HEADER    EXTRACELLULAR MATRIX                    22-JAN-98   1A3I              
TITLE     X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A COLLAGEN-LIKE               
TITLE    2 PEPTIDE WITH THE REPEATING SEQUENCE (PRO-PRO-GLY)                    
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: COLLAGEN-LIKE PEPTIDE;                                     
COMPND   3 CHAIN: A, B, C;                                                      
COMPND   4 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES                                                       
KEYWDS    COLLAGEN, EXTRACELLULAR MATRIX                                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    R.Z.KRAMER,L.VITAGLIANO,J.BELLA,R.BERISIO,L.MAZZARELLA,               
AUTHOR   2 B.BRODSKY,A.ZAGARI,H.M.BERMAN                                        
REVDAT   2   23-JUN-99 1A3I    1       JRNL                                     
REVDAT   1   06-MAY-98 1A3I    0                                                
JRNL        AUTH   R.Z.KRAMER,L.VITAGLIANO,J.BELLA,R.BERISIO,                   
JRNL        AUTH 2 L.MAZZARELLA,B.BRODSKY,A.ZAGARI,H.M.BERMAN                   
JRNL        TITL   X-RAY CRYSTALLOGRAPHIC DETERMINATION OF A                    
JRNL        TITL 2 COLLAGEN-LIKE PEPTIDE WITH THE REPEATING SEQUENCE            
JRNL        TITL 3 (PRO-PRO-GLY)                                                
JRNL        REF    J.MOL.BIOL.                   V. 280   623 1998              
JRNL        REFN   ASTM JMOBAK  UK ISSN 0022-2836                 0070          
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION. 1.97 ANGSTROMS.                                          
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : X-PLOR 3.1                                           
REMARK   3   AUTHORS     : BRUNGER                                              
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.97                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 8.                             
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.                             
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 1000000.                       
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.1                            
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 76.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 861                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE            (WORKING SET) : 0.181                           
REMARK   3   FREE R VALUE                     : NULL                            
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : NULL                            
REMARK   3   FREE R VALUE TEST SET COUNT      : NULL                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : NULL                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 10                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.97                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.04                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 63.3                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 69.                          
REMARK   3   BIN R VALUE           (WORKING SET) : 0.22                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 126                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 45                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 15.9                           
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  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.01                            
REMARK   3   BOND ANGLES            (DEGREES) : 2.07                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : 2.11                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : GROUP                                     
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  NCS MODEL : NONE                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: DUE TO THE QUASI-INFINITE,                
REMARK   3  AVERAGED NATURE OF THE TRIPLE HELIX, DURING REFINEMENT              
REMARK   3  COVALENT BONDS ARE NECESSARY TO JOIN THE MOLECULE WITH              
REMARK   3  ITS SYMMETRY MATES BOTH ABOVE IT AND BELOW IT ALONG THE             
REMARK   3  HELICAL AXIS AND TIGHT REFINEMENT CONSTRAINTS WERE                  
REMARK   3  MAINTAINED.                                                         
REMARK   4                                                                      
REMARK   4 1A3I COMPLIES WITH FORMAT V. 2.2, 16-DEC-1996                        
REMARK   6                                                                      
REMARK   6 THE 21 RESIDUE ASYMMETRIC UNIT CORRESPONDS TO ONE                    
REMARK   6 TRIPLE-HELICAL REPEAT AND IS SMALLER THAN THE ENTIRE 90              
REMARK   6 RESIDUE PEPTIDE DUE TO TRANSLATIONAL DISORDER ALONG THE              
REMARK   6 HELICAL AXIS.  THE RESULT IS A POLYMER-LIKE STRUCTURE WITH           
REMARK   6 NO DEFINED ENDS.                                                     
REMARK   7                                                                      
REMARK   7 THE POLYMER STRUCTURE IS FORMED BY CONTINUATION OF THE               
REMARK   7 CHAINS USING THE SYMMETRY-RELATED MOLECULES ALONG THE                
REMARK   7 HELICAL AXIS.  THE TVECT RECORD BELOW PRESENTS THE                   
REMARK   7 TRANSLATION THAT WILL GENERATE THE POLYMER.  NOTE:                   
REMARK   7 THEREFORE, CLOSE CONTACTS BETWEEN SYMMETRY-RELATED                   
REMARK   7 MOLECULES ARE INTENTIONAL AND NECESSARY.  INTERCHAIN                 
REMARK   7 HYDROGEN BONDING AT THE END OF CHAINS ALSO UTILIZES                  
REMARK   7 SYMMETRY-RELATED MOLECULES.                                          
REMARK   8                                                                      
REMARK   8 THE ENTIRE 30 RESIDUE LONG PEPTIDE CAN BE GENERATED FROM             
REMARK   8 THE SUBMITTED ASYMMETRIC UNIT BY APPLYING THE FOLLOWING              
REMARK   8 TRANSLATIONS (USING FRACTIONAL COORDINATES):                         
REMARK   8 CHAIN A: TRANSLATE RESIDUES 1 - 9 BY (0 0 1), (0 0 2), AND           
REMARK   8          (0 0 3) AND RESIDUES 7 - 9 BY (0 0 4).                      
