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LongText Report for: 6kf1-pdb

Name Class
6kf1-pdb
HEADER    HYDROLASE                               05-JUL-19   6KF1              
TITLE     MICROBIAL HORMONE-SENSITIVE LIPASE- E53 MUTANT S162A                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPASE;                                                    
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 MOL_ID: 2;                                                           
COMPND   7 MOLECULE: LIPASE;                                                    
COMPND   8 CHAIN: D;                                                            
COMPND   9 ENGINEERED: YES;                                                     
COMPND  10 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 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   7 MOL_ID: 2;                                                           
SOURCE   8 ORGANISM_SCIENTIFIC: ERYTHROBACTER LONGUS;                           
SOURCE   9 ORGANISM_TAXID: 1044;                                                
SOURCE  10 GENE: EH31_02760;                                                    
SOURCE  11 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE  12 EXPRESSION_SYSTEM_TAXID: 866768                                      
KEYWDS    ESTERASE, MICROBIAL HORMONE-SENSITIVE LIPASE, HYDROLASE               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.XIAOCHEN,L.ZHENGYANG,X.XUEWEI,L.JIXI                                
REVDAT   1   08-JUL-20 6KF1    0                                                
JRNL        AUTH   Y.XIAOCHEN,H.YINGYI,L.ZHENGYANG,J.SHULING,R.ZHEN,W.ZHAO,     
JRNL        AUTH 2 H.XIAOJIAN,C.HENGLIN,L.JIXI,X.XUEWEI                         
JRNL        TITL   FUNCTIONAL AND STRUCTURAL INSIGHTS INTO ENVIRONMENTAL        
JRNL        TITL 2 ADAPTATION OF A NOVEL HORMONE-SENSITIVE LIPASE, E53,         
JRNL        TITL 3 OBTAINED FROM ERYTHROBACTER LONGUS                           
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0253                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.70                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 136861                         
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : FREE R-VALUE                    
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.189                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.922                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6777                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 9485                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.12                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1940                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 472                          
REMARK   3   BIN FREE R VALUE                    : 0.2290                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 9121                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 186                                     
REMARK   3   SOLVENT ATOMS            : 1429                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 31.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 32.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.03500                                              
REMARK   3    B22 (A**2) : -0.02900                                             
REMARK   3    B33 (A**2) : -0.00600                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.113         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.110         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.071         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.525         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.957                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  9505 ; 0.013 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  8977 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 12953 ; 1.738 ; 1.643       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 20705 ; 1.461 ; 1.568       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1233 ; 6.613 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   431 ;24.575 ;20.812       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1378 ;12.399 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    72 ;23.875 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1286 ; 0.092 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 10795 ; 0.011 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1973 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2143 ; 0.210 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    58 ; 0.176 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4871 ; 0.168 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  1169 ; 0.202 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  4954 ; 3.085 ; 3.181       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  4949 ; 3.065 ; 3.179       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6178 ; 3.517 ; 4.746       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  6177 ; 3.519 ; 4.746       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4551 ; 3.829 ; 3.501       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  4552 ; 3.829 ; 3.501       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  6775 ; 5.140 ; 5.128       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  6776 ; 5.140 ; 5.128       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THEIR        
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 6KF1 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300012860.                                   
