M
REMARK 200 WAVELENGTH OR RANGE (A) : 1.0000
REMARK 200 MONOCHROMATOR : NULL
REMARK 200 OPTICS : NULL
REMARK 200
REMARK 200 DETECTOR TYPE : CCD
REMARK 200 DETECTOR MANUFACTURER : RAYONIX MX225HE
REMARK 200 INTENSITY-INTEGRATION SOFTWARE : XDS
REMARK 200 DATA SCALING SOFTWARE : XDS
REMARK 200
REMARK 200 NUMBER OF UNIQUE REFLECTIONS : 24745
REMARK 200 RESOLUTION RANGE HIGH (A) : 3.000
REMARK 200 RESOLUTION RANGE LOW (A) : 50.000
REMARK 200 REJECTION CRITERIA (SIGMA(I)) : NULL
REMARK 200
REMARK 200 OVERALL.
REMARK 200 COMPLETENESS FOR RANGE (%) : 91.4
REMARK 200 DATA REDUNDANCY : 2.900
REMARK 200 R MERGE (I) : 0.13000
REMARK 200 R SYM (I) : NULL
REMARK 200 <I/SIGMA(I)> FOR THE DATA SET : 5.0000
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) : 3.16
REMARK 200 COMPLETENESS FOR SHELL (%) : 87.7
REMARK 200 DATA REDUNDANCY IN SHELL : 2.30
REMARK 200 R MERGE FOR SHELL (I) : 0.60000
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: PDB 5EE7 AND 212L
REMARK 200
REMARK 200 REMARK: NULL
REMARK 280
REMARK 280 CRYSTAL
REMARK 280 SOLVENT CONTENT, VS (%): 62.92
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.32
REMARK 280
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.4-0.45 M AMMONIUM ACETATE, 0.1 M
REMARK 280 SODIUM ACETATE, PH 5.0-5.8, 38-40% PEG400, LIPIDIC CUBIC PHASE,
REMARK 280 TEMPERATURE 293K
REMARK 290
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1
REMARK 290
REMARK 290 SYMOP SYMMETRY
REMARK 290 NNNMMM OPERATOR
REMARK 290 1555 X,Y,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
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 300 REMARK: THE AUTHORS STATE THAT THE BIOLOGICAL UNIT IS UNKNOWN.
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
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 350
REMARK 350 BIOMOLECULE: 2
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC
REMARK 350 SOFTWARE USED: PISA
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B
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 SER A 127
REMARK 465 GLU A 128
REMARK 465 SER A 129
REMARK 465 LYS A 130
REMARK 465 ARG A 131
REMARK 465 GLY A 132
REMARK 465 GLU A 133
REMARK 465 ARG A 134
REMARK 465 SER A 135
REMARK 465 MET A 211
REMARK 465 GLY A 212
REMARK 465 SER A 213
REMARK 465 GLY A 214
REMARK 465 ASP A 215
REMARK 465 GLY A 216
REMARK 465 LEU A 217
REMARK 465 GLU A 373
REMARK 465 HIS A 374
REMARK 465 ALA A 375
REMARK 465 ARG A 376
REMARK 465 GLY A 377
REMARK 465 THR A 378
REMARK 465 LEU A 379
REMARK 465 GLU A 423
REMARK 465 HIS A 424
REMARK 465 LEU A 425
REMARK 465 HIS A 426
REMARK 465 ILE A 427
REMARK 465 GLN A 428
REMARK 465 ARG A 429
