HEADER    PROTEIN FIBRIL                          25-JUL-17   5WKD              
TITLE     CRYSTAL STRUCTURE OF THE SEGMENT, GNNQGSN, FROM THE LOW COMPLEXITY    
TITLE    2 DOMAIN OF TDP-43, RESIDUES 300-306                                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: TAR DNA-BINDING PROTEIN 43;                                
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 300-306;                                      
COMPND   5 SYNONYM: TDP-43;                                                     
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES;                                                      
SOURCE   3 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   4 ORGANISM_COMMON: HUMAN;                                              
SOURCE   5 ORGANISM_TAXID: 9606                                                 
KEYWDS    TDP-43, AMYLOID, LOW COMPLEXITY DOMAIN, PROTEIN FIBRIL                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    E.L.GUENTHER,H.TRINH,M.R.SAWAYA,D.CASCIO,D.S.EISENBERG                
REVDAT   6   18-DEC-19 5WKD    1       REMARK                                   
REVDAT   5   20-FEB-19 5WKD    1       REMARK                                   
REVDAT   4   20-JUN-18 5WKD    1       JRNL                                     
REVDAT   3   06-JUN-18 5WKD    1       JRNL                                     
REVDAT   2   30-MAY-18 5WKD    1       JRNL                                     
REVDAT   1   18-APR-18 5WKD    0                                                
JRNL        AUTH   E.L.GUENTHER,Q.CAO,H.TRINH,J.LU,M.R.SAWAYA,D.CASCIO,         
JRNL        AUTH 2 D.R.BOYER,J.A.RODRIGUEZ,M.P.HUGHES,D.S.EISENBERG             
JRNL        TITL   ATOMIC STRUCTURES OF TDP-43 LCD SEGMENTS AND INSIGHTS INTO   
JRNL        TITL 2 REVERSIBLE OR PATHOGENIC AGGREGATION.                        
JRNL        REF    NAT. STRUCT. MOL. BIOL.       V.  25   463 2018              
JRNL        REFN                   ESSN 1545-9985                               
JRNL        PMID   29786080                                                     
JRNL        DOI    10.1038/S41594-018-0064-2                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC                                               
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) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.65                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 90.4                           
REMARK   3   NUMBER OF REFLECTIONS             : 345                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.184                           
REMARK   3   R VALUE            (WORKING SET) : 0.184                           
REMARK   3   FREE R VALUE                     : 0.195                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 6.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 22                              
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 48                                      
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 2                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 8.83                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.16000                                             
REMARK   3    B22 (A**2) : -0.24000                                             
REMARK   3    B33 (A**2) : 0.32000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.14000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.205         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.141         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.114         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.915         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   DISTANCE RESTRAINTS.                    RMS    SIGMA               
REMARK   3    BOND LENGTH                     (A) : NULL  ; NULL                
REMARK   3    ANGLE DISTANCE                  (A) : NULL  ; 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) : NULL  ; NULL                
REMARK   3   CHIRAL-CENTER RESTRAINT       (A**3) : NULL  ; 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) : NULL  ; 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) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 5WKD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-AUG-17.                  
REMARK 100 THE DEPOSITION ID IS D_1000229073.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 13-AUG-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 24-ID-E                            
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9791                             
REMARK 200  MONOCHROMATOR                  : SI(220)                            
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 373                                
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 100.000                            
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.6                               
REMARK 200  DATA REDUNDANCY                : 2.300                              
REMARK 200  R MERGE                    (I) : 0.15800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 5.4000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.8                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.25000                            
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: IDEALIZED BETA STRAND                                
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 2.45                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.26                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 100MM BIS-TRIS PROPANE, PH 7.5, 200 MM   
REMARK 280  SODIUM SULFATE, 20% PEG3350, VAPOR DIFFUSION, HANGING DROP,         
REMARK 280  TEMPERATURE 298K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       25.17350            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        2.38850            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       25.17350            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000        2.38850            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
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: DECAMERIC                         
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 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        4.77700            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   3  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        9.55400            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000       -4.77700            
REMARK 350   BIOMT3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   5  0.000000  1.000000  0.000000       -9.55400            
REMARK 350   BIOMT3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   6 -1.000000  0.000000  0.000000       25.17350            
REMARK 350   BIOMT2   6  0.000000  1.000000  0.000000        2.38850            
REMARK 350   BIOMT3   6  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   7 -1.000000  0.000000  0.000000       25.17350            
REMARK 350   BIOMT2   7  0.000000  1.000000  0.000000        7.16550            
REMARK 350   BIOMT3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   8 -1.000000  0.000000  0.000000       25.17350            
REMARK 350   BIOMT2   8  0.000000  1.000000  0.000000       11.94250            
REMARK 350   BIOMT3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   9 -1.000000  0.000000  0.000000       25.17350            
REMARK 350   BIOMT2   9  0.000000  1.000000  0.000000       -2.38850            
REMARK 350   BIOMT3   9  0.000000  0.000000 -1.000000        0.00000            
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1  10 -1.000000  0.000000  0.000000       25.17350            
REMARK 350   BIOMT2  10  0.000000  1.000000  0.000000       -7.16550            
REMARK 350   BIOMT3  10  0.000000  0.000000 -1.000000        0.00000            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 401  LIES ON A SPECIAL POSITION.                          
