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LongText Report for: 3QMV-pdb

Name Class
3QMV-pdb
HEADER    HYDROLASE                               05-FEB-11   3QMV              
TITLE     REDJ-THIOESTERASE FROM THE PRODIGININE BIOSYNTHETIC PATHWAY IN        
TITLE    2 STREPTOMYCES COELICOLOR                                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THIOESTERASE;                                              
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 FRAGMENT: UNP RESIDUES 6-261;                                        
COMPND   5 SYNONYM: REDJ;                                                       
COMPND   6 EC: 3.1.2.-;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STREPTOMYCES COELICOLOR;                        
SOURCE   3 ORGANISM_TAXID: 1902;                                                
SOURCE   4 GENE: SCO5894, SC3F7.14;                                             
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ALPHA/BETA HYDROLASE FOLD, HYDROLASE                                  
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.R.WHICHER,J.L.SMITH                                                 
REVDAT   1   04-MAY-11 3QMV    0                                                
JRNL        AUTH   J.R.WHICHER,G.FLOROVA,P.K.SYDOR,R.SINGH,M.ALHAMADSHEH,       
JRNL        AUTH 2 G.L.CHALLIS,K.A.REYNOLDS,J.L.SMITH                           
JRNL        TITL   STRUCTURE AND FUNCTION OF REDJ, A THIOESTERASE FROM THE      
JRNL        TITL 2 PRODIGININE BIOSYNTHETIC PATHWAY IN STREPTOMYCES COELICOLOR  
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.12 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                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.12                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 50.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 57954                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.201                           
REMARK   3   FREE R VALUE                     : 0.249                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2945                            
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) : 2.12                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.17                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3814                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 93.47                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2420                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 192                          
REMARK   3   BIN FREE R VALUE                    : 0.2960                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 8088                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 452                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 26.21                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.10000                                             
REMARK   3    B22 (A**2) : -1.97000                                             
REMARK   3    B33 (A**2) : 3.07000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.75000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.280         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.213         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.954                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.926                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  8425 ; 0.012 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  5959 ; 0.000 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES): 11507 ; 1.241 ; 1.969       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 14216 ; 4.027 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):  1045 ; 5.387 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   413 ;25.361 ;20.775       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1216 ;13.468 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):   125 ;14.997 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1209 ; 0.075 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  9627 ; 0.006 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  1946 ; 0.005 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  5235 ; 0.678 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2058 ; 0.000 ; 1.500       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  8390 ; 1.271 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  3190 ; 1.670 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  3117 ; 2.762 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
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  : NULL                                       
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:                                           
REMARK   3  HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS                   
REMARK   3  U VALUES      : REFINED INDIVIDUALLY                                
REMARK   4                                                                      
REMARK   4 3QMV COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-FEB-11.                  
REMARK 100 THE RCSB ID CODE IS RCSB063844.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-AUG-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 23-ID-D                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9794                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 300 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 57954                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.120                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 7.700                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08900                            
REMARK 200   FOR THE DATA SET  : 22.1200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.12                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.20                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.50                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.42000                            
REMARK 200   FOR SHELL         : 5.200                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.07                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 12% PEG2000, 0.7 M SODIUM CHLORIDE, 2    
REMARK 280  MM DTT, 0.1 M HEPES, PH 7.6, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 293K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       39.69950            
