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Database: PDB
Entry: 3WZF
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Original site: 3WZF 
HEADER    TRANSFERASE                             24-SEP-14   3WZF              
TITLE     CRYSTAL STRUCTURE OF HUMAN CYTOPLASMIC ASPARTATE AMINOTRANSFERASE     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ASPARTATE AMINOTRANSFERASE, CYTOPLASMIC;                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: CASPAT, CYSTEINE AMINOTRANSFERASE, CYTOPLASMIC, CYSTEINE    
COMPND   5 TRANSAMINASE, CYTOPLASMIC, CCAT, GLUTAMATE OXALOACETATE TRANSAMINASE 
COMPND   6 1, TRANSAMINASE A;                                                   
COMPND   7 EC: 2.6.1.1, 2.6.1.3;                                                
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: GOT1;                                                          
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET22B-GOT1                               
KEYWDS    GLUTAMIC-OXALOACETIC TRANSAMINASE 1, GROWTH-INHIBITING PROTEIN 18,    
KEYWDS   2 CYSTEINE TRANSAMINASE, CYTOPLASMIC, TRANSFERASE                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.JIANG,H.CHANG,Y.ZHOU,L.CHEN,Q.YANG                                  
REVDAT   1   07-OCT-15 3WZF    0                                                
JRNL        AUTH   X.JIANG,H.CHANG,Y.ZHOU,L.CHEN,Q.YANG                         
JRNL        TITL   RECOMBINANT EXPRESSION, PURIFICATION AND PRELIMINARY         
JRNL        TITL 2 CRYSTALLOGRAPHIC STUDIES OF HUMAN CYTOPLASMIC ASPARTATE      
JRNL        TITL 3 AMINOTRANSFERASE                                             
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.99 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.8.4_1496)                   
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.99                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 33.43                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 97.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 9837                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.257                           
REMARK   3   R VALUE            (WORKING SET) : 0.254                           
REMARK   3   FREE R VALUE                     : 0.298                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 689                             
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 33.4306 -  5.1098    0.98     1950   147  0.2149 0.2621        
REMARK   3     2  5.1098 -  4.0581    0.99     1844   139  0.2273 0.2654        
REMARK   3     3  4.0581 -  3.5458    0.98     1823   137  0.2567 0.3080        
REMARK   3     4  3.5458 -  3.2219    0.98     1777   134  0.3122 0.3024        
REMARK   3     5  3.2219 -  2.9911    0.96     1754   132  0.3689 0.4962        
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              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.480            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 31.610           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 82.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
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      :  0.008           3346                                  
REMARK   3   ANGLE     :  1.189           4550                                  
REMARK   3   CHIRALITY :  0.050            493                                  
REMARK   3   PLANARITY :  0.006            596                                  
REMARK   3   DIHEDRAL  : 15.683           1218                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: CHAIN A                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  20.6108 113.4765  18.1214              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.8552 T22:   0.2433                                     
REMARK   3      T33:   0.4639 T12:  -0.2472                                     
REMARK   3      T13:   0.0320 T23:   0.0215                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2353 L22:   1.3088                                     
REMARK   3      L33:   7.1270 L12:  -0.6200                                     
REMARK   3      L13:  -2.0752 L23:   1.1596                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.4006 S12:  -0.1731 S13:  -0.1558                       
REMARK   3      S21:   0.6335 S22:   0.0349 S23:   0.0428                       
REMARK   3      S31:   1.9975 S32:  -0.4193 S33:   0.2115                       
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 3WZF COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 02-OCT-14.                  
