GenomeNet

Database: PDB
Entry: 5OTW
LinkDB: 5OTW
Original site: 5OTW 
HEADER    SIGNALING PROTEIN                       22-AUG-17   5OTW              
TITLE     EXTRACELLULAR DOMAIN OF GLP-1 RECEPTOR IN COMPLEX WITH GLP-1 VARIANT  
TITLE    2 ALA8HCS/THR11CYS                                                     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR;                          
COMPND   3 CHAIN: C, A;                                                         
COMPND   4 FRAGMENT: EXTRACELLULAR DOMAIN, UNP RESIDUES 24-139;                 
COMPND   5 SYNONYM: GLP-1R;                                                     
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: GLUCAGON;                                                  
COMPND   9 CHAIN: D, B;                                                         
COMPND  10 ENGINEERED: YES;                                                     
COMPND  11 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GLP1R;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 MOL_ID: 2;                                                           
SOURCE   9 SYNTHETIC: YES;                                                      
SOURCE  10 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  11 ORGANISM_COMMON: HUMAN;                                              
SOURCE  12 ORGANISM_TAXID: 9606                                                 
KEYWDS    GLUCAGON-LIKE PEPTIDE 1, GPCR, CYCLIC PEPTIDES, SIGNALING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MORTENSEN                                                           
REVDAT   2   25-JUL-18 5OTW    1       JRNL                                     
REVDAT   1   04-JUL-18 5OTW    0                                                
JRNL        AUTH   A.ODDO,S.MORTENSEN,H.THOGERSEN,L.DE MARIA,S.HENNEN,          
JRNL        AUTH 2 J.N.MCGUIRE,J.KOFOED,L.LINDEROTH,S.REEDTZ-RUNGE              
JRNL        TITL   ALPHA-HELIX OR BETA-TURN? AN INVESTIGATION INTO N-TERMINALLY 
JRNL        TITL 2 CONSTRAINED ANALOGUES OF GLUCAGON-LIKE PEPTIDE 1 (GLP-1) AND 
JRNL        TITL 3 EXENDIN-4.                                                   
JRNL        REF    BIOCHEMISTRY                  V.  57  4148 2018              
JRNL        REFN                   ISSN 1520-4995                               
JRNL        PMID   29877701                                                     
JRNL        DOI    10.1021/ACS.BIOCHEM.8B00105                                  
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (DEV_2689: ???)                               
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 42.25                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 15288                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.189                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.239                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.360                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2796                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 42.2606 -  5.6959    1.00     1377   153  0.1773 0.2330        
REMARK   3     2  5.6959 -  4.5227    0.98     1342   144  0.1528 0.1710        
REMARK   3     3  4.5227 -  3.9514    0.98     1356   140  0.1535 0.1653        
REMARK   3     4  3.9514 -  3.5904    0.99     1344   146  0.1515 0.2292        
REMARK   3     5  3.5904 -  3.3331    0.99     1379   134  0.1482 0.1999        
REMARK   3     6  3.3331 -  3.1367    1.00     1365   154  0.1662 0.2321        
REMARK   3     7  3.1367 -  2.9796    0.99     1351   136  0.1969 0.2785        
REMARK   3     8  2.9796 -  2.8500    1.00     1383   141  0.1873 0.2471        
REMARK   3     9  2.8500 -  2.7403    0.99     1418   141  0.1954 0.2476        
REMARK   3    10  2.7403 -  2.6457    0.99     1352   135  0.1848 0.2205        
REMARK   3    11  2.6457 -  2.5630    0.98     1346   145  0.2062 0.3383        
REMARK   3    12  2.5630 -  2.4898    0.97     1333   122  0.2010 0.2408        
REMARK   3    13  2.4898 -  2.4242    0.97     1366   147  0.2203 0.2851        
REMARK   3    14  2.4242 -  2.3651    0.98     1370   143  0.2006 0.2537        
REMARK   3    15  2.3651 -  2.3113    0.98     1283   130  0.2143 0.2832        
REMARK   3    16  2.3113 -  2.2621    0.97     1394   128  0.2314 0.3382        
REMARK   3    17  2.2621 -  2.2169    0.96     1319   154  0.2719 0.3789        
REMARK   3    18  2.2169 -  2.1751    0.98     1335   161  0.2508 0.3255        
REMARK   3    19  2.1751 -  2.1362    0.97     1330   120  0.2525 0.2666        
REMARK   3    20  2.1362 -  2.1000    0.94     1343   122  0.2977 0.3896        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.280            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 25.540           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.005           2150                                  