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) : 0.97776                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 136953                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.996                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.701                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 13.20                              
REMARK 200  R MERGE                    (I) : 0.10700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 42.6330                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.35700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: 4YPV                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 68.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.88                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: CALCIUM CHLORIDE, BIS-TRIS, PEG MME      
REMARK 280  550, PH 6.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K        
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       35.19700            
REMARK 290   SMTRY2   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000      110.29100            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       35.19700            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      110.29100            
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: 10070 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 42880 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 26.0 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 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     GLU A  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU A  79    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 183    CG                                                  
REMARK 470     GLU A 204    CG   CD   OE1  OE2                                  
REMARK 470     THR B   4    OG1  CG2                                            
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  51    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  76    CG   CD   OE1  OE2                                  
REMARK 470     GLU C  79    CG   CD   OE1  OE2                                  
REMARK 470     GLU C 204    CG   CD   OE1  OE2                                  
REMARK 470     GLU D 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   O    HOH A   686     O    HOH A   829              1.70            
REMARK 500   O    HOH C   756     O    HOH C   789              1.72            
REMARK 500   O    HOH D   712     O    HOH D   771              1.79            
REMARK 500   NH2  ARG A   228     O    HOH A   501              1.80            
REMARK 500   O    HOH D   807     O    HOH D   828              1.84            
REMARK 500   O    HOH C   728     O    HOH C   833              1.93            
REMARK 500   O    HOH D   829     O    HOH D   840              1.99            
REMARK 500   O    HOH D   666     O    HOH D   752              2.04            
REMARK 500   O    HOH A   703     O    HOH A   734              2.06            
REMARK 500   OE1  GLU A   280     O    HOH A   502              2.06            
REMARK 500   OD1  ASP B   230     O    HOH B   501              2.06            
REMARK 500   O    HOH C   748     O    HOH C   755              2.08            
REMARK 500   O    HOH C   732     O    HOH C   808              2.11            
REMARK 500   O    HOH D   809     O    HOH D   828              2.13            
REMARK 500   O    HOH C   656     O    HOH C   758              2.14            
REMARK 500   CZ   ARG A   228     O    HOH A   501              2.14            
REMARK 500   O    HOH B   687     O    HOH B   715              2.14            
REMARK 500   O    HOH C   615     O    HOH C   833              2.15            
REMARK 500   O    HOH C   671     O    HOH C   820              2.16            
REMARK 500   O    HOH B   683     O    HOH B   707              2.16            
REMARK 500   O    HOH A   733     O    HOH A   805              2.17            
REMARK 500   O    HOH A   638     O    HOH A   726              2.18            
REMARK 500   O    HOH A   518     O    HOH A   541              2.18            
REMARK 500   O    HOH D   550     O    HOH D   720              2.19            
REMARK 500   O    HOH C   793     O    HOH C   888              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH B   606     O    HOH B   606     2755     1.10            
REMARK 500   O    HOH D   520     O    HOH D   520     2556     1.34            
REMARK 500   O    HOH B   767     O    HOH B   767     2755     1.60            
REMARK 500   O    HOH B   794     O    HOH B   794     2755     1.79            
REMARK 500   O    HOH B   581     O    HOH D   794     3565     2.06            
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 133   CD    GLU A 133   OE2    -0.090                       
REMARK 500    GLU B  76   CD    GLU B  76   OE2     0.074                       
REMARK 500    GLU B 280   CD    GLU B 280   OE2     0.070                       
REMARK 500    GLU C 133   CD    GLU C 133   OE2    -0.112                       
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    ARG B 257   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.0 DEGREES          
