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LongText Report for: 7ci0-pdb

Name Class
7ci0-pdb
HEADER    HYDROLASE                               06-JUL-20   7CI0              
TITLE     MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT S162A                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;                           
SOURCE   3 ORGANISM_TAXID: 1044;                                                
SOURCE   4 GENE: EH31_02760;                                                    
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI K-12;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: K-12                                       
KEYWDS    ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.YANG,Z.LI,X.XU,J.LI                                                 
REVDAT   1   14-JUL-21 7CI0    0                                                
JRNL        AUTH   X.YANG                                                       
JRNL        TITL   MICROBIAL HORMONE-SENSITIVE LIPASE E53 MUTANT S162A          
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3247                                     
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 : CDL V1.2                                      
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 47.35                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.340                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 221017                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.172                           
REMARK   3   R VALUE            (WORKING SET) : 0.171                           
REMARK   3   FREE R VALUE                     : 0.191                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.010                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 11063                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 47.3500 -  5.2900    1.00     7477   390  0.1683 0.1898        
REMARK   3     2  5.2900 -  4.2000    1.00     7174   389  0.1316 0.1346        
REMARK   3     3  4.2000 -  3.6700    1.00     7119   392  0.1435 0.1539        
REMARK   3     4  3.6700 -  3.3300    1.00     7102   368  0.1574 0.1740        
REMARK   3     5  3.3300 -  3.0900    1.00     7060   358  0.1732 0.1952        
REMARK   3     6  3.0900 -  2.9100    1.00     7040   381  0.1773 0.1948        
REMARK   3     7  2.9100 -  2.7600    1.00     7026   367  0.1733 0.1922        
REMARK   3     8  2.7600 -  2.6400    1.00     7033   371  0.1687 0.1989        
REMARK   3     9  2.6400 -  2.5400    1.00     6945   395  0.1730 0.1939        
REMARK   3    10  2.5400 -  2.4500    1.00     6991   370  0.1730 0.2034        
REMARK   3    11  2.4500 -  2.3800    1.00     6982   402  0.1707 0.1999        
REMARK   3    12  2.3800 -  2.3100    1.00     6969   381  0.1708 0.2004        
REMARK   3    13  2.3100 -  2.2500    1.00     6954   359  0.1761 0.2186        
REMARK   3    14  2.2500 -  2.1900    1.00     6988   356  0.1815 0.2018        
REMARK   3    15  2.1900 -  2.1400    1.00     6920   406  0.1866 0.2111        
REMARK   3    16  2.1400 -  2.1000    1.00     6985   381  0.1897 0.2195        
REMARK   3    17  2.1000 -  2.0600    1.00     6898   400  0.1906 0.2100        
REMARK   3    18  2.0600 -  2.0200    1.00     6950   370  0.1945 0.2129        
REMARK   3    19  2.0200 -  1.9800    1.00     6977   354  0.1907 0.2101        
REMARK   3    20  1.9800 -  1.9500    1.00     6944   357  0.1938 0.2268        
REMARK   3    21  1.9500 -  1.9200    1.00     6941   371  0.1962 0.2207        
REMARK   3    22  1.9200 -  1.8900    1.00     6968   369  0.1998 0.2156        
REMARK   3    23  1.8900 -  1.8600    1.00     6923   357  0.2056 0.2405        
REMARK   3    24  1.8600 -  1.8300    1.00     6958   355  0.2144 0.2458        
REMARK   3    25  1.8300 -  1.8100    1.00     6902   372  0.2274 0.2614        
REMARK   3    26  1.8100 -  1.7900    1.00     6967   346  0.2344 0.2582        
REMARK   3    27  1.7900 -  1.7600    1.00     6890   354  0.2467 0.2766        
REMARK   3    28  1.7600 -  1.7400    1.00     7008   335  0.2478 0.2580        
REMARK   3    29  1.7400 -  1.7200    1.00     6892   346  0.2622 0.2848        
REMARK   3    30  1.7200 -  1.7000    0.97     6796   311  0.3302 0.3628        
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)     : 0.184            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 22.245           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 27.09                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.54                          
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      :  0.011           9678                                  
REMARK   3   ANGLE     :  1.001          13119                                  
REMARK   3   CHIRALITY :  0.067           1478                                  
REMARK   3   PLANARITY :  0.006           1715                                  
REMARK   3   DIHEDRAL  : 17.103           3453                                  
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 7CI0 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 08-JUL-20.                  
