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Database: PDB
Entry: 3IOL
LinkDB: 3IOL
Original site: 3IOL 
HEADER    SIGNALING PROTEIN/SIGNALING PROTEIN     14-AUG-09   3IOL              
TITLE     CRYSTAL STRUCTURE OF GLUCAGON-LIKE PEPTIDE-1 IN COMPLEX WITH THE      
TITLE    2 EXTRACELLULAR DOMAIN OF THE GLUCAGON-LIKE PEPTIDE-1 RECEPTOR         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR;                          
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: N-TERMINAL EXTRACELLULAR DOMAIN, UNP RESIDUES 24-145;      
COMPND   5 SYNONYM: GLP-1 RECEPTOR, GLP-1-R, GLP-1R;                            
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GLUCAGON;                                                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 98-128;                                       
COMPND  11 SYNONYM: GLP-1, GLUCAGON-LIKE PEPTIDE 1, GLICENTIN, GLICENTIN-RELATED
COMPND  12 POLYPEPTIDE;                                                         
COMPND  13 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 SYNTHETIC: YES;                                                      
SOURCE  12 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  13 ORGANISM_COMMON: HUMAN;                                              
SOURCE  14 ORGANISM_TAXID: 9606;                                                
SOURCE  15 OTHER_DETAILS: THIS PEPTIDE HAS BEEN CHEMICALLY SYNTHESIZED          
KEYWDS    RECEPTOR-LIGAND COMPLEX, CELL MEMBRANE, DISULFIDE BOND, G-PROTEIN     
KEYWDS   2 COUPLED RECEPTOR, GLYCOPROTEIN, MEMBRANE, RECEPTOR, TRANSDUCER,      
KEYWDS   3 TRANSMEMBRANE, AMIDATION, CLEAVAGE ON PAIR OF BASIC RESIDUES,        
KEYWDS   4 HORMONE, SECRETED, SIGNALING PROTEIN-SIGNALING PROTEIN COMPLEX       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.REEDTZ-RUNGE                                                        
REVDAT   4   23-MAY-18 3IOL    1       REMARK                                   
REVDAT   3   13-JUL-11 3IOL    1       VERSN                                    
REVDAT   2   05-JAN-10 3IOL    1       JRNL                                     
REVDAT   1   27-OCT-09 3IOL    0                                                
JRNL        AUTH   C.R.UNDERWOOD,P.GARIBAY,L.B.KNUDSEN,S.HASTRUP,G.H.PETERS,    
JRNL        AUTH 2 R.RUDOLPH,S.REEDTZ-RUNGE                                     
JRNL        TITL   CRYSTAL STRUCTURE OF GLUCAGON-LIKE PEPTIDE-1 IN COMPLEX WITH 
JRNL        TITL 2 THE EXTRACELLULAR DOMAIN OF THE GLUCAGON-LIKE PEPTIDE-1      
JRNL        TITL 3 RECEPTOR                                                     
JRNL        REF    J.BIOL.CHEM.                  V. 285   723 2010              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   19861722                                                     
JRNL        DOI    10.1074/JBC.M109.033829                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0088                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 28.53                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 8357                           
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) : 0.181                           
REMARK   3   R VALUE            (WORKING SET) : 0.178                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 429                             
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 581                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 96.55                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1870                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 35                           
REMARK   3   BIN FREE R VALUE                    : 0.2550                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1024                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 73                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : 25.80                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.66                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 2.61000                                              
REMARK   3    B22 (A**2) : -1.42000                                             
REMARK   3    B33 (A**2) : -1.19000                                             
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): 0.204         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.177         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.130         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.679        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.947                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.914                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1074 ; 0.020 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):   742 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1466 ; 1.681 ; 1.934       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  1788 ; 1.072 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   124 ; 6.462 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    53 ;30.406 ;23.585       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   156 ;14.042 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     7 ;13.082 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   147 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1184 ; 0.008 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   235 ; 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):   629 ; 1.003 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   249 ; 0.263 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1015 ; 1.885 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   445 ; 2.859 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   448 ; 4.717 ; 4.500       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    29        A   128                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -5.9740 -16.6120  13.5130              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0249 T22:   0.0359                                     