REMARK   8 CHAIN B: TRANSLATE RESIDUES 31 - 36 BY (0 0 1), (0 0 2),             
REMARK   8          AND (0 0 3).                                                
REMARK   8 CHAIN C: TRANSLATE RESIDUES 61 - 66 BY (0 0 1), (0 0 2),             
REMARK   8          AND (0 0 3) AND RESIDUES 64 - 66 BY (004).                  
REMARK   8 THIS WILL RESULT IN A MOLECULE WITH A TOTAL OF 90 RESIDUES,          
REMARK   8 30 IN EACH CHAIN.                                                    
REMARK   9                                                                      
REMARK   9 HYDROGEN BONDS BETWEEN PEPTIDE CHAINS FOLLOW THE RICH AND            
REMARK   9 CRICK MODEL II FOR COLLAGEN.                                         
REMARK  10                                                                      
REMARK  10 THE UNIT CELL AXES WERE CHOSEN TO COINCIDE WITH A                    
REMARK  10 PREVIOUS STRUCTURE DETERMINATION (OKUYAMA 1981) OF THIS              
REMARK  10 PEPTIDE.                                                             
REMARK  11                                                                      
REMARK  11 FOR EACH CHAIN, RESIDUE NUMBERING CORRESPONDS TO THE ENTIRE          
REMARK  11 MOLECULE RATHER THAN THE SHORTER ASYMMETRIC UNIT.                    
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : OCT-1991                           
REMARK 200  TEMPERATURE           (KELVIN) : 259.0                              
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.542                              
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CAD4 DIFFRACTOMETER                
REMARK 200  DETECTOR MANUFACTURER          : ENRAF-NONIUS                       
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOLEN                              
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 1136                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.97                               
REMARK 200  RESOLUTION RANGE LOW       (A) : INFINITY                           
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.                                 
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.5                               
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) : 1.97                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.2                      
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
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 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR                    
REMARK 200    REPLACEMENT                                                       
REMARK 200 SOFTWARE USED: LALS                                                  
REMARK 200 STARTING MODEL: IDEALIZED SEVEN-FOLD TRIPLE-HELIX                    
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): NULL                                      
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): NULL                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEPTIDE WAS CRYSTALLIZED FROM            
REMARK 280 4.0 MG/ML PEPTIDE IN 10% ACETIC ACID, 0.1% SODIUM AZIDE,             
REMARK 280 AND 3.0% PEG400.                                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   1/2-X,-Y,1/2+Z                                          
REMARK 290       3555   -X,1/2+Y,1/2-Z                                          
REMARK 290       4555   1/2+X,1/2-Y,-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       13.40986            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       10.09000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       13.14510            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       10.09000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       13.40986            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       13.14510            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 THIS ENTRY IS RELATED TO PDB ENTRY 1A3J.                             
