Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 5xmd-pdb

Name Class
5xmd-pdb
HEADER    HYDROLASE                               14-MAY-17   5XMD              
TITLE     CRYSTAL STRUCTURE OF EPOXIDE HYDROLASE VREH1 FROM VIGNA RADIATA       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EPOXIDE HYDROLASE A;                                       
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: VIGNA RADIATA;                                  
SOURCE   3 ORGANISM_COMMON: MUNG BEAN;                                          
SOURCE   4 ORGANISM_TAXID: 157791;                                              
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    EPOXIDE HYDROLASE ENANTIOCONVERGENT, HYDROLASE                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.D.KONG,J.H.XU,J.H.ZHOU                                              
REVDAT   1   16-MAY-18 5XMD    0                                                
JRNL        AUTH   X.D.KONG,J.H.XU,J.H.ZHOU                                     
JRNL        TITL   CRYSTAL STRUCTURE OF CARBOXYL REDUCTASE                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 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) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.32                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 82530                          
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   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4127                            
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 41.3251 -  6.1313    0.97     2976   158  0.1490 0.1658        
REMARK   3     2  6.1313 -  4.8691    0.99     2948   141  0.1538 0.1702        
REMARK   3     3  4.8691 -  4.2543    0.99     2895   148  0.1295 0.1497        
REMARK   3     4  4.2543 -  3.8656    0.97     2830   159  0.1446 0.1615        
REMARK   3     5  3.8656 -  3.5887    0.91     2676   144  0.1513 0.1959        
REMARK   3     6  3.5887 -  3.3772    0.92     2669   134  0.1775 0.2410        
REMARK   3     7  3.3772 -  3.2082    0.96     2796   141  0.1881 0.2279        
REMARK   3     8  3.2082 -  3.0686    0.95     2768   148  0.1990 0.2544        
REMARK   3     9  3.0686 -  2.9505    0.93     2688   163  0.2116 0.2394        
REMARK   3    10  2.9505 -  2.8487    0.92     2624   148  0.2140 0.2657        
REMARK   3    11  2.8487 -  2.7596    0.92     2690   117  0.2062 0.2652        
REMARK   3    12  2.7596 -  2.6808    0.90     2581   150  0.1983 0.2397        
REMARK   3    13  2.6808 -  2.6102    0.91     2615   147  0.1977 0.2721        
REMARK   3    14  2.6102 -  2.5465    0.90     2592   146  0.1884 0.2980        
REMARK   3    15  2.5465 -  2.4886    0.92     2601   152  0.1973 0.2407        
REMARK   3    16  2.4886 -  2.4357    0.91     2645   136  0.2012 0.2520        
REMARK   3    17  2.4357 -  2.3870    0.92     2664   119  0.1976 0.2633        
REMARK   3    18  2.3870 -  2.3419    0.92     2624   141  0.1948 0.2784        
REMARK   3    19  2.3419 -  2.3001    0.92     2690   121  0.2013 0.2311        
REMARK   3    20  2.3001 -  2.2611    0.94     2662   126  0.2088 0.3032        
REMARK   3    21  2.2611 -  2.2247    0.93     2710   139  0.2204 0.2826        
REMARK   3    22  2.2247 -  2.1904    0.94     2686   125  0.2231 0.2493        
REMARK   3    23  2.1904 -  2.1582    0.94     2664   138  0.2087 0.2771        
REMARK   3    24  2.1582 -  2.1278    0.94     2765   138  0.2115 0.2668        
REMARK   3    25  2.1278 -  2.0991    0.95     2695   155  0.2265 0.3292        
REMARK   3    26  2.0991 -  2.0718    0.95     2656   149  0.2246 0.2751        
REMARK   3    27  2.0718 -  2.0459    0.95     2785   143  0.2346 0.3145        
REMARK   3    28  2.0459 -  2.0213    0.95     2713   164  0.2504 0.2967        
REMARK   3    29  2.0213 -  1.9978    0.89     2495   137  0.2642 0.3102        
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)     : 0.220            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.670           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.26                          
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          10281                                  
REMARK   3   ANGLE     :  1.047          13986                                  
REMARK   3   CHIRALITY :  0.074           1502                                  
REMARK   3   PLANARITY :  0.005           1795                                  
REMARK   3   DIHEDRAL  : 14.142           3741                                  
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 5XMD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 24-MAY-17.                  
