HEADER    PROTEIN FIBRIL                          22-JUN-09   3HYD              
TITLE     LVEALYL PEPTIDE DERIVED FROM HUMAN INSULIN CHAIN B, RESIDUES          
TITLE    2 11-17                                                                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: INSULIN;                                                   
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 34-41 OF CHAIN B;                             
COMPND   5 SYNONYM: INSULIN B CHAIN;                                            
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 SYNTHETIC: YES                                                       
KEYWDS    AMYLOID-LIKE PROTOFIBRIL, CARBOHYDRATE METABOLISM, CLEAVAGE           
KEYWDS   2 ON PAIR OF BASIC RESIDUES, DIABETES MELLITUS, DISEASE                
KEYWDS   3 MUTATION, DISULFIDE BOND, GLUCOSE METABOLISM, HORMONE,               
KEYWDS   4 PHARMACEUTICAL, SECRETED, PROTEIN FIBRIL                             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.I.IVANOVA,M.R.SAWAYA,D.EISENBERG                                    
REVDAT   2   24-NOV-09 3HYD    1       JRNL                                     
REVDAT   1   06-OCT-09 3HYD    0                                                
JRNL        AUTH   M.I.IVANOVA,S.A.SIEVERS,M.R.SAWAYA,J.S.WALL,                 
JRNL        AUTH 2 D.EISENBERG                                                  
JRNL        TITL   MOLECULAR BASIS FOR INSULIN FIBRIL ASSEMBLY.                 
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 106 18990 2009              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   19864624                                                     
JRNL        DOI    10.1073/PNAS.0910080106                                      
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.5.0072                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.14                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 95.1                           
REMARK   3   NUMBER OF REFLECTIONS             : 2644                           
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) : 0.149                           
REMARK   3   R VALUE            (WORKING SET) : 0.146                           
REMARK   3   FREE R VALUE                     : 0.180                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.400                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 248                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 5                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.12                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 583                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 88.45                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2320                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 133                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 0                                       
REMARK   3   SOLVENT ATOMS            : 3                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 6.60                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 6.56                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : -0.55000                                             
REMARK   3    B33 (A**2) : 0.45000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.28000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.030         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.032         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.019         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 0.849         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.966                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.961                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):    65 ; 0.015 ; 0.023       
REMARK   3   BOND LENGTHS OTHERS               (A):    69 ; 0.005 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):    90 ; 1.790 ; 2.122       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):   158 ; 0.851 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):     8 ; 7.471 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):     3 ;23.570 ;26.667       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):    12 ;10.059 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):    12 ; 0.147 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):    69 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):    11 ; 0.000 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):    38 ; 2.258 ; 2.000       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):    17 ; 0.821 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):    61 ; 3.043 ; 3.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):    27 ; 3.713 ; 2.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):    28 ; 5.334 ; 3.000       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):   134 ; 2.469 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):     3 ;15.407 ; 3.000       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):   133 ; 3.708 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE          
REMARK   3  RIDING POSITIONS U VALUES : REFINED INDIVIDUALLY                    
REMARK   4                                                                      
REMARK   4 3HYD COMPLIES WITH FORMAT V. 3.20, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 15-JUL-09.                  
REMARK 100 THE RCSB ID CODE IS RCSB053733.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-NOV-06; 19-NOV-06               
REMARK 200  TEMPERATURE           (KELVIN) : 100; 100                           
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 2                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : SLS; SLS                           
REMARK 200  BEAMLINE                       : X10SA; X10SA                       
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; M                               
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97645; 0.97645                   
REMARK 200  MONOCHROMATOR                  : NULL; NULL                         
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; CCD                           
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD;              
REMARