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LongText Report for: 6f9o-pdb

Name Class
6f9o-pdb
HEADER    HYDROLASE                               15-DEC-17   6F9O              
TITLE     CRYSTAL STRUCTURE OF COLD-ADAPTED HALOALKANE DEHALOGENASE DPCA FROM   
TITLE    2 PSYCHROBACTER CRYOHALOLENTIS K5                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HALOALKANE DEHALOGENASE;                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.8.1.5;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSYCHROBACTER CRYOHALOLENTIS (STRAIN K5);       
SOURCE   3 ORGANISM_TAXID: 335284;                                              
SOURCE   4 STRAIN: K5;                                                          
SOURCE   5 GENE: DHMA, PCRYO_1253;                                              
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI 'BL21-GOLD(DE3)PLYSS AG';        
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 866768;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: DE3;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET21B                                    
KEYWDS    MICROBIAL ENZYMES, HALOALKANE DEHALOGENASES, HLDS, ALPHA/BETA-        
KEYWDS   2 HYDROLASE FOLD ENZYMES, HYDROLASE, 2 DOMAINS, THE HIGHEST ACTIVITY   
KEYWDS   3 TOWARDS 1-BROMOBUTANE, 1-BROMOHEXANE AND 1, 3-DIBROMOPROPANE         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TRATSIAK,T.PRUDNIKOVA,I.DRIENOVSKA,J.DAMBORSKY,J.BRYNDA,P.PACHL,    
AUTHOR   2 M.KUTY,R.CHALOUPKOVA,I.KUTA SMATANOVA,P.REZACOVA                     
REVDAT   1   27-FEB-19 6F9O    0                                                
JRNL        AUTH   K.TRATSIAK,P.MALOY REZACOVA,R.CHALUPKOVA,I.KUTA SMATANOVA,   
JRNL        AUTH 2 J.DAMBORSKY                                                  
JRNL        TITL   CRYSTAL STRUCTURE OF COLD-ADAPTED HALOALKANE DEHALOGENASE    
JRNL        TITL 2 DPCA FROM PSYCHROBACTER CRYOHALOLENTIS K5                    
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   K.TRATSIAK,O.DEGTJARIK,I.DRIENOVSKA,L.CHRAST,P.REZACOVA,     
REMARK   1  AUTH 2 M.KUTY,R.CHALOUPKOVA,J.DAMBORSKY,I.KUTA SMATANOVA            
REMARK   1  TITL   CRYSTALLOGRAPHIC ANALYSIS OF NEW PSYCHROPHILIC HALOALKANE    
REMARK   1  TITL 2 DEHALOGENASES: DPCA FROM PSYCHROBACTER CRYOHALOLENTIS K5 AND 
REMARK   1  TITL 3 DMXA FROM MARINOBACTER SP. ELB17.                            
REMARK   1  REF    ACTA CRYSTALLOGR. SECT. F     V.  69   683 2013              
REMARK   1  REF  2 STRUCT. BIOL. CRYST. COMMUN.                                 
REMARK   1  REFN                   ESSN 1744-3091                               
REMARK   1  PMID   23722854                                                     
REMARK   1  DOI    10.1107/S1744309113012979                                    
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   I.DRIENOVSKA,E.CHOVANCOVA,T.KOUDELAKOVA,J.DAMBORSKY,         
REMARK   1  AUTH 2 R.CHALOUPKOVA                                                
REMARK   1  TITL   BIOCHEMICAL CHARACTERIZATION OF A NOVEL HALOALKANE           
REMARK   1  TITL 2 DEHALOGENASE FROM A COLD-ADAPTED BACTERIUM.                  