REMARK 100 THE DEPOSITION ID IS D_1300017607.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-MAY-17                          
REMARK 200  TEMPERATURE           (KELVIN) : 80                                 
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                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9778                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 221017                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.660                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.01500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 20.1600                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.76                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.490                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4YPV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 67.64                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.80                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: MES PH 6.5, PEG, AMMONIUM SULFATE,       
REMARK 280  DIOXANE, PEG 1000, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  291.15K                                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 2 21                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,-Y,-Z+1/2                                         
REMARK 290       4555   -X+1/2,-Y,Z+1/2                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       35.19850            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      110.33050            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.19850            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.33050            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4                                              
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: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375 C1   NPO D 812  LIES ON A SPECIAL POSITION.                          
REMARK 375 N1   NPO D 812  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B2843  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH B3092  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     THR A   313                                                      
REMARK 465     ALA A   314                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     THR B   313                                                      
REMARK 465     ALA B   314                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     ASP C     3                                                      
REMARK 465     THR C   313                                                      
REMARK 465     ALA C   314                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     ASP D     3                                                      
REMARK 465     THR D   313                                                      
REMARK 465     ALA D   314                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   4    OG1  CG2                                            
REMARK 470     LYS A  12    CG   CD   CE   NZ                                   
REMARK 470     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  32    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 204    CG   CD   OE1  OE2                                  
REMARK 470     THR C   4    OG1  CG2                                            
REMARK 470     GLU C  79    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 204    CG   CD   OE1  OE2                                  
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   O3   NPO D   801     HO1  EDO D   804              1.56            
REMARK 500   O    HOH C   699     O    HOH C   765              1.74            
REMARK 500   O    HOH B  3010     O    HOH B  3021              1.74            
REMARK 500   O    HOH A   675     O    HOH A   723              1.96            
REMARK 500   O    HOH A   677     O    HOH C   740              1.98            
REMARK 500   O    DMS D   806     O    HOH D   901              1.99            
REMARK 500   O1   DIO B  2714     O    HOH B  2801              2.01            
REMARK 500   O    HOH D  1108     O    HOH D  1182              2.04            
REMARK 500   O    HOH B  3016     O    HOH B  3024              2.05            
REMARK 500   O    HOH A   676     O    HOH A   840              2.07            
REMARK 500   O    HOH D  1062     O    HOH D  1097              2.07            
REMARK 500   OE2  GLU A   133     O    HOH A   501              2.11            
REMARK 500   O    HOH A   838     O    HOH A   842              2.11            
REMARK 500   O    HOH B  2877     O    HOH B  3062              2.12            
REMARK 500   NH1  ARG B    50     O    HOH B  2802              2.13            
REMARK 500   O    DMS C   406     O    HOH C   501              2.14            
REMARK 500   OE1  GLU C   280     O    HOH C   502              2.14            
REMARK 500   OE1  GLU D   280     O    HOH D   902              2.14            
REMARK 500   OE2  GLU A   280     O    HOH A   502              2.16            
REMARK 500   O    HOH D  1090     O    HOH D  1177              2.16            
REMARK 500   O    GLU A    76     O2   GOL A   415              2.17            
REMARK 500   O2   GOL A   414     O    HOH A   503              2.17            
REMARK 500   O2   EDO B  2703     O    HOH B  2803              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  2807     O    HOH D   932     3554     1.97            
REMARK 500   O    HOH A   721     O    HOH C   801     3544     2.11            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
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,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
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   ATM2   ATM3                                     
REMARK 500    VAL D 211   C   -  N   -  CA  ANGL. DEV. =  15.2 DEGREES          
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    ALA A  22     -132.37     54.52                                   