DBREF  1A3I A    1     9  PDB    1A3I     1A3I             1      9             
DBREF  1A3I B   31    36  PDB    1A3I     1A3I            31     36             
DBREF  1A3I C   61    66  PDB    1A3I     1A3I            61     66             
SEQRES   1 A    9  PRO PRO GLY PRO PRO GLY PRO PRO GLY                          
SEQRES   1 B    6  PRO PRO GLY PRO PRO GLY                                      
SEQRES   1 C    6  PRO PRO GLY PRO PRO GLY                                      
HET    ACY    401       4                                                       
HET    ACY    402       4                                                       
HETNAM     ACY ACETIC ACID                                                      
FORMUL   4  ACY    2(C2 H4 O2)                                                  
FORMUL   5  HOH   *37(H2 O1)                                                    
LINK         N   PRO C  61                 C   GLY A   9            1556        
LINK         N   PRO A   1                 C   GLY B  36            1556        
LINK         N   PRO B  31                 C   GLY C  66            1556        
CRYST1   26.820   26.290   20.180  90.00  90.00  90.00 P 21 21 21    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      0.037286  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.038037  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.049554        0.00000                         
TVECT    1   0.00000   0.00000  20.18000                                        
ATOM      1  N   PRO A   1       8.316  21.206  21.530  1.00 17.44           N  
ATOM      2  CA  PRO A   1       7.608  20.729  20.336  1.00 17.44           C  
ATOM      3  C   PRO A   1       8.487  20.707  19.092  1.00 17.44           C  
ATOM      4  O   PRO A   1       9.466  21.457  19.005  1.00 17.44           O  
ATOM      5  CB  PRO A   1       6.460  21.723  20.211  1.00 22.26           C  
ATOM      6  CG  PRO A   1       7.110  23.002  20.661  1.00 22.26           C  
ATOM      7  CD  PRO A   1       7.873  22.569  21.889  1.00 22.26           C  
ATOM      8  N   PRO A   2       8.177  19.849  18.107  1.00 13.49           N  
ATOM      9  CA  PRO A   2       9.057  19.896  16.936  1.00 13.49           C  
ATOM     10  C   PRO A   2       9.087  21.308  16.377  1.00 13.49           C  
ATOM     11  O   PRO A   2       8.318  22.186  16.816  1.00 13.49           O  
ATOM     12  CB  PRO A   2       8.426  18.899  15.970  1.00 18.26           C  
ATOM     13  CG  PRO A   2       7.776  17.914  16.886  1.00 18.26           C  
ATOM     14  CD  PRO A   2       7.166  18.797  17.954  1.00 18.26           C  
ATOM     15  N   GLY A   3       9.981  21.517  15.426  1.00 12.07           N  
ATOM     16  CA  GLY A   3      10.060  22.799  14.777  1.00 12.07           C  
ATOM     17  C   GLY A   3       9.119  22.720  13.589  1.00 12.07           C  
ATOM     18  O   GLY A   3       8.531  21.655  13.334  1.00 12.07           O  
ATOM     19  N   PRO A   4       8.954  23.832  12.847  1.00 14.22           N  
ATOM     20  CA  PRO A   4       8.095  23.907  11.675  1.00 14.22           C  
ATOM     21  C   PRO A   4       8.733  23.310  10.437  1.00 14.22           C  
ATOM     22  O   PRO A   4       9.963  23.078  10.402  1.00 14.22           O  
ATOM     23  CB  PRO A   4       7.863  25.403  11.527  1.00  8.61           C  
ATOM     24  CG  PRO A   4       9.218  25.934  11.895  1.00  8.61           C  
ATOM     25  CD  PRO A   4       9.530  25.158  13.143  1.00  8.61           C  
ATOM     26  N   PRO A   5       7.918  23.027   9.412  1.00 14.03           N  
ATOM     27  CA  PRO A   5       8.416  22.493   8.135  1.00 14.03           C  
ATOM     28  C   PRO A   5       9.621  23.306   7.672  1.00 14.03           C  
ATOM     29  O   PRO A   5       9.876  24.379   8.181  1.00 14.03           O  
ATOM     30  CB  PRO A   5       7.229  22.641   7.193  1.00 10.90           C  
ATOM     31  CG  PRO A   5       6.082  22.382   8.123  1.00 10.90           C  
ATOM     32  CD  PRO A   5       6.452  23.069   9.415  1.00 10.90           C  
