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LongText Report for: 3OM8-pdb

Name Class
3OM8-pdb
HEADER    HYDROLASE                               26-AUG-10   3OM8              
TITLE     THE CRYSTAL STRUCTURE OF A HYDROLASE FROM PSEUDOMONAS AERUGINOSA PA01 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE HYDROLASE;                                        
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: PSEUDOMONAS AERUGINOSA;                         
SOURCE   3 ORGANISM_TAXID: 208964;                                              
SOURCE   4 STRAIN: PA01;                                                        
SOURCE   5 GENE: PA0480;                                                        
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: PPK1037;                                   
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PMCSG19B                                  
KEYWDS    STRUCTURAL GENOMICS, PSI-2, PROTEIN STRUCTURE INITIATIVE, MIDWEST     
KEYWDS   2 CENTER FOR STRUCTURAL GENOMICS, MCSG, HYDROLASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAN,G.CHHOR,K.BUCK,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL       
AUTHOR   2 GENOMICS (MCSG)                                                      
REVDAT   1   22-SEP-10 3OM8    0                                                
JRNL        AUTH   K.TAN,G.CHHOR,K.BUCK,A.JOACHIMIAK                            
JRNL        TITL   THE CRYSTAL STRUCTURE OF A HYDROLASE FROM PSEUDOMONAS        
JRNL        TITL 2 AERUGINOSA PA01                                              
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.5_2)                        
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.020                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 86.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 50526                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.194                           
REMARK   3   R VALUE            (WORKING SET) : 0.192                           
REMARK   3   FREE R VALUE                     : 0.223                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2562                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 48.2420 -  4.8454    0.97     5784   299  0.1817 0.1989        
REMARK   3     2  4.8454 -  3.8465    0.98     5491   291  0.1417 0.1687        
REMARK   3     3  3.8465 -  3.3604    0.97     5365   306  0.1786 0.2063        
REMARK   3     4  3.3604 -  3.0532    0.95     5222   277  0.2057 0.2372        
REMARK   3     5  3.0532 -  2.8344    0.90     5010   246  0.2124 0.2378        
REMARK   3     6  2.8344 -  2.6673    0.88     4805   266  0.2253 0.2864        
REMARK   3     7  2.6673 -  2.5337    0.84     4556   251  0.2254 0.2707        
REMARK   3     8  2.5337 -  2.4234    0.78     4288   216  0.2385 0.2857        
REMARK   3     9  2.4234 -  2.3301    0.72     3929   189  0.2690 0.3125        
REMARK   3    10  2.3301 -  2.2497    0.65     3514   221  0.2959 0.3553        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.31                                          
REMARK   3   B_SOL              : 48.16                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : NULL             
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 14.61500                                             
REMARK   3    B22 (A**2) : 14.61500                                             
REMARK   3    B33 (A**2) : -29.23000                                            
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           4123                                  
REMARK   3   ANGLE     :  0.977           5619                                  
REMARK   3   CHIRALITY :  0.059            644                                  
REMARK   3   PLANARITY :  0.004            732                                  
REMARK   3   DIHEDRAL  : 18.889           1461                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 2                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  22.8227  56.1346  21.3082              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.4501 T22:   0.4349                                     
REMARK   3      T33:   0.2844 T12:  -0.0378                                     
REMARK   3      T13:  -0.0083 T23:  -0.0025                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.8579 L22:   0.6602                                     
REMARK   3      L33:   1.3214 L12:  -0.3773                                     
REMARK   3      L13:  -0.6040 L23:   0.9317                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0835 S12:   0.0271 S13:   0.0242                       
REMARK   3      S21:  -0.1296 S22:  -0.0514 S23:  -0.0267                       
