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Database: PDB
Entry: 1O6C
LinkDB: 1O6C
Original site: 1O6C 
HEADER    ISOMERASE                               03-NOV-03   1O6C              
TITLE     CRYSTAL STRUCTURE OF UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UDP-N-ACETYLGLUCOSAMINE 2-EPIMERASE;                       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: UDP-GLCNAC-2-EPIMERASE;                                     
COMPND   5 EC: 5.1.3.14;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS SUBTILIS;                              
SOURCE   3 ORGANISM_TAXID: 1423;                                                
SOURCE   4 GENE: MNAA, BSU35660;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    STRUCTURAL GENOMICS, ISOMERASE                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    STRUCTURAL GENOMIX                                                    
REVDAT   7   27-DEC-23 1O6C    1       SEQADV LINK                              
REVDAT   6   04-OCT-17 1O6C    1       REMARK                                   
REVDAT   5   13-JUL-11 1O6C    1       VERSN                                    
REVDAT   4   24-FEB-09 1O6C    1       VERSN                                    
REVDAT   3   30-AUG-05 1O6C    1       JRNL                                     
REVDAT   2   30-DEC-03 1O6C    1       JRNL                                     
REVDAT   1   25-NOV-03 1O6C    0                                                
JRNL        AUTH   J.BADGER,J.M.SAUDER,J.M.ADAMS,S.ANTONYSAMY,K.BAIN,           
JRNL        AUTH 2 M.G.BERGSEID,S.G.BUCHANAN,M.D.BUCHANAN,Y.BATIYENKO,          
JRNL        AUTH 3 J.A.CHRISTOPHER,S.EMTAGE,A.EROSHKINA,I.FEIL,E.B.FURLONG,     
JRNL        AUTH 4 K.S.GAJIWALA,X.GAO,D.HE,J.HENDLE,A.HUBER,K.HODA,P.KEARINS,   
JRNL        AUTH 5 C.KISSINGER,B.LAUBERT,H.A.LEWIS,J.LIN,K.LOOMIS,D.LORIMER,    
JRNL        AUTH 6 G.LOUIE,M.MALETIC,C.D.MARSH,I.MILLER,J.MOLINARI,             
JRNL        AUTH 7 H.J.MULLER-DIECKMANN,J.M.NEWMAN,B.W.NOLAND,B.PAGARIGAN,      
JRNL        AUTH 8 F.PARK,T.S.PEAT,K.W.POST,S.RADOJICIC,A.RAMOS,R.ROMERO,       
JRNL        AUTH 9 M.E.RUTTER,W.E.SANDERSON,K.D.SCHWINN,J.TRESSER,J.WINHOVEN,   
JRNL        AUTH10 T.A.WRIGHT,L.WU,J.XU,T.J.HARRIS                              
JRNL        TITL   STRUCTURAL ANALYSIS OF A SET OF PROTEINS RESULTING FROM A    
JRNL        TITL 2 BACTERIAL GENOMICS PROJECT                                   
JRNL        REF    PROTEINS                      V.  60   787 2005              
JRNL        REFN                   ISSN 0887-3585                               
JRNL        PMID   16021622                                                     
JRNL        DOI    10.1002/PROT.20541                                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 4.0                                           
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 48.71                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : 21936                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.274                           
REMARK   3   FREE R VALUE                     : 0.334                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : 2141                            
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5495                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 12                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 49.12                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.65300                                             
REMARK   3    B22 (A**2) : -0.65300                                             
REMARK   3    B33 (A**2) : 1.30600                                              
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): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): NULL          
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): NULL          
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): NULL          
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : 0.012 ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : 2.120 ; NULL                
REMARK   3    INTRAPLANAR 1-4 DISTANCE        (A) : NULL  ; NULL                
REMARK   3    H-BOND OR METAL COORDINATION    (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   PLANE RESTRAINT                  (A) : 0.013 ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : 0.135 ; NULL                
REMARK   3                                                                      
REMARK   3   NON-BONDED CONTACT RESTRAINTS.                                     
REMARK   3    SINGLE TORSION                  (A) : NULL  ; NULL                
REMARK   3    MULTIPLE TORSION                (A) : NULL  ; NULL                
REMARK   3    H-BOND (X...Y)                  (A) : NULL  ; NULL                
REMARK   3    H-BOND (X-H...Y)                (A) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3   CONFORMATIONAL TORSION ANGLE RESTRAINTS.                           