REMARK 465 ASP A 430
REMARK 465 SER A 431
REMARK 465 SER B 127
REMARK 465 GLU B 128
REMARK 465 SER B 129
REMARK 465 LYS B 130
REMARK 465 ARG B 131
REMARK 465 GLY B 132
REMARK 465 GLU B 133
REMARK 465 ARG B 134
REMARK 465 SER B 135
REMARK 465 MET B 211
REMARK 465 GLY B 212
REMARK 465 SER B 213
REMARK 465 GLY B 214
REMARK 465 ASP B 215
REMARK 465 GLY B 216
REMARK 465 LEU B 217
REMARK 465 GLU B 373
REMARK 465 HIS B 374
REMARK 465 ALA B 375
REMARK 465 ARG B 376
REMARK 465 GLY B 377
REMARK 465 THR B 378
REMARK 465 LEU B 379
REMARK 465 GLU B 423
REMARK 465 HIS B 424
REMARK 465 LEU B 425
REMARK 465 HIS B 426
REMARK 465 ILE B 427
REMARK 465 GLN B 428
REMARK 465 ARG B 429
REMARK 465 ASP B 430
REMARK 465 SER B 431
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 SER A 136 OG
REMARK 470 GLU A 138 CG CD OE1 OE2
REMARK 470 GLN A 140 CG CD OE1 NE2
REMARK 470 LEU A 141 CG CD1 CD2
REMARK 470 LEU A 142 CG CD1 CD2
REMARK 470 ARG A 170 CG CD NE CZ NH1 NH2
REMARK 470 TRP A 203 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP A 203 CZ3 CH2
REMARK 470 GLN A 221 CG CD OE1 NE2
REMARK 470 ARG A1008 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1019 CG CD CE NZ
REMARK 470 THR A1021 OG1 CG2
REMARK 470 LYS A1043 CG CD CE NZ
REMARK 470 GLU A1045 CG CD OE1 OE2
REMARK 470 ASP A1047 CG OD1 OD2
REMARK 470 ARG A1052 CG CD NE CZ NH1 NH2
REMARK 470 LEU A1066 CG CD1 CD2
REMARK 470 ASP A1072 CG OD1 OD2
REMARK 470 ARG A1080 CG CD NE CZ NH1 NH2
REMARK 470 LYS A1083 CG CD CE NZ
REMARK 470 GLU A1108 CG CD OE1 OE2
REMARK 470 LYS A1147 CG CD CE NZ
REMARK 470 GLN A 263 CG CD OE1 NE2
REMARK 470 GLU A 294 CG CD OE1 OE2
REMARK 470 THR A 298 OG1 CG2
REMARK 470 ARG A 299 CG CD NE CZ NH1 NH2
REMARK 470 ASN A 300 CG OD1 ND2
REMARK 470 SER A 301 OG
REMARK 470 VAL A 370 CG1 CG2
REMARK 470 MET A 371 CG SD CE
REMARK 470 ASP A 372 CG OD1 OD2
REMARK 470 ARG A 380 CG CD NE CZ NH1 NH2
REMARK 470 PHE A 381 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS A 383 CG CD CE NZ
REMARK 470 PHE A 385 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG A 414 CG CD NE CZ NH1 NH2
REMARK 470 ARG A 421 CG CD NE CZ NH1 NH2
REMARK 470 LEU A 422 CG CD1 CD2
REMARK 470 SER B 136 OG
REMARK 470 GLN B 140 CG CD OE1 NE2
REMARK 470 LEU B 141 CG CD1 CD2
REMARK 470 LEU B 142 CG CD1 CD2
REMARK 470 ARG B 170 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 192 CG CD1 CD2
REMARK 470 TRP B 203 CG CD1 CD2 NE1 CE2 CE3 CZ2
REMARK 470 TRP B 203 CZ3 CH2
REMARK 470 LEU B 218 CG CD1 CD2
REMARK 470 SER B 219 OG
REMARK 470 GLN B 221 CG CD OE1 NE2
REMARK 470 ASP B 222 CG OD1 OD2
REMARK 470 ARG B1008 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1019 CG CD CE NZ
