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Database: PDB
Entry: 2POD
LinkDB: 2POD
Original site: 2POD 
HEADER    STRUCTURAL GENOMICS, UNKNOWN FUNCTION   26-APR-07   2POD              
TITLE     CRYSTAL STRUCTURE OF A MEMBER OF ENOLASE SUPERFAMILY FROM BURKHOLDERIA
TITLE    2 PSEUDOMALLEI K96243                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: MANDELATE RACEMASE / MUCONATE LACTONIZING ENZYME;          
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BURKHOLDERIA PSEUDOMALLEI;                      
SOURCE   3 ORGANISM_TAXID: 272560;                                              
SOURCE   4 STRAIN: K96243;                                                      
SOURCE   5 GENE: BPSS2072;                                                      
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PET;                                       
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: BC-PSGX3(BC)                              
KEYWDS    ENOLASE, RACEMASE, STRUCTURAL GENOMICS, PSI, PROTEIN STRUCTURE        
KEYWDS   2 INITIATIVE, NYSGRC, NEW YORK STRUCTURAL GENOMICS RESEARCH            
KEYWDS   3 CONSORTIUM, NEW YORK SGX RESEARCH CENTER FOR STRUCTURAL GENOMICS,    
KEYWDS   4 NYSGXRC, UNKNOWN FUNCTION                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    Y.PATSKOVSKY,J.BONANNO,J.M.SAUDER,J.M.GILMORE,M.IIZUKA,S.OZYURT,      
AUTHOR   2 S.R.WASSERMAN,D.SMITH,J.GERLT,S.K.BURLEY,S.C.ALMO,NEW YORK SGX       
AUTHOR   3 RESEARCH CENTER FOR STRUCTURAL GENOMICS (NYSGXRC)                    
REVDAT   5   03-FEB-21 2POD    1       AUTHOR JRNL   REMARK SEQADV              
REVDAT   5 2                   1       LINK                                     
REVDAT   4   14-NOV-18 2POD    1       AUTHOR                                   
REVDAT   3   13-JUL-11 2POD    1       VERSN                                    
REVDAT   2   24-FEB-09 2POD    1       VERSN                                    
REVDAT   1   05-JUN-07 2POD    0                                                
JRNL        AUTH   Y.PATSKOVSKY,J.BONANNO,J.M.SAUDER,J.M.GILMORE,M.IIZUKA,      
JRNL        AUTH 2 M.GHEYI,S.OZYURT,S.R.WASSERMAN,D.SMITH,J.GERLT,S.K.BURLEY,   
JRNL        AUTH 3 S.C.ALMO                                                     
JRNL        TITL   CRYSTAL STRUCTURE OF A MEMBER OF ENOLASE SUPERFAMILY FROM    
JRNL        TITL 2 BURKHOLDERIA PSEUDOMALLEI.                                   
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.34 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.3.0034                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.34                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 33656                          
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) : 0.211                           
REMARK   3   R VALUE            (WORKING SET) : 0.209                           
REMARK   3   FREE R VALUE                     : 0.275                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 3.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1076                            
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) : 2.34                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.40                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1763                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 65.91                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2950                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 62                           
REMARK   3   BIN FREE R VALUE                    : 0.3890                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5967                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 152                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 47.00                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 51.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.60000                                             
REMARK   3    B22 (A**2) : -1.60000                                             
REMARK   3    B33 (A**2) : 3.19000                                              
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): 0.418         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.286         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.232         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.664         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.953                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.922                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  6116 ; 0.008 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  8326 ; 1.272 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   759 ; 8.807 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   278 ;40.527 ;23.165       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   984 ;21.516 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    49 ;15.577 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   917 ; 0.121 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  4691 ; 0.003 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2899 ; 0.143 ; 0.300       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  4068 ; 0.296 ; 0.500       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   449 ; 0.162 ; 0.500       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):     2 ; 0.031 ; 0.500       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    91 ; 0.102 ; 0.300       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    28 ; 0.140 ; 0.500       
