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LongText Report for: 3OOS-pdb

Name Class
3OOS-pdb
HEADER    HYDROLASE                               31-AUG-10   3OOS              
TITLE     THE STRUCTURE OF AN ALPHA/BETA FOLD FAMILY HYDROLASE FROM BACILLUS    
TITLE    2 ANTHRACIS STR. STERNE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ALPHA/BETA HYDROLASE FAMILY PROTEIN;                       
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: HYDROLASE, ALPHA/BETA FOLD FAMILY;                          
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_TAXID: 260799;                                              
SOURCE   4 STRAIN: STERNE;                                                      
SOURCE   5 GENE: BAS2502, BA_2687, GBAA2687, GBAA_2687;                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    APC67239.0, PROTEIN STRUCTURE INITIATIVE, PSI-2, STRUCTURAL GENOMICS, 
KEYWDS   2 MIDWEST CENTER FOR STRUCTURAL GENOMICS, MCSG, MEDICAL STRUCTURAL     
KEYWDS   3 GENOMICS OF PATHOGENIC PROTOZOA, MSGPP, ALPHA/BETA FOLD FAMILY,      
KEYWDS   4 HYDROLASE                                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.FAN,K.TAN,L.BIGELOW,J.HAMILTON,H.LI,Y.ZHOU,S.CLANCY,K.BUCK,         
AUTHOR   2 A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL GENOMICS (MCSG)           
REVDAT   1   10-NOV-10 3OOS    0                                                
JRNL        AUTH   Y.FAN,K.TAN,L.BIGELOW,J.HAMILTON,H.LI,Y.ZHOU,S.CLANCY,       
JRNL        AUTH 2 K.BUCK,A.JOACHIMIAK                                          
JRNL        TITL   THE STRUCTURE OF AN ALPHA/BETA FOLD FAMILY HYDROLASE FROM    
JRNL        TITL 2 BACILLUS ANTHRACIS STR. STERNE                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.65 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0109                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.65                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 65.92                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 38732                          
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) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.147                           
REMARK   3   FREE R VALUE                     : 0.182                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2040                            
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) : 1.66                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.70                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2719                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.93                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1720                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 139                          
REMARK   3   BIN FREE R VALUE                    : 0.2080                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2227                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 56                                      
REMARK   3   SOLVENT ATOMS            : 414                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.16000                                             
REMARK   3    B22 (A**2) : 0.11000                                              
REMARK   3    B33 (A**2) : 0.05000                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.047         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.974         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.967                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.956                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2593 ; 0.006 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3534 ; 0.897 ; 1.968       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   348 ; 5.093 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   127 ;38.774 ;25.433       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   485 ;11.908 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;15.479 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   372 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1988 ; 0.004 ; 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):  1524 ; 0.408 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2505 ; 0.775 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1069 ; 1.299 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1000 ; 2.103 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  2593 ; 0.533 ; 3.000       
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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A   -10        A  9999                          
REMARK   3    ORIGIN FOR THE GROUP (A):  26.3391  21.7885  37.2034              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0034 T22:   0.0011                                     
REMARK   3      T33:   0.0045 T12:  -0.0015                                     
REMARK   3      T13:   0.0006 T23:   0.0005                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.1669 L22:   0.0818                                     
REMARK   3      L33:   0.1232 L12:  -0.0457                                     
REMARK   3      L13:   0.0633 L23:   0.0136                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0026 S12:   0.0009 S13:  -0.0136                       
REMARK   3      S21:  -0.0022 S22:   0.0026 S23:   0.0048                       
REMARK   3      S31:  -0.0069 S32:   0.0010 S33:   0.0000                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
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 3OOS COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 09-SEP-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061384.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 22-JUL-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-BM                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9797                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : SBC-3                              
