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LongText Report for: 5xm6-pdb

Name Class
5xm6-pdb
HEADER    HYDROLASE                               12-MAY-17   5XM6              
TITLE     THE OVERALL STRUCTURE OF VREH2                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE;                                         
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 EC: 3.3.2.-;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIGNA RADIATA;                                  
SOURCE   3 ORGANISM_COMMON: MUNG BEAN;                                          
SOURCE   4 ORGANISM_TAXID: 157791;                                              
SOURCE   5 GENE: VREH3;                                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    EPOXIDE HYDROLASE, HYDROLASE                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    F.L.LI,X.D.KONG,H.L.YU,Y.P.SHANG,J.H.ZHOU,J.H.XU                      
REVDAT   1   05-SEP-18 5XM6    0                                                
JRNL        AUTH   F.L.LI,X.D.KONG,Q.CHEN,Y.C.ZHENG,Q.XU,F.F.CHEN,L.Q.FAN,      
JRNL        AUTH 2 G.Q.LIN,J.H.ZHOU,H.L.YU,J.H.XU                               
JRNL        TITL   REGIOSELECTIVITY ENGINEERING OF EPOXIDE HYDROLASE:           
JRNL        TITL 2 NEAR-PERFECT ENANTIOCONVERGENCE THROUGH A SINGLE SITE        
JRNL        TITL 3 MUTATION                                                     
JRNL        REF    ACS CATALYSIS                 V.   8  8314 2018              
JRNL        REFN                   ESSN 2155-5435                               
JRNL        DOI    10.1021/ACSCATAL.8B02622                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.8.2_1309                                    
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) : 2.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.53                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 50310                          
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                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.080                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2556                            
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 41.5382 -  6.5463    0.99     2898   144  0.1795 0.2078        
REMARK   3     2  6.5463 -  5.1992    1.00     2731   151  0.1909 0.2088        
REMARK   3     3  5.1992 -  4.5429    1.00     2698   136  0.1522 0.2026        
REMARK   3     4  4.5429 -  4.1280    1.00     2695   161  0.1494 0.1785        
REMARK   3     5  4.1280 -  3.8323    1.00     2649   156  0.1607 0.1971        
REMARK   3     6  3.8323 -  3.6065    1.00     2659   141  0.1756 0.2154        
REMARK   3     7  3.6065 -  3.4260    1.00     2628   142  0.1794 0.1903        
REMARK   3     8  3.4260 -  3.2769    1.00     2658   143  0.1818 0.2248        
REMARK   3     9  3.2769 -  3.1508    1.00     2629   128  0.1976 0.2862        
REMARK   3    10  3.1508 -  3.0421    1.00     2625   138  0.1912 0.2529        
REMARK   3    11  3.0421 -  2.9470    1.00     2619   138  0.1964 0.2413        
REMARK   3    12  2.9470 -  2.8628    1.00     2624   143  0.1983 0.2603        
REMARK   3    13  2.8628 -  2.7875    1.00     2610   151  0.1914 0.2446        
REMARK   3    14  2.7875 -  2.7195    1.00     2600   135  0.1968 0.2530        
REMARK   3    15  2.7195 -  2.6577    1.00     2620   137  0.1967 0.2618        
REMARK   3    16  2.6577 -  2.6011    1.00     2611   128  0.2129 0.2948        
REMARK   3    17  2.6011 -  2.5491    1.00     2614   150  0.2056 0.2811        
REMARK   3    18  2.5491 -  2.5010    0.99     2586   134  0.2096 0.2893        
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)     : 0.270            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.780           
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      :  0.008           7906                                  
REMARK   3   ANGLE     :  1.119          10757                                  
REMARK   3   CHIRALITY :  0.077           1132                                  
REMARK   3   PLANARITY :  0.006           1392                                  
REMARK   3   DIHEDRAL  : 14.136           2868                                  
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 5XM6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003764.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 27-APR-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 50435                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.500                              
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     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 27.90                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.2500                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.50                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.59                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 29.50                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: CCP4I 6.3.0                                           
