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LongText Report for: 7yc4-pdb

Name Class
7yc4-pdb
HEADER    HYDROLASE                               30-JUN-22   7YC4              
TITLE     ACETYLESTERASE (LGESTI) F207A                                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE;                                      
COMPND   3 CHAIN: A, B, C, D, E, F, G, H;                                       
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LACTOCOCCUS GARVIEAE SUBSP. GARVIEAE;           
SOURCE   3 ORGANISM_TAXID: 1890280;                                             
SOURCE   4 GENE: F4V47_03290;                                                   
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ESTERASE, LIPASE, HYDROLASE, PATHOGEN BACTERIA                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.DO,J.H.LEE                                                          
REVDAT   1   07-JUN-23 7YC4    0                                                
JRNL        AUTH   H.DO,W.YOO,Y.WANG,Y.NAM,S.C.SHIN,H.W.KIM,K.K.KIM,J.H.LEE     
JRNL        TITL   CRYSTAL STRUCTURE AND BIOCHEMICAL ANALYSIS OF ACETYLESTERASE 
JRNL        TITL 2 (LGESTI) FROM LACTOCOCCUS GARVIEAE.                          
JRNL        REF    PLOS ONE                      V.  18 80988 2023              
JRNL        REFN                   ESSN 1932-6203                               
JRNL        PMID   36745644                                                     
JRNL        DOI    10.1371/JOURNAL.PONE.0280988                                 
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0267                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 29.37                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 151386                         
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) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.245                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.008                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 7581                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 10604                        
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2570                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 566                          
REMARK   3   BIN FREE R VALUE                    : 0.3130                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 20140                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 577                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 36.44                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01500                                             
REMARK   3    B22 (A**2) : 0.01000                                              
REMARK   3    B33 (A**2) : 0.00500                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00100                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.239         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.199         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.156         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.972         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.923                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 20556 ; 0.008 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A): 19145 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 27917 ; 1.538 ; 1.642       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 44008 ; 1.281 ; 1.579       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  2511 ; 7.410 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  1198 ;34.714 ;23.255       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  3488 ;15.884 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   128 ;18.890 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  2703 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A): 23593 ; 0.007 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  4775 ; 0.001 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  4435 ; 0.199 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):    96 ; 0.253 ; 0.200       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  9846 ; 0.160 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   883 ; 0.159 ; 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): 10068 ; 2.657 ; 3.724       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2): 10067 ; 2.657 ; 3.723       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2): 12571 ; 3.605 ; 5.573       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2): 12572 ; 3.606 ; 5.573       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2): 10488 ; 3.050 ; 4.044       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2): 10489 ; 3.051 ; 4.044       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2): 15346 ; 4.584 ; 5.955       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2): 15347 ; 4.584 ; 5.955       
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 : MASK BULK SOLVENT                                    
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 7YC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 12-JUL-22.                  
REMARK 100 THE DEPOSITION ID IS D_1300030631.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-APR-21                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : PAL/PLS                            
REMARK 200  BEAMLINE                       : 5C (4A)                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1                                  
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS EIGER X 9M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS                            
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 151387                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 29.365                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 6.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 10.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.71200                            
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: MOLREP                                                
REMARK 200 STARTING MODEL: 7YC0                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.89                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M POTASSIUM FORMATE, PH 7.3, 20%      
REMARK 280  (W/V) PEG 3350, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       63.69500            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, G                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, H                                  
