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Database: PDB
Entry: 3M8N
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Original site: 3M8N 
HEADER    TRANSFERASE                             18-MAR-10   3M8N              
TITLE     CRYSTAL STRUCTURE OF A POSSIBLE GUTATHIONE S-TRANFERASE FROM          
TITLE    2 RHODOPSEUDOMONAS PALUSTRIS                                           
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: POSSIBLE GLUTATHIONE S-TRANSFERASE;                        
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 EC: 2.5.1.18;                                                        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: RHODOPSEUDOMONAS PALUSTRIS;                     
SOURCE   3 ORGANISM_TAXID: 1076;                                                
SOURCE   4 GENE: GSTA1, RPA4332;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   7 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   8 EXPRESSION_SYSTEM_PLASMID: PSGX3(BC)                                 
KEYWDS    PSI-II, STRUCTURAL GENOMICS, PROTEIN STRUCTURE INITIATIVE,            
KEYWDS   2 NYSGXRC, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL                 
KEYWDS   3 GENOMICS, TRANSFERASE                                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    L.DAMODHARAN,S.K.BURLEY,S.SWAMINATHAN,NEW YORK SGX RESEARCH           
AUTHOR   2 CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                             
REVDAT   1   07-APR-10 3M8N    0                                                
JRNL        AUTH   L.DAMODHARAN,S.K.BURLEY,S.SWAMINATHAN                        
JRNL        TITL   CRYSTAL STRUCTURE OF A POSSIBLE GUTATHIONE                   
JRNL        TITL 2 S-TRANFERASE FROM RHODOPSEUDOMONAS PALUSTRIS                 
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.04 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) : 2.04                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 45.67                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 91.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 52010                          
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) : 0.201                           
REMARK   3   R VALUE            (WORKING SET) : 0.199                           
REMARK   3   FREE R VALUE                     : 0.259                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.200                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1718                            
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) : 2.04                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.10                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 3125                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 72.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3260                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 0                            
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6382                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 15                                      
REMARK   3   SOLVENT ATOMS            : 239                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.38                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.01000                                             
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
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): 0.216         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.197         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.171         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 7.022         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.959                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.900                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6569 ; 0.023 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8960 ; 1.964 ; 1.948       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   795 ; 7.280 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   316 ;35.396 ;23.386       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1002 ;20.250 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    46 ;23.357 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   969 ; 0.139 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5097 ; 0.009 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
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):  4000 ; 1.019 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6390 ; 1.925 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2569 ; 3.062 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2570 ; 4.669 ; 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: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS                                                    
REMARK   4                                                                      
REMARK   4 3M8N COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 25-MAR-10.                  