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):  3783 ; 2.585 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  6067 ; 4.182 ; 3.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2461 ; 6.558 ; 4.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  2257 ; 8.904 ; 6.000       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 2                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A     385      1                      
REMARK   3           2     B      1       B     385      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):   2951 ;  0.25 ;  0.05           
REMARK   3   TIGHT THERMAL      1    B (A**2):   2951 ;  3.45 ;  2.00           
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 RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2POD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 01-MAY-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000042602.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 09-APR-06                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 31-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97960                            
REMARK 200  MONOCHROMATOR                  : MIRRORS                            
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MAR CCD 165 MM                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 38379                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.340                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -5.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.8                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : 0.07100                            
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.2000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.34                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.42                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 86.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.60000                            
REMARK 200  R SYM FOR SHELL            (I) : 0.42000                            
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 0.900                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: SHELX                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 53.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.45                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS-HCL, PH 5.5, 45% MPD,     
REMARK 280  200MM AMMONIUM ACETATE, 10% GLYCEROL, VAPOR DIFFUSION, SITTING      
REMARK 280  DROP, TEMPERATURE 294K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: I 4                              
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   -Y,X,Z                                                  
REMARK 290       4555   Y,-X,Z                                                  
REMARK 290       5555   X+1/2,Y+1/2,Z+1/2                                       
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -Y+1/2,X+1/2,Z+1/2                                      
REMARK 290       8555   Y+1/2,-X+1/2,Z+1/2                                      
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       73.38550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       73.38550            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       42.76550            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       73.38550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       73.38550            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       42.76550            
REMARK 290   SMTRY1   7  0.000000 -1.000000  0.000000       73.38550            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000       73.38550            
REMARK 290   SMTRY3   7  0.000000  0.000000  1.000000       42.76550            
REMARK 290   SMTRY1   8  0.000000  1.000000  0.000000       73.38550            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000       73.38550            
REMARK 290   SMTRY3   8  0.000000  0.000000  1.000000       42.76550            
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 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: OCTAMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: OCTAMERIC                  