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 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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4200 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23010 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, C                                  
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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4300 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23190 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, D                                  
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     MSE A   -18                                                      
REMARK 465     HIS A   -17                                                      
REMARK 465     HIS A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     SER A   -11                                                      
REMARK 465     SER A   -10                                                      
REMARK 465     GLY A    -9                                                      
REMARK 465     VAL A    -8                                                      
REMARK 465     ASP A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     GLY A    -5                                                      
REMARK 465     THR A    -4                                                      
REMARK 465     GLU A    -3                                                      
REMARK 465     ASN A    -2                                                      
REMARK 465     LEU A    -1                                                      
REMARK 465     TYR A     0                                                      
REMARK 465     PHE A     1                                                      
REMARK 465     GLN A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     ASN A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     LEU A     6                                                      
REMARK 465     LEU A     7                                                      
REMARK 465     SER A     8                                                      
REMARK 465     ASP A   167                                                      
REMARK 465     ALA A   168                                                      
REMARK 465     ASP A   169                                                      
REMARK 465     THR A   170                                                      
REMARK 465     LEU A   171                                                      
REMARK 465     GLY A   172                                                      
REMARK 465     ALA A   173                                                      
REMARK 465     ALA A   174                                                      
REMARK 465     TYR A   175                                                      
REMARK 465     MSE B   -18                                                      
REMARK 465     HIS B   -17                                                      
REMARK 465     HIS B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     SER B   -11                                                      
REMARK 465     SER B   -10                                                      
REMARK 465     GLY B    -9                                                      
REMARK 465     VAL B    -8                                                      
REMARK 465     ASP B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     GLY B    -5                                                      
REMARK 465     THR B    -4                                                      
REMARK 465     GLU B    -3                                                      
REMARK 465     ASN B    -2                                                      
REMARK 465     LEU B    -1                                                      
REMARK 465     TYR B     0                                                      
REMARK 465     PHE B     1                                                      
REMARK 465     GLN B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     ASN B     4                                                      
REMARK 465     ALA B     5                                                      
REMARK 465     LEU B     6                                                      
REMARK 465     LEU B     7                                                      
REMARK 465     MSE C   -18                                                      
REMARK 465     HIS C   -17                                                      
REMARK 465     HIS C   -16                                                      
REMARK 465     HIS C   -15                                                      
REMARK 465     HIS C   -14                                                      
REMARK 465     HIS C   -13                                                      
REMARK 465     HIS C   -12                                                      
REMARK 465     SER C   -11                                                      
REMARK 465     SER C   -10                                                      
REMARK 465     GLY C    -9                                                      
REMARK 465     VAL C    -8                                                      
REMARK 465     ALA C    23                                                      
REMARK 465     MSE D   -18                                                      
REMARK 465     HIS D   -17                                                      
REMARK 465     HIS D   -16                                                      
REMARK 465     HIS D   -15                                                      
REMARK 465     HIS D   -14                                                      
REMARK 465     HIS D   -13                                                      
REMARK 465     HIS D   -12                                                      
REMARK 465     SER D   -11                                                      
REMARK 465     SER D   -10                                                      
REMARK 465     GLY D    -9                                                      
REMARK 465     VAL D    -8                                                      
REMARK 465     PRO D    21                                                      
REMARK 465     ALA D    22                                                      
REMARK 465     ALA D    23                                                      
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    SER A 107     -124.71     58.61                                   
