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Database: PDB
Entry: 3S40
LinkDB: 3S40
Original site: 3S40 
HEADER    TRANSFERASE                             18-MAY-11   3S40              
TITLE     THE CRYSTAL STRUCTURE OF A DIACYLGLYCEROL KINASES FROM BACILLUS       
TITLE    2 ANTHRACIS STR. STERNE                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DIACYLGLYCEROL KINASE;                                     
COMPND   3 CHAIN: A, B, C, D;                                                   
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX,ANTHRAX BACTERIUM;                          
SOURCE   4 ORGANISM_TAXID: 260799;                                              
SOURCE   5 STRAIN: STERNE;                                                      
SOURCE   6 GENE: BAS4713, BA_5075, GBAA_5075;                                   
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: P15TV LIC                                 
KEYWDS    DIACYLGLYCEROL KINASES, STRUCTURAL GENOMICS, THE CENTER FOR           
KEYWDS   2 STRUCTURAL GENOMICS OF INFECTIOUS DISEASES, CSGID, TRANSFERASE       
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.TAN,R.ZHANG,X.XU,H.CUI,S.PETERSON,A.SAVCHENKO,W.F.ANDERSON,         
AUTHOR   2 A.JOACHIMIAK,CENTER FOR STRUCTURAL GENOMICS OF INFECTIOUS DISEASES   
AUTHOR   3 (CSGID)                                                              
REVDAT   3   06-DEC-23 3S40    1       REMARK                                   
REVDAT   2   13-SEP-23 3S40    1       SEQADV LINK                              
REVDAT   1   01-JUN-11 3S40    0                                                
JRNL        AUTH   K.TAN,R.ZHANG,X.XU,H.CUI,S.PETERSON,A.SAVCHENKO,             
JRNL        AUTH 2 W.F.ANDERSON,A.JOACHIMIAK                                    
JRNL        TITL   THE CRYSTAL STRUCTURE OF A DIACYLGLYCEROL KINASES FROM       
JRNL        TITL 2 BACILLUS ANTHRACIS STR. STERNE                               
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7_650)                      
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 43.23                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.6                           
REMARK   3   NUMBER OF REFLECTIONS             : 58777                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.178                           
REMARK   3   R VALUE            (WORKING SET) : 0.175                           
REMARK   3   FREE R VALUE                     : 0.238                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.070                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2979                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 43.2406 -  5.7886    0.99     2891   130  0.1638 0.2179        
REMARK   3     2  5.7886 -  4.5963    1.00     2880   140  0.1435 0.1949        
REMARK   3     3  4.5963 -  4.0158    1.00     2848   158  0.1419 0.1778        
REMARK   3     4  4.0158 -  3.6488    1.00     2820   144  0.1473 0.2078        
REMARK   3     5  3.6488 -  3.3874    1.00     2847   156  0.1643 0.2192        
REMARK   3     6  3.3874 -  3.1877    0.99     2769   167  0.1826 0.2218        
REMARK   3     7  3.1877 -  3.0281    0.98     2818   132  0.1885 0.2823        
REMARK   3     8  3.0281 -  2.8963    0.98     2793   143  0.2161 0.3072        
REMARK   3     9  2.8963 -  2.7849    0.97     2764   153  0.1955 0.2901        
REMARK   3    10  2.7849 -  2.6888    0.96     2704   156  0.1978 0.2454        
REMARK   3    11  2.6888 -  2.6047    0.95     2717   128  0.1962 0.3247        
REMARK   3    12  2.6047 -  2.5303    0.95     2667   156  0.1933 0.2513        
REMARK   3    13  2.5303 -  2.4637    0.93     2617   139  0.1900 0.2835        
REMARK   3    14  2.4637 -  2.4036    0.92     2624   138  0.1905 0.2605        
REMARK   3    15  2.4036 -  2.3489    0.90     2523   149  0.1952 0.2895        
REMARK   3    16  2.3489 -  2.2989    0.90     2581   127  0.1854 0.2448        
REMARK   3    17  2.2989 -  2.2530    0.89     2491   143  0.1931 0.2222        
REMARK   3    18  2.2530 -  2.2104    0.87     2453   134  0.1974 0.3054        
REMARK   3    19  2.2104 -  2.1710    0.86     2432   122  0.2094 0.3139        
REMARK   3    20  2.1710 -  2.1342    0.84     2378   134  0.2380 0.2971        
REMARK   3    21  2.1342 -  2.0997    0.77     2181   130  0.2604 0.3527        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 43.94                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 24.480           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.19460                                             
REMARK   3    B22 (A**2) : 0.26840                                              
REMARK   3    B33 (A**2) : 3.92620                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.49340                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.007           8776                                  
REMARK   3   ANGLE     :  1.077          11902                                  
REMARK   3   CHIRALITY :  0.075           1382                                  
