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Database: PDB
Entry: 5GLH
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Original site: 5GLH 
HEADER    SIGNALING PROTEIN                       11-JUL-16   5GLH              
TITLE     HUMAN ENDOTHELIN RECEPTOR TYPE-B IN COMPLEX WITH ET-1                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ENDOTHELIN RECEPTOR SUBTYPE-B;                             
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: PEPTIDE FROM ENDOTHELIN-1;                                 
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: PREPROENDOTHELIN-1,PPET1;                                   
COMPND   9 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_TAXID: 9606;                                                
SOURCE   4 GENE: EDNRB;                                                         
SOURCE   5 EXPRESSION_SYSTEM: SPODOPTERA FRUGIPERDA;                            
SOURCE   6 EXPRESSION_SYSTEM_COMMON: FALL ARMYWORM;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 7108;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: SF9;                                    
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: MODIFIED PFASTBAC;                        
SOURCE  11 MOL_ID: 2;                                                           
SOURCE  12 SYNTHETIC: YES;                                                      
SOURCE  13 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE  14 ORGANISM_COMMON: HUMAN;                                              
SOURCE  15 ORGANISM_TAXID: 9606                                                 
KEYWDS    ALPHA HELICAL, SIGNALING PROTEIN                                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    W.SHIHOYA,T.NISHIZAWA,A.OKUTA,K.TANI,Y.FUJIYOSHI,N.DOHMAE,O.NUREKI,   
AUTHOR   2 T.DOI                                                                
REVDAT   4   26-FEB-20 5GLH    1       JRNL   REMARK                            
REVDAT   3   28-SEP-16 5GLH    1       JRNL                                     
REVDAT   2   21-SEP-16 5GLH    1       HEADER AUTHOR JRNL                       
REVDAT   1   07-SEP-16 5GLH    0                                                
JRNL        AUTH   W.SHIHOYA,T.NISHIZAWA,A.OKUTA,K.TANI,N.DOHMAE,Y.FUJIYOSHI,   
JRNL        AUTH 2 O.NUREKI,T.DOI                                               
JRNL        TITL   ACTIVATION MECHANISM OF ENDOTHELIN ETB RECEPTOR BY           
JRNL        TITL 2 ENDOTHELIN-1.                                                
JRNL        REF    NATURE                        V. 537   363 2016              
JRNL        REFN                   ESSN 1476-4687                               
JRNL        PMID   27595334                                                     
JRNL        DOI    10.1038/NATURE19319                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.10_2155                                     
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 : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.21                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.350                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 17403                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.238                           
REMARK   3   R VALUE            (WORKING SET) : 0.234                           
REMARK   3   FREE R VALUE                     : 0.277                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 1741                            
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 46.2206 -  6.4054    0.99     1398   155  0.1953 0.2111        
REMARK   3     2  6.4054 -  5.0862    1.00     1326   147  0.2426 0.2892        
REMARK   3     3  5.0862 -  4.4439    1.00     1319   147  0.2139 0.2432        
REMARK   3     4  4.4439 -  4.0378    1.00     1294   145  0.2153 0.2877        
REMARK   3     5  4.0378 -  3.7486    1.00     1314   146  0.2351 0.2870        
REMARK   3     6  3.7486 -  3.5276    1.00     1300   144  0.2415 0.3063        
REMARK   3     7  3.5276 -  3.3510    1.00     1276   142  0.2506 0.3144        
REMARK   3     8  3.3510 -  3.2052    1.00     1300   145  0.2583 0.2978        
REMARK   3     9  3.2052 -  3.0818    1.00     1303   145  0.2798 0.3262        
REMARK   3    10  3.0818 -  2.9755    1.00     1282   141  0.2925 0.3644        
REMARK   3    11  2.9755 -  2.8825    1.00     1276   142  0.3288 0.3789        
REMARK   3    12  2.8825 -  2.8001    1.00     1274   142  0.3194 0.3431        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
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)     : 0.400            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 30.840           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.14                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 84.53                          
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      :  0.002           3720                                  
REMARK   3   ANGLE     :  0.472           5072                                  
REMARK   3   CHIRALITY :  0.036            609                                  
REMARK   3   PLANARITY :  0.004            626                                  
REMARK   3   DIHEDRAL  : 15.143           2209                                  
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 5GLH COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 21-JUL-16.                  
