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LongText Report for: 7al6-pdb

Name Class
7al6-pdb
HEADER    UNKNOWN FUNCTION                        05-OCT-20   7AL6              
TITLE     CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN PA1622 FROM PSEUDOMONAS 
TITLE    2 AERUGINOSA PAO1                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HYDROLASE;                                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA (STRAIN ATCC 15692 / DSM 
SOURCE   3 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1);   
SOURCE   4 ORGANISM_TAXID: 208964;                                              
SOURCE   5 STRAIN: ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228  
SOURCE   6 / 1C / PRS 101 / PAO1;                                               
SOURCE   7 GENE: PA1622;                                                        
SOURCE   8 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   9 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    PSEUDOMONAS AERUGINOSA, HYPOTHETICAL PROTEIN, ALPHA/BETA HYDROLASE    
KEYWDS   2 FOLD, PUTATIVE LIPOLYTIC ENZYME, UNKNOWN FUNCTION                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.G.FEILER,W.BLANKENFELDT                                             
REVDAT   1   14-OCT-20 7AL6    0                                                
JRNL        AUTH   C.G.FEILER,W.BLANKENFELDT                                    
JRNL        TITL   CRYSTAL STRUCTURE OF THE HYPOTHETICAL PROTEIN PA1622 FROM    
JRNL        TITL 2 PSEUDOMONAS AERUGINOSA PAO1                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (1.18.2_3874: ???)                            
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 44.76                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 91329                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.163                           
REMARK   3   FREE R VALUE                     : 0.207                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.970                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4540                            
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 44.7600 -  6.5200    1.00     2911   175  0.1703 0.1762        
REMARK   3     2  6.5200 -  5.1800    1.00     2946   139  0.1648 0.2276        
REMARK   3     3  5.1800 -  4.5200    1.00     2905   172  0.1298 0.1542        
REMARK   3     4  4.5200 -  4.1100    1.00     2877   154  0.1268 0.1686        
REMARK   3     5  4.1100 -  3.8200    1.00     2938   125  0.1359 0.1641        
REMARK   3     6  3.8200 -  3.5900    1.00     2904   146  0.1467 0.1721        
REMARK   3     7  3.5900 -  3.4100    1.00     2874   161  0.1576 0.2285        
REMARK   3     8  3.4100 -  3.2600    1.00     2908   161  0.1711 0.2372        
REMARK   3     9  3.2600 -  3.1400    1.00     2899   153  0.1789 0.2376        
REMARK   3    10  3.1400 -  3.0300    1.00     2862   175  0.1676 0.2388        
REMARK   3    11  3.0300 -  2.9300    1.00     2919   145  0.1763 0.2096        
REMARK   3    12  2.9300 -  2.8500    1.00     2825   170  0.1682 0.2096        
REMARK   3    13  2.8500 -  2.7800    1.00     2911   175  0.1666 0.2119        
REMARK   3    14  2.7700 -  2.7100    1.00     2883   165  0.1707 0.2132        
REMARK   3    15  2.7100 -  2.6500    1.00     2880   149  0.1774 0.2409        
REMARK   3    16  2.6500 -  2.5900    1.00     2909   122  0.1762 0.2233        
REMARK   3    17  2.5900 -  2.5400    1.00     2897   144  0.1671 0.2559        
REMARK   3    18  2.5400 -  2.4900    1.00     2870   143  0.1721 0.2447        
REMARK   3    19  2.4900 -  2.4500    1.00     2906   149  0.1750 0.2242        
REMARK   3    20  2.4500 -  2.4000    1.00     2892   160  0.1718 0.2403        
REMARK   3    21  2.4000 -  2.3700    1.00     2889   146  0.1722 0.2070        
REMARK   3    22  2.3700 -  2.3300    1.00     2877   151  0.1786 0.2161        
REMARK   3    23  2.3300 -  2.2900    1.00     2925   136  0.1791 0.2349        
REMARK   3    24  2.2900 -  2.2600    1.00     2922   142  0.1840 0.2422        
REMARK   3    25  2.2600 -  2.2300    1.00     2891   121  0.1894 0.2672        
REMARK   3    26  2.2300 -  2.2000    1.00     2876   152  0.2026 0.2094        
REMARK   3    27  2.2000 -  2.1800    1.00     2896   141  0.2012 0.2715        
REMARK   3    28  2.1800 -  2.1500    1.00     2851   169  0.2195 0.2496        
REMARK   3    29  2.1500 -  2.1200    1.00     2902   148  0.2155 0.2845        
REMARK   3    30  2.1200 -  2.1000    1.00     2844   151  0.2336 0.2772        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.210            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 21.230           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 34.36                          
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      :  0.013           9101                                  
REMARK   3   ANGLE     :  1.463          12332                                  
REMARK   3   CHIRALITY :  0.066           1369                                  
REMARK   3   PLANARITY :  0.010           1604                                  
REMARK   3   DIHEDRAL  : 20.754           1290                                  
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 7AL6 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 05-OCT-20.                  
