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LongText Report for: 2OG1-pdb

Name Class
2OG1-pdb
HEADER    HYDROLASE                               04-JAN-07   2OG1              
TITLE     CRYSTAL STRUCTURE OF BPHD, A C-C HYDROLASE FROM                       
TITLE    2 BURKHOLDERIA XENOVORANS LB400                                        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 2-HYDROXY-6-OXO-6-PHENYLHEXA-2,4-DIENOATE                  
COMPND   3 HYDROLASE;                                                           
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 EC: 3.7.1.8;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA XENOVORANS;                        
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 STRAIN: LB400;                                                       
SOURCE   5 GENE: BPHD;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_COMMON: BACTERIA;                                  
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DH5ALPHA;                                  
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PSS314                                    
KEYWDS    BPHD, ALPHA/BETA HYDROLASE, PCB DEGRADATION, META CLEAVAGE            
KEYWDS   2 PRODUCT HYDROLASE, MCP HYDROLASE, 2-HYDROXY-6-OXO-6-                 
KEYWDS   3 PHENYLHEXA-2,4-DIENOATE HYDROLASE                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.DAI,J.KE,J.T.BOLIN                                                  
REVDAT   1   16-JAN-07 2OG1    0                                                
JRNL        AUTH   G.P.HORSMAN,J.KE,S.DAI,S.Y.SEAH,J.T.BOLIN,L.D.ELTIS          
JRNL        TITL   KINETIC AND STRUCTURAL INSIGHT INTO THE MECHANISM            
JRNL        TITL 2 OF BPHD, A C-C BOND HYDROLASE FROM THE BIPHENYL              
JRNL        TITL 3 DEGRADATION PATHWAY                                          
JRNL        REF    BIOCHEMISTRY                  V.  45 11071 2006              
JRNL        REFN   ASTM BICHAW  US ISSN 0006-2960                               
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.60 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.87                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2428265.500                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 96.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 88125                          
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 SET) : 0.208                           
REMARK   3   FREE R VALUE                     : 0.224                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 8856                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.002                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 81.50                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 11071                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2690                       
REMARK   3   BIN FREE R VALUE                    : 0.2920                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 10.20                        
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 1262                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.008                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4532                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 35                                      
REMARK   3   SOLVENT ATOMS            : 469                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 27.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.32000                                              
REMARK   3    B22 (A**2) : 0.32000                                              
REMARK   3    B33 (A**2) : -0.64000                                             
REMARK   3    B12 (A**2) : 1.25000                                              
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) : 0.20                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.15                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.22                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.16                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.20                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.70                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 1.120 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.770 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.760 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.720 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.34                                                 
REMARK   3   BSOL        : 50.25                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : LIGAND.PAR                                     
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : LIGAND.TOP                                     
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2OG1 COMPLIES WITH FORMAT V. 2.3, 09-JULY-1998                       
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-2007.                
REMARK 100 THE RCSB ID CODE IS RCSB041089.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-SEP-1998; 05-DEC-1998           
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 8.20                               
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; APS                           
REMARK 200  BEAMLINE                       : 14-BM-D; 14-BM-D                   
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795; 0.9537,0.9793,0.9795       
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 1; ADSC QUANTUM 1     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 88125                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
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     (%) : 96.6                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : 0.06000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 9.9000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.63                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; MAD                         
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.90                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.75                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2.0-2.4 M AMMONIUM SULFATE, 6-10%        
REMARK 280  ETHANOL, 0.1M TRIS-HCL, PH 8.2, VAPOR DIFFUSION, HANGING DROP,      
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,1/3+Z                                            
REMARK 290       3555   -X+Y,-X,2/3+Z                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,1/3+Z                                            
REMARK 290       6555   X-Y,X,2/3+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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       22.24167            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       44.48333            
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  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       22.24167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       44.48333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 THIS ENTRY CONTAINS THE CRYSTALLOGRAPHIC ASYMMETRIC UNIT             
REMARK 300 WHICH CONSISTS OF 2 CHAIN(S). SEE REMARK 350 FOR                     
REMARK 300 INFORMATION ON GENERATING THE BIOLOGICAL MOLECULE(S).                