REMARK 100 THE DEPOSITION ID IS D_1300000996.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-NOV-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SPRING-8                           
REMARK 200  BEAMLINE                       : BL32XU                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : DOUBLE-CRYSTAL MONOCHROMATOR       
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX225HE                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17421                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 15.20                              
REMARK 200  R MERGE                    (I) : 0.15430                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 15.2000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.90                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.80                              
REMARK 200  R MERGE FOR SHELL          (I) : 1.49600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.760                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.32                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.95                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 400, MES, (NH4)2SO4, 1,4             
REMARK 280  -BUTANEDIOL, PH 6.0, LIPIDIC CUBIC PHASE, TEMPERATURE 293K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
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                                         
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       54.67500            
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       54.67500            
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       36.48500            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       86.48500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.48500            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       86.48500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       54.67500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.48500            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       86.48500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       54.67500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.48500            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       86.48500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
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: 3130 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 22360 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -20.0 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     GLY A    63                                                      
REMARK 465     GLY A    64                                                      
REMARK 465     GLY A    65                                                      
REMARK 465     LEU A    66                                                      
REMARK 465     ALA A    67                                                      
REMARK 465     PRO A    68                                                      
REMARK 465     ALA A    69                                                      
REMARK 465     GLU A    70                                                      
REMARK 465     VAL A    71                                                      
REMARK 465     PRO A    72                                                      
REMARK 465     LYS A    73                                                      
REMARK 465     GLY A    74                                                      
REMARK 465     ASP A    75                                                      
REMARK 465     ARG A    76                                                      
REMARK 465     THR A    77                                                      
REMARK 465     ALA A    78                                                      
REMARK 465     GLY A    79                                                      
REMARK 465     SER A    80                                                      
REMARK 465     PRO A    81                                                      
REMARK 465     PRO A    82                                                      
REMARK 465     ARG A    83                                                      
REMARK 465     THR A    84                                                      
REMARK 465     ILE A    85                                                      
REMARK 465     SER A    86                                                      
REMARK 465     PRO A    87                                                      
REMARK 465     LYS A   130                                                      
REMARK 465     CYS A   131                                                      
REMARK 465     MET A   132                                                      
REMARK 465     ARG A   133                                                      
REMARK 465     ASN A   134                                                      
REMARK 465     SER A   207                                                      
REMARK 465     ARG A   208                                                      
REMARK 465     ILE A   209                                                      