REMARK 470 THR B1021 OG1 CG2
REMARK 470 LYS B1043 CG CD CE NZ
REMARK 470 GLU B1045 CG CD OE1 OE2
REMARK 470 ASP B1047 CG OD1 OD2
REMARK 470 ARG B1052 CG CD NE CZ NH1 NH2
REMARK 470 LEU B1066 CG CD1 CD2
REMARK 470 ASP B1072 CG OD1 OD2
REMARK 470 ARG B1080 CG CD NE CZ NH1 NH2
REMARK 470 LYS B1083 CG CD CE NZ
REMARK 470 GLU B1108 CG CD OE1 OE2
REMARK 470 LYS B1147 CG CD CE NZ
REMARK 470 GLU B 294 CG CD OE1 OE2
REMARK 470 THR B 298 OG1 CG2
REMARK 470 ASN B 300 CG OD1 ND2
REMARK 470 MET B 371 CG SD CE
REMARK 470 ASP B 372 CG OD1 OD2
REMARK 470 ARG B 380 CG CD NE CZ NH1 NH2
REMARK 470 PHE B 381 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 LYS B 383 CG CD CE NZ
REMARK 470 PHE B 385 CG CD1 CD2 CE1 CE2 CZ
REMARK 470 ARG B 414 CG CD NE CZ NH1 NH2
REMARK 470 ARG B 421 CG CD NE CZ NH1 NH2
REMARK 470 LEU B 422 CG CD1 CD2
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 A1033 -87.12 -109.32
REMARK 500 ASN A1055 -40.77 73.14
REMARK 500 LYS A1135 38.10 -88.94
REMARK 500 TYR A 291 -69.49 -127.83
REMARK 500 ASN A 302 -83.56 -148.81
REMARK 500 MET A 303 -156.24 -128.57
REMARK 500 ASN A 304 -7.02 -59.68
REMARK 500 ILE A 309 -23.20 -142.98
REMARK 500 PHE A 367 53.97 -100.85
REMARK 500 PHE A 369 57.38 -119.19
REMARK 500 MET A 371 -60.49 -90.84
REMARK 500 CYS A 403 -66.35 -151.60
REMARK 500 LEU B1033 -86.54 -109.22
REMARK 500 ASN B1055 -40.84 73.14
REMARK 500 LYS B1135 38.23 -88.94
REMARK 500 GLU B 292 -104.48 -130.06
REMARK 500 ASP B 293 90.79 70.02
REMARK 500 ASN B 302 -86.73 -131.84
REMARK 500 MET B 303 -145.69 -132.45
REMARK 500 ASN B 304 2.77 -61.05
REMARK 500 PHE B 367 54.28 -100.67
REMARK 500 PHE B 369 56.76 -119.63
REMARK 500 CYS B 403 -66.45 -151.59
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 97V A 1201
REMARK 800
REMARK 800 SITE_IDENTIFIER: AC2
REMARK 800 EVIDENCE_CODE: SOFTWARE
REMARK 800 SITE_DESCRIPTION: binding site for residue 97V B 1201
REMARK 900
REMARK 900 RELATED ENTRIES
REMARK 900 RELATED ID: 5VEW RELATED DB: PDB
DBREF 5VEX A 128 257 UNP P43220 GLP1R_HUMAN 128 257
DBREF 5VEX A 1002 1161 UNP P00720 ENLYS_BPT4 2 161
DBREF 5VEX A 261 431 UNP P43220 GLP1R_HUMAN 261 431
DBREF 5VEX B 128 257 UNP P43220 GLP1R_HUMAN 128 257
DBREF 5VEX B 1002 1161 UNP P00720 ENLYS_BPT4 2 161
DBREF 5VEX B 261 431 UNP P43220 GLP1R_HUMAN 261 431
SEQADV 5VEX SER A 127 UNP P43220 EXPRESSION TAG
SEQADV 5VEX CYS A 193 UNP P43220 SER 193 ENGINEERED MUTATION
SEQADV 5VEX PHE A 196 UNP P43220 ILE 196 ENGINEERED MUTATION
SEQADV 5VEX GLY A 212 UNP P43220 TYR 205 LINKER
SEQADV 5VEX A UNP P43220 THR 207 DELETION
SEQADV 5VEX A UNP P43220 ALA 208 DELETION