REMARK   3   PLANARITY :  0.005           1528                                  
REMARK   3   DIHEDRAL  : 15.333           3171                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: ALL                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  25.7048  33.0817  37.1669              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1217 T22:   0.0942                                     
REMARK   3      T33:   0.0958 T12:  -0.0028                                     
REMARK   3      T13:  -0.0224 T23:   0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.5572 L22:   0.1781                                     
REMARK   3      L33:   0.3274 L12:   0.0478                                     
REMARK   3      L13:  -0.1427 L23:  -0.0095                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0603 S12:  -0.0160 S13:  -0.0759                       
REMARK   3      S21:   0.0355 S22:  -0.0313 S23:  -0.0081                       
REMARK   3      S31:  -0.0823 S32:   0.0137 S33:  -0.0009                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 3S40 COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 19-MAY-11.                  
REMARK 100 THE DEPOSITION ID IS D_1000065732.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-DEC-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 19-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97924                            
REMARK 200  MONOCHROMATOR                  : SI 111 CRYSTAL                     
REMARK 200  OPTICS                         : MIRROR                             
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-3000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-3000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 62575                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 44.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 4.900                              
REMARK 200  R MERGE                    (I) : 0.09000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 16.7000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.14                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.65600                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 1.400                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: PDB ENTRY 2QVL                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 40.14                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.05                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS, 0.4M NH4CL, 16% PEG       
REMARK 280  3350, 4% JEFFAMINE M-600, PH 5.8, VAPOR DIFFUSION, SITTING DROP,    
REMARK 280  TEMPERATURE 289K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       65.37900            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2, 3, 4, 5                                           
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 300 REMARK: EXPERIMENTALLY UNKNOWN. IT IS PREDICTED THAT THE MOLECULE    
REMARK 300 IS MONOMERIC.                                                        
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 3                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 4                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: D                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 5                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6380 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 44260 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B, C, D                            
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MSE A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     LEU A   144                                                      
REMARK 465     VAL A   145                                                      
REMARK 465     SER A   146                                                      
REMARK 465     GLU A   147                                                      
REMARK 465     VAL A   148                                                      
REMARK 465     SER A   149                                                      
REMARK 465     ASN A   150                                                      
REMARK 465     ASN A   151                                                      
REMARK 465     ILE A   152                                                      
REMARK 465     ASP A   153                                                      
REMARK 465     ALA A   154                                                      
REMARK 465     GLU A   155                                                      
REMARK 465     GLU A   156                                                      
REMARK 465     LYS A   157                                                      
REMARK 465     ALA A   158                                                      
REMARK 465     LYS A   159                                                      
REMARK 465     LEU A   160                                                      
REMARK 465     GLY A   161                                                      