REMARK 100 THE DEPOSITION ID IS D_1292111082.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.91841                            
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 91339                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.760                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 8.700                              
REMARK 200  R MERGE                    (I) : 0.09500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 15.7100                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.18                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.91800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.320                              
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: 7AL5                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 61.71                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.24 M MAGNESIUM FORMATE 22% PEG 3350    
REMARK 280  20MG/ML PROTEIN CONCENTRATION, PH 7, VAPOR DIFFUSION, HANGING       
REMARK 280  DROP, TEMPERATURE 293K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       49.37533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       98.75067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       74.06300            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      123.43833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       24.68767            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 14610 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 43670 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -47.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     MET C     1                                                      
REMARK 465     MET D     1                                                      
REMARK 465     SER D     2                                                      
REMARK 465     LEU D     3                                                      
REMARK 465     GLN D     4                                                      
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  HH11  ARG B    45     OE1  GLU B   270              1.12            
REMARK 500   OE1  GLU B   242     H    MET B   245              1.39            
REMARK 500   OE1  GLU C   255    HH12  ARG C   286              1.39            
REMARK 500   OE2  GLU A   235     O    HOH A   501              1.79            
REMARK 500   NH1  ARG B    45     OE1  GLU B   270              1.90            
REMARK 500   OE1  GLU A   235     O    HOH A   502              1.96            
REMARK 500   OE2  GLU C    94     O    HOH C   401              2.06            
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   HE1  MET B   171     HB3  HIS D   154     5554     1.25            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 226   CD    GLU A 226   OE1    -0.073                       
REMARK 500    GLU A 235   N     GLU A 235   CA      0.168                       
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    ASP A  38     -154.21    -95.81                                   
REMARK 500    TYR A  75       57.02   -118.90                                   
REMARK 500    SER A 102     -121.18     53.42                                   
REMARK 500    LEU A 128      -62.29   -149.54                                   
REMARK 500    VAL A 174     -139.26     54.08                                   
REMARK 500    GLU A 242       86.41   -155.18                                   
REMARK 500    ASP B  38     -153.07    -95.06                                   
REMARK 500    LEU B  50       70.96   -114.33                                   
REMARK 500    TYR B  75       62.80   -112.38                                   
REMARK 500    SER B 102     -120.15     57.37                                   
REMARK 500    LEU B 128      -57.16   -154.03                                   
REMARK 500    GLN B 236       39.33    -93.33                                   
REMARK 500    HIS B 264       41.42    -99.58                                   
REMARK 500    ASP C  38     -153.90    -90.10                                   
REMARK 500    TYR C  75       56.21   -117.47                                   
REMARK 500    SER C 102     -116.03     51.67                                   
REMARK 500    LEU C 128      -62.98   -151.28                                   
REMARK 500    VAL C 174     -135.52     49.45                                   
REMARK 500    ASP D  38     -152.07    -89.96                                   
REMARK 500    TYR D  75       53.54   -111.04                                   
REMARK 500    SER D 102     -118.65     54.56                                   
REMARK 500    LEU D 128      -61.61   -149.93                                   