REMARK 350                                                                      
REMARK 350 GENERATING THE BIOMOLECULE                                           
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 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   BIOMT1   2 -1.000000  0.000000  0.000000       67.50000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000      116.91343            
REMARK 350   BIOMT3   2  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     1                                                      
REMARK 465     MET B     1                                                      
REMARK 465     THR B     2                                                      
REMARK 465     ALA B     3                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),F6.3)                  
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    TYR A  52   CD1   TYR A  52   CE1    0.030                        
REMARK 500    MET A 171   SD    MET A 171   CE     0.031                        
REMARK 500    ARG A 190   CB    ARG A 190   CG    -0.030                        
REMARK 500    MET B  98   SD    MET B  98   CE    -0.044                        
REMARK 500    MET B 135   SD    MET B 135   CE    -0.031                        
REMARK 500    MET B 135   SD    MET B 135   CE    -0.043                        
REMARK 500    PRO B 163   CG    PRO B 163   CD     0.034                        
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: ENGH AND HUBER, 1991                                
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    GLY A  42   N   -  CA  -  C   ANGL. DEV. =  7.1 DEGREES           
REMARK 500    TYR A  52   N   -  CA  -  C   ANGL. DEV. = 10.5 DEGREES           
REMARK 500    ARG A  65   N   -  CA  -  C   ANGL. DEV. =-10.8 DEGREES           
REMARK 500    LEU A  68   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    ASP A  70   N   -  CA  -  C   ANGL. DEV. = -7.4 DEGREES           
REMARK 500    VAL A  81   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES           
REMARK 500    HIS A 107   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    VAL A 109   N   -  CA  -  C   ANGL. DEV. = -8.7 DEGREES           
REMARK 500    GLY A 130   N   -  CA  -  C   ANGL. DEV. = -7.6 DEGREES           
REMARK 500    TYR A 177   N   -  CA  -  C   ANGL. DEV. = -7.9 DEGREES           
REMARK 500    LYS A 228   N   -  CA  -  C   ANGL. DEV. = -7.5 DEGREES           
REMARK 500    PRO A 241   N   -  CA  -  C   ANGL. DEV. =  9.4 DEGREES           
REMARK 500    HIS A 285   N   -  CA  -  C   ANGL. DEV. =  9.1 DEGREES           
REMARK 500    GLY B 234   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    HIS B 285   N   -  CA  -  C   ANGL. DEV. =  7.5 DEGREES           
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  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER A 112     -114.13     52.85                                   
REMARK 500    SER B 112     -113.24     50.64                                   
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525 THE FOLLOWING SOLVENT MOLECULES LIE FARTHER THAN EXPECTED            
REMARK 525 FROM THE PROTEIN OR NUCLEIC ACID MOLECULE AND MAY BE                 
REMARK 525 ASSOCIATED WITH A SYMMETRY RELATED MOLECULE (M=MODEL                 
REMARK 525 NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE          
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH   252        DISTANCE =  6.16 ANGSTROMS                       
REMARK 525    HOH   266        DISTANCE =  6.54 ANGSTROMS                       
REMARK 525    HOH   291        DISTANCE =  5.88 ANGSTROMS                       
REMARK 525    HOH   343        DISTANCE =  5.23 ANGSTROMS                       
DBREF  2OG1 A    1   286  UNP    P47229   BPHD_BURXL       1    286             
DBREF  2OG1 B    1   286  UNP    P47229   BPHD_BURXL       1    286             
SEQRES   1 A  286  MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL          
SEQRES   2 A  286  LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS          
SEQRES   3 A  286  TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU          
SEQRES   4 A  286  HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR          
SEQRES   5 A  286  TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG          
SEQRES   6 A  286  VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP          
