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LongText Report for: 5hc4-pdb

Name Class
5hc4-pdb
HEADER    HYDROLASE                               04-JAN-16   5HC4              
TITLE     STRUCTURE OF ESTERASE EST22                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: LIPOLYTIC ENZYME;                                          
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 3.1.1.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: UNCULTURED BACTERIUM;                           
SOURCE   3 ORGANISM_TAXID: 77133;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ESTERASE, EST22, HYDROLASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.LI,J.HUANG                                                          
REVDAT   1   18-JAN-17 5HC4    0                                                
JRNL        AUTH   J.HUANG,Y.Y.HUO,R.JI,S.KUANG,C.JI,X.W.XU,J.LI                
JRNL        TITL   STRUCTURAL INSIGHTS OF A HORMONE SENSITIVE LIPASE HOMOLOGUE  
JRNL        TITL 2 EST22.                                                       
JRNL        REF    SCI REP                       V.   6 28550 2016              
JRNL        REFN                   ESSN 2045-2322                               
JRNL        PMID   27328716                                                     
JRNL        DOI    10.1038/SREP28550                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0131                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 91396                          
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) : 0.177                           
REMARK   3   R VALUE            (WORKING SET) : 0.174                           
REMARK   3   FREE R VALUE                     : 0.233                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4786                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 5334                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 75.72                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 280                          
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 10183                                   
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 14                                      
REMARK   3   SOLVENT ATOMS            : 1131                                    
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 33.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.15000                                             
REMARK   3    B22 (A**2) : 1.18000                                              
REMARK   3    B33 (A**2) : -1.03000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.179         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.170         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.127         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.781         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.960                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.931                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A): 10408 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 14123 ; 1.918 ; 1.966       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1361 ; 6.797 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   455 ;37.792 ;24.549       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1619 ;15.547 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    64 ;19.741 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1544 ; 0.128 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  8024 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
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):  5454 ; 2.932 ; 3.096       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6808 ; 3.945 ; 4.620       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  4954 ; 4.219 ; 3.289       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2): 17703 ; 7.975 ;26.971       
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                                                 
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 USED IF PRESENT IN    
REMARK   3  THE INPUT U VALUES                                                  
REMARK   4                                                                      
REMARK   4 5HC4 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 14-JAN-16.                  
REMARK 100 THE DEPOSITION ID IS D_1000216808.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 05-MAY-15                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL19U1                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9785                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 101542                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.50                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 12.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.10                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.52                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES SODIUM, PH7.5, 1.5M LI2SO4,   
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       40.62150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       75.26100            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       60.90550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       75.26100            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       40.62150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       60.90550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DIMERIC                           
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
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 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   -20                                                      
REMARK 465     GLY A   -19                                                      
REMARK 465     SER A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     MET B   -20                                                      
REMARK 465     GLY B   -19                                                      
REMARK 465     SER B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ASN B     3                                                      
REMARK 465     MET C   -20                                                      
REMARK 465     GLY C   -19                                                      
REMARK 465     SER C   -18                                                      
REMARK 465     SER C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     HIS C   -11                                                      
REMARK 465     HIS C   -10                                                      
REMARK 465     SER C    -9                                                      
REMARK 465     SER C    -8                                                      
REMARK 465     GLY C    -7                                                      
REMARK 465     LEU C    -6                                                      
REMARK 465     VAL C    -5                                                      
REMARK 465     PRO C    -4                                                      
REMARK 465     ARG C    -3                                                      
REMARK 465     GLY C    -2                                                      
REMARK 465     SER C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MET C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     GLY C    25                                                      
REMARK 465     GLY C    26                                                      
REMARK 465     MET D   -20                                                      
REMARK 465     GLY D   -19                                                      