REMARK 500    HIS D 264       41.28   -105.30                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG C 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE C 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG D 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 303                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO D 304                 
DBREF  7AL6 A    1   286  UNP    Q9I3A0   Q9I3A0_PSEAE     1    286             
DBREF  7AL6 B    1   286  UNP    Q9I3A0   Q9I3A0_PSEAE     1    286             
DBREF  7AL6 C    1   286  UNP    Q9I3A0   Q9I3A0_PSEAE     1    286             
DBREF  7AL6 D    1   286  UNP    Q9I3A0   Q9I3A0_PSEAE     1    286             
SEQRES   1 A  286  MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO          
SEQRES   2 A  286  HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP          
SEQRES   3 A  286  GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN          
SEQRES   4 A  286  ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY          
SEQRES   5 A  286  LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS          
SEQRES   6 A  286  SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP          
SEQRES   7 A  286  ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU          
SEQRES   8 A  286  GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY          
SEQRES   9 A  286  ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU          
SEQRES  10 A  286  ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO          
SEQRES  11 A  286  TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY          
SEQRES  12 A  286  GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG          
SEQRES  13 A  286  LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA          
SEQRES  14 A  286  ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA          
SEQRES  15 A  286  GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY          
SEQRES  16 A  286  GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO          
SEQRES  17 A  286  SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE          
SEQRES  18 A  286  VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA          
SEQRES  19 A  286  GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA          
SEQRES  20 A  286  LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO          
SEQRES  21 A  286  GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA          
SEQRES  22 A  286  GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG          
SEQRES   1 B  286  MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO          
SEQRES   2 B  286  HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP          
SEQRES   3 B  286  GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN          
SEQRES   4 B  286  ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY          
SEQRES   5 B  286  LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS          
SEQRES   6 B  286  SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP          
SEQRES   7 B  286  ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU          
SEQRES   8 B  286  GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY          
SEQRES   9 B  286  ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU          
SEQRES  10 B  286  ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO          
SEQRES  11 B  286  TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY          
SEQRES  12 B  286  GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG          
SEQRES  13 B  286  LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA          
SEQRES  14 B  286  ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA          
SEQRES  15 B  286  GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY          
SEQRES  16 B  286  GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO          
SEQRES  17 B  286  SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE          
SEQRES  18 B  286  VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA          
SEQRES  19 B  286  GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA          
SEQRES  20 B  286  LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO          
SEQRES  21 B  286  GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA          
SEQRES  22 B  286  GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG          
SEQRES   1 C  286  MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO          
SEQRES   2 C  286  HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP          
SEQRES   3 C  286  GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN          
SEQRES   4 C  286  ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY          