REMARK 200 STARTING MODEL: 2CJP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RHOMBUS                                                      
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 62.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.25                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 20000, PEG500MME, HEPES, MOPS,       
REMARK 280  SODIUM NITRATE, AMMONIUM SULFATE, DISODIUM HYDROGEN PHOSPHATE.,     
REMARK 280  PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 285K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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      118.48350            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       54.59000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       54.59000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       59.24175            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       54.59000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       54.59000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      177.72525            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       54.59000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       54.59000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       59.24175            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       54.59000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       54.59000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      177.72525            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      118.48350            
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: TRIMERIC                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C                               
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     MET A   -33                                                      
REMARK 465     GLY A   -32                                                      
REMARK 465     SER A   -31                                                      
REMARK 465     SER A   -30                                                      
REMARK 465     HIS A   -29                                                      
REMARK 465     HIS A   -28                                                      
REMARK 465     HIS A   -27                                                      
REMARK 465     HIS A   -26                                                      
REMARK 465     HIS A   -25                                                      
REMARK 465     HIS A   -24                                                      
REMARK 465     SER A   -23                                                      
REMARK 465     SER A   -22                                                      
REMARK 465     GLY A   -21                                                      
REMARK 465     LEU A   -20                                                      
REMARK 465     VAL A   -19                                                      
REMARK 465     PRO A   -18                                                      
REMARK 465     ARG A   -17                                                      
REMARK 465     GLY A   -16                                                      
REMARK 465     SER A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     MET A   -13                                                      
REMARK 465     ALA A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     MET A   -10                                                      
REMARK 465     THR A    -9                                                      
REMARK 465     GLY A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     GLN A    -6                                                      
REMARK 465     GLN A    -5                                                      
REMARK 465     MET A    -4                                                      
REMARK 465     GLY A    -3                                                      
REMARK 465     ARG A    -2                                                      
REMARK 465     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET B   -33                                                      
REMARK 465     GLY B   -32                                                      
REMARK 465     SER B   -31                                                      
REMARK 465     SER B   -30                                                      
REMARK 465     HIS B   -29                                                      
REMARK 465     HIS B   -28                                                      
REMARK 465     HIS B   -27                                                      
REMARK 465     HIS B   -26                                                      
REMARK 465     HIS B   -25                                                      