REMARK   3    SPECIFIED                 (DEGREES) : NULL  ; NULL                
REMARK   3    PLANAR                    (DEGREES) : 2.883 ; NULL                
REMARK   3    STAGGERED                 (DEGREES) : NULL  ; NULL                
REMARK   3    TRANSVERSE                (DEGREES) : NULL  ; NULL                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : 2.137 ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 3.962 ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : 3.581 ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 5.544 ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1O6C COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 05-NOV-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000001850.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 32-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9795                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM, TRUNCATE                   
REMARK 200  DATA SCALING SOFTWARE          : SCALA, CCP4 (SCALA, TRUNCATE       
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21936                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 48.710                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : 0.07200                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 21.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.06                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 6.40                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 8.300                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SE-MET SAD PHASING           
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 52.86                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.61                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 43 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+3/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+1/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+3/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+1/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-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      226.21500            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       31.91000            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       31.91000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000      339.32250            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       31.91000            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       31.91000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      113.10750            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       31.91000            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       31.91000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000      339.32250            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       31.91000            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       31.91000            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      113.10750            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000      226.21500            
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA,PQS                                              
REMARK 350 TOTAL BURIED SURFACE AREA: 2710 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 30590 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -22.0 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 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     ALA A   206                                                      
REMARK 465     HIS A   207                                                      
REMARK 465     ARG A   208                                                      
REMARK 465     ARG A   209                                                      
REMARK 465     GLU A   210                                                      
REMARK 465     ASN A   211                                                      
REMARK 465     LEU A   212                                                      
REMARK 465     GLY A   213                                                      
REMARK 465     GLU A   214                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     VAL A   239                                                      
REMARK 465     HIS A   240                                                      
REMARK 465     LEU A   241                                                      
REMARK 465     ASN A   242                                                      
REMARK 465     PHE A   253                                                      
REMARK 465     GLY A   254                                                      
REMARK 465     SER A   284                                                      
REMARK 465     GLY A   285                                                      
