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Database: PDB
Entry: 1QWX
LinkDB: 1QWX
Original site: 1QWX 
HEADER    CHAPERONE                               03-SEP-03   1QWX              
TITLE     CRYSTAL STRUCTURE OF A STAPHYLOCOCCAL INHIBITOR/CHAPERONE             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CYSTEINE PROTEASE;                                         
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: STAPHYLOCOCCUS AUREUS SUBSP. AUREUS;            
SOURCE   3 ORGANISM_TAXID: 196620;                                              
SOURCE   4 STRAIN: MW2;                                                         
SOURCE   5 GENE: SSPC;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    BETA BARREL, CHAPERONE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    C.K.BROWN,Z.-Y.GU,N.NICKERSON,M.J.MCGAVIN,D.H.OHLENDORF,C.A.EARHART   
REVDAT   4   12-MAR-14 1QWX    1       REMARK                                   
REVDAT   3   13-JUL-11 1QWX    1       VERSN                                    
REVDAT   2   24-FEB-09 1QWX    1       VERSN                                    
REVDAT   1   10-FEB-04 1QWX    0                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.50 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
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) : 1.50                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 62.02                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 3.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 42519                          
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) : 0.202                           
REMARK   3   R VALUE            (WORKING SET) : 0.200                           
REMARK   3   FREE R VALUE                     : 0.221                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2241                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.50                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.54                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3050                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2580                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 176                          
REMARK   3   BIN FREE R VALUE                    : 0.3140                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1802                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 267                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   B VALUE TYPE : LIKELY RESIDUAL                                     
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 22.16                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.57000                                             
REMARK   3    B22 (A**2) : 0.39000                                              
REMARK   3    B33 (A**2) : 0.18000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.075         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.075         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.045         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 1.174         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.949                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1842 ; 0.018 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2492 ; 1.423 ; 1.913       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   214 ; 5.778 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   278 ; 0.101 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1400 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   728 ; 0.207 ; 0.200       
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):   173 ; 0.154 ; 0.200       
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):    47 ; 0.216 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    27 ; 0.152 ; 0.200       
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):  1074 ; 1.044 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1754 ; 2.057 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   768 ; 3.053 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   738 ; 4.944 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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  : 2                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A   108                          
REMARK   3    ORIGIN FOR THE GROUP (A):  31.6492  33.3169  68.7065              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0157 T22:   0.0166                                     
REMARK   3      T33:   0.0165 T12:  -0.0095                                     
REMARK   3      T13:   0.0038 T23:  -0.0086                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5420 L22:   0.4317                                     
REMARK   3      L33:   0.4890 L12:  -0.1291                                     
REMARK   3      L13:   0.1956 L23:   0.0158                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0089 S12:   0.0020 S13:   0.0300                       
REMARK   3      S21:   0.0168 S22:  -0.0182 S23:  -0.0117                       
REMARK   3      S31:   0.0055 S32:  -0.0238 S33:   0.0093                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     1        B   108                          
REMARK   3    ORIGIN FOR THE GROUP (A):  38.6449  35.3818  41.2011              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0161 T22:   0.0166                                     
REMARK   3      T33:   0.0125 T12:   0.0028                                     