REMARK   3   ANGLE     :  0.723           2936                                  
REMARK   3   CHIRALITY :  0.042            291                                  
REMARK   3   PLANARITY :  0.006            377                                  
REMARK   3   DIHEDRAL  : 10.684           1231                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 4                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: (CHAIN 'A' AND RESID 29 THROUGH 128)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  38.4694   7.6415   6.1330              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1735 T22:   0.1330                                     
REMARK   3      T33:   0.1683 T12:   0.0013                                     
REMARK   3      T13:   0.0138 T23:  -0.0165                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   1.8546 L22:   1.4478                                     
REMARK   3      L33:   5.8822 L12:  -0.1628                                     
REMARK   3      L13:   0.7228 L23:   0.1215                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0399 S12:   0.0493 S13:   0.0114                       
REMARK   3      S21:  -0.0871 S22:   0.0407 S23:  -0.0442                       
REMARK   3      S31:  -0.0799 S32:   0.1686 S33:  -0.0940                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: (CHAIN 'B' AND RESID 7 THROUGH 35)                     
REMARK   3    ORIGIN FOR THE GROUP (A):  29.0140  -2.4290  25.8497              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.2445 T22:   0.2805                                     
REMARK   3      T33:   0.2634 T12:  -0.0175                                     
REMARK   3      T13:   0.0298 T23:  -0.0031                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9598 L22:   4.2344                                     
REMARK   3      L33:   6.7198 L12:   0.3680                                     
REMARK   3      L13:  -0.8617 L23:  -5.2673                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.2428 S12:   0.0837 S13:  -0.2595                       
REMARK   3      S21:   0.1710 S22:   0.2227 S23:  -0.2224                       
REMARK   3      S31:  -0.2418 S32:  -0.2938 S33:  -0.1556                       
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    SELECTION: (CHAIN 'C' AND RESID 29 THROUGH 128)                   
REMARK   3    ORIGIN FOR THE GROUP (A):  56.1492 -11.7774   2.6235              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1955 T22:   0.1479                                     
REMARK   3      T33:   0.1740 T12:   0.0009                                     
REMARK   3      T13:  -0.0054 T23:   0.0130                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.6586 L22:   2.1670                                     
REMARK   3      L33:   5.6562 L12:   0.5676                                     
REMARK   3      L13:  -1.9538 L23:   0.2346                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0458 S12:  -0.0607 S13:   0.0351                       
REMARK   3      S21:  -0.0994 S22:   0.0140 S23:   0.0436                       
REMARK   3      S31:   0.0249 S32:   0.0117 S33:  -0.0390                       
REMARK   3   TLS GROUP : 4                                                      
REMARK   3    SELECTION: (CHAIN 'D' AND RESID 10 THROUGH 35)                    
REMARK   3    ORIGIN FOR THE GROUP (A):  59.4444  -3.4531  23.6755              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1729 T22:   0.2368                                     
REMARK   3      T33:   0.1933 T12:  -0.0222                                     
REMARK   3      T13:   0.0007 T23:   0.0143                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.9660 L22:   7.2173                                     
REMARK   3      L33:   7.9542 L12:   1.0482                                     
REMARK   3      L13:   1.4928 L23:   4.2965                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1691 S12:   0.0141 S13:   0.1347                       
REMARK   3      S21:   0.2126 S22:   0.2446 S23:   0.1460                       
REMARK   3      S31:   0.1513 S32:   0.1221 S33:  -0.1538                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 5OTW COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 22-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200004580.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-X                        