REMARK 465     ARG A   307                                                      
REMARK 465     PRO A   308                                                      
REMARK 465     GLU A   309                                                      
REMARK 465     GLY A   379                                                      
REMARK 465     LYS A   380                                                      
REMARK 465     GLY A   381                                                      
REMARK 465     SER A   382                                                      
REMARK 465     HIS A   383                                                      
REMARK 465     HIS A   384                                                      
REMARK 465     HIS A   385                                                      
REMARK 465     HIS A   386                                                      
REMARK 465     HIS A   387                                                      
REMARK 465     HIS A   388                                                      
REMARK 465     HIS B   207                                                      
REMARK 465     ARG B   208                                                      
REMARK 465     ARG B   209                                                      
REMARK 465     GLU B   210                                                      
REMARK 465     ASN B   211                                                      
REMARK 465     LEU B   212                                                      
REMARK 465     GLY B   213                                                      
REMARK 465     GLU B   214                                                      
REMARK 465     LYS B   380                                                      
REMARK 465     GLY B   381                                                      
REMARK 465     SER B   382                                                      
REMARK 465     HIS B   383                                                      
REMARK 465     HIS B   384                                                      
REMARK 465     HIS B   385                                                      
REMARK 465     HIS B   386                                                      
REMARK 465     HIS B   387                                                      
REMARK 465     HIS B   388                                                      
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     GLN A  41    CD   OE1  NE2                                       
REMARK 470     GLN A  44    CG   CD   OE1  NE2                                  
REMARK 470     MSE A  45    CB   CG  SE    CE                                   
REMARK 470     LEU A  46    CD1  CD2                                            
REMARK 470     ASP A  47    CG   OD1  OD2                                       
REMARK 470     GLU A  66    CB   CG   CD   OE1  OE2                             
REMARK 470     GLU A  83    CG   CD   OE1  OE2                                  
REMARK 470     ASP A  87    CG   OD1  OD2                                       
REMARK 470     SER A 189    CB   OG                                             
REMARK 470     PRO A 191    CG   CD                                             
REMARK 470     LEU A 193    CG   CD1  CD2                                       
REMARK 470     GLU A 198    CG   CD   OE1  OE2                                  
REMARK 470     ASP A 199    CB   CG   OD1  OD2                                  
REMARK 470     LYS A 200    CD   CE   NZ                                        
REMARK 470     MSE A 216    CB   CG  SE    CE                                   
REMARK 470     GLU A 217    CB   CG   CD   OE1  OE2                             
REMARK 470     MSE A 219    CB   CG  SE    CE                                   
REMARK 470     LYS A 221    CG   CD   CE   NZ                                   
REMARK 470     GLU A 231    CB   CG   CD   OE1  OE2                             
REMARK 470     ASP A 232    CG   OD1  OD2                                       
REMARK 470     VAL A 245    CB   CG1  CG2                                       
REMARK 470     ARG A 246    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     GLU A 247    CG   CD   OE1  OE2                                  
REMARK 470     HIS A 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS A 251    NZ                                                  
REMARK 470     ASP A 255    CG   OD1  OD2                                       
REMARK 470     ASP A 257    CG   OD1  OD2                                       
REMARK 470     ARG A 258    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     VAL A 259    CG1  CG2                                            
REMARK 470     LEU A 261    CD1  CD2                                            
REMARK 470     ILE A 262    CG1  CG2  CD1                                       
REMARK 470     LEU A 265    CG   CD1  CD2                                       