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 40740 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 86460 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -173.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   4  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   4  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     VAL A   127                                                      
REMARK 465     ARG A   128                                                      
REMARK 465     THR A   129                                                      
REMARK 465     ALA A   130                                                      
REMARK 465     LYS A   131                                                      
REMARK 465     GLN A   132                                                      
REMARK 465     GLN A   133                                                      
REMARK 465     SER A   134                                                      
REMARK 465     VAL A   135                                                      
REMARK 465     ALA A   136                                                      
REMARK 465     ASN A   137                                                      
REMARK 465     TRP A   138                                                      
REMARK 465     GLY A   139                                                      
REMARK 465     LEU A   140                                                      
REMARK 465     ALA A   141                                                      
REMARK 465     ASN A   142                                                      
REMARK 465     SER A   143                                                      
REMARK 465     VAL A   144                                                      
REMARK 465     SER A   145                                                      
REMARK 465     SER A   398                                                      
REMARK 465     ASP A   399                                                      
REMARK 465     CYS A   400                                                      
REMARK 465     GLU A   401                                                      
REMARK 465     GLY A   402                                                      
REMARK 465     HIS A   403                                                      
REMARK 465     HIS A   404                                                      
REMARK 465     HIS A   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     HIS A   407                                                      
REMARK 465     HIS A   408                                                      
REMARK 465     MSE B    -1                                                      
REMARK 465     VAL B   127                                                      
REMARK 465     ARG B   128                                                      
REMARK 465     THR B   129                                                      
REMARK 465     ALA B   130                                                      
REMARK 465     LYS B   131                                                      
REMARK 465     GLN B   132                                                      
REMARK 465     GLN B   133                                                      
REMARK 465     SER B   134                                                      
REMARK 465     VAL B   135                                                      
REMARK 465     ALA B   136                                                      
REMARK 465     ASN B   137                                                      
REMARK 465     TRP B   138                                                      
REMARK 465     GLY B   139                                                      
REMARK 465     LEU B   140                                                      
REMARK 465     ALA B   141                                                      
REMARK 465     ASN B   142                                                      
REMARK 465     SER B   143                                                      
REMARK 465     VAL B   144                                                      
REMARK 465     SER B   145                                                      
REMARK 465     ALA B   146                                                      
REMARK 465     CYS B   400                                                      
REMARK 465     GLU B   401                                                      
REMARK 465     GLY B   402                                                      
REMARK 465     HIS B   403                                                      
REMARK 465     HIS B   404                                                      
REMARK 465     HIS B   405                                                      