REMARK   3      S31:  -0.1027 S32:   0.0160 S33:  -0.0339                       
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    SELECTION: CHAIN B                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  34.7511  21.3155  16.8059              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.3895 T22:   0.5216                                     
REMARK   3      T33:   0.3804 T12:   0.0359                                     
REMARK   3      T13:   0.0046 T23:  -0.0010                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.0543 L22:   1.0949                                     
REMARK   3      L33:   1.8552 L12:   0.2373                                     
REMARK   3      L13:  -0.1064 L23:  -0.8036                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0141 S12:  -0.0653 S13:  -0.0130                       
REMARK   3      S21:  -0.0393 S22:  -0.0441 S23:   0.0145                       
REMARK   3      S31:  -0.0091 S32:   0.0383 S33:   0.0548                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3OM8 COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 31-AUG-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB061292.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 25-AUG-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-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924                            
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 56314                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.3                               
REMARK 200  DATA REDUNDANCY                : 9.000                              
REMARK 200  R MERGE                    (I) : 0.13100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.1000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.29                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.30                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.67700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: SHELXD/MLPHARE/DM/ARP/WARP/HKL3000                    
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 76.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 5.20                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.2M PROLINE, 0.1M HEPES, 10% W/V        
REMARK 280  PEG3350, PH 7.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 289K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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      141.87250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       45.76450            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       45.76450            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       70.93625            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       45.76450            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       45.76450            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      212.80875            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       45.76450            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       45.76450            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       70.93625            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       45.76450            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       45.76450            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      212.80875            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      141.87250            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
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 300 REMARK: EXPERIMENTALLY UNKNOWN. IT IS PREDICTED THAT THE MOLECULE    
REMARK 300 IS MONOMERIC.                                                        
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6920 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 38630 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -8.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 20480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 2.0 KCAL/MOL                          
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 2880 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 19900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: 7.0 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 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       45.76450            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000       45.76450            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       70.93625            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