REMARK 470     GLU A 266    CG   CD   OE1  OE2                                  
REMARK 470     ILE A 268    CG1  CG2  CD1                                       
REMARK 470     SER A 277    CB   OG                                             
REMARK 470     GLU A 289    CG   CD   OE1  OE2                                  
REMARK 470     PRO A 292    CG   CD                                             
REMARK 470     ARG A 302    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     ASP A 303    CG   OD1  OD2                                       
REMARK 470     VAL A 311    CG1  CG2                                            
REMARK 470     THR A 315    OG1  CG2                                            
REMARK 470     LEU A 316    CB   CG   CD1  CD2                                  
REMARK 470     LYS A 317    CD   CE   NZ                                        
REMARK 470     GLN A 332    CG   CD   OE1  NE2                                  
REMARK 470     ASP A 338    CG   OD1  OD2                                       
REMARK 470     TYR A 340    CG   CD1  CD2  CE1  CE2  CZ   OH                    
REMARK 470     LYS A 342    CB   CG   CD   CE   NZ                              
REMARK 470     SER A 344    OG                                                  
REMARK 470     LYS A 371    CD   CE   NZ                                        
REMARK 470     ASP A 375    CG   OD1  OD2                                       
REMARK 470     PHE A 377    CG   CD1  CD2  CE1  CE2  CZ                         
REMARK 470     GLU B  83    CB   CG   CD   OE1  OE2                             
REMARK 470     LYS B  86    CD   CE   NZ                                        
REMARK 470     ASP B 186    CG   OD1  OD2                                       
REMARK 470     PRO B 215    CG   CD                                             
REMARK 470     GLU B 231    CG   CD   OE1  OE2                                  
REMARK 470     GLU B 247    CG   CD   OE1  OE2                                  
REMARK 470     HIS B 250    CG   ND1  CD2  CE1  NE2                             
REMARK 470     LYS B 251    CD   CE   NZ                                        
REMARK 470     ASP B 255    CG   OD1  OD2                                       
REMARK 470     SER B 256    OG                                                  
REMARK 470     ASP B 257    CG   OD1  OD2                                       
REMARK 470     ARG B 302    CB   CG   CD   NE   CZ   NH1  NH2                   
REMARK 470     THR B 304    OG1  CG2                                            
REMARK 470     GLU B 306    CB   CG   CD   OE1  OE2                             
REMARK 470     THR B 321    OG1  CG2                                            
REMARK 470     ASP B 338    CB   CG   OD1  OD2                                  
REMARK 470     LYS B 342    CG   CD   CE   NZ                                   
REMARK 470     LYS B 371    CG   CD   CE   NZ                                   
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 370   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.4 DEGREES          
REMARK 500    ARG B  80   NE  -  CZ  -  NH1 ANGL. DEV. =  -4.8 DEGREES          
REMARK 500    ARG B 138   NE  -  CZ  -  NH2 ANGL. DEV. =  -3.7 DEGREES          
REMARK 500    ARG B 225   NE  -  CZ  -  NH1 ANGL. DEV. =   3.3 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    ILE A  17      -76.34    -61.44                                   
REMARK 500    LYS A  18      -26.50    -37.29                                   
REMARK 500    THR A  39       54.38   -111.34                                   
REMARK 500    GLU A 120       60.60     67.53                                   
REMARK 500    ALA A 145      130.01    -36.83                                   
REMARK 500    ASP A 167        2.75    -57.87                                   
REMARK 500    ASN A 181       11.17    -64.02                                   
REMARK 500    THR A 182      -34.50   -134.64                                   
REMARK 500    VAL A 267      -66.15    -28.06                                   
REMARK 500    GLN A 288        3.72    -62.76                                   
REMARK 500    THR A 335      -74.72    -81.36                                   
REMARK 500    ASP A 336      103.34    -47.04                                   
REMARK 500    LYS B  27        1.57    -67.24                                   
REMARK 500    SER B 130      107.47   -165.73                                   
REMARK 500    LEU B 241      152.91    -44.47                                   
REMARK 500    ASP B 283       11.23   -153.24                                   
REMARK 500    ARG B 307       75.42   -117.97                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: MAIN CHAIN PLANARITY                                       
REMARK 500                                                                      