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54187                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 R 1M              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15304                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 42.260                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : 5.600                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : 0.11800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.9000                            
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) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 95.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 5.53                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.98000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.900                              
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: 4ZGM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.07                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MORPHEUS FROM MOLECULAR DIMENSIONS,      
REMARK 280  SOLUTION E12: 0.12 M ETHYLENE GLYCOLS, 0.1 M BUFFER SYSTEM 3 PH     
REMARK 280  8.5, 12.5% (V/V) MPD, 12.5% (W/V) PEG1000, 12.5% (W/V) PEG3350,     
REMARK 280  VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       40.60000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8080 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -11.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1100 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8380 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 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 C    24                                                      
REMARK 465     PRO C    25                                                      
REMARK 465     GLN C    26                                                      
REMARK 465     GLY C    27                                                      
REMARK 465     ALA C    28                                                      
REMARK 465     SER C   129                                                      
REMARK 465     LYS C   130                                                      
REMARK 465     ARG C   131                                                      
REMARK 465     GLY C   132                                                      
REMARK 465     GLU C   133                                                      
REMARK 465     ARG C   134                                                      
REMARK 465     SER C   135                                                      
REMARK 465     SER C   136                                                      
REMARK 465     PRO C   137                                                      
REMARK 465     GLU C   138                                                      
REMARK 465     GLU C   139                                                      
REMARK 465     HIS D     7                                                      
REMARK 465     HCS D     8                                                      
REMARK 465     GLU D     9                                                      
REMARK 465     ARG D    36                                                      
REMARK 465     GLY D    37                                                      
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     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 C 115    CB   CG   OD1  ND2                                  
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   OD1  ASN A    63     O    HOH A   201              1.98            
REMARK 500   O    HOH A   224     O    HOH A   245              2.06            
REMARK 500   O    HOH C   249     O    HOH A   249              2.14            
REMARK 500   O    HOH C   253     O    HOH C   259              2.15            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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 C   207     O    HOH B   104     1554     1.87            
REMARK 500   O    HOH D   110     O    HOH B   113     1655     1.90            
REMARK 500   O    HOH C   259     O    HOH B   115     1654     2.06            
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 C  68      -21.28     84.49                                   
REMARK 500    ARG A  64      151.19    -47.00                                   
REMARK 500    THR A  65      146.26   -170.22                                   
REMARK 500    GLU A  68      -20.47     83.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5OTW C   24   139  UNP    P43220   GLP1R_HUMAN     24    139             
DBREF  5OTW D    7    37  UNP    P01275   GLUC_HUMAN      98    128             
DBREF  5OTW A   24   139  UNP    P43220   GLP1R_HUMAN     24    139             
DBREF  5OTW B    7    37  UNP    P01275   GLUC_HUMAN      98    128             