REMARK 465     ARG A   171                                                      
REMARK 465     THR A   172                                                      
REMARK 465     VAL A   173                                                      
REMARK 465     LYS A   174                                                      
REMARK 465     ASN A   175                                                      
REMARK 465     ALA A   176                                                      
REMARK 465     GLY A   274                                                      
REMARK 465     GLU A   275                                                      
REMARK 465     GLY A   301                                                      
REMARK 465     SER A   302                                                      
REMARK 465     GLY B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MSE B     1                                                      
REMARK 465     LYS B   174                                                      
REMARK 465     SER B   247                                                      
REMARK 465     ASN B   248                                                      
REMARK 465     GLU B   249                                                      
REMARK 465     ASN B   250                                                      
REMARK 465     ASP B   251                                                      
REMARK 465     GLY B   301                                                      
REMARK 465     SER B   302                                                      
REMARK 465     GLY C    -1                                                      
REMARK 465     HIS C     0                                                      
REMARK 465     MSE C     1                                                      
REMARK 465     THR C     2                                                      
REMARK 465     LEU C   144                                                      
REMARK 465     VAL C   145                                                      
REMARK 465     SER C   146                                                      
REMARK 465     GLU C   147                                                      
REMARK 465     VAL C   148                                                      
REMARK 465     SER C   149                                                      
REMARK 465     ASN C   150                                                      
REMARK 465     ASN C   151                                                      
REMARK 465     ILE C   152                                                      
REMARK 465     LYS C   174                                                      
REMARK 465     ASN C   175                                                      
REMARK 465     GLY C   301                                                      
REMARK 465     SER C   302                                                      
REMARK 465     GLY D    -1                                                      
REMARK 465     HIS D     0                                                      
REMARK 465     MSE D     1                                                      
REMARK 465     THR D     2                                                      
REMARK 465     SER D   146                                                      
REMARK 465     GLU D   147                                                      
REMARK 465     VAL D   148                                                      
REMARK 465     SER D   149                                                      
REMARK 465     ASN D   150                                                      
REMARK 465     ASN D   151                                                      
REMARK 465     ILE D   152                                                      
REMARK 465     ASP D   153                                                      
REMARK 465     ALA D   154                                                      
REMARK 465     GLU D   155                                                      
REMARK 465     GLU D   156                                                      
REMARK 465     LYS D   157                                                      
REMARK 465     ALA D   158                                                      
REMARK 465     LYS D   159                                                      
REMARK 465     LEU D   160                                                      
REMARK 465     ILE D   170                                                      
REMARK 465     ARG D   171                                                      
REMARK 465     THR D   172                                                      
REMARK 465     VAL D   173                                                      
REMARK 465     LYS D   174                                                      
REMARK 465     ASN D   175                                                      
REMARK 465     GLY D   187                                                      
REMARK 465     GLY D   240                                                      