REMARK 465     HIS B   -24                                                      
REMARK 465     SER B   -23                                                      
REMARK 465     SER B   -22                                                      
REMARK 465     GLY B   -21                                                      
REMARK 465     LEU B   -20                                                      
REMARK 465     VAL B   -19                                                      
REMARK 465     PRO B   -18                                                      
REMARK 465     ARG B   -17                                                      
REMARK 465     GLY B   -16                                                      
REMARK 465     SER B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     MET B   -13                                                      
REMARK 465     ALA B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     MET B   -10                                                      
REMARK 465     THR B    -9                                                      
REMARK 465     GLY B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     GLN B    -6                                                      
REMARK 465     GLN B    -5                                                      
REMARK 465     MET B    -4                                                      
REMARK 465     GLY B    -3                                                      
REMARK 465     ARG B    -2                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     SER B     0                                                      
REMARK 465     MET C   -33                                                      
REMARK 465     GLY C   -32                                                      
REMARK 465     SER C   -31                                                      
REMARK 465     SER C   -30                                                      
REMARK 465     HIS C   -29                                                      
REMARK 465     HIS C   -28                                                      
REMARK 465     HIS C   -27                                                      
REMARK 465     HIS C   -26                                                      
REMARK 465     HIS C   -25                                                      
REMARK 465     HIS C   -24                                                      
REMARK 465     SER C   -23                                                      
REMARK 465     SER C   -22                                                      
REMARK 465     GLY C   -21                                                      
REMARK 465     LEU C   -20                                                      
REMARK 465     VAL C   -19                                                      
REMARK 465     PRO C   -18                                                      
REMARK 465     ARG C   -17                                                      
REMARK 465     GLY C   -16                                                      
REMARK 465     SER C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     MET C   -13                                                      
REMARK 465     ALA C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     MET C   -10                                                      
REMARK 465     THR C    -9                                                      
REMARK 465     GLY C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     GLN C    -6                                                      
REMARK 465     GLN C    -5                                                      
REMARK 465     MET C    -4                                                      
REMARK 465     GLY C    -3                                                      
REMARK 465     ARG C    -2                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     SER C     0                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH C   511     O    HOH C   517              1.81            
REMARK 500   O    HOH B   434     O    HOH B   563              1.81            
REMARK 500   OE2  GLU A   305     O    HOH A   401              1.82            
REMARK 500   O    HOH A   609     O    HOH A   610              1.84            
REMARK 500   O    HOH C   430     O    HOH C   437              1.84            
REMARK 500   O    HOH B   573     O    HOH B   599              1.87            
REMARK 500   O    HOH B   587     O    HOH B   608              1.87            
REMARK 500   O    HOH A   527     O    HOH B   548              1.88            
REMARK 500   O    HOH B   626     O    HOH B   632              1.92            
REMARK 500   O    HOH B   610     O    HOH B   617              1.94            
REMARK 500   OD1  ASN C   197     O    HOH C   401              1.97            
REMARK 500   O    HOH B   476     O    HOH B   533              1.98            
REMARK 500   O    HOH C   456     O    HOH C   480              1.98            
