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LongText Report for: 2HDW-pdb

Name Class
2HDW-pdb
HEADER    HYDROLASE                               21-JUN-06   2HDW              
TITLE     CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN PA2218 FROM                 
TITLE    2 PSEUDOMONAS AERUGINOSA                                               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HYPOTHETICAL PROTEIN PA2218;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_COMMON: BACTERIA;                                           
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_COMMON: BACTERIA                                   
KEYWDS    PA2218, ALPHA/BETA HYDROLASE FOLD, STRUCTURAL GENOMICS, PSI,          
KEYWDS   2 PROTEIN STRUCTURE INITIATIVE, NEW YORK STRUCTURAL GENOMIX            
KEYWDS   3 RESEARCH CONSORTIUM, NYSGXRC                                         
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.A.FEDOROV,E.V.FEDOROV,U.RAMAGOPAL,S.C.ALMO,S.K.BURLEY,NEW           
AUTHOR   2 YORK STRUCTURAL GENOMIX RESEARCH CONSORTIUM (NYSGXRC)                
REVDAT   1   28-NOV-06 2HDW    0                                                
JRNL        AUTH   A.A.FEDOROV,E.V.FEDOROV,U.RAMAGOPAL,S.C.ALMO                 
JRNL        TITL   CRYSTAL STRUCTURE OF HYPOTHETICAL PROTEIN PA2218             
JRNL        TITL 2 FROM PSEUDOMONAS AERUGINOSA                                  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 2.00 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 : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 22.72                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.100                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 261609.240                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 98.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 37451                          
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) : 0.198                           
REMARK   3   FREE R VALUE                     : 0.231                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1904                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.005                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.07                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.20                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3491                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1980                       
REMARK   3   BIN FREE R VALUE                    : 0.2460                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.10                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 187                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.018                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5027                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 194                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.40                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 14.20                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 9.50000                                              
REMARK   3    B22 (A**2) : -7.37000                                             
REMARK   3    B33 (A**2) : -2.13000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 2.05000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.22                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.08                            
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) : 0.27                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.16                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.007                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.40                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.86                            
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) : 1.090 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.530 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 2.100 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.530 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.39                                                 
REMARK   3   BSOL        : 41.99                                                
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  : 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   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2HDW COMPLIES WITH FORMAT V. 3.0, 1-DEC-2006                         
REMARK   4                                                                      
REMARK   4 THIS IS THE REMEDIATED VERSION OF THIS PDB ENTRY.                    
REMARK   4 REMEDIATED DATA FILE REVISION 3.100 (2007-03-18)                     
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB .                              
REMARK 100 THE RCSB ID CODE IS RCSB038239.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 6.50                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X4A                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979, 0.97934, 0.97911,           