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: 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 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E, F                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LYS A   317                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     VAL C     2                                                      
REMARK 465     GLU C     3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     VAL D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     LYS D   317                                                      
REMARK 465     GLY E    -2                                                      
REMARK 465     SER E    -1                                                      
REMARK 465     HIS E     0                                                      
REMARK 465     LYS E   317                                                      
REMARK 465     GLY F    -2                                                      
REMARK 465     SER F    -1                                                      
REMARK 465     HIS F     0                                                      
REMARK 465     MET F     1                                                      
REMARK 465     LYS F   317                                                      
REMARK 465     GLY G    -2                                                      
REMARK 465     SER G    -1                                                      
REMARK 465     HIS G     0                                                      
REMARK 465     MET G     1                                                      
REMARK 465     GLY H    -2                                                      
REMARK 465     SER H    -1                                                      
REMARK 465     HIS H     0                                                      
REMARK 465     MET H     1                                                      
REMARK 465     VAL H     2                                                      
REMARK 465     LYS H   317                                                      
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   OG1  THR A   221     OE1  GLU A   226              2.11            
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  87       36.28     92.07                                   
REMARK 500    TRP A  89       -9.65     80.34                                   
REMARK 500    ASN A  93     -178.85   -179.95                                   
REMARK 500    HIS A 152       75.78   -114.18                                   
REMARK 500    SER A 159     -119.59     59.75                                   
REMARK 500    TYR A 187       61.32     39.68                                   
REMARK 500    ALA A 192       44.60   -100.23                                   
REMARK 500    ASN A 205        8.40     87.07                                   
REMARK 500    ALA A 207      -78.49     69.80                                   
REMARK 500    ALA A 232      -51.95   -122.50                                   
REMARK 500    ALA A 255       65.46   -100.08                                   
REMARK 500    LYS B  76      150.99    -47.96                                   
REMARK 500    ALA B  87       34.12     96.61                                   
REMARK 500    TRP B  89       -9.92     76.28                                   
REMARK 500    ASN B  93     -176.37   -174.94                                   
REMARK 500    ASN B 109       61.32     39.52                                   
REMARK 500    HIS B 152       63.88   -111.43                                   
REMARK 500    SER B 159     -120.07     62.35                                   
REMARK 500    GLN B 178      131.99    -38.84                                   
REMARK 500    TYR B 187       62.59     35.30                                   
REMARK 500    ALA B 192       47.88    -78.97                                   
REMARK 500    ASN B 205        1.27     86.85                                   
REMARK 500    ALA B 207      -84.18     71.93                                   
REMARK 500    THR B 221      122.42   -178.59                                   
REMARK 500    SER B 223       99.17    -61.26                                   
REMARK 500    ALA B 255       63.09   -103.30                                   
REMARK 500    ARG B 316      -69.66    -95.60                                   
REMARK 500    ALA C  87       35.32     87.87                                   
REMARK 500    TRP C  89      -16.39     76.92                                   
REMARK 500    PRO C 126       44.15   -100.48                                   
REMARK 500    HIS C 152       65.41   -119.64                                   
REMARK 500    SER C 159     -112.07     64.76                                   
REMARK 500    TYR C 187       63.53     38.70                                   
REMARK 500    ALA C 192       45.35    -84.58                                   
REMARK 500    ASN C 205       -0.65     91.63                                   
REMARK 500    ALA C 207      -74.98     45.63                                   
REMARK 500    THR C 221      132.53   -173.62                                   
REMARK 500    ALA C 247      136.78    -39.32                                   
REMARK 500    HIS D  73       61.52     38.50                                   
REMARK 500    ALA D  87       44.16     90.20                                   
REMARK 500    TRP D  89       -8.72     78.06                                   
REMARK 500    TYR D 125      133.09    -29.75                                   
REMARK 500    SER D 159     -118.75     67.85                                   
REMARK 500    TYR D 187       68.40     35.60                                   
REMARK 500    ALA D 192       37.53    -83.35                                   
REMARK 500    ASN D 205       19.12     84.29                                   
REMARK 500    ALA D 207      -78.56     53.24                                   
REMARK 500    SER D 223       98.63    -65.62                                   
REMARK 500    ALA D 247      133.30    -34.97                                   
REMARK 500    ALA D 255       68.01   -100.74                                   
REMARK 500                                                                      
REMARK 500 THIS ENTRY HAS      90 RAMACHANDRAN OUTLIERS.                        