REMARK 100 THE RCSB ID CODE IS RCSB096985.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-JUN-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SSRF                               
REMARK 200  BEAMLINE                       : BL17U                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9                                
REMARK 200  MONOCHROMATOR                  : DOUBLE CRYSTAL                     
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315R                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 10049                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.991                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.4                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.90                              
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 1AJR                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 51.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.54                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M BIS-TRIS 21%(W/V) PEG 3350, PH      
REMARK 280  6.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K                
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       53.70100            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       46.69400            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       46.69400            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       80.55150            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       46.69400            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       46.69400            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       26.85050            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       46.69400            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       46.69400            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       80.55150            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       46.69400            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       46.69400            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       26.85050            
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       53.70100            
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                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6370 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 32180 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -25.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000      -93.38800            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000       93.38800            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
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    PRO A   3      168.21    -45.14                                   
REMARK 500    LEU A  16      -74.57    -47.01                                   
REMARK 500    ALA A 120       21.65    -78.53                                   
REMARK 500    ARG A 121      -18.19   -155.37                                   
REMARK 500    GLU A 141       -7.63    -53.32                                   
REMARK 500    ASN A 142       43.50   -146.49                                   
REMARK 500    ALA A 149        1.98    -69.92                                   
REMARK 500    PHE A 152      131.06    -31.76                                   
REMARK 500    TYR A 160      -43.91   -133.59                                   
REMARK 500    LYS A 165       -8.11     86.05                                   
REMARK 500    ASP A 169       75.82   -103.98                                   
REMARK 500    LEU A 170      -73.26    -56.84                                   
REMARK 500    ALA A 180      152.07    -46.71                                   
REMARK 500    ALA A 192       77.31     45.58                                   
REMARK 500    ALA A 209      -76.62    -62.58                                   
REMARK 500    HIS A 214      -27.10    -22.71                                   
REMARK 500    ARG A 215       73.66   -161.62                                   
REMARK 500    ASN A 232      145.89   -175.71                                   
REMARK 500    LEU A 262       54.04    -93.24                                   
REMARK 500    PRO A 277       -5.70    -37.37                                   
REMARK 500    GLU A 278      -83.62    -47.26                                   
REMARK 500    THR A 294      -64.37    -97.66                                   
REMARK 500    ALA A 327      -71.03    -60.46                                   
REMARK 500    PRO A 367      -25.11    -36.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1AJR   RELATED DB: PDB                                   
DBREF  3WZF A    1   412  UNP    P17174   AATC_HUMAN       2    413             
SEQRES   1 A  412  ALA PRO PRO SER VAL PHE ALA GLU VAL PRO GLN ALA GLN          
SEQRES   2 A  412  PRO VAL LEU VAL PHE LYS LEU THR ALA ASP PHE ARG GLU          
SEQRES   3 A  412  ASP PRO ASP PRO ARG LYS VAL ASN LEU GLY VAL GLY ALA          
SEQRES   4 A  412  TYR ARG THR ASP ASP CYS HIS PRO TRP VAL LEU PRO VAL          
SEQRES   5 A  412  VAL LYS LYS VAL GLU GLN LYS ILE ALA ASN ASP ASN SER          
SEQRES   6 A  412  LEU ASN HIS GLU TYR LEU PRO ILE LEU GLY LEU ALA GLU          