SEQRES   5 C  286  LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS          
SEQRES   6 C  286  SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP          
SEQRES   7 C  286  ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU          
SEQRES   8 C  286  GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY          
SEQRES   9 C  286  ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU          
SEQRES  10 C  286  ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO          
SEQRES  11 C  286  TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY          
SEQRES  12 C  286  GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG          
SEQRES  13 C  286  LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA          
SEQRES  14 C  286  ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA          
SEQRES  15 C  286  GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY          
SEQRES  16 C  286  GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO          
SEQRES  17 C  286  SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE          
SEQRES  18 C  286  VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA          
SEQRES  19 C  286  GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA          
SEQRES  20 C  286  LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO          
SEQRES  21 C  286  GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA          
SEQRES  22 C  286  GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG          
SEQRES   1 D  286  MET SER LEU GLN VAL GLU GLU VAL ARG ILE SER LEU PRO          
SEQRES   2 D  286  HIS ILE GLU LEU ALA ALA HIS LEU PHE GLY PRO PRO ASP          
SEQRES   3 D  286  GLY LYS PRO VAL ILE ALA LEU HIS GLY TRP LEU ASP ASN          
SEQRES   4 D  286  ALA MET SER PHE SER ARG LEU ALA PRO LYS LEU ALA GLY          
SEQRES   5 D  286  LEU ARG ILE VAL ALA LEU ASP PHE ALA GLY HIS GLY HIS          
SEQRES   6 D  286  SER ALA HIS ARG ALA GLU GLY ALA SER TYR LEU LEU TRP          
SEQRES   7 D  286  ASP TYR ALA LEU ASP VAL LEU MET VAL ALA GLU GLN LEU          
SEQRES   8 D  286  GLY TRP GLU ARG PHE SER LEU LEU GLY HIS SER MET GLY          
SEQRES   9 D  286  ALA ILE VAL SER VAL LEU LEU ALA GLY ALA LEU PRO GLU          
SEQRES  10 D  286  ARG ILE GLU ARG LEU ALA LEU ILE ASP GLY LEU ILE PRO          
SEQRES  11 D  286  TYR THR GLY GLU ALA ASP LYS ALA PRO GLN LYS LEU GLY          
SEQRES  12 D  286  GLU ALA LEU LYS ALA GLN LEU ALA LEU ARG HIS LYS ARG          
SEQRES  13 D  286  LYS PRO VAL TYR ALA GLU LEU GLU LYS ALA VAL GLU ALA          
SEQRES  14 D  286  ARG MET ARG GLY VAL GLY GLU ILE SER ARG GLU ALA ALA          
SEQRES  15 D  286  GLU LEU LEU ALA GLN ARG GLY LEU GLU PRO VAL PRO GLY          
SEQRES  16 D  286  GLY TYR THR TRP ARG THR ASP ALA ARG LEU THR LEU PRO          
SEQRES  17 D  286  SER PRO LEU ARG LEU THR GLN ALA HIS ALA LEU ASN PHE          
SEQRES  18 D  286  VAL ARG SER VAL GLU CYS PRO VAL SER LEU VAL LEU ALA          
SEQRES  19 D  286  GLU GLN GLY MET LEU ALA VAL GLU PRO ARG MET ARG ALA          
SEQRES  20 D  286  LEU LEU GLU THR LEU PRO PHE GLU ARG HIS HIS LEU PRO          
SEQRES  21 D  286  GLY GLY HIS HIS LEU HIS LEU ASP ASP GLU ALA GLY ALA          
SEQRES  22 D  286  GLN ALA VAL ALA ARG VAL PHE ALA ALA PHE PHE ALA ARG          
HET    PEG  A 401      17                                                       
HET    PEG  A 402      17                                                       
HET    PGE  A 403      24                                                       
HET    EDO  A 404      10                                                       
HET    PEG  C 301      17                                                       
HET    PEG  C 302      17                                                       
HET    PGE  C 303      24                                                       
HET    PEG  D 301      17                                                       
HET    EDO  D 302      10                                                       
HET    EDO  D 303      10                                                       
HET    EDO  D 304      10                                                       
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  PEG    5(C4 H10 O3)                                                 
FORMUL   7  PGE    2(C6 H14 O4)                                                 
FORMUL   8  EDO    4(C2 H6 O2)                                                  
FORMUL  16  HOH   *665(H2 O)                                                    
HELIX    1 AA1 ASN A   39  SER A   44  5                                   6    
HELIX    2 AA2 LEU A   46  LEU A   50  5                                   5    
HELIX    3 AA3 LEU A   76  GLY A   92  1                                  17    
