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Database: PDB
Entry: 3C59
LinkDB: 3C59
Original site: 3C59 
HEADER    SIGNALING PROTEIN/SIGNALING PROTEIN     31-JAN-08   3C59              
TITLE     CRYSTAL STRUCTURE OF THE LIGAND-BOUND GLUCAGON-LIKE PEPTIDE-1 RECEPTOR
TITLE    2 EXTRACELLULAR DOMAIN                                                 
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: EXENDIN-4;                                                 
COMPND   9 CHAIN: B;                                                            
COMPND  10 FRAGMENT: UNP RESIDUES 56-86;                                        
COMPND  11 SYNONYM: EXENATIDE;                                                  
COMPND  12 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GLUCAGON-LIKE PEPTIDE-1 RECEPTOR(GLP1R);                       
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET15B;                                   
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 OTHER_DETAILS: THIS PEPTIDE HAS BEEN CHEMICALLY SYNTHESIZED; THIS    
SOURCE  14 SEQUENCE OCCURS NATURALLY IN HELODERMA SUSPECTUM.                    
KEYWDS    LIGAND-BOUND G PROTEIN-COUPLED RECEPTOR, G-PROTEIN COUPLED RECEPTOR,  
KEYWDS   2 GLYCOPROTEIN, MEMBRANE, TRANSDUCER, TRANSMEMBRANE, AMIDATION,        
KEYWDS   3 CLEAVAGE ON PAIR OF BASIC RESIDUES, SECRETED, SIGNALING PROTEIN-     
KEYWDS   4 SIGNALING PROTEIN COMPLEX                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.RUNGE                                                               
REVDAT   5   23-MAY-18 3C59    1       REMARK                                   
REVDAT   4   13-JUL-11 3C59    1       VERSN                                    
REVDAT   3   24-FEB-09 3C59    1       VERSN                                    
REVDAT   2   06-MAY-08 3C59    1       JRNL                                     
REVDAT   1   19-FEB-08 3C59    0                                                
JRNL        AUTH   S.RUNGE,H.THOGERSEN,K.MADSEN,J.LAU,R.RUDOLPH                 
JRNL        TITL   CRYSTAL STRUCTURE OF THE LIGAND-BOUND GLUCAGON-LIKE          
JRNL        TITL 2 PEPTIDE-1 RECEPTOR EXTRACELLULAR DOMAIN                      
JRNL        REF    J.BIOL.CHEM.                  V. 283 11340 2008              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   18287102                                                     
JRNL        DOI    10.1074/JBC.M708740200                                       
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0040                                      
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) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 37.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 12615                          
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) : 0.199                           
REMARK   3   R VALUE            (WORKING SET) : 0.196                           
REMARK   3   FREE R VALUE                     : 0.241                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 658                             
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) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.36                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 914                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.28                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1830                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.2490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1059                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 33                                      
REMARK   3   SOLVENT ATOMS            : 105                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 54.75                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.01000                                              
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : -0.01000                                             
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): 0.180         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.174         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.103         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.491         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.933                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.904                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1130 ; 0.019 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1539 ; 1.994 ; 1.962       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   128 ;19.764 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    56 ;34.747 ;23.929       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   171 ;17.264 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;15.888 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   157 ; 0.136 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):   865 ; 0.008 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   479 ; 0.228 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):   748 ; 0.307 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    98 ; 0.164 ; 0.200       
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):    24 ; 0.206 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    12 ; 0.253 ; 0.200       
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):   669 ; 1.398 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1050 ; 2.078 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   553 ; 2.960 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   489 ; 4.576 ; 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   131                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -2.2190  49.0430   7.3580              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.2040 T22:  -0.2406                                     
REMARK   3      T33:  -0.2602 T12:   0.0312                                     
REMARK   3      T13:  -0.0438 T23:   0.0088                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.6888 L22:   3.8775                                     
REMARK   3      L33:   5.0338 L12:   0.5820                                     
REMARK   3      L13:   1.0861 L23:  -1.3784                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.3038 S12:  -0.0492 S13:   0.1225                       
REMARK   3      S21:  -0.0338 S22:   0.1273 S23:   0.1824                       
REMARK   3      S31:  -0.6874 S32:  -0.0872 S33:   0.1764                       
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     9        B    35                          
REMARK   3    ORIGIN FOR THE GROUP (A): -13.0260  34.4990   7.1020              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:  -0.3904 T22:  -0.1280                                     
REMARK   3      T33:  -0.1648 T12:  -0.1292                                     
REMARK   3      T13:  -0.0270 T23:   0.1154                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.5734 L22:  32.9234                                     
REMARK   3      L33:   6.8451 L12:   5.6583                                     
REMARK   3      L13:   3.5320 L23:   3.9685                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0318 S12:  -0.1565 S13:   0.1944                       
REMARK   3      S21:   0.0295 S22:   0.4030 S23:   1.1760                       
REMARK   3      S31:   0.2179 S32:  -0.9370 S33:  -0.3711                       
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                                                           
REMARK   4                                                                      
REMARK   4 3C59 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 04-FEB-08.                  