REMARK 100 THE RCSB ID CODE IS RCSB058246.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 11-FEB-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9792                             
REMARK 200  MONOCHROMATOR                  : SI 111 CHANNEL                     
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 53728                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.040                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.700                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.7                               
REMARK 200  DATA REDUNDANCY                : 12.600                             
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 11.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.04                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.11                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.9                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.500                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX, SOLVE & RESOLVE                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.48                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M HEPES PH 7.5, 2.0M AMMONIUM         
REMARK 280  SULFATE, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 298K            
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       28.48600            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       76.06400            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       52.54400            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       76.06400            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.48600            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       52.54400            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 3140 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -40.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 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: 2950 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18910 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -29.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C, 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    -1                                                      
REMARK 465     GLU A   204                                                      
REMARK 465     THR A   205                                                      
REMARK 465     ILE A   206                                                      
REMARK 465     ALA A   207                                                      
REMARK 465     ALA A   208                                                      
REMARK 465     ASP A   209                                                      
REMARK 465     PRO A   210                                                      
REMARK 465     THR A   211                                                      
REMARK 465     SER A   212                                                      
REMARK 465     PHE A   213                                                      
REMARK 465     ALA A   214                                                      
REMARK 465     ALA A   215                                                      
REMARK 465     GLU A   216                                                      
REMARK 465     GLY A   217                                                      
REMARK 465     HIS A   218                                                      
REMARK 465     HIS A   219                                                      
REMARK 465     HIS A   220                                                      
REMARK 465     HIS A   221                                                      
REMARK 465     HIS A   222                                                      
REMARK 465     HIS A   223                                                      
REMARK 465     MSE B    -1                                                      
REMARK 465     ASN B   105                                                      
REMARK 465     ILE B   106                                                      
REMARK 465     GLY B   107                                                      
REMARK 465     SER B   108                                                      
REMARK 465     ALA B   109                                                      
REMARK 465     TYR B   110                                                      
REMARK 465     PHE B   111                                                      
REMARK 465     TRP B   112                                                      
REMARK 465     LEU B   113                                                      
REMARK 465     CYS B   114                                                      
REMARK 465     LEU B   115                                                      
REMARK 465     VAL B   116                                                      
REMARK 465     LYS B   117                                                      
REMARK 465     GLY B   118                                                      
REMARK 465     GLY B   119                                                      