REMARK 500   O    HOH B   586     O    HOH B   606              1.98            
REMARK 500   O    HOH C   472     O    HOH C   484              2.01            
REMARK 500   O    HOH B   537     O    HOH B   619              2.02            
REMARK 500   O    HOH C   502     O    HOH C   513              2.03            
REMARK 500   O    HOH A   505     O    HOH A   577              2.03            
REMARK 500   O    HOH A   571     O    HOH B   470              2.04            
REMARK 500   O    HOH A   566     O    HOH A   594              2.06            
REMARK 500   O    HOH A   459     O    HOH A   559              2.09            
REMARK 500   O    HOH B   618     O    HOH B   626              2.11            
REMARK 500   O    HOH A   540     O    HOH B   499              2.11            
REMARK 500   OE1  GLU A    35     O    HOH A   402              2.11            
REMARK 500   OD1  ASN A   300     O    HOH A   403              2.12            
REMARK 500   O    HOH B   592     O    HOH B   606              2.13            
REMARK 500   OE1  GLU B   159     O    HOH B   401              2.16            
REMARK 500   ND2  ASN C   175     O    GLY C   195              2.17            
REMARK 500   OE1  GLU C    10     O    HOH C   402              2.17            
REMARK 500   O    HOH B   560     O    HOH B   572              2.18            
REMARK 500   OE1  GLN B   281     O    HOH B   402              2.19            
REMARK 500   O    LYS B   156     O    HOH B   403              2.19            
REMARK 500   O    HOH A   412     O    HOH A   544              2.19            
REMARK 500   O    HOH A   611     O    HOH C   505              2.19            
REMARK 500   O    HOH B   436     O    HOH B   532              2.19            
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   458     O    HOH C   473     6554     1.87            
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  34       78.27   -102.26                                   
REMARK 500    GLU A  35     -158.14   -115.96                                   
REMARK 500    ASP A 101     -128.48     56.49                                   
REMARK 500    SER A 125      -52.09     72.22                                   
REMARK 500    ALA A 296     -146.97    -93.25                                   
REMARK 500    ALA A 303       51.48   -112.05                                   
REMARK 500    PRO B  34       78.35   -101.86                                   
REMARK 500    GLU B  35     -157.77   -112.84                                   
REMARK 500    ASP B 101     -128.76     61.31                                   
REMARK 500    SER B 125      -55.99     70.67                                   
REMARK 500    THR B 194       71.09     45.92                                   
REMARK 500    ALA B 296     -152.05   -100.83                                   
REMARK 500    ALA B 303       51.17   -118.57                                   
REMARK 500    LYS B 317        4.50    -68.04                                   
REMARK 500    PRO C  34       71.66   -101.89                                   
REMARK 500    GLU C  35     -155.45   -103.68                                   
REMARK 500    ASP C 101     -123.35     62.74                                   
REMARK 500    SER C 125      -61.94     75.99                                   
REMARK 500    VAL C 167      -27.43     75.64                                   
REMARK 500    PHE C 196      -41.77    100.02                                   
REMARK 500    LEU C 268       26.96     45.74                                   
REMARK 500    GLU C 288      152.81    178.62                                   
REMARK 500    ALA C 296     -140.82    -94.58                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF1 5XM6 A    1   318  UNP                  A0A0G3F3K2_VIGRA                 
DBREF2 5XM6 A     A0A0G3F3K2                          1         318             
DBREF1 5XM6 B    1   318  UNP                  A0A0G3F3K2_VIGRA                 
DBREF2 5XM6 B     A0A0G3F3K2                          1         318             
DBREF1 5XM6 C    1   318  UNP                  A0A0G3F3K2_VIGRA                 
DBREF2 5XM6 C     A0A0G3F3K2                          1         318             