SEQADV 5VEX A UNP P43220 ALA 209 DELETION
SEQADV 5VEX A UNP P43220 GLN 210 DELETION
SEQADV 5VEX A UNP P43220 GLN 211 DELETION
SEQADV 5VEX A UNP P43220 HIS 212 DELETION
SEQADV 5VEX A UNP P43220 GLN 213 DELETION
SEQADV 5VEX GLY A 214 UNP P43220 TRP 214 LINKER
SEQADV 5VEX ALA A 225 UNP P43220 SER 225 ENGINEERED MUTATION
SEQADV 5VEX CSD A 233 UNP P43220 MET 233 ENGINEERED MUTATION
SEQADV 5VEX GLY A 1012 UNP P00720 ARG 12 ENGINEERED MUTATION
SEQADV 5VEX THR A 1054 UNP P00720 CYS 54 ENGINEERED MUTATION
SEQADV 5VEX ALA A 1097 UNP P00720 CYS 97 ENGINEERED MUTATION
SEQADV 5VEX ARG A 1137 UNP P00720 ILE 137 ENGINEERED MUTATION
SEQADV 5VEX ALA A 271 UNP P43220 SER 271 ENGINEERED MUTATION
SEQADV 5VEX CYS A 317 UNP P43220 ILE 317 ENGINEERED MUTATION
SEQADV 5VEX ILE A 318 UNP P43220 GLY 318 ENGINEERED MUTATION
SEQADV 5VEX ALA A 346 UNP P43220 LYS 346 ENGINEERED MUTATION
SEQADV 5VEX PHE A 347 UNP P43220 CYS 347 ENGINEERED MUTATION
SEQADV 5VEX CYS A 361 UNP P43220 GLY 361 ENGINEERED MUTATION
SEQADV 5VEX SER B 127 UNP P43220 EXPRESSION TAG
SEQADV 5VEX CYS B 193 UNP P43220 SER 193 ENGINEERED MUTATION
SEQADV 5VEX PHE B 196 UNP P43220 ILE 196 ENGINEERED MUTATION
SEQADV 5VEX GLY B 212 UNP P43220 TYR 205 LINKER
SEQADV 5VEX B UNP P43220 THR 207 DELETION
SEQADV 5VEX B UNP P43220 ALA 208 DELETION
SEQADV 5VEX B UNP P43220 ALA 209 DELETION
SEQADV 5VEX B UNP P43220 GLN 210 DELETION
SEQADV 5VEX B UNP P43220 GLN 211 DELETION
SEQADV 5VEX B UNP P43220 HIS 212 DELETION
SEQADV 5VEX B UNP P43220 GLN 213 DELETION
SEQADV 5VEX GLY B 214 UNP P43220 TRP 214 LINKER
SEQADV 5VEX ALA B 225 UNP P43220 SER 225 ENGINEERED MUTATION
SEQADV 5VEX CSD B 233 UNP P43220 MET 233 ENGINEERED MUTATION
SEQADV 5VEX GLY B 1012 UNP P00720 ARG 12 ENGINEERED MUTATION
SEQADV 5VEX THR B 1054 UNP P00720 CYS 54 ENGINEERED MUTATION
SEQADV 5VEX ALA B 1097 UNP P00720 CYS 97 ENGINEERED MUTATION
SEQADV 5VEX ARG B 1137 UNP P00720 ILE 137 ENGINEERED MUTATION
SEQADV 5VEX ALA B 271 UNP P43220 SER 271 ENGINEERED MUTATION
SEQADV 5VEX CYS B 317 UNP P43220 ILE 317 ENGINEERED MUTATION
SEQADV 5VEX ILE B 318 UNP P43220 GLY 318 ENGINEERED MUTATION
SEQADV 5VEX ALA B 346 UNP P43220 LYS 346 ENGINEERED MUTATION
SEQADV 5VEX PHE B 347 UNP P43220 CYS 347 ENGINEERED MUTATION
SEQADV 5VEX CYS B 361 UNP P43220 GLY 361 ENGINEERED MUTATION
SEQRES 1 A 455 SER GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU
SEQRES 2 A 455 GLN LEU LEU PHE LEU TYR ILE ILE TYR THR VAL GLY TYR
SEQRES 3 A 455 ALA LEU SER PHE SER ALA LEU VAL ILE ALA SER ALA ILE
SEQRES 4 A 455 LEU LEU GLY PHE ARG HIS LEU HIS CYS THR ARG ASN TYR
SEQRES 5 A 455 ILE HIS LEU ASN LEU PHE ALA SER PHE ILE LEU ARG ALA