REMARK 100 THE DEPOSITION ID IS D_1300003775.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-MAY-11                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
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) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000, HKL                      
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000, HKL                      
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 82570                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
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     (%) : 93.7                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.8000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.72100                            
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: PHASER                                                
REMARK 200 STARTING MODEL: 2CJP                                                 
REMARK 200                                                                      
REMARK 200 REMARK: PLATE                                                        
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.81                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.27                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 25% PEG 3350, 0.1M HEPES PH 6.5-7.0,     
REMARK 280  0.2M NACL, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K          
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       25.94600            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: BIOLOGICAL UNIT IS THE SAME AS ASYM.                         
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -51.89200            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000      -92.43649            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000      -25.94600            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000     -123.94899            
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     ASN A   167                                                      
REMARK 465     ASN A   168                                                      
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     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     SER C   166                                                      
REMARK 465     ASN C   167                                                      
REMARK 465     ASN C   168                                                      
REMARK 465     GLU C   191                                                      
REMARK 465     GLY C   192                                                      
REMARK 465     VAL C   193                                                      
REMARK 465     ALA C   194                                                      
REMARK 465     LEU C   195                                                      
REMARK 465     PRO C   196                                                      
REMARK 465     SER C   197                                                      
REMARK 465     GLY C   198                                                      
REMARK 465     SER C   199                                                      
REMARK 465     LEU C   200                                                      
REMARK 465     PRO C   201                                                      
REMARK 465     SER C   202                                                      
REMARK 465     ARG C   203                                                      
REMARK 465     MET D   -33                                                      
REMARK 465     GLY D   -32                                                      
REMARK 465     SER D   -31                                                      
REMARK 465     SER D   -30                                                      
REMARK 465     HIS D   -29                                                      
REMARK 465     HIS D   -28                                                      
REMARK 465     HIS D   -27                                                      
REMARK 465     HIS D   -26                                                      
REMARK 465     HIS D   -25                                                      
REMARK 465     HIS D   -24                                                      
REMARK 465     SER D   -23                                                      
REMARK 465     SER D   -22                                                      
REMARK 465     GLY D   -21                                                      
REMARK 465     LEU D   -20                                                      
REMARK 465     VAL D   -19                                                      
REMARK 465     PRO D   -18                                                      
REMARK 465     ARG D   -17                                                      
REMARK 465     GLY D   -16                                                      
REMARK 465     SER D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     MET D   -13                                                      
REMARK 465     ALA D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     MET D   -10                                                      
REMARK 465     THR D    -9                                                      
REMARK 465     GLY D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     GLN D    -6                                                      
REMARK 465     GLN D    -5                                                      
REMARK 465     MET D    -4                                                      
REMARK 465     GLY D    -3                                                      
REMARK 465     ARG D    -2                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     GLY D   192                                                      
REMARK 465     VAL D   193                                                      
REMARK 465     ALA D   194                                                      
REMARK 465     LEU D   195                                                      
