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Database: PDB
Entry: 2FPN
LinkDB: 2FPN
Original site: 2FPN 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   16-JAN-06   2FPN              
TITLE     THE CRYSTAL STRUCTURE OF THE YWMB PROTEIN FROM BACILLUS SUBTILIS      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: YWMB;                                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 STRAIN: 168;                                                         
SOURCE   5 GENE: YWMB;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PDM68                                     
KEYWDS    YWMB, BACILLUS SUBTILIS, STRUCTURAL GENOMOCS, DOMAIN SWAPPING,        
KEYWDS   2 STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE INITIATIVE, MIDWEST      
KEYWDS   3 CENTER FOR STRUCTURAL GENOMICS, MCSG, UNKNOWN FUNCTION               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.ZHANG,R.WU,S.MOY,A.JOACHIMIAK,MIDWEST CENTER FOR STRUCTURAL         
AUTHOR   2 GENOMICS (MCSG)                                                      
REVDAT   3   13-JUL-11 2FPN    1       VERSN                                    
REVDAT   2   24-FEB-09 2FPN    1       VERSN                                    
REVDAT   1   14-MAR-06 2FPN    0                                                
JRNL        AUTH   R.ZHANG,R.WU,S.MOY,A.JOACHIMIAK                              
JRNL        TITL   THE CRYSTAL STRUCTURE OF THE YWMB PROTEIN FROM BACILLUS      
JRNL        TITL 2 SUBTILIS                                                     
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.49 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.49                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 80.85                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 96.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 11820                          
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) : 0.244                           
REMARK   3   R VALUE            (WORKING SET) : 0.242                           
REMARK   3   FREE R VALUE                     : 0.281                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 610                             
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) : 2.49                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.55                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 692                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 74.46                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2970                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 28                           
REMARK   3   BIN FREE R VALUE                    : 0.3770                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1700                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 53                                      
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) : 34.22                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.03000                                             
REMARK   3    B22 (A**2) : -0.84000                                             
REMARK   3    B33 (A**2) : 2.17000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 1.30000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.378         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.278         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.237         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 19.923        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.927                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.898                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1743 ; 0.011 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2355 ; 1.386 ; 1.942       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   204 ; 7.260 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    88 ;39.887 ;25.227       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   330 ;21.617 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     8 ;24.326 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   267 ; 0.097 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1288 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   742 ; 0.230 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1146 ; 0.306 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    76 ; 0.127 ; 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):    58 ; 0.248 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    10 ; 0.110 ; 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):  1059 ; 0.703 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1683 ; 1.223 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   775 ; 1.482 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   672 ; 2.572 ; 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  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 4                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     1        A    50                          
REMARK   3    RESIDUE RANGE :   A    51        A   100                          
REMARK   3    RESIDUE RANGE :   A   101        A   152                          
REMARK   3    RESIDUE RANGE :   A   155        A   214                          
REMARK   3    ORIGIN FOR THE GROUP (A):  46.3720  10.3690  22.3510              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1682 T22:   0.4780                                     
REMARK   3      T33:   0.2382 T12:   0.0060                                     
REMARK   3      T13:   0.0481 T23:   0.0029                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.9749 L22:   1.0967                                     
REMARK   3      L33:   3.8455 L12:   0.8289                                     
REMARK   3      L13:  -1.6647 L23:  -0.7887                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0344 S12:  -0.2001 S13:   0.0936                       
REMARK   3      S21:   0.1007 S22:  -0.1452 S23:  -0.1480                       
REMARK   3      S31:  -0.0223 S32:  -0.2293 S33:   0.1108                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2FPN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 27-JAN-06.                  