SEQRES   7 A  286  ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA          
SEQRES   8 A  286  ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP          
SEQRES   9 A  286  ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR          
SEQRES  10 A  286  ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY          
SEQRES  11 A  286  LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER          
SEQRES  12 A  286  MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU          
SEQRES  13 A  286  PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS          
SEQRES  14 A  286  GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE          
SEQRES  15 A  286  THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN          
SEQRES  16 A  286  ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA          
SEQRES  17 A  286  GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG          
SEQRES  18 A  286  LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY          
SEQRES  19 A  286  ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS          
SEQRES  20 A  286  LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE          
SEQRES  21 A  286  SER LYS CYS GLY HIS TRP ALA GLN TRP GLU HIS ALA ASP          
SEQRES  22 A  286  GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA          
SEQRES   1 B  286  MET THR ALA LEU THR GLU SER SER THR SER LYS PHE VAL          
SEQRES   2 B  286  LYS ILE ASN GLU LYS GLY PHE SER ASP PHE ASN ILE HIS          
SEQRES   3 B  286  TYR ASN GLU ALA GLY ASN GLY GLU THR VAL ILE MET LEU          
SEQRES   4 B  286  HIS GLY GLY GLY PRO GLY ALA GLY GLY TRP SER ASN TYR          
SEQRES   5 B  286  TYR ARG ASN VAL GLY PRO PHE VAL ASP ALA GLY TYR ARG          
SEQRES   6 B  286  VAL ILE LEU LYS ASP SER PRO GLY PHE ASN LYS SER ASP          
SEQRES   7 B  286  ALA VAL VAL MET ASP GLU GLN ARG GLY LEU VAL ASN ALA          
SEQRES   8 B  286  ARG ALA VAL LYS GLY LEU MET ASP ALA LEU ASP ILE ASP          
SEQRES   9 B  286  ARG ALA HIS LEU VAL GLY ASN SER MET GLY GLY ALA THR          
SEQRES  10 B  286  ALA LEU ASN PHE ALA LEU GLU TYR PRO ASP ARG ILE GLY          
SEQRES  11 B  286  LYS LEU ILE LEU MET GLY PRO GLY GLY LEU GLY PRO SER          
SEQRES  12 B  286  MET PHE ALA PRO MET PRO MET GLU GLY ILE LYS LEU LEU          
SEQRES  13 B  286  PHE LYS LEU TYR ALA GLU PRO SER TYR GLU THR LEU LYS          
SEQRES  14 B  286  GLN MET LEU GLN VAL PHE LEU TYR ASP GLN SER LEU ILE          
SEQRES  15 B  286  THR GLU GLU LEU LEU GLN GLY ARG TRP GLU ALA ILE GLN          
SEQRES  16 B  286  ARG GLN PRO GLU HIS LEU LYS ASN PHE LEU ILE SER ALA          
SEQRES  17 B  286  GLN LYS ALA PRO LEU SER THR TRP ASP VAL THR ALA ARG          
SEQRES  18 B  286  LEU GLY GLU ILE LYS ALA LYS THR PHE ILE THR TRP GLY          
SEQRES  19 B  286  ARG ASP ASP ARG PHE VAL PRO LEU ASP HIS GLY LEU LYS          
SEQRES  20 B  286  LEU LEU TRP ASN ILE ASP ASP ALA ARG LEU HIS VAL PHE          
SEQRES  21 B  286  SER LYS CYS GLY HIS TRP ALA GLN TRP GLU HIS ALA ASP          
SEQRES  22 B  286  GLU PHE ASN ARG LEU VAL ILE ASP PHE LEU ARG HIS ALA          
HET    SO4    501       5                                                       
HET    SO4    502       5                                                       
HET    SO4    503       5                                                       
HET    SO4    504       5                                                       
HET    GOL    601       6                                                       
HET    EOH    701       3                                                       
HET    EOH    702       3                                                       
HET    EOH    703       3                                                       
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     EOH ETHANOL                                                          
FORMUL   3  SO4    4(O4 S1 2-)                                                  
FORMUL   7  GOL    C3 H8 O3                                                     
FORMUL   8  EOH    3(C2 H6 O1)                                                  
FORMUL  11  HOH   *469(H2 O1)                                                   
HELIX    1   1 THR A    5  THR A    9  1                                   5    
HELIX    2   2 GLY A   47  TYR A   53  1                                   7    