SEQRES   7 A  412  PHE ARG SER CYS ALA SER ARG LEU ALA LEU GLY ASP ASP          
SEQRES   8 A  412  SER PRO ALA LEU LYS GLU LYS ARG VAL GLY GLY VAL GLN          
SEQRES   9 A  412  SER LEU GLY GLY THR GLY ALA LEU ARG ILE GLY ALA ASP          
SEQRES  10 A  412  PHE LEU ALA ARG TRP TYR ASN GLY THR ASN ASN LYS ASN          
SEQRES  11 A  412  THR PRO VAL TYR VAL SER SER PRO THR TRP GLU ASN HIS          
SEQRES  12 A  412  ASN ALA VAL PHE SER ALA ALA GLY PHE LYS ASP ILE ARG          
SEQRES  13 A  412  SER TYR ARG TYR TRP ASP ALA GLU LYS ARG GLY LEU ASP          
SEQRES  14 A  412  LEU GLN GLY PHE LEU ASN ASP LEU GLU ASN ALA PRO GLU          
SEQRES  15 A  412  PHE SER ILE VAL VAL LEU HIS ALA CYS ALA HIS ASN PRO          
SEQRES  16 A  412  THR GLY ILE ASP PRO THR PRO GLU GLN TRP LYS GLN ILE          
SEQRES  17 A  412  ALA SER VAL MET LYS HIS ARG PHE LEU PHE PRO PHE PHE          
SEQRES  18 A  412  ASP SER ALA TYR GLN GLY PHE ALA SER GLY ASN LEU GLU          
SEQRES  19 A  412  ARG ASP ALA TRP ALA ILE ARG TYR PHE VAL SER GLU GLY          
SEQRES  20 A  412  PHE GLU PHE PHE CYS ALA GLN SER PHE SER LYS ASN PHE          
SEQRES  21 A  412  GLY LEU TYR ASN GLU ARG VAL GLY ASN LEU THR VAL VAL          
SEQRES  22 A  412  GLY LYS GLU PRO GLU SER ILE LEU GLN VAL LEU SER GLN          
SEQRES  23 A  412  MET GLU LYS ILE VAL ARG ILE THR TRP SER ASN PRO PRO          
SEQRES  24 A  412  ALA GLN GLY ALA ARG ILE VAL ALA SER THR LEU SER ASN          
SEQRES  25 A  412  PRO GLU LEU PHE GLU GLU TRP THR GLY ASN VAL LYS THR          
SEQRES  26 A  412  MET ALA ASP ARG ILE LEU THR MET ARG SER GLU LEU ARG          
SEQRES  27 A  412  ALA ARG LEU GLU ALA LEU LYS THR PRO GLY THR TRP ASN          
SEQRES  28 A  412  HIS ILE THR ASP GLN ILE GLY MET PHE SER PHE THR GLY          
SEQRES  29 A  412  LEU ASN PRO LYS GLN VAL GLU TYR LEU VAL ASN GLU LYS          
SEQRES  30 A  412  HIS ILE TYR LEU LEU PRO SER GLY ARG ILE ASN VAL SER          
SEQRES  31 A  412  GLY LEU THR THR LYS ASN LEU ASP TYR VAL ALA THR SER          
SEQRES  32 A  412  ILE HIS GLU ALA VAL THR LYS ILE GLN                          
FORMUL   2  HOH   *2(H2 O)                                                      
HELIX    1   1 VAL A   15  ASP A   27  1                                  13    
HELIX    2   2 LEU A   50  ASP A   63  1                                  14    
HELIX    3   3 LEU A   76  GLY A   89  1                                  14    
HELIX    4   4 SER A   92  GLU A   97  1                                   6    
HELIX    5   5 GLY A  107  TYR A  123  1                                  17    
HELIX    6   6 ASN A  142  ALA A  149  1                                   8    
HELIX    7   7 ASP A  169  ASN A  175  1                                   7    
HELIX    8   8 ASN A  175  ALA A  180  1                                   6    
HELIX    9   9 THR A  201  HIS A  214  1                                  14    
HELIX   10  10 ALA A  237  GLY A  247  1                                  11    
HELIX   11  11 LEU A  262  GLU A  265  5                                   4    
HELIX   12  12 SER A  279  ILE A  293  1                                  15    
HELIX   13  13 ALA A  300  ASN A  312  1                                  13    
HELIX   14  14 ASN A  312  LEU A  344  1                                  33    
HELIX   15  15 ASN A  351  GLN A  356  1                                   6    
HELIX   16  16 ASN A  366  GLU A  376  1                                  11    
HELIX   17  17 SER A  390  LEU A  392  5                                   3    
HELIX   18  18 ASN A  396  ILE A  411  1                                  16    
SHEET    1   A 2 VAL A  33  ASN A  34  0                                        
SHEET    2   A 2 ILE A 379  TYR A 380  1  O  TYR A 380   N  VAL A  33           
SHEET    1   B 7 VAL A 100  LEU A 106  0                                        
SHEET    2   B 7 VAL A 267  VAL A 273 -1  O  GLY A 268   N  SER A 105           
SHEET    3   B 7 PHE A 251  SER A 255 -1  N  CYS A 252   O  THR A 271           
SHEET    4   B 7 PHE A 218  SER A 223  1  N  SER A 223   O  SER A 255           
SHEET    5   B 7 ILE A 185  VAL A 186  1  N  VAL A 186   O  PHE A 218           
SHEET    6   B 7 VAL A 133  SER A 137  1  N  TYR A 134   O  ILE A 185           
SHEET    7   B 7 ARG A 156  ARG A 159  1  O  ARG A 156   N  VAL A 133           
SHEET    1   C 2 TRP A 161  ASP A 162  0                                        
SHEET    2   C 2 GLY A 167  LEU A 168 -1  O  GLY A 167   N  ASP A 162           
SHEET    1   D 2 PHE A 360  PHE A 362  0                                        
SHEET    2   D 2 ARG A 386  ASN A 388 -1  O  ILE A 387   N  SER A 361           
CISPEP   1 SER A  137    PRO A  138          0        -1.13                     
CISPEP   2 ASN A  194    PRO A  195          0         3.27                     
CRYST1   93.388   93.388  107.402  90.00  90.00  90.00 P 43 21 2     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      0.010708  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010708  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009311        0.00000                         
(ATOM LINES ARE NOT SHOWN.)
END                                                                             
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