Tree Display

AceDB Schema

XML Display

Feedback

LongText Report for: 7qjm-pdb

Name Class
7qjm-pdb
HEADER    HYDROLASE                               17-DEC-21   7QJM              
TITLE     CRYSTAL STRUCTURE OF AN ALPHA/BETA-HYDROLASE ENZYME FROM CHLOROFLEXUS 
TITLE    2 SP. MS-G (202)                                                       
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA-HYDROLASE (202);                                
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: CHLOROFLEXUS SP. MS-G;                          
SOURCE   3 ORGANISM_TAXID: 1521187;                                             
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 469008                                      
KEYWDS    PLASTIC DEGRADATION, PEPTIDASE, HYDROLASE                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.ZAHN,R.GRAHAM,G.T.BECKHAM,J.E.MCGEEHAN                              
REVDAT   1   28-DEC-22 7QJM    0                                                
JRNL        AUTH   E.ERICKSON,J.E.GADO,L.AVILAN,F.BRATTI,R.K.BRIZENDINE,        
JRNL        AUTH 2 P.A.COX,R.GILL,R.GRAHAM,D.J.KIM,G.KONIG,W.E.MICHENER,        
JRNL        AUTH 3 S.POUDEL,K.J.RAMIREZ,T.J.SHAKESPEARE,M.ZAHN,E.S.BOYD,        
JRNL        AUTH 4 C.M.PAYNE,J.L.DUBOIS,A.R.PICKFORD,G.T.BECKHAM,J.E.MCGEEHAN   
JRNL        TITL   SOURCING THERMOTOLERANT POLY(ETHYLENE TEREPHTHALATE)         
JRNL        TITL 2 HYDROLASE SCAFFOLDS FROM NATURAL DIVERSITY                   
JRNL        REF    NAT COMMUN                    V.  13  7850 2022              
JRNL        REFN                   ESSN 2041-1723                               
JRNL        DOI    10.1038/S41467-022-35237-X                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.19 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.4                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.19                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.33                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 49979                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.217                          
REMARK   3   R VALUE            (WORKING SET)  : 0.216                          
REMARK   3   FREE R VALUE                      : 0.244                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : NULL                           
REMARK   3   FREE R VALUE TEST SET COUNT       : 2537                           
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : NULL                     
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 2.19                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 2.21                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 100.0                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : NULL                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : NULL                     
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : NULL                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.3833                   
REMARK   3   BIN FREE R VALUE                        : 0.3464                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : NULL                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 50                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : NULL                     
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4629                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 139                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 79.76                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.58380                                              
REMARK   3    B22 (A**2) : 0.50050                                              
REMARK   3    B33 (A**2) : -4.08420                                             
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 COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.320               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : 0.182               
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.162               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : 0.185               
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : 0.165               
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.957                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.935                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 4736   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 6452   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1611   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : NULL   ; NULL   ; NULL                
REMARK   3    GENERAL PLANES            : 802    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 4736   ; 10.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : NULL   ; NULL   ; NULL                
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 604    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 3802   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.008                    
REMARK   3    BOND ANGLES                  (DEGREES) : 0.97                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 3.16                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 17.54                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):   14.1544  -33.7073   17.6131           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:    0.0344 T22:    0.0154                                    
REMARK   3     T33:   -0.0567 T12:   -0.0184                                    
REMARK   3     T13:   -0.1298 T23:    0.0793                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.9144 L22:    0.7022                                    
REMARK   3     L33:    2.6189 L12:    0.5012                                    
REMARK   3     L13:    1.0858 L23:    0.9359                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1655 S12:   -0.0756 S13:    0.0122                     
REMARK   3     S21:   -0.0756 S22:     0.109 S23:     0.223                     
REMARK   3     S31:    0.0122 S32:     0.223 S33:    0.0564                     
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: { B|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -13.6795  -18.5367   30.8241           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.0752 T22:    0.1161                                    
REMARK   3     T33:    0.2169 T12:   -0.0207                                    
REMARK   3     T13:   -0.0899 T23:    0.0241                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:     2.387 L22:    2.9126                                    
REMARK   3     L33:    2.9522 L12:    0.9996                                    
REMARK   3     L13:   -0.1658 L23:    2.0696                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.1563 S12:   -0.3097 S13:   -0.1802                     
REMARK   3     S21:   -0.3097 S22:   -0.2441 S23:   -0.7702                     
REMARK   3     S31:   -0.1802 S32:   -0.7702 S33:    0.4004                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7QJM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 17-DEC-21.                  
REMARK 100 THE DEPOSITION ID IS D_1292118047.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 26-JAN-20                          
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               : DIAMOND                            
REMARK 200  BEAMLINE                       : I24                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9686                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS3 6M                
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XIA2                               
REMARK 200  DATA SCALING SOFTWARE          : XIA2                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 49979                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.190                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.330                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 13.10                              
REMARK 200  R MERGE                    (I) : 0.08900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.19                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.23                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 13.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 3.18100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.900                              
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: 7D78                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 56.74                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.84                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15 % PEG 3350, 0.1 M SUCCINIC ACID,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
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,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-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        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       45.34000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       62.45500            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       84.99500            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       45.34000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       62.45500            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       84.99500            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       45.34000            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       62.45500            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       84.99500            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       45.34000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       62.45500            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       84.99500            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 407  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     VAL A     2                                                      
REMARK 465     ASP A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     GLY A     8                                                      
REMARK 465     MET A     9                                                      
REMARK 465     ALA A    10                                                      
REMARK 465     ALA A    11                                                      
REMARK 465     THR A    12                                                      
REMARK 465     ALA A    13                                                      
REMARK 465     PRO A    14                                                      
REMARK 465     THR A    15                                                      
REMARK 465     ASP A    16                                                      
REMARK 465     GLU A    17                                                      
REMARK 465     ARG A    18                                                      
REMARK 465     ILE A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     ASP A    21                                                      
REMARK 465     LYS A    22                                                      
REMARK 465     PRO A    23                                                      
REMARK 465     LEU A    24                                                      
REMARK 465     PRO A    25                                                      
REMARK 465     GLN A    26                                                      
REMARK 465     PRO A    27                                                      
REMARK 465     GLN A    28                                                      
REMARK 465     ILE A    29                                                      
REMARK 465     ARG A    30                                                      
REMARK 465     SER A    31                                                      
REMARK 465     GLY A    32                                                      
REMARK 465     ASN A    33                                                      
REMARK 465     VAL A    34                                                      
REMARK 465     ARG A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     MET A    37                                                      
REMARK 465     PRO A    38                                                      
REMARK 465     ALA A    39                                                      
REMARK 465     ALA A    40                                                      
REMARK 465     ARG A    41                                                      
REMARK 465     LYS A    42                                                      
REMARK 465     LEU A    43                                                      
REMARK 465     ALA A    44                                                      
REMARK 465     GLN A    45                                                      
REMARK 465     GLU A    46                                                      
REMARK 465     HIS A    47                                                      
REMARK 465     GLY A    48                                                      
REMARK 465     ILE A    49                                                      
REMARK 465     ASP A    50                                                      
REMARK 465     LEU A    51                                                      
REMARK 465     SER A    52                                                      
REMARK 465     THR A    53                                                      
REMARK 465     LEU A    54                                                      
REMARK 465     THR A    55                                                      
REMARK 465     GLY A    56                                                      
REMARK 465     SER A    57                                                      
REMARK 465     GLY A    58                                                      
REMARK 465     PRO A    59                                                      
REMARK 465     GLY A    60                                                      
REMARK 465     GLY A    61                                                      
REMARK 465     VAL A    62                                                      
REMARK 465     ILE A    63                                                      
REMARK 465     VAL A    64                                                      
REMARK 465     LYS A    65                                                      
REMARK 465     GLU A    66                                                      
REMARK 465     ASP A    67                                                      
REMARK 465     VAL A    68                                                      
REMARK 465     GLU A    69                                                      
REMARK 465     ARG A    70                                                      
REMARK 465     ALA A    71                                                      
REMARK 465     ILE A    72                                                      
REMARK 465     THR A    73                                                      
REMARK 465     ALA A    74                                                      
REMARK 465     ARG A    75                                                      
REMARK 465     ALA A    76                                                      
REMARK 465     ALA A   378                                                      
REMARK 465     ASP A   379                                                      
REMARK 465     ASN A   380                                                      
REMARK 465     LEU A   381                                                      
REMARK 465     GLU A   382                                                      
REMARK 465     HIS A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     MET B     1                                                      
REMARK 465     VAL B     2                                                      
REMARK 465     ASP B     3                                                      
REMARK 465     ILE B     4                                                      
REMARK 465     THR B     5                                                      
REMARK 465     GLY B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     GLY B     8                                                      
REMARK 465     MET B     9                                                      
REMARK 465     ALA B    10                                                      
REMARK 465     ALA B    11                                                      
REMARK 465     THR B    12                                                      
REMARK 465     ALA B    13                                                      
REMARK 465     PRO B    14                                                      
REMARK 465     THR B    15                                                      
REMARK 465     ASP B    16                                                      
REMARK 465     GLU B    17                                                      
REMARK 465     ARG B    18                                                      
REMARK 465     ILE B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     ASP B    21                                                      
REMARK 465     LYS B    22                                                      
REMARK 465     PRO B    23                                                      
REMARK 465     LEU B    24                                                      
REMARK 465     PRO B    25                                                      
REMARK 465     GLN B    26                                                      
REMARK 465     PRO B    27                                                      
REMARK 465     GLN B    28                                                      
REMARK 465     ILE B    29                                                      
REMARK 465     ARG B    30                                                      
REMARK 465     SER B    31                                                      
REMARK 465     GLY B    32                                                      
REMARK 465     ASN B    33                                                      
REMARK 465     VAL B    34                                                      
REMARK 465     ARG B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     MET B    37                                                      
REMARK 465     PRO B    38                                                      
REMARK 465     ALA B    39                                                      
REMARK 465     ALA B    40                                                      
REMARK 465     ARG B    41                                                      
REMARK 465     LYS B    42                                                      
REMARK 465     LEU B    43                                                      
REMARK 465     ALA B    44                                                      
REMARK 465     GLN B    45                                                      
REMARK 465     GLU B    46                                                      
REMARK 465     HIS B    47                                                      
REMARK 465     GLY B    48                                                      
REMARK 465     ILE B    49                                                      
REMARK 465     ASP B    50                                                      
REMARK 465     LEU B    51                                                      
REMARK 465     SER B    52                                                      
REMARK 465     THR B    53                                                      
REMARK 465     LEU B    54                                                      
REMARK 465     THR B    55                                                      
REMARK 465     GLY B    56                                                      
REMARK 465     SER B    57                                                      
REMARK 465     GLY B    58                                                      
REMARK 465     PRO B    59                                                      
REMARK 465     GLY B    60                                                      
REMARK 465     GLY B    61                                                      
REMARK 465     VAL B    62                                                      
REMARK 465     ILE B    63                                                      
REMARK 465     VAL B    64                                                      
REMARK 465     LYS B    65                                                      
REMARK 465     GLU B    66                                                      
REMARK 465     ASP B    67                                                      
REMARK 465     VAL B    68                                                      
REMARK 465     GLU B    69                                                      
REMARK 465     ARG B    70                                                      
REMARK 465     ALA B    71                                                      
REMARK 465     ILE B    72                                                      
REMARK 465     THR B    73                                                      
REMARK 465     ALA B    74                                                      
REMARK 465     ARG B    75                                                      
REMARK 465     ALA B    76                                                      
REMARK 465     VAL B    77                                                      
REMARK 465     PRO B    78                                                      
REMARK 465     VAL B    79                                                      
REMARK 465     SER B   377                                                      
REMARK 465     ALA B   378                                                      
REMARK 465     ASP B   379                                                      
REMARK 465     ASN B   380                                                      
REMARK 465     LEU B   381                                                      
REMARK 465     GLU B   382                                                      
REMARK 465     HIS B   383                                                      
REMARK 465     HIS B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     HIS B   386                                                      
REMARK 465     HIS B   387                                                      
REMARK 465     HIS B   388                                                      
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    TYR A 119      107.77    -47.37                                   
REMARK 500    VAL A 126      -51.08     71.90                                   
REMARK 500    SER A 192     -113.29     56.88                                   
REMARK 500    PHE A 279       74.51   -115.59                                   
REMARK 500    ALA A 307     -121.85     41.17                                   
REMARK 500    HIS B 103       40.20     37.69                                   
REMARK 500    TYR B 119      108.81    -49.84                                   
REMARK 500    VAL B 126      -51.21     74.47                                   
REMARK 500    SER B 192     -111.90     57.01                                   
REMARK 500    ALA B 307     -121.79     41.94                                   
REMARK 500    SER B 337      -10.07     70.19                                   
REMARK 500    SER B 347     -138.95    -87.94                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  7QJM A    1   388  PDB    7QJM     7QJM             1    388             
DBREF  7QJM B    1   388  PDB    7QJM     7QJM             1    388             
SEQRES   1 A  388  MET VAL ASP ILE THR GLY ASN GLY MET ALA ALA THR ALA          
SEQRES   2 A  388  PRO THR ASP GLU ARG ILE VAL ASP LYS PRO LEU PRO GLN          
SEQRES   3 A  388  PRO GLN ILE ARG SER GLY ASN VAL ARG ALA MET PRO ALA          
SEQRES   4 A  388  ALA ARG LYS LEU ALA GLN GLU HIS GLY ILE ASP LEU SER          
SEQRES   5 A  388  THR LEU THR GLY SER GLY PRO GLY GLY VAL ILE VAL LYS          
SEQRES   6 A  388  GLU ASP VAL GLU ARG ALA ILE THR ALA ARG ALA VAL PRO          
SEQRES   7 A  388  VAL SER PRO LEU GLN ARG VAL ASN PHE TYR SER ALA GLY          
SEQRES   8 A  388  TYR ARG LEU ASP GLY LEU LEU TYR THR PRO ARG HIS LEU          
SEQRES   9 A  388  PRO ALA GLY GLU ARG ARG PRO GLY VAL VAL LEU LEU VAL          
SEQRES  10 A  388  GLY TYR THR TYR LEU LYS THR MET VAL MET PRO ASP ILE          
SEQRES  11 A  388  ALA LYS VAL LEU ASN ALA ALA GLY TYR VAL ALA LEU VAL          
SEQRES  12 A  388  PHE ASP TYR ARG GLY PHE GLY GLU SER GLU GLY PRO ARG          
SEQRES  13 A  388  GLY ARG LEU ILE PRO LEU GLU GLN VAL ALA ASP ALA ARG          
SEQRES  14 A  388  ALA ALA LEU THR PHE LEU ALA GLU GLN SER MET VAL ASP          
SEQRES  15 A  388  PRO ASP ARG LEU ALA VAL ILE GLY ILE SER LEU GLY GLY          
SEQRES  16 A  388  ALA HIS ALA ILE THR THR ALA ALA LEU ASP GLN ARG VAL          
SEQRES  17 A  388  ARG ALA VAL VAL ALA LEU GLU PRO PRO GLY HIS GLY ALA          
SEQRES  18 A  388  ARG TRP LEU ARG SER LEU ARG ARG HIS TRP GLU TRP ARG          
SEQRES  19 A  388  GLN PHE LEU SER ARG LEU ALA GLU ASP ARG ARG GLN ARG          
SEQRES  20 A  388  VAL LEU SER GLY GLY SER THR MET VAL ASP PRO LEU GLU          
SEQRES  21 A  388  ILE VAL LEU PRO ASP PRO GLU SER GLN ALA PHE LEU ASP          
SEQRES  22 A  388  GLN VAL ALA ALA GLU PHE PRO GLN MET LYS VAL THR LEU          
SEQRES  23 A  388  PRO LEU GLU SER ALA GLU ALA LEU ILE GLU TYR VAL SER          
SEQRES  24 A  388  GLU ASP LEU ALA GLY ARG ILE ALA PRO ARG PRO LEU LEU          
SEQRES  25 A  388  ILE ILE HIS SER ASP ALA ASP GLN LEU VAL PRO VAL ALA          
SEQRES  26 A  388  GLU ALA GLN ALA ILE ALA GLU ARG ALA GLY SER SER ALA          
SEQRES  27 A  388  GLN LEU GLU ILE ILE PRO GLY MET SER HIS PHE ASN TRP          
SEQRES  28 A  388  VAL MET PRO GLY SER PRO GLY PHE THR ARG VAL THR ASP          
SEQRES  29 A  388  SER ILE VAL LYS PHE LEU ARG ASN THR LEU PRO VAL SER          
SEQRES  30 A  388  ALA ASP ASN LEU GLU HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  388  MET VAL ASP ILE THR GLY ASN GLY MET ALA ALA THR ALA          
SEQRES   2 B  388  PRO THR ASP GLU ARG ILE VAL ASP LYS PRO LEU PRO GLN          
SEQRES   3 B  388  PRO GLN ILE ARG SER GLY ASN VAL ARG ALA MET PRO ALA          
SEQRES   4 B  388  ALA ARG LYS LEU ALA GLN GLU HIS GLY ILE ASP LEU SER          
SEQRES   5 B  388  THR LEU THR GLY SER GLY PRO GLY GLY VAL ILE VAL LYS          
SEQRES   6 B  388  GLU ASP VAL GLU ARG ALA ILE THR ALA ARG ALA VAL PRO          
SEQRES   7 B  388  VAL SER PRO LEU GLN ARG VAL ASN PHE TYR SER ALA GLY          
SEQRES   8 B  388  TYR ARG LEU ASP GLY LEU LEU TYR THR PRO ARG HIS LEU          
SEQRES   9 B  388  PRO ALA GLY GLU ARG ARG PRO GLY VAL VAL LEU LEU VAL          
SEQRES  10 B  388  GLY TYR THR TYR LEU LYS THR MET VAL MET PRO ASP ILE          
SEQRES  11 B  388  ALA LYS VAL LEU ASN ALA ALA GLY TYR VAL ALA LEU VAL          
SEQRES  12 B  388  PHE ASP TYR ARG GLY PHE GLY GLU SER GLU GLY PRO ARG          
SEQRES  13 B  388  GLY ARG LEU ILE PRO LEU GLU GLN VAL ALA ASP ALA ARG          
SEQRES  14 B  388  ALA ALA LEU THR PHE LEU ALA GLU GLN SER MET VAL ASP          
SEQRES  15 B  388  PRO ASP ARG LEU ALA VAL ILE GLY ILE SER LEU GLY GLY          
SEQRES  16 B  388  ALA HIS ALA ILE THR THR ALA ALA LEU ASP GLN ARG VAL          
SEQRES  17 B  388  ARG ALA VAL VAL ALA LEU GLU PRO PRO GLY HIS GLY ALA          
SEQRES  18 B  388  ARG TRP LEU ARG SER LEU ARG ARG HIS TRP GLU TRP ARG          
SEQRES  19 B  388  GLN PHE LEU SER ARG LEU ALA GLU ASP ARG ARG GLN ARG          
SEQRES  20 B  388  VAL LEU SER GLY GLY SER THR MET VAL ASP PRO LEU GLU          
SEQRES  21 B  388  ILE VAL LEU PRO ASP PRO GLU SER GLN ALA PHE LEU ASP          
SEQRES  22 B  388  GLN VAL ALA ALA GLU PHE PRO GLN MET LYS VAL THR LEU          
SEQRES  23 B  388  PRO LEU GLU SER ALA GLU ALA LEU ILE GLU TYR VAL SER          
SEQRES  24 B  388  GLU ASP LEU ALA GLY ARG ILE ALA PRO ARG PRO LEU LEU          
SEQRES  25 B  388  ILE ILE HIS SER ASP ALA ASP GLN LEU VAL PRO VAL ALA          
SEQRES  26 B  388  GLU ALA GLN ALA ILE ALA GLU ARG ALA GLY SER SER ALA          
SEQRES  27 B  388  GLN LEU GLU ILE ILE PRO GLY MET SER HIS PHE ASN TRP          
SEQRES  28 B  388  VAL MET PRO GLY SER PRO GLY PHE THR ARG VAL THR ASP          
SEQRES  29 B  388  SER ILE VAL LYS PHE LEU ARG ASN THR LEU PRO VAL SER          
SEQRES  30 B  388  ALA ASP ASN LEU GLU HIS HIS HIS HIS HIS HIS                  
FORMUL   3  HOH   *139(H2 O)                                                    
HELIX    1 AA1 VAL A  126  ALA A  137  1                                  12    
HELIX    2 AA2 ILE A  160  GLU A  177  1                                  18    
HELIX    3 AA3 SER A  192  ASP A  205  1                                  14    
HELIX    4 AA4 HIS A  219  LEU A  227  1                                   9    
HELIX    5 AA5 ARG A  229  GLY A  251  1                                  23    
HELIX    6 AA6 ASP A  257  ILE A  261  5                                   5    
HELIX    7 AA7 ASP A  265  PHE A  279  1                                  15    
HELIX    8 AA8 PRO A  280  LYS A  283  5                                   4    
HELIX    9 AA9 LEU A  288  GLU A  296  1                                   9    
HELIX   10 AB1 SER A  299  GLY A  304  1                                   6    
HELIX   11 AB2 ARG A  305  ALA A  307  5                                   3    
HELIX   12 AB3 PRO A  323  GLY A  335  1                                  13    
HELIX   13 AB4 SER A  356  ASN A  372  1                                  17    
HELIX   14 AB5 VAL B  126  ALA B  137  1                                  12    
HELIX   15 AB6 ILE B  160  GLU B  177  1                                  18    
HELIX   16 AB7 SER B  192  ASP B  205  1                                  14    
HELIX   17 AB8 HIS B  219  LEU B  227  1                                   9    
HELIX   18 AB9 ARG B  229  GLY B  251  1                                  23    
HELIX   19 AC1 ASP B  257  ILE B  261  5                                   5    
HELIX   20 AC2 ASP B  265  PHE B  279  1                                  15    
HELIX   21 AC3 PRO B  280  LYS B  283  5                                   4    
HELIX   22 AC4 LEU B  288  GLU B  296  1                                   9    
HELIX   23 AC5 SER B  299  GLY B  304  1                                   6    
HELIX   24 AC6 ARG B  305  ALA B  307  5                                   3    
HELIX   25 AC7 PRO B  323  ALA B  334  1                                  12    
HELIX   26 AC8 SER B  356  ASN B  372  1                                  17    
SHEET    1 AA1 8 LEU A  82  SER A  89  0                                        
SHEET    2 AA1 8 TYR A  92  TYR A  99 -1  O  LEU A  94   N  PHE A  87           
SHEET    3 AA1 8 VAL A 140  PHE A 144 -1  O  ALA A 141   N  TYR A  99           
SHEET    4 AA1 8 ARG A 110  LEU A 116  1  N  LEU A 115   O  LEU A 142           
SHEET    5 AA1 8 VAL A 181  ILE A 191  1  O  ILE A 189   N  LEU A 116           
SHEET    6 AA1 8 VAL A 208  LEU A 214  1  O  ARG A 209   N  LEU A 186           
SHEET    7 AA1 8 LEU A 311  HIS A 315  1  O  LEU A 312   N  ALA A 213           
SHEET    8 AA1 8 ALA A 338  ILE A 342  1  O  GLU A 341   N  ILE A 313           
SHEET    1 AA2 2 MET A 255  VAL A 256  0                                        
SHEET    2 AA2 2 LEU A 286  PRO A 287 -1  O  LEU A 286   N  VAL A 256           
SHEET    1 AA3 8 LEU B  82  SER B  89  0                                        
SHEET    2 AA3 8 TYR B  92  TYR B  99 -1  O  LEU B  94   N  PHE B  87           
SHEET    3 AA3 8 VAL B 140  PHE B 144 -1  O  ALA B 141   N  TYR B  99           
SHEET    4 AA3 8 ARG B 110  LEU B 116  1  N  LEU B 115   O  LEU B 142           
SHEET    5 AA3 8 VAL B 181  ILE B 191  1  O  ILE B 189   N  LEU B 116           
SHEET    6 AA3 8 VAL B 208  LEU B 214  1  O  ARG B 209   N  LEU B 186           
SHEET    7 AA3 8 LEU B 311  HIS B 315  1  O  LEU B 312   N  ALA B 213           
SHEET    8 AA3 8 ALA B 338  ILE B 342  1  O  GLU B 341   N  ILE B 313           
SHEET    1 AA4 2 MET B 255  VAL B 256  0                                        
SHEET    2 AA4 2 LEU B 286  PRO B 287 -1  O  LEU B 286   N  VAL B 256           
CRYST1   90.680  124.910  169.990  90.00  90.00  90.00 I 2 2 2      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      0.011028  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008006  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005883        0.00000                         
TER    2329      SER A 377                                                      
TER    4631      VAL B 376                                                      
MASTER      488    0    0   26   20    0    0    6 4768    2    0   60          
END                                                                             

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

Acknowledgements and disclaimer