ATOM     33  N   GLY A   6      10.369  22.765   6.725  1.00 10.80           N  
ATOM     34  CA  GLY A   6      11.517  23.464   6.204  1.00 10.80           C  
ATOM     35  C   GLY A   6      11.139  24.138   4.928  1.00 10.80           C  
ATOM     36  O   GLY A   6      10.028  23.948   4.418  1.00 10.80           O  
ATOM     37  N   PRO A   7      12.050  24.922   4.355  1.00 11.55           N  
ATOM     38  CA  PRO A   7      11.797  25.641   3.111  1.00 11.55           C  
ATOM     39  C   PRO A   7      11.484  24.709   1.970  1.00 11.55           C  
ATOM     40  O   PRO A   7      11.783  23.500   2.038  1.00 11.55           O  
ATOM     41  CB  PRO A   7      13.091  26.440   2.901  1.00 10.61           C  
ATOM     42  CG  PRO A   7      14.119  25.540   3.516  1.00 10.61           C  
ATOM     43  CD  PRO A   7      13.456  25.102   4.796  1.00 10.61           C  
ATOM     44  N   PRO A   8      10.853  25.225   0.900  1.00 14.31           N  
ATOM     45  CA  PRO A   8      10.571  24.322  -0.220  1.00 14.31           C  
ATOM     46  C   PRO A   8      11.897  23.973  -0.901  1.00 14.31           C  
ATOM     47  O   PRO A   8      12.973  24.425  -0.473  1.00 14.31           O  
ATOM     48  CB  PRO A   8       9.623  25.131  -1.124  1.00 16.14           C  
ATOM     49  CG  PRO A   8       9.080  26.188  -0.206  1.00 16.14           C  
ATOM     50  CD  PRO A   8      10.279  26.556   0.633  1.00 16.14           C  
ATOM     51  N   GLY A   9      11.816  23.125  -1.918  1.00 11.65           N  
ATOM     52  CA  GLY A   9      12.996  22.720  -2.639  1.00 11.65           C  
ATOM     53  C   GLY A   9      13.234  23.577  -3.852  1.00 11.65           C  
ATOM     54  O   GLY A   9      12.433  24.459  -4.180  1.00 11.65           O  
TER      55      GLY A   9                                                      
ATOM     56  N   PRO B  31      12.731  18.403  18.599  1.00  8.71           N  
ATOM     57  CA  PRO B  31      13.374  17.891  17.389  1.00  8.71           C  
ATOM     58  C   PRO B  31      13.142  18.745  16.166  1.00  8.71           C  
ATOM     59  O   PRO B  31      12.207  19.526  16.121  1.00  8.71           O  
ATOM     60  CB  PRO B  31      12.784  16.471  17.255  1.00 15.38           C  
ATOM     61  CG  PRO B  31      11.434  16.598  17.873  1.00 15.38           C  
ATOM     62  CD  PRO B  31      11.660  17.490  19.065  1.00 15.38           C  
ATOM     63  N   PRO B  32      14.011  18.647  15.178  1.00 13.67           N  
ATOM     64  CA  PRO B  32      13.833  19.426  13.967  1.00 13.67           C  
ATOM     65  C   PRO B  32      12.523  19.099  13.336  1.00 13.67           C  
ATOM     66  O   PRO B  32      12.038  17.968  13.473  1.00 13.67           O  
ATOM     67  CB  PRO B  32      15.025  19.023  13.125  1.00  9.03           C  
ATOM     68  CG  PRO B  32      16.077  18.799  14.163  1.00  9.03           C  
ATOM     69  CD  PRO B  32      15.320  17.975  15.152  1.00  9.03           C  
ATOM     70  N   GLY B  33      11.928  20.070  12.640  1.00 14.26           N  
ATOM     71  CA  GLY B  33      10.661  19.801  12.008  1.00 14.26           C  
ATOM     72  C   GLY B  33      10.802  18.911  10.797  1.00 14.26           C  
ATOM     73  O   GLY B  33      11.882  18.368  10.516  1.00 14.26           O  
ATOM     74  N   PRO B  34       9.708  18.736  10.046  1.00 11.50           N  
ATOM     75  CA  PRO B  34       9.665  17.922   8.836  1.00 11.50           C  
ATOM     76  C   PRO B  34      10.227  18.620   7.654  1.00 11.50           C  
ATOM     77  O   PRO B  34      10.284  19.836   7.639  1.00 11.50           O  
ATOM     78  CB  PRO B  34       8.192  17.649   8.657  1.00  9.66           C  
ATOM     79  CG  PRO B  34       7.586  18.930   9.132  1.00  9.66           C  
ATOM     80  CD  PRO B  34       8.350  19.245  10.373  1.00  9.66           C  
ATOM     81  N   PRO B  35      10.677  17.860   6.651  1.00 16.25           N  
ATOM     82  CA  PRO B  35      11.228  18.392   5.413  1.00 16.25           C  
ATOM     83  C   PRO B  35      10.219  19.317   4.794  1.00 16.25           C  