REMARK 465     HIS B   406                                                      
REMARK 465     HIS B   407                                                      
REMARK 465     HIS B   408                                                      
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    PHE A  14       79.89   -118.49                                   
REMARK 500    TYR A  36      141.72     66.08                                   
REMARK 500    ALA A  77       47.14    -90.90                                   
REMARK 500    TYR A 148       63.29   -108.02                                   
REMARK 500    HIS A 156      -36.07   -131.63                                   
REMARK 500    ASP A 250      -64.70    -97.49                                   
REMARK 500    THR A 274      172.77     68.14                                   
REMARK 500    ASP A 321     -106.31   -111.92                                   
REMARK 500    CYS A 322       19.90     48.92                                   
REMARK 500    THR A 323     -137.53   -127.84                                   
REMARK 500    LEU A 342      -65.81   -120.40                                   
REMARK 500    TYR B  36      145.31     65.94                                   
REMARK 500    TRP B  48      -46.82   -134.51                                   
REMARK 500    SER B  76     -157.49   -158.27                                   
REMARK 500    ALA B  77       40.42    -92.17                                   
REMARK 500    TYR B 148       75.79   -109.64                                   
REMARK 500    ARG B 157       58.43   -118.47                                   
REMARK 500    ASP B 245       59.01     36.43                                   
REMARK 500    ASP B 250      -70.15   -100.05                                   
REMARK 500    THR B 274      170.43     69.00                                   
REMARK 500    ASP B 321     -100.68   -113.89                                   
REMARK 500    CYS B 322       25.46     42.36                                   
REMARK 500    THR B 323     -131.80   -130.41                                   
REMARK 500    LEU B 342      -61.43   -103.52                                   
REMARK 500    MSE B 383      131.50    -39.03                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 409  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 218   OE1                                                    
REMARK 620 2 GLU A 244   OE2  81.3                                              
REMARK 620 3 GLU A 270   OE2 135.7  96.5                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA B 409  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU B 218   OE1                                                    
REMARK 620 2 GLU B 244   OE2  70.8                                              
REMARK 620 3 GLU B 270   OE2 126.5  87.9                                        
REMARK 620 N                    1     2                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 409                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA B 409                  
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: NYSGXRC-9253E   RELATED DB: TARGETDB                     
DBREF  2POD A    2   400  UNP    Q63IJ7   Q63IJ7_BURPS     2    400             
DBREF  2POD B    2   400  UNP    Q63IJ7   Q63IJ7_BURPS     2    400             
SEQADV 2POD MSE A   -1  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD SER A    0  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD LEU A    1  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD MSE A   81  UNP  Q63IJ7    MET    81 MODIFIED RESIDUE               
SEQADV 2POD MSE A  173  UNP  Q63IJ7    MET   173 MODIFIED RESIDUE               
SEQADV 2POD MSE A  213  UNP  Q63IJ7    MET   213 MODIFIED RESIDUE               
SEQADV 2POD MSE A  216  UNP  Q63IJ7    MET   216 MODIFIED RESIDUE               
SEQADV 2POD MSE A  249  UNP  Q63IJ7    MET   249 MODIFIED RESIDUE               
SEQADV 2POD MSE A  291  UNP  Q63IJ7    MET   291 MODIFIED RESIDUE               
SEQADV 2POD MSE A  309  UNP  Q63IJ7    MET   309 MODIFIED RESIDUE               
SEQADV 2POD MSE A  383  UNP  Q63IJ7    MET   383 MODIFIED RESIDUE               
SEQADV 2POD GLU A  401  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD GLY A  402  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS A  403  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS A  404  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS A  405  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS A  406  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS A  407  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS A  408  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD MSE B   -1  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD SER B    0  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD LEU B    1  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD MSE B   81  UNP  Q63IJ7    MET    81 MODIFIED RESIDUE               