REMARK 465     SER D   -18                                                      
REMARK 465     SER D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     HIS D   -11                                                      
REMARK 465     HIS D   -10                                                      
REMARK 465     SER D    -9                                                      
REMARK 465     SER D    -8                                                      
REMARK 465     GLY D    -7                                                      
REMARK 465     LEU D    -6                                                      
REMARK 465     VAL D    -5                                                      
REMARK 465     PRO D    -4                                                      
REMARK 465     ARG D    -3                                                      
REMARK 465     GLY D    -2                                                      
REMARK 465     SER D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MET D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLU A  43    CG   CD   OE1  OE2                                  
REMARK 470     GLU B  44    CG   CD   OE1  OE2                                  
REMARK 470     ASN C   3    CG   OD1  ND2                                       
REMARK 470     LYS C   4    CG   CD   CE   NZ                                   
REMARK 470     GLU C   7    CG   CD   OE1  OE2                                  
REMARK 470     ASP C  23    CG   OD1  OD2                                       
REMARK 470     LEU C  24    CG   CD1  CD2                                       
REMARK 470     GLU C  31    CG   CD   OE1  OE2                                  
REMARK 470     ASN D   3    CG   OD1  ND2                                       
REMARK 470     SER D  41    OG                                                  
REMARK 470     GLU D  43    CG   CD   OE1  OE2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH B   600     O    HOH B   632              1.91            
REMARK 500   NH1  ARG D   331     O    HOH D   401              1.94            
REMARK 500   O    HOH C   610     O    HOH C   626              2.03            
REMARK 500   SD   MET C   258     O    HOH C   601              2.08            
REMARK 500   OE1  GLU D   204     O    HOH D   402              2.11            
REMARK 500   O    HOH C   615     O    HOH C   657              2.11            
REMARK 500   O    GLY D   109     O    HOH D   403              2.12            
REMARK 500   O    HOH A   623     O    HOH A   763              2.13            
REMARK 500   NH1  ARG A   121     O    HOH A   501              2.13            
REMARK 500   OE1  GLU A   204     O    HOH A   502              2.16            
REMARK 500   O    HOH C   615     O    HOH C   622              2.16            
REMARK 500   OE1  GLU C   204     O    HOH C   401              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   SD   MET D   258     O    HOH A   747     3545     2.08            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG A 181   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG A 200   NE  -  CZ  -  NH1 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP B 241   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ARG C 200   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    ARG C 200   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.4 DEGREES          
REMARK 500    ASP C 241   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG C 290   NE  -  CZ  -  NH1 ANGL. DEV. =   3.4 DEGREES          
REMARK 500    GLY D  26   N   -  CA  -  C   ANGL. DEV. = -17.4 DEGREES          
REMARK 500    VAL D 137   CB  -  CA  -  C   ANGL. DEV. = -15.2 DEGREES          
REMARK 500    ARG D 181   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP D 228   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A  42      153.45    -46.70                                   
REMARK 500    LEU A 113     -179.99     81.95                                   
REMARK 500    LEU A 143      -54.40   -135.82                                   
REMARK 500    SER A 146     -149.93    -87.93                                   
REMARK 500    SER A 188     -115.02     62.78                                   
REMARK 500    CYS A 217       56.14     22.90                                   
REMARK 500    LEU A 239      -54.05     71.22                                   
REMARK 500    CYS A 286       42.06    -98.02                                   
REMARK 500    SER A 306      102.52    -58.60                                   
REMARK 500    PHE A 322       70.78   -119.26                                   
REMARK 500    LEU B  24       88.77    -61.81                                   
REMARK 500    SER B  95     -179.85   -176.56                                   
REMARK 500    LEU B 113      177.59     71.01                                   
REMARK 500    LEU B 143      -61.68   -131.99                                   
REMARK 500    SER B 146     -149.94   -101.87                                   
REMARK 500    SER B 188     -124.79     66.09                                   
REMARK 500    CYS B 217       53.26     30.94                                   
REMARK 500    LEU B 239      -55.47     74.58                                   
REMARK 500    CYS B 286       46.32   -100.97                                   
REMARK 500    PHE B 322       69.64   -117.90                                   
REMARK 500    LEU C 113      178.77     83.72                                   
REMARK 500    LEU C 143      -62.17   -127.28                                   
REMARK 500    SER C 146     -151.16    -74.10                                   
REMARK 500    SER C 188     -116.67     61.32                                   
REMARK 500    CYS C 217       57.29     24.97                                   
REMARK 500    THR C 233      -61.45    -96.00                                   
REMARK 500    LEU C 239      -55.42     64.34                                   
REMARK 500    CYS C 286       47.32    -98.97                                   
REMARK 500    ILE D   5      -69.59    123.71                                   
REMARK 500    LEU D 113      176.46     77.11                                   
REMARK 500    LEU D 143      -62.07   -127.31                                   
REMARK 500    SER D 146     -153.78    -83.64                                   
REMARK 500    SER D 188     -117.88     59.60                                   
REMARK 500    ASP D 208      -45.19    -17.44                                   
REMARK 500    CYS D 217       57.63     22.97                                   
REMARK 500    LEU D 239      -42.95     68.26                                   
REMARK 500    CYS D 286       52.42   -100.28                                   
REMARK 500    PHE D 322       70.04   -111.48                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLY B   26     GLY B   27                 -145.57                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 682        DISTANCE =  5.81 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue GOL A 401                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue TRS A 402                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 5HC0   RELATED DB: PDB                                   
REMARK 900 5HC0 CONTAINS THE SAME PROTEIN COMPLEXED WITH THE LIGAND P-          
REMARK 900 NITROPHENOL.                                                         
REMARK 900 RELATED ID: 5HC2   RELATED DB: PDB                                   
REMARK 900 5HC2 CONTAINS THE SAME PROTEIN COMPLEXED WITH THE LIGAND P-          
REMARK 900 NITROPHENOL. AT THE SAME TIME, IT HAVE A MUTATION SER188ALA.         
REMARK 900 RELATED ID: 5HC3   RELATED DB: PDB                                   
REMARK 900 5HC3 CONTAINS THE SAME PROTEIN AND HAVE A MUTATION SER170ALA.        
REMARK 900 RELATED ID: 5HC5   RELATED DB: PDB                                   
DBREF  5HC4 A    1   344  UNP    H6BDX1   H6BDX1_9BACT     1    344             
DBREF  5HC4 B    1   344  UNP    H6BDX1   H6BDX1_9BACT     1    344             
DBREF  5HC4 C    1   344  UNP    H6BDX1   H6BDX1_9BACT     1    344             
DBREF  5HC4 D    1   344  UNP    H6BDX1   H6BDX1_9BACT     1    344             
SEQADV 5HC4 MET A  -20  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY A  -19  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER A  -18  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER A  -17  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -16  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -15  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -14  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -13  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -12  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -11  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A  -10  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER A   -9  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER A   -8  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY A   -7  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 LEU A   -6  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 VAL A   -5  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 PRO A   -4  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 ARG A   -3  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY A   -2  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER A   -1  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS A    0  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 MET B  -20  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY B  -19  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER B  -18  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER B  -17  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -16  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -15  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -14  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -13  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -12  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -11  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B  -10  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER B   -9  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER B   -8  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY B   -7  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 LEU B   -6  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 VAL B   -5  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 PRO B   -4  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 ARG B   -3  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY B   -2  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER B   -1  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS B    0  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 MET C  -20  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY C  -19  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER C  -18  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER C  -17  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -16  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -15  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -14  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -13  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -12  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -11  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C  -10  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER C   -9  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER C   -8  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY C   -7  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 LEU C   -6  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 VAL C   -5  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 PRO C   -4  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 ARG C   -3  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY C   -2  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER C   -1  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS C    0  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 MET D  -20  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY D  -19  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER D  -18  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER D  -17  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -16  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -15  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -14  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -13  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -12  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -11  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D  -10  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER D   -9  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER D   -8  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY D   -7  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 LEU D   -6  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 VAL D   -5  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 PRO D   -4  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 ARG D   -3  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 GLY D   -2  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 SER D   -1  UNP  H6BDX1              EXPRESSION TAG                 
SEQADV 5HC4 HIS D    0  UNP  H6BDX1              EXPRESSION TAG                 
SEQRES   1 A  365  MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER          
SEQRES   2 A  365  GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE          
SEQRES   3 A  365  ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE          
SEQRES   4 A  365  PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU          
SEQRES   5 A  365  SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU          
SEQRES   6 A  365  ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP          
SEQRES   7 A  365  ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU          
SEQRES   8 A  365  LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY          
SEQRES   9 A  365  ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR          
SEQRES  10 A  365  ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY          
SEQRES  11 A  365  MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA          
SEQRES  12 A  365  TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA          
SEQRES  13 A  365  MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU          
SEQRES  14 A  365  PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS          
SEQRES  15 A  365  VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU          
SEQRES  16 A  365  LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU          
SEQRES  17 A  365  SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG          
SEQRES  18 A  365  LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU          
SEQRES  19 A  365  TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER          
SEQRES  20 A  365  GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU          
SEQRES  21 A  365  LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY          
SEQRES  22 A  365  ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO          
SEQRES  23 A  365  GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO          
SEQRES  24 A  365  THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP          
SEQRES  25 A  365  GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY          
SEQRES  26 A  365  VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS          
SEQRES  27 A  365  GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER          
SEQRES  28 A  365  ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY          
SEQRES  29 A  365  GLY                                                          
SEQRES   1 B  365  MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER          
SEQRES   2 B  365  GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE          
SEQRES   3 B  365  ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE          
SEQRES   4 B  365  PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU          
SEQRES   5 B  365  SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU          
SEQRES   6 B  365  ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP          
SEQRES   7 B  365  ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU          
SEQRES   8 B  365  LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY          
SEQRES   9 B  365  ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR          
SEQRES  10 B  365  ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY          
SEQRES  11 B  365  MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA          
SEQRES  12 B  365  TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA          
SEQRES  13 B  365  MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU          
SEQRES  14 B  365  PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS          
SEQRES  15 B  365  VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU          
SEQRES  16 B  365  LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU          
SEQRES  17 B  365  SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG          
SEQRES  18 B  365  LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU          
SEQRES  19 B  365  TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER          
SEQRES  20 B  365  GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU          
SEQRES  21 B  365  LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY          
SEQRES  22 B  365  ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO          
SEQRES  23 B  365  GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO          
SEQRES  24 B  365  THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP          
SEQRES  25 B  365  GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY          
SEQRES  26 B  365  VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS          
SEQRES  27 B  365  GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER          
SEQRES  28 B  365  ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY          
SEQRES  29 B  365  GLY                                                          
SEQRES   1 C  365  MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER          
SEQRES   2 C  365  GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE          
SEQRES   3 C  365  ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE          
SEQRES   4 C  365  PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU          
SEQRES   5 C  365  SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU          
SEQRES   6 C  365  ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP          
SEQRES   7 C  365  ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU          
SEQRES   8 C  365  LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY          
SEQRES   9 C  365  ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR          
SEQRES  10 C  365  ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY          
SEQRES  11 C  365  MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA          
SEQRES  12 C  365  TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA          
SEQRES  13 C  365  MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU          
SEQRES  14 C  365  PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS          
SEQRES  15 C  365  VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU          
SEQRES  16 C  365  LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU          
SEQRES  17 C  365  SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG          
SEQRES  18 C  365  LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU          
SEQRES  19 C  365  TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER          
SEQRES  20 C  365  GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU          
SEQRES  21 C  365  LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY          
SEQRES  22 C  365  ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO          
SEQRES  23 C  365  GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO          
SEQRES  24 C  365  THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP          
SEQRES  25 C  365  GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY          
SEQRES  26 C  365  VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS          
SEQRES  27 C  365  GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER          
SEQRES  28 C  365  ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY          
SEQRES  29 C  365  GLY                                                          
SEQRES   1 D  365  MET GLY SER SER HIS HIS HIS HIS HIS HIS HIS SER SER          
SEQRES   2 D  365  GLY LEU VAL PRO ARG GLY SER HIS MET THR ASN LYS ILE          
SEQRES   3 D  365  ALA GLU ASP PRO ARG ILE ASP PRO ARG ILE LYS ALA ILE          
SEQRES   4 D  365  PHE SER GLY MET ASP LEU GLY GLY GLY GLY ASP VAL GLU          
SEQRES   5 D  365  SER ARG GLU ALA MET LEU GLU ALA ALA SER SER GLU GLU          
SEQRES   6 D  365  ALA THR ALA VAL ARG ASP GLY LEU ARG VAL PHE LEU ASP          
SEQRES   7 D  365  ALA CYS ASP ASN GLU GLU ILE ALA PRO SER ALA GLY LEU          
SEQRES   8 D  365  LYS ILE GLU ASP TYR GLU PHE THR SER GLU PRO ASP GLY          
SEQRES   9 D  365  ASN ILE ALA LYS ILE GLN TYR ILE ARG PRO ASP SER THR          
SEQRES  10 D  365  ASP LYS LEU PRO CYS VAL TYR TYR ILE HIS GLY GLY GLY          
SEQRES  11 D  365  MET GLN SER LEU SER CYS TYR TYR GLY ASN TYR ARG ALA          
SEQRES  12 D  365  TRP GLY LYS ILE ILE ALA SER ASN GLY VAL ALA VAL ALA          
SEQRES  13 D  365  MET VAL GLU PHE ARG ASN ALA LEU VAL PRO SER ALA LEU          
SEQRES  14 D  365  PRO GLU VAL ALA PRO TYR PRO ALA GLY LEU ASN ASP CYS          
SEQRES  15 D  365  VAL SER GLY VAL LYS TRP VAL ALA SER HIS ALA ASP GLU          
SEQRES  16 D  365  LEU GLY ILE ASP ALA SER ARG ILE ILE ILE ALA GLY GLU          
SEQRES  17 D  365  SER GLY GLY GLY ASN LEU THR LEU ALA ALA GLY LEU ARG          
SEQRES  18 D  365  LEU LYS GLN GLU GLY SER GLN ASP LEU ILE GLN GLY LEU          
SEQRES  19 D  365  TYR ALA LEU CYS PRO TYR ILE ALA GLY SER TRP PRO SER          
SEQRES  20 D  365  GLU ASP SER PRO SER SER THR GLU ASN ASN GLY ILE LEU          
SEQRES  21 D  365  LEU ASP LEU HIS ASN ASN GLN GLY ALA MET GLY TYR GLY          
SEQRES  22 D  365  ILE GLU ALA TYR GLU MET ARG ASP PRO LEU ALA TRP PRO          
SEQRES  23 D  365  GLY PHE ALA THR GLU GLU ASP VAL SER GLY LEU VAL PRO          
SEQRES  24 D  365  THR PHE ILE SER VAL ASN GLU CYS ASP PRO LEU ARG ASP          
SEQRES  25 D  365  GLU GLY ILE ASN PHE TYR ARG LEU LEU LEU ARG ALA GLY          
SEQRES  26 D  365  VAL SER ALA LYS CYS ARG GLN VAL MET GLY THR ILE HIS          
SEQRES  27 D  365  GLY THR GLU ILE PHE PRO ILE ALA CYS PRO ASP VAL SER          
SEQRES  28 D  365  ARG ASP THR ALA ALA SER ILE ALA ASN PHE CYS LYS GLY          
SEQRES  29 D  365  GLY                                                          
HET    GOL  A 401       6                                                       
HET    TRS  A 402       8                                                       
HETNAM     GOL GLYCEROL                                                         
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   5  GOL    C3 H8 O3                                                     
FORMUL   6  TRS    C4 H12 N O3 1+                                               
FORMUL   7  HOH   *1131(H2 O)                                                   
HELIX    1 AA1 ASP A   12  SER A   20  1                                   9    
HELIX    2 AA2 SER A   32  SER A   41  1                                  10    
HELIX    3 AA3 SER A   42  ALA A   58  1                                  17    
HELIX    4 AA4 TYR A  117  SER A  129  1                                  13    
HELIX    5 AA5 PRO A  155  HIS A  171  1                                  17    
HELIX    6 AA6 HIS A  171  GLY A  176  1                                   6    
HELIX    7 AA7 SER A  188  GLY A  205  1                                  18    
HELIX    8 AA8 SER A  206  ILE A  210  5                                   5    
HELIX    9 AA9 PRO A  230  ASN A  235  1                                   6    
HELIX   10 AB1 ASN A  245  MET A  258  1                                  14    
HELIX   11 AB2 TRP A  264  ALA A  268  5                                   5    
HELIX   12 AB3 THR A  269  SER A  274  1                                   6    
HELIX   13 AB4 LEU A  289  ALA A  303  1                                  15    
HELIX   14 AB5 GLY A  318  PHE A  322  5                                   5    
HELIX   15 AB6 CYS A  326  GLY A  344  1                                  19    
HELIX   16 AB7 LYS B    4  ASP B    8  5                                   5    
HELIX   17 AB8 ASP B   12  SER B   20  1                                   9    
HELIX   18 AB9 SER B   32  SER B   41  1                                  10    
HELIX   19 AC1 SER B   42  CYS B   59  1                                  18    
HELIX   20 AC2 TYR B  117  SER B  129  1                                  13    
HELIX   21 AC3 PRO B  155  HIS B  171  1                                  17    
HELIX   22 AC4 HIS B  171  GLY B  176  1                                   6    
HELIX   23 AC5 SER B  188  GLU B  204  1                                  17    
HELIX   24 AC6 SER B  206  ILE B  210  5                                   5    
HELIX   25 AC7 SER B  229  ASN B  235  1                                   7    
HELIX   26 AC8 ASN B  245  MET B  258  1                                  14    
HELIX   27 AC9 TRP B  264  ALA B  268  5                                   5    
HELIX   28 AD1 THR B  269  SER B  274  1                                   6    
HELIX   29 AD2 LEU B  289  GLY B  304  1                                  16    
HELIX   30 AD3 GLY B  318  PHE B  322  5                                   5    
HELIX   31 AD4 CYS B  326  GLY B  343  1                                  18    
HELIX   32 AD5 LYS C    4  ASP C    8  1                                   5    
HELIX   33 AD6 ASP C   12  SER C   20  1                                   9    
HELIX   34 AD7 SER C   32  SER C   41  1                                  10    
HELIX   35 AD8 SER C   42  ALA C   58  1                                  17    
HELIX   36 AD9 TYR C  117  SER C  129  1                                  13    
HELIX   37 AE1 PRO C  155  HIS C  171  1                                  17    
HELIX   38 AE2 HIS C  171  GLY C  176  1                                   6    
HELIX   39 AE3 SER C  188  GLU C  204  1                                  17    
HELIX   40 AE4 SER C  206  ILE C  210  5                                   5    
HELIX   41 AE5 SER C  229  ASN C  235  1                                   7    
HELIX   42 AE6 ASN C  245  MET C  258  1                                  14    
HELIX   43 AE7 TRP C  264  ALA C  268  5                                   5    
HELIX   44 AE8 THR C  269  SER C  274  1                                   6    
HELIX   45 AE9 LEU C  289  ALA C  303  1                                  15    
HELIX   46 AF1 GLY C  318  PHE C  322  5                                   5    
HELIX   47 AF2 CYS C  326  GLY C  343  1                                  18    
HELIX   48 AF3 ASP D   12  SER D   20  1                                   9    
HELIX   49 AF4 SER D   32  SER D   42  1                                  11    
HELIX   50 AF5 SER D   42  CYS D   59  1                                  18    
HELIX   51 AF6 TYR D  117  SER D  129  1                                  13    
HELIX   52 AF7 PRO D  155  HIS D  171  1                                  17    
HELIX   53 AF8 SER D  188  GLU D  204  1                                  17    
HELIX   54 AF9 SER D  206  ILE D  210  5                                   5    
HELIX   55 AG1 PRO D  230  ASN D  235  1                                   6    
HELIX   56 AG2 ASN D  245  MET D  258  1                                  14    
HELIX   57 AG3 TRP D  264  ALA D  268  5                                   5    
HELIX   58 AG4 THR D  269  SER D  274  1                                   6    
HELIX   59 AG5 LEU D  289  ALA D  303  1                                  15    
HELIX   60 AG6 GLY D  318  PHE D  322  5                                   5    
HELIX   61 AG7 CYS D  326  GLY D  344  1                                  19    
SHEET    1 AA116 LEU A  70  THR A  78  0                                        
SHEET    2 AA116 ILE A  85  PRO A  93 -1  O  TYR A  90   N  GLU A  73           
SHEET    3 AA116 ALA A 133  GLU A 138 -1  O  MET A 136   N  GLN A  89           
SHEET    4 AA116 LEU A  99  ILE A 105  1  N  VAL A 102   O  ALA A 133           
SHEET    5 AA116 ILE A 177  GLU A 187  1  O  ILE A 183   N  TYR A 103           
SHEET    6 AA116 GLY A 212  LEU A 216  1  O  LEU A 216   N  GLY A 186           
SHEET    7 AA116 THR A 279  ASN A 284  1  O  PHE A 280   N  LEU A 213           
SHEET    8 AA116 ALA A 307  MET A 313  1  O  VAL A 312   N  VAL A 283           
SHEET    9 AA116 ALA B 307  VAL B 312 -1  O  GLN B 311   N  GLN A 311           
SHEET   10 AA116 THR B 279  ASN B 284  1  N  VAL B 283   O  VAL B 312           
SHEET   11 AA116 GLY B 212  LEU B 216  1  N  LEU B 213   O  PHE B 280           
SHEET   12 AA116 ILE B 177  GLU B 187  1  N  ILE B 184   O  TYR B 214           
SHEET   13 AA116 LEU B  99  ILE B 105  1  N  TYR B 103   O  ILE B 183           
SHEET   14 AA116 ALA B 133  GLU B 138  1  O  ALA B 133   N  VAL B 102           
SHEET   15 AA116 ILE B  85  PRO B  93 -1  N  LYS B  87   O  GLU B 138           
SHEET   16 AA116 LEU B  70  THR B  78 -1  N  GLU B  73   O  TYR B  90           
SHEET    1 AA216 LEU C  70  THR C  78  0                                        
SHEET    2 AA216 ILE C  85  PRO C  93 -1  O  ALA C  86   N  PHE C  77           
SHEET    3 AA216 ALA C 133  GLU C 138 -1  O  VAL C 134   N  ILE C  91           
SHEET    4 AA216 LEU C  99  ILE C 105  1  N  VAL C 102   O  ALA C 133           
SHEET    5 AA216 ILE C 177  GLU C 187  1  O  ALA C 185   N  TYR C 103           
SHEET    6 AA216 GLY C 212  LEU C 216  1  O  LEU C 216   N  GLY C 186           
SHEET    7 AA216 THR C 279  CYS C 286  1  O  PHE C 280   N  LEU C 213           
SHEET    8 AA216 ALA C 307  ILE C 316  1  O  VAL C 312   N  VAL C 283           
SHEET    9 AA216 ALA D 307  ILE D 316 -1  O  GLN D 311   N  GLN C 311           
SHEET   10 AA216 THR D 279  CYS D 286  1  N  VAL D 283   O  VAL D 312           
SHEET   11 AA216 GLY D 212  LEU D 216  1  N  LEU D 213   O  PHE D 280           
SHEET   12 AA216 ILE D 177  GLU D 187  1  N  GLY D 186   O  LEU D 216           
SHEET   13 AA216 LEU D  99  ILE D 105  1  N  TYR D 103   O  ILE D 183           
SHEET   14 AA216 ALA D 133  GLU D 138  1  O  ALA D 133   N  VAL D 102           
SHEET   15 AA216 ILE D  85  PRO D  93 -1  N  LYS D  87   O  GLU D 138           
SHEET   16 AA216 LEU D  70  THR D  78 -1  N  PHE D  77   O  ALA D  86           
CISPEP   1 GLU A   80    PRO A   81          0        13.05                     
CISPEP   2 TYR A  154    PRO A  155          0         7.11                     
CISPEP   3 TRP A  224    PRO A  225          0        -0.87                     
CISPEP   4 GLY A  343    GLY A  344          0        -3.28                     
CISPEP   5 GLU B   80    PRO B   81          0         0.59                     
CISPEP   6 TYR B  154    PRO B  155          0         7.82                     
CISPEP   7 TRP B  224    PRO B  225          0         3.28                     
CISPEP   8 GLU C   80    PRO C   81          0         4.54                     
CISPEP   9 TYR C  154    PRO C  155          0         4.42                     
CISPEP  10 TRP C  224    PRO C  225          0        -2.98                     
CISPEP  11 GLY C  343    GLY C  344          0       -12.12                     
CISPEP  12 GLY D   25    GLY D   26          0        -6.94                     
CISPEP  13 GLU D   80    PRO D   81          0         3.09                     
CISPEP  14 TYR D  154    PRO D  155          0         7.65                     
CISPEP  15 TRP D  224    PRO D  225          0        -1.77                     
SITE     1 AC1  7 ARG A  49  LEU A  52  ARG A  53  SER A 112                    
SITE     2 AC1  7 LEU A 113  TYR A 117  VAL A 144                               
SITE     1 AC2  9 GLY A 108  GLY A 109  TYR A 120  GLU A 187                    
SITE     2 AC2  9 SER A 188  GLY A 189  HIS A 317  ILE A 321                    
SITE     3 AC2  9 HOH A 660                                                     
CRYST1   81.243  121.811  150.522  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012309  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.008209  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006644        0.00000                         
TER    2550      GLY A 344                                                      
TER    5100      GLY B 344                                                      
TER    7638      GLY C 344                                                      
TER   10192      GLY D 344                                                      
MASTER      529    0    2   61   32    0    5    611328    4   14  116          
END                                                                             

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Mail to: Nicolas Lenfant, Thierry Hotelier, Yves Bourne, Pascale Marchot and Arnaud Chatonnet.
Please cite: Lenfant 2013 Nucleic.Acids.Res. or Marchot Chatonnet 2012 Prot.Pept Lett.
For technical information about these pages see:
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