REMARK 500    ARG C 151   CG  -  CD  -  NE  ANGL. DEV. =  13.1 DEGREES          
REMARK 500    ARG C 151   NE  -  CZ  -  NH1 ANGL. DEV. =   3.1 DEGREES          
REMARK 500    ARG C 151   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.2 DEGREES          
REMARK 500    ARG C 228   NE  -  CZ  -  NH1 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    ARG C 228   NE  -  CZ  -  NH2 ANGL. DEV. =   4.3 DEGREES          
REMARK 500    ARG D 228   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 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  80      130.88    -39.33                                   
REMARK 500    ASP A  96     -165.77   -170.46                                   
REMARK 500    PRO A 129       32.35    -97.97                                   
REMARK 500    ALA A 162     -116.46     65.18                                   
REMARK 500    PHE A 191       63.35     29.05                                   
REMARK 500    VAL A 211      -73.19     73.40                                   
REMARK 500    HIS A 284      144.78    -38.62                                   
REMARK 500    ASP B  96     -156.26   -168.35                                   
REMARK 500    ALA B 162     -114.78     66.93                                   
REMARK 500    LEU B 186      140.03   -170.83                                   
REMARK 500    PHE B 191       61.40     31.94                                   
REMARK 500    VAL B 211      -68.69     72.79                                   
REMARK 500    HIS B 284      142.04    -38.58                                   
REMARK 500    SER B 285        7.88     82.79                                   
REMARK 500    ASP C  96     -166.41   -167.98                                   
REMARK 500    PRO C 129       32.20    -98.22                                   
REMARK 500    ALA C 162     -118.30     64.49                                   
REMARK 500    LEU C 186      139.70   -171.33                                   
REMARK 500    PHE C 191       62.22     30.60                                   
REMARK 500    VAL C 211      -72.11     73.32                                   
REMARK 500    HIS C 284      144.36    -37.08                                   
REMARK 500    ASP D  96     -162.79   -164.83                                   
REMARK 500    PRO D 129       31.15    -98.55                                   
REMARK 500    ALA D 162     -117.36     64.44                                   
REMARK 500    PHE D 191       63.05     24.96                                   
REMARK 500    VAL D 211      -71.31     71.62                                   
REMARK 500    HIS D 284      136.32    -35.93                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 THR A  283     HIS A  284                  149.26                    
REMARK 500 THR D  283     HIS D  284                  149.57                    
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 A 871        DISTANCE =  6.08 ANGSTROMS                       
REMARK 525    HOH A 872        DISTANCE =  6.36 ANGSTROMS                       
REMARK 525    HOH A 873        DISTANCE =  6.59 ANGSTROMS                       
REMARK 525    HOH D 841        DISTANCE =  6.76 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PGE A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO B 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue EDO B 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA B 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO C 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 C 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA C 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO D 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NPO D 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue MES D 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue SO4 D 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA D 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 6NA D 406                 
DBREF1 6KF1 A    4   312  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF1 A     A0A074MDU6                          4         312             
DBREF1 6KF1 B    4   312  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF1 B     A0A074MDU6                          4         312             
DBREF1 6KF1 C    4   312  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF1 C     A0A074MDU6                          4         312             
DBREF1 6KF1 D    3   312  UNP                  A0A074MDU6_ERYLO                 
DBREF2 6KF1 D     A0A074MDU6                          3         312             
SEQADV 6KF1 ALA A  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQADV 6KF1 ALA B  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQADV 6KF1 ALA C  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQADV 6KF1 ALA D  162  UNP  A0A074MDU SER   162 ENGINEERED MUTATION            
SEQRES   1 A  309  THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU          
SEQRES   2 A  309  ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET          
SEQRES   3 A  309  THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS          