REMARK 465     ARG B   120                                                      
REMARK 465     ASP B   121                                                      
REMARK 465     LEU B   122                                                      
REMARK 465     GLN B   123                                                      
REMARK 465     THR B   124                                                      
REMARK 465     HIS B   125                                                      
REMARK 465     GLU B   204                                                      
REMARK 465     THR B   205                                                      
REMARK 465     ILE B   206                                                      
REMARK 465     ALA B   207                                                      
REMARK 465     ALA B   208                                                      
REMARK 465     ASP B   209                                                      
REMARK 465     PRO B   210                                                      
REMARK 465     THR B   211                                                      
REMARK 465     SER B   212                                                      
REMARK 465     PHE B   213                                                      
REMARK 465     ALA B   214                                                      
REMARK 465     ALA B   215                                                      
REMARK 465     GLU B   216                                                      
REMARK 465     GLY B   217                                                      
REMARK 465     HIS B   218                                                      
REMARK 465     HIS B   219                                                      
REMARK 465     HIS B   220                                                      
REMARK 465     HIS B   221                                                      
REMARK 465     HIS B   222                                                      
REMARK 465     HIS B   223                                                      
REMARK 465     MSE C    -1                                                      
REMARK 465     VAL C   116                                                      
REMARK 465     LYS C   117                                                      
REMARK 465     GLY C   118                                                      
REMARK 465     GLY C   119                                                      
REMARK 465     ARG C   120                                                      
REMARK 465     ASP C   121                                                      
REMARK 465     LEU C   122                                                      
REMARK 465     GLN C   123                                                      
REMARK 465     THR C   124                                                      
REMARK 465     HIS C   125                                                      
REMARK 465     ALA C   126                                                      
REMARK 465     GLU C   204                                                      
REMARK 465     THR C   205                                                      
REMARK 465     ILE C   206                                                      
REMARK 465     ALA C   207                                                      
REMARK 465     ALA C   208                                                      
REMARK 465     ASP C   209                                                      
REMARK 465     PRO C   210                                                      
REMARK 465     THR C   211                                                      
REMARK 465     SER C   212                                                      
REMARK 465     PHE C   213                                                      
REMARK 465     ALA C   214                                                      
REMARK 465     ALA C   215                                                      
REMARK 465     GLU C   216                                                      
REMARK 465     GLY C   217                                                      
REMARK 465     HIS C   218                                                      
REMARK 465     HIS C   219                                                      
REMARK 465     HIS C   220                                                      
REMARK 465     HIS C   221                                                      
REMARK 465     HIS C   222                                                      
REMARK 465     HIS C   223                                                      
REMARK 465     MSE D    -1                                                      
REMARK 465     GLU D   204                                                      
REMARK 465     THR D   205                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     LEU B 127    CG   CD1  CD2                                       
REMARK 470     LEU C 127    CG   CD1  CD2                                       
REMARK 470     GLU C 128    CG   CD   OE1  OE2                                  