REMARK 500 THE FOLLOWING RESIDUES HAVE A PSEUDO PLANARITY                       
REMARK 500 TORSION ANGLE, C(I) - CA(I) - N(I+1) - O(I), GREATER                 
REMARK 500 10.0 DEGREES. (M=MODEL NUMBER; RES=RESIDUE NAME;                     
REMARK 500 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;                            
REMARK 500 I=INSERTION CODE).                                                   
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        ANGLE                                           
REMARK 500    ASP B  58         10.38                                           
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
DBREF  1O6C A    2   380  UNP    P39131   MNAA_BACSU       2    380             
DBREF  1O6C B    2   380  UNP    P39131   MNAA_BACSU       2    380             
SEQADV 1O6C MSE A    1  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C MSE A    7  UNP  P39131    MET     7 MODIFIED RESIDUE               
SEQADV 1O6C MSE A   19  UNP  P39131    MET    19 MODIFIED RESIDUE               
SEQADV 1O6C MSE A   45  UNP  P39131    MET    45 MODIFIED RESIDUE               
SEQADV 1O6C MSE A   64  UNP  P39131    MET    64 MODIFIED RESIDUE               
SEQADV 1O6C MSE A  140  UNP  P39131    MET   140 MODIFIED RESIDUE               
SEQADV 1O6C MSE A  201  UNP  P39131    MET   201 MODIFIED RESIDUE               
SEQADV 1O6C MSE A  216  UNP  P39131    MET   216 MODIFIED RESIDUE               
SEQADV 1O6C MSE A  219  UNP  P39131    MET   219 MODIFIED RESIDUE               
SEQADV 1O6C MSE A  343  UNP  P39131    MET   343 MODIFIED RESIDUE               
SEQADV 1O6C GLY A  381  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C SER A  382  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS A  383  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS A  384  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS A  385  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS A  386  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS A  387  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS A  388  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C MSE B    1  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C MSE B    7  UNP  P39131    MET     7 MODIFIED RESIDUE               
SEQADV 1O6C MSE B   19  UNP  P39131    MET    19 MODIFIED RESIDUE               
SEQADV 1O6C MSE B   45  UNP  P39131    MET    45 MODIFIED RESIDUE               
SEQADV 1O6C MSE B   64  UNP  P39131    MET    64 MODIFIED RESIDUE               
SEQADV 1O6C MSE B  140  UNP  P39131    MET   140 MODIFIED RESIDUE               
SEQADV 1O6C MSE B  201  UNP  P39131    MET   201 MODIFIED RESIDUE               
SEQADV 1O6C MSE B  216  UNP  P39131    MET   216 MODIFIED RESIDUE               
SEQADV 1O6C MSE B  219  UNP  P39131    MET   219 MODIFIED RESIDUE               
SEQADV 1O6C MSE B  343  UNP  P39131    MET   343 MODIFIED RESIDUE               
SEQADV 1O6C GLY B  381  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C SER B  382  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS B  383  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS B  384  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS B  385  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS B  386  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS B  387  UNP  P39131              CLONING ARTIFACT               
SEQADV 1O6C HIS B  388  UNP  P39131              CLONING ARTIFACT               
SEQRES   1 A  388  MSE LYS LYS LEU LYS VAL MSE THR VAL PHE GLY THR ARG          
SEQRES   2 A  388  PRO GLU ALA ILE LYS MSE ALA PRO LEU VAL LEU GLU LEU          
SEQRES   3 A  388  LYS LYS TYR PRO GLU ILE ASP SER TYR VAL THR VAL THR          
SEQRES   4 A  388  ALA GLN HIS ARG GLN MSE LEU ASP GLN VAL LEU ASP ALA          
SEQRES   5 A  388  PHE HIS ILE LYS PRO ASP PHE ASP LEU ASN ILE MSE LYS          
SEQRES   6 A  388  GLU ARG GLN THR LEU ALA GLU ILE THR SER ASN ALA LEU          
SEQRES   7 A  388  VAL ARG LEU ASP GLU LEU PHE LYS ASP ILE LYS PRO ASP          
SEQRES   8 A  388  ILE VAL LEU VAL HIS GLY ASP THR THR THR THR PHE ALA          
SEQRES   9 A  388  GLY SER LEU ALA ALA PHE TYR HIS GLN ILE ALA VAL GLY          
SEQRES  10 A  388  HIS VAL GLU ALA GLY LEU ARG THR GLY ASN LYS TYR SER          
SEQRES  11 A  388  PRO PHE PRO GLU GLU LEU ASN ARG GLN MSE THR GLY ALA          
SEQRES  12 A  388  ILE ALA ASP LEU HIS PHE ALA PRO THR GLY GLN ALA LYS          
SEQRES  13 A  388  ASP ASN LEU LEU LYS GLU ASN LYS LYS ALA ASP SER ILE          
SEQRES  14 A  388  PHE VAL THR GLY ASN THR ALA ILE ASP ALA LEU ASN THR          
SEQRES  15 A  388  THR VAL ARG ASP GLY TYR SER HIS PRO VAL LEU ASP GLN          
SEQRES  16 A  388  VAL GLY GLU ASP LYS MSE ILE LEU LEU THR ALA HIS ARG          
SEQRES  17 A  388  ARG GLU ASN LEU GLY GLU PRO MSE GLU ASN MSE PHE LYS          
SEQRES  18 A  388  ALA ILE ARG ARG ILE VAL GLY GLU PHE GLU ASP VAL GLN          