HELIX    4 AA4 SER A  102  LEU A  115  1                                  14    
HELIX    5 AA5 GLU A  134  ASP A  136  5                                   3    
HELIX    6 AA6 LYS A  137  ALA A  151  1                                  15    
HELIX    7 AA7 LEU A  152  LYS A  155  5                                   4    
HELIX    8 AA8 GLU A  162  GLY A  173  1                                  12    
HELIX    9 AA9 SER A  178  GLY A  189  1                                  12    
HELIX   10 AB1 ASP A  202  LEU A  207  5                                   6    
HELIX   11 AB2 THR A  214  SER A  224  1                                  11    
HELIX   12 AB3 GLY A  237  GLU A  242  1                                   6    
HELIX   13 AB4 ARG A  244  THR A  251  1                                   8    
HELIX   14 AB5 HIS A  264  ASP A  269  1                                   6    
HELIX   15 AB6 ASP A  269  ALA A  285  1                                  17    
HELIX   16 AB7 ASN B   39  SER B   44  5                                   6    
HELIX   17 AB8 LEU B   46  LEU B   50  5                                   5    
HELIX   18 AB9 LEU B   76  GLY B   92  1                                  17    
HELIX   19 AC1 SER B  102  LEU B  115  1                                  14    
HELIX   20 AC2 GLU B  134  ASP B  136  5                                   3    
HELIX   21 AC3 LYS B  137  LEU B  152  1                                  16    
HELIX   22 AC4 ARG B  153  LYS B  155  5                                   3    
HELIX   23 AC5 GLU B  162  ARG B  172  1                                  11    
HELIX   24 AC6 SER B  178  GLY B  189  1                                  12    
HELIX   25 AC7 ASP B  202  LEU B  207  5                                   6    
HELIX   26 AC8 THR B  214  ARG B  223  1                                  10    
HELIX   27 AC9 GLY B  237  GLU B  242  1                                   6    
HELIX   28 AD1 GLU B  242  THR B  251  1                                  10    
HELIX   29 AD2 HIS B  264  ASP B  269  1                                   6    
HELIX   30 AD3 ASP B  269  ARG B  286  1                                  18    
HELIX   31 AD4 ASN C   39  SER C   44  5                                   6    
HELIX   32 AD5 ARG C   45  LEU C   50  1                                   6    
HELIX   33 AD6 LEU C   76  GLY C   92  1                                  17    
HELIX   34 AD7 SER C  102  LEU C  115  1                                  14    
HELIX   35 AD8 GLU C  134  ASP C  136  5                                   3    
HELIX   36 AD9 LYS C  137  LEU C  152  1                                  16    
HELIX   37 AE1 GLU C  162  ARG C  172  1                                  11    
HELIX   38 AE2 SER C  178  GLY C  189  1                                  12    
HELIX   39 AE3 ASP C  202  LEU C  207  5                                   6    
HELIX   40 AE4 THR C  214  SER C  224  1                                  11    
HELIX   41 AE5 MET C  238  VAL C  241  5                                   4    
HELIX   42 AE6 GLU C  242  THR C  251  1                                  10    
HELIX   43 AE7 HIS C  264  ASP C  269  1                                   6    
HELIX   44 AE8 ASP C  269  ARG C  286  1                                  18    
HELIX   45 AE9 ASN D   39  SER D   44  5                                   6    
HELIX   46 AF1 LEU D   46  LEU D   50  5                                   5    
HELIX   47 AF2 LEU D   76  GLY D   92  1                                  17    
HELIX   48 AF3 SER D  102  LEU D  115  1                                  14    
HELIX   49 AF4 GLU D  134  ASP D  136  5                                   3    
HELIX   50 AF5 LYS D  137  LEU D  152  1                                  16    
HELIX   51 AF6 GLU D  162  ARG D  172  1                                  11    
HELIX   52 AF7 SER D  178  GLY D  189  1                                  12    
HELIX   53 AF8 ASP D  202  LEU D  207  5                                   6    
HELIX   54 AF9 THR D  214  SER D  224  1                                  11    
HELIX   55 AG1 GLY D  237  GLU D  242  1                                   6    
HELIX   56 AG2 GLU D  242  THR D  251  1                                  10    
HELIX   57 AG3 HIS D  264  ASP D  269  1                                   6    
HELIX   58 AG4 ASP D  269  ARG D  286  1                                  18    
SHEET    1 AA1 8 GLU A   7  SER A  11  0                                        
SHEET    2 AA1 8 GLU A  16  PHE A  22 -1  O  LEU A  17   N  ILE A  10           
SHEET    3 AA1 8 LEU A  53  LEU A  58 -1  O  ALA A  57   N  HIS A  20           
SHEET    4 AA1 8 LYS A  28  LEU A  33  1  N  LYS A  28   O  ARG A  54           
SHEET    5 AA1 8 PHE A  96  HIS A 101  1  O  LEU A  99   N  LEU A  33           