REMARK 465     LYS A   210                                                      
REMARK 465     GLY A   211                                                      
REMARK 465     ILE A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     LYS A   216                                                      
REMARK 465     CYS A   402                                                      
REMARK 465     CYS A   403                                                      
REMARK 465     TRP A   404                                                      
REMARK 465     ALA A   405                                                      
REMARK 465     GLN A   406                                                      
REMARK 465     SER A   407                                                      
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     GLN A  91    CG   CD   OE1  NE2                                  
REMARK 470     GLU A  95    CG   CD   OE1  OE2                                  
REMARK 470     LYS A  97    CG   CD   CE   NZ                                   
REMARK 470     GLU A  98    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 101    CG   CD   CE   NZ                                   
REMARK 470     TYR A 124    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     TYR A 127    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 128    CG   CD   CE   NZ                                   
REMARK 470     ARG A 201    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     TRP A 217    CG   CD1  CD2  NE1  CE2  CE3  CZ2                   
REMARK 470     TRP A 217    CZ3  CH2                                            
REMARK 470     LYS A 248    CG   CD   CE   NZ                                   
REMARK 470     LYS A 262    CG   CD   CE   NZ                                   
REMARK 470     ARG A1014    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1016    CG   CD   CE   NZ                                   
REMARK 470     TYR A1018    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1019    CG   CD   CE   NZ                                   
REMARK 470     ASP A1020    CG   OD1  OD2                                       
REMARK 470     THR A1021    OG1  CG2                                            
REMARK 470     GLU A1022    CG   CD   OE1  OE2                                  
REMARK 470     TYR A1025    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A1035    CG   CD   CE   NZ                                   
REMARK 470     LEU A1039    CG   CD1  CD2                                       
REMARK 470     LEU A1046    CG   CD1  CD2                                       
REMARK 470     ARG A1052    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A1065    CG   CD   CE   NZ                                   
REMARK 470     GLN A 317    CG   CD   OE1  NE2                                  
REMARK 470     LYS A 323    CG   CD   CE   NZ                                   
REMARK 470     ASP A 354    CG   OD1  OD2                                       
REMARK 470     LYS A 391    CG   CD   CE   NZ                                   
REMARK 470     LYS A 398    CG   CD   CE   NZ                                   
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   OG1  THR A  1054     O    VAL A  1057              2.19            
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    PRO A  89     -175.01    -64.52                                   
REMARK 500    GLU A  95     -136.16     41.21                                   
REMARK 500    LYS A 248     -117.20     51.50                                   
REMARK 500    PHE A 282      -63.56   -143.64                                   
REMARK 500    THR A1054       42.77    -90.96                                   
REMARK 500    ASN A1055       -3.90     78.98                                   
REMARK 500    LYS A 391      -54.01     61.38                                   
REMARK 500    ALA A 400      -73.77    -67.41                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5GLI   RELATED DB: PDB                                   
DBREF  5GLH A   63   407  PDB    5GLH     5GLH            63    407             
DBREF  5GLH B    1    21  UNP    P05305   EDN1_HUMAN      53     73             
SEQRES   1 A  498  GLY GLY GLY LEU ALA PRO ALA GLU VAL PRO LYS GLY ASP          
SEQRES   2 A  498  ARG THR ALA GLY SER PRO PRO ARG THR ILE SER PRO PRO          
SEQRES   3 A  498  PRO CYS GLN GLY PRO ILE GLU ILE LYS GLU THR PHE LYS          
SEQRES   4 A  498  TYR ILE ASN THR VAL VAL SER CYS LEU VAL PHE VAL LEU          
SEQRES   5 A  498  GLY ILE ILE GLY ASN SER THR LEU LEU TYR ILE ILE TYR          
SEQRES   6 A  498  LYS ASN LYS CYS MET ARG ASN GLY PRO ASN ILE LEU ILE          
SEQRES   7 A  498  ALA SER LEU ALA LEU GLY ASP LEU LEU HIS ILE VAL ILE          
SEQRES   8 A  498  ALA ILE PRO ILE ASN VAL TYR LYS LEU LEU ALA GLU ASP          
SEQRES   9 A  498  TRP PRO PHE GLY ALA GLU MET CYS LYS LEU VAL PRO PHE          
SEQRES  10 A  498  ILE GLN LYS ALA SER VAL GLY ILE THR VAL LEU SER LEU          
SEQRES  11 A  498  CYS ALA LEU SER ILE ASP ARG TYR ARG ALA VAL ALA SER          
SEQRES  12 A  498  TRP SER ARG ILE LYS GLY ILE GLY VAL PRO LYS TRP THR          