REMARK   1  REF    APPL. ENVIRON. MICROBIOL.     V.  78  4995 2012              
REMARK   1  REFN                   ESSN 1098-5336                               
REMARK   1  PMID   22582053                                                     
REMARK   1  DOI    10.1128/AEM.00485-12                                         
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.05 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0158                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.05                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 92.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 114202                         
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) : 0.111                           
REMARK   3   R VALUE            (WORKING SET) : 0.110                           
REMARK   3   FREE R VALUE                     : 0.132                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 6066                            
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) : 1.05                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4716                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 51.27                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2180                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 244                          
REMARK   3   BIN FREE R VALUE                    : 0.2380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2465                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 28                                      
REMARK   3   SOLVENT ATOMS            : 576                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 16.72                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.67                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.024         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.024         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.013         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.543         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.982                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.976                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2740 ; 0.012 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  2445 ; 0.002 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3748 ; 1.634 ; 1.945       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  5721 ; 1.030 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   352 ; 6.086 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   138 ;33.671 ;24.058       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   442 ;12.244 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    18 ;16.682 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   390 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3156 ; 0.010 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):   570 ; 0.003 ; 0.020       
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):  1324 ; 0.710 ; 0.645       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  1323 ; 0.710 ; 0.645       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1683 ; 1.023 ; 0.978       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  1684 ; 1.022 ; 0.979       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1416 ; 1.083 ; 0.804       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  1416 ; 1.082 ; 0.804       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  2059 ; 1.322 ; 1.147       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3451 ; 2.693 ;10.367       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  3452 ; 2.693 ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  5182 ; 2.273 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):   305 ;22.761 ; 5.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  5399 ; 7.178 ; 5.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 6F9O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 15-DEC-17.                  
REMARK 100 THE DEPOSITION ID IS D_1200007830.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.6-5.9                            
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.2                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.978260                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : SAGITALLY BENDED SI111 CRYSTAL     
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RAYONIX MX-225                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000 VERSION NOVEMBER 1,       
REMARK 200                                   2011                               
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000 VERSION NOVEMBER 1,       
REMARK 200                                   2011                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 120315                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.050                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 92.2                               
REMARK 200  DATA REDUNDANCY                : 5.700                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 39.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.05                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.09                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 56.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.30700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 3.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1B6G                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NEEDLE                                                       