SEQADV 5XM6 MET A  -33  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A  -32  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A  -31  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A  -30  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -29  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -28  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -27  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -26  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -25  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -24  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A  -23  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A  -22  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A  -21  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 LEU A  -20  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 VAL A  -19  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 PRO A  -18  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ARG A  -17  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A  -16  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A  -15  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS A  -14  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET A  -13  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ALA A  -12  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A  -11  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET A  -10  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 THR A   -9  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A   -8  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A   -7  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLN A   -6  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLN A   -5  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET A   -4  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A   -3  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ARG A   -2  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY A   -1  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER A    0  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLU A    3  UNP  A0A0G3F3K GLY     3 ENGINEERED MUTATION            
SEQADV 5XM6 ILE A    4  UNP  A0A0G3F3K VAL     4 ENGINEERED MUTATION            
SEQADV 5XM6 HIS A  114  UNP  A0A0G3F3K ARG   114 ENGINEERED MUTATION            
SEQADV 5XM6 MET B  -33  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B  -32  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B  -31  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B  -30  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -29  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -28  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -27  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -26  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -25  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -24  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B  -23  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B  -22  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B  -21  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 LEU B  -20  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 VAL B  -19  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 PRO B  -18  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ARG B  -17  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B  -16  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B  -15  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS B  -14  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET B  -13  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ALA B  -12  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B  -11  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET B  -10  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 THR B   -9  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B   -8  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B   -7  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLN B   -6  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLN B   -5  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET B   -4  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B   -3  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ARG B   -2  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY B   -1  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER B    0  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLU B    3  UNP  A0A0G3F3K GLY     3 ENGINEERED MUTATION            
SEQADV 5XM6 ILE B    4  UNP  A0A0G3F3K VAL     4 ENGINEERED MUTATION            
SEQADV 5XM6 HIS B  114  UNP  A0A0G3F3K ARG   114 ENGINEERED MUTATION            
SEQADV 5XM6 MET C  -33  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C  -32  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C  -31  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C  -30  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -29  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -28  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -27  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -26  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -25  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -24  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C  -23  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C  -22  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C  -21  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 LEU C  -20  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 VAL C  -19  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 PRO C  -18  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ARG C  -17  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C  -16  