REMARK 465     PRO D   196                                                      
REMARK 465     SER D   197                                                      
REMARK 465     GLY D   198                                                      
REMARK 465     SER D   199                                                      
REMARK 465     LEU D   200                                                      
REMARK 465     PRO D   201                                                      
REMARK 465     SER D   202                                                      
REMARK 465     ARG D   203                                                      
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    SER B   202     O    HOH B   401              2.01            
REMARK 500   O    HOH B   438     O    HOH B   525              2.15            
REMARK 500   O    HOH B   495     O    HOH B   516              2.16            
REMARK 500   O    HOH A   515     O    HOH A   549              2.17            
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 B   475     O    HOH D   512     2444     2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    GLU A  35     -160.07   -122.01                                   
REMARK 500    ASP A 101     -133.99     59.48                                   
REMARK 500    SER A 125      -58.47     76.77                                   
REMARK 500    TYR A 164      -75.27    -76.38                                   
REMARK 500    ALA A 297     -156.12    -94.73                                   
REMARK 500    GLU B  35     -164.85   -124.35                                   
REMARK 500    ASP B 101     -128.12     60.68                                   
REMARK 500    SER B 125      -49.70     75.87                                   
REMARK 500    ASN B 168       39.75   -156.13                                   
REMARK 500    VAL B 193       15.43   -148.35                                   
REMARK 500    SER B 202       87.90     76.63                                   
REMARK 500    ALA B 297     -152.64    -94.89                                   
REMARK 500    PHE B 299       59.06    -94.11                                   
REMARK 500    SER C   0      120.04     77.34                                   
REMARK 500    GLU C  35     -169.39   -115.92                                   
REMARK 500    SER C  72        1.99    -69.06                                   
REMARK 500    ASP C 101     -128.50     57.89                                   
REMARK 500    SER C 125      -50.10     77.26                                   
REMARK 500    PRO C 185      108.81    -50.35                                   
REMARK 500    PRO C 189     -110.53    -69.45                                   
REMARK 500    ALA C 297     -153.71    -93.53                                   
REMARK 500    GLU D  35     -162.94   -124.10                                   
REMARK 500    ASP D 101     -133.63     57.77                                   
REMARK 500    SER D 125      -44.42     76.44                                   
REMARK 500    ASN D 169       87.19   -162.31                                   
REMARK 500    ALA D 297     -149.92    -89.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 RESIDUE 285 SHOULD BE PRO AND WAS CONFIRMED BY SEQUENCING OF THE     
REMARK 999 ORIGINAL CONSTRUCT. THE CONFLICT SHOULD BE DUE TO MISTAKE IN         
REMARK 999 SEQUENCE REFERENCE E5L4L1_VIGRA.                                     
DBREF  5XMD A    1   319  UNP    E5L4L1   E5L4L1_VIGRA     1    319             
DBREF  5XMD B    1   319  UNP    E5L4L1   E5L4L1_VIGRA     1    319             
DBREF  5XMD C    1   319  UNP    E5L4L1   E5L4L1_VIGRA     1    319             
DBREF  5XMD D    1   319  UNP    E5L4L1   E5L4L1_VIGRA     1    319             
SEQADV 5XMD MET A  -33  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A  -32  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A  -31  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A  -30  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -29  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -28  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -27  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -26  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -25  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -24  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A  -23  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A  -22  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A  -21  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD LEU A  -20  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD VAL A  -19  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO A  -18  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG A  -17  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A  -16  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A  -15  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS A  -14  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET A  -13  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ALA A  -12  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A  -11  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET A  -10  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD THR A   -9  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A   -8  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A   -7  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN A   -6  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN A   -5  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET A   -4  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A   -3  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG A   -2  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY A   -1  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER A    0  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO A  285  UNP  E5L4L1    HIS   285 SEE SEQUENCE DETAILS           