REMARK 465     LYS D   241                                                      
REMARK 465     LYS D   242                                                      
REMARK 465     LEU D   243                                                      
REMARK 465     PHE D   244                                                      
REMARK 465     GLU D   245                                                      
REMARK 465     ASP D   246                                                      
REMARK 465     SER D   247                                                      
REMARK 465     ASN D   248                                                      
REMARK 465     GLU D   249                                                      
REMARK 465     ASN D   250                                                      
REMARK 465     ASP D   251                                                      
REMARK 465     GLY D   301                                                      
REMARK 465     SER D   302                                                      
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     LYS A 162    CG   CD   CE   NZ                                   
REMARK 470     ILE A 163    CG1  CG2  CD1                                       
REMARK 470     ARG B 171    CG   CD   NE   CZ   NH1  NH2                        
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    ASN A 138      -60.98   -107.51                                   
REMARK 500    ASP A 192     -177.84   -175.04                                   
REMARK 500    ASN A 201      -40.97   -130.25                                   
REMARK 500    ASN A 214       28.87     47.73                                   
REMARK 500    ASN A 248       72.64   -108.34                                   
REMARK 500    GLU A 249      -14.88    -49.73                                   
REMARK 500    ASN B 132       56.49     36.86                                   
REMARK 500    ASN B 138      -63.01   -102.80                                   
REMARK 500    ASP B 192     -176.95    173.29                                   
REMARK 500    PHE B 244       48.31   -106.52                                   
REMARK 500    ASN C 132       63.63     32.54                                   
REMARK 500    ASN C 138      -65.84    -98.12                                   
REMARK 500    LYS C 241       47.87    -97.38                                   
REMARK 500    ASP C 246      -76.80    -96.73                                   
REMARK 500    GLU C 267       93.78    -55.05                                   
REMARK 500    GLU C 275      107.86    -49.08                                   
REMARK 500    ASN D 132       66.36     34.98                                   
REMARK 500    ASN D 138      -73.55    -95.74                                   
REMARK 500    PHE D 179      130.54   -179.33                                   
REMARK 500    ASP D 192     -179.24   -176.95                                   
REMARK 500    THR D 230       26.89    -75.43                                   
REMARK 500    GLU D 265      -84.32    -36.99                                   
REMARK 500    GLU D 267      164.68    -47.91                                   
REMARK 500    SER D 277       54.16   -107.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: IDP90228   RELATED DB: TARGETDB                          
DBREF  3S40 A    1   300  UNP    Q81KC6   Q81KC6_BACAN     1    300             
DBREF  3S40 B    1   300  UNP    Q81KC6   Q81KC6_BACAN     1    300             
DBREF  3S40 C    1   300  UNP    Q81KC6   Q81KC6_BACAN     1    300             
DBREF  3S40 D    1   300  UNP    Q81KC6   Q81KC6_BACAN     1    300             
SEQADV 3S40 GLY A   -1  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 HIS A    0  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY A  301  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 SER A  302  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY B   -1  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 HIS B    0  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY B  301  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 SER B  302  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY C   -1  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 HIS C    0  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY C  301  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 SER C  302  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY D   -1  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 HIS D    0  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 GLY D  301  UNP  Q81KC6              EXPRESSION TAG                 
SEQADV 3S40 SER D  302  UNP  Q81KC6              EXPRESSION TAG                 
SEQRES   1 A  304  GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU          
SEQRES   2 A  304  ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR          
SEQRES   3 A  304  ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE          
SEQRES   4 A  304  PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP          