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C  -15  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 HIS C  -14  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET C  -13  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ALA C  -12  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C  -11  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET C  -10  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 THR C   -9  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C   -8  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C   -7  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLN C   -6  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLN C   -5  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 MET C   -4  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C   -3  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 ARG C   -2  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLY C   -1  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 SER C    0  UNP  A0A0G3F3K           EXPRESSION TAG                 
SEQADV 5XM6 GLU C    3  UNP  A0A0G3F3K GLY     3 ENGINEERED MUTATION            
SEQADV 5XM6 ILE C    4  UNP  A0A0G3F3K VAL     4 ENGINEERED MUTATION            
SEQADV 5XM6 HIS C  114  UNP  A0A0G3F3K ARG   114 ENGINEERED MUTATION            
SEQRES   1 A  352  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  352  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 A  352  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 A  352  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 A  352  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 A  352  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 A  352  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 A  352  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO VAL SER          
SEQRES   9 A  352  ILE SER SER TYR THR GLY PHE HIS ILE VAL GLY ASP LEU          
SEQRES  10 A  352  ILE ALA LEU ILE ASP LEU LEU GLY VAL ASP GLN VAL PHE          
SEQRES  11 A  352  LEU VAL ALA HIS ASP TRP GLY ALA ILE ILE GLY TRP TYR          
SEQRES  12 A  352  LEU CYS THR PHE HIS PRO ASP ARG VAL LYS ALA TYR VAL          
SEQRES  13 A  352  CYS LEU SER VAL PRO LEU LEU HIS ARG ASP PRO ASN ILE          
SEQRES  14 A  352  ARG THR VAL ASP ALA MET ARG ALA MET TYR GLY ASP ASP          
SEQRES  15 A  352  TYR TYR ILE CYS ARG PHE GLN LYS PRO GLY GLU MET GLU          
SEQRES  16 A  352  ALA GLN MET ALA GLU VAL GLY THR GLU TYR VAL LEU LYS          
SEQRES  17 A  352  ASN ILE LEU THR THR ARG LYS PRO GLY PRO PRO ILE PHE          
SEQRES  18 A  352  PRO LYS GLY GLU TYR GLY THR GLY PHE ASN PRO ASP MET          
SEQRES  19 A  352  PRO ASN SER LEU PRO SER TRP LEU THR GLN ASP ASP LEU          
SEQRES  20 A  352  ALA TYR TYR VAL SER LYS TYR GLU LYS THR GLY PHE THR          
SEQRES  21 A  352  GLY PRO LEU ASN TYR TYR ARG ASN MET ASN LEU ASN TRP          
SEQRES  22 A  352  GLU LEU THR ALA PRO TRP SER GLY GLY LYS ILE GLN VAL          
SEQRES  23 A  352  PRO VAL LYS PHE ILE THR GLY GLU LEU ASP MET VAL TYR          
SEQRES  24 A  352  THR SER LEU ASN MET LYS GLU TYR ILE HIS GLY GLY GLY          
SEQRES  25 A  352  PHE LYS GLN ASP VAL PRO ASN LEU GLU GLU VAL ILE VAL          
SEQRES  26 A  352  GLN LYS ASN VAL ALA HIS PHE ASN ASN GLN GLU ALA ALA          
SEQRES  27 A  352  GLU GLU ILE ASN ASN HIS ILE TYR ASP PHE ILE LYS LYS          
SEQRES  28 A  352  PHE                                                          
SEQRES   1 B  352  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  352  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 B  352  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 B  352  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 B  352  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 B  352  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 B  352  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 B  352  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO VAL SER          
SEQRES   9 B  352  ILE SER SER TYR THR GLY PHE HIS ILE VAL GLY ASP LEU          
SEQRES  10 B  352  ILE ALA LEU ILE ASP LEU LEU GLY VAL ASP GLN VAL PHE          
SEQRES  11 B  352  LEU VAL ALA HIS ASP TRP GLY ALA ILE ILE GLY TRP TYR          
SEQRES  12 B  352  LEU CYS THR PHE HIS PRO ASP ARG VAL LYS ALA TYR VAL          
SEQRES  13 B  352  CYS LEU SER VAL PRO LEU LEU HIS ARG ASP PRO ASN ILE          
SEQRES  14 B  352  ARG THR VAL ASP ALA MET ARG ALA MET TYR GLY ASP ASP          
SEQRES  15 B  352  TYR TYR ILE CYS ARG PHE GLN LYS PRO GLY GLU MET GLU          
SEQRES  16 B  352  ALA GLN MET ALA GLU VAL GLY THR GLU TYR VAL LEU LYS          
SEQRES  17 B  352  ASN ILE LEU THR THR ARG LYS PRO GLY PRO PRO ILE PHE          
SEQRES  18 B  352  PRO LYS GLY GLU TYR GLY THR GLY PHE ASN PRO ASP MET          
SEQRES  19 B  352  PRO ASN SER LEU PRO SER TRP LEU THR GLN ASP ASP LEU          
SEQRES  20 B  352  ALA TYR TYR VAL SER LYS TYR GLU LYS THR GLY PHE THR          
SEQRES  21 B  352  GLY PRO LEU ASN TYR TYR ARG ASN MET ASN LEU ASN TRP          