REMARK 100 THE RCSB ID CODE IS RCSB036158.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 16-DEC-04                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9798                             
REMARK 200  MONOCHROMATOR                  : SI CHANNEL 111                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SBCCOLLECT                         
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11820                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.490                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 81.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.4                               
REMARK 200  DATA REDUNDANCY                : 4.500                              
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 34.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.49                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.55                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 74.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.43800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 2.370                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 65.33                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.55                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 10% PEG4000, 45% TACSIMATE, PH 7.0,      
REMARK 280  VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
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        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       44.39500            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       25.42800            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       44.39500            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       25.42800            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: THIS PROTEIN EXISTED AS DIMER, THE SECOND PART OF THE        
REMARK 300 BIOLOGICAL ASSEMBLY IS GENERATED BY THE OPERATION: 1-X,Y,1-Z         
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,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 3430 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 23480 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -21.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000       79.60531            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000       80.73826            
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     ALA A   156                                                      
REMARK 465     ARG A   157                                                      
REMARK 465     SER A   158                                                      
REMARK 465     ALA A   197                                                      
REMARK 465     GLY A   198                                                      
REMARK 465     MSE A   199                                                      
REMARK 465     GLY A   200                                                      
REMARK 465     GLY A   201                                                      
REMARK 465     LYS A   202                                                      
REMARK 465     GLU A   215                                                      
REMARK 465     TYR A   216                                                      
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   O    GLN A   155     O    HOH A   258              1.09            
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 182   CG    MSE A 182  SE       1.089                       
REMARK 500    MSE A 182  SE     MSE A 182   CE      0.421                       
REMARK 500    MSE A 188   CG    MSE A 188  SE       0.446                       
REMARK 500    MSE A 188  SE     MSE A 188   CE      0.418                       
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    MSE A 182   CB  -  CG  - SE   ANGL. DEV. = -50.1 DEGREES          
REMARK 500    MSE A 182   CG  - SE   -  CE  ANGL. DEV. = -35.6 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    TYR A  47       73.83   -117.07                                   
REMARK 500    LYS A  59       71.69   -100.14                                   
REMARK 500    LYS A  86      136.66    178.90                                   
REMARK 500    ASN A 138       93.12    -64.66                                   
REMARK 500    GLU A 160      139.46    145.94                                   
REMARK 500    VAL A 163      131.83    175.56                                   
REMARK 500    PRO A 165      -57.81    -24.50                                   
REMARK 500    SER A 184      109.32    -26.50                                   
REMARK 500    LYS A 185       70.57     19.17                                   
REMARK 500    HIS A 186     -143.87    179.86                                   
REMARK 500    ASN A 189       22.22   -158.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 GLU A  160     HIS A  161                 -110.95                    
REMARK 500 LYS A  185     HIS A  186                  100.79                    
REMARK 500 HIS A  186     LYS A  187                 -148.47                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: APC1972   RELATED DB: TARGETDB                           
DBREF  2FPN A    1   216  GB     2636202  CAB15694        31    246             
SEQADV 2FPN MSE A    7  GB   2636202   MET    37 MODIFIED RESIDUE               
SEQADV 2FPN MSE A   11  GB   2636202   MET    41 MODIFIED RESIDUE               
SEQADV 2FPN MSE A   60  GB   2636202   MET    90 MODIFIED RESIDUE               
SEQADV 2FPN MSE A   98  GB   2636202   MET   128 MODIFIED RESIDUE               
SEQADV 2FPN MSE A  139  GB   2636202   MET   169 MODIFIED RESIDUE               