SEQRES   5 A  304  ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP          
SEQRES   6 A  304  LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU          
SEQRES   7 A  304  CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR          
SEQRES   8 A  304  LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER          
SEQRES   9 A  304  ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA          
SEQRES  10 A  304  LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL          
SEQRES  11 A  304  ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY          
SEQRES  12 A  304  ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA          
SEQRES  13 A  304  GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU          
SEQRES  14 A  304  SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO          
SEQRES  15 A  304  VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU          
SEQRES  16 A  304  ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY          
SEQRES  17 A  304  GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP          
SEQRES  18 A  304  GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE          
SEQRES  19 A  304  GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU          
SEQRES  20 A  304  ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS          
SEQRES  21 A  304  SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP          
SEQRES  22 A  304  THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE          
SEQRES  23 A  304  GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO          
SEQRES  24 A  304  ALA VAL VAL GLY SER                                          
SEQRES   1 B  304  GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU          
SEQRES   2 B  304  ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR          
SEQRES   3 B  304  ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE          
SEQRES   4 B  304  PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP          
SEQRES   5 B  304  ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP          
SEQRES   6 B  304  LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU          
SEQRES   7 B  304  CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR          
SEQRES   8 B  304  LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER          
SEQRES   9 B  304  ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA          
SEQRES  10 B  304  LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL          
SEQRES  11 B  304  ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY          
SEQRES  12 B  304  ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA          
SEQRES  13 B  304  GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU          
SEQRES  14 B  304  SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO          
SEQRES  15 B  304  VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU          
SEQRES  16 B  304  ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY          
SEQRES  17 B  304  GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP          
SEQRES  18 B  304  GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE          
SEQRES  19 B  304  GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU          
SEQRES  20 B  304  ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS          
SEQRES  21 B  304  SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP          
SEQRES  22 B  304  THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE          
SEQRES  23 B  304  GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO          
SEQRES  24 B  304  ALA VAL VAL GLY SER                                          
SEQRES   1 C  304  GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU          
SEQRES   2 C  304  ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR          
SEQRES   3 C  304  ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE          
SEQRES   4 C  304  PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP          
SEQRES   5 C  304  ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP          
SEQRES   6 C  304  LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU          
SEQRES   7 C  304  CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR          
SEQRES   8 C  304  LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER          
SEQRES   9 C  304  ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA          
SEQRES  10 C  304  LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL          
SEQRES  11 C  304  ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY          
SEQRES  12 C  304  ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA          
SEQRES  13 C  304  GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU          
SEQRES  14 C  304  SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO          
SEQRES  15 C  304  VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU          
SEQRES  16 C  304  ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY          
SEQRES  17 C  304  GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP          