SEQADV 5XMD MET B  -33  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B  -32  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B  -31  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B  -30  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -29  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -28  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -27  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -26  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -25  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -24  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B  -23  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B  -22  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B  -21  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD LEU B  -20  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD VAL B  -19  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO B  -18  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG B  -17  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B  -16  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B  -15  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS B  -14  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET B  -13  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ALA B  -12  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B  -11  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET B  -10  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD THR B   -9  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B   -8  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B   -7  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN B   -6  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN B   -5  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET B   -4  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B   -3  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG B   -2  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY B   -1  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER B    0  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO B  285  UNP  E5L4L1    HIS   285 SEE SEQUENCE DETAILS           
SEQADV 5XMD MET C  -33  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C  -32  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C  -31  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C  -30  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -29  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -28  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -27  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -26  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -25  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -24  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C  -23  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C  -22  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C  -21  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD LEU C  -20  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD VAL C  -19  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO C  -18  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG C  -17  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C  -16  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C  -15  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS C  -14  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET C  -13  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ALA C  -12  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C  -11  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET C  -10  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD THR C   -9  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C   -8  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C   -7  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN C   -6  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN C   -5  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET C   -4  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C   -3  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG C   -2  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY C   -1  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER C    0  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO C  285  UNP  E5L4L1    HIS   285 SEE SEQUENCE DETAILS           
SEQADV 5XMD MET D  -33  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D  -32  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D  -31  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D  -30  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -29  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -28  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -27  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -26  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -25  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -24  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D  -23  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D  -22  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D  -21  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD LEU D  -20  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD VAL D  -19  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO D  -18  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG D  -17  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D  -16  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D  -15  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD HIS D  -14  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET D  -13  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ALA D  -12  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D  -11  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET D  -10  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD THR D   -9  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D   -8  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D   -7  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN D   -6  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLN D   -5  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD MET D   -4  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D   -3  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD ARG D   -2  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD GLY D   -1  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD SER D    0  UNP  E5L4L1              EXPRESSION TAG                 