SEQRES 6 A 455 LEU CYS VAL PHE PHE LYS ASP ALA ALA LEU LYS TRP MET
SEQRES 7 A 455 GLY SER GLY ASP GLY LEU LEU SER TYR GLN ASP SER LEU
SEQRES 8 A 455 ALA CYS ARG LEU VAL PHE LEU LEU CSD GLN TYR CYS VAL
SEQRES 9 A 455 ALA ALA ASN TYR TYR TRP LEU LEU VAL GLU GLY VAL TYR
SEQRES 10 A 455 LEU TYR THR LEU LEU ALA PHE ASN ILE PHE GLU MET LEU
SEQRES 11 A 455 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP
SEQRES 12 A 455 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU
SEQRES 13 A 455 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU
SEQRES 14 A 455 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR
SEQRES 15 A 455 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP
SEQRES 16 A 455 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS
SEQRES 17 A 455 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA
SEQRES 18 A 455 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL
SEQRES 19 A 455 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS
SEQRES 20 A 455 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG
SEQRES 21 A 455 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE
SEQRES 22 A 455 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR SER GLU
SEQRES 23 A 455 GLN TRP ILE PHE ARG LEU TYR VAL ALA ILE GLY TRP GLY
SEQRES 24 A 455 VAL PRO LEU LEU PHE VAL VAL PRO TRP GLY ILE VAL LYS
SEQRES 25 A 455 TYR LEU TYR GLU ASP GLU GLY CYS TRP THR ARG ASN SER
SEQRES 26 A 455 ASN MET ASN TYR TRP LEU ILE ILE ARG LEU PRO ILE LEU
SEQRES 27 A 455 PHE ALA CYS ILE VAL ASN PHE LEU ILE PHE VAL ARG VAL
SEQRES 28 A 455 ILE CYS ILE VAL VAL SER LYS LEU LYS ALA ASN LEU MET
SEQRES 29 A 455 CYS LYS THR ASP ILE ALA PHE ARG LEU ALA LYS SER THR
SEQRES 30 A 455 LEU THR LEU ILE PRO LEU LEU CYS THR HIS GLU VAL ILE
SEQRES 31 A 455 PHE ALA PHE VAL MET ASP GLU HIS ALA ARG GLY THR LEU
SEQRES 32 A 455 ARG PHE ILE LYS LEU PHE THR GLU LEU SER PHE THR SER
SEQRES 33 A 455 PHE GLN GLY LEU MET VAL ALA ILE LEU TYR CYS PHE VAL
SEQRES 34 A 455 ASN ASN GLU VAL GLN LEU GLU PHE ARG LYS SER TRP GLU
SEQRES 35 A 455 ARG TRP ARG LEU GLU HIS LEU HIS ILE GLN ARG ASP SER
SEQRES 1 B 455 SER GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU
SEQRES 2 B 455 GLN LEU LEU PHE LEU TYR ILE ILE TYR THR VAL GLY TYR
SEQRES 3 B 455 ALA LEU SER PHE SER ALA LEU VAL ILE ALA SER ALA ILE
SEQRES 4 B 455 LEU LEU GLY PHE ARG HIS LEU HIS CYS THR ARG ASN TYR
SEQRES 5 B 455 ILE HIS LEU ASN LEU PHE ALA SER PHE ILE LEU ARG ALA
SEQRES 6 B 455 LEU CYS VAL PHE PHE LYS ASP ALA ALA LEU LYS TRP MET
SEQRES 7 B 455 GLY SER GLY ASP GLY LEU LEU SER TYR GLN ASP SER LEU
SEQRES 8 B 455 ALA CYS ARG LEU VAL PHE LEU LEU CSD GLN TYR CYS VAL