REMARK 470     ASP C 129    CG   OD1  OD2                                       
REMARK 470     ASP C 174    CG   OD1  OD2                                       
REMARK 470     PHE C 175    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     ASP C 176    CG   OD1  OD2                                       
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    ARG A  17   NE  -  CZ  -  NH1 ANGL. DEV. =   4.5 DEGREES          
REMARK 500    ARG A  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    CYS A 114   CA  -  CB  -  SG  ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ARG A 189   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    PRO B  49   C   -  N   -  CA  ANGL. DEV. =  10.1 DEGREES          
REMARK 500    ASP B  87   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    ARG B  88   NE  -  CZ  -  NH1 ANGL. DEV. =  -3.8 DEGREES          
REMARK 500    ARG B 189   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.5 DEGREES          
REMARK 500    ARG C  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.6 DEGREES          
REMARK 500    ARG D  17   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.9 DEGREES          
REMARK 500    PRO D 203   C   -  N   -  CA  ANGL. DEV. =  10.9 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    THR A  58      -95.83    -77.30                                   
REMARK 500    GLU A  66      106.18     77.86                                   
REMARK 500    ASN A 105      -62.09   -122.33                                   
REMARK 500    ASP A 174        8.98     94.93                                   
REMARK 500    LEU B   1      -95.27   -100.38                                   
REMARK 500    TYR B   2      110.43     -7.35                                   
REMARK 500    ARG B   9       49.80    -98.95                                   
REMARK 500    ARG B  36     -153.66   -157.88                                   
REMARK 500    GLU B  66      112.95     77.48                                   
REMARK 500    ASP B 174       -5.33     77.62                                   
REMARK 500    PHE B 180       64.66   -118.97                                   
REMARK 500    ARG C  36       30.43    -95.54                                   
REMARK 500    ARG C  40       66.71   -116.33                                   
REMARK 500    PRO C  49      -69.01    -11.13                                   
REMARK 500    ALA C  59     -160.75   -120.36                                   
REMARK 500    GLU C  66      103.79     80.73                                   
REMARK 500    ASN C 105      -70.43   -107.16                                   
REMARK 500    CYS C 114       42.63   -107.78                                   
REMARK 500    CYS C 173       14.09    -47.33                                   
REMARK 500    ASP C 174      -85.38     61.73                                   
REMARK 500    PHE C 175      105.12     38.41                                   
REMARK 500    ASP C 176       94.50    -57.28                                   
REMARK 500    SER C 178      -57.82    -29.62                                   
REMARK 500    PHE C 180       64.80   -119.14                                   
REMARK 500    ASN C 184      -38.67    -39.64                                   
REMARK 500    GLU D  66      105.09     74.76                                   
REMARK 500    LEU D 102      -61.99    -92.69                                   
REMARK 500    ASN D 105      -60.26   -105.83                                   
REMARK 500    ASP D 171      -48.73    -29.83                                   
REMARK 500    ASP D 174       14.04     93.44                                   
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 SER B    0     LEU B    1                  135.36                    
REMARK 500 SER D    0     LEU D    1                  128.09                    
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    ASP B 200        24.3      L          L   OUTSIDE RANGE           
REMARK 500    GLU D 103        23.8      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 C 244        DISTANCE =  8.88 ANGSTROMS                       
REMARK 525    HOH C 248        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH B 255        DISTANCE =  5.63 ANGSTROMS                       
REMARK 525    HOH B 267        DISTANCE =  6.80 ANGSTROMS                       
REMARK 525    HOH D 267        DISTANCE =  9.15 ANGSTROMS                       
REMARK 525    HOH B 297        DISTANCE =  5.21 ANGSTROMS                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 230                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 B 232                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE SO4 D 231                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-21017D   RELATED DB: TARGETDB                    
DBREF  3M8N A    2   216  UNP    Q6N1S2   Q6N1S2_RHOPA     2    216             
DBREF  3M8N B    2   216  UNP    Q6N1S2   Q6N1S2_RHOPA     2    216             
DBREF  3M8N C    2   216  UNP    Q6N1S2   Q6N1S2_RHOPA     2    216             