SEQRES  18 C  304  GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE          
SEQRES  19 C  304  GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU          
SEQRES  20 C  304  ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS          
SEQRES  21 C  304  SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP          
SEQRES  22 C  304  THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE          
SEQRES  23 C  304  GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO          
SEQRES  24 C  304  ALA VAL VAL GLY SER                                          
SEQRES   1 D  304  GLY HIS MSE THR LYS THR LYS PHE GLU LYS VAL LEU LEU          
SEQRES   2 D  304  ILE VAL ASN PRO LYS ALA GLY GLN GLY ASP LEU HIS THR          
SEQRES   3 D  304  ASN LEU THR LYS ILE VAL PRO PRO LEU ALA ALA ALA PHE          
SEQRES   4 D  304  PRO ASP LEU HIS ILE LEU HIS THR LYS GLU GLN GLY ASP          
SEQRES   5 D  304  ALA THR LYS TYR CYS GLN GLU PHE ALA SER LYS VAL ASP          
SEQRES   6 D  304  LEU ILE ILE VAL PHE GLY GLY ASP GLY THR VAL PHE GLU          
SEQRES   7 D  304  CYS THR ASN GLY LEU ALA PRO LEU GLU ILE ARG PRO THR          
SEQRES   8 D  304  LEU ALA ILE ILE PRO GLY GLY THR CYS ASN ASP PHE SER          
SEQRES   9 D  304  ARG THR LEU GLY VAL PRO GLN ASN ILE ALA GLU ALA ALA          
SEQRES  10 D  304  LYS LEU ILE THR LYS GLU HIS VAL LYS PRO VAL ASP VAL          
SEQRES  11 D  304  ALA LYS ALA ASN GLY GLN HIS PHE LEU ASN PHE TRP GLY          
SEQRES  12 D  304  ILE GLY LEU VAL SER GLU VAL SER ASN ASN ILE ASP ALA          
SEQRES  13 D  304  GLU GLU LYS ALA LYS LEU GLY LYS ILE GLY TYR TYR LEU          
SEQRES  14 D  304  SER THR ILE ARG THR VAL LYS ASN ALA GLU THR PHE PRO          
SEQRES  15 D  304  VAL LYS ILE THR TYR ASP GLY GLN VAL TYR GLU ASP GLU          
SEQRES  16 D  304  ALA VAL LEU VAL MSE VAL GLY ASN GLY GLU TYR LEU GLY          
SEQRES  17 D  304  GLY ILE PRO SER PHE ILE PRO ASN VAL LYS CYS ASP ASP          
SEQRES  18 D  304  GLY THR LEU ASP ILE PHE VAL VAL LYS SER THR GLY ILE          
SEQRES  19 D  304  GLN ALA PHE LYS ASP TYR ILE GLY LYS LYS LEU PHE GLU          
SEQRES  20 D  304  ASP SER ASN GLU ASN ASP ILE PHE HIS VAL LYS ALA LYS          
SEQRES  21 D  304  SER ILE HIS ILE GLU THR GLU GLU GLU LYS GLU VAL ASP          
SEQRES  22 D  304  THR ASP GLY GLU SER SER LEU HIS THR PRO CYS GLN ILE          
SEQRES  23 D  304  GLU LEU LEU GLN GLY HIS PHE THR MSE ILE TYR ASN PRO          
SEQRES  24 D  304  ALA VAL VAL GLY SER                                          
MODRES 3S40 MSE A  198  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE A  293  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE B  198  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE B  293  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE C  198  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE C  293  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE D  198  MET  SELENOMETHIONINE                                   
MODRES 3S40 MSE D  293  MET  SELENOMETHIONINE                                   
HET    MSE  A 198       8                                                       
HET    MSE  A 293       8                                                       
HET    MSE  B 198       8                                                       
HET    MSE  B 293       8                                                       
HET    MSE  C 198       8                                                       
HET    MSE  C 293       8                                                       
HET    MSE  D 198       8                                                       
HET    MSE  D 293       8                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
FORMUL   1  MSE    8(C5 H11 N O2 SE)                                            
FORMUL   5  HOH   *329(H2 O)                                                    
HELIX    1   1 ASP A   21  PHE A   37  1                                  17    
HELIX    2   2 GLY A   49  ALA A   59  1                                  11    
HELIX    3   3 GLY A   70  ALA A   82  1                                  13    
HELIX    4   4 ASN A   99  LEU A  105  1                                   7    
HELIX    5   5 ASN A  110  THR A  119  1                                  10    
HELIX    6   6 LYS A  162  LEU A  167  1                                   6    
HELIX    7   7 GLY A  231  ILE A  239  1                                   9    
HELIX    8   8 ASP B   21  PHE B   37  1                                  17    
HELIX    9   9 GLY B   49  ALA B   59  1                                  11    
HELIX   10  10 GLY B   70  ALA B   82  1                                  13    
HELIX   11  11 ASN B   99  LEU B  105  1                                   7    
HELIX   12  12 ASN B  110  GLU B  121  1                                  12    
HELIX   13  13 ASN B  150  THR B  169  1                                  20    
HELIX   14  14 GLY B  231  LYS B  242  1                                  12    
HELIX   15  15 ASP C   21  PHE C   37  1                                  17    