REMARK 500    SER B 107     -119.36     57.72                                   
REMARK 500    SER C 107     -121.19     59.11                                   
REMARK 500    SER D 107     -120.72     60.66                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH C 274        DISTANCE =  5.10 ANGSTROMS                       
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3QMW   RELATED DB: PDB                                   
REMARK 900 STRUCTURE OF REDJ WITH PEG BOUND IN THE ACTIVE SITE.                 
DBREF  3QMV A    6   261  UNP    O54157   O54157_STRCO     6    261             
DBREF  3QMV B    6   261  UNP    O54157   O54157_STRCO     6    261             
DBREF  3QMV C    6   261  UNP    O54157   O54157_STRCO     6    261             
DBREF  3QMV D    6   261  UNP    O54157   O54157_STRCO     6    261             
SEQADV 3QMV MSE A  -18  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS A  -17  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS A  -16  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS A  -15  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS A  -14  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS A  -13  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS A  -12  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER A  -11  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER A  -10  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY A   -9  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV VAL A   -8  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASP A   -7  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU A   -6  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY A   -5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV THR A   -4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLU A   -3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN A   -2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU A   -1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV TYR A    0  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV PHE A    1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLN A    2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER A    3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN A    4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ALA A    5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV MSE B  -18  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS B  -17  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS B  -16  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS B  -15  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS B  -14  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS B  -13  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS B  -12  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER B  -11  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER B  -10  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY B   -9  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV VAL B   -8  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASP B   -7  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU B   -6  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY B   -5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV THR B   -4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLU B   -3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN B   -2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU B   -1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV TYR B    0  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV PHE B    1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLN B    2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER B    3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN B    4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ALA B    5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV MSE C  -18  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS C  -17  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS C  -16  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS C  -15  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS C  -14  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS C  -13  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS C  -12  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER C  -11  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER C  -10  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY C   -9  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV VAL C   -8  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASP C   -7  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU C   -6  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY C   -5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV THR C   -4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLU C   -3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN C   -2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU C   -1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV TYR C    0  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV PHE C    1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLN C    2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER C    3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN C    4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ALA C    5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV MSE D  -18  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS D  -17  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS D  -16  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS D  -15  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS D  -14  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS D  -13  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV HIS D  -12  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER D  -11  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER D  -10  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY D   -9  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV VAL D   -8  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASP D   -7  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU D   -6  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLY D   -5  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV THR D   -4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLU D   -3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN D   -2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV LEU D   -1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV TYR D    0  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV PHE D    1  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV GLN D    2  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV SER D    3  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ASN D    4  UNP  O54157              EXPRESSION TAG                 