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 7YC0   RELATED DB: PDB                                   
REMARK 900 7YC0 IS THE WILD TYPE                                                
DBREF1 7YC4 A    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 A     A0A5M9R5N4                          1         317             
DBREF1 7YC4 B    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 B     A0A5M9R5N4                          1         317             
DBREF1 7YC4 C    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 C     A0A5M9R5N4                          1         317             
DBREF1 7YC4 D    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 D     A0A5M9R5N4                          1         317             
DBREF1 7YC4 E    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 E     A0A5M9R5N4                          1         317             
DBREF1 7YC4 F    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 F     A0A5M9R5N4                          1         317             
DBREF1 7YC4 G    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 G     A0A5M9R5N4                          1         317             
DBREF1 7YC4 H    1   317  UNP                  A0A5M9R5N4_9LACT                 
DBREF2 7YC4 H     A0A5M9R5N4                          1         317             
SEQADV 7YC4 GLY A   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER A   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS A    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA A  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY B   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER B   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS B    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA B  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY C   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER C   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS C    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA C  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY D   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER D   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS D    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA D  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY E   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER E   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS E    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA E  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY F   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER F   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS F    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA F  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY G   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER G   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS G    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA G  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQADV 7YC4 GLY H   -2  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 SER H   -1  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 HIS H    0  UNP  A0A5M9R5N           EXPRESSION TAG                 
SEQADV 7YC4 ALA H  207  UNP  A0A5M9R5N PHE   207 ENGINEERED MUTATION            
SEQRES   1 A  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 A  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 A  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 A  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 A  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 A  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 A  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 A  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 A  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 A  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 A  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 A  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 A  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 A  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 A  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 A  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 A  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 A  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 A  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 A  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 A  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 A  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 A  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 A  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 A  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 B  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 B  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 B  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 B  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 B  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 B  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 B  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 B  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 B  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 B  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 B  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 B  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 B  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 B  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 B  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 B  