HELIX   16  16 GLY C   49  ALA C   59  1                                  11    
HELIX   17  17 GLY C   70  ALA C   82  1                                  13    
HELIX   18  18 ASN C   99  LEU C  105  1                                   7    
HELIX   19  19 ASN C  110  LYS C  120  1                                  11    
HELIX   20  20 ASP C  153  GLY C  161  1                                   9    
HELIX   21  21 GLY C  161  VAL C  173  1                                  13    
HELIX   22  22 GLY C  231  LYS C  241  1                                  11    
HELIX   23  23 ASP D   21  PHE D   37  1                                  17    
HELIX   24  24 GLY D   49  ALA D   59  1                                  11    
HELIX   25  25 GLY D   70  ALA D   82  1                                  13    
HELIX   26  26 ASN D   99  LEU D  105  1                                   7    
HELIX   27  27 ASN D  110  THR D  119  1                                  10    
HELIX   28  28 ILE D  163  THR D  169  1                                   7    
HELIX   29  29 GLY D  231  ILE D  239  1                                   9    
SHEET    1   A 8 THR A  89  PRO A  94  0                                        
SHEET    2   A 8 LEU A  64  GLY A  69  1  N  VAL A  67   O  ILE A  93           
SHEET    3   A 8 VAL A   9  VAL A  13  1  N  LEU A  10   O  ILE A  66           
SHEET    4   A 8 ASP A  39  HIS A  44  1  O  HIS A  41   N  LEU A  11           
SHEET    5   A 8 ASP B  39  HIS B  44 -1  O  LEU B  40   N  ILE A  42           
SHEET    6   A 8 VAL B   9  VAL B  13  1  N  LEU B  11   O  HIS B  41           
SHEET    7   A 8 LEU B  64  GLY B  69  1  O  ILE B  66   N  ILE B  12           
SHEET    8   A 8 THR B  89  PRO B  94  1  O  ILE B  93   N  VAL B  67           
SHEET    1   B 8 GLN A 134  PHE A 136  0                                        
SHEET    2   B 8 VAL A 123  ALA A 131 -1  N  ALA A 131   O  GLN A 134           
SHEET    3   B 8 CYS A 282  ILE A 294 -1  O  LEU A 287   N  VAL A 128           
SHEET    4   B 8 SER A 259  THR A 264 -1  N  ILE A 260   O  ILE A 284           
SHEET    5   B 8 PHE A 179  TYR A 185 -1  N  THR A 184   O  HIS A 261           
SHEET    6   B 8 GLN A 188  GLY A 200 -1  O  TYR A 190   N  ILE A 183           
SHEET    7   B 8 LEU A 222  LYS A 228 -1  O  PHE A 225   N  MSE A 198           
SHEET    8   B 8 ILE A 252  ALA A 257 -1  O  PHE A 253   N  VAL A 226           
SHEET    1   C 9 GLN A 134  PHE A 136  0                                        
SHEET    2   C 9 VAL A 123  ALA A 131 -1  N  ALA A 131   O  GLN A 134           
SHEET    3   C 9 CYS A 282  ILE A 294 -1  O  LEU A 287   N  VAL A 128           
SHEET    4   C 9 SER A 259  THR A 264 -1  N  ILE A 260   O  ILE A 284           
SHEET    5   C 9 PHE A 179  TYR A 185 -1  N  THR A 184   O  HIS A 261           
SHEET    6   C 9 GLN A 188  GLY A 200 -1  O  TYR A 190   N  ILE A 183           
SHEET    7   C 9 PHE A 139  ILE A 142 -1  N  TRP A 140   O  VAL A 199           
SHEET    8   C 9 GLU A 269  THR A 272 -1  O  ASP A 271   N  GLY A 141           
SHEET    9   C 9 LEU A 278  HIS A 279 -1  O  LEU A 278   N  VAL A 270           
SHEET    1   D 2 TYR A 204  LEU A 205  0                                        
SHEET    2   D 2 ILE A 208  PRO A 209 -1  O  ILE A 208   N  LEU A 205           
SHEET    1   E 7 GLN B 134  PHE B 136  0                                        
SHEET    2   E 7 VAL B 123  ALA B 131 -1  N  ALA B 131   O  GLN B 134           
SHEET    3   E 7 CYS B 282  ILE B 294 -1  O  GLU B 285   N  LYS B 130           
SHEET    4   E 7 SER B 259  THR B 264 -1  N  ILE B 260   O  ILE B 284           
SHEET    5   E 7 PHE B 179  TYR B 185 -1  N  LYS B 182   O  GLU B 263           
SHEET    6   E 7 VAL B 189  GLY B 200 -1  O  ASP B 192   N  VAL B 181           
SHEET    7   E 7 PHE B 139  ILE B 142 -1  N  TRP B 140   O  VAL B 199           
SHEET    1   F 8 GLN B 134  PHE B 136  0                                        
SHEET    2   F 8 VAL B 123  ALA B 131 -1  N  ALA B 131   O  GLN B 134           
SHEET    3   F 8 CYS B 282  ILE B 294 -1  O  GLU B 285   N  LYS B 130           
SHEET    4   F 8 SER B 259  THR B 264 -1  N  ILE B 260   O  ILE B 284           
SHEET    5   F 8 PHE B 179  TYR B 185 -1  N  LYS B 182   O  GLU B 263           
SHEET    6   F 8 VAL B 189  GLY B 200 -1  O  ASP B 192   N  VAL B 181           
SHEET    7   F 8 LEU B 222  LYS B 228 -1  O  PHE B 225   N  MSE B 198           
SHEET    8   F 8 PHE B 253  ALA B 257 -1  O  VAL B 255   N  ILE B 224           
SHEET    1   G 2 TYR B 204  LEU B 205  0                                        
SHEET    2   G 2 ILE B 208  PRO B 209 -1  O  ILE B 208   N  LEU B 205           
SHEET    1   H 8 THR C  89  PRO C  94  0                                        
SHEET    2   H 8 LEU C  64  GLY C  69  1  N  VAL C  67   O  ILE C  93           
SHEET    3   H 8 VAL C   9  VAL C  13  1  N  ILE C  12   O  ILE C  66           
SHEET    4   H 8 ASP C  39  HIS C  44  1  O  HIS C  41   N  LEU C  11           
SHEET    5   H 8 ASP D  39  HIS D  44 -1  O  LEU D  40   N  ILE C  42           