ATOM     84  O   PRO B  35       9.010  19.249   5.127  1.00 16.25           O  
ATOM     85  CB  PRO B  35      11.468  17.160   4.542  1.00 10.89           C  
ATOM     86  CG  PRO B  35      11.668  16.066   5.531  1.00 10.89           C  
ATOM     87  CD  PRO B  35      10.798  16.385   6.703  1.00 10.89           C  
ATOM     88  N   GLY B  36      10.709  20.223   3.948  1.00 19.34           N  
ATOM     89  CA  GLY B  36       9.836  21.154   3.260  1.00 19.34           C  
ATOM     90  C   GLY B  36       9.207  20.491   2.050  1.00 19.34           C  
ATOM     91  O   GLY B  36       9.565  19.355   1.710  1.00 19.34           O  
TER      92      GLY B  36                                                      
ATOM     93  N   PRO C  61      14.309  23.332  15.622  1.00 10.63           N  
ATOM     94  CA  PRO C  61      14.643  24.095  14.422  1.00 10.63           C  
ATOM     95  C   PRO C  61      13.859  23.751  13.161  1.00 10.63           C  
ATOM     96  O   PRO C  61      13.189  22.726  13.091  1.00 10.63           O  
ATOM     97  CB  PRO C  61      16.144  23.846  14.270  1.00 19.41           C  
ATOM     98  CG  PRO C  61      16.308  22.475  14.820  1.00 19.41           C  
ATOM     99  CD  PRO C  61      15.451  22.510  16.056  1.00 19.41           C  
ATOM    100  N   PRO C  62      13.910  24.631  12.163  1.00 15.75           N  
ATOM    101  CA  PRO C  62      13.234  24.402  10.876  1.00 15.75           C  
ATOM    102  C   PRO C  62      13.686  23.039  10.262  1.00 15.75           C  
ATOM    103  O   PRO C  62      14.874  22.653  10.369  1.00 15.75           O  
ATOM    104  CB  PRO C  62      13.668  25.600  10.024  1.00  9.87           C  
ATOM    105  CG  PRO C  62      13.859  26.675  11.052  1.00  9.87           C  
ATOM    106  CD  PRO C  62      14.515  25.976  12.213  1.00  9.87           C  
ATOM    107  N   GLY C  63      12.761  22.316   9.639  1.00 16.50           N  
ATOM    108  CA  GLY C  63      13.167  21.066   9.028  1.00 16.50           C  
ATOM    109  C   GLY C  63      14.105  21.312   7.849  1.00 16.50           C  
ATOM    110  O   GLY C  63      14.435  22.472   7.518  1.00 16.50           O  
ATOM    111  N   PRO C  64      14.571  20.246   7.184  1.00 15.53           N  
ATOM    112  CA  PRO C  64      15.458  20.417   6.037  1.00 15.53           C  
ATOM    113  C   PRO C  64      14.684  20.927   4.823  1.00 15.53           C  
ATOM    114  O   PRO C  64      13.463  20.829   4.772  1.00 15.53           O  
ATOM    115  CB  PRO C  64      16.001  19.018   5.816  1.00  5.63           C  
ATOM    116  CG  PRO C  64      14.806  18.201   6.163  1.00  5.63           C  
ATOM    117  CD  PRO C  64      14.354  18.810   7.450  1.00  5.63           C  
ATOM    118  N   PRO C  65      15.378  21.485   3.840  1.00 10.50           N  
ATOM    119  CA  PRO C  65      14.622  21.927   2.689  1.00 10.50           C  
ATOM    120  C   PRO C  65      14.079  20.706   1.955  1.00 10.50           C  
ATOM    121  O   PRO C  65      14.505  19.531   2.221  1.00 10.50           O  
ATOM    122  CB  PRO C  65      15.615  22.734   1.892  1.00 11.55           C  
ATOM    123  CG  PRO C  65      16.951  22.189   2.279  1.00 11.55           C  
ATOM    124  CD  PRO C  65      16.808  21.850   3.742  1.00 11.55           C  
ATOM    125  N   GLY C  66      13.102  20.952   1.076  1.00  9.96           N  
ATOM    126  CA  GLY C  66      12.479  19.874   0.334  1.00  9.96           C  
ATOM    127  C   GLY C  66      13.226  19.430  -0.900  1.00  9.96           C  
ATOM    128  O   GLY C  66      14.206  20.054  -1.286  1.00  9.96           O  
TER     129      GLY C  66                                                      
HETATM  130  C   ACY   401       3.682  22.541  11.236  1.00 21.19           C  
HETATM  131  O   ACY   401       2.807  23.097  10.553  1.00 21.19           O  
HETATM  132  OXT ACY   401       4.306  23.101  12.291  1.00 21.19           O  
HETATM  133  CH3 ACY   401       4.134  21.141  10.915  1.00 21.19           C  