HELIX    3   3 ASN A   55  ALA A   62  1                                   8    
HELIX    4   4 GLN A   85  LEU A  101  1                                  17    
HELIX    5   5 SER A  112  TYR A  125  1                                  14    
HELIX    6   6 MET A  150  GLU A  162  1                                  13    
HELIX    7   7 SER A  164  PHE A  175  1                                  12    
HELIX    8   8 ASP A  178  ILE A  182  5                                   5    
HELIX    9   9 THR A  183  GLN A  197  1                                  15    
HELIX   10  10 GLN A  197  ALA A  211  1                                  15    
HELIX   11  11 PRO A  212  ASP A  217  5                                   6    
HELIX   12  12 VAL A  218  ILE A  225  5                                   8    
HELIX   13  13 LEU A  242  ILE A  252  1                                  11    
HELIX   14  14 TRP A  266  HIS A  271  1                                   6    
HELIX   15  15 HIS A  271  ALA A  286  1                                  16    
HELIX   16  16 THR B    5  THR B    9  1                                   5    
HELIX   17  17 GLY B   47  TYR B   53  1                                   7    
HELIX   18  18 ASN B   55  ALA B   62  1                                   8    
HELIX   19  19 GLN B   85  LEU B  101  1                                  17    
HELIX   20  20 SER B  112  TYR B  125  1                                  14    
HELIX   21  21 MET B  150  GLU B  162  1                                  13    
HELIX   22  22 SER B  164  LEU B  176  1                                  13    
HELIX   23  23 ASP B  178  ILE B  182  5                                   5    
HELIX   24  24 THR B  183  GLN B  197  1                                  15    
HELIX   25  25 GLN B  197  ALA B  211  1                                  15    
HELIX   26  26 PRO B  212  TRP B  216  5                                   5    
HELIX   27  27 VAL B  218  ILE B  225  5                                   8    
HELIX   28  28 LEU B  242  ILE B  252  1                                  11    
HELIX   29  29 TRP B  266  HIS B  271  1                                   6    
HELIX   30  30 HIS B  271  ALA B  286  1                                  16    
SHEET    1   A16 SER A  10  GLU A  17  0                                        
SHEET    2   A16 PHE A  20  ALA A  30 -1  O  TYR A  27   N  LYS A  11           
SHEET    3   A16 TYR A  64  LYS A  69 -1  O  VAL A  66   N  ALA A  30           
SHEET    4   A16 GLU A  34  LEU A  39  1  N  MET A  38   O  ILE A  67           
SHEET    5   A16 ALA A 106  ASN A 111  1  O  VAL A 109   N  LEU A  39           
SHEET    6   A16 ILE A 129  MET A 135  1  O  ILE A 133   N  LEU A 108           
SHEET    7   A16 THR A 229  GLY A 234  1  O  THR A 232   N  LEU A 134           
SHEET    8   A16 ALA A 255  PHE A 260  1  O  ARG A 256   N  ILE A 231           
SHEET    9   A16 ALA B 255  PHE B 260 -1  O  VAL B 259   N  LEU A 257           
SHEET   10   A16 THR B 229  GLY B 234  1  N  ILE B 231   O  ARG B 256           
SHEET   11   A16 ILE B 129  MET B 135  1  N  LEU B 134   O  THR B 232           
SHEET   12   A16 ALA B 106  ASN B 111  1  N  ALA B 106   O  GLY B 130           
SHEET   13   A16 GLU B  34  LEU B  39  1  N  LEU B  39   O  VAL B 109           
SHEET   14   A16 TYR B  64  LYS B  69  1  O  ARG B  65   N  GLU B  34           
SHEET   15   A16 PHE B  20  ALA B  30 -1  N  ASN B  28   O  LEU B  68           
SHEET   16   A16 SER B  10  GLU B  17 -1  N  VAL B  13   O  ILE B  25           
CISPEP   1 MET A  148    PRO A  149          0         0.95                     
CISPEP   2 MET B  148    PRO B  149          0         0.09                     
CRYST1  135.000  135.000   66.725  90.00  90.00 120.00 P 64         12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007407  0.004277  0.000000        0.00000                         
SCALE2      0.000000  0.008553  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.014987        0.00000                         
TER    2285      ALA A 286                                                      
TER    4534      ALA B 286                                                      
MASTER      317    0    8   30   16    0    0    6 5036    2   35   44          
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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