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 B  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 B  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 B  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 B  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 B  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 B  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 B  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 B  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 B  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 C  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 C  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 C  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 C  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 C  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 C  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 C  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 C  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 C  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 C  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 C  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 C  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 C  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 C  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 C  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 C  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 C  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 C  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 C  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 C  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 C  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 C  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 C  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 C  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 C  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 D  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 D  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 D  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 D  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 D  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 D  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 D  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 D  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 D  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 D  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 D  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 D  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 D  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 D  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 D  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 D  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 D  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 D  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 D  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 D  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 D  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 D  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 D  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 D  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 D  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 E  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 E  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 E  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 E  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 E  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 E  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 E  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 E  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 E  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 E  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 E  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 E  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 E  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 E  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 E  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 E  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 E  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 E  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 E  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 E  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 E  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 E  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 E  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 E  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 E  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 F  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 F  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 F  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 F  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 F  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 F  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 F  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 F  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 F  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 F  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 F  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 F  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 F  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 F  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 F  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 F  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 F  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 F  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 F  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 F  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 F  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 F  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 F  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 F  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 F  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 G  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 G  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 G  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 G  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 G  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 G  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 G  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 G  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 G  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 G  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 G  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 G  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 G  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 G  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 G  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 G  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 G  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 G  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 G  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 G  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 G  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 G  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 G  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 G  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 G  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
SEQRES   1 H  320  GLY SER HIS MET VAL GLU ARG ILE SER LEU GLU LYS ALA          
SEQRES   2 H  320  ALA LEU GLU PHE SER GLU ALA ASN ALA PRO HIS PRO ARG          
SEQRES   3 H  320  ILE TYR GLU LEU PRO VAL GLU GLU GLY ARG SER LEU LEU          
SEQRES   4 H  320  ASN GLU VAL GLN ASP SER PRO VAL VAL LYS GLU ASP VAL          
SEQRES   5 H  320  ASP ILE GLU ASP ILE ALA VAL ASP THR GLY GLU TRP GLY          
SEQRES   6 H  320  GLU ILE ASN VAL ARG PHE ILE ARG PRO LEU HIS GLN GLU          
SEQRES   7 H  320  LYS LYS LEU PRO VAL ILE PHE TYR ILE HIS GLY ALA GLY          
SEQRES   8 H  320  TRP VAL PHE GLY ASN ALA HIS THR HIS ASP LYS LEU ILE          
SEQRES   9 H  320  ARG GLU LEU ALA VAL ARG THR ASN SER VAL VAL VAL PHE          
SEQRES  10 H  320  SER GLU TYR SER LEU SER PRO GLU ALA LYS TYR PRO THR          
SEQRES  11 H  320  ALA ILE GLU GLN ASN TYR ALA VAL LEU GLN GLN LEU LYS          
SEQRES  12 H  320  ASP PHE ALA ASN ASP LYS LYS PHE ASP VAL ASN HIS LEU          
SEQRES  13 H  320  THR VAL ALA GLY ASP SER VAL GLY GLY ASN MET ALA THR          
SEQRES  14 H  320  VAL MET THR LEU LEU THR LYS GLN ARG GLY GLY GLN LYS          
SEQRES  15 H  320  ILE GLY GLN GLN VAL LEU TYR TYR PRO VAL THR ASP ALA          
SEQRES  16 H  320  ASN PHE ASP THR ASP SER TYR ASN GLU PHE ALA GLU ASN          
SEQRES  17 H  320  TYR ALA LEU THR LYS GLU GLY MET ILE TRP PHE TRP ASP          
SEQRES  18 H  320  GLN TYR THR THR SER GLN GLU GLU ARG HIS GLN ILE THR          
SEQRES  19 H  320  ALA SER PRO LEU ARG ALA THR LYS GLU ASP LEU ALA ASP          
SEQRES  20 H  320  LEU PRO ALA ALA LEU ILE ILE THR GLY GLU ALA ASP VAL          
SEQRES  21 H  320  LEU ARG ASP GLU GLY GLU ALA TYR ALA ARG LYS LEU ARG          
SEQRES  22 H  320  GLU ALA ASP VAL GLU VAL THR GLN VAL ARG PHE GLN ALA          
SEQRES  23 H  320  ILE ILE HIS ASP PHE VAL MET VAL ASN SER MET ASN GLU          
SEQRES  24 H  320  THR HIS ALA THR ARG ALA ALA MET SER LEU SER THR GLN          
SEQRES  25 H  320  TRP ILE ASN GLU LYS ASN ARG LYS                              
FORMUL   9  HOH   *577(H2 O)                                                    
HELIX    1 AA1 GLU A    8  ASN A   18  1                                  11    
HELIX    2 AA2 ARG A   23  LEU A   27  5                                   5    
HELIX    3 AA3 PRO A   28  GLN A   40  1                                  13    
HELIX    4 AA4 GLY A   59  TRP A   61  5                                   3    
HELIX    5 AA5 HIS A   97  THR A  108  1                                  12    
HELIX    6 AA6 PRO A  126  GLN A  138  1                                  13    
HELIX    7 AA7 GLN A  138  ALA A  143  1                                   6    
HELIX    8 AA8 SER A  159  GLY A  176  1                                  18    
HELIX    9 AA9 THR A  196  PHE A  202  1                                   7    
HELIX   10 AB1 THR A  209  THR A  221  1                                  13    
HELIX   11 AB2 SER A  223  HIS A  228  1                                   6    
HELIX   12 AB3 SER A  233  ALA A  237  5                                   5    
HELIX   13 AB4 THR A  238  ALA A  243  1                                   6    
HELIX   14 AB5 LEU A  258  ALA A  272  1                                  15    
HELIX   15 AB6 VAL A  291  ASN A  295  5                                   5    
HELIX   16 AB7 THR A  297  ASN A  315  1                                  19    
HELIX   17 AB8 GLU B    8  ASN B   18  1                                  11    