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 40780                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.660                              
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                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.04300                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 56.0300                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.66                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.69                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.18100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 12.000                             
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/ARP/WARP/HKL3000                       
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.77                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.66                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M AMMONIUM SULFATE, 0.1M HEPES        
REMARK 280  PH7.5, 16%W/V PEG4000, 10%W/V ISOPROPANOL, VAPOR DIFFUSION,         
REMARK 280  SITTING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 2 2 2                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X,Y,-Z                                                 
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z+1/2                                     
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       36.85850            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       40.41950            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       56.93350            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       36.85850            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       40.41950            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       56.93350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       36.85850            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       40.41950            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       56.93350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       36.85850            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       40.41950            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       56.93350            
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 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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 468  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    TYR A  31       50.48   -150.73                                   
REMARK 500    SER A  98     -117.90     62.23                                   
REMARK 500    ALA A 111       45.29   -144.32                                   
REMARK 500    ALA A 123     -168.73   -114.32                                   
REMARK 500    ASP A 211      114.22   -167.53                                   
REMARK 500    GLN A 233      -73.22    -93.93                                   
REMARK 500    ASN A 258      -98.27    -94.64                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 A 278                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 279                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 280                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 281                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PG4 A 282                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GOL A 283                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC67239.0   RELATED DB: TARGETDB                        
DBREF  3OOS A    1   277  UNP    Q81PV7   Q81PV7_BACAN     1    277             
SEQADV 3OOS ALA A    0  UNP  Q81PV7              EXPRESSION TAG                 
SEQRES   1 A  278  ALA MSE TRP THR THR ASN ILE ILE LYS THR PRO ARG GLY          
SEQRES   2 A  278  LYS PHE GLU TYR PHE LEU LYS GLY GLU GLY PRO PRO LEU          
SEQRES   3 A  278  CYS VAL THR HIS LEU TYR SER GLU TYR ASN ASP ASN GLY          
SEQRES   4 A  278  ASN THR PHE ALA ASN PRO PHE THR ASP HIS TYR SER VAL          
SEQRES   5 A  278  TYR LEU VAL ASN LEU LYS GLY CYS GLY ASN SER ASP SER          
SEQRES   6 A  278  ALA LYS ASN ASP SER GLU TYR SER MSE THR GLU THR ILE          
SEQRES   7 A  278  LYS ASP LEU GLU ALA ILE ARG GLU ALA LEU TYR ILE ASN          
SEQRES   8 A  278  LYS TRP GLY PHE ALA GLY HIS SER ALA GLY GLY MSE LEU          
SEQRES   9 A  278  ALA LEU VAL TYR ALA THR GLU ALA GLN GLU SER LEU THR          
SEQRES  10 A  278  LYS ILE ILE VAL GLY GLY ALA ALA ALA SER LYS GLU TYR          
SEQRES  11 A  278  ALA SER HIS LYS ASP SER ILE TYR CYS SER LYS ASN VAL          
SEQRES  12 A  278  LYS PHE ASN ARG ILE VAL SER ILE MSE ASN ALA LEU ASN          
SEQRES  13 A  278  ASP ASP SER THR VAL GLN GLU GLU ARG LYS ALA LEU SER          
SEQRES  14 A  278  ARG GLU TRP ALA LEU MSE SER PHE TYR SER GLU GLU LYS          
SEQRES  15 A  278  LEU GLU GLU ALA LEU LYS LEU PRO ASN SER GLY LYS THR          
SEQRES  16 A  278  VAL GLY ASN ARG LEU ASN TYR PHE ARG GLN VAL GLU TYR          
SEQRES  17 A  278  LYS ASP TYR ASP VAL ARG GLN LYS LEU LYS PHE VAL LYS          
SEQRES  18 A  278  ILE PRO SER PHE ILE TYR CYS GLY LYS HIS ASP VAL GLN          
SEQRES  19 A  278  CYS PRO TYR ILE PHE SER CYS GLU ILE ALA ASN LEU ILE          
SEQRES  20 A  278  PRO ASN ALA THR LEU THR LYS PHE GLU GLU SER ASN HIS          
SEQRES  21 A  278  ASN PRO PHE VAL GLU GLU ILE ASP LYS PHE ASN GLN PHE          
SEQRES  22 A  278  VAL ASN ASP THR LEU                                          
MODRES 3OOS MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 3OOS MSE A   73  MET  SELENOMETHIONINE                                   
MODRES 3OOS MSE A  102  MET  SELENOMETHIONINE                                   
MODRES 3OOS MSE A  151  MET  SELENOMETHIONINE                                   
MODRES 3OOS MSE A  174  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  73      16                                                       