SEQADV 3QMV ALA D    5  UNP  O54157              EXPRESSION TAG                 
SEQRES   1 A  280  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 A  280  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU          
SEQRES   3 A  280  SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA          
SEQRES   4 A  280  PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU          
SEQRES   5 A  280  ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER          
SEQRES   6 A  280  ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL          
SEQRES   7 A  280  ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG          
SEQRES   8 A  280  LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA          
SEQRES   9 A  280  GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR          
SEQRES  10 A  280  HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU          
SEQRES  11 A  280  LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY          
SEQRES  12 A  280  ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG          
SEQRES  13 A  280  ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU          
SEQRES  14 A  280  SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY          
SEQRES  15 A  280  GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE          
SEQRES  16 A  280  ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA          
SEQRES  17 A  280  CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP          
SEQRES  18 A  280  CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE          
SEQRES  19 A  280  ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR          
SEQRES  20 A  280  THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS          
SEQRES  21 A  280  PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU          
SEQRES  22 A  280  ALA HIS LEU GLY THR GLU LEU                                  
SEQRES   1 B  280  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 B  280  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU          
SEQRES   3 B  280  SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA          
SEQRES   4 B  280  PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU          
SEQRES   5 B  280  ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER          
SEQRES   6 B  280  ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL          
SEQRES   7 B  280  ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG          
SEQRES   8 B  280  LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA          
SEQRES   9 B  280  GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR          
SEQRES  10 B  280  HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU          
SEQRES  11 B  280  LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY          
SEQRES  12 B  280  ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG          
SEQRES  13 B  280  ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU          
SEQRES  14 B  280  SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY          
SEQRES  15 B  280  GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE          
SEQRES  16 B  280  ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA          
SEQRES  17 B  280  CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP          
SEQRES  18 B  280  CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE          
SEQRES  19 B  280  ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR          
SEQRES  20 B  280  THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS          
SEQRES  21 B  280  PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU          
SEQRES  22 B  280  ALA HIS LEU GLY THR GLU LEU                                  
SEQRES   1 C  280  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 C  280  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU          
SEQRES   3 C  280  SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA          
SEQRES   4 C  280  PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU          
SEQRES   5 C  280  ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER          
SEQRES   6 C  280  ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL          
SEQRES   7 C  280  ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG          
SEQRES   8 C  280  LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA          
SEQRES   9 C  280  GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR          
SEQRES  10 C  280  HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU          
SEQRES  11 C  280  LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY          
SEQRES  12 C  280  ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG          
SEQRES  13 C  280  ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU          
SEQRES  14 C  280  SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY          
SEQRES  15 C  280  GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE          
SEQRES  16 C  280  ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA          
SEQRES  17 C  280  CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP          
SEQRES  18 C  280  CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE          
SEQRES  19 C  280  ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR          
SEQRES  20 C  280  THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS          
SEQRES  21 C  280  PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU          
SEQRES  22 C  280  ALA HIS LEU GLY THR GLU LEU                                  
SEQRES   1 D  280  MSE HIS HIS HIS HIS HIS HIS SER SER GLY VAL ASP LEU          
SEQRES   2 D  280  GLY THR GLU ASN LEU TYR PHE GLN SER ASN ALA LEU LEU          
SEQRES   3 D  280  SER GLN ARG SER ALA TRP PHE PRO ARG PRO VAL ALA ALA          
SEQRES   4 D  280  PRO ALA ALA GLU PRO PRO ASP PRO ALA ALA ALA PRO LEU          
SEQRES   5 D  280  ARG LEU VAL CYS PHE PRO TYR ALA GLY GLY THR VAL SER          
SEQRES   6 D  280  ALA PHE ARG GLY TRP GLN GLU ARG LEU GLY ASP GLU VAL          
SEQRES   7 D  280  ALA VAL VAL PRO VAL GLN LEU PRO GLY ARG GLY LEU ARG          
SEQRES   8 D  280  LEU ARG GLU ARG PRO TYR ASP THR MSE GLU PRO LEU ALA          
SEQRES   9 D  280  GLU ALA VAL ALA ASP ALA LEU GLU GLU HIS ARG LEU THR          
SEQRES  10 D  280  HIS ASP TYR ALA LEU PHE GLY HIS SER MSE GLY ALA LEU          