REMARK 500    ASP A  96     -164.53   -163.61                                   
REMARK 500    PRO A 129       30.91    -99.83                                   
REMARK 500    ALA A 162     -113.45     58.39                                   
REMARK 500    LEU A 186      137.10   -173.94                                   
REMARK 500    PHE A 191       57.88     36.17                                   
REMARK 500    VAL A 211      -72.89     70.09                                   
REMARK 500    HIS A 284      146.75    -39.66                                   
REMARK 500    ASP B  96     -160.24   -163.00                                   
REMARK 500    ALA B 162     -128.78     60.02                                   
REMARK 500    PHE B 191       57.88     36.59                                   
REMARK 500    VAL B 211      -71.85     70.24                                   
REMARK 500    HIS B 284      150.68    -48.26                                   
REMARK 500    ASP C  96     -160.29   -168.69                                   
REMARK 500    PRO C 129       34.34    -99.32                                   
REMARK 500    ALA C 162     -112.58     56.97                                   
REMARK 500    PHE C 191       58.09     33.02                                   
REMARK 500    VAL C 211      -72.57     70.19                                   
REMARK 500    ASP D  96     -159.03   -165.77                                   
REMARK 500    PRO D 129       34.75    -99.22                                   
REMARK 500    ALA D 162     -113.68     55.09                                   
REMARK 500    PHE D 191       57.23     34.90                                   
REMARK 500    VAL D 211      -62.71     71.37                                   
REMARK 500    SER D 285       12.60     80.28                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 864        DISTANCE =  5.81 ANGSTROMS                       
REMARK 525    HOH C 865        DISTANCE =  5.87 ANGSTROMS                       
REMARK 525    HOH C 866        DISTANCE =  5.91 ANGSTROMS                       
DBREF1 7CI0 A    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 7CI0 A     A0A074MDU6                          1         314             
DBREF1 7CI0 B    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 7CI0 B     A0A074MDU6                          1         314             
DBREF1 7CI0 C    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 7CI0 C     A0A074MDU6                          1         314             
DBREF1 7CI0 D    1   314  UNP                  A0A074MDU6_ERYLO                 
DBREF2 7CI0 D     A0A074MDU6                          1         314             
SEQADV 7CI0 ALA A  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQADV 7CI0 ALA B  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQADV 7CI0 ALA C  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQADV 7CI0 ALA D  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQRES   1 A  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 A  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 A  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 A  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 A  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 A  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 A  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 A  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 A  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 A  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 A  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 A  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 A  314  ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 A  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 A  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 A  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 A  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 A  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 A  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 A  314  VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY          
SEQRES  21 A  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 A  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 A  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 A  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 A  314  THR ALA                                                      
SEQRES   1 B  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 B  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 B  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 B  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 B  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 B  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 B  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 B  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 B  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 B  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 B  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 B  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 B  314  ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 B  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 B  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 B  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 B  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 B  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 B  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 B  314  VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY          
SEQRES  21 B  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 B  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 B  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 B  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 B  314  THR ALA                                                      