HET    MSE  A 102       8                                                       
HET    MSE  A 151       8                                                       
HET    MSE  A 174       8                                                       
HET    SO4  A 278       5                                                       
HET    GOL  A 279       6                                                       
HET    PG4  A 280      13                                                       
HET    PG4  A 281      13                                                       
HET    PG4  A 282      13                                                       
HET    GOL  A 283       6                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
HETNAM     GOL GLYCEROL                                                         
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   1  MSE    5(C5 H11 N O2 SE)                                            
FORMUL   2  SO4    O4 S 2-                                                      
FORMUL   3  GOL    2(C3 H8 O3)                                                  
FORMUL   4  PG4    3(C8 H18 O5)                                                 
FORMUL   8  HOH   *414(H2 O)                                                    
HELIX    1   1 ALA A   42  HIS A   48  5                                   7    
HELIX    2   2 ASN A   67  TYR A   71  5                                   5    
HELIX    3   3 SER A   72  LEU A   87  1                                  16    
HELIX    4   4 SER A   98  GLN A  112  1                                  15    
HELIX    5   5 SER A  126  HIS A  132  5                                   7    
HELIX    6   6 LYS A  143  ASN A  155  1                                  13    
HELIX    7   7 VAL A  160  PHE A  176  1                                  17    
HELIX    8   8 SER A  178  LEU A  186  1                                   9    
HELIX    9   9 VAL A  195  VAL A  205  1                                  11    
HELIX   10  10 GLU A  206  TYR A  210  5                                   5    
HELIX   11  11 VAL A  212  LYS A  217  1                                   6    
HELIX   12  12 PRO A  235  ILE A  246  1                                  12    
HELIX   13  13 ASN A  260  GLU A  265  1                                   6    
HELIX   14  14 GLU A  265  THR A  276  1                                  12    
SHEET    1   A 8 THR A   3  THR A   9  0                                        
SHEET    2   A 8 GLY A  12  LYS A  19 -1  O  LEU A  18   N  THR A   3           
SHEET    3   A 8 SER A  50  VAL A  54 -1  O  LEU A  53   N  PHE A  17           
SHEET    4   A 8 PRO A  24  VAL A  27  1  N  LEU A  25   O  TYR A  52           
SHEET    5   A 8 TRP A  92  HIS A  97  1  O  GLY A  93   N  CYS A  26           
SHEET    6   A 8 LEU A 115  GLY A 121  1  O  GLY A 121   N  GLY A  96           
SHEET    7   A 8 SER A 223  GLY A 228  1  O  PHE A 224   N  ILE A 118           
SHEET    8   A 8 ALA A 249  PHE A 254  1  O  THR A 250   N  ILE A 225           
SHEET    1   B 2 SER A  32  GLU A  33  0                                        
SHEET    2   B 2 LYS A 193  THR A 194 -1  O  LYS A 193   N  GLU A  33           
LINK         C   ALA A   0                 N   MSE A   1     1555   1555  1.33  
LINK         C   MSE A   1                 N   TRP A   2     1555   1555  1.33  
LINK         C   SER A  72                 N  AMSE A  73     1555   1555  1.33  
LINK         C   SER A  72                 N  BMSE A  73     1555   1555  1.33  
LINK         C  AMSE A  73                 N  ATHR A  74     1555   1555  1.33  
LINK         C  BMSE A  73                 N  BTHR A  74     1555   1555  1.33  
LINK         C   GLY A 101                 N   MSE A 102     1555   1555  1.33  
LINK         C   MSE A 102                 N   LEU A 103     1555   1555  1.33  
LINK         C   ILE A 150                 N   MSE A 151     1555   1555  1.33  
LINK         C   MSE A 151                 N   ASN A 152     1555   1555  1.33  
LINK         C   LEU A 173                 N   MSE A 174     1555   1555  1.33  
LINK         C   MSE A 174                 N   SER A 175     1555   1555  1.33  
SITE     1 AC1  8 HIS A  29  TYR A  31  SER A  98  ALA A  99                    
SITE     2 AC1  8 GLN A 233  HIS A 259  PG4 A 281  HOH A 598                    
SITE     1 AC2 10 ARG A 146  SER A 149  ALA A 153  GLU A 163                    
SITE     2 AC2 10 THR A 250  LEU A 251  HOH A 487  HOH A 639                    
SITE     3 AC2 10 HOH A 643  HOH A 647                                          
SITE     1 AC3  5 TYR A 137  ARG A 164  SER A 168  TRP A 171                    
SITE     2 AC3  5 HOH A 326                                                     
SITE     1 AC4 11 TYR A  31  SER A  98  TYR A 129  TYR A 137                    
SITE     2 AC4 11 PHE A 202  ARG A 203  TYR A 207  GLN A 233                    
SITE     3 AC4 11 CYS A 234  SO4 A 278  HOH A 338                               
SITE     1 AC5  9 GLU A  33  ASN A  35  SER A 191  GLY A 192                    
SITE     2 AC5  9 LYS A 193  GOL A 283  HOH A 500  HOH A 545                    
SITE     3 AC5  9 HOH A 548                                                     
SITE     1 AC6  5 ASN A 190  GLY A 192  PG4 A 282  HOH A 542                    
SITE     2 AC6  5 HOH A 545                                                     
CRYST1   73.717   80.839  113.867  90.00  90.00  90.00 I 2 2 2       8          
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      0.013565  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012370  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008782        0.00000                         
TER    2456      LEU A 277                                                      
MASTER      325    0   11   14   10    0   15    6 2697    1  115   22          
END                                                                             

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