SEQRES 9 B 455 ALA ALA ASN TYR TYR TRP LEU LEU VAL GLU GLY VAL TYR
SEQRES 10 B 455 LEU TYR THR LEU LEU ALA PHE ASN ILE PHE GLU MET LEU
SEQRES 11 B 455 ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP
SEQRES 12 B 455 THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU
SEQRES 13 B 455 THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU
SEQRES 14 B 455 ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR
SEQRES 15 B 455 LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP
SEQRES 16 B 455 ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS
SEQRES 17 B 455 PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA
SEQRES 18 B 455 LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL
SEQRES 19 B 455 ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS
SEQRES 20 B 455 ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG
SEQRES 21 B 455 TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE
SEQRES 22 B 455 THR THR PHE ARG THR GLY THR TRP ASP ALA TYR SER GLU
SEQRES 23 B 455 GLN TRP ILE PHE ARG LEU TYR VAL ALA ILE GLY TRP GLY
SEQRES 24 B 455 VAL PRO LEU LEU PHE VAL VAL PRO TRP GLY ILE VAL LYS
SEQRES 25 B 455 TYR LEU TYR GLU ASP GLU GLY CYS TRP THR ARG ASN SER
SEQRES 26 B 455 ASN MET ASN TYR TRP LEU ILE ILE ARG LEU PRO ILE LEU
SEQRES 27 B 455 PHE ALA CYS ILE VAL ASN PHE LEU ILE PHE VAL ARG VAL
SEQRES 28 B 455 ILE CYS ILE VAL VAL SER LYS LEU LYS ALA ASN LEU MET
SEQRES 29 B 455 CYS LYS THR ASP ILE ALA PHE ARG LEU ALA LYS SER THR
SEQRES 30 B 455 LEU THR LEU ILE PRO LEU LEU CYS THR HIS GLU VAL ILE
SEQRES 31 B 455 PHE ALA PHE VAL MET ASP GLU HIS ALA ARG GLY THR LEU
SEQRES 32 B 455 ARG PHE ILE LYS LEU PHE THR GLU LEU SER PHE THR SER
SEQRES 33 B 455 PHE GLN GLY LEU MET VAL ALA ILE LEU TYR CYS PHE VAL
SEQRES 34 B 455 ASN ASN GLU VAL GLN LEU GLU PHE ARG LYS SER TRP GLU
SEQRES 35 B 455 ARG TRP ARG LEU GLU HIS LEU HIS ILE GLN ARG ASP SER
HET CSD A 233 8
HET CSD B 233 8
HET 97V A1201 41
HET 97V B1201 41
HETNAM CSD 3-SULFINOALANINE
HETNAM 97V 4-{[(4-CYCLOHEXYLPHENYL){[3-(METHYLSULFONYL)
HETNAM 2 97V PHENYL]CARBAMOYL}AMINO]METHYL}-N-(1H-TETRAZOL-5-YL)
HETNAM 3 97V BENZAMIDE
HETSYN CSD S-CYSTEINESULFINIC ACID; S-SULFINOCYSTEINE
FORMUL 1 CSD 2(C3 H7 N O4 S)
FORMUL 3 97V 2(C29 H31 N7 O4 S)
HELIX 1 AA1 SER A 136 PHE A 169 1 34
HELIX 2 AA2 ARG A 170 HIS A 173 5 4
HELIX 3 AA3 CYS A 174 ALA A 200 1 27
HELIX 4 AA4 SER A 223 PHE A 257 1 35
HELIX 5 AA5 ASN A 1002 GLU A 1011 1 10
HELIX 6 AA6 SER A 1038 GLY A 1051 1 14
HELIX 7 AA7 THR A 1059 ASN A 1081 1 23
HELIX 8 AA8 LEU A 1084 LEU A 1091 1 8
HELIX 9 AA9 ASP A 1092 MET A 1106 1 15
HELIX 10 AB1 GLY A 1107 ALA A 1112 1 6