DBREF  5WKD A  300   306  UNP    Q13148   TADBP_HUMAN    300    306             
SEQRES   1 A    7  GLY ASN ASN GLN GLY SER ASN                                  
FORMUL   2  HOH   *2(H2 O)                                                      
CRYST1   50.347    4.777   14.746  90.00 101.73  90.00 C 1 2 1       4          
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      0.019862  0.000000  0.004125        0.00000                         
SCALE2      0.000000  0.209336  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.069262        0.00000                         
ATOM      1  N   GLY A 300       0.958   0.885   3.506  1.00 13.41           N  
ATOM      2  CA  GLY A 300       2.189   0.130   3.261  1.00 11.45           C  
ATOM      3  C   GLY A 300       3.414   0.816   3.766  1.00 10.36           C  
ATOM      4  O   GLY A 300       3.427   2.050   3.946  1.00  9.06           O  
ATOM      5  N   ASN A 301       4.441  -0.005   3.969  1.00  8.48           N  
ATOM      6  CA  ASN A 301       5.752   0.443   4.412  1.00 10.23           C  
ATOM      7  C   ASN A 301       6.828  -0.143   3.505  1.00  8.85           C  
ATOM      8  O   ASN A 301       6.776  -1.337   3.163  1.00  7.98           O  
ATOM      9  CB  ASN A 301       6.006  -0.049   5.828  1.00 11.40           C  
ATOM     10  CG  ASN A 301       5.126   0.629   6.880  1.00 16.85           C  
ATOM     11  OD1 ASN A 301       4.735  -0.040   7.857  1.00 24.53           O  
ATOM     12  ND2 ASN A 301       4.822   1.937   6.717  1.00 15.59           N  
ATOM     13  N   ASN A 302       7.781   0.706   3.092  1.00  7.99           N  
ATOM     14  CA  ASN A 302       8.977   0.318   2.342  1.00  6.37           C  
ATOM     15  C   ASN A 302      10.144   0.930   3.095  1.00  5.74           C  
ATOM     16  O   ASN A 302      10.139   2.121   3.335  1.00  4.44           O  
ATOM     17  CB  ASN A 302       8.907   0.767   0.863  1.00  7.61           C  
ATOM     18  CG  ASN A 302       7.687   0.222   0.186  1.00  6.18           C  
ATOM     19  OD1 ASN A 302       7.544  -0.988   0.138  1.00  6.49           O  
ATOM     20  ND2 ASN A 302       6.752   1.071  -0.209  1.00  6.54           N  
ATOM     21  N   GLN A 303      11.123   0.091   3.421  1.00  5.85           N  
ATOM     22  CA  GLN A 303      12.339   0.491   4.084  1.00  6.53           C  
ATOM     23  C   GLN A 303      13.553  -0.176   3.442  1.00  7.08           C  
ATOM     24  O   GLN A 303      13.543  -1.391   3.298  1.00  7.14           O  
ATOM     25  CB  GLN A 303      12.238   0.037   5.494  1.00  7.41           C  
ATOM     26  CG  GLN A 303      13.445   0.409   6.333  1.00  9.08           C  
ATOM     27  CD  GLN A 303      13.208   0.022   7.714  1.00  9.34           C  
ATOM     28  OE1 GLN A 303      13.186  -1.168   8.041  1.00 11.92           O  
ATOM     29  NE2 GLN A 303      12.938   0.994   8.522  1.00  8.56           N  
ATOM     30  N   GLY A 304      14.611   0.578   3.107  1.00  6.92           N  
ATOM     31  CA  GLY A 304      15.837  -0.029   2.607  1.00  7.01           C  
ATOM     32  C   GLY A 304      17.086   0.682   3.069  1.00  8.20           C  
ATOM     33  O   GLY A 304      17.093   1.900   3.287  1.00  9.03           O  
ATOM     34  N   SER A 305      18.183  -0.053   3.159  1.00  8.14           N  
ATOM     35  CA  SER A 305      19.433   0.516   3.537  1.00  7.93           C  
ATOM     36  C   SER A 305      20.546  -0.109   2.760  1.00  7.64           C  
ATOM     37  O   SER A 305      20.581  -1.341   2.608  1.00  5.66           O  
ATOM     38  CB  SER A 305      19.664   0.285   5.045  1.00 10.87           C  
ATOM     39  OG  SER A 305      19.910  -1.065   5.271  1.00 12.12           O  
ATOM     40  N   ASN A 306      21.497   0.739   2.326  1.00  7.94           N  
ATOM     41  CA  ASN A 306      22.687   0.282   1.614  1.00  9.04           C  
ATOM     42  C   ASN A 306      23.906   0.883   2.357  1.00 15.55           C  
ATOM     43  O   ASN A 306      23.769   1.630   3.382  1.00 18.57           O  
ATOM     44  CB  ASN A 306      22.679   0.726   0.136  1.00  9.12           C  
ATOM     45  CG  ASN A 306      21.520   0.146  -0.601  1.00 10.74           C  
ATOM     46  OD1 ASN A 306      21.411  -1.102  -0.709  1.00 15.42           O  
ATOM     47  ND2 ASN A 306      20.643   1.001  -1.125  1.00 10.39           N  
ATOM     48  OXT ASN A 306      25.061   0.620   1.925  1.00 21.94           O  
TER      49      ASN A 306                                                      
HETATM   50  O   HOH A 401      25.165   2.934   0.008  0.50 23.31           O  
HETATM   51  O   HOH A 402      12.554  -2.226   0.065  1.00 13.65           O  
MASTER      234    0    0    0    0    0    0    6   50    1    0    1          
END                                                                             