DBREF  3M8N D    2   216  UNP    Q6N1S2   Q6N1S2_RHOPA     2    216             
SEQADV 3M8N MSE A   -1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N SER A    0  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N LEU A    1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N GLY A  217  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS A  218  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS A  219  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS A  220  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS A  221  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS A  222  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS A  223  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N MSE B   -1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N SER B    0  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N LEU B    1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N GLY B  217  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS B  218  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS B  219  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS B  220  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS B  221  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS B  222  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS B  223  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N MSE C   -1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N SER C    0  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N LEU C    1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N GLY C  217  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS C  218  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS C  219  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS C  220  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS C  221  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS C  222  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS C  223  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N MSE D   -1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N SER D    0  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N LEU D    1  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N GLY D  217  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS D  218  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS D  219  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS D  220  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS D  221  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS D  222  UNP  Q6N1S2              EXPRESSION TAG                 
SEQADV 3M8N HIS D  223  UNP  Q6N1S2              EXPRESSION TAG                 
SEQRES   1 A  225  MSE SER LEU TYR LYS LEU TYR SER MSE GLN ARG SER GLY          
SEQRES   2 A  225  ASN SER TYR LYS VAL ARG LEU ALA LEU ALA LEU LEU ASP          
SEQRES   3 A  225  ALA PRO TYR ARG ALA VAL GLU VAL ASP ILE LEU ARG GLY          
SEQRES   4 A  225  GLU SER ARG THR PRO ASP PHE LEU ALA LYS ASN PRO SER          
SEQRES   5 A  225  GLY GLN VAL PRO LEU LEU GLU THR ALA PRO GLY ARG TYR          
SEQRES   6 A  225  LEU ALA GLU SER ASN ALA ILE LEU TRP TYR LEU ALA VAL          
SEQRES   7 A  225  GLY THR SER LEU ALA PRO ASP THR ARG MSE ASP ARG ALA          
SEQRES   8 A  225  GLU ALA LEU GLN TRP MSE PHE PHE GLU GLN HIS ALA LEU          
SEQRES   9 A  225  GLU PRO ASN ILE GLY SER ALA TYR PHE TRP LEU CYS LEU          
SEQRES  10 A  225  VAL LYS GLY GLY ARG ASP LEU GLN THR HIS ALA LEU GLU          
SEQRES  11 A  225  ASP TRP LEU GLU ARG GLY TYR ALA ALA LEU GLN VAL MSE          
SEQRES  12 A  225  GLU ASN HIS LEU LYS THR ASN ASP TYR PHE ALA ALA GLY          
SEQRES  13 A  225  GLN LEU THR ILE ALA ASP ILE ALA LEU TYR GLY TYR THR          
SEQRES  14 A  225  HIS VAL ALA ASP GLN CYS ASP PHE ASP LEU SER THR PHE          
SEQRES  15 A  225  PRO ALA VAL ASN ALA TRP LEU ARG ARG VAL GLU GLN THR          
SEQRES  16 A  225  PRO GLY PHE ILE THR MSE ASP TRP THR PRO GLU THR ILE          
SEQRES  17 A  225  ALA ALA ASP PRO THR SER PHE ALA ALA GLU GLY HIS HIS          
SEQRES  18 A  225  HIS HIS HIS HIS                                              
SEQRES   1 B  225  MSE SER LEU TYR LYS LEU TYR SER MSE GLN ARG SER GLY          
SEQRES   2 B  225  ASN SER TYR LYS VAL ARG LEU ALA LEU ALA LEU LEU ASP          
SEQRES   3 B  225  ALA PRO TYR ARG ALA VAL GLU VAL ASP ILE LEU ARG GLY          
SEQRES   4 B  225  GLU SER ARG THR PRO ASP PHE LEU ALA LYS ASN PRO SER          
SEQRES   5 B  225  GLY GLN VAL PRO LEU LEU GLU THR ALA PRO GLY ARG TYR          
SEQRES   6 B  225  LEU ALA GLU SER ASN ALA ILE LEU TRP TYR LEU ALA VAL          
SEQRES   7 B  225  GLY THR SER LEU ALA PRO ASP THR ARG MSE ASP ARG ALA          
SEQRES   8 B  225  GLU ALA LEU GLN TRP MSE PHE PHE GLU GLN HIS ALA LEU          
SEQRES   9 B  225  GLU PRO ASN ILE GLY SER ALA TYR PHE TRP LEU CYS LEU          
SEQRES  10 B  225  VAL LYS GLY GLY ARG ASP LEU GLN THR HIS ALA LEU GLU          
SEQRES  11 B  225  ASP TRP LEU GLU ARG GLY TYR ALA ALA LEU GLN VAL MSE          
SEQRES  12 B  225  GLU ASN HIS LEU LYS THR ASN ASP TYR PHE ALA ALA GLY          
SEQRES  13 B  225  GLN LEU THR ILE ALA ASP ILE ALA LEU TYR GLY TYR THR          