SEQADV 2POD MSE B  173  UNP  Q63IJ7    MET   173 MODIFIED RESIDUE               
SEQADV 2POD MSE B  213  UNP  Q63IJ7    MET   213 MODIFIED RESIDUE               
SEQADV 2POD MSE B  216  UNP  Q63IJ7    MET   216 MODIFIED RESIDUE               
SEQADV 2POD MSE B  249  UNP  Q63IJ7    MET   249 MODIFIED RESIDUE               
SEQADV 2POD MSE B  291  UNP  Q63IJ7    MET   291 MODIFIED RESIDUE               
SEQADV 2POD MSE B  309  UNP  Q63IJ7    MET   309 MODIFIED RESIDUE               
SEQADV 2POD MSE B  383  UNP  Q63IJ7    MET   383 MODIFIED RESIDUE               
SEQADV 2POD GLU B  401  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD GLY B  402  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS B  403  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS B  404  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS B  405  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS B  406  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS B  407  UNP  Q63IJ7              CLONING ARTIFACT               
SEQADV 2POD HIS B  408  UNP  Q63IJ7              CLONING ARTIFACT               
SEQRES   1 A  410  MSE SER LEU LYS ILE THR GLU ILE GLU THR LEU ARG PRO          
SEQRES   2 A  410  GLU GLU PHE PRO ASN LEU LEU TRP VAL LEU VAL HIS THR          
SEQRES   3 A  410  ASP GLU GLY ILE THR GLY LEU GLY GLU THR PHE TYR GLY          
SEQRES   4 A  410  ALA CYS SER ALA GLU ALA TYR ILE HIS GLU TRP ALA ALA          
SEQRES   5 A  410  ASN ARG LEU ILE GLY GLU ASP PRO LEU GLN ILE ASP ARG          
SEQRES   6 A  410  HIS ALA LYS ARG LEU SER GLY TYR LEU GLY PHE ARG SER          
SEQRES   7 A  410  ALA GLY ALA GLU MSE ARG GLY ASN SER ALA LEU ASP ILE          
SEQRES   8 A  410  ALA LEU TRP ASP ILE PHE GLY LYS ALA THR GLY GLN PRO          
SEQRES   9 A  410  ILE TYR GLN LEU LEU GLY GLY LYS CYS ARG ASP THR ILE          
SEQRES  10 A  410  ARG THR TYR ASN THR CYS ALA GLY PRO HIS TYR VAL ARG          
SEQRES  11 A  410  THR ALA LYS GLN GLN SER VAL ALA ASN TRP GLY LEU ALA          
SEQRES  12 A  410  ASN SER VAL SER ALA ARG TYR ASP ASP LEU ASN ALA PHE          
SEQRES  13 A  410  LEU HIS ARG ALA ASP GLU LEU ALA LEU ASP LEU LEU ASP          
SEQRES  14 A  410  SER GLY ILE THR ALA MSE LYS ILE TRP PRO PHE ASP PRO          
SEQRES  15 A  410  TYR ALA GLU ALA SER ASP GLY TYR TYR ILE SER LYS SER          
SEQRES  16 A  410  ASP LEU LYS ARG ALA LEU GLU PRO PHE GLU LYS ILE ARG          
SEQRES  17 A  410  ARG ALA VAL GLY ASP LYS MSE ASP VAL MSE VAL GLU PHE          
SEQRES  18 A  410  HIS SER LEU TRP ASN LEU PRO PRO ALA LEU GLN ILE ALA          
SEQRES  19 A  410  GLU ALA LEU ARG GLU TYR GLU THR PHE TRP HIS GLU ASP          
SEQRES  20 A  410  PRO ILE ARG MSE ASP SER LEU SER SER LEU LYS ARG TYR          
SEQRES  21 A  410  ALA GLU ARG SER LEU ALA PRO VAL CYS ALA SER GLU THR          
SEQRES  22 A  410  LEU ALA THR ARG TRP GLY PHE ARG ASP LEU LEU GLU THR          
SEQRES  23 A  410  ASN ALA ALA GLY ILE VAL MSE LEU ASP ILE SER TRP CYS          
SEQRES  24 A  410  GLY GLY LEU SER GLU ALA ARG LYS ILE ALA SER MSE ALA          
SEQRES  25 A  410  GLU ALA TRP HIS LEU PRO VAL ALA PRO HIS ASP CYS THR          
SEQRES  26 A  410  GLY PRO VAL VAL LEU THR ALA SER THR HIS LEU SER LEU          
SEQRES  27 A  410  ASN ALA PRO ASN ALA LEU VAL GLN GLU SER VAL ARG ALA          
SEQRES  28 A  410  PHE TYR ASP GLY TRP TYR ARG ASP LEU VAL THR ALA LEU          
SEQRES  29 A  410  PRO THR VAL LYS ASP GLY HIS ILE THR VAL PRO ASP GLY          
SEQRES  30 A  410  PRO GLY LEU GLY LEU GLU LEU MSE PRO ASP ILE ARG GLU          
SEQRES  31 A  410  ARG LEU THR ILE ALA VAL ARG ASN THR SER ASP CYS GLU          
SEQRES  32 A  410  GLY HIS HIS HIS HIS HIS HIS                                  
SEQRES   1 B  410  MSE SER LEU LYS ILE THR GLU ILE GLU THR LEU ARG PRO          
SEQRES   2 B  410  GLU GLU PHE PRO ASN LEU LEU TRP VAL LEU VAL HIS THR          
SEQRES   3 B  410  ASP GLU GLY ILE THR GLY LEU GLY GLU THR PHE TYR GLY          
SEQRES   4 B  410  ALA CYS SER ALA GLU ALA TYR ILE HIS GLU TRP ALA ALA          
SEQRES   5 B  410  ASN ARG LEU ILE GLY GLU ASP PRO LEU GLN ILE ASP ARG          
SEQRES   6 B  410  HIS ALA LYS ARG LEU SER GLY TYR LEU GLY PHE ARG SER          
SEQRES   7 B  410  ALA GLY ALA GLU MSE ARG GLY ASN SER ALA LEU ASP ILE          
SEQRES   8 B  410  ALA LEU TRP ASP ILE PHE GLY LYS ALA THR GLY GLN PRO          
SEQRES   9 B  410  ILE TYR GLN LEU LEU GLY GLY LYS CYS ARG ASP THR ILE          
SEQRES  10 B  410  ARG THR TYR ASN THR CYS ALA GLY PRO HIS TYR VAL ARG          
SEQRES  11 B  410  THR ALA LYS GLN GLN SER VAL ALA ASN TRP GLY LEU ALA          
SEQRES  12 B  410  ASN SER VAL SER ALA ARG TYR ASP ASP LEU ASN ALA PHE          
SEQRES  13 B  410  LEU HIS ARG ALA ASP GLU LEU ALA LEU ASP LEU LEU ASP          
SEQRES  14 B  410  SER GLY ILE THR ALA MSE LYS ILE TRP PRO PHE ASP PRO          