SEQRES  19 A  388  VAL VAL TYR PRO VAL HIS LEU ASN PRO VAL VAL ARG GLU          
SEQRES  20 A  388  ALA ALA HIS LYS HIS PHE GLY ASP SER ASP ARG VAL HIS          
SEQRES  21 A  388  LEU ILE GLU PRO LEU GLU VAL ILE ASP PHE HIS ASN PHE          
SEQRES  22 A  388  ALA ALA LYS SER HIS PHE ILE LEU THR ASP SER GLY GLY          
SEQRES  23 A  388  VAL GLN GLU GLU ALA PRO SER LEU GLY LYS PRO VAL LEU          
SEQRES  24 A  388  VAL LEU ARG ASP THR THR GLU ARG PRO GLU GLY VAL GLU          
SEQRES  25 A  388  ALA GLY THR LEU LYS LEU ALA GLY THR ASP GLU GLU ASN          
SEQRES  26 A  388  ILE TYR GLN LEU ALA LYS GLN LEU LEU THR ASP PRO ASP          
SEQRES  27 A  388  GLU TYR LYS LYS MSE SER GLN ALA SER ASN PRO TYR GLY          
SEQRES  28 A  388  ASP GLY GLU ALA SER ARG ARG ILE VAL GLU GLU LEU LEU          
SEQRES  29 A  388  PHE HIS TYR GLY TYR ARG LYS GLU GLN PRO ASP SER PHE          
SEQRES  30 A  388  THR GLY LYS GLY SER HIS HIS HIS HIS HIS HIS                  
SEQRES   1 B  388  MSE LYS LYS LEU LYS VAL MSE THR VAL PHE GLY THR ARG          
SEQRES   2 B  388  PRO GLU ALA ILE LYS MSE ALA PRO LEU VAL LEU GLU LEU          
SEQRES   3 B  388  LYS LYS TYR PRO GLU ILE ASP SER TYR VAL THR VAL THR          
SEQRES   4 B  388  ALA GLN HIS ARG GLN MSE LEU ASP GLN VAL LEU ASP ALA          
SEQRES   5 B  388  PHE HIS ILE LYS PRO ASP PHE ASP LEU ASN ILE MSE LYS          
SEQRES   6 B  388  GLU ARG GLN THR LEU ALA GLU ILE THR SER ASN ALA LEU          
SEQRES   7 B  388  VAL ARG LEU ASP GLU LEU PHE LYS ASP ILE LYS PRO ASP          
SEQRES   8 B  388  ILE VAL LEU VAL HIS GLY ASP THR THR THR THR PHE ALA          
SEQRES   9 B  388  GLY SER LEU ALA ALA PHE TYR HIS GLN ILE ALA VAL GLY          
SEQRES  10 B  388  HIS VAL GLU ALA GLY LEU ARG THR GLY ASN LYS TYR SER          
SEQRES  11 B  388  PRO PHE PRO GLU GLU LEU ASN ARG GLN MSE THR GLY ALA          
SEQRES  12 B  388  ILE ALA ASP LEU HIS PHE ALA PRO THR GLY GLN ALA LYS          
SEQRES  13 B  388  ASP ASN LEU LEU LYS GLU ASN LYS LYS ALA ASP SER ILE          
SEQRES  14 B  388  PHE VAL THR GLY ASN THR ALA ILE ASP ALA LEU ASN THR          
SEQRES  15 B  388  THR VAL ARG ASP GLY TYR SER HIS PRO VAL LEU ASP GLN          
SEQRES  16 B  388  VAL GLY GLU ASP LYS MSE ILE LEU LEU THR ALA HIS ARG          
SEQRES  17 B  388  ARG GLU ASN LEU GLY GLU PRO MSE GLU ASN MSE PHE LYS          
SEQRES  18 B  388  ALA ILE ARG ARG ILE VAL GLY GLU PHE GLU ASP VAL GLN          
SEQRES  19 B  388  VAL VAL TYR PRO VAL HIS LEU ASN PRO VAL VAL ARG GLU          
SEQRES  20 B  388  ALA ALA HIS LYS HIS PHE GLY ASP SER ASP ARG VAL HIS          
SEQRES  21 B  388  LEU ILE GLU PRO LEU GLU VAL ILE ASP PHE HIS ASN PHE          
SEQRES  22 B  388  ALA ALA LYS SER HIS PHE ILE LEU THR ASP SER GLY GLY          
SEQRES  23 B  388  VAL GLN GLU GLU ALA PRO SER LEU GLY LYS PRO VAL LEU          
SEQRES  24 B  388  VAL LEU ARG ASP THR THR GLU ARG PRO GLU GLY VAL GLU          
SEQRES  25 B  388  ALA GLY THR LEU LYS LEU ALA GLY THR ASP GLU GLU ASN          
SEQRES  26 B  388  ILE TYR GLN LEU ALA LYS GLN LEU LEU THR ASP PRO ASP          
SEQRES  27 B  388  GLU TYR LYS LYS MSE SER GLN ALA SER ASN PRO TYR GLY          
SEQRES  28 B  388  ASP GLY GLU ALA SER ARG ARG ILE VAL GLU GLU LEU LEU          
SEQRES  29 B  388  PHE HIS TYR GLY TYR ARG LYS GLU GLN PRO ASP SER PHE          
SEQRES  30 B  388  THR GLY LYS GLY SER HIS HIS HIS HIS HIS HIS                  
MODRES 1O6C MSE A    7  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A   19  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A   45  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A   64  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A  201  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A  216  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A  219  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE A  343  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B    1  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B    7  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B   19  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B   45  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B   64  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B  140  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B  201  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B  216  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B  219  MET  SELENOMETHIONINE                                   
MODRES 1O6C MSE B  343  MET  SELENOMETHIONINE                                   
HET    MSE  A   7       8                                                       
HET    MSE  A  19       8                                                       
HET    MSE  A  45       4                                                       
HET    MSE  A  64       8                                                       
HET    MSE  A 140       8                                                       
HET    MSE  A 201       8                                                       