SEQRES  14 B  225  HIS VAL ALA ASP GLN CYS ASP PHE ASP LEU SER THR PHE          
SEQRES  15 B  225  PRO ALA VAL ASN ALA TRP LEU ARG ARG VAL GLU GLN THR          
SEQRES  16 B  225  PRO GLY PHE ILE THR MSE ASP TRP THR PRO GLU THR ILE          
SEQRES  17 B  225  ALA ALA ASP PRO THR SER PHE ALA ALA GLU GLY HIS HIS          
SEQRES  18 B  225  HIS HIS HIS HIS                                              
SEQRES   1 C  225  MSE SER LEU TYR LYS LEU TYR SER MSE GLN ARG SER GLY          
SEQRES   2 C  225  ASN SER TYR LYS VAL ARG LEU ALA LEU ALA LEU LEU ASP          
SEQRES   3 C  225  ALA PRO TYR ARG ALA VAL GLU VAL ASP ILE LEU ARG GLY          
SEQRES   4 C  225  GLU SER ARG THR PRO ASP PHE LEU ALA LYS ASN PRO SER          
SEQRES   5 C  225  GLY GLN VAL PRO LEU LEU GLU THR ALA PRO GLY ARG TYR          
SEQRES   6 C  225  LEU ALA GLU SER ASN ALA ILE LEU TRP TYR LEU ALA VAL          
SEQRES   7 C  225  GLY THR SER LEU ALA PRO ASP THR ARG MSE ASP ARG ALA          
SEQRES   8 C  225  GLU ALA LEU GLN TRP MSE PHE PHE GLU GLN HIS ALA LEU          
SEQRES   9 C  225  GLU PRO ASN ILE GLY SER ALA TYR PHE TRP LEU CYS LEU          
SEQRES  10 C  225  VAL LYS GLY GLY ARG ASP LEU GLN THR HIS ALA LEU GLU          
SEQRES  11 C  225  ASP TRP LEU GLU ARG GLY TYR ALA ALA LEU GLN VAL MSE          
SEQRES  12 C  225  GLU ASN HIS LEU LYS THR ASN ASP TYR PHE ALA ALA GLY          
SEQRES  13 C  225  GLN LEU THR ILE ALA ASP ILE ALA LEU TYR GLY TYR THR          
SEQRES  14 C  225  HIS VAL ALA ASP GLN CYS ASP PHE ASP LEU SER THR PHE          
SEQRES  15 C  225  PRO ALA VAL ASN ALA TRP LEU ARG ARG VAL GLU GLN THR          
SEQRES  16 C  225  PRO GLY PHE ILE THR MSE ASP TRP THR PRO GLU THR ILE          
SEQRES  17 C  225  ALA ALA ASP PRO THR SER PHE ALA ALA GLU GLY HIS HIS          
SEQRES  18 C  225  HIS HIS HIS HIS                                              
SEQRES   1 D  225  MSE SER LEU TYR LYS LEU TYR SER MSE GLN ARG SER GLY          
SEQRES   2 D  225  ASN SER TYR LYS VAL ARG LEU ALA LEU ALA LEU LEU ASP          
SEQRES   3 D  225  ALA PRO TYR ARG ALA VAL GLU VAL ASP ILE LEU ARG GLY          
SEQRES   4 D  225  GLU SER ARG THR PRO ASP PHE LEU ALA LYS ASN PRO SER          
SEQRES   5 D  225  GLY GLN VAL PRO LEU LEU GLU THR ALA PRO GLY ARG TYR          
SEQRES   6 D  225  LEU ALA GLU SER ASN ALA ILE LEU TRP TYR LEU ALA VAL          
SEQRES   7 D  225  GLY THR SER LEU ALA PRO ASP THR ARG MSE ASP ARG ALA          
SEQRES   8 D  225  GLU ALA LEU GLN TRP MSE PHE PHE GLU GLN HIS ALA LEU          
SEQRES   9 D  225  GLU PRO ASN ILE GLY SER ALA TYR PHE TRP LEU CYS LEU          
SEQRES  10 D  225  VAL LYS GLY GLY ARG ASP LEU GLN THR HIS ALA LEU GLU          
SEQRES  11 D  225  ASP TRP LEU GLU ARG GLY TYR ALA ALA LEU GLN VAL MSE          
SEQRES  12 D  225  GLU ASN HIS LEU LYS THR ASN ASP TYR PHE ALA ALA GLY          
SEQRES  13 D  225  GLN LEU THR ILE ALA ASP ILE ALA LEU TYR GLY TYR THR          
SEQRES  14 D  225  HIS VAL ALA ASP GLN CYS ASP PHE ASP LEU SER THR PHE          
SEQRES  15 D  225  PRO ALA VAL ASN ALA TRP LEU ARG ARG VAL GLU GLN THR          
SEQRES  16 D  225  PRO GLY PHE ILE THR MSE ASP TRP THR PRO GLU THR ILE          
SEQRES  17 D  225  ALA ALA ASP PRO THR SER PHE ALA ALA GLU GLY HIS HIS          
SEQRES  18 D  225  HIS HIS HIS HIS                                              
MODRES 3M8N MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE A   86  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE A   95  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE A  141  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE A  199  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE B    7  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE B   86  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE B   95  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE B  141  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE B  199  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE C    7  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE C   86  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE C   95  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE C  141  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE C  199  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE D    7  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE D   86  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE D   95  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE D  141  MET  SELENOMETHIONINE                                   
MODRES 3M8N MSE D  199  MET  SELENOMETHIONINE                                   
HET    MSE  A   7       8                                                       
HET    MSE  A  86       8                                                       
HET    MSE  A  95       8                                                       
HET    MSE  A 141       8                                                       
HET    MSE  A 199       8                                                       
HET    MSE  B   7       8                                                       
HET    MSE  B  86       8                                                       