HELIX 11 AB2 PHE A 1114 GLN A 1123 1 10
HELIX 12 AB3 ARG A 1125 LYS A 1135 1 11
HELIX 13 AB4 SER A 1136 THR A 1142 1 7
HELIX 14 AB5 THR A 1142 GLY A 1156 1 15
HELIX 15 AB6 TRP A 1158 SER A 261 5 5
HELIX 16 AB7 GLU A 262 TRP A 274 1 13
HELIX 17 AB8 TRP A 274 TYR A 291 1 18
HELIX 18 AB9 MET A 303 TYR A 305 5 3
HELIX 19 AC1 TRP A 306 ALA A 337 1 32
HELIX 20 AC2 ASP A 344 CYS A 361 1 18
HELIX 21 AC3 CYS A 361 PHE A 367 1 7
HELIX 22 AC4 PHE A 381 PHE A 385 1 5
HELIX 23 AC5 THR A 386 PHE A 393 1 8
HELIX 24 AC6 PHE A 393 CYS A 403 1 11
HELIX 25 AC7 ASN A 406 LEU A 422 1 17
HELIX 26 AC8 PRO B 137 PHE B 169 1 33
HELIX 27 AC9 ARG B 170 HIS B 173 5 4
HELIX 28 AD1 CYS B 174 ALA B 200 1 27
HELIX 29 AD2 SER B 223 PHE B 257 1 35
HELIX 30 AD3 ASN B 1002 GLU B 1011 1 10
HELIX 31 AD4 SER B 1038 GLY B 1051 1 14
HELIX 32 AD5 THR B 1059 ASN B 1081 1 23
HELIX 33 AD6 LEU B 1084 LEU B 1091 1 8
HELIX 34 AD7 ASP B 1092 MET B 1106 1 15
HELIX 35 AD8 GLY B 1107 ALA B 1112 1 6
HELIX 36 AD9 PHE B 1114 GLN B 1123 1 10
HELIX 37 AE1 ARG B 1125 LYS B 1135 1 11
HELIX 38 AE2 SER B 1136 THR B 1142 1 7
HELIX 39 AE3 THR B 1142 GLY B 1156 1 15
HELIX 40 AE4 TRP B 1158 SER B 261 5 5
HELIX 41 AE5 GLU B 262 TRP B 274 1 13
HELIX 42 AE6 TRP B 274 GLU B 292 1 19
HELIX 43 AE7 MET B 303 TYR B 305 5 3
HELIX 44 AE8 TRP B 306 ALA B 337 1 32
HELIX 45 AE9 ASP B 344 CYS B 361 1 18
HELIX 46 AF1 CYS B 361 PHE B 367 1 7
HELIX 47 AF2 PHE B 381 PHE B 385 1 5
HELIX 48 AF3 THR B 386 PHE B 393 1 8
HELIX 49 AF4 PHE B 393 CYS B 403 1 11
HELIX 50 AF5 ASN B 406 LEU B 422 1 17
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 LEU A1032 -1 O HIS A1031 N ILE A1027
SHEET 1 AA2 3 ARG B1014 LYS B1019 0
SHEET 2 AA2 3 TYR B1025 GLY B1028 -1 O THR B1026 N TYR B1018
SHEET 3 AA2 3 HIS B1031 LEU B1032 -1 O HIS B1031 N ILE B1027
SSBOND 1 CYS A 226 CYS A 296 1555 1555 2.03
SSBOND 2 CYS A 317 CYS A 361 1555 1555 2.06
SSBOND 3 CYS B 226 CYS B 296 1555 1555 2.03
SSBOND 4 CYS B 317 CYS B 361 1555 1555 2.05
LINK C LEU A 232 N CSD A 233 1555 1555 1.36
LINK C CSD A 233 N GLN A 234 1555 1555 1.36
LINK C LEU B 232 N CSD B 233 1555 1555 1.36
LINK C CSD B 233 N GLN B 234 1555 1555 1.36
SITE 1 AC1 9 PHE A 347 ARG A 348 LYS A 351 SER A 352
SITE 2 AC1 9 LEU A 354 THR A 355 LEU A 401 VAL A 405
SITE 3 AC1 9 ASN A 406
SITE 1 AC2 8 PHE B 347 ARG B 348 LYS B 351 SER B 352
SITE 2 AC2 8 THR B 355 LEU B 401 VAL B 405 ASN B 406
CRYST1 64.810 67.510 83.660 91.55 89.88 107.56 P 1 2
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 0.015430 0.004883 0.000103 0.00000
SCALE2 0.000000 0.015537 0.000431 0.00000
SCALE3 0.000000 0.000000 0.011958 0.00000
(ATOM LINES ARE NOT SHOWN.)
END