SEQADV 5XMD PRO D  285  UNP  E5L4L1    HIS   285 SEE SEQUENCE DETAILS           
SEQRES   1 A  353  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  353  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 A  353  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 A  353  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 A  353  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 A  353  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 A  353  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 A  353  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER          
SEQRES   9 A  353  ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE          
SEQRES  10 A  353  VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE          
SEQRES  11 A  353  LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR          
SEQRES  12 A  353  LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL          
SEQRES  13 A  353  CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL          
SEQRES  14 A  353  ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP          
SEQRES  15 A  353  TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU          
SEQRES  16 A  353  ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE          
SEQRES  17 A  353  LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE          
SEQRES  18 A  353  LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU          
SEQRES  19 A  353  PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP          
SEQRES  20 A  353  VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU          
SEQRES  21 A  353  THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN          
SEQRES  22 A  353  TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS          
SEQRES  23 A  353  VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL          
SEQRES  24 A  353  TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY          
SEQRES  25 A  353  ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL          
SEQRES  26 A  353  VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA          
SEQRES  27 A  353  ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS          
SEQRES  28 A  353  LYS PHE                                                      
SEQRES   1 B  353  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 B  353  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 B  353  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 B  353  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 B  353  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 B  353  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 B  353  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 B  353  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER          
SEQRES   9 B  353  ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE          
SEQRES  10 B  353  VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE          
SEQRES  11 B  353  LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR          
SEQRES  12 B  353  LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL          
SEQRES  13 B  353  CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL          
SEQRES  14 B  353  ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP          
SEQRES  15 B  353  TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU          
SEQRES  16 B  353  ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE          
SEQRES  17 B  353  LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE          
SEQRES  18 B  353  LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU          
SEQRES  19 B  353  PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP          
SEQRES  20 B  353  VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU          
SEQRES  21 B  353  THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN          
SEQRES  22 B  353  TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS          
SEQRES  23 B  353  VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL          
SEQRES  24 B  353  TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY          
SEQRES  25 B  353  ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL          
SEQRES  26 B  353  VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA          
SEQRES  27 B  353  ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS          
SEQRES  28 B  353  LYS PHE                                                      
SEQRES   1 C  353  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 C  353  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 C  353  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 C  353  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 C  353  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 C  353  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 C  353  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 C  353  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER          
SEQRES   9 C  353  ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE          
SEQRES  10 C  353  VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE          
SEQRES  11 C  353  LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR          
SEQRES  12 C  353  LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL          
SEQRES  13 C  353  CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL          
SEQRES  14 C  353  ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP          
SEQRES  15 C  353  TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU          
SEQRES  16 C  353  ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE          
SEQRES  17 C  353  LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE          
SEQRES  18 C  353  LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU          
SEQRES  19 C  353  PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP          
SEQRES  20 C  353  VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU          
SEQRES  21 C  353  THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN          