REMARK 200                                   0.97166                            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 37451                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 23.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.5                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.07                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 97.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 20% PEG3350, 0.1M BIS-TRIS, 0.1M         
REMARK 280  NACL, PH 6.5, VAPOR 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,1/2+Y,-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       68.16850            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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                                     
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 BIOMOLECULE: 2                                                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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     GLU A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     LYS A     4                                                      
REMARK 465     HIS A     5                                                      
REMARK 465     SER A     6                                                      
REMARK 465     ASN A     7                                                      
REMARK 465     ARG A     8                                                      
REMARK 465     ALA A     9                                                      
REMARK 465     ARG A    10                                                      
REMARK 465     SER A    11                                                      
REMARK 465     ARG A    12                                                      
REMARK 465     LYS A    13                                                      
REMARK 465     GLY A    14                                                      
REMARK 465     ALA A    15                                                      
REMARK 465     LEU A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     GLY A    18                                                      
REMARK 465     ALA A    19                                                      
REMARK 465     VAL A    20                                                      
REMARK 465     LEU A    21                                                      
REMARK 465     ALA A    22                                                      
REMARK 465     GLY A    23                                                      
REMARK 465     ALA A    24                                                      
REMARK 465     LEU A    25                                                      
REMARK 465     MET A    26                                                      
REMARK 465     ALA A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     VAL A    29                                                      
REMARK 465     GLY A    30                                                      
REMARK 465     CYS A    31                                                      
REMARK 465     GLN A    32                                                      
REMARK 465     THR A    33                                                      
REMARK 465     SER A    34                                                      
REMARK 465     PRO A    35                                                      
REMARK 465     ALA A    36                                                      
REMARK 465     ALA A    37                                                      
REMARK 465     THR A    38                                                      
REMARK 465     THR A    39                                                      
REMARK 465     SER A    40                                                      
REMARK 465     SER A    41                                                      
REMARK 465     ASN A    42                                                      
REMARK 465     THR A    43                                                      
REMARK 465     GLY A    44                                                      
REMARK 465     GLY A    45                                                      
REMARK 465     THR A    46                                                      
REMARK 465     MET B     1                                                      
REMARK 465     GLU B     2                                                      
REMARK 465     THR B     3                                                      
REMARK 465     LYS B     4                                                      
REMARK 465     HIS B     5                                                      
REMARK 465     SER B     6                                                      
REMARK 465     ASN B     7                                                      