SEQADV 2FPN MSE A  182  GB   2636202   MET   212 MODIFIED RESIDUE               
SEQADV 2FPN MSE A  188  GB   2636202   MET   218 MODIFIED RESIDUE               
SEQADV 2FPN MSE A  199  GB   2636202   MET   229 MODIFIED RESIDUE               
SEQRES   1 A  216  LEU THR PRO LEU ALA GLN MSE ALA GLU GLY MSE GLU ARG          
SEQRES   2 A  216  GLN ASP VAL SER ILE ASP LYS TRP THR LEU HIS ALA LYS          
SEQRES   3 A  216  GLN ASN LEU SER LEU THR GLU LYS GLU PHE TYR GLN LYS          
SEQRES   4 A  216  VAL GLN ARG LEU LYS GLN GLU TYR ARG GLN TYR ASP TRP          
SEQRES   5 A  216  VAL ILE ALA ARG GLU ASP LYS MSE ILE LYS ALA ILE GLY          
SEQRES   6 A  216  THR TYR THR ASP LYS LYS ASN ARG THR SER PHE ARG LEU          
SEQRES   7 A  216  GLN LEU VAL THR THR LEU LYS LYS HIS ASN PRO THR SER          
SEQRES   8 A  216  TYR LEU LEU TYR GLU GLN MSE SER LEU GLU THR PRO ASP          
SEQRES   9 A  216  SER TRP ASN ASP THR TYR GLU GLN PHE GLU ARG GLU THR          
SEQRES  10 A  216  LEU GLY ILE PHE GLN GLU LYS VAL VAL ILE PHE THR CYS          
SEQRES  11 A  216  LEU ASN GLY HIS LEU ASP ASP ASN MSE ASN ILE VAL LEU          
SEQRES  12 A  216  GLN LYS LYS ALA ASN GLN LEU LEU ASN GLU PHE GLN ALA          
SEQRES  13 A  216  ARG SER VAL GLU HIS VAL VAL GLU PRO ASN PHE VAL SER          
SEQRES  14 A  216  ILE SER ALA PHE THR ASP GLU TRP GLU GLU TYR ILE MSE          
SEQRES  15 A  216  THR SER LYS HIS LYS MSE ASN LEU GLN ILE ALA LEU ARG          
SEQRES  16 A  216  SER ALA GLY MSE GLY GLY LYS HIS THR VAL THR VAL GLY          
SEQRES  17 A  216  THR PRO ILE VAL THR THR GLU TYR                              
MODRES 2FPN MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 2FPN MSE A   11  MET  SELENOMETHIONINE                                   
MODRES 2FPN MSE A   60  MET  SELENOMETHIONINE                                   
MODRES 2FPN MSE A   98  MET  SELENOMETHIONINE                                   
MODRES 2FPN MSE A  139  MET  SELENOMETHIONINE                                   
MODRES 2FPN MSE A  182  MET  SELENOMETHIONINE                                   
MODRES 2FPN MSE A  188  MET  SELENOMETHIONINE                                   
HET    MSE  A   7       8                                                       
HET    MSE  A  11       8                                                       
HET    MSE  A  60       8                                                       
HET    MSE  A  98       8                                                       
HET    MSE  A 139       8                                                       
HET    MSE  A 182       8                                                       
HET    MSE  A 188       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    7(C5 H11 N O2 SE)                                            
FORMUL   2  HOH   *53(H2 O)                                                     
HELIX    1   1 THR A    2  GLN A   14  1                                  13    
HELIX    2   2 THR A   32  TYR A   47  1                                  16    
HELIX    3   3 SER A  105  GLN A  122  1                                  18    
HELIX    4   4 ASN A  138  GLN A  155  1                                  18    
SHEET    1   A 6 ASP A  51  ALA A  55  0                                        
SHEET    2   A 6 MSE A  60  ASP A  69 -1  O  LYS A  62   N  ALA A  55           
SHEET    3   A 6 THR A  74  THR A  83 -1  O  LEU A  78   N  GLY A  65           
SHEET    4   A 6 SER A  91  SER A  99 -1  O  MSE A  98   N  SER A  75           
SHEET    5   A 6 VAL A  16  LEU A  29 -1  N  LEU A  23   O  GLN A  97           
SHEET    6   A 6 ILE A 127  LEU A 135 -1  O  ASN A 132   N  LYS A  20           
SHEET    1   B 3 PHE A 167  ALA A 172  0                                        
SHEET    2   B 3 LEU A 190  ARG A 195 -1  O  LEU A 194   N  VAL A 168           
SHEET    3   B 3 THR A 204  GLY A 208 -1  O  THR A 204   N  ARG A 195           
SHEET    1   C 2 ILE A 181  THR A 183  0                                        
SHEET    2   C 2 HIS A 186  MSE A 188 -1  O  MSE A 188   N  ILE A 181           
LINK         C   GLN A   6                 N   MSE A   7     1555   1555  1.33  
LINK         C   MSE A   7                 N   ALA A   8     1555   1555  1.33  
LINK         C   GLY A  10                 N   MSE A  11     1555   1555  1.33  
LINK         C   MSE A  11                 N   GLU A  12     1555   1555  1.34  
LINK         C   LYS A  59                 N   MSE A  60     1555   1555  1.34  
LINK         C   MSE A  60                 N   ILE A  61     1555   1555  1.34  
LINK         C   GLN A  97                 N   MSE A  98     1555   1555  1.34  
LINK         C   MSE A  98                 N   SER A  99     1555   1555  1.34  
LINK         C   ASN A 138                 N   MSE A 139     1555   1555  1.33  
LINK         C   MSE A 139                 N   ASN A 140     1555   1555  1.34  
LINK         C   ILE A 181                 N   MSE A 182     1555   1555  1.33  
LINK         C   MSE A 182                 N   THR A 183     1555   1555  1.33  
LINK         C   LYS A 187                 N   MSE A 188     1555   1555  1.33  
LINK         C   MSE A 188                 N   ASN A 189     1555   1555  1.33  
CISPEP   1 ASP A   58    LYS A   59          0        -2.00                     
CISPEP   2 THR A  209    PRO A  210          0       -14.32                     
CRYST1   88.790   50.856   81.259  90.00  96.49  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.011263  0.000000  0.001281        0.00000                         
SCALE2      0.000000  0.019663  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012386        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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