HELIX   18 AB9 ARG B   23  LEU B   27  5                                   5    
HELIX   19 AC1 PRO B   28  GLN B   40  1                                  13    
HELIX   20 AC2 GLY B   59  TRP B   61  5                                   3    
HELIX   21 AC3 HIS B   97  THR B  108  1                                  12    
HELIX   22 AC4 PRO B  126  GLN B  137  1                                  12    
HELIX   23 AC5 GLN B  138  LYS B  147  1                                  10    
HELIX   24 AC6 SER B  159  GLY B  176  1                                  18    
HELIX   25 AC7 THR B  196  PHE B  202  1                                   7    
HELIX   26 AC8 THR B  209  THR B  221  1                                  13    
HELIX   27 AC9 SER B  223  GLN B  229  1                                   7    
HELIX   28 AD1 SER B  233  ALA B  237  5                                   5    
HELIX   29 AD2 THR B  238  ALA B  243  1                                   6    
HELIX   30 AD3 LEU B  258  ALA B  272  1                                  15    
HELIX   31 AD4 VAL B  291  ASN B  295  5                                   5    
HELIX   32 AD5 THR B  297  LYS B  317  1                                  21    
HELIX   33 AD6 GLU C    8  ASN C   18  1                                  11    
HELIX   34 AD7 PRO C   28  GLN C   40  1                                  13    
HELIX   35 AD8 GLY C   59  TRP C   61  5                                   3    
HELIX   36 AD9 HIS C   97  ASN C  109  1                                  13    
HELIX   37 AE1 PRO C  126  GLN C  138  1                                  13    
HELIX   38 AE2 LEU C  139  PHE C  142  5                                   4    
HELIX   39 AE3 SER C  159  GLY C  176  1                                  18    
HELIX   40 AE4 THR C  196  PHE C  202  1                                   7    
HELIX   41 AE5 THR C  209  THR C  221  1                                  13    
HELIX   42 AE6 SER C  223  HIS C  228  1                                   6    
HELIX   43 AE7 SER C  233  ALA C  237  5                                   5    
HELIX   44 AE8 THR C  238  ALA C  243  1                                   6    
HELIX   45 AE9 LEU C  258  ALA C  272  1                                  15    
HELIX   46 AF1 VAL C  291  ASN C  295  5                                   5    
HELIX   47 AF2 THR C  297  LYS C  317  1                                  21    
HELIX   48 AF3 GLU D    8  ASN D   18  1                                  11    
HELIX   49 AF4 ARG D   23  LEU D   27  5                                   5    
HELIX   50 AF5 PRO D   28  GLN D   40  1                                  13    
HELIX   51 AF6 GLY D   59  TRP D   61  5                                   3    
HELIX   52 AF7 HIS D   97  THR D  108  1                                  12    
HELIX   53 AF8 PRO D  126  LEU D  139  1                                  14    
HELIX   54 AF9 LYS D  140  PHE D  142  5                                   3    
HELIX   55 AG1 SER D  159  GLY D  176  1                                  18    
HELIX   56 AG2 THR D  196  PHE D  202  1                                   7    
HELIX   57 AG3 THR D  209  THR D  221  1                                  13    
HELIX   58 AG4 GLU D  225  GLN D  229  5                                   5    
HELIX   59 AG5 SER D  233  ALA D  237  5                                   5    
HELIX   60 AG6 THR D  238  ALA D  243  1                                   6    
HELIX   61 AG7 LEU D  258  ALA D  272  1                                  15    
HELIX   62 AG8 VAL D  291  ASN D  295  5                                   5    
HELIX   63 AG9 THR D  297  ASN D  315  1                                  19    
HELIX   64 AH1 GLU E    8  ASN E   18  1                                  11    
HELIX   65 AH2 ARG E   23  LEU E   27  5                                   5    
HELIX   66 AH3 PRO E   28  GLN E   40  1                                  13    
HELIX   67 AH4 HIS E   97  ASN E  109  1                                  13    
HELIX   68 AH5 PRO E  126  LYS E  147  1                                  22    
HELIX   69 AH6 SER E  159  GLY E  176  1                                  18    
HELIX   70 AH7 THR E  196  PHE E  202  1                                   7    
HELIX   71 AH8 THR E  209  THR E  221  1                                  13    
HELIX   72 AH9 SER E  223  HIS E  228  1                                   6    
HELIX   73 AI1 SER E  233  ALA E  237  5                                   5    
HELIX   74 AI2 THR E  238  ALA E  243  1                                   6    
HELIX   75 AI3 LEU E  258  ALA E  272  1                                  15    
HELIX   76 AI4 VAL E  291  ASN E  295  5                                   5    
HELIX   77 AI5 THR E  297  ARG E  316  1                                  20    
HELIX   78 AI6 GLU F    8  ASN F   18  1                                  11    
HELIX   79 AI7 ARG F   23  LEU F   27  5                                   5    
HELIX   80 AI8 PRO F   28  GLN F   40  1                                  13    
HELIX   81 AI9 HIS F   97  ASN F  109  1                                  13    
HELIX   82 AJ1 PRO F  126  GLN F  138  1                                  13    
HELIX   83 AJ2 GLN F  138  ASN F  144  1                                   7    
HELIX   84 AJ3 SER F  159  GLY F  176  1                                  18    
HELIX   85 AJ4 THR F  196  PHE F  202  1                                   7    
HELIX   86 AJ5 THR F  209  THR F  221  1                                  13    