SEQRES  22 C  353  TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS          
SEQRES  23 C  353  VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL          
SEQRES  24 C  353  TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY          
SEQRES  25 C  353  ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL          
SEQRES  26 C  353  VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA          
SEQRES  27 C  353  ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS          
SEQRES  28 C  353  LYS PHE                                                      
SEQRES   1 D  353  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 D  353  LEU VAL PRO ARG GLY SER HIS MET ALA SER MET THR GLY          
SEQRES   3 D  353  GLY GLN GLN MET GLY ARG GLY SER MET GLU GLU ILE GLU          
SEQRES   4 D  353  HIS ARG THR VAL GLU VAL ASN GLY ILE LYS MET HIS VAL          
SEQRES   5 D  353  ALA GLU LYS GLY GLU GLY PRO VAL VAL LEU PHE LEU HIS          
SEQRES   6 D  353  GLY PHE PRO GLU LEU TRP TYR SER TRP ARG HIS GLN ILE          
SEQRES   7 D  353  LEU ALA LEU SER SER ARG GLY TYR ARG ALA VAL ALA PRO          
SEQRES   8 D  353  ASP LEU ARG GLY TYR GLY ASP THR GLU ALA PRO GLU SER          
SEQRES   9 D  353  ILE SER SER TYR THR ILE MET HIS LEU VAL GLY ASP ILE          
SEQRES  10 D  353  VAL ALA LEU ILE ASP SER LEU GLY VAL GLY GLN VAL PHE          
SEQRES  11 D  353  LEU VAL ALA HIS ASP TRP GLY ALA ILE VAL GLY TRP TYR          
SEQRES  12 D  353  LEU CYS LEU PHE ARG PRO GLU LYS ILE LYS ALA TYR VAL          
SEQRES  13 D  353  CYS LEU SER VAL PRO PHE MET PRO ARG ASN PRO LYS VAL          
SEQRES  14 D  353  ARG PRO VAL ASP ALA MET ARG ALA LEU TYR GLY ASP ASP          
SEQRES  15 D  353  TYR TYR ILE CYS ARG PHE GLN GLU PRO GLY LYS ALA GLU          
SEQRES  16 D  353  ALA LEU TYR GLY SER ASN ASN ASN ILE GLY GLU VAL ILE          
SEQRES  17 D  353  LYS SER ILE LEU THR ASN ARG ARG PRO GLY PRO PRO ILE          
SEQRES  18 D  353  LEU PRO LYS GLU GLY VAL ALA LEU PRO SER GLY SER LEU          
SEQRES  19 D  353  PRO SER ARG PRO LEU PRO SER TRP LEU SER GLU GLU ASP          
SEQRES  20 D  353  VAL THR TYR TYR ALA SER LYS PHE SER LYS THR GLY LEU          
SEQRES  21 D  353  THR GLY GLY LEU ASN TYR TYR ARG ASN LEU ASN LEU ASN          
SEQRES  22 D  353  TRP GLU LEU THR ALA ALA TRP THR GLY ALA LYS VAL LYS          
SEQRES  23 D  353  VAL PRO VAL LYS PHE ILE THR GLY ASP LEU ASP VAL VAL          
SEQRES  24 D  353  TYR THR SER LEU GLY ILE LYS ASP TYR ILE ASP SER GLY          
SEQRES  25 D  353  ALA PHE LYS ARG ASP VAL PRO TYR LEU GLU GLU VAL VAL          
SEQRES  26 D  353  VAL GLN GLU GLY VAL ALA HIS PHE ASN ASN GLN GLU ALA          
SEQRES  27 D  353  ALA GLU ASP ILE SER ASN HIS ILE TYR GLU PHE ILE LYS          
SEQRES  28 D  353  LYS PHE                                                      
FORMUL   5  HOH   *543(H2 O)                                                    
HELIX    1 AA1 SER A    0  ILE A    4  5                                   5    
HELIX    2 AA2 LEU A   36  SER A   39  5                                   4    
HELIX    3 AA3 TRP A   40  SER A   49  1                                  10    
HELIX    4 AA4 SER A   70  TYR A   74  5                                   5    
HELIX    5 AA5 THR A   75  LEU A   90  1                                  16    
HELIX    6 AA6 ASP A  101  ARG A  114  1                                  14    
HELIX    7 AA7 ARG A  136  GLY A  146  1                                  11    
HELIX    8 AA8 TYR A  149  PHE A  154  1                                   6    
HELIX    9 AA9 GLY A  158  SER A  166  1                                   9    
HELIX   10 AB1 ILE A  170  ASN A  180  1                                  11    
HELIX   11 AB2 LEU A  195  LEU A  200  5                                   6    
HELIX   12 AB3 SER A  210  GLY A  225  1                                  16    
HELIX   13 AB4 LEU A  226  ARG A  234  1                                   9    
HELIX   14 AB5 ASN A  235  THR A  243  1                                   9    
HELIX   15 AB6 ALA A  244  THR A  247  5                                   4    
HELIX   16 AB7 GLY A  270  SER A  277  1                                   8    
HELIX   17 AB8 GLY A  278  VAL A  284  1                                   7    
HELIX   18 AB9 PHE A  299  ALA A  304  1                                   6    
HELIX   19 AC1 ALA A  304  LYS A  317  1                                  14    
HELIX   20 AC2 SER B    0  ILE B    4  5                                   5    
HELIX   21 AC3 LEU B   36  SER B   39  5                                   4    
HELIX   22 AC4 TRP B   40  SER B   49  1                                  10    
HELIX   23 AC5 SER B   70  TYR B   74  5                                   5    
HELIX   24 AC6 THR B   75  GLY B   91  1                                  17    
HELIX   25 AC7 ASP B  101  ARG B  114  1                                  14    
HELIX   26 AC8 ARG B  136  GLY B  146  1                                  11    
HELIX   27 AC9 TYR B  149  PHE B  154  1                                   6    
HELIX   28 AD1 GLY B  158  GLY B  165  1                                   8    
HELIX   29 AD2 ASN B  169  ASN B  180  1                                  12    
HELIX   30 AD3 PRO B  196  LEU B  200  5                                   5    
HELIX   31 AD4 SER B  210  GLY B  225  1                                  16    
HELIX   32 AD5 LEU B  226  ARG B  234  1                                   9    
HELIX   33 AD6 ASN B  235  THR B  243  1                                   9    
HELIX   34 AD7 ALA B  244  THR B  247  5                                   4    
HELIX   35 AD8 ASP B  263  SER B  268  1                                   6    
HELIX   36 AD9 GLY B  270  SER B  277  1                                   8    
HELIX   37 AE1 GLY B  278  VAL B  284  1                                   7    
HELIX   38 AE2 PHE B  299  ALA B  304  1                                   6    
HELIX   39 AE3 ALA B  304  LYS B  317  1                                  14    
HELIX   40 AE4 SER C    0  ILE C    4  5                                   5    