HETATM  134  C   ACY   402      19.091  22.160   7.837  1.00 38.32           C  
HETATM  135  O   ACY   402      19.334  21.755   6.694  1.00 38.32           O  
HETATM  136  OXT ACY   402      18.633  21.338   8.768  1.00 38.32           O  
HETATM  137  CH3 ACY   402      19.293  23.618   8.266  1.00 38.32           C  
HETATM  138  O   HOH   101       5.594  21.889  15.805  1.00 28.97           O  
HETATM  139  O   HOH   102       7.355  25.253  16.293  1.00 22.47           O  
HETATM  140  O   HOH   103       6.457  20.993  12.327  1.00 29.02           O  
HETATM  141  O   HOH   104       7.423  26.270   8.119  1.00 30.44           O  
HETATM  142  O   HOH   105      11.373  26.588   6.950  1.00 23.32           O  
HETATM  143  O   HOH   106       7.408  25.371   4.091  1.00  5.05           O  
HETATM  144  O   HOH   107      13.153  27.296  -0.172  1.00 21.02           O  
HETATM  145  O   HOH   108      15.664  24.810  -1.390  1.00 11.17           O  
HETATM  146  O   HOH   109      12.152  26.921  -4.540  1.00  9.23           O  
HETATM  147  O   HOH   111      13.443  15.615  12.881  1.00 13.59           O  
HETATM  148  O   HOH   112       9.758  16.818  12.994  1.00 27.99           O  
HETATM  149  O   HOH   113      12.963  16.325   9.228  1.00 23.25           O  
HETATM  150  O   HOH   115       5.878  20.610   4.485  1.00 24.12           O  
HETATM  151  O   HOH   116       8.848  16.145   2.532  1.00 47.48           O  
HETATM  152  O   HOH   121      18.638  24.296  11.397  1.00 27.03           O  
HETATM  153  O   HOH   122      16.444  20.463  10.447  1.00 25.94           O  
HETATM  154  O   HOH   123      16.295  24.230   6.930  1.00 19.70           O  
HETATM  155  O   HOH   124      17.331  17.619   2.413  1.00 31.73           O  
HETATM  156  O   HOH   125      13.985  16.977   0.817  1.00 53.43           O  
HETATM  157  O   HOH   126      16.914  19.363  -0.910  1.00  9.43           O  
HETATM  158  O   HOH   201       5.473  23.666   4.098  1.00 14.40           O  
HETATM  159  O   HOH   202      21.595  24.992   9.644  1.00 17.29           O  
HETATM  160  O   HOH   204       4.187  25.027   5.974  1.00  7.43           O  
HETATM  161  O   HOH   205      13.466  14.688   2.583  1.00  7.90           O  
HETATM  162  O   HOH   208      16.622  16.376  -0.560  1.00 22.05           O  
HETATM  163  O   HOH   209      17.417  23.063  -0.970  1.00 23.97           O  
HETATM  164  O   HOH   210      17.034  27.356   9.718  1.00 20.07           O  
HETATM  165  O   HOH   218       3.280  23.836   8.294  1.00 17.32           O  
HETATM  166  O   HOH   220      16.159  26.500  -3.605  1.00 26.00           O  
HETATM  167  O   HOH   241      17.060  26.756   1.465  1.00 16.81           O  
HETATM  168  O   HOH   242       6.144  15.504   5.728  1.00 23.11           O  
HETATM  169  O   HOH   243      18.532  26.812  12.585  1.00 13.40           O  
HETATM  170  O   HOH   244       9.783  28.384   5.130  1.00 21.62           O  
HETATM  171  O   HOH   245      10.552  28.648  13.053  1.00 23.05           O  
HETATM  172  O   HOH   246       9.269  14.976  15.672  1.00 28.60           O  
HETATM  173  O   HOH   247       6.015  15.569  15.283  1.00 26.87           O  
HETATM  174  O   HOH   248      20.598  27.021   8.450  1.00 22.69           O  
CONECT  130  131  132  133                                                      
CONECT  131  130                                                                
CONECT  132  130                                                                
CONECT  133  130                                                                
CONECT  134  135  136  137                                                      
CONECT  135  134                                                                
CONECT  136  134                                                                
CONECT  137  134                                                                
MASTER      226    0    2    0    0    0    0    6  171    3    8    3          
END                                                                             