HELIX   87 AJ6 SER F  223  HIS F  228  1                                   6    
HELIX   88 AJ7 SER F  233  ALA F  237  5                                   5    
HELIX   89 AJ8 THR F  238  ALA F  243  1                                   6    
HELIX   90 AJ9 LEU F  258  ALA F  272  1                                  15    
HELIX   91 AK1 VAL F  291  ASN F  295  5                                   5    
HELIX   92 AK2 THR F  297  ARG F  316  1                                  20    
HELIX   93 AK3 GLU G    8  ASN G   18  1                                  11    
HELIX   94 AK4 ARG G   23  LEU G   27  5                                   5    
HELIX   95 AK5 PRO G   28  GLN G   40  1                                  13    
HELIX   96 AK6 HIS G   97  ASN G  109  1                                  13    
HELIX   97 AK7 PRO G  126  GLN G  137  1                                  12    
HELIX   98 AK8 GLN G  138  ALA G  143  1                                   6    
HELIX   99 AK9 SER G  159  GLY G  176  1                                  18    
HELIX  100 AL1 THR G  196  PHE G  202  1                                   7    
HELIX  101 AL2 THR G  209  THR G  221  1                                  13    
HELIX  102 AL3 SER G  233  ALA G  237  5                                   5    
HELIX  103 AL4 THR G  238  ALA G  243  1                                   6    
HELIX  104 AL5 LEU G  258  ALA G  272  1                                  15    
HELIX  105 AL6 VAL G  291  ASN G  295  5                                   5    
HELIX  106 AL7 THR G  297  LYS G  317  1                                  21    
HELIX  107 AL8 GLU H    8  ASN H   18  1                                  11    
HELIX  108 AL9 ARG H   23  LEU H   27  5                                   5    
HELIX  109 AM1 PRO H   28  GLN H   40  1                                  13    
HELIX  110 AM2 HIS H   97  THR H  108  1                                  12    
HELIX  111 AM3 PRO H  126  ALA H  143  1                                  18    
HELIX  112 AM4 SER H  159  GLY H  176  1                                  18    
HELIX  113 AM5 THR H  196  PHE H  202  1                                   7    
HELIX  114 AM6 THR H  209  THR H  221  1                                  13    
HELIX  115 AM7 SER H  223  HIS H  228  1                                   6    
HELIX  116 AM8 SER H  233  ALA H  237  5                                   5    
HELIX  117 AM9 THR H  238  ALA H  243  1                                   6    
HELIX  118 AN1 LEU H  258  ALA H  272  1                                  15    
HELIX  119 AN2 VAL H  291  ASN H  295  5                                   5    
HELIX  120 AN3 THR H  297  ASN H  315  1                                  19    
SHEET    1 AA116 ASP A  50  ASP A  57  0                                        
SHEET    2 AA116 GLU A  63  ARG A  70 -1  O  PHE A  68   N  GLU A  52           
SHEET    3 AA116 VAL A 111  GLU A 116 -1  O  PHE A 114   N  ARG A  67           
SHEET    4 AA116 LEU A  78  ILE A  84  1  N  ILE A  81   O  VAL A 113           
SHEET    5 AA116 PHE A 148  ASP A 158  1  O  HIS A 152   N  VAL A  80           
SHEET    6 AA116 GLN A 182  TYR A 186  1  O  GLN A 182   N  VAL A 155           
SHEET    7 AA116 ALA A 247  ALA A 255  1  O  LEU A 249   N  LEU A 185           
SHEET    8 AA116 VAL A 276  ILE A 285  1  O  PHE A 281   N  THR A 252           
SHEET    9 AA116 VAL G 276  ILE G 285 -1  O  ARG G 280   N  ARG A 280           
SHEET   10 AA116 ALA G 247  ALA G 255  1  N  ILE G 250   O  THR G 277           
SHEET   11 AA116 GLN G 182  TYR G 186  1  N  LEU G 185   O  LEU G 249           
SHEET   12 AA116 PHE G 148  ASP G 158  1  N  GLY G 157   O  TYR G 186           
SHEET   13 AA116 LEU G  78  ILE G  84  1  N  PHE G  82   O  THR G 154           
SHEET   14 AA116 VAL G 111  SER G 115  1  O  VAL G 113   N  TYR G  83           
SHEET   15 AA116 GLU G  63  PRO G  71 -1  N  ARG G  67   O  PHE G 114           
SHEET   16 AA116 VAL G  49  ASP G  57 -1  N  GLU G  52   O  PHE G  68           
SHEET    1 AA216 ASP B  50  ASP B  57  0                                        
SHEET    2 AA216 GLU B  63  ARG B  70 -1  O  PHE B  68   N  GLU B  52           
SHEET    3 AA216 VAL B 111  SER B 115 -1  O  PHE B 114   N  ARG B  67           
SHEET    4 AA216 LEU B  78  ILE B  84  1  N  TYR B  83   O  VAL B 113           
SHEET    5 AA216 PHE B 148  ASP B 158  1  O  THR B 154   N  PHE B  82           
SHEET    6 AA216 GLN B 182  TYR B 186  1  O  TYR B 186   N  GLY B 157           
SHEET    7 AA216 ALA B 247  ALA B 255  1  O  LEU B 249   N  LEU B 185           
SHEET    8 AA216 VAL B 276  ILE B 285  1  O  THR B 277   N  ALA B 248           
SHEET    9 AA216 VAL H 276  ILE H 285 -1  O  ARG H 280   N  ARG B 280           
SHEET   10 AA216 ALA H 247  ALA H 255  1  N  ILE H 250   O  THR H 277           
SHEET   11 AA216 GLN H 182  TYR H 186  1  N  LEU H 185   O  LEU H 249           
SHEET   12 AA216 PHE H 148  ASP H 158  1  N  GLY H 157   O  TYR H 186           
SHEET   13 AA216 LEU H  78  ILE H  84  1  N  PHE H  82   O  THR H 154           
SHEET   14 AA216 VAL H 111  SER H 115  1  O  VAL H 111   N  ILE H  81           
SHEET   15 AA216 GLU H  63  ARG H  70 -1  N  ARG H  67   O  PHE H 114           
SHEET   16 AA216 ASP H  50  ASP H  57 -1  N  ASP H  50   O  ARG H  70           
SHEET    1 AA316 ASP C  50  ASP C  57  0                                        
SHEET    2 AA316 GLU C  63  ARG C  70 -1  O  VAL C  66   N  ILE C  54           
SHEET    3 AA316 VAL C 111  SER C 115 -1  O  PHE C 114   N  ARG C  67           
SHEET    4 AA316 LEU C  78  ILE C  84  1  N  TYR C  83   O  VAL C 113           