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 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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     SER A    -1                                                      
REMARK 465     ASN A     0                                                      
REMARK 465     SER B    -1                                                      
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    ARG A  60      125.89    -37.18                                   
REMARK 500    SER A  99     -114.28     58.34                                   
REMARK 500    ALA A 112       53.10   -140.63                                   
REMARK 500    GLU A 117      -95.63    -96.92                                   
REMARK 500    ASN A 123       61.23     33.00                                   
REMARK 500    PRO A 241       48.03    -78.82                                   
REMARK 500    VAL A 243     -130.38    -84.46                                   
REMARK 500    ALA B   1     -115.70     50.61                                   
REMARK 500    SER B  99     -118.56     57.74                                   
REMARK 500    GLU B 117      -94.79    -84.94                                   
REMARK 500    ASN B 123       63.85     39.01                                   
REMARK 500    TRP B 127      116.28   -168.53                                   
REMARK 500    ALA B 167      102.97    -38.10                                   
REMARK 500    PRO B 241       49.94    -77.67                                   
REMARK 500    VAL B 243      -92.00    -88.20                                   
REMARK 500    LEU B 245       75.68   -102.21                                   
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 MES A 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO A 266                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MES B 265                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE EDO B 266                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC37789.1   RELATED DB: TARGETDB                        
DBREF  3OM8 A    2   264  UNP    Q9I638   Q9I638_PSEAE     2    264             
DBREF  3OM8 B    2   264  UNP    Q9I638   Q9I638_PSEAE     2    264             
SEQADV 3OM8 SER A   -1  UNP  Q9I638              EXPRESSION TAG                 
SEQADV 3OM8 ASN A    0  UNP  Q9I638              EXPRESSION TAG                 
SEQADV 3OM8 ALA A    1  UNP  Q9I638              EXPRESSION TAG                 
SEQADV 3OM8 SER B   -1  UNP  Q9I638              EXPRESSION TAG                 
SEQADV 3OM8 ASN B    0  UNP  Q9I638              EXPRESSION TAG                 
SEQADV 3OM8 ALA B    1  UNP  Q9I638              EXPRESSION TAG                 
SEQRES   1 A  266  SER ASN ALA GLY ASN LEU SER PHE LEU ALA THR SER ASP          
SEQRES   2 A  266  GLY ALA SER LEU ALA TYR ARG LEU ASP GLY ALA ALA GLU          
SEQRES   3 A  266  LYS PRO LEU LEU ALA LEU SER ASN SER ILE GLY THR THR          
SEQRES   4 A  266  LEU HIS MSE TRP ASP ALA GLN LEU PRO ALA LEU THR ARG          
SEQRES   5 A  266  HIS PHE ARG VAL LEU ARG TYR ASP ALA ARG GLY HIS GLY          
SEQRES   6 A  266  ALA SER SER VAL PRO PRO GLY PRO TYR THR LEU ALA ARG          
SEQRES   7 A  266  LEU GLY GLU ASP VAL LEU GLU LEU LEU ASP ALA LEU GLU          
SEQRES   8 A  266  VAL ARG ARG ALA HIS PHE LEU GLY LEU SER LEU GLY GLY          
SEQRES   9 A  266  ILE VAL GLY GLN TRP LEU ALA LEU HIS ALA PRO GLN ARG          
SEQRES  10 A  266  ILE GLU ARG LEU VAL LEU ALA ASN THR SER ALA TRP LEU          
SEQRES  11 A  266  GLY PRO ALA ALA GLN TRP ASP GLU ARG ILE ALA ALA VAL          
SEQRES  12 A  266  LEU GLN ALA GLU ASP MSE SER GLU THR ALA ALA GLY PHE          
SEQRES  13 A  266  LEU GLY ASN TRP PHE PRO PRO ALA LEU LEU GLU ARG ALA          
SEQRES  14 A  266  GLU PRO VAL VAL GLU ARG PHE ARG ALA MSE LEU MSE ALA          
SEQRES  15 A  266  THR ASN ARG HIS GLY LEU ALA GLY SER PHE ALA ALA VAL          
SEQRES  16 A  266  ARG ASP THR ASP LEU ARG ALA GLN LEU ALA ARG ILE GLU          
SEQRES  17 A  266  ARG PRO THR LEU VAL ILE ALA GLY ALA TYR ASP THR VAL          
SEQRES  18 A  266  THR ALA ALA SER HIS GLY GLU LEU ILE ALA ALA SER ILE          
SEQRES  19 A  266  ALA GLY ALA ARG LEU VAL THR LEU PRO ALA VAL HIS LEU          
SEQRES  20 A  266  SER ASN VAL GLU PHE PRO GLN ALA PHE GLU GLY ALA VAL          
SEQRES  21 A  266  LEU SER PHE LEU GLY ALA                                      
SEQRES   1 B  266  SER ASN ALA GLY ASN LEU SER PHE LEU ALA THR SER ASP          
SEQRES   2 B  266  GLY ALA SER LEU ALA TYR ARG LEU ASP GLY ALA ALA GLU          
SEQRES   3 B  266  LYS PRO LEU LEU ALA LEU SER ASN SER ILE GLY THR THR          
SEQRES   4 B  266  LEU HIS MSE TRP ASP ALA GLN LEU PRO ALA LEU THR ARG          
SEQRES   5 B  266  HIS PHE ARG VAL LEU ARG TYR ASP ALA ARG GLY HIS GLY          