SEQRES   4 A  309  GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE          
SEQRES   5 A  309  ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO          
SEQRES   6 A  309  LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY          
SEQRES   7 A  309  PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE          
SEQRES   8 A  309  GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE          
SEQRES   9 A  309  ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR          
SEQRES  10 A  309  ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU          
SEQRES  11 A  309  ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO          
SEQRES  12 A  309  SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE          
SEQRES  13 A  309  GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL SER          
SEQRES  14 A  309  GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL          
SEQRES  15 A  309  LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL          
SEQRES  16 A  309  GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL          
SEQRES  17 A  309  LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR          
SEQRES  18 A  309  LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU          
SEQRES  19 A  309  GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR          
SEQRES  20 A  309  ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR          
SEQRES  21 A  309  ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR          
SEQRES  22 A  309  LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE          
SEQRES  23 A  309  ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG          
SEQRES  24 A  309  ILE ILE ALA ALA MET LYS MET MET LEU GLY                      
SEQRES   1 B  309  THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU          
SEQRES   2 B  309  ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET          
SEQRES   3 B  309  THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS          
SEQRES   4 B  309  GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE          
SEQRES   5 B  309  ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO          
SEQRES   6 B  309  LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY          
SEQRES   7 B  309  PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE          
SEQRES   8 B  309  GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE          
SEQRES   9 B  309  ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR          
SEQRES  10 B  309  ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU          
SEQRES  11 B  309  ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO          
SEQRES  12 B  309  SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE          
SEQRES  13 B  309  GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL SER          
SEQRES  14 B  309  GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL          
SEQRES  15 B  309  LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL          
SEQRES  16 B  309  GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL          
SEQRES  17 B  309  LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR          
SEQRES  18 B  309  LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU          
SEQRES  19 B  309  GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR          
SEQRES  20 B  309  ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR          
SEQRES  21 B  309  ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR          
SEQRES  22 B  309  LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE          
SEQRES  23 B  309  ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG          
SEQRES  24 B  309  ILE ILE ALA ALA MET LYS MET MET LEU GLY                      
SEQRES   1 C  309  THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU GLU          
SEQRES   2 C  309  ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU MET          
SEQRES   3 C  309  THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU HIS          
SEQRES   4 C  309  GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL ILE          
SEQRES   5 C  309  ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE PRO          
SEQRES   6 C  309  LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA GLY          
SEQRES   7 C  309  PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL ILE          
SEQRES   8 C  309  GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU ILE          
SEQRES   9 C  309  ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP TYR          
SEQRES  10 C  309  ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE GLU          
SEQRES  11 C  309  ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER PRO          
SEQRES  12 C  309  SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO ILE          
SEQRES  13 C  309  GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL SER          
SEQRES  14 C  309  GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL VAL          
SEQRES  15 C  309  LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA VAL          
SEQRES  16 C  309  GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE VAL          