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.63                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2 M AMMONIUM ACETATE, 30%(W/V) PEG     
REMARK 280  4000 AND 0.1 M SODIUM ACETATE TRIHYDRATE PH 4.6 AND WITH THE        
REMARK 280  ADDITION OF 0.6 UL OF 0.1M L-PROLINE (ADDITIVE SCREEN KIT,          
REMARK 280  HAMPTON RESEARCH) TO THE CRYSTALLIZATION DROP, PH 5.88, VAPOR       
REMARK 280  DIFFUSION, HANGING DROP, TEMPERATURE 293K                           
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.72550            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 1120 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 13280 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -28.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1054     O    HOH A  1057              1.51            
REMARK 500   O    HOH A   727     O    HOH A   906              1.60            
REMARK 500   O    HOH A   961     O    HOH A  1054              1.68            
REMARK 500   O    HOH A   781     O    HOH A  1019              2.13            
REMARK 500   OE1  GLN A   173     O    HOH A   502              2.16            
REMARK 500   O    HOH A   522     O    HOH A   861              2.17            
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    ASN A  18       33.00   -144.49                                   
REMARK 500    SER A  29       -4.99     77.94                                   
REMARK 500    SER A  32     -154.59   -141.13                                   
REMARK 500    PRO A  56       57.73    -98.65                                   
REMARK 500    SER A  57     -166.47   -102.09                                   
REMARK 500    ASP A 123     -139.00     56.76                                   
REMARK 500    ASP A 123     -134.04     48.30                                   
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 A1076        DISTANCE =  5.82 ANGSTROMS                       
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     PEG A  405                                                       
REMARK 610     PEG A  406                                                       
REMARK 610     PEG A  407                                                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 408  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN A 261   O                                                      
REMARK 620 2 THR A 267   OG1  64.0                                              
REMARK 620 3 HOH A 727   O    63.5 122.6                                        
REMARK 620 4 HOH A 892   O   154.8 125.9 111.5                                  
REMARK 620 5 HOH A 906   O    80.0 143.5  33.3  84.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CL A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 404                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue PEG A 407                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue NA A 408                  
DBREF  6F9O A    1   303  UNP    Q1QBB9   DHMA_PSYCK       1    303             
SEQADV 6F9O HIS A  304  UNP  Q1QBB9              EXPRESSION TAG                 
SEQADV 6F9O HIS A  305  UNP  Q1QBB9              EXPRESSION TAG                 
SEQADV 6F9O HIS A  306  UNP  Q1QBB9              EXPRESSION TAG                 
SEQADV 6F9O HIS A  307  UNP  Q1QBB9              EXPRESSION TAG                 
SEQADV 6F9O HIS A  308  UNP  Q1QBB9              EXPRESSION TAG                 
SEQADV 6F9O HIS A  309  UNP  Q1QBB9              EXPRESSION TAG                 
SEQRES   1 A  309  MET LYS ILE LEU ARG THR PRO ASP SER ARG PHE ALA ASN          
SEQRES   2 A  309  LEU PRO ASP TYR ASN PHE ASP PRO HIS TYR LEU MET VAL          
SEQRES   3 A  309  ASP ASP SER GLU ASP SER GLU LEU ARG VAL HIS TYR LEU          
SEQRES   4 A  309  ASP GLU GLY PRO ARG ASP ALA ASP PRO VAL LEU LEU LEU          
SEQRES   5 A  309  HIS GLY GLU PRO SER TRP CYS TYR LEU TYR ARG LYS MET          
SEQRES   6 A  309  ILE PRO ILE LEU THR ALA ALA GLY HIS ARG VAL ILE ALA          
SEQRES   7 A  309  PRO ASP LEU PRO GLY PHE GLY ARG SER ASP LYS PRO ALA          
SEQRES   8 A  309  SER ARG THR ASP TYR THR TYR GLN ARG HIS VAL ASN TRP          
SEQRES   9 A  309  MET GLN SER VAL LEU ASP GLN LEU ASP LEU ASN ASN ILE          
SEQRES  10 A  309  THR LEU PHE CYS GLN ASP TRP GLY GLY LEU ILE GLY LEU          
SEQRES  11 A  309  ARG LEU VAL ALA GLU ASN PRO ASP ARG PHE ALA ARG VAL          
SEQRES  12 A  309  ALA ALA GLY ASN THR MET LEU PRO THR GLY ASP HIS ASP          
SEQRES  13 A  309  LEU GLY GLU GLY PHE ARG LYS TRP GLN GLN PHE SER GLN          
SEQRES  14 A  309  GLU ILE PRO GLN PHE HIS VAL GLY GLY THR ILE LYS SER          
SEQRES  15 A  309  GLY THR VAL THR LYS LEU SER GLN ALA VAL ILE ASP ALA          
SEQRES  16 A  309  TYR ASN ALA PRO PHE PRO ASP GLU SER TYR LYS GLU GLY          
SEQRES  17 A  309  ALA ARG GLN PHE PRO LEU LEU VAL PRO SER THR PRO ASP          
SEQRES  18 A  309  ASP PRO ALA SER GLU ASN ASN ARG ALA ALA TRP ILE GLU          
SEQRES  19 A  309  LEU SER LYS TRP THR LYS PRO PHE ILE THR LEU PHE SER          
SEQRES  20 A  309  ASP SER ASP PRO VAL THR ALA GLY GLY ASP ARG ILE MET          
SEQRES  21 A  309  GLN LYS ILE ILE PRO GLY THR LYS GLY GLN ALA HIS THR          
SEQRES  22 A  309  THR ILE ALA ASN GLY GLY HIS PHE LEU GLN GLU ASP GLN          
SEQRES  23 A  309  GLY GLU LYS VAL ALA LYS LEU LEU VAL GLN PHE ILE HIS          