SEQRES   1 C  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 C  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 C  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 C  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 C  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 C  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 C  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 C  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 C  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 C  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 C  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 C  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 C  314  ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 C  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 C  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 C  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 C  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 C  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 C  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 C  314  VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY          
SEQRES  21 C  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 C  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 C  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 C  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 C  314  THR ALA                                                      
SEQRES   1 D  314  MET THR ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA          
SEQRES   2 D  314  PHE LEU GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU          
SEQRES   3 D  314  ALA GLU MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL          
SEQRES   4 D  314  ALA LEU HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU          
SEQRES   5 D  314  ALA VAL ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY          
SEQRES   6 D  314  ASP ILE PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG          
SEQRES   7 D  314  GLU ALA GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY          
SEQRES   8 D  314  PHE VAL ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS          
SEQRES   9 D  314  THR GLU ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA          
SEQRES  10 D  314  VAL ASP TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA          
SEQRES  11 D  314  ALA ILE GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA          
SEQRES  12 D  314  SER SER PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL          
SEQRES  13 D  314  ILE PRO ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE          
SEQRES  14 D  314  VAL VAL SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL          
SEQRES  15 D  314  PRO VAL VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER          
SEQRES  16 D  314  ASP ALA VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU          
SEQRES  17 D  314  GLY PHE VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP          
SEQRES  18 D  314  THR ALA TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE          
SEQRES  19 D  314  PRO ILE LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE          
SEQRES  20 D  314  VAL ALA THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY          
SEQRES  21 D  314  ARG ASP TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP          
SEQRES  22 D  314  VAL VAL TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE          
SEQRES  23 D  314  THR ASN ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP          
SEQRES  24 D  314  LEU GLU ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY          
SEQRES  25 D  314  THR ALA                                                      
HET    NPO  A 401      15                                                       
HET    NPO  A 402      15                                                       
HET    NPO  A 403      15                                                       
HET    6NA  A 404      19                                                       
HET    PEG  A 405      17                                                       
HET    EDO  A 406      10                                                       
HET    DMS  A 407      10                                                       
HET    DMS  A 408      10                                                       
HET    DIO  A 409      14                                                       
HET    EDO  A 410      10                                                       
HET    DIO  A 411      14                                                       
HET    6NA  A 412      19                                                       
HET    DIO  A 413      14                                                       
HET    GOL  A 414      12                                                       
HET    GOL  A 415      13                                                       
HET    GOL  A 416      14                                                       
HET    GOL  A 417      14                                                       
HET    SO4  A 418       5                                                       
HET    PGE  B2701      23                                                       
HET    NPO  B2702      15                                                       
HET    EDO  B2703      10                                                       
HET    NPO  B2704      15                                                       
HET    6NA  B2705      19                                                       
HET    DMS  B2706      10                                                       
HET    DMS  B2707      10                                                       
HET    EDO  B2708      10                                                       
HET    EDO  B2709      10                                                       
HET    DMS  B2710      10                                                       
HET    EDO  B2711      10                                                       
HET    EDO  B2712      10                                                       
HET    GOL  B2713      12                                                       