SEQRES  17 C  309  LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA TYR          
SEQRES  18 C  309  LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE LEU          
SEQRES  19 C  309  GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA THR          
SEQRES  20 C  309  ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP TYR          
SEQRES  21 C  309  ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL TYR          
SEQRES  22 C  309  LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN ILE          
SEQRES  23 C  309  ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU ARG          
SEQRES  24 C  309  ILE ILE ALA ALA MET LYS MET MET LEU GLY                      
SEQRES   1 D  310  ASP THR PRO PHE ILE ARG PRO ASP MET LYS ALA PHE LEU          
SEQRES   2 D  310  GLU ALA ILE ALA ALA MET ALA GLY PRO THR LEU ALA GLU          
SEQRES   3 D  310  MET THR LEU GLU GLU ALA ARG ALA SER TYR VAL ALA LEU          
SEQRES   4 D  310  HIS GLY MET ALA ASP ARG PRO ALA ARG GLU LEU ALA VAL          
SEQRES   5 D  310  ILE ARG ASN LEU SER CYS PRO GLY PRO ALA GLY ASP ILE          
SEQRES   6 D  310  PRO LEU ARG LEU TYR ASP ALA ARG GLU SER ARG GLU ALA          
SEQRES   7 D  310  GLY PRO VAL ILE THR PHE TYR HIS GLY GLY GLY PHE VAL          
SEQRES   8 D  310  ILE GLY ASP LEU ASP THR HIS HIS ASN LEU CYS THR GLU          
SEQRES   9 D  310  ILE ALA ALA LEU MET ASP LEU PRO VAL VAL ALA VAL ASP          
SEQRES  10 D  310  TYR ARG LEU ALA PRO GLU HIS PRO PHE PRO ALA ALA ILE          
SEQRES  11 D  310  GLU ASP CYS GLU ALA ALA THR ARG TRP VAL ALA SER SER          
SEQRES  12 D  310  PRO SER GLU LEU GLY ARG THR ALA SER GLY VAL ILE PRO          
SEQRES  13 D  310  ILE GLY ASP ALA ALA GLY GLY ASN ALA THR ILE VAL VAL          
SEQRES  14 D  310  SER GLN LEU LEU GLY ALA LYS PRO ALA ASP VAL PRO VAL          
SEQRES  15 D  310  VAL LEU GLN VAL PRO ILE PHE PRO LEU ALA SER ASP ALA          
SEQRES  16 D  310  VAL GLY SER ALA SER LEU GLU ALA PHE ALA GLU GLY PHE          
SEQRES  17 D  310  VAL LEU THR LYS ALA SER ILE GLU PHE PHE ASP THR ALA          
SEQRES  18 D  310  TYR LYS ALA ASP ARG ALA ASP PRO ARG GLY PHE PRO ILE          
SEQRES  19 D  310  LEU GLY ASP HIS THR ALA ALA PRO PRO THR ILE VAL ALA          
SEQRES  20 D  310  THR ALA SER LEU ASP PRO ILE ARG ASP SER GLY ARG ASP          
SEQRES  21 D  310  TYR ALA LYS ALA LEU VAL GLU ALA GLY ARG ASP VAL VAL          
SEQRES  22 D  310  TYR LEU GLU MET GLU GLY VAL THR HIS SER PHE THR ASN          
SEQRES  23 D  310  ILE ARG ALA ALA VAL PRO SER THR GLN GLY ASP LEU GLU          
SEQRES  24 D  310  ARG ILE ILE ALA ALA MET LYS MET MET LEU GLY                  
HET    NPO  A 401      10                                                       
HET    NPO  A 402      10                                                       
HET    NPO  A 403      10                                                       
HET    6NA  A 404       8                                                       
HET    PGE  A 405      10                                                       
HET    NPO  B 401      10                                                       
HET    NPO  B 402      10                                                       
HET    NPO  B 403      10                                                       
HET    EDO  B 404       4                                                       
HET    6NA  B 405       8                                                       
HET    NPO  C 401      10                                                       
HET    NPO  C 402      10                                                       
HET    NPO  C 403      10                                                       
HET    SO4  C 404       5                                                       
HET    6NA  C 405       8                                                       
HET    NPO  D 401      10                                                       
HET    NPO  D 402      10                                                       
HET    MES  D 403      12                                                       
HET    SO4  D 404       5                                                       
HET    6NA  D 405       8                                                       
HET    6NA  D 406       8                                                       
HETNAM     NPO P-NITROPHENOL                                                    
HETNAM     6NA HEXANOIC ACID                                                    
HETNAM     PGE TRIETHYLENE GLYCOL                                               
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETNAM     SO4 SULFATE ION                                                      
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   5  NPO    11(C6 H5 N O3)                                               
FORMUL   8  6NA    5(C6 H12 O2)                                                 
FORMUL   9  PGE    C6 H14 O4                                                    
FORMUL  13  EDO    C2 H6 O2                                                     
FORMUL  18  SO4    2(O4 S 2-)                                                   
FORMUL  22  MES    C6 H13 N O4 S                                                