SEQRES   6 B  266  ALA SER SER VAL PRO PRO GLY PRO TYR THR LEU ALA ARG          
SEQRES   7 B  266  LEU GLY GLU ASP VAL LEU GLU LEU LEU ASP ALA LEU GLU          
SEQRES   8 B  266  VAL ARG ARG ALA HIS PHE LEU GLY LEU SER LEU GLY GLY          
SEQRES   9 B  266  ILE VAL GLY GLN TRP LEU ALA LEU HIS ALA PRO GLN ARG          
SEQRES  10 B  266  ILE GLU ARG LEU VAL LEU ALA ASN THR SER ALA TRP LEU          
SEQRES  11 B  266  GLY PRO ALA ALA GLN TRP ASP GLU ARG ILE ALA ALA VAL          
SEQRES  12 B  266  LEU GLN ALA GLU ASP MSE SER GLU THR ALA ALA GLY PHE          
SEQRES  13 B  266  LEU GLY ASN TRP PHE PRO PRO ALA LEU LEU GLU ARG ALA          
SEQRES  14 B  266  GLU PRO VAL VAL GLU ARG PHE ARG ALA MSE LEU MSE ALA          
SEQRES  15 B  266  THR ASN ARG HIS GLY LEU ALA GLY SER PHE ALA ALA VAL          
SEQRES  16 B  266  ARG ASP THR ASP LEU ARG ALA GLN LEU ALA ARG ILE GLU          
SEQRES  17 B  266  ARG PRO THR LEU VAL ILE ALA GLY ALA TYR ASP THR VAL          
SEQRES  18 B  266  THR ALA ALA SER HIS GLY GLU LEU ILE ALA ALA SER ILE          
SEQRES  19 B  266  ALA GLY ALA ARG LEU VAL THR LEU PRO ALA VAL HIS LEU          
SEQRES  20 B  266  SER ASN VAL GLU PHE PRO GLN ALA PHE GLU GLY ALA VAL          
SEQRES  21 B  266  LEU SER PHE LEU GLY ALA                                      
MODRES 3OM8 MSE A   40  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE A  147  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE A  177  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE A  179  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE B   40  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE B  147  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE B  177  MET  SELENOMETHIONINE                                   
MODRES 3OM8 MSE B  179  MET  SELENOMETHIONINE                                   
HET    MSE  A  40       8                                                       
HET    MSE  A 147       8                                                       
HET    MSE  A 177       8                                                       
HET    MSE  A 179       8                                                       
HET    MSE  B  40       8                                                       
HET    MSE  B 147       8                                                       
HET    MSE  B 177       8                                                       
HET    MSE  B 179       8                                                       
HET    MES  A 265      12                                                       
HET    EDO  A 266       4                                                       
HET    MES  B 265      12                                                       
HET    EDO  B 266       4                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     MES 2-(N-MORPHOLINO)-ETHANESULFONIC ACID                             
HETNAM     EDO 1,2-ETHANEDIOL                                                   
HETSYN     EDO ETHYLENE GLYCOL                                                  
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   3  MES    2(C6 H13 N O4 S)                                             
FORMUL   4  EDO    2(C2 H6 O2)                                                  
FORMUL   7  HOH   *118(H2 O)                                                    
HELIX    1   1 THR A   37  ALA A   43  5                                   7    
HELIX    2   2 GLN A   44  ARG A   50  1                                   7    
HELIX    3   3 THR A   73  LEU A   88  1                                  16    
HELIX    4   4 SER A   99  ALA A  112  1                                  14    
HELIX    5   5 ALA A  131  ALA A  144  1                                  14    
HELIX    6   6 MSE A  147  PHE A  159  1                                  13    
HELIX    7   7 PRO A  160  ARG A  166  1                                   7    
HELIX    8   8 GLU A  168  ALA A  180  1                                  13    
HELIX    9   9 ASN A  182  ASP A  195  1                                  14    
HELIX   10  10 GLN A  201  ILE A  205  5                                   5    
HELIX   11  11 ALA A  221  ILE A  232  1                                  12    
HELIX   12  12 LEU A  245  PHE A  250  1                                   6    
HELIX   13  13 PHE A  250  GLY A  263  1                                  14    
HELIX   14  14 THR B   37  ALA B   43  5                                   7    
HELIX   15  15 GLN B   44  ARG B   50  1                                   7    
HELIX   16  16 THR B   73  GLU B   89  1                                  17    
HELIX   17  17 SER B   99  ALA B  112  1                                  14    
HELIX   18  18 ALA B  131  ALA B  144  1                                  14    