SHEET    6   H 8 VAL D   9  VAL D  13  1  N  VAL D  13   O  LEU D  43           
SHEET    7   H 8 LEU D  64  GLY D  69  1  O  ILE D  66   N  ILE D  12           
SHEET    8   H 8 THR D  89  PRO D  94  1  O  ILE D  93   N  VAL D  67           
SHEET    1   I 8 GLN C 134  PHE C 136  0                                        
SHEET    2   I 8 VAL C 123  ALA C 131 -1  N  ALA C 131   O  GLN C 134           
SHEET    3   I 8 CYS C 282  ILE C 294 -1  O  GLU C 285   N  LYS C 130           
SHEET    4   I 8 SER C 259  THR C 264 -1  N  ILE C 260   O  ILE C 284           
SHEET    5   I 8 PHE C 179  TYR C 185 -1  N  LYS C 182   O  GLU C 263           
SHEET    6   I 8 GLN C 188  GLY C 200 -1  O  TYR C 190   N  ILE C 183           
SHEET    7   I 8 LEU C 222  LYS C 228 -1  O  PHE C 225   N  MSE C 198           
SHEET    8   I 8 PHE C 253  ALA C 257 -1  O  VAL C 255   N  ILE C 224           
SHEET    1   J 8 GLN C 134  PHE C 136  0                                        
SHEET    2   J 8 VAL C 123  ALA C 131 -1  N  ALA C 131   O  GLN C 134           
SHEET    3   J 8 CYS C 282  ILE C 294 -1  O  GLU C 285   N  LYS C 130           
SHEET    4   J 8 SER C 259  THR C 264 -1  N  ILE C 260   O  ILE C 284           
SHEET    5   J 8 PHE C 179  TYR C 185 -1  N  LYS C 182   O  GLU C 263           
SHEET    6   J 8 GLN C 188  GLY C 200 -1  O  TYR C 190   N  ILE C 183           
SHEET    7   J 8 PHE C 139  ILE C 142 -1  N  TRP C 140   O  VAL C 199           
SHEET    8   J 8 ASP C 271  THR C 272 -1  O  ASP C 271   N  GLY C 141           
SHEET    1   K 2 TYR C 204  LEU C 205  0                                        
SHEET    2   K 2 ILE C 208  PRO C 209 -1  O  ILE C 208   N  LEU C 205           
SHEET    1   L 8 GLN D 134  PHE D 136  0                                        
SHEET    2   L 8 VAL D 123  ALA D 131 -1  N  ALA D 131   O  GLN D 134           
SHEET    3   L 8 CYS D 282  ILE D 294 -1  O  GLU D 285   N  LYS D 130           
SHEET    4   L 8 SER D 259  THR D 264 -1  N  ILE D 260   O  ILE D 284           
SHEET    5   L 8 PHE D 179  TYR D 185 -1  N  THR D 184   O  HIS D 261           
SHEET    6   L 8 VAL D 189  GLY D 200 -1  O  ASP D 192   N  VAL D 181           
SHEET    7   L 8 LEU D 222  LYS D 228 -1  O  PHE D 225   N  MSE D 198           
SHEET    8   L 8 PHE D 253  ALA D 257 -1  O  ALA D 257   N  LEU D 222           
SHEET    1   M 8 GLN D 134  PHE D 136  0                                        
SHEET    2   M 8 VAL D 123  ALA D 131 -1  N  ALA D 131   O  GLN D 134           
SHEET    3   M 8 CYS D 282  ILE D 294 -1  O  GLU D 285   N  LYS D 130           
SHEET    4   M 8 SER D 259  THR D 264 -1  N  ILE D 260   O  ILE D 284           
SHEET    5   M 8 PHE D 179  TYR D 185 -1  N  THR D 184   O  HIS D 261           
SHEET    6   M 8 VAL D 189  GLY D 200 -1  O  ASP D 192   N  VAL D 181           
SHEET    7   M 8 PHE D 139  ILE D 142 -1  N  TRP D 140   O  VAL D 199           
SHEET    8   M 8 ASP D 271  THR D 272 -1  O  ASP D 271   N  GLY D 141           
SHEET    1   N 2 TYR D 204  LEU D 205  0                                        
SHEET    2   N 2 ILE D 208  PRO D 209 -1  O  ILE D 208   N  LEU D 205           
LINK         C   VAL A 197                 N   MSE A 198     1555   1555  1.32  
LINK         C   MSE A 198                 N   VAL A 199     1555   1555  1.33  
LINK         C   THR A 292                 N   MSE A 293     1555   1555  1.33  
LINK         C   MSE A 293                 N   ILE A 294     1555   1555  1.32  
LINK         C   VAL B 197                 N   MSE B 198     1555   1555  1.33  
LINK         C   MSE B 198                 N   VAL B 199     1555   1555  1.33  
LINK         C   THR B 292                 N   MSE B 293     1555   1555  1.33  
LINK         C   MSE B 293                 N   ILE B 294     1555   1555  1.33  
LINK         C   VAL C 197                 N   MSE C 198     1555   1555  1.33  
LINK         C   MSE C 198                 N   VAL C 199     1555   1555  1.33  
LINK         C   THR C 292                 N   MSE C 293     1555   1555  1.33  
LINK         C   MSE C 293                 N   ILE C 294     1555   1555  1.33  
LINK         C   VAL D 197                 N   MSE D 198     1555   1555  1.33  
LINK         C   MSE D 198                 N   VAL D 199     1555   1555  1.33  
LINK         C   THR D 292                 N   MSE D 293     1555   1555  1.33  
LINK         C   MSE D 293                 N   ILE D 294     1555   1555  1.32  
CISPEP   1 THR A  280    PRO A  281          0        -4.65                     
CISPEP   2 THR B  280    PRO B  281          0        -1.69                     
CISPEP   3 THR C  280    PRO C  281          0        -2.67                     
CISPEP   4 THR D  280    PRO D  281          0        -2.49                     
CRYST1   63.608  130.758   72.794  90.00 115.04  90.00 P 1 21 1      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.015721  0.000000  0.007344        0.00000                         
SCALE2      0.000000  0.007648  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015162        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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