SHEET    5 AA316 PHE C 148  ASP C 158  1  O  THR C 154   N  PHE C  82           
SHEET    6 AA316 GLN C 182  TYR C 186  1  O  TYR C 186   N  GLY C 157           
SHEET    7 AA316 ALA C 247  GLY C 253  1  O  ALA C 247   N  GLN C 183           
SHEET    8 AA316 VAL C 276  PHE C 281  1  O  THR C 277   N  ILE C 250           
SHEET    9 AA316 VAL D 276  ILE D 285 -1  O  ARG D 280   N  ARG C 280           
SHEET   10 AA316 ALA D 247  ALA D 255  1  N  ILE D 250   O  THR D 277           
SHEET   11 AA316 GLN D 182  TYR D 186  1  N  LEU D 185   O  LEU D 249           
SHEET   12 AA316 PHE D 148  ASP D 158  1  N  GLY D 157   O  TYR D 186           
SHEET   13 AA316 LEU D  78  ILE D  84  1  N  PHE D  82   O  THR D 154           
SHEET   14 AA316 VAL D 111  SER D 115  1  O  VAL D 113   N  ILE D  81           
SHEET   15 AA316 GLU D  63  ARG D  70 -1  N  ARG D  67   O  PHE D 114           
SHEET   16 AA316 ASP D  50  ASP D  57 -1  N  GLU D  52   O  PHE D  68           
SHEET    1 AA416 VAL E  49  ASP E  57  0                                        
SHEET    2 AA416 GLU E  63  PRO E  71 -1  O  PHE E  68   N  GLU E  52           
SHEET    3 AA416 VAL E 111  SER E 115 -1  O  PHE E 114   N  ARG E  67           
SHEET    4 AA416 LEU E  78  ILE E  84  1  N  ILE E  81   O  VAL E 111           
SHEET    5 AA416 PHE E 148  ASP E 158  1  O  THR E 154   N  PHE E  82           
SHEET    6 AA416 GLN E 182  TYR E 186  1  O  TYR E 186   N  GLY E 157           
SHEET    7 AA416 ALA E 247  ALA E 255  1  O  LEU E 249   N  LEU E 185           
SHEET    8 AA416 VAL E 276  ILE E 285  1  O  THR E 277   N  ILE E 250           
SHEET    9 AA416 VAL F 276  ILE F 285 -1  O  ARG F 280   N  ARG E 280           
SHEET   10 AA416 ALA F 247  ALA F 255  1  N  ILE F 250   O  THR F 277           
SHEET   11 AA416 GLN F 182  TYR F 186  1  N  LEU F 185   O  LEU F 249           
SHEET   12 AA416 PHE F 148  ASP F 158  1  N  GLY F 157   O  TYR F 186           
SHEET   13 AA416 LEU F  78  ILE F  84  1  N  PHE F  82   O  THR F 154           
SHEET   14 AA416 VAL F 111  SER F 115  1  O  VAL F 111   N  ILE F  81           
SHEET   15 AA416 GLU F  63  PRO F  71 -1  N  ARG F  67   O  PHE F 114           
SHEET   16 AA416 VAL F  49  ASP F  57 -1  N  GLU F  52   O  PHE F  68           
CISPEP   1 HIS A   21    PRO A   22          0         2.65                     
CISPEP   2 SER A  120    PRO A  121          0        -2.73                     
CISPEP   3 TYR A  125    PRO A  126          0         3.21                     
CISPEP   4 HIS B   21    PRO B   22          0        -8.05                     
CISPEP   5 SER B  120    PRO B  121          0         0.11                     
CISPEP   6 TYR B  125    PRO B  126          0        -2.80                     
CISPEP   7 HIS C   21    PRO C   22          0        -4.68                     
CISPEP   8 SER C  120    PRO C  121          0        -1.35                     
CISPEP   9 TYR C  125    PRO C  126          0        -4.99                     
CISPEP  10 HIS D   21    PRO D   22          0        -3.98                     
CISPEP  11 SER D  120    PRO D  121          0        16.86                     
CISPEP  12 TYR D  125    PRO D  126          0        -1.66                     
CISPEP  13 HIS E   21    PRO E   22          0         6.23                     
CISPEP  14 SER E  120    PRO E  121          0        -2.86                     
CISPEP  15 TYR E  125    PRO E  126          0        -2.35                     
CISPEP  16 HIS F   21    PRO F   22          0        -5.08                     
CISPEP  17 SER F  120    PRO F  121          0        -5.27                     
CISPEP  18 TYR F  125    PRO F  126          0        -4.61                     
CISPEP  19 HIS G   21    PRO G   22          0        -5.58                     
CISPEP  20 SER G  120    PRO G  121          0        -0.38                     
CISPEP  21 TYR G  125    PRO G  126          0        -0.27                     
CISPEP  22 HIS H   21    PRO H   22          0         2.28                     
CISPEP  23 SER H  120    PRO H  121          0        -3.13                     
CISPEP  24 TYR H  125    PRO H  126          0        -5.26                     
CRYST1   99.200  127.390  104.760  90.00  90.17  90.00 P 1 21 1     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      0.010081  0.000000  0.000030        0.00000                         
SCALE2      0.000000  0.007850  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009546        0.00000                         
TER    2519      ARG A 316                                                      
TER    5047      LYS B 317                                                      
TER    7559      LYS C 317                                                      
TER   10062      ARG D 316                                                      
TER   12589      ARG E 316                                                      
TER   15108      ARG F 316                                                      
TER   17636      LYS G 317                                                      
TER   20148      ARG H 316                                                      
MASTER      378    0    0  120   64    0    0    620717    8    0  200          
END                                                                             

Send your questions or comments to :
Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
ESTHER Home Page and ACEDB Home Page
AcePerl Lincoln Stein Home Page
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