REMARK   3      T13:   0.0134 T23:   0.0070                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4578 L22:   0.7251                                     
REMARK   3      L33:   0.7101 L12:   0.2768                                     
REMARK   3      L13:   0.0110 L23:   0.0285                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0423 S12:  -0.0130 S13:  -0.0112                       
REMARK   3      S21:   0.0613 S22:  -0.0562 S23:   0.0470                       
REMARK   3      S31:  -0.0326 S32:   0.0614 S33:   0.0139                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH 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: NULL                                      
REMARK   4                                                                      
REMARK   4 1QWX COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-SEP-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB020167.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-MAR-03                          
REMARK 200  TEMPERATURE           (KELVIN) : 113                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X25                                
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.99876                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 4                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 42519                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.500                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 60.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : 6.000                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SOLVE, MAID                                           
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: VAPOR DIFFUSION, HANGING DROP            
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-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       17.22000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       50.99500            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.95500            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       50.99500            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       17.22000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.95500            
REMARK 290   SMTRY3   4  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: MONOMERIC                         
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: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
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     VAL A   109                                                      
REMARK 465     VAL B   109                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OD1  ASP A    71     O    HOH A   190              1.63            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    MSE A  89  SE     MSE A  89   CE     -0.408                       
REMARK 500    MSE B  89  SE     MSE B  89   CE     -0.358                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP A  46   CB  -  CG  -  OD2 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    ASP A  83   CB  -  CG  -  OD2 ANGL. DEV. =   6.0 DEGREES          
REMARK 500    ASP B  71   CB  -  CG  -  OD2 ANGL. DEV. =   5.6 DEGREES          
REMARK 500    ASP B  80   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ASP B  82   CB  -  CG  -  OD2 ANGL. DEV. =   5.8 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  46     -165.44   -160.08                                   
REMARK 500    ASP A  82      -62.32   -108.29                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CHIRAL CENTERS                                             
REMARK 500                                                                      
REMARK 500 UNEXPECTED CONFIGURATION OF THE FOLLOWING CHIRAL                     
REMARK 500 CENTER(S) USING IMPROPER CA--C--CB--N CHIRALITY                      
REMARK 500 FOR AMINO ACIDS AND C1'--O4'--N1(N9)--C2' FOR                        
REMARK 500 NUCLEIC ACIDS OR EQUIVALENT ANGLE                                    
REMARK 500 M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN                            
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE                   
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,6X,F5.1,6X,A1,10X,A1,3X,A16)       
REMARK 500                                                                      
REMARK 500  M RES CSSEQI    IMPROPER   EXPECTED   FOUND DETAILS                 
REMARK 500    THR B  22        24.9      L          L   OUTSIDE RANGE           
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 B 151        DISTANCE =  5.40 ANGSTROMS                       
DBREF  1QWX A    1   109  UNP    Q7A189   SSPC_STAAW       1    109             
DBREF  1QWX B    1   109  UNP    Q7A189   SSPC_STAAW       1    109             
SEQADV 1QWX MSE A   28  UNP  Q7A189    ILE    28 CONFLICT                       
SEQADV 1QWX MSE B   28  UNP  Q7A189    ILE    28 CONFLICT                       
SEQRES   1 A  109  MSE TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR ASP THR          
SEQRES   2 A  109  THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE ASN LEU          
SEQRES   3 A  109  PHE MSE GLY ASN TRP SER ASN HIS GLN LEU GLN LYS SER          
SEQRES   4 A  109  ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS ASN GLN          
SEQRES   5 A  109  TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN ARG ILE          
SEQRES   6 A  109  LYS PHE SER SER ILE ASP ASN GLU GLU ILE ILE TYR ILE          