HET    MSE  A 216       4                                                       
HET    MSE  A 219       4                                                       
HET    MSE  A 343       8                                                       
HET    MSE  B   1       8                                                       
HET    MSE  B   7       8                                                       
HET    MSE  B  19       8                                                       
HET    MSE  B  45       8                                                       
HET    MSE  B  64       8                                                       
HET    MSE  B 140       8                                                       
HET    MSE  B 201       8                                                       
HET    MSE  B 216       8                                                       
HET    MSE  B 219       8                                                       
HET    MSE  B 343       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    19(C5 H11 N O2 SE)                                           
FORMUL   3  HOH   *12(H2 O)                                                     
HELIX    1   1 THR A   12  LEU A   26  1                                  15    
HELIX    2   2 LYS A   27  TYR A   29  5                                   3    
HELIX    3   3 HIS A   42  MSE A   45  5                                   4    
HELIX    4   4 LEU A   46  PHE A   53  1                                   8    
HELIX    5   5 THR A   69  LYS A   89  1                                  21    
HELIX    6   6 THR A   99  HIS A  112  1                                  14    
HELIX    7   7 PRO A  133  ALA A  145  1                                  13    
HELIX    8   8 THR A  152  GLU A  162  1                                  11    
HELIX    9   9 LYS A  165  ASP A  167  5                                   3    
HELIX   10  10 ASN A  174  VAL A  184  1                                  11    
HELIX   11  11 MSE A  216  PHE A  230  1                                  15    
HELIX   12  12 PRO A  243  HIS A  252  1                                  10    
HELIX   13  13 GLU A  266  SER A  277  1                                  12    
HELIX   14  14 GLY A  286  ALA A  291  1                                   6    
HELIX   15  15 PRO A  292  GLY A  295  5                                   4    
HELIX   16  16 ASP A  322  ASP A  336  1                                  15    
HELIX   17  17 ASP A  336  ALA A  346  1                                  11    
HELIX   18  18 GLU A  354  TYR A  367  1                                  14    
HELIX   19  19 THR B   12  LYS B   27  1                                  16    
HELIX   20  20 HIS B   42  MSE B   45  5                                   4    
HELIX   21  21 LEU B   46  PHE B   53  1                                   8    
HELIX   22  22 THR B   69  LYS B   89  1                                  21    
HELIX   23  23 THR B   99  HIS B  112  1                                  14    
HELIX   24  24 PRO B  133  ALA B  145  1                                  13    
HELIX   25  25 THR B  152  LYS B  161  1                                  10    
HELIX   26  26 LYS B  165  ASP B  167  5                                   3    
HELIX   27  27 ASN B  174  VAL B  184  1                                  11    
HELIX   28  28 HIS B  190  GLY B  197  1                                   8    
HELIX   29  29 PRO B  215  PHE B  230  1                                  16    
HELIX   30  30 ASN B  242  PHE B  253  1                                  12    
HELIX   31  31 GLU B  266  SER B  277  1                                  12    
HELIX   32  32 SER B  284  ALA B  291  1                                   8    
HELIX   33  33 PRO B  292  GLY B  295  5                                   4    
HELIX   34  34 ARG B  307  ALA B  313  1                                   7    
HELIX   35  35 ASP B  322  ASP B  336  1                                  15    
HELIX   36  36 ASP B  336  GLN B  345  1                                  10    
HELIX   37  37 GLU B  354  TYR B  367  1                                  14    
SHEET    1   A 7 PHE A  59  ASP A  60  0                                        
SHEET    2   A 7 ILE A  32  VAL A  38  1  N  VAL A  38   O  PHE A  59           
SHEET    3   A 7 LEU A   4  PHE A  10  1  N  PHE A  10   O  THR A  37           
SHEET    4   A 7 ILE A  92  HIS A  96  1  O  LEU A  94   N  MSE A   7           
SHEET    5   A 7 ALA A 115  VAL A 119  1  O  ALA A 115   N  VAL A  93           
SHEET    6   A 7 LEU A 147  ALA A 150  1  O  LEU A 147   N  HIS A 118           
SHEET    7   A 7 ILE A 169  VAL A 171  1  O  PHE A 170   N  HIS A 148           
SHEET    1   B 6 VAL A 259  LEU A 261  0                                        
SHEET    2   B 6 VAL A 233  TYR A 237  1  N  TYR A 237   O  HIS A 260           