SEQRES  15 B  410  TYR ALA GLU ALA SER ASP GLY TYR TYR ILE SER LYS SER          
SEQRES  16 B  410  ASP LEU LYS ARG ALA LEU GLU PRO PHE GLU LYS ILE ARG          
SEQRES  17 B  410  ARG ALA VAL GLY ASP LYS MSE ASP VAL MSE VAL GLU PHE          
SEQRES  18 B  410  HIS SER LEU TRP ASN LEU PRO PRO ALA LEU GLN ILE ALA          
SEQRES  19 B  410  GLU ALA LEU ARG GLU TYR GLU THR PHE TRP HIS GLU ASP          
SEQRES  20 B  410  PRO ILE ARG MSE ASP SER LEU SER SER LEU LYS ARG TYR          
SEQRES  21 B  410  ALA GLU ARG SER LEU ALA PRO VAL CYS ALA SER GLU THR          
SEQRES  22 B  410  LEU ALA THR ARG TRP GLY PHE ARG ASP LEU LEU GLU THR          
SEQRES  23 B  410  ASN ALA ALA GLY ILE VAL MSE LEU ASP ILE SER TRP CYS          
SEQRES  24 B  410  GLY GLY LEU SER GLU ALA ARG LYS ILE ALA SER MSE ALA          
SEQRES  25 B  410  GLU ALA TRP HIS LEU PRO VAL ALA PRO HIS ASP CYS THR          
SEQRES  26 B  410  GLY PRO VAL VAL LEU THR ALA SER THR HIS LEU SER LEU          
SEQRES  27 B  410  ASN ALA PRO ASN ALA LEU VAL GLN GLU SER VAL ARG ALA          
SEQRES  28 B  410  PHE TYR ASP GLY TRP TYR ARG ASP LEU VAL THR ALA LEU          
SEQRES  29 B  410  PRO THR VAL LYS ASP GLY HIS ILE THR VAL PRO ASP GLY          
SEQRES  30 B  410  PRO GLY LEU GLY LEU GLU LEU MSE PRO ASP ILE ARG GLU          
SEQRES  31 B  410  ARG LEU THR ILE ALA VAL ARG ASN THR SER ASP CYS GLU          
SEQRES  32 B  410  GLY HIS HIS HIS HIS HIS HIS                                  
MODRES 2POD MSE A   81  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  173  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  213  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  216  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  249  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  291  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  309  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE A  383  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B   81  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  173  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  213  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  216  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  249  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  291  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  309  MET  SELENOMETHIONINE                                   
MODRES 2POD MSE B  383  MET  SELENOMETHIONINE                                   
HET    MSE  A  81       8                                                       
HET    MSE  A 173       8                                                       
HET    MSE  A 213       8                                                       
HET    MSE  A 216       8                                                       
HET    MSE  A 249       8                                                       
HET    MSE  A 291       8                                                       
HET    MSE  A 309       8                                                       
HET    MSE  A 383       8                                                       
HET    MSE  B  81       8                                                       
HET    MSE  B 173       8                                                       
HET    MSE  B 213       8                                                       
HET    MSE  B 216       8                                                       
HET    MSE  B 249       8                                                       
HET    MSE  B 291       8                                                       
HET    MSE  B 309       8                                                       
HET    MSE  B 383       8                                                       
HET     NA  A 409       1                                                       
HET     NA  B 409       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM      NA SODIUM ION                                                       
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3   NA    2(NA 1+)                                                     
FORMUL   5  HOH   *152(H2 O)                                                    
HELIX    1   1 GLY A   37  TRP A   48  1                                  12    
HELIX    2   2 ALA A   49  ILE A   54  1                                   6    
HELIX    3   3 GLN A   60  LEU A   68  1                                   9    
HELIX    4   4 GLY A   78  GLY A  100  1                                  23    
HELIX    5   5 PRO A  102  LEU A  107  1                                   6    
HELIX    6   6 ASP A  149  ARG A  157  1                                   9    
HELIX    7   7 ARG A  157  GLY A  169  1                                  13    
HELIX    8   8 PHE A  178  ASP A  186  5                                   9    
HELIX    9   9 SER A  191  LEU A  199  1                                   9    