SEQRES  11 D  280  LEU ALA TYR GLU VAL ALA CYS VAL LEU ARG ARG ARG GLY          
SEQRES  12 D  280  ALA PRO ARG PRO ARG HIS LEU PHE VAL SER GLY SER ARG          
SEQRES  13 D  280  ALA PRO HIS LEU TYR GLY ASP ARG ALA ASP HIS THR LEU          
SEQRES  14 D  280  SER ASP THR ALA LEU ARG GLU VAL ILE ARG ASP LEU GLY          
SEQRES  15 D  280  GLY LEU ASP ASP ALA ASP THR LEU GLY ALA ALA TYR PHE          
SEQRES  16 D  280  ASP ARG ARG LEU PRO VAL LEU ARG ALA ASP LEU ARG ALA          
SEQRES  17 D  280  CYS GLU ARG TYR ASP TRP HIS PRO ARG PRO PRO LEU ASP          
SEQRES  18 D  280  CYS PRO THR THR ALA PHE SER ALA ALA ALA ASP PRO ILE          
SEQRES  19 D  280  ALA THR PRO GLU MSE VAL GLU ALA TRP ARG PRO TYR THR          
SEQRES  20 D  280  THR GLY SER PHE LEU ARG ARG HIS LEU PRO GLY ASN HIS          
SEQRES  21 D  280  PHE PHE LEU ASN GLY GLY PRO SER ARG ASP ARG LEU LEU          
SEQRES  22 D  280  ALA HIS LEU GLY THR GLU LEU                                  
MODRES 3QMV MSE A   81  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE A  108  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE A  220  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE B   81  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE B  108  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE B  220  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE C   81  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE C  108  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE C  220  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE D   81  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE D  108  MET  SELENOMETHIONINE                                   
MODRES 3QMV MSE D  220  MET  SELENOMETHIONINE                                   
HET    MSE  A  81       8                                                       
HET    MSE  A 108       8                                                       
HET    MSE  A 220       8                                                       
HET    MSE  B  81       8                                                       
HET    MSE  B 108       8                                                       
HET    MSE  B 220       8                                                       
HET    MSE  C  81       8                                                       
HET    MSE  C 108       8                                                       
HET    MSE  C 220       8                                                       
HET    MSE  D  81       8                                                       
HET    MSE  D 108       8                                                       
HET    MSE  D 220       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    12(C5 H11 N O2 SE)                                           
FORMUL   5  HOH   *452(H2 O)                                                    
HELIX    1   1 GLN A    9  PHE A   14  1                                   6    
HELIX    2   2 THR A   44  ARG A   49  5                                   6    
HELIX    3   3 GLY A   50  GLY A   56  1                                   7    
HELIX    4   4 ARG A   69  LEU A   73  5                                   5    
HELIX    5   5 THR A   80  HIS A   95  1                                  16    
HELIX    6   6 SER A  107  ARG A  123  1                                  17    
HELIX    7   7 ALA A  138  TYR A  142  5                                   5    
HELIX    8   8 ALA A  146  LEU A  150  5                                   5    
HELIX    9   9 SER A  151  GLY A  163  1                                  13    
HELIX   10  10 ARG A  179  ARG A  192  1                                  14    
HELIX   11  11 THR A  217  ALA A  223  1                                   7    
HELIX   12  12 TRP A  224  THR A  228  5                                   5    
HELIX   13  13 PHE A  242  GLY A  246  5                                   5    
HELIX   14  14 GLY A  247  THR A  259  1                                  13    
HELIX   15  15 GLN B    9  PHE B   14  1                                   6    
HELIX   16  16 THR B   44  ARG B   49  5                                   6    
HELIX   17  17 GLY B   50  GLY B   56  1                                   7    
HELIX   18  18 ARG B   69  LEU B   73  5                                   5    
HELIX   19  19 THR B   80  HIS B   95  1                                  16    
HELIX   20  20 SER B  107  ARG B  123  1                                  17    
HELIX   21  21 ALA B  138  TYR B  142  5                                   5    
HELIX   22  22 ALA B  146  LEU B  150  5                                   5    
HELIX   23  23 SER B  151  GLY B  163  1                                  13    
HELIX   24  24 ASP B  167  THR B  170  5                                   4    
HELIX   25  25 LEU B  171  ARG B  192  1                                  22    
HELIX   26  26 THR B  217  ALA B  223  1                                   7    
HELIX   27  27 TRP B  224  THR B  228  5                                   5    
HELIX   28  28 PHE B  242  ASN B  245  5                                   4    
HELIX   29  29 GLY B  246  LEU B  261  1                                  16    
HELIX   30  30 GLY C   -5  LEU C   -1  5                                   5    
HELIX   31  31 ASN C    4  SER C    8  5                                   5    
HELIX   32  32 GLN C    9  PHE C   14  1                                   6    
HELIX   33  33 THR C   44  ARG C   49  5                                   6    
HELIX   34  34 GLY C   50  GLY C   56  1                                   7    
HELIX   35  35 ARG C   69  LEU C   73  5                                   5    
HELIX   36  36 THR C   80  HIS C   95  1                                  16    
HELIX   37  37 SER C  107  ARG C  123  1                                  17    
HELIX   38  38 ALA C  138  TYR C  142  5                                   5    
HELIX   39  39 ALA C  146  LEU C  150  5                                   5    
HELIX   40  40 SER C  151  GLY C  163  1                                  13    
HELIX   41  41 ASP C  167  GLY C  172  1                                   6    
HELIX   42  42 ALA C  173  ARG C  178  1                                   6    
HELIX   43  43 ARG C  179  ARG C  192  1                                  14    
HELIX   44  44 THR C  217  ALA C  223  1                                   7    
HELIX   45  45 TRP C  224  THR C  228  5                                   5    
HELIX   46  46 PHE C  242  GLY C  246  5                                   5    