REMARK   3      T33:   0.0053 T12:  -0.0108                                     
REMARK   3      T13:   0.0049 T23:  -0.0051                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.3386 L22:   1.8018                                     
REMARK   3      L33:   0.4454 L12:  -0.1889                                     
REMARK   3      L13:  -0.1748 L23:   0.3468                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0147 S12:   0.0236 S13:   0.0261                       
REMARK   3      S21:  -0.0322 S22:  -0.0162 S23:  -0.0010                       
REMARK   3      S31:  -0.0059 S32:   0.0315 S33:   0.0014                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B    11        B    35                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -3.6670   3.3610   3.5740              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0381 T22:   0.0499                                     
REMARK   3      T33:   0.0219 T12:  -0.0167                                     
REMARK   3      T13:   0.0031 T23:  -0.0079                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9042 L22:   9.3486                                     
REMARK   3      L33:   5.3619 L12:  -2.3283                                     
REMARK   3      L13:   1.9602 L23:  -6.9668                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0231 S12:  -0.0813 S13:   0.0030                       
REMARK   3      S21:  -0.1982 S22:  -0.0459 S23:  -0.0498                       
REMARK   3      S31:   0.1499 S32:  -0.0427 S33:   0.0227                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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                                                           
REMARK   4                                                                      
REMARK   4 3IOL COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 19-AUG-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000054669.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-NOV-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.9                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : MAX II                             
REMARK 200  BEAMLINE                       : I911-3                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10348                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 95.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY                : 7.000                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.11100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 14.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.44900                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 5.300                              
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 3C59 WITHOUT LIGAND                        
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.47                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.00                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M N-(2-ACETAMIDO) IMINODIACETIC       
REMARK 280  ACID (ADA), PH 6.9, 14 VOL-% (+/-)-2-METHYL-2,4-PENTANEDIOL (MPD)   
REMARK 280  , 9MM N-DECYL-BETA-D-THIOMALTOSIDE, VAPOR DIFFUSION, HANGING        
REMARK 280  DROP, TEMPERATURE 291K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
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,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
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       17.83500            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       47.54500            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       17.83500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       47.54500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8030 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -10.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, 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 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 O6   10M A   1  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 191  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     GLY A    20                                                      
REMARK 465     SER A    21                                                      
REMARK 465     HIS A    22                                                      
REMARK 465     MET A    23                                                      
REMARK 465     ARG A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     GLY A    27                                                      
REMARK 465     ALA A    28                                                      
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     SER A   136                                                      
REMARK 465     PRO A   137                                                      
REMARK 465     GLU A   138                                                      
REMARK 465     GLU A   139                                                      
REMARK 465     GLN A   140                                                      
REMARK 465     LEU A   141                                                      
REMARK 465     LEU A   142                                                      
REMARK 465     PHE A   143                                                      
REMARK 465     LEU A   144                                                      