SEQRES  13 A  498  ALA VAL GLU ILE VAL LEU ILE TRP VAL VAL SER VAL VAL          
SEQRES  14 A  498  LEU ALA VAL PRO GLU ALA ILE GLY PHE ASP ILE ILE THR          
SEQRES  15 A  498  MET ASP TYR LYS GLY SER TYR LEU ARG ILE CYS LEU LEU          
SEQRES  16 A  498  HIS PRO VAL GLN LYS THR ALA PHE MET GLN PHE TYR ALA          
SEQRES  17 A  498  THR ALA LYS ASP TRP TRP LEU PHE SER PHE TYR PHE CYS          
SEQRES  18 A  498  LEU PRO LEU ALA ILE THR ALA PHE PHE TYR THR LEU MET          
SEQRES  19 A  498  THR CYS GLU MET LEU ARG LYS ASN ILE PHE GLU MET LEU          
SEQRES  20 A  498  ARG ILE ASP GLU GLY LEU ARG LEU LYS ILE TYR LYS ASP          
SEQRES  21 A  498  THR GLU GLY TYR TYR THR ILE GLY ILE GLY HIS LEU LEU          
SEQRES  22 A  498  THR LYS SER PRO SER LEU ASN ALA ALA LYS SER GLU LEU          
SEQRES  23 A  498  ASP LYS ALA ILE GLY ARG ASN THR ASN GLY VAL ILE THR          
SEQRES  24 A  498  LYS ASP GLU ALA GLU LYS LEU PHE ASN GLN ASP VAL ASP          
SEQRES  25 A  498  ALA ALA VAL ARG GLY ILE LEU ARG ASN ALA LYS LEU LYS          
SEQRES  26 A  498  PRO VAL TYR ASP SER LEU ASP ALA VAL ARG ARG ALA ALA          
SEQRES  27 A  498  LEU ILE ASN MET VAL PHE GLN MET GLY GLU THR GLY VAL          
SEQRES  28 A  498  ALA GLY PHE THR ASN SER LEU ARG MET LEU GLN GLN LYS          
SEQRES  29 A  498  ARG TRP ASP GLU ALA ALA VAL ASN LEU ALA LYS SER ARG          
SEQRES  30 A  498  TRP TYR ASN GLN THR PRO ASN ARG ALA LYS ARG VAL ILE          
SEQRES  31 A  498  THR THR PHE ARG THR GLY THR TRP ASP ALA TYR LEU ASN          
SEQRES  32 A  498  ASP HIS LEU LYS GLN ARG ARG GLU VAL ALA LYS THR VAL          
SEQRES  33 A  498  PHE CYS LEU VAL LEU VAL PHE ALA LEU CYS TRP LEU PRO          
SEQRES  34 A  498  LEU HIS LEU ALA ARG ILE LEU LYS LEU THR LEU TYR ASN          
SEQRES  35 A  498  GLN ASN ASP PRO ASN ARG CYS GLU LEU LEU SER PHE LEU          
SEQRES  36 A  498  LEU VAL LEU ASP TYR ILE GLY ILE ASN MET ALA SER LEU          
SEQRES  37 A  498  ASN SER CYS ALA ASN PRO ILE ALA LEU TYR LEU VAL SER          
SEQRES  38 A  498  LYS ARG PHE LYS ASN ALA PHE LYS SER ALA LEU CYS CYS          
SEQRES  39 A  498  TRP ALA GLN SER                                              
SEQRES   1 B   21  CYS SER CYS SER SER LEU MET ASP LYS GLU CYS VAL TYR          
SEQRES   2 B   21  PHE CYS HIS LEU ASP ILE ILE TRP                              
FORMUL   3  HOH   *4(H2 O)                                                      
HELIX    1 AA1 LYS A   97  ASN A  129  1                                  33    
HELIX    2 AA2 PRO A  136  ILE A  155  1                                  20    
HELIX    3 AA3 ILE A  155  ALA A  164  1                                  10    
HELIX    4 AA4 GLY A  170  SER A  205  1                                  36    
HELIX    5 AA5 THR A  218  GLY A  239  1                                  22    
HELIX    6 AA6 THR A  263  TYR A  281  1                                  19    
HELIX    7 AA7 PHE A  282  GLY A 1012  1                                  33    
HELIX    8 AA8 SER A 1038  GLY A 1051  1                                  14    
HELIX    9 AA9 THR A 1059  ASN A 1081  1                                  23    
HELIX   10 AB1 LEU A 1084  LEU A 1091  1                                   8    
HELIX   11 AB2 ASP A 1092  ALA A 1112  1                                  21    
HELIX   12 AB3 PHE A 1114  GLN A 1123  1                                  10    
HELIX   13 AB4 ARG A 1125  ALA A 1134  1                                  10    
HELIX   14 AB5 SER A 1136  THR A 1142  1                                   7    
HELIX   15 AB6 THR A 1142  GLY A 1156  1                                  15    
HELIX   16 AB7 ASN A  312  PHE A  326  1                                  15    
HELIX   17 AB8 PHE A  326  TRP A  336  1                                  11    
HELIX   18 AB9 TRP A  336  TYR A  350  1                                  15    
HELIX   19 AC1 ASN A  356  LYS A  391  1                                  36    
HELIX   20 AC2 LYS A  391  SER A  399  1                                   9    
HELIX   21 AC3 ASP B    8  ASP B   18  1                                  11    
SHEET    1 AA1 2 PHE A 240  TYR A 247  0                                        
SHEET    2 AA1 2 SER A 250  LEU A 257 -1  O  ILE A 254   N  ILE A 243           
SHEET    1 AA2 3 ARG A1014  LYS A1019  0                                        
SHEET    2 AA2 3 TYR A1025  GLY A1028 -1  O  THR A1026   N  TYR A1018           
SHEET    3 AA2 3 HIS A1031  LEU A1032 -1  O  HIS A1031   N  ILE A1027           
SSBOND   1 CYS A   90    CYS A  358                          1555   1555  2.04  
SSBOND   2 CYS A  174    CYS A  255                          1555   1555  2.04  
SSBOND   3 CYS B    1    CYS B   15                          1555   1555  2.04  
SSBOND   4 CYS B    3    CYS B   11                          1555   1555  2.04  
CRYST1   72.970  172.970  109.350  90.00  90.00  90.00 C 2 2 21      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      0.013704  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.005781  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009145        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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