SHEET    3   B 6 LYS A 200  LEU A 204  1  N  ILE A 202   O  GLN A 234           
SHEET    4   B 6 PHE A 279  THR A 282  1  O  LEU A 281   N  LEU A 203           
SHEET    5   B 6 VAL A 298  LEU A 301  1  O  LEU A 301   N  THR A 282           
SHEET    6   B 6 LYS A 317  ALA A 319  1  O  ALA A 319   N  VAL A 300           
SHEET    1   C 7 PHE B  59  ASP B  60  0                                        
SHEET    2   C 7 ILE B  32  VAL B  38  1  N  VAL B  38   O  PHE B  59           
SHEET    3   C 7 LEU B   4  PHE B  10  1  N  VAL B   6   O  TYR B  35           
SHEET    4   C 7 ILE B  92  HIS B  96  1  O  LEU B  94   N  MSE B   7           
SHEET    5   C 7 ALA B 115  VAL B 119  1  O  VAL B 119   N  VAL B  95           
SHEET    6   C 7 LEU B 147  ALA B 150  1  O  LEU B 147   N  HIS B 118           
SHEET    7   C 7 ILE B 169  VAL B 171  1  O  PHE B 170   N  ALA B 150           
SHEET    1   D 6 VAL B 259  ILE B 262  0                                        
SHEET    2   D 6 VAL B 233  PRO B 238  1  N  TYR B 237   O  HIS B 260           
SHEET    3   D 6 LYS B 200  LEU B 204  1  N  ILE B 202   O  GLN B 234           
SHEET    4   D 6 PHE B 279  THR B 282  1  O  LEU B 281   N  LEU B 203           
SHEET    5   D 6 VAL B 298  VAL B 300  1  O  LEU B 299   N  ILE B 280           
SHEET    6   D 6 LEU B 316  LEU B 318  1  O  LYS B 317   N  VAL B 300           
LINK         C   VAL A   6                 N   MSE A   7     1555   1555  1.33  
LINK         C   MSE A   7                 N   THR A   8     1555   1555  1.32  
LINK         C   LYS A  18                 N   MSE A  19     1555   1555  1.30  
LINK         C   MSE A  19                 N   ALA A  20     1555   1555  1.34  
LINK         C   GLN A  44                 N   MSE A  45     1555   1555  1.33  
LINK         C   MSE A  45                 N   LEU A  46     1555   1555  1.33  
LINK         C   ILE A  63                 N   MSE A  64     1555   1555  1.32  
LINK         C   MSE A  64                 N   LYS A  65     1555   1555  1.33  
LINK         C   GLN A 139                 N   MSE A 140     1555   1555  1.33  
LINK         C   MSE A 140                 N   THR A 141     1555   1555  1.33  
LINK         C   LYS A 200                 N   MSE A 201     1555   1555  1.33  
LINK         C   MSE A 201                 N   ILE A 202     1555   1555  1.32  
LINK         C   MSE A 216                 N   GLU A 217     1555   1555  1.33  
LINK         C   ASN A 218                 N   MSE A 219     1555   1555  1.33  
LINK         C   MSE A 219                 N   PHE A 220     1555   1555  1.33  
LINK         C   LYS A 342                 N   MSE A 343     1555   1555  1.33  
LINK         C   MSE A 343                 N   SER A 344     1555   1555  1.32  
LINK         C   MSE B   1                 N   LYS B   2     1555   1555  1.34  
LINK         C   VAL B   6                 N   MSE B   7     1555   1555  1.33  
LINK         C   MSE B   7                 N   THR B   8     1555   1555  1.32  
LINK         C   LYS B  18                 N   MSE B  19     1555   1555  1.30  
LINK         C   MSE B  19                 N   ALA B  20     1555   1555  1.33  
LINK         C   GLN B  44                 N   MSE B  45     1555   1555  1.33  
LINK         C   MSE B  45                 N   LEU B  46     1555   1555  1.33  
LINK         C   ILE B  63                 N   MSE B  64     1555   1555  1.34  
LINK         C   MSE B  64                 N   LYS B  65     1555   1555  1.33  
LINK         C   GLN B 139                 N   MSE B 140     1555   1555  1.33  
LINK         C   MSE B 140                 N   THR B 141     1555   1555  1.33  
LINK         C   LYS B 200                 N   MSE B 201     1555   1555  1.35  
LINK         C   MSE B 201                 N   ILE B 202     1555   1555  1.33  
LINK         C   PRO B 215                 N   MSE B 216     1555   1555  1.34  
LINK         C   MSE B 216                 N   GLU B 217     1555   1555  1.33  
LINK         C   ASN B 218                 N   MSE B 219     1555   1555  1.32  
LINK         C   MSE B 219                 N   PHE B 220     1555   1555  1.32  
LINK         C   LYS B 342                 N   MSE B 343     1555   1555  1.33  
LINK         C   MSE B 343                 N   SER B 344     1555   1555  1.32  
CISPEP   1 SER A  130    PRO A  131          0        -1.24                     
CISPEP   2 PHE A  132    PRO A  133          0        -0.66                     
CISPEP   3 SER B  130    PRO B  131          0        -2.56                     
CISPEP   4 PHE B  132    PRO B  133          0         1.71                     
CRYST1   63.820   63.820  452.430  90.00  90.00  90.00 P 43 21 2    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      0.015669  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.015669  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.002210        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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