REMARK 465     TYR A   145                                                      
REMARK 465     HIS B     7                                                      
REMARK 465     ALA B     8                                                      
REMARK 465     GLU B     9                                                      
REMARK 465     ARG B    36                                                      
REMARK 465     GLY B    37                                                      
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     ASN A 115    CB   CG   OD1  ND2                                  
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   O    HOH A    17     O    HOH A   188              2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    VAL A  83   CB    VAL A  83   CG2    -0.147                       
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    GLU A  68      -18.62     88.31                                   
REMARK 500    ASN A 115      -72.55     76.33                                   
REMARK 500    LYS B  34       79.54   -101.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 615                                                                      
REMARK 615 ZERO OCCUPANCY ATOM                                                  
REMARK 615 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 615 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 615 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 615 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 615   M RES C  SSEQI                                                     
REMARK 615     10M A     1                                                      
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 10M A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C59   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH THE ANTAGONIST (SEMET14,21)-        
REMARK 900 EXENDIN-4(9-39)                                                      
REMARK 900 RELATED ID: 3C5T   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH THE ANTAGONIST EXENDIN-4(9-39)      
DBREF  3IOL A   24   145  UNP    P43220   GLP1R_HUMAN     24    145             
DBREF  3IOL B    7    37  UNP    P01275   GLUC_HUMAN      98    128             
SEQADV 3IOL GLY A   20  UNP  P43220              EXPRESSION TAG                 
SEQADV 3IOL SER A   21  UNP  P43220              EXPRESSION TAG                 
SEQADV 3IOL HIS A   22  UNP  P43220              EXPRESSION TAG                 
SEQADV 3IOL MET A   23  UNP  P43220              EXPRESSION TAG                 
SEQRES   1 A  126  GLY SER HIS MET ARG PRO GLN GLY ALA THR VAL SER LEU          
SEQRES   2 A  126  TRP GLU THR VAL GLN LYS TRP ARG GLU TYR ARG ARG GLN          
SEQRES   3 A  126  CYS GLN ARG SER LEU THR GLU ASP PRO PRO PRO ALA THR          
SEQRES   4 A  126  ASP LEU PHE CYS ASN ARG THR PHE ASP GLU TYR ALA CYS          
SEQRES   5 A  126  TRP PRO ASP GLY GLU PRO GLY SER PHE VAL ASN VAL SER          
SEQRES   6 A  126  CYS PRO TRP TYR LEU PRO TRP ALA SER SER VAL PRO GLN          
SEQRES   7 A  126  GLY HIS VAL TYR ARG PHE CYS THR ALA GLU GLY LEU TRP          
SEQRES   8 A  126  LEU GLN LYS ASP ASN SER SER LEU PRO TRP ARG ASP LEU          
SEQRES   9 A  126  SER GLU CYS GLU GLU SER LYS ARG GLY GLU ARG SER SER          
SEQRES  10 A  126  PRO GLU GLU GLN LEU LEU PHE LEU TYR                          
SEQRES   1 B   31  HIS ALA GLU GLY THR PHE THR SER ASP VAL SER SER TYR          
SEQRES   2 B   31  LEU GLU GLY GLN ALA ALA LYS GLU PHE ILE ALA TRP LEU          
SEQRES   3 B   31  VAL LYS GLY ARG GLY                                          
HET    10M  A   1      33                                                       
HETNAM     10M DECYL 4-O-ALPHA-D-GLUCOPYRANOSYL-1-THIO-BETA-D-                  
HETNAM   2 10M  GLUCOPYRANOSIDE                                                 
HETSYN     10M (2R,3R,4S,5S,6R)-2-((2R,3S,4R,5R,6S)-6-DECYLSULFANYL-4,          
HETSYN   2 10M  5-DIHYDROXY-2-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3-YLOXY)-          
HETSYN   3 10M  6-HYDROXYMETHYL-TETRAHYDRO-PYRAN-3,4,5-TRIOL, N-DECYL-          
HETSYN   4 10M  BETA-D-THIOMALTOSIDE                                            
FORMUL   3  10M    C22 H42 O10 S                                                
FORMUL   4  HOH   *73(H2 O)                                                     
HELIX    1   1 SER A   31  ASP A   53  1                                  23    
HELIX    2   2 TRP A   91  VAL A   95  5                                   5    
HELIX    3   3 LEU A  123  GLU A  127  5                                   5    
HELIX    4   4 PHE B   12  LYS B   34  1                                  23    
SHEET    1   A 2 THR A  65  PHE A  66  0                                        
SHEET    2   A 2 CYS A  71  TRP A  72 -1  O  TRP A  72   N  THR A  65           
SHEET    1   B 2 SER A  79  SER A  84  0                                        
SHEET    2   B 2 HIS A  99  CYS A 104 -1  O  CYS A 104   N  SER A  79           
SSBOND   1 CYS A   46    CYS A   71                          1555   1555  2.14  
SSBOND   2 CYS A   62    CYS A  104                          1555   1555  2.06  
SSBOND   3 CYS A   85    CYS A  126                          1555   1555  1.98  
SITE     1 AC1  8 TYR A 101  LEU A 111  ASP A 114  TRP A 120                    
SITE     2 AC1  8 ASP A 122  THR B  13  VAL B  16  SER B  17                    
CRYST1   35.670   42.670   95.090  90.00  90.00  90.00 P 21 2 21     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      0.028035  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.023436  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.010516        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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