HET    MSE  B  95       8                                                       
HET    MSE  B 141       8                                                       
HET    MSE  B 199       8                                                       
HET    MSE  C   7       8                                                       
HET    MSE  C  86       8                                                       
HET    MSE  C  95       8                                                       
HET    MSE  C 141       8                                                       
HET    MSE  C 199       8                                                       
HET    MSE  D   7       8                                                       
HET    MSE  D  86       8                                                       
HET    MSE  D  95       8                                                       
HET    MSE  D 141       8                                                       
HET    MSE  D 199       8                                                       
HET    SO4  B 230       5                                                       
HET    SO4  B 232       5                                                       
HET    SO4  D 231       5                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     SO4 SULFATE ION                                                      
FORMUL   1  MSE    20(C5 H11 N O2 SE)                                           
FORMUL   5  SO4    3(O4 S 2-)                                                   
FORMUL   8  HOH   *239(H2 O)                                                    
HELIX    1   1 SER A   10  LEU A   23  1                                  14    
HELIX    2   2 ASP A   33  GLY A   37  5                                   5    
HELIX    3   3 THR A   41  ALA A   46  1                                   6    
HELIX    4   4 GLU A   66  VAL A   76  1                                  11    
HELIX    5   5 THR A   84  LEU A  102  1                                  19    
HELIX    6   6 ASN A  105  LEU A  115  1                                  11    
HELIX    7   7 ARG A  120  THR A  124  5                                   5    
HELIX    8   8 ALA A  126  LEU A  145  1                                  20    
HELIX    9   9 THR A  157  HIS A  168  1                                  12    
HELIX   10  10 VAL A  169  CYS A  173  5                                   5    
HELIX   11  11 PHE A  180  GLN A  192  1                                  13    
HELIX   12  12 SER B   10  ASP B   24  1                                  15    
HELIX   13  13 THR B   41  ALA B   46  1                                   6    
HELIX   14  14 GLU B   66  VAL B   76  1                                  11    
HELIX   15  15 THR B   84  LEU B  102  1                                  19    
HELIX   16  16 ALA B  126  LYS B  146  1                                  21    
HELIX   17  17 THR B  157  CYS B  173  1                                  17    
HELIX   18  18 PHE B  180  GLN B  192  1                                  13    
HELIX   19  19 SER C   10  ASP C   24  1                                  15    
HELIX   20  20 THR C   41  ALA C   46  1                                   6    
HELIX   21  21 GLU C   66  VAL C   76  1                                  11    
HELIX   22  22 THR C   84  LEU C  102  1                                  19    
HELIX   23  23 LEU C  102  CYS C  114  1                                  13    
HELIX   24  24 LEU C  127  LYS C  146  1                                  20    
HELIX   25  25 THR C  157  HIS C  168  1                                  12    
HELIX   26  26 HIS C  168  CYS C  173  1                                   6    
HELIX   27  27 ASP C  176  THR C  179  5                                   4    
HELIX   28  28 PHE C  180  GLN C  192  1                                  13    
HELIX   29  29 SER D   10  LEU D   23  1                                  14    
HELIX   30  30 ASP D   33  GLY D   37  5                                   5    
HELIX   31  31 THR D   41  ASN D   48  1                                   8    
HELIX   32  32 GLU D   66  VAL D   76  1                                  11    
HELIX   33  33 THR D   84  LEU D  102  1                                  19    
HELIX   34  34 ASN D  105  LEU D  115  1                                  11    
HELIX   35  35 GLN D  123  LYS D  146  1                                  24    
HELIX   36  36 THR D  157  HIS D  168  1                                  12    
HELIX   37  37 VAL D  169  ASP D  174  5                                   6    
HELIX   38  38 PHE D  180  GLN D  192  1                                  13    
HELIX   39  39 ASP D  209  ALA D  214  5                                   6    
SHEET    1   A 4 TYR A  27  GLU A  31  0                                        
SHEET    2   A 4 TYR A   2  SER A   6  1  N  LEU A   4   O  VAL A  30           
SHEET    3   A 4 LEU A  55  GLU A  57 -1  O  LEU A  55   N  TYR A   5           
SHEET    4   A 4 TYR A  63  ALA A  65 -1  O  LEU A  64   N  LEU A  56           
SHEET    1   B 4 ARG B  28  GLU B  31  0                                        