REMARK 465     ARG B     8                                                      
REMARK 465     ALA B     9                                                      
REMARK 465     ARG B    10                                                      
REMARK 465     SER B    11                                                      
REMARK 465     ARG B    12                                                      
REMARK 465     LYS B    13                                                      
REMARK 465     GLY B    14                                                      
REMARK 465     ALA B    15                                                      
REMARK 465     LEU B    16                                                      
REMARK 465     ARG B    17                                                      
REMARK 465     GLY B    18                                                      
REMARK 465     ALA B    19                                                      
REMARK 465     VAL B    20                                                      
REMARK 465     LEU B    21                                                      
REMARK 465     ALA B    22                                                      
REMARK 465     GLY B    23                                                      
REMARK 465     ALA B    24                                                      
REMARK 465     LEU B    25                                                      
REMARK 465     MET B    26                                                      
REMARK 465     ALA B    27                                                      
REMARK 465     LEU B    28                                                      
REMARK 465     VAL B    29                                                      
REMARK 465     GLY B    30                                                      
REMARK 465     CYS B    31                                                      
REMARK 465     GLN B    32                                                      
REMARK 465     THR B    33                                                      
REMARK 465     SER B    34                                                      
REMARK 465     PRO B    35                                                      
REMARK 465     ALA B    36                                                      
REMARK 465     ALA B    37                                                      
REMARK 465     THR B    38                                                      
REMARK 465     THR B    39                                                      
REMARK 465     SER B    40                                                      
REMARK 465     SER B    41                                                      
REMARK 465     ASN B    42                                                      
REMARK 465     THR B    43                                                      
REMARK 465     GLY B    44                                                      
REMARK 465     GLY B    45                                                      
REMARK 465     THR B    46                                                      
REMARK 465     ASN B    47                                                      
REMARK 465     MET B    48                                                      
REMARK 465     GLN B    49                                                      
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    MET A 120   SD    MET A 120   CE    -0.093                        
REMARK 500    MET A 203   CG    MET A 203   SD     0.043                        
REMARK 500    MET A 206   CG    MET A 206   SD     0.042                        
REMARK 500    MET A 210   SD    MET A 210   CE    -0.046                        
REMARK 500    MET A 268   SD    MET A 268   CE     0.040                        
REMARK 500    MET A 293   SD    MET A 293   CE    -0.051                        
REMARK 500    MET B 120   SD    MET B 120   CE    -0.152                        
REMARK 500    MET B 203   CG    MET B 203   SD     0.047                        
REMARK 500    MET B 286   SD    MET B 286   CE    -0.048                        
REMARK 500    MET B 293   SD    MET B 293   CE    -0.049                        
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    PRO A  97   N   -  CA  -  C   ANGL. DEV. = -9.0 DEGREES           
REMARK 500    VAL A 126   N   -  CA  -  C   ANGL. DEV. =-11.6 DEGREES           
REMARK 500    VAL A 145   N   -  CA  -  C   ANGL. DEV. = -9.4 DEGREES           
REMARK 500    TYR A 204   N   -  CA  -  C   ANGL. DEV. = -9.7 DEGREES           
REMARK 500    ASP A 205   N   -  CA  -  C   ANGL. DEV. =-15.6 DEGREES           
REMARK 500    ILE A 304   N   -  CA  -  C   ANGL. DEV. = -9.1 DEGREES           
REMARK 500    PRO A 306   C   -  N   -  CA  ANGL. DEV. =  8.4 DEGREES           
REMARK 500    PRO B  97   N   -  CA  -  C   ANGL. DEV. = -9.3 DEGREES           
REMARK 500    SER B 112   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES           