SEQRES  24 A  309  ASP ASN PRO ARG HIS HIS HIS HIS HIS HIS                      
HET     CL  A 401       1                                                       
HET     CL  A 402       1                                                       
HET    PEG  A 403       7                                                       
HET    PEG  A 404       7                                                       
HET    PEG  A 405       4                                                       
HET    PEG  A 406       3                                                       
HET    PEG  A 407       4                                                       
HET     NA  A 408       1                                                       
HETNAM      CL CHLORIDE ION                                                     
HETNAM     PEG DI(HYDROXYETHYL)ETHER                                            
HETNAM      NA SODIUM ION                                                       
FORMUL   2   CL    2(CL 1-)                                                     
FORMUL   4  PEG    5(C4 H10 O3)                                                 
FORMUL   9   NA    NA 1+                                                        
FORMUL  10  HOH   *576(H2 O)                                                    
HELIX    1 AA1 PRO A    7  ALA A   12  5                                   6    
HELIX    2 AA2 TRP A   58  ARG A   63  5                                   6    
HELIX    3 AA3 MET A   65  ALA A   72  1                                   8    
HELIX    4 AA4 SER A   92  TYR A   96  5                                   5    
HELIX    5 AA5 THR A   97  ASP A  113  1                                  17    
HELIX    6 AA6 ASP A  123  ASN A  136  1                                  14    
HELIX    7 AA7 GLY A  158  ILE A  171  1                                  14    
HELIX    8 AA8 HIS A  175  GLY A  183  1                                   9    
HELIX    9 AA9 SER A  189  ALA A  198  1                                  10    
HELIX   10 AB1 ASP A  202  TYR A  205  5                                   4    
HELIX   11 AB2 LYS A  206  PHE A  212  1                                   7    
HELIX   12 AB3 PRO A  213  VAL A  216  5                                   4    
HELIX   13 AB4 ALA A  224  SER A  236  1                                  13    
HELIX   14 AB5 GLY A  255  ILE A  264  1                                  10    
HELIX   15 AB6 PRO A  265  LYS A  268  5                                   4    
HELIX   16 AB7 PHE A  281  ASP A  300  1                                  20    
SHEET    1 AA1 2 ILE A   3  LEU A   4  0                                        
SHEET    2 AA1 2 LYS A  89  PRO A  90 -1  O  LYS A  89   N  LEU A   4           
SHEET    1 AA2 7 HIS A  22  ASP A  27  0                                        
SHEET    2 AA2 7 GLU A  33  GLU A  41 -1  O  VAL A  36   N  LEU A  24           
SHEET    3 AA2 7 ARG A  75  PRO A  79 -1  O  VAL A  76   N  GLU A  41           
SHEET    4 AA2 7 PRO A  48  LEU A  52  1  N  LEU A  51   O  ILE A  77           
SHEET    5 AA2 7 ILE A 117  CYS A 121  1  O  PHE A 120   N  LEU A  50           
SHEET    6 AA2 7 PHE A 140  ALA A 145  1  O  ALA A 144   N  LEU A 119           
SHEET    7 AA2 7 PHE A 242  THR A 244  1  O  ILE A 243   N  VAL A 143           
SHEET    1 AA3 2 SER A 247  SER A 249  0                                        
SHEET    2 AA3 2 ILE A 275  GLY A 279  1  O  ILE A 275   N  ASP A 248           
LINK         O   GLN A 261                NA    NA A 408     1555   1555  3.02  
LINK         OG1 THR A 267                NA    NA A 408     1555   1555  2.82  
LINK        NA    NA A 408                 O   HOH A 727     1555   1555  2.92  
LINK        NA    NA A 408                 O   HOH A 892     1555   1555  2.56  
LINK        NA    NA A 408                 O   HOH A 906     1555   1555  2.43  
CISPEP   1 GLU A   55    PRO A   56          0       -28.57                     
SITE     1 AC1  4 TRP A 124  TRP A 164  PRO A 213  HOH A 610                    
SITE     1 AC2  3 GLY A 177  GLY A 178  ASN A 197                               
SITE     1 AC3  5 THR A  94  HOH A 708  HOH A 782  HOH A 793                    
SITE     2 AC3  5 HOH A1058                                                     
SITE     1 AC4 10 ARG A  93  LEU A 214  HOH A 519  HOH A 528                    
SITE     2 AC4 10 HOH A 578  HOH A 713  HOH A 785  HOH A 851                    
SITE     3 AC4 10 HOH A 900  HOH A 934                                          
SITE     1 AC5  4 GLU A 135  HOH A 693  HOH A 849  HOH A 860                    
SITE     1 AC6  3 PRO A  43  HOH A 573  HOH A 608                               
SITE     1 AC7  7 PRO A  21  ARG A  86  HOH A 506  HOH A 589                    
SITE     2 AC7  7 HOH A 597  HOH A 618  HOH A 916                               
SITE     1 AC8  6 GLN A 261  THR A 267  LYS A 268  HOH A 727                    
SITE     2 AC8  6 HOH A 892  HOH A 906                                          
CRYST1   41.332   79.451   43.489  90.00  94.98  90.00 P 1 21 1      2          
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      0.024194  0.000000  0.002109        0.00000                         
SCALE2      0.000000  0.012586  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.023081        0.00000                         
TER    2625      HIS A 309                                                      
MASTER      365    0    8   16   11    0   13    6 3069    1   32   24          
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.
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