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Database: PDB
Entry: 5OTT
LinkDB: 5OTT
Original site: 5OTT 
HEADER    SIGNALING PROTEIN                       22-AUG-17   5OTT              
TITLE     EXTRACELLULAR DOMAIN OF GLP-1 RECEPTOR IN COMPLEX WITH EXENDIN-4      
TITLE    2 VARIANT GLY2HCS/THR5HCS                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: GLUCAGON-LIKE PEPTIDE 1 RECEPTOR;                          
COMPND   3 CHAIN: 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: EXENDIN-4;                                                 
COMPND   9 CHAIN: 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: HELODERMA SUSPECTUM;                            
SOURCE  11 ORGANISM_COMMON: GILA MONSTER;                                       
SOURCE  12 ORGANISM_TAXID: 8554                                                 
KEYWDS    GLUCAGON-LIKE PEPTIDE 1, GPCR, CYCLIC PEPTIDES, SIGNALING PROTEIN     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.MORTENSEN                                                           
REVDAT   2   25-JUL-18 5OTT    1       JRNL                                     
REVDAT   1   04-JUL-18 5OTT    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.    1.92 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) : 1.92                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.38                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 15001                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.182                           
REMARK   3   R VALUE            (WORKING SET) : 0.180                           
REMARK   3   FREE R VALUE                     : 0.209                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.560                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2704                            
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 47.3963 -  5.1213    1.00     1366   141  0.1961 0.2030        
REMARK   3     2  5.1213 -  4.0657    0.98     1350   136  0.1585 0.1812        
REMARK   3     3  4.0657 -  3.5519    0.98     1315   140  0.1566 0.1817        
REMARK   3     4  3.5519 -  3.2273    0.98     1332   144  0.1610 0.1882        
REMARK   3     5  3.2273 -  2.9960    0.99     1336   140  0.1788 0.2274        
REMARK   3     6  2.9960 -  2.8194    1.00     1371   149  0.1898 0.2080        
REMARK   3     7  2.8194 -  2.6782    0.99     1353   142  0.1799 0.2191        
REMARK   3     8  2.6782 -  2.5616    1.00     1341   144  0.1703 0.2166        
REMARK   3     9  2.5616 -  2.4630    0.99     1351   142  0.1713 0.1868        
REMARK   3    10  2.4630 -  2.3780    1.00     1365   142  0.1743 0.2046        
REMARK   3    11  2.3780 -  2.3037    1.00     1356   140  0.1785 0.2468        
REMARK   3    12  2.3037 -  2.2378    1.00     1338   145  0.1887 0.2318        
REMARK   3    13  2.2378 -  2.1789    1.00     1357   146  0.1638 0.1720        
REMARK   3    14  2.1789 -  2.1257    0.99     1346   142  0.1889 0.2277        
REMARK   3    15  2.1257 -  2.0774    1.00     1347   147  0.1869 0.2369        
REMARK   3    16  2.0774 -  2.0332    0.99     1362   146  0.2106 0.2247        
REMARK   3    17  2.0332 -  1.9925    1.00     1334   140  0.1956 0.2467        
REMARK   3    18  1.9925 -  1.9549    0.97     1347   142  0.2282 0.2734        
REMARK   3    19  1.9549 -  1.9200    0.97     1308   136  0.3435 0.3438        
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)     : 0.170            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.350           
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      :  0.015           1132                                  
REMARK   3   ANGLE     :  1.253           1542                                  
REMARK   3   CHIRALITY :  0.070            151                                  
REMARK   3   PLANARITY :  0.009            201                                  
REMARK   3   DIHEDRAL  :  7.852            660                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
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 5OTT 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_1200004586.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-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   : 15019                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.920                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 47.382                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY                : 12.90                              
REMARK 200  R MERGE                    (I) : 0.10300                            
REMARK 200  R SYM                      (I) : 0.10800                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 19.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.92                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.66                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.14500                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.300                              
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: 4ZGM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.53                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.71                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M IMIDAZOLE PH 6.5, 1.0 M SODIUM     
REMARK 280  ACETATE TRIHYDRATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE      
REMARK 280  293K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  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       25.84500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.46000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       59.27500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       25.84500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.46000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       59.27500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       25.84500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       31.46000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       59.27500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       25.84500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       31.46000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       59.27500            
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: 1310 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 8830 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -12.0 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      HOH A 282  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B 111  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     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     THR A    29                                                      
REMARK 465     ALA A    57                                                      
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     HIS B     1                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     SER B    39                                                      
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   N    HCS B     2     O    HOH B   101              1.95            
REMARK 500   OE1  GLN A    37     O    HOH A   201              1.96            
REMARK 500   O    HOH A   290     O    HOH A   297              2.11            
REMARK 500   O    HOH A   232     O    HOH A   277              2.17            
REMARK 500   OE1  GLN A    47     O    HOH A   202              2.18            
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 A   245     O    HOH A   266     8444     2.01            
REMARK 500   O    HOH A   246     O    HOH A   273     2555     2.07            
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      -19.43     83.38                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  5OTT A   24   139  UNP    P43220   GLP1R_HUMAN     24    139             
DBREF  5OTT B    1    39  UNP    P26349   EXE4_HELSU      48     86             
SEQADV 5OTT HCS B    2  UNP  P26349    GLY    49 ENGINEERED MUTATION            
SEQADV 5OTT HCS B    5  UNP  P26349    THR    52 ENGINEERED MUTATION            
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   39  HIS HCS GLU GLY HCS PHE THR SER ASP LEU SER LYS GLN          
SEQRES   2 B   39  MET GLU GLU GLU ALA VAL ARG LEU PHE ILE GLU TRP LEU          
SEQRES   3 B   39  LYS ASN GLY GLY PRO SER SER GLY ALA PRO PRO PRO SER          
HET    HCS  B   2       7                                                       
HET    HCS  B   5       7                                                       
HETNAM     HCS 2-AMINO-4-MERCAPTO-BUTYRIC ACID                                  
FORMUL   2  HCS    2(C4 H9 N O2 S)                                              
FORMUL   3  HOH   *118(H2 O)                                                    
HELIX    1 AA1 SER A   31  ASP A   53  1                                  23    
HELIX    2 AA2 TRP A   91  VAL A   95  5                                   5    
HELIX    3 AA3 LEU A  123  GLU A  127  5                                   5    
HELIX    4 AA4 ASP B    9  ASN B   28  1                                  20    
HELIX    5 AA5 GLY B   29  SER B   33  5                                   5    
SHEET    1 AA1 2 THR A  65  PHE A  66  0                                        
SHEET    2 AA1 2 CYS A  71  TRP A  72 -1  O  TRP A  72   N  THR A  65           
SHEET    1 AA2 2 SER A  79  SER A  84  0                                        
SHEET    2 AA2 2 HIS A  99  CYS A 104 -1  O  VAL A 100   N  VAL A  83           
SSBOND   1 CYS A   46    CYS A   71                          1555   1555  2.13  
SSBOND   2 CYS A   62    CYS A  104                          1555   1555  2.02  
SSBOND   3 CYS A   85    CYS A  126                          1555   1555  1.96  
SSBOND   4 HCS B    2    HCS B    5                          1555   1555  2.01  
LINK         C   HCS B   2                 N   GLU B   3     1555   1555  1.32  
LINK         C   GLY B   4                 N   HCS B   5     1555   1555  1.33  
LINK         C   HCS B   5                 N   PHE B   6     1555   1555  1.33  
CRYST1   51.690   62.920  118.550  90.00  90.00  90.00 I 2 2 2       8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.019346  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015893  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008435        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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