REMARK 500    VAL B 126   N   -  CA  -  C   ANGL. DEV. =-11.6 DEGREES           
REMARK 500    VAL B 145   N   -  CA  -  C   ANGL. DEV. =-10.4 DEGREES           
REMARK 500    MET B 203   N   -  CA  -  C   ANGL. DEV. =  9.0 DEGREES           
REMARK 500    TYR B 204   N   -  CA  -  C   ANGL. DEV. = -8.6 DEGREES           
REMARK 500    ASP B 205   N   -  CA  -  C   ANGL. DEV. =-15.0 DEGREES           
REMARK 500    ILE B 304   N   -  CA  -  C   ANGL. DEV. = -8.8 DEGREES           
REMARK 500    ASP B 349   N   -  CA  -  C   ANGL. DEV. =  8.4 DEGREES           
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-2896C   RELATED DB: TARGETDB                     
DBREF  2HDW A    1   367  UNP    Q01609   Y2218_PSEAE      5    371             
DBREF  2HDW B    1   367  UNP    Q01609   Y2218_PSEAE      5    371             
SEQRES   1 A  367  MET GLU THR LYS HIS SER ASN ARG ALA ARG SER ARG LYS          
SEQRES   2 A  367  GLY ALA LEU ARG GLY ALA VAL LEU ALA GLY ALA LEU MET          
SEQRES   3 A  367  ALA LEU VAL GLY CYS GLN THR SER PRO ALA ALA THR THR          
SEQRES   4 A  367  SER SER ASN THR GLY GLY THR ASN MET GLN LEU GLN LEU          
SEQRES   5 A  367  THR GLN GLU TRP ASP LYS THR PHE PRO LEU SER ALA LYS          
SEQRES   6 A  367  VAL GLU HIS ARG LYS VAL THR PHE ALA ASN ARG TYR GLY          
SEQRES   7 A  367  ILE THR LEU ALA ALA ASP LEU TYR LEU PRO LYS ASN ARG          
SEQRES   8 A  367  GLY GLY ASP ARG LEU PRO ALA ILE VAL ILE GLY GLY PRO          
SEQRES   9 A  367  PHE GLY ALA VAL LYS GLU GLN SER SER GLY LEU TYR ALA          
SEQRES  10 A  367  GLN THR MET ALA GLU ARG GLY PHE VAL THR LEU ALA PHE          
SEQRES  11 A  367  ASP PRO SER TYR THR GLY GLU SER GLY GLY GLN PRO ARG          
SEQRES  12 A  367  ASN VAL ALA SER PRO ASP ILE ASN THR GLU ASP PHE SER          
SEQRES  13 A  367  ALA ALA VAL ASP PHE ILE SER LEU LEU PRO GLU VAL ASN          
SEQRES  14 A  367  ARG GLU ARG ILE GLY VAL ILE GLY ILE CYS GLY TRP GLY          
SEQRES  15 A  367  GLY MET ALA LEU ASN ALA VAL ALA VAL ASP LYS ARG VAL          
SEQRES  16 A  367  LYS ALA VAL VAL THR SER THR MET TYR ASP MET THR ARG          
SEQRES  17 A  367  VAL MET SER LYS GLY TYR ASN ASP SER VAL THR LEU GLU          
SEQRES  18 A  367  GLN ARG THR ARG THR LEU GLU GLN LEU GLY GLN GLN ARG          
SEQRES  19 A  367  TRP LYS ASP ALA GLU SER GLY THR PRO ALA TYR GLN PRO          
SEQRES  20 A  367  PRO TYR ASN GLU LEU LYS GLY GLY GLU ALA GLN PHE LEU          
SEQRES  21 A  367  VAL ASP TYR HIS ASP TYR TYR MET THR PRO ARG GLY TYR          
SEQRES  22 A  367  HIS PRO ARG ALA VAL ASN SER GLY ASN ALA TRP THR MET          
SEQRES  23 A  367  THR THR PRO LEU SER PHE MET ASN MET PRO ILE LEU THR          
SEQRES  24 A  367  TYR ILE LYS GLU ILE SER PRO ARG PRO ILE LEU LEU ILE          
SEQRES  25 A  367  HIS GLY GLU ARG ALA HIS SER ARG TYR PHE SER GLU THR          
SEQRES  26 A  367  ALA TYR ALA ALA ALA ALA GLU PRO LYS GLU LEU LEU ILE          
SEQRES  27 A  367  VAL PRO GLY ALA SER HIS VAL ASP LEU TYR ASP ARG LEU          
SEQRES  28 A  367  ASP ARG ILE PRO PHE ASP ARG ILE ALA GLY PHE PHE ASP          
SEQRES  29 A  367  GLU HIS LEU                                                  
SEQRES   1 B  367  MET GLU THR LYS HIS SER ASN ARG ALA ARG SER ARG LYS          
SEQRES   2 B  367  GLY ALA LEU ARG GLY ALA VAL LEU ALA GLY ALA LEU MET          
SEQRES   3 B  367  ALA LEU VAL GLY CYS GLN THR SER PRO ALA ALA THR THR          
SEQRES   4 B  367  SER SER ASN THR GLY GLY THR ASN MET GLN LEU GLN LEU          
SEQRES   5 B  367  THR GLN GLU TRP ASP LYS THR PHE PRO LEU SER ALA LYS          
SEQRES   6 B  367  VAL GLU HIS ARG LYS VAL THR PHE ALA ASN ARG TYR GLY          
SEQRES   7 B  367  ILE THR LEU ALA ALA ASP LEU TYR LEU PRO LYS ASN ARG          
SEQRES   8 B  367  GLY GLY ASP ARG LEU PRO ALA ILE VAL ILE GLY GLY PRO          
SEQRES   9 B  367  PHE GLY ALA VAL LYS GLU GLN SER SER GLY LEU TYR ALA          
SEQRES  10 B  367  GLN THR MET ALA GLU ARG GLY PHE VAL THR LEU ALA PHE          
SEQRES  11 B  367  ASP PRO SER TYR THR GLY GLU SER GLY GLY GLN PRO ARG          
SEQRES  12 B  367  ASN VAL ALA SER PRO ASP ILE ASN THR GLU ASP PHE SER          
SEQRES  13 B  367  ALA ALA VAL ASP PHE ILE SER LEU LEU PRO GLU VAL ASN          
SEQRES  14 B  367  ARG GLU ARG ILE GLY VAL ILE GLY ILE CYS GLY TRP GLY          
SEQRES  15 B  367  GLY MET ALA LEU ASN ALA VAL ALA VAL ASP LYS ARG VAL          
SEQRES  16 B  367  LYS ALA VAL VAL THR SER THR MET TYR ASP MET THR ARG          
SEQRES  17 B  367  VAL MET SER LYS GLY TYR ASN ASP SER VAL THR LEU GLU          
SEQRES  18 B  367  GLN ARG THR ARG THR LEU GLU GLN LEU GLY GLN GLN ARG          
SEQRES  19 B  367  TRP LYS ASP ALA GLU SER GLY THR PRO ALA TYR GLN PRO          
SEQRES  20 B  367  PRO TYR ASN GLU LEU LYS GLY GLY GLU ALA GLN PHE LEU          
SEQRES  21 B  367  VAL ASP TYR HIS ASP TYR TYR MET THR PRO ARG GLY TYR          
SEQRES  22 B  367  HIS PRO ARG ALA VAL ASN SER GLY ASN ALA TRP THR MET          
SEQRES  23 B  367  THR THR PRO LEU SER PHE MET ASN MET PRO ILE LEU THR          