HELIX   10  10 LEU A  199  VAL A  209  1                                  11    
HELIX   11  11 GLY A  210  MSE A  213  5                                   4    
HELIX   12  12 ASN A  224  ARG A  236  1                                  13    
HELIX   13  13 GLU A  237  GLU A  239  5                                   3    
HELIX   14  14 SER A  251  SER A  253  5                                   3    
HELIX   15  15 SER A  254  ARG A  261  1                                   8    
HELIX   16  16 ALA A  273  THR A  284  1                                  12    
HELIX   17  17 GLY A  298  TRP A  313  1                                  16    
HELIX   18  18 GLY A  324  ALA A  338  1                                  15    
HELIX   19  19 VAL A  347  ASP A  352  1                                   6    
HELIX   20  20 ASP A  385  LEU A  390  1                                   6    
HELIX   21  21 GLY B   37  TRP B   48  1                                  12    
HELIX   22  22 TRP B   48  ILE B   54  1                                   7    
HELIX   23  23 GLN B   60  LEU B   68  1                                   9    
HELIX   24  24 GLY B   78  GLY B  100  1                                  23    
HELIX   25  25 PRO B  102  LEU B  107  1                                   6    
HELIX   26  26 ASP B  149  ARG B  157  1                                   9    
HELIX   27  27 ARG B  157  GLY B  169  1                                  13    
HELIX   28  28 PHE B  178  GLU B  183  1                                   6    
HELIX   29  29 SER B  191  LEU B  199  1                                   9    
HELIX   30  30 LEU B  199  VAL B  209  1                                  11    
HELIX   31  31 GLY B  210  MSE B  213  5                                   4    
HELIX   32  32 ASN B  224  ARG B  236  1                                  13    
HELIX   33  33 GLU B  237  GLU B  239  5                                   3    
HELIX   34  34 SER B  251  SER B  253  5                                   3    
HELIX   35  35 SER B  254  SER B  262  1                                   9    
HELIX   36  36 ALA B  273  THR B  284  1                                  12    
HELIX   37  37 GLY B  298  TRP B  313  1                                  16    
HELIX   38  38 GLY B  324  ALA B  338  1                                  15    
HELIX   39  39 VAL B  347  ASP B  352  1                                   6    
HELIX   40  40 ASP B  385  LEU B  390  1                                   6    
SHEET    1   A 4 THR A  29  PHE A  35  0                                        
SHEET    2   A 4 LEU A  17  THR A  24 -1  N  VAL A  20   O  GLY A  32           
SHEET    3   A 4 ILE A   3  PRO A  11 -1  N  GLU A   5   O  HIS A  23           
SHEET    4   A 4 ILE A 392  THR A 397 -1  O  ALA A 393   N  ARG A  10           
SHEET    1   B 8 VAL A 317  PRO A 319  0                                        
SHEET    2   B 8 ALA A 287  LEU A 292  1  N  VAL A 290   O  ALA A 318           
SHEET    3   B 8 VAL A 266  ALA A 268  1  N  VAL A 266   O  GLY A 288           
SHEET    4   B 8 TRP A 242  GLU A 244  1  N  HIS A 243   O  CYS A 267           
SHEET    5   B 8 ASP A 214  GLU A 218  1  N  VAL A 217   O  GLU A 244           
SHEET    6   B 8 ALA A 172  ILE A 175  1  N  MSE A 173   O  MSE A 216           
SHEET    7   B 8 ILE A 115  THR A 120  1  N  ASN A 119   O  ALA A 172           
SHEET    8   B 8 GLN A 344  SER A 346  1  O  GLN A 344   N  ARG A 116           
SHEET    1   C 9 VAL A 317  PRO A 319  0                                        
SHEET    2   C 9 ALA A 287  LEU A 292  1  N  VAL A 290   O  ALA A 318           
SHEET    3   C 9 VAL A 266  ALA A 268  1  N  VAL A 266   O  GLY A 288           
SHEET    4   C 9 TRP A 242  GLU A 244  1  N  HIS A 243   O  CYS A 267           
SHEET    5   C 9 ASP A 214  GLU A 218  1  N  VAL A 217   O  GLU A 244           
SHEET    6   C 9 ALA A 172  ILE A 175  1  N  MSE A 173   O  MSE A 216           
SHEET    7   C 9 ILE A 115  THR A 120  1  N  ASN A 119   O  ALA A 172           
SHEET    8   C 9 HIS A 369  THR A 371 -1  O  ILE A 370   N  ILE A 115           
SHEET    9   C 9 THR A 364  LYS A 366 -1  N  LYS A 366   O  HIS A 369           
SHEET    1   D 4 THR B  29  PHE B  35  0                                        
SHEET    2   D 4 LEU B  17  THR B  24 -1  N  VAL B  20   O  GLY B  32           
SHEET    3   D 4 ILE B   3  PRO B  11 -1  N  GLU B   5   O  HIS B  23           
SHEET    4   D 4 ILE B 392  SER B 398 -1  O  ALA B 393   N  ARG B  10           
SHEET    1   E 8 VAL B 317  PRO B 319  0                                        
SHEET    2   E 8 ALA B 287  LEU B 292  1  N  VAL B 290   O  ALA B 318           
SHEET    3   E 8 VAL B 266  ALA B 268  1  N  ALA B 268   O  MSE B 291           
SHEET    4   E 8 TRP B 242  GLU B 244  1  N  HIS B 243   O  CYS B 267           
SHEET    5   E 8 ASP B 214  GLU B 218  1  N  VAL B 217   O  GLU B 244           