HET    DIO  B2714      14                                                       
HET    SO4  B2715       5                                                       
HET    SO4  B2716       5                                                       
HET     NA  B2717       1                                                       
HET    NPO  C 401      15                                                       
HET    NPO  C 402      15                                                       
HET    NPO  C 403      15                                                       
HET    EDO  C 404      10                                                       
HET    DMS  C 405       8                                                       
HET    DMS  C 406      10                                                       
HET    GOL  C 407      13                                                       
HET    DMS  C 408      10                                                       
HET    DIO  C 409      14                                                       
HET    GOL  C 410      14                                                       
HET    PGE  C 411      22                                                       
HET    GOL  C 412      12                                                       
HET    EDO  C 413      10                                                       
HET    DIO  C 414      14                                                       
HET    DMS  C 415      10                                                       
HET    SO4  C 416       5                                                       
HET    NPO  D 801      15                                                       
HET    NPO  D 802      15                                                       
HET    PEG  D 803      17                                                       
HET    EDO  D 804      10                                                       
HET    DMS  D 805      10                                                       
HET    DMS  D 806      10                                                       
HET    MES  D 807      24                                                       
HET    DMS  D 808      10                                                       
HET    DMS  D 809      10                                                       
HET    DMS  D 810      10                                                       
HET    GOL  D 811      14                                                       
HET    NPO  D 812      15                                                       
HET    SO4  D 813       5                                                       
HETNAM     NPO P-NITROPHENOL                                                    
HETNAM     6NA HEXANOIC ACID                                                    
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     DMS DIMETHYL SULFOXIDE                                               
HETNAM     DIO 1,4-DIETHYLENE DIOXIDE                                           
HETNAM     GOL GLYCEROL                                                         
HETNAM     SO4 SULFATE ION                                                      
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM      NA SODIUM ION                                                       
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   5  NPO    11(C6 H5 N O3)                                               
FORMUL   8  6NA    3(C6 H12 O2)                                                 
FORMUL   9  PEG    2(C4 H10 O3)                                                 
FORMUL  10  EDO    10(C2 H6 O2)                                                 
FORMUL  11  DMS    14(C2 H6 O S)                                                
FORMUL  13  DIO    6(C4 H8 O2)                                                  
FORMUL  18  GOL    9(C3 H8 O3)                                                  
FORMUL  22  SO4    5(O4 S 2-)                                                   
FORMUL  23  PGE    2(C6 H14 O4)                                                 
FORMUL  39   NA    NA 1+                                                        
FORMUL  62  MES    C6 H13 N O4 S                                                
FORMUL  69  HOH   *1361(H2 O)                                                   
HELIX    1 AA1 ARG A    8  ALA A   22  1                                  15    
HELIX    2 AA2 THR A   30  ASP A   46  1                                  17    
HELIX    3 AA3 HIS A  100  ASP A  112  1                                  13    
HELIX    4 AA4 PRO A  129  SER A  144  1                                  16    
HELIX    5 AA5 ALA A  162  LYS A  178  1                                  17    
HELIX    6 AA6 SER A  200  PHE A  206  1                                   7    
HELIX    7 AA7 THR A  213  LYS A  225  1                                  13    
HELIX    8 AA8 PHE A  234  GLY A  238  5                                   5    
HELIX    9 AA9 ILE A  256  ALA A  270  1                                  15    
HELIX   10 AB1 SER A  285  ILE A  289  5                                   5    
HELIX   11 AB2 SER A  295  GLY A  312  1                                  18    
HELIX   12 AB3 ARG B    8  ALA B   22  1                                  15    
HELIX   13 AB4 THR B   30  ASP B   46  1                                  17    
HELIX   14 AB5 HIS B  100  ASP B  112  1                                  13    
HELIX   15 AB6 PRO B  129  SER B  144  1                                  16    
HELIX   16 AB7 SER B  145  GLY B  150  5                                   6    
HELIX   17 AB8 ALA B  162  LYS B  178  1                                  17    
HELIX   18 AB9 SER B  200  PHE B  206  1                                   7    
HELIX   19 AC1 THR B  213  LYS B  225  1                                  13    
HELIX   20 AC2 PHE B  234  GLY B  238  5                                   5    
HELIX   21 AC3 ILE B  256  ALA B  270  1                                  15    
HELIX   22 AC4 SER B  285  ILE B  289  5                                   5    