HELIX   41 AE5 LEU C   36  SER C   39  5                                   4    
HELIX   42 AE6 TRP C   40  SER C   49  1                                  10    
HELIX   43 AE7 SER C   70  TYR C   74  5                                   5    
HELIX   44 AE8 THR C   75  LEU C   90  1                                  16    
HELIX   45 AE9 ASP C  101  ARG C  114  1                                  14    
HELIX   46 AF1 ARG C  136  GLY C  146  1                                  11    
HELIX   47 AF2 TYR C  149  GLN C  155  1                                   7    
HELIX   48 AF3 GLY C  158  GLY C  165  1                                   8    
HELIX   49 AF4 ILE C  170  ASN C  180  1                                  11    
HELIX   50 AF5 SER C  210  GLY C  225  1                                  16    
HELIX   51 AF6 LEU C  226  ARG C  234  1                                   9    
HELIX   52 AF7 ASN C  235  THR C  243  1                                   9    
HELIX   53 AF8 ALA C  244  THR C  247  5                                   4    
HELIX   54 AF9 GLY C  270  SER C  277  1                                   8    
HELIX   55 AG1 GLY C  278  VAL C  284  1                                   7    
HELIX   56 AG2 PHE C  299  ALA C  304  1                                   6    
HELIX   57 AG3 ALA C  304  LYS C  317  1                                  14    
HELIX   58 AG4 LYS C  318  PHE C  319  5                                   2    
HELIX   59 AG5 SER D    0  ILE D    4  5                                   5    
HELIX   60 AG6 LEU D   36  SER D   39  5                                   4    
HELIX   61 AG7 TRP D   40  SER D   49  1                                  10    
HELIX   62 AG8 SER D   70  TYR D   74  5                                   5    
HELIX   63 AG9 THR D   75  LEU D   90  1                                  16    
HELIX   64 AH1 ASP D  101  ARG D  114  1                                  14    
HELIX   65 AH2 ARG D  136  GLY D  146  1                                  11    
HELIX   66 AH3 TYR D  149  PHE D  154  1                                   6    
HELIX   67 AH4 GLY D  158  SER D  166  1                                   9    
HELIX   68 AH5 ASN D  169  ASN D  180  1                                  12    
HELIX   69 AH6 SER D  210  GLY D  225  1                                  16    
HELIX   70 AH7 LEU D  226  ARG D  234  1                                   9    
HELIX   71 AH8 ASN D  235  THR D  243  1                                   9    
HELIX   72 AH9 ALA D  244  THR D  247  5                                   4    
HELIX   73 AI1 ASP D  263  SER D  268  1                                   6    
HELIX   74 AI2 GLY D  270  SER D  277  1                                   8    
HELIX   75 AI3 GLY D  278  VAL D  284  1                                   7    
HELIX   76 AI4 PHE D  299  ALA D  304  1                                   6    
HELIX   77 AI5 ALA D  304  LYS D  317  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  MET A  16   N  VAL A   9           
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  PHE A  29   O  VAL A  55           
SHEET    5 AA1 8 VAL A  95  HIS A 100  1  O  VAL A  98   N  LEU A  28           
SHEET    6 AA1 8 ILE A 118  LEU A 124  1  O  VAL A 122   N  LEU A  97           
SHEET    7 AA1 8 VAL A 255  GLY A 260  1  O  ILE A 258   N  CYS A 123           
SHEET    8 AA1 8 VAL A 291  GLN A 293  1  O  GLN A 293   N  THR A 259           
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  PHE B  29   O  VAL B  55           
SHEET    5 AA2 8 VAL B  95  HIS B 100  1  O  PHE B  96   N  LEU B  28           
SHEET    6 AA2 8 ILE B 118  LEU B 124  1  O  VAL B 122   N  LEU B  97           
SHEET    7 AA2 8 VAL B 255  GLY B 260  1  O  ILE B 258   N  CYS B 123           
SHEET    8 AA2 8 LEU B 287  GLN B 293  1  O  GLN B 293   N  THR B 259           
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  PHE C  29   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 ILE C 118  LEU C 124  1  O  VAL C 122   N  LEU C  97           
SHEET    7 AA3 8 VAL C 255  GLY C 260  1  O  ILE C 258   N  CYS C 123           
SHEET    8 AA3 8 VAL C 291  GLN C 293  1  O  GLN C 293   N  THR C 259           
SHEET    1 AA4 8 GLU D   5  VAL D  11  0                                        
SHEET    2 AA4 8 ILE D  14  LYS D  21 -1  O  MET D  16   N  VAL D   9           
SHEET    3 AA4 8 ARG D  53  PRO D  57 -1  O  ALA D  56   N  ALA D  19           
SHEET    4 AA4 8 VAL D  26  LEU D  30  1  N  PHE D  29   O  VAL D  55           
SHEET    5 AA4 8 VAL D  95  HIS D 100  1  O  PHE D  96   N  LEU D  28           
SHEET    6 AA4 8 ILE D 118  LEU D 124  1  O  VAL D 122   N  LEU D  97           
SHEET    7 AA4 8 VAL D 255  GLY D 260  1  O  ILE D 258   N  CYS D 123           
SHEET    8 AA4 8 LEU D 287  GLN D 293  1  O  GLN D 293   N  THR D 259           
CISPEP   1 PHE A   33    PRO A   34          0        -6.43                     
CISPEP   2 PHE B   33    PRO B   34          0        -5.24                     
CISPEP   3 PHE C   33    PRO C   34          0        -5.35                     
CISPEP   4 PHE D   33    PRO D   34          0       -10.39                     
CRYST1  101.691   51.892  124.294  90.00  94.27  90.00 P 1 21 1      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      0.009834  0.000000  0.000734        0.00000                         
SCALE2      0.000000  0.019271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008068        0.00000                         
TER    2550      PHE A 319                                                      
TER    5101      PHE B 319                                                      
TER    7531      PHE C 319                                                      
TER   10005      PHE D 319                                                      
MASTER      467    0    0   77   32    0    0    610512    4    0  112          
END                                                                             

Send your questions or comments to :
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:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
webmaster

Acknowledgements and disclaimer