REMARK 100 THE DEPOSITION ID IS D_1000046357.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-OCT-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
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) : 0.9782, 0.9790, 0.96               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
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          : XDS, XSCALE                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 13273                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 40.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 5.800                              
REMARK 200  R MERGE                    (I) : 0.07400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.56100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 4.050                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: AUTOSHARP                                             
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.87                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.08                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M TRIS-HCL PH 8.5, 0.1M MGCL2, 0.4M   
REMARK 280  MGTARTRATE, 9MM N-DECYL-BETA-D-THIOMALTOSIDE, VAPOR DIFFUSION,      
REMARK 280  HANGING DROP, TEMPERATURE 293K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       29.18333            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       58.36667            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       58.36667            
REMARK 290   SMTRY1   6 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       29.18333            
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: 1350 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8830 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 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 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     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     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     PRO B    36                                                      
REMARK 465     PRO B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     SER B    39                                                      
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 131    CG   CD   NE   CZ   NH1  NH2                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   222     O    HOH A   223     3564     2.16            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    GLN A  97   N   -  CA  -  C   ANGL. DEV. =  20.6 DEGREES          
REMARK 500    ALA A 106   N   -  CA  -  C   ANGL. DEV. =  17.7 DEGREES          
REMARK 500    GLU A 107   C   -  N   -  CA  ANGL. DEV. =  15.3 DEGREES          
REMARK 500    LEU A 123   CA  -  CB  -  CG  ANGL. DEV. =  15.1 DEGREES          
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    PHE A  61      149.09   -171.90                                   
REMARK 500    ARG A  64      153.80    -48.14                                   
REMARK 500    GLU A  68      -19.48     90.54                                   
REMARK 500    GLU A 107      -51.50    129.05                                   
REMARK 500    GLN A 112      -73.26   -115.94                                   
REMARK 500    LYS A 113      -73.60    164.89                                   
REMARK 500    ASN A 115       47.86   -148.52                                   
REMARK 500    SER A 116     -164.47   -115.92                                   
REMARK 500    SER A 117     -173.29    -54.22                                   
REMARK 500    LEU A 118      125.29     89.61                                   
REMARK 500    LYS A 130     -152.05    -66.93                                   
REMARK 500    SER B  33      -81.68   -126.95                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 PRO A   96     GLN A   97                  134.86                    
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 10M A 1                   
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3C5T   RELATED DB: PDB                                   
REMARK 900 THE SAME PROTEIN IN COMPLEX WITH THE NATIVE LIGAND EXENDIN-4(9-39)   
DBREF  3C59 A   24   145  UNP    P43220   GLP1R_HUMAN     24    145             
DBREF  3C59 B    9    39  UNP    P26349   EXE4_HELSU      56     86             
SEQADV 3C59 MSE B   21  UNP  P26349    LEU    68 MODIFIED RESIDUE               
SEQRES   1 A  122  ARG PRO GLN GLY ALA THR VAL SER LEU TRP GLU THR VAL          
SEQRES   2 A  122  GLN LYS TRP ARG GLU TYR ARG ARG GLN CYS GLN ARG SER          
SEQRES   3 A  122  LEU THR GLU ASP PRO PRO PRO ALA THR ASP LEU PHE CYS          
SEQRES   4 A  122  ASN ARG THR PHE ASP GLU TYR ALA CYS TRP PRO ASP GLY          
SEQRES   5 A  122  GLU PRO GLY SER PHE VAL ASN VAL SER CYS PRO TRP TYR          
SEQRES   6 A  122  LEU PRO TRP ALA SER SER VAL PRO GLN GLY HIS VAL TYR          
SEQRES   7 A  122  ARG PHE CYS THR ALA GLU GLY LEU TRP LEU GLN LYS ASP          
SEQRES   8 A  122  ASN SER SER LEU PRO TRP ARG ASP LEU SER GLU CYS GLU          
SEQRES   9 A  122  GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU GLN          
SEQRES  10 A  122  LEU LEU PHE LEU TYR                                          
SEQRES   1 B   31  ASP LEU SER LYS GLN MSE GLU GLU GLU ALA VAL ARG MSE          
SEQRES   2 B   31  PHE ILE GLU TRP LEU LYS ASN GLY GLY PRO SER SER GLY          
SEQRES   3 B   31  ALA PRO PRO PRO SER                                          
MODRES 3C59 MSE B   14  MET  SELENOMETHIONINE                                   
MODRES 3C59 MSE B   21  MET  SELENOMETHIONINE                                   
HET    MSE  B  14       8                                                       
HET    MSE  B  21       8                                                       
HET    10M  A   1      33                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
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   2  MSE    2(C5 H11 N O2 SE)                                            
FORMUL   3  10M    C22 H42 O10 S                                                
FORMUL   4  HOH   *105(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 ASP B    9  ASN B   28  1                                  20    
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  2.17  
SSBOND   2 CYS A   62    CYS A  104                          1555   1555  2.07  
SSBOND   3 CYS A   85    CYS A  126                          1555   1555  2.03  
LINK         C   GLN B  13                 N   MSE B  14     1555   1555  1.34  
LINK         C   MSE B  14                 N   GLU B  15     1555   1555  1.33  
LINK         C   ARG B  20                 N   MSE B  21     1555   1555  1.35  
LINK         C   MSE B  21                 N   PHE B  22     1555   1555  1.33  
CISPEP   1 ALA A  106    GLU A  107          0       -18.16                     
CISPEP   2 LYS A  113    ASP A  114          0       -26.53                     
CISPEP   3 ASN A  115    SER A  116          0        10.62                     
SITE     1 AC1  7 ARG A  43  PHE A  80  ASN A  82  HIS A  99                    
SITE     2 AC1  7 TYR A 101  HOH A 155  HOH A 222                               
CRYST1   75.850   75.850   87.550  90.00  90.00 120.00 P 31 2 1      6          
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      0.013184  0.007612  0.000000        0.00000                         
SCALE2      0.000000  0.015223  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011422        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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