SHEET    6 AA1 8 ILE A 119  ILE A 125  1  O  ILE A 125   N  GLY A 100           
SHEET    7 AA1 8 VAL A 229  ALA A 234  1  O  SER A 230   N  LEU A 124           
SHEET    8 AA1 8 GLU A 255  LEU A 259  1  O  GLU A 255   N  LEU A 231           
SHEET    1 AA2 2 LEU A 190  VAL A 193  0                                        
SHEET    2 AA2 2 GLY A 196  TRP A 199 -1  O  GLY A 196   N  VAL A 193           
SHEET    1 AA3 8 GLU B   7  SER B  11  0                                        
SHEET    2 AA3 8 GLU B  16  PHE B  22 -1  O  LEU B  17   N  ILE B  10           
SHEET    3 AA3 8 LEU B  53  LEU B  58 -1  O  ALA B  57   N  HIS B  20           
SHEET    4 AA3 8 LYS B  28  LEU B  33  1  N  LYS B  28   O  ARG B  54           
SHEET    5 AA3 8 PHE B  96  HIS B 101  1  O  HIS B 101   N  LEU B  33           
SHEET    6 AA3 8 ILE B 119  ILE B 125  1  O  ALA B 123   N  LEU B  98           
SHEET    7 AA3 8 VAL B 229  ALA B 234  1  O  SER B 230   N  LEU B 122           
SHEET    8 AA3 8 GLU B 255  LEU B 259  1  O  GLU B 255   N  LEU B 231           
SHEET    1 AA4 2 LEU B 190  VAL B 193  0                                        
SHEET    2 AA4 2 GLY B 196  TRP B 199 -1  O  GLY B 196   N  VAL B 193           
SHEET    1 AA5 8 GLU C   7  SER C  11  0                                        
SHEET    2 AA5 8 GLU C  16  PHE C  22 -1  O  LEU C  17   N  ILE C  10           
SHEET    3 AA5 8 LEU C  53  LEU C  58 -1  O  ALA C  57   N  HIS C  20           
SHEET    4 AA5 8 LYS C  28  LEU C  33  1  N  VAL C  30   O  VAL C  56           
SHEET    5 AA5 8 PHE C  96  HIS C 101  1  O  LEU C  99   N  LEU C  33           
SHEET    6 AA5 8 ILE C 119  ILE C 125  1  O  ILE C 125   N  GLY C 100           
SHEET    7 AA5 8 VAL C 229  ALA C 234  1  O  SER C 230   N  LEU C 124           
SHEET    8 AA5 8 GLU C 255  LEU C 259  1  O  HIS C 257   N  LEU C 233           
SHEET    1 AA6 2 LEU C 190  VAL C 193  0                                        
SHEET    2 AA6 2 GLY C 196  TRP C 199 -1  O  GLY C 196   N  VAL C 193           
SHEET    1 AA7 8 GLU D   7  SER D  11  0                                        
SHEET    2 AA7 8 GLU D  16  PHE D  22 -1  O  LEU D  17   N  ILE D  10           
SHEET    3 AA7 8 LEU D  53  LEU D  58 -1  O  ALA D  57   N  HIS D  20           
SHEET    4 AA7 8 LYS D  28  LEU D  33  1  N  VAL D  30   O  VAL D  56           
SHEET    5 AA7 8 PHE D  96  HIS D 101  1  O  LEU D  99   N  LEU D  33           
SHEET    6 AA7 8 ILE D 119  ILE D 125  1  O  ALA D 123   N  LEU D  98           
SHEET    7 AA7 8 VAL D 229  ALA D 234  1  O  SER D 230   N  LEU D 124           
SHEET    8 AA7 8 GLU D 255  LEU D 259  1  O  GLU D 255   N  LEU D 231           
SHEET    1 AA8 2 LEU D 190  VAL D 193  0                                        
SHEET    2 AA8 2 GLY D 196  TRP D 199 -1  O  GLY D 196   N  VAL D 193           
SITE     1 AC1  3 LEU A  77  SER A 209  ARG A 212                               
SITE     1 AC2  5 ARG A  95  GLU A 117  HOH A 665  GLU C 235                    
SITE     2 AC2  5 HIS C 258                                                     
SITE     1 AC3  2 LYS A  28  ALA A 285                                          
SITE     1 AC4  7 PRO A 228  VAL A 229  PRO A 253  GLU A 255                    
SITE     2 AC4  7 HOH A 563  HOH A 609  ARG C 278                               
SITE     1 AC5  3 ARG A  54  TRP A  93  TYR C 197                               
SITE     1 AC6  7 GLU C 176  SER C 178  GLN C 236  GLY C 261                    
SITE     2 AC6  7 GLY C 262  ASP C 268  HOH C 553                               
SITE     1 AC7  1 LEU C   3                                                     
SITE     1 AC8  4 LEU C 184  GLU D 250  HOH D 513  HOH D 515                    
SITE     1 AC9  2 LEU D  21  ARG D  54                                          
SITE     1 AD1  3 SER D 209  ARG D 212  HOH D 444                               
SITE     1 AD2  3 ILE D 129  PRO D 130  TYR D 131                               
CRYST1  136.758  136.758  148.126  90.00  90.00 120.00 P 61         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      0.007312  0.004222  0.000000        0.00000                         
SCALE2      0.000000  0.008443  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006751        0.00000                         
TER    4472      ARG A 286                                                      
TER    8905      ARG B 286                                                      
TER   13357      ARG C 286                                                      
TER   17768      ARG D 286                                                      
MASTER      384    0   11   58   40    0   14    6 9513    4  173   88          
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
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