SEQRES  22 B  352  GLU LEU THR ALA PRO TRP SER GLY GLY LYS ILE GLN VAL          
SEQRES  23 B  352  PRO VAL LYS PHE ILE THR GLY GLU LEU ASP MET VAL TYR          
SEQRES  24 B  352  THR SER LEU ASN MET LYS GLU TYR ILE HIS GLY GLY GLY          
SEQRES  25 B  352  PHE LYS GLN ASP VAL PRO ASN LEU GLU GLU VAL ILE VAL          
SEQRES  26 B  352  GLN LYS ASN VAL ALA HIS PHE ASN ASN GLN GLU ALA ALA          
SEQRES  27 B  352  GLU GLU ILE ASN ASN HIS ILE TYR ASP PHE ILE LYS LYS          
SEQRES  28 B  352  PHE                                                          
SEQRES   1 C  352  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  352  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 C  352  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 C  352  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 C  352  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 C  352  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 C  352  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 C  352  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO VAL SER          
SEQRES   9 C  352  ILE SER SER TYR THR GLY PHE HIS ILE VAL GLY ASP LEU          
SEQRES  10 C  352  ILE ALA LEU ILE ASP LEU LEU GLY VAL ASP GLN VAL PHE          
SEQRES  11 C  352  LEU VAL ALA HIS ASP TRP GLY ALA ILE ILE GLY TRP TYR          
SEQRES  12 C  352  LEU CYS THR PHE HIS PRO ASP ARG VAL LYS ALA TYR VAL          
SEQRES  13 C  352  CYS LEU SER VAL PRO LEU LEU HIS ARG ASP PRO ASN ILE          
SEQRES  14 C  352  ARG THR VAL ASP ALA MET ARG ALA MET TYR GLY ASP ASP          
SEQRES  15 C  352  TYR TYR ILE CYS ARG PHE GLN LYS PRO GLY GLU MET GLU          
SEQRES  16 C  352  ALA GLN MET ALA GLU VAL GLY THR GLU TYR VAL LEU LYS          
SEQRES  17 C  352  ASN ILE LEU THR THR ARG LYS PRO GLY PRO PRO ILE PHE          
SEQRES  18 C  352  PRO LYS GLY GLU TYR GLY THR GLY PHE ASN PRO ASP MET          
SEQRES  19 C  352  PRO ASN SER LEU PRO SER TRP LEU THR GLN ASP ASP LEU          
SEQRES  20 C  352  ALA TYR TYR VAL SER LYS TYR GLU LYS THR GLY PHE THR          
SEQRES  21 C  352  GLY PRO LEU ASN TYR TYR ARG ASN MET ASN LEU ASN TRP          
SEQRES  22 C  352  GLU LEU THR ALA PRO TRP SER GLY GLY LYS ILE GLN VAL          
SEQRES  23 C  352  PRO VAL LYS PHE ILE THR GLY GLU LEU ASP MET VAL TYR          
SEQRES  24 C  352  THR SER LEU ASN MET LYS GLU TYR ILE HIS GLY GLY GLY          
SEQRES  25 C  352  PHE LYS GLN ASP VAL PRO ASN LEU GLU GLU VAL ILE VAL          
SEQRES  26 C  352  GLN LYS ASN VAL ALA HIS PHE ASN ASN GLN GLU ALA ALA          
SEQRES  27 C  352  GLU GLU ILE ASN ASN HIS ILE TYR ASP PHE ILE LYS LYS          
SEQRES  28 C  352  PHE                                                          
FORMUL   4  HOH   *572(H2 O)                                                    
HELIX    1 AA1 LEU A   36  SER A   39  5                                   4    
HELIX    2 AA2 TRP A   40  SER A   49  1                                  10    
HELIX    3 AA3 SER A   70  TYR A   74  5                                   5    
HELIX    4 AA4 THR A   75  GLY A   91  1                                  17    
HELIX    5 AA5 ASP A  101  HIS A  114  1                                  14    
HELIX    6 AA6 ARG A  136  GLY A  146  1                                  11    
HELIX    7 AA7 TYR A  149  PHE A  154  1                                   6    
HELIX    8 AA8 GLY A  158  GLY A  168  1                                  11    
HELIX    9 AA9 GLY A  168  THR A  179  1                                  12    
HELIX   10 AB1 THR A  209  GLY A  224  1                                  16    
HELIX   11 AB2 PHE A  225  ASN A  234  1                                  10    
HELIX   12 AB3 ASN A  234  THR A  242  1                                   9    
HELIX   13 AB4 ALA A  243  SER A  246  5                                   4    
HELIX   14 AB5 ASN A  269  GLY A  277  1                                   9    
HELIX   15 AB6 GLY A  277  VAL A  283  1                                   7    
HELIX   16 AB7 PHE A  298  ALA A  303  1                                   6    
HELIX   17 AB8 ALA A  303  LYS A  316  1                                  14    
HELIX   18 AB9 LEU B   36  SER B   39  5                                   4    
HELIX   19 AC1 TRP B   40  SER B   49  1                                  10    
HELIX   20 AC2 SER B   70  TYR B   74  5                                   5    
HELIX   21 AC3 THR B   75  GLY B   91  1                                  17    
HELIX   22 AC4 ASP B  101  HIS B  114  1                                  14    
HELIX   23 AC5 ARG B  136  GLY B  146  1                                  11    
HELIX   24 AC6 TYR B  149  PHE B  154  1                                   6    
HELIX   25 AC7 GLY B  158  GLY B  168  1                                  11    
HELIX   26 AC8 GLY B  168  THR B  178  1                                  11    
HELIX   27 AC9 THR B  209  GLY B  224  1                                  16    
HELIX   28 AD1 PHE B  225  ARG B  233  1                                   9    