HELIX   19  19 MSE B  147  PHE B  159  1                                  13    
HELIX   20  20 PRO B  160  ARG B  166  1                                   7    
HELIX   21  21 GLU B  168  ALA B  180  1                                  13    
HELIX   22  22 ASN B  182  ASP B  195  1                                  14    
HELIX   23  23 LEU B  198  ILE B  205  5                                   8    
HELIX   24  24 ALA B  221  ILE B  232  1                                  12    
HELIX   25  25 LEU B  245  PHE B  250  1                                   6    
HELIX   26  26 PHE B  250  GLY B  263  1                                  14    
SHEET    1   A 8 SER A   5  ALA A   8  0                                        
SHEET    2   A 8 SER A  14  ASP A  20 -1  O  LEU A  15   N  LEU A   7           
SHEET    3   A 8 ARG A  53  TYR A  57 -1  O  VAL A  54   N  ASP A  20           
SHEET    4   A 8 LEU A  27  SER A  31  1  N  LEU A  28   O  ARG A  53           
SHEET    5   A 8 ALA A  93  LEU A  98  1  O  LEU A  96   N  ALA A  29           
SHEET    6   A 8 ILE A 116  ALA A 122  1  O  VAL A 120   N  PHE A  95           
SHEET    7   A 8 THR A 209  GLY A 214  1  O  ILE A 212   N  LEU A 121           
SHEET    8   A 8 ARG A 236  LEU A 240  1  O  LEU A 240   N  ALA A 213           
SHEET    1   B 8 SER B   5  ALA B   8  0                                        
SHEET    2   B 8 SER B  14  ASP B  20 -1  O  TYR B  17   N  SER B   5           
SHEET    3   B 8 ARG B  53  TYR B  57 -1  O  VAL B  54   N  ASP B  20           
SHEET    4   B 8 LEU B  27  SER B  31  1  N  LEU B  28   O  ARG B  53           
SHEET    5   B 8 ALA B  93  LEU B  98  1  O  LEU B  96   N  ALA B  29           
SHEET    6   B 8 ILE B 116  ALA B 122  1  O  GLU B 117   N  ALA B  93           
SHEET    7   B 8 THR B 209  GLY B 214  1  O  LEU B 210   N  LEU B 119           
SHEET    8   B 8 ARG B 236  LEU B 240  1  O  VAL B 238   N  VAL B 211           
LINK         C   HIS A  39                 N   MSE A  40     1555   1555  1.33  
LINK         C   MSE A  40                 N   TRP A  41     1555   1555  1.33  
LINK         C   ASP A 146                 N   MSE A 147     1555   1555  1.33  
LINK         C   MSE A 147                 N   SER A 148     1555   1555  1.33  
LINK         C   ALA A 176                 N   MSE A 177     1555   1555  1.33  
LINK         C   MSE A 177                 N   LEU A 178     1555   1555  1.33  
LINK         C   LEU A 178                 N   MSE A 179     1555   1555  1.33  
LINK         C   MSE A 179                 N   ALA A 180     1555   1555  1.33  
LINK         C   HIS B  39                 N   MSE B  40     1555   1555  1.33  
LINK         C   MSE B  40                 N   TRP B  41     1555   1555  1.33  
LINK         C   ASP B 146                 N   MSE B 147     1555   1555  1.33  
LINK         C   MSE B 147                 N   SER B 148     1555   1555  1.33  
LINK         C   ALA B 176                 N   MSE B 177     1555   1555  1.33  
LINK         C   MSE B 177                 N   LEU B 178     1555   1555  1.33  
LINK         C   LEU B 178                 N   MSE B 179     1555   1555  1.33  
LINK         C   MSE B 179                 N   ALA B 180     1555   1555  1.33  
CISPEP   1 GLY A   70    PRO A   71          0        -2.66                     
CISPEP   2 GLY A  129    PRO A  130          0        -2.68                     
CISPEP   3 GLY B   70    PRO B   71          0        -0.55                     
CISPEP   4 GLY B  129    PRO B  130          0         0.54                     
SITE     1 AC1  6 ASP A 195  THR A 196  ASP A 197  LEU A 198                    
SITE     2 AC1  6 GLN A 201  HOH A 322                                          
SITE     1 AC2  4 SER A  33  ILE A  34  SER A  99  LEU A 100                    
SITE     1 AC3  5 ASP B 195  THR B 196  ASP B 197  LEU B 198                    
SITE     2 AC3  5 GLN B 201                                                     
SITE     1 AC4  5 SER B  33  ILE B  34  SER B  99  LEU B 100                    
SITE     2 AC4  5 LEU B 128                                                     
CRYST1   91.529   91.529  283.745  90.00  90.00  90.00 P 41 21 2    16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010925  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010925  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.003524        0.00000                         
TER    1998      ALA A 264                                                      
TER    4004      ALA B 264                                                      
MASTER      357    0   12   26   16    0    7    6 4136    2  112   42          
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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