FORMUL  26  HOH   *1429(H2 O)                                                   
HELIX    1 AA1 ARG A    8  ALA A   22  1                                  15    
HELIX    2 AA2 THR A   25  MET A   29  5                                   5    
HELIX    3 AA3 THR A   30  ASP A   46  1                                  17    
HELIX    4 AA4 HIS A  100  ASP A  112  1                                  13    
HELIX    5 AA5 PRO A  129  SER A  144  1                                  16    
HELIX    6 AA6 SER A  145  GLY A  150  5                                   6    
HELIX    7 AA7 ALA A  162  LYS A  178  1                                  17    
HELIX    8 AA8 SER A  200  PHE A  206  1                                   7    
HELIX    9 AA9 THR A  213  LYS A  225  1                                  13    
HELIX   10 AB1 PHE A  234  GLY A  238  5                                   5    
HELIX   11 AB2 ILE A  256  ALA A  270  1                                  15    
HELIX   12 AB3 SER A  285  ILE A  289  5                                   5    
HELIX   13 AB4 SER A  295  GLY A  312  1                                  18    
HELIX   14 AB5 ARG B    8  ALA B   22  1                                  15    
HELIX   15 AB6 THR B   30  ASP B   46  1                                  17    
HELIX   16 AB7 HIS B  100  ASP B  112  1                                  13    
HELIX   17 AB8 PRO B  129  SER B  144  1                                  16    
HELIX   18 AB9 SER B  145  GLY B  150  5                                   6    
HELIX   19 AC1 ALA B  162  LYS B  178  1                                  17    
HELIX   20 AC2 SER B  200  PHE B  206  1                                   7    
HELIX   21 AC3 THR B  213  LYS B  225  1                                  13    
HELIX   22 AC4 PHE B  234  GLY B  238  5                                   5    
HELIX   23 AC5 ILE B  256  ALA B  270  1                                  15    
HELIX   24 AC6 SER B  285  ILE B  289  5                                   5    
HELIX   25 AC7 SER B  295  GLY B  312  1                                  18    
HELIX   26 AC8 ARG C    8  ALA C   22  1                                  15    
HELIX   27 AC9 THR C   30  ASP C   46  1                                  17    
HELIX   28 AD1 HIS C  100  ASP C  112  1                                  13    
HELIX   29 AD2 PRO C  129  SER C  144  1                                  16    
HELIX   30 AD3 SER C  145  GLY C  150  5                                   6    
HELIX   31 AD4 ALA C  162  LYS C  178  1                                  17    
HELIX   32 AD5 SER C  200  PHE C  206  1                                   7    
HELIX   33 AD6 THR C  213  LYS C  225  1                                  13    
HELIX   34 AD7 PHE C  234  GLY C  238  5                                   5    
HELIX   35 AD8 ILE C  256  ALA C  270  1                                  15    
HELIX   36 AD9 SER C  285  ILE C  289  5                                   5    
HELIX   37 AE1 SER C  295  GLY C  312  1                                  18    
HELIX   38 AE2 ARG D    8  ALA D   22  1                                  15    
HELIX   39 AE3 THR D   30  ASP D   46  1                                  17    
HELIX   40 AE4 HIS D  100  ASP D  112  1                                  13    
HELIX   41 AE5 PRO D  129  SER D  144  1                                  16    
HELIX   42 AE6 SER D  145  GLY D  150  5                                   6    
HELIX   43 AE7 ALA D  162  LYS D  178  1                                  17    
HELIX   44 AE8 SER D  200  PHE D  206  1                                   7    
HELIX   45 AE9 THR D  213  LYS D  225  1                                  13    
HELIX   46 AF1 PHE D  234  GLY D  238  5                                   5    
HELIX   47 AF2 ILE D  256  ALA D  270  1                                  15    
HELIX   48 AF3 SER D  285  ILE D  289  5                                   5    
HELIX   49 AF4 SER D  295  GLY D  312  1                                  18    
SHEET    1 AA1 6 VAL A  54  PRO A  61  0                                        
SHEET    2 AA1 6 ASP A  66  ASP A  73 -1  O  LEU A  71   N  ARG A  56           
SHEET    3 AA1 6 VAL A 115  VAL A 118 -1  O  ALA A 117   N  ARG A  70           
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  THR A  85           
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  MET A 279   N  THR A 250           
SHEET    3 AA2 4 VAL B 274  MET B 279 -1  O  TYR B 276   N  VAL A 274           
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  ALA B 117   N  ARG B  70           
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  GLY B 155   N  VAL B  83           
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  GLY C  62  0                                        
SHEET    2 AA4 6 GLY C  65  ASP C  73 -1  O  LEU C  71   N  ARG C  56           
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  VAL D 274   N  TYR C 276           
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  ILE D 159   N  THR D  85           
SHEET    6 AA6 6 VAL D 188  ILE D 190  1  O  ILE D 190   N  GLY D 160           