HELIX   29 AD2 ASN B  234  THR B  242  1                                   9    
HELIX   30 AD3 ALA B  243  SER B  246  5                                   4    
HELIX   31 AD4 ASN B  269  GLY B  277  1                                   9    
HELIX   32 AD5 GLY B  277  VAL B  283  1                                   7    
HELIX   33 AD6 PHE B  298  ALA B  303  1                                   6    
HELIX   34 AD7 ALA B  303  LYS B  316  1                                  14    
HELIX   35 AD8 LEU C   36  SER C   39  5                                   4    
HELIX   36 AD9 TRP C   40  ARG C   50  1                                  11    
HELIX   37 AE1 SER C   70  TYR C   74  5                                   5    
HELIX   38 AE2 THR C   75  LEU C   90  1                                  16    
HELIX   39 AE3 ASP C  101  HIS C  114  1                                  14    
HELIX   40 AE4 ARG C  136  GLY C  146  1                                  11    
HELIX   41 AE5 TYR C  149  PHE C  154  1                                   6    
HELIX   42 AE6 GLY C  158  GLU C  166  1                                   9    
HELIX   43 AE7 GLY C  168  THR C  179  1                                  12    
HELIX   44 AE8 THR C  209  GLY C  224  1                                  16    
HELIX   45 AE9 PHE C  225  ARG C  233  1                                   9    
HELIX   46 AF1 ASN C  234  THR C  242  1                                   9    
HELIX   47 AF2 ALA C  243  SER C  246  5                                   4    
HELIX   48 AF3 ASN C  269  GLY C  277  1                                   9    
HELIX   49 AF4 GLY C  277  VAL C  283  1                                   7    
HELIX   50 AF5 PHE C  298  ALA C  303  1                                   6    
HELIX   51 AF6 ALA C  303  LYS C  316  1                                  14    
SHEET    1 AA1 8 GLU A   5  VAL A  11  0                                        
SHEET    2 AA1 8 ILE A  14  LYS A  21 -1  O  VAL A  18   N  ARG A   7           
SHEET    3 AA1 8 ARG A  53  PRO A  57 -1  O  ALA A  56   N  ALA A  19           
SHEET    4 AA1 8 VAL A  26  LEU A  30  1  N  VAL A  27   O  ARG A  53           
SHEET    5 AA1 8 VAL A  95  HIS A 100  1  O  PHE A  96   N  LEU A  28           
SHEET    6 AA1 8 VAL A 118  LEU A 124  1  O  VAL A 122   N  LEU A  97           
SHEET    7 AA1 8 VAL A 254  GLY A 259  1  O  ILE A 257   N  CYS A 123           
SHEET    8 AA1 8 LEU A 286  GLN A 292  1  O  GLN A 292   N  THR A 258           
SHEET    1 AA2 8 GLU B   5  VAL B  11  0                                        
SHEET    2 AA2 8 ILE B  14  LYS B  21 -1  O  VAL B  18   N  ARG B   7           
SHEET    3 AA2 8 ARG B  53  PRO B  57 -1  O  ALA B  56   N  ALA B  19           
SHEET    4 AA2 8 VAL B  26  LEU B  30  1  N  VAL B  27   O  ARG B  53           
SHEET    5 AA2 8 VAL B  95  HIS B 100  1  O  PHE B  96   N  LEU B  28           
SHEET    6 AA2 8 VAL B 118  LEU B 124  1  O  VAL B 122   N  LEU B  97           
SHEET    7 AA2 8 VAL B 254  GLY B 259  1  O  ILE B 257   N  CYS B 123           
SHEET    8 AA2 8 LEU B 286  GLN B 292  1  O  ILE B 290   N  PHE B 256           
SHEET    1 AA3 8 GLU C   5  VAL C  11  0                                        
SHEET    2 AA3 8 ILE C  14  LYS C  21 -1  O  VAL C  18   N  ARG C   7           
SHEET    3 AA3 8 ARG C  53  PRO C  57 -1  O  ALA C  56   N  ALA C  19           
SHEET    4 AA3 8 VAL C  26  LEU C  30  1  N  VAL C  27   O  VAL C  55           
SHEET    5 AA3 8 VAL C  95  HIS C 100  1  O  PHE C  96   N  LEU C  28           
SHEET    6 AA3 8 VAL C 118  LEU C 124  1  O  VAL C 122   N  LEU C  97           
SHEET    7 AA3 8 VAL C 254  GLY C 259  1  O  LYS C 255   N  TYR C 121           
SHEET    8 AA3 8 LEU C 286  GLN C 292  1  O  GLN C 292   N  THR C 258           
CISPEP   1 PHE A   33    PRO A   34          0        -6.97                     
CISPEP   2 GLY A  195    PHE A  196          0        16.36                     
CISPEP   3 PRO A  201    ASN A  202          0        -7.18                     
CISPEP   4 PHE B   33    PRO B   34          0        -4.01                     
CISPEP   5 GLY B  193    THR B  194          0        19.60                     
CISPEP   6 PHE C   33    PRO C   34          0        -7.05                     
CRYST1  109.180  109.180  236.967  90.00  90.00  90.00 P 41 21 2    24          
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      0.009159  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009159  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004220        0.00000                         
TER    2560      PHE A 318                                                      
TER    5120      PHE B 318                                                      
TER    7680      PHE C 318                                                      
MASTER      433    0    0   51   24    0    0    6 8249    3    0   84          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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