HELIX   47  47 GLY C  247  LEU C  261  1                                  15    
HELIX   48  48 GLY D   -5  LEU D   -1  5                                   5    
HELIX   49  49 ALA D    5  SER D    8  5                                   4    
HELIX   50  50 GLN D    9  PHE D   14  1                                   6    
HELIX   51  51 THR D   44  ARG D   49  5                                   6    
HELIX   52  52 GLY D   50  GLY D   56  1                                   7    
HELIX   53  53 ARG D   69  LEU D   73  5                                   5    
HELIX   54  54 THR D   80  HIS D   95  1                                  16    
HELIX   55  55 SER D  107  ARG D  123  1                                  17    
HELIX   56  56 ALA D  138  TYR D  142  5                                   5    
HELIX   57  57 ALA D  146  LEU D  150  5                                   5    
HELIX   58  58 SER D  151  GLY D  163  1                                  13    
HELIX   59  59 ASP D  167  GLY D  172  1                                   6    
HELIX   60  60 GLY D  172  ARG D  178  1                                   7    
HELIX   61  61 ARG D  179  ARG D  192  1                                  14    
HELIX   62  62 THR D  217  ALA D  223  1                                   7    
HELIX   63  63 TRP D  224  THR D  228  5                                   5    
HELIX   64  64 PHE D  242  GLY D  246  5                                   5    
HELIX   65  65 GLY D  247  GLU D  260  1                                  14    
SHEET    1   A 6 VAL A  59  PRO A  63  0                                        
SHEET    2   A 6 LEU A  33  PHE A  38  1  N  LEU A  35   O  ALA A  60           
SHEET    3   A 6 TYR A 101  HIS A 106  1  O  ALA A 102   N  VAL A  36           
SHEET    4   A 6 LEU A 131  SER A 134  1  O  PHE A 132   N  LEU A 103           
SHEET    5   A 6 THR A 205  ALA A 212  1  O  THR A 206   N  LEU A 131           
SHEET    6   A 6 PHE A 232  ASN A 240  1  O  LEU A 237   N  SER A 209           
SHEET    1   B 6 ALA B  60  PRO B  63  0                                        
SHEET    2   B 6 ARG B  34  PHE B  38  1  N  LEU B  35   O  VAL B  62           
SHEET    3   B 6 TYR B 101  HIS B 106  1  O  ALA B 102   N  VAL B  36           
SHEET    4   B 6 LEU B 131  SER B 134  1  O  PHE B 132   N  LEU B 103           
SHEET    5   B 6 THR B 205  ALA B 212  1  O  PHE B 208   N  VAL B 133           
SHEET    6   B 6 PHE B 232  ASN B 240  1  O  LEU B 237   N  SER B 209           
SHEET    1   C 6 VAL C  59  PRO C  63  0                                        
SHEET    2   C 6 LEU C  33  PHE C  38  1  N  LEU C  35   O  VAL C  62           
SHEET    3   C 6 TYR C 101  HIS C 106  1  O  ALA C 102   N  VAL C  36           
SHEET    4   C 6 LEU C 131  SER C 134  1  O  PHE C 132   N  LEU C 103           
SHEET    5   C 6 THR C 205  ALA C 210  1  O  THR C 206   N  LEU C 131           
SHEET    6   C 6 PHE C 232  LEU C 237  1  O  LEU C 233   N  ALA C 207           
SHEET    1   D 6 VAL D  59  PRO D  63  0                                        
SHEET    2   D 6 LEU D  33  PHE D  38  1  N  LEU D  35   O  VAL D  62           
SHEET    3   D 6 TYR D 101  HIS D 106  1  O  PHE D 104   N  VAL D  36           
SHEET    4   D 6 LEU D 131  SER D 134  1  O  PHE D 132   N  LEU D 103           
SHEET    5   D 6 THR D 205  ALA D 210  1  O  THR D 206   N  LEU D 131           
SHEET    6   D 6 PHE D 232  LEU D 237  1  O  LEU D 233   N  ALA D 207           
LINK         C   THR A  80                 N   MSE A  81     1555   1555  1.33  
LINK         C   MSE A  81                 N   GLU A  82     1555   1555  1.33  
LINK         C  ASER A 107                 N   MSE A 108     1555   1555  1.31  
LINK         C  BSER A 107                 N   MSE A 108     1555   1555  1.31  
LINK         C   MSE A 108                 N   GLY A 109     1555   1555  1.33  
LINK         C   GLU A 219                 N   MSE A 220     1555   1555  1.33  
LINK         C   MSE A 220                 N   VAL A 221     1555   1555  1.33  
LINK         C   THR B  80                 N   MSE B  81     1555   1555  1.33  
LINK         C   MSE B  81                 N   GLU B  82     1555   1555  1.34  
LINK         C  ASER B 107                 N   MSE B 108     1555   1555  1.31  
LINK         C  BSER B 107                 N   MSE B 108     1555   1555  1.31  
LINK         C   MSE B 108                 N   GLY B 109     1555   1555  1.33  
LINK         C   GLU B 219                 N   MSE B 220     1555   1555  1.33  
LINK         C   MSE B 220                 N   VAL B 221     1555   1555  1.34  
LINK         C   THR C  80                 N   MSE C  81     1555   1555  1.33  
LINK         C   MSE C  81                 N   GLU C  82     1555   1555  1.33  
LINK         C   SER C 107                 N   MSE C 108     1555   1555  1.32  
LINK         C   MSE C 108                 N   GLY C 109     1555   1555  1.32  
LINK         C   GLU C 219                 N   MSE C 220     1555   1555  1.33  
LINK         C   MSE C 220                 N   VAL C 221     1555   1555  1.33  
LINK         C   THR D  80                 N   MSE D  81     1555   1555  1.34  
LINK         C   MSE D  81                 N   GLU D  82     1555   1555  1.33  
LINK         C  ASER D 107                 N   MSE D 108     1555   1555  1.31  
LINK         C  BSER D 107                 N   MSE D 108     1555   1555  1.31  
LINK         C   MSE D 108                 N   GLY D 109     1555   1555  1.34  
LINK         C   GLU D 219                 N   MSE D 220     1555   1555  1.33  
LINK         C   MSE D 220                 N   VAL D 221     1555   1555  1.33  
CISPEP   1 GLU C   24    PRO C   25          0        16.67                     
CISPEP   2 GLU D   24    PRO D   25          0        -3.83                     
CRYST1   74.813   79.399   87.438  90.00  90.12  90.00 P 1 21 1      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      0.013367  0.000000  0.000029        0.00000                         
SCALE2      0.000000  0.012595  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011437        0.00000                         
TER    1944      LEU A 261                                                      
TER    3947      LEU B 261                                                      
TER    6075      LEU C 261                                                      
TER    8180      LEU D 261                                                      
MASTER      372    0   12   65   24    0    0    6 8540    4  123   88          
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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