SHEET    2   B 4 LYS B   3  SER B   6  1  N  SER B   6   O  VAL B  30           
SHEET    3   B 4 LEU B  55  ALA B  59 -1  O  LEU B  55   N  TYR B   5           
SHEET    4   B 4 ARG B  62  ALA B  65 -1  O  LEU B  64   N  LEU B  56           
SHEET    1   C 4 ARG C  28  GLU C  31  0                                        
SHEET    2   C 4 LYS C   3  SER C   6  1  N  SER C   6   O  VAL C  30           
SHEET    3   C 4 LEU C  55  GLU C  57 -1  O  LEU C  55   N  TYR C   5           
SHEET    4   C 4 TYR C  63  ALA C  65 -1  O  LEU C  64   N  LEU C  56           
SHEET    1   D 4 TYR D  27  GLU D  31  0                                        
SHEET    2   D 4 TYR D   2  SER D   6  1  N  LEU D   4   O  VAL D  30           
SHEET    3   D 4 LEU D  55  ALA D  59 -1  O  LEU D  55   N  TYR D   5           
SHEET    4   D 4 ARG D  62  ALA D  65 -1  O  LEU D  64   N  LEU D  56           
SSBOND   1 CYS C  114    CYS C  173                          1555   1555  2.04  
LINK         C   SER A   6                 N   MSE A   7     1555   1555  1.31  
LINK         C   MSE A   7                 N   GLN A   8     1555   1555  1.31  
LINK         C   ARG A  85                 N   MSE A  86     1555   1555  1.33  
LINK         C   MSE A  86                 N   ASP A  87     1555   1555  1.31  
LINK         C   TRP A  94                 N   MSE A  95     1555   1555  1.33  
LINK         C   MSE A  95                 N   PHE A  96     1555   1555  1.33  
LINK         C   VAL A 140                 N   MSE A 141     1555   1555  1.32  
LINK         C   MSE A 141                 N   GLU A 142     1555   1555  1.33  
LINK         C   THR A 198                 N   MSE A 199     1555   1555  1.33  
LINK         C   MSE A 199                 N   ASP A 200     1555   1555  1.33  
LINK         C   SER B   6                 N   MSE B   7     1555   1555  1.33  
LINK         C   MSE B   7                 N   GLN B   8     1555   1555  1.33  
LINK         C   ARG B  85                 N   MSE B  86     1555   1555  1.33  
LINK         C   MSE B  86                 N   ASP B  87     1555   1555  1.32  
LINK         C   TRP B  94                 N   MSE B  95     1555   1555  1.33  
LINK         C   MSE B  95                 N   PHE B  96     1555   1555  1.32  
LINK         C   VAL B 140                 N   MSE B 141     1555   1555  1.32  
LINK         C   MSE B 141                 N   GLU B 142     1555   1555  1.33  
LINK         C   THR B 198                 N   MSE B 199     1555   1555  1.32  
LINK         C   MSE B 199                 N   ASP B 200     1555   1555  1.32  
LINK         C   SER C   6                 N   MSE C   7     1555   1555  1.32  
LINK         C   MSE C   7                 N   GLN C   8     1555   1555  1.34  
LINK         C   ARG C  85                 N   MSE C  86     1555   1555  1.35  
LINK         C   MSE C  86                 N   ASP C  87     1555   1555  1.32  
LINK         C   TRP C  94                 N   MSE C  95     1555   1555  1.33  
LINK         C   MSE C  95                 N   PHE C  96     1555   1555  1.32  
LINK         C   VAL C 140                 N   MSE C 141     1555   1555  1.33  
LINK         C   MSE C 141                 N   GLU C 142     1555   1555  1.34  
LINK         C   THR C 198                 N   MSE C 199     1555   1555  1.33  
LINK         C   MSE C 199                 N   ASP C 200     1555   1555  1.32  
LINK         C   SER D   6                 N   MSE D   7     1555   1555  1.32  
LINK         C   MSE D   7                 N   GLN D   8     1555   1555  1.33  
LINK         C   ARG D  85                 N   MSE D  86     1555   1555  1.32  
LINK         C   MSE D  86                 N   ASP D  87     1555   1555  1.33  
LINK         C   TRP D  94                 N   MSE D  95     1555   1555  1.31  
LINK         C   MSE D  95                 N   PHE D  96     1555   1555  1.33  
LINK         C   VAL D 140                 N   MSE D 141     1555   1555  1.34  
LINK         C   MSE D 141                 N   GLU D 142     1555   1555  1.31  
LINK         C   THR D 198                 N   MSE D 199     1555   1555  1.33  
LINK         C   MSE D 199                 N   ASP D 200     1555   1555  1.34  
CISPEP   1 VAL A   53    PRO A   54          0         7.25                     
CISPEP   2 VAL B   53    PRO B   54          0        12.35                     
CISPEP   3 VAL C   53    PRO C   54          0        10.45                     
CISPEP   4 VAL D   53    PRO D   54          0         6.27                     
SITE     1 AC1  4 ARG B  88  ARG B 189  HOH B 275  HOH B 280                    
SITE     1 AC2  3 SER B  10  GLY B  11  TYR B 166                               
SITE     1 AC3  3 ARG D  88  ARG D 189  HOH D 273                               
CRYST1   56.972  105.088  152.128  90.00  90.00  90.00 P 21 21 21   16          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017552  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009516  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.006573        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
DBGET integrated database retrieval system