SHEET    6   E 8 ALA B 172  ILE B 175  1  N  ILE B 175   O  GLU B 218           
SHEET    7   E 8 ILE B 115  THR B 120  1  N  ASN B 119   O  ALA B 172           
SHEET    8   E 8 GLN B 344  SER B 346  1  O  SER B 346   N  TYR B 118           
SHEET    1   F 9 VAL B 317  PRO B 319  0                                        
SHEET    2   F 9 ALA B 287  LEU B 292  1  N  VAL B 290   O  ALA B 318           
SHEET    3   F 9 VAL B 266  ALA B 268  1  N  ALA B 268   O  MSE B 291           
SHEET    4   F 9 TRP B 242  GLU B 244  1  N  HIS B 243   O  CYS B 267           
SHEET    5   F 9 ASP B 214  GLU B 218  1  N  VAL B 217   O  GLU B 244           
SHEET    6   F 9 ALA B 172  ILE B 175  1  N  ILE B 175   O  GLU B 218           
SHEET    7   F 9 ILE B 115  THR B 120  1  N  ASN B 119   O  ALA B 172           
SHEET    8   F 9 HIS B 369  THR B 371 -1  O  ILE B 370   N  ILE B 115           
SHEET    9   F 9 THR B 364  LYS B 366 -1  N  LYS B 366   O  HIS B 369           
LINK         C   GLU A  80                 N   MSE A  81     1555   1555  1.33  
LINK         C   MSE A  81                 N   ARG A  82     1555   1555  1.33  
LINK         C   ALA A 172                 N   MSE A 173     1555   1555  1.33  
LINK         C   MSE A 173                 N   LYS A 174     1555   1555  1.33  
LINK         C   LYS A 212                 N   MSE A 213     1555   1555  1.33  
LINK         C   MSE A 213                 N   ASP A 214     1555   1555  1.33  
LINK         C   VAL A 215                 N   MSE A 216     1555   1555  1.32  
LINK         C   MSE A 216                 N   VAL A 217     1555   1555  1.33  
LINK         C   ARG A 248                 N   MSE A 249     1555   1555  1.33  
LINK         C   MSE A 249                 N   ASP A 250     1555   1555  1.33  
LINK         C   VAL A 290                 N   MSE A 291     1555   1555  1.33  
LINK         C   MSE A 291                 N   LEU A 292     1555   1555  1.33  
LINK         C   SER A 308                 N   MSE A 309     1555   1555  1.33  
LINK         C   MSE A 309                 N   ALA A 310     1555   1555  1.33  
LINK         C   LEU A 382                 N   MSE A 383     1555   1555  1.33  
LINK         C   MSE A 383                 N   PRO A 384     1555   1555  1.35  
LINK         C   GLU B  80                 N   MSE B  81     1555   1555  1.33  
LINK         C   MSE B  81                 N   ARG B  82     1555   1555  1.33  
LINK         C   ALA B 172                 N   MSE B 173     1555   1555  1.34  
LINK         C   MSE B 173                 N   LYS B 174     1555   1555  1.33  
LINK         C   LYS B 212                 N   MSE B 213     1555   1555  1.33  
LINK         C   MSE B 213                 N   ASP B 214     1555   1555  1.33  
LINK         C   VAL B 215                 N   MSE B 216     1555   1555  1.33  
LINK         C   MSE B 216                 N   VAL B 217     1555   1555  1.33  
LINK         C   ARG B 248                 N   MSE B 249     1555   1555  1.33  
LINK         C   MSE B 249                 N   ASP B 250     1555   1555  1.33  
LINK         C   VAL B 290                 N   MSE B 291     1555   1555  1.33  
LINK         C   MSE B 291                 N   LEU B 292     1555   1555  1.33  
LINK         C   SER B 308                 N   MSE B 309     1555   1555  1.33  
LINK         C   MSE B 309                 N   ALA B 310     1555   1555  1.33  
LINK         C   LEU B 382                 N   MSE B 383     1555   1555  1.33  
LINK         C   MSE B 383                 N   PRO B 384     1555   1555  1.35  
LINK         OE1 GLU A 218                NA    NA A 409     1555   1555  2.09  
LINK         OE2 GLU A 244                NA    NA A 409     1555   1555  2.20  
LINK         OE2 GLU A 270                NA    NA A 409     1555   1555  2.12  
LINK         OE1 GLU B 218                NA    NA B 409     1555   1555  2.26  
LINK         OE2 GLU B 244                NA    NA B 409     1555   1555  2.65  
LINK         OE2 GLU B 270                NA    NA B 409     1555   1555  2.19  
CISPEP   1 ALA A  268    SER A  269          0       -22.61                     
CISPEP   2 ALA B  268    SER B  269          0       -21.50                     
SITE     1 AC1  5 LYS A 174  GLU A 218  GLU A 244  GLU A 270                    
SITE     2 AC1  5 HIS A 320                                                     
SITE     1 AC2  5 LYS B 174  GLU B 218  GLU B 244  GLU B 270                    
SITE     2 AC2  5 HIS B 320                                                     
CRYST1  146.771  146.771   85.531  90.00  90.00  90.00 I 4          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      0.006813  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.006813  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011692        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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