CISPEP   1 ALA A  123    PRO A  124          0        -2.11                     
CISPEP   2 PHE A  128    PRO A  129          0        -1.43                     
CISPEP   3 ALA B  123    PRO B  124          0         0.24                     
CISPEP   4 PHE B  128    PRO B  129          0         4.48                     
CISPEP   5 ALA C  123    PRO C  124          0        -3.16                     
CISPEP   6 PHE C  128    PRO C  129          0        -0.67                     
CISPEP   7 ALA D  123    PRO D  124          0        -1.60                     
CISPEP   8 PHE D  128    PRO D  129          0        -0.59                     
SITE     1 AC1  9 GLY A  91  LEU A 193  ILE A 217  PHE A 220                    
SITE     2 AC1  9 ASP A 221  ILE A 256  NPO A 402  HOH A 555                    
SITE     3 AC1  9 HOH A 562                                                     
SITE     1 AC2 12 GLY A  91  PHE A  92  ALA A 163  ASN A 166                    
SITE     2 AC2 12 LEU A 193  ASP A 221  TYR A 224  ALA A 226                    
SITE     3 AC2 12 ARG A 228  PHE A 234  NPO A 401  HOH A 503                    
SITE     1 AC3 10 TYR A  38  LEU A  41  VAL A 211  PHE A 220                    
SITE     2 AC3 10 HIS A 284  SER A 285  HOH A 516  HOH A 540                    
SITE     3 AC3 10 HOH A 687  HOH A 688                                          
SITE     1 AC4  3 ARG A 257  ARG A 261  HOH B 590                               
SITE     1 AC5  9 LYS A 265  ALA A 266  HOH A 618  HOH A 625                    
SITE     2 AC5  9 HOH A 715  LYS B 265  ALA B 266  GLU B 269                    
SITE     3 AC5  9 HOH B 561                                                     
SITE     1 AC6 11 GLY B  91  PHE B  92  ALA B 163  ASN B 166                    
SITE     2 AC6 11 LEU B 193  ASP B 221  ALA B 226  ARG B 228                    
SITE     3 AC6 11 PHE B 234  NPO B 402  HOH B 539                               
SITE     1 AC7  9 GLY B  91  LEU B 193  ILE B 217  PHE B 220                    
SITE     2 AC7  9 ASP B 221  ILE B 256  NPO B 401  HOH B 529                    
SITE     3 AC7  9 HOH B 596                                                     
SITE     1 AC8  6 LEU B  41  PHE B 220  HIS B 284  SER B 285                    
SITE     2 AC8  6 HOH B 513  HOH B 532                                          
SITE     1 AC9  4 MET A 309  MET A 310  ARG B 302  HOH B 624                    
SITE     1 AD1  3 ARG B 257  ARG B 261  HOH B 626                               
SITE     1 AD2 11 GLY C  91  PHE C  92  ALA C 163  ASN C 166                    
SITE     2 AD2 11 LEU C 193  ASP C 221  TYR C 224  ALA C 226                    
SITE     3 AD2 11 PHE C 234  NPO C 402  HOH C 504                               
SITE     1 AD3  9 GLY C  91  LEU C 193  ILE C 217  PHE C 220                    
SITE     2 AD3  9 ASP C 221  ILE C 256  NPO C 401  HOH C 516                    
SITE     3 AD3  9 HOH C 558                                                     
SITE     1 AD4  6 VAL C 211  PHE C 220  HIS C 284  SER C 285                    
SITE     2 AD4  6 HOH C 647  HOH C 670                                          
SITE     1 AD5  3 ARG C 272  HOH C 693  GLU D 280                               
SITE     1 AD6  4 ARG C 257  ARG C 261  HOH C 848  HOH D 595                    
SITE     1 AD7  9 GLY D  91  LEU D 193  ILE D 217  PHE D 220                    
SITE     2 AD7  9 ASP D 221  ILE D 256  NPO D 402  HOH D 583                    
SITE     3 AD7  9 HOH D 598                                                     
SITE     1 AD8 11 GLY D  91  PHE D  92  ALA D 163  ASN D 166                    
SITE     2 AD8 11 LEU D 193  ASP D 221  TYR D 224  ALA D 226                    
SITE     3 AD8 11 PHE D 234  NPO D 401  HOH D 529                               
SITE     1 AD9 13 SER B 145  PRO B 146  SER B 147  GLY B 150                    
SITE     2 AD9 13 ARG B 151  THR B 152  SER D 145  PRO D 146                    
SITE     3 AD9 13 GLY D 150  ARG D 151  THR D 152  HOH D 558                    
SITE     4 AD9 13 HOH D 572                                                     
SITE     1 AE1  1 ARG D  75                                                     
SITE     1 AE2  4 THR D  30  LEU D  31  GLU D  32  HOH D 662                    
SITE     1 AE3  6 ALA D 201  ARG D 257  ARG D 261  HOH D 679                    
SITE     2 AE3  6 HOH D 772  HOH D 816                                          
CRYST1   70.394  129.786  220.582  90.00  90.00  90.00 P 21 2 21    12          
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      0.014206  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.007705  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.004533        0.00000                         
TER    2276      GLY A 312                                                      
TER    4557      GLY B 312                                                      
TER    6830      GLY C 312                                                      
TER    9125      GLY D 312                                                      
MASTER      521    0   21   49   32    0   47    610736    4  186   96          
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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