SEQRES  24 B  367  TYR ILE LYS GLU ILE SER PRO ARG PRO ILE LEU LEU ILE          
SEQRES  25 B  367  HIS GLY GLU ARG ALA HIS SER ARG TYR PHE SER GLU THR          
SEQRES  26 B  367  ALA TYR ALA ALA ALA ALA GLU PRO LYS GLU LEU LEU ILE          
SEQRES  27 B  367  VAL PRO GLY ALA SER HIS VAL ASP LEU TYR ASP ARG LEU          
SEQRES  28 B  367  ASP ARG ILE PRO PHE ASP ARG ILE ALA GLY PHE PHE ASP          
SEQRES  29 B  367  GLU HIS LEU                                                  
FORMUL   3  HOH   *194(H2 O)                                                    
HELIX    1   1 GLN A  111  ARG A  123  1                                  13    
HELIX    2   2 SER A  147  LEU A  165  1                                  19    
HELIX    3   3 GLY A  180  ASP A  192  1                                  13    
HELIX    4   4 ASP A  205  GLY A  213  1                                   9    
HELIX    5   5 THR A  219  GLY A  241  1                                  23    
HELIX    6   6 ALA A  257  MET A  268  1                                  12    
HELIX    7   7 THR A  288  MET A  293  1                                   6    
HELIX    8   8 TYR A  300  SER A  305  5                                   6    
HELIX    9   9 SER A  319  ALA A  330  1                                  12    
HELIX   10  10 VAL A  345  ARG A  350  1                                   6    
HELIX   11  11 PRO A  355  LEU A  367  1                                  13    
HELIX   12  12 GLN B  111  ARG B  123  1                                  13    
HELIX   13  13 SER B  147  SER B  163  1                                  17    
HELIX   14  14 GLY B  180  ASP B  192  1                                  13    
HELIX   15  15 ASP B  205  GLY B  213  1                                   9    
HELIX   16  16 TYR B  214  SER B  217  5                                   4    
HELIX   17  17 THR B  219  GLY B  241  1                                  23    
HELIX   18  18 ALA B  257  MET B  268  1                                  12    
HELIX   19  19 THR B  288  MET B  293  1                                   6    
HELIX   20  20 TYR B  300  ILE B  304  5                                   5    
HELIX   21  21 SER B  319  ALA B  330  1                                  12    
HELIX   22  22 VAL B  345  ARG B  350  1                                   6    
HELIX   23  23 PRO B  355  LEU B  367  1                                  13    
SHEET    1   A 8 VAL A  66  ALA A  74  0                                        
SHEET    2   A 8 THR A  80  PRO A  88 -1  O  LEU A  81   N  PHE A  73           
SHEET    3   A 8 VAL A 126  PHE A 130 -1  O  THR A 127   N  TYR A  86           
SHEET    4   A 8 LEU A  96  GLY A 102  1  N  ILE A 101   O  LEU A 128           
SHEET    5   A 8 VAL A 168  ILE A 178  1  O  ARG A 172   N  ALA A  98           
SHEET    6   A 8 ALA A 197  SER A 201  1  O  SER A 201   N  GLY A 177           
SHEET    7   A 8 ILE A 309  GLY A 314  1  O  ILE A 312   N  THR A 200           
SHEET    8   A 8 LYS A 334  VAL A 339  1  O  LEU A 337   N  LEU A 311           
SHEET    1   B 8 VAL B  66  ALA B  74  0                                        
SHEET    2   B 8 THR B  80  PRO B  88 -1  O  LEU B  81   N  PHE B  73           
SHEET    3   B 8 VAL B 126  PHE B 130 -1  O  ALA B 129   N  ASP B  84           
SHEET    4   B 8 LEU B  96  GLY B 102  1  N  ILE B 101   O  LEU B 128           
SHEET    5   B 8 VAL B 168  ILE B 178  1  O  ILE B 178   N  GLY B 102           
SHEET    6   B 8 VAL B 195  SER B 201  1  O  LYS B 196   N  ILE B 173           
SHEET    7   B 8 ILE B 309  GLY B 314  1  O  ILE B 312   N  THR B 200           
SHEET    8   B 8 LYS B 334  VAL B 339  1  O  LEU B 337   N  LEU B 311           
CISPEP   1 GLY A  103    PRO A  104          0        -0.36                     
CISPEP   2 GLN A  141    PRO A  142          0        -0.03                     
CISPEP   3 SER A  305    PRO A  306          0         0.20                     
CISPEP   4 GLU A  332    PRO A  333          0         0.00                     
CISPEP   5 GLY B  103    PRO B  104          0        -0.23                     
CISPEP   6 GLN B  141    PRO B  142          0         0.27                     
CISPEP   7 SER B  305    PRO B  306          0         0.21                     
CISPEP   8 GLU B  332    PRO B  333          0         0.02                     
CRYST1   46.264  136.337   48.134  90.00 108.74  90.00 P 1 21 1      4          
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      0.021615  0.000000  0.007333        0.00000                         
SCALE2      0.000000  0.007335  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021938        0.00000                         
TER    2527      LEU A 367                                                      
TER    5029      LEU B 367                                                      
MASTER      375    0    0   23   16    0    0    6 5221    2    0   58          
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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