SEQADV 5OTW HCS D    8  UNP  P01275    ALA    99 ENGINEERED MUTATION            
SEQADV 5OTW CYS D   11  UNP  P01275    THR   102 ENGINEERED MUTATION            
SEQADV 5OTW HCS B    8  UNP  P01275    ALA    99 ENGINEERED MUTATION            
SEQADV 5OTW CYS B   11  UNP  P01275    THR   102 ENGINEERED MUTATION            
SEQRES   1 C  116  ARG PRO GLN GLY ALA THR VAL SER LEU TRP GLU THR VAL          
SEQRES   2 C  116  GLN LYS TRP ARG GLU TYR ARG ARG GLN CYS GLN ARG SER          
SEQRES   3 C  116  LEU THR GLU ASP PRO PRO PRO ALA THR ASP LEU PHE CYS          
SEQRES   4 C  116  ASN ARG THR PHE ASP GLU TYR ALA CYS TRP PRO ASP GLY          
SEQRES   5 C  116  GLU PRO GLY SER PHE VAL ASN VAL SER CYS PRO TRP TYR          
SEQRES   6 C  116  LEU PRO TRP ALA SER SER VAL PRO GLN GLY HIS VAL TYR          
SEQRES   7 C  116  ARG PHE CYS THR ALA GLU GLY LEU TRP LEU GLN LYS ASP          
SEQRES   8 C  116  ASN SER SER LEU PRO TRP ARG ASP LEU SER GLU CYS GLU          
SEQRES   9 C  116  GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU              
SEQRES   1 D   31  HIS HCS GLU GLY CYS PHE THR SER ASP VAL SER SER TYR          
SEQRES   2 D   31  LEU GLU GLY GLN ALA ALA LYS GLU PHE ILE ALA TRP LEU          
SEQRES   3 D   31  VAL LYS GLY ARG GLY                                          
SEQRES   1 A  116  ARG PRO GLN GLY ALA THR VAL SER LEU TRP GLU THR VAL          
SEQRES   2 A  116  GLN LYS TRP ARG GLU TYR ARG ARG GLN CYS GLN ARG SER          
SEQRES   3 A  116  LEU THR GLU ASP PRO PRO PRO ALA THR ASP LEU PHE CYS          
SEQRES   4 A  116  ASN ARG THR PHE ASP GLU TYR ALA CYS TRP PRO ASP GLY          
SEQRES   5 A  116  GLU PRO GLY SER PHE VAL ASN VAL SER CYS PRO TRP TYR          
SEQRES   6 A  116  LEU PRO TRP ALA SER SER VAL PRO GLN GLY HIS VAL TYR          
SEQRES   7 A  116  ARG PHE CYS THR ALA GLU GLY LEU TRP LEU GLN LYS ASP          
SEQRES   8 A  116  ASN SER SER LEU PRO TRP ARG ASP LEU SER GLU CYS GLU          
SEQRES   9 A  116  GLU SER LYS ARG GLY GLU ARG SER SER PRO GLU GLU              
SEQRES   1 B   31  HIS HCS GLU GLY CYS 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    HCS  B   8       7                                                       
HETNAM     HCS 2-AMINO-4-MERCAPTO-BUTYRIC ACID                                  
FORMUL   4  HCS    C4 H9 N O2 S                                                 
FORMUL   5  HOH   *135(H2 O)                                                    
HELIX    1 AA1 SER C   31  ASP C   53  1                                  23    
HELIX    2 AA2 TRP C   91  VAL C   95  5                                   5    
HELIX    3 AA3 LEU C  123  GLU C  127  5                                   5    
HELIX    4 AA4 PHE D   12  LYS D   34  1                                  23    
HELIX    5 AA5 SER A   31  ASP A   53  1                                  23    
HELIX    6 AA6 TRP A   91  VAL A   95  5                                   5    
HELIX    7 AA7 LEU A  123  GLU A  127  5                                   5    
HELIX    8 AA8 PHE B   12  LYS B   34  1                                  23    
SHEET    1 AA1 2 THR C  65  PHE C  66  0                                        
SHEET    2 AA1 2 CYS C  71  TRP C  72 -1  O  TRP C  72   N  THR C  65           
SHEET    1 AA2 2 SER C  79  SER C  84  0                                        
SHEET    2 AA2 2 HIS C  99  CYS C 104 -1  O  VAL C 100   N  VAL C  83           
SHEET    1 AA3 2 THR A  65  PHE A  66  0                                        
SHEET    2 AA3 2 CYS A  71  TRP A  72 -1  O  TRP A  72   N  THR A  65           
SHEET    1 AA4 2 SER A  79  SER A  84  0                                        
SHEET    2 AA4 2 HIS A  99  CYS A 104 -1  O  VAL A 100   N  VAL A  83           
SSBOND   1 CYS C   46    CYS C   71                          1555   1555  2.06  
SSBOND   2 CYS C   62    CYS C  104                          1555   1555  2.04  
SSBOND   3 CYS C   85    CYS C  126                          1555   1555  2.03  
SSBOND   4 CYS A   46    CYS A   71                          1555   1555  2.05  
SSBOND   5 CYS A   62    CYS A  104                          1555   1555  2.05  
SSBOND   6 CYS A   85    CYS A  126                          1555   1555  2.02  
SSBOND   7 HCS B    8    CYS B   11                          1555   1555  2.04  
LINK         C   HIS B   7                 N   HCS B   8     1555   1555  1.33  
LINK         C   HCS B   8                 N   GLU B   9     1555   1555  1.33  
CRYST1   39.260   81.200   42.740  90.00  98.67  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.025471  0.000000  0.003882        0.00000                         
SCALE2      0.000000  0.012315  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023667        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system