SEQRES   7 A  109  LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MSE GLN THR          
SEQRES   8 A  109  SER SER LYS GLN GLY ILE GLY THR SER ARG PRO ILE VAL          
SEQRES   9 A  109  TYR GLU ARG LEU VAL                                          
SEQRES   1 B  109  MSE TYR GLN LEU GLN PHE ILE ASN LEU VAL TYR ASP THR          
SEQRES   2 B  109  THR LYS LEU THR HIS LEU GLU GLN THR ASN ILE ASN LEU          
SEQRES   3 B  109  PHE MSE GLY ASN TRP SER ASN HIS GLN LEU GLN LYS SER          
SEQRES   4 B  109  ILE CYS ILE ARG HIS GLY ASP ASP THR SER HIS ASN GLN          
SEQRES   5 B  109  TYR HIS ILE LEU PHE ILE ASP THR ALA HIS GLN ARG ILE          
SEQRES   6 B  109  LYS PHE SER SER ILE ASP ASN GLU GLU ILE ILE TYR ILE          
SEQRES   7 B  109  LEU ASP TYR ASP ASP THR GLN HIS ILE LEU MSE GLN THR          
SEQRES   8 B  109  SER SER LYS GLN GLY ILE GLY THR SER ARG PRO ILE VAL          
SEQRES   9 B  109  TYR GLU ARG LEU VAL                                          
MODRES 1QWX MSE A    1  MET  SELENOMETHIONINE                                   
MODRES 1QWX MSE A   28  MET  SELENOMETHIONINE                                   
MODRES 1QWX MSE A   89  MET  SELENOMETHIONINE                                   
MODRES 1QWX MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1QWX MSE B   28  MET  SELENOMETHIONINE                                   
MODRES 1QWX MSE B   89  MET  SELENOMETHIONINE                                   
HET    MSE  A   1       8                                                       
HET    MSE  A  28       8                                                       
HET    MSE  A  89       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B  28       8                                                       
HET    MSE  B  89       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    6(C5 H11 N O2 SE)                                            
FORMUL   3  HOH   *267(H2 O)                                                    
HELIX    1   1 ASP A   12  LEU A   16  5                                   5    
HELIX    2   2 THR A   17  LEU A   26  1                                  10    
HELIX    3   3 ASP B   12  LEU B   16  5                                   5    
HELIX    4   4 THR B   17  LEU B   26  1                                  10    
SHEET    1   A18 TYR A   2  VAL A  10  0                                        
SHEET    2   A18 LYS A  38  HIS A  44  1  O  SER A  39   N  GLN A   3           
SHEET    3   A18 GLY A  29  ASN A  33 -1  N  GLY A  29   O  ILE A  42           
SHEET    4   A18 ILE A 103  ARG A 107 -1  O  GLU A 106   N  SER A  32           
SHEET    5   A18 HIS A  86  SER A  93 -1  N  ILE A  87   O  TYR A 105           
SHEET    6   A18 ASN A  72  ASP A  83 -1  N  ILE A  76   O  SER A  92           
SHEET    7   A18 ARG A  64  SER A  69 -1  N  PHE A  67   O  TYR A  77           
SHEET    8   A18 GLN A  52  ASP A  59 -1  N  ASP A  59   O  ARG A  64           
SHEET    9   A18 TYR A   2  VAL A  10  1  N  VAL A  10   O  TYR A  53           
SHEET   10   A18 TYR B   2  VAL B  10 -1  O  LEU B   4   N  TYR A   2           
SHEET   11   A18 GLN B  52  ASP B  59  1  O  TYR B  53   N  VAL B  10           
SHEET   12   A18 ARG B  64  SER B  69 -1  O  SER B  68   N  HIS B  54           
SHEET   13   A18 ASN B  72  ASP B  83 -1  O  TYR B  77   N  PHE B  67           
SHEET   14   A18 HIS B  86  SER B  93 -1  O  SER B  92   N  ILE B  76           
SHEET   15   A18 ILE B 103  LEU B 108 -1  O  TYR B 105   N  ILE B  87           
SHEET   16   A18 GLY B  29  ASN B  33 -1  N  ASN B  30   O  LEU B 108           
SHEET   17   A18 LYS B  38  HIS B  44 -1  O  ILE B  42   N  GLY B  29           
SHEET   18   A18 TYR B   2  VAL B  10  1  N  ILE B   7   O  CYS B  41           
LINK         C   MSE A   1                 N   TYR A   2     1555   1555  1.32  
LINK         C   PHE A  27                 N   MSE A  28     1555   1555  1.32  
LINK         C   MSE A  28                 N   GLY A  29     1555   1555  1.33  
LINK         C   LEU A  88                 N   MSE A  89     1555   1555  1.32  
LINK         C   MSE A  89                 N   GLN A  90     1555   1555  1.32  
LINK         C   MSE B   1                 N   TYR B   2     1555   1555  1.32  
LINK         C   PHE B  27                 N   MSE B  28     1555   1555  1.32  
LINK         C   MSE B  28                 N   GLY B  29     1555   1555  1.32  
LINK         C   LEU B  88                 N   MSE B  89     1555   1555  1.32  
LINK         C   MSE B  89                 N   GLN B  90     1555   1555  1.33  
CRYST1   34.440   77.910  101.990  90.00  90.00  90.00 P 21 21 21    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      0.029036  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012835  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009805        0.00000                         
HETATM    1  N   MSE A   1      29.707  46.063  49.738  1.00 26.06           N  
HETATM    2  CA  MSE A   1      30.773  45.622  50.686  1.00 25.88           C  
HETATM    3  C   MSE A   1      30.241  45.484  52.107  1.00 24.52           C  
HETATM    4  O   MSE A   1      29.504  46.342  52.606  1.00 24.88           O  
HETATM    5  CB  MSE A   1      31.928  46.618  50.683  1.00 27.05           C  
HETATM    6  CG  MSE A   1      33.289  45.994  50.885  1.00 31.12           C  
HETATM    7 SE   MSE A   1      34.475  46.220  49.354  1.00 36.01          SE  
HETATM    8  CE  MSE A   1      34.425  48.192  49.255  1.00 37.51           C  
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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