HELIX   23 AC5 PRO B  294  GLY B  312  1                                  19    
HELIX   24 AC6 ARG C    8  ALA C   22  1                                  15    
HELIX   25 AC7 THR C   25  MET C   29  5                                   5    
HELIX   26 AC8 THR C   30  ASP C   46  1                                  17    
HELIX   27 AC9 HIS C  100  ASP C  112  1                                  13    
HELIX   28 AD1 PRO C  129  SER C  144  1                                  16    
HELIX   29 AD2 ALA C  162  LYS C  178  1                                  17    
HELIX   30 AD3 SER C  200  PHE C  206  1                                   7    
HELIX   31 AD4 THR C  213  LYS C  225  1                                  13    
HELIX   32 AD5 PHE C  234  GLY C  238  5                                   5    
HELIX   33 AD6 ILE C  256  ALA C  270  1                                  15    
HELIX   34 AD7 SER C  285  ILE C  289  5                                   5    
HELIX   35 AD8 SER C  295  GLY C  312  1                                  18    
HELIX   36 AD9 ARG D    8  ALA D   22  1                                  15    
HELIX   37 AE1 THR D   30  ASP D   46  1                                  17    
HELIX   38 AE2 HIS D  100  ASP D  112  1                                  13    
HELIX   39 AE3 PRO D  129  SER D  144  1                                  16    
HELIX   40 AE4 SER D  145  GLY D  150  5                                   6    
HELIX   41 AE5 ALA D  162  LYS D  178  1                                  17    
HELIX   42 AE6 SER D  200  PHE D  206  1                                   7    
HELIX   43 AE7 THR D  213  LYS D  225  1                                  13    
HELIX   44 AE8 PHE D  234  GLY D  238  5                                   5    
HELIX   45 AE9 ILE D  256  ALA D  270  1                                  15    
HELIX   46 AF1 SER D  285  ILE D  289  5                                   5    
HELIX   47 AF2 SER D  295  GLY D  312  1                                  18    
SHEET    1 AA1 6 VAL A  54  GLY A  62  0                                        
SHEET    2 AA1 6 GLY A  65  ASP A  73 -1  O  LEU A  69   N  LEU A  58           
SHEET    3 AA1 6 VAL A 115  VAL A 118 -1  O  VAL A 115   N  TYR A  72           
SHEET    4 AA1 6 GLY A  81  TYR A  87  1  N  ILE A  84   O  VAL A 116           
SHEET    5 AA1 6 ALA A 153  ASP A 161  1  O  ILE A 157   N  VAL A  83           
SHEET    6 AA1 6 VAL A 188  ILE A 190  1  O  ILE A 190   N  GLY A 160           
SHEET    1 AA2 4 THR A 246  ALA A 251  0                                        
SHEET    2 AA2 4 VAL A 274  MET A 279  1  O  VAL A 275   N  VAL A 248           
SHEET    3 AA2 4 VAL B 274  MET B 279 -1  O  VAL B 274   N  TYR A 276           
SHEET    4 AA2 4 THR B 246  ALA B 251  1  N  VAL B 248   O  VAL B 275           
SHEET    1 AA3 6 VAL B  54  GLY B  62  0                                        
SHEET    2 AA3 6 GLY B  65  ASP B  73 -1  O  ILE B  67   N  CYS B  60           
SHEET    3 AA3 6 VAL B 115  VAL B 118 -1  O  VAL B 115   N  TYR B  72           
SHEET    4 AA3 6 GLY B  81  TYR B  87  1  N  ILE B  84   O  VAL B 116           
SHEET    5 AA3 6 ALA B 153  ASP B 161  1  O  ILE B 159   N  THR B  85           
SHEET    6 AA3 6 VAL B 188  ILE B 190  1  O  ILE B 190   N  GLY B 160           
SHEET    1 AA4 6 VAL C  54  PRO C  61  0                                        
SHEET    2 AA4 6 ASP C  66  ASP C  73 -1  O  ILE C  67   N  CYS C  60           
SHEET    3 AA4 6 VAL C 115  VAL C 118 -1  O  VAL C 115   N  TYR C  72           
SHEET    4 AA4 6 GLY C  81  TYR C  87  1  N  ILE C  84   O  VAL C 116           
SHEET    5 AA4 6 ALA C 153  ASP C 161  1  O  ILE C 157   N  VAL C  83           
SHEET    6 AA4 6 VAL C 188  ILE C 190  1  O  ILE C 190   N  GLY C 160           
SHEET    1 AA5 4 THR C 246  ALA C 251  0                                        
SHEET    2 AA5 4 VAL C 274  MET C 279  1  O  VAL C 275   N  VAL C 248           
SHEET    3 AA5 4 VAL D 274  MET D 279 -1  O  TYR D 276   N  VAL C 274           
SHEET    4 AA5 4 THR D 246  ALA D 251  1  N  VAL D 248   O  VAL D 275           
SHEET    1 AA6 6 VAL D  54  CYS D  60  0                                        
SHEET    2 AA6 6 ILE D  67  ASP D  73 -1  O  ILE D  67   N  CYS D  60           
SHEET    3 AA6 6 VAL D 115  VAL D 118 -1  O  VAL D 115   N  TYR D  72           
SHEET    4 AA6 6 GLY D  81  TYR D  87  1  N  ILE D  84   O  VAL D 116           
SHEET    5 AA6 6 ALA D 153  ASP D 161  1  O  GLY D 155   N  VAL D  83           
SHEET    6 AA6 6 VAL D 188  ILE D 190  1  O  ILE D 190   N  GLY D 160           
LINK        NA    NA B2717                 O   HOH B3043     1555   1555  2.71  
CISPEP   1 ALA A  123    PRO A  124          0         0.02                     
CISPEP   2 PHE A  128    PRO A  129          0         2.54                     
CISPEP   3 ALA B  123    PRO B  124          0         2.84                     
CISPEP   4 PHE B  128    PRO B  129          0         4.02                     
CISPEP   5 ALA C  123    PRO C  124          0         1.66                     
CISPEP   6 PHE C  128    PRO C  129          0         0.88                     
CISPEP   7 ALA D  123    PRO D  124          0         3.13                     
CISPEP   8 PHE D  128    PRO D  129          0         3.69                     
CRYST1   70.397  129.771  220.661  90.00  90.00  90.00 P 21 2 21    16          
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      0.014205  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007706  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004532        0.00000                         
TER    4534      GLY A 312                                                      
TER    9088      GLY B 312                                                      
TER   13635      GLY C 312                                                      
TER   18200      GLY D 312                                                      
MASTER      418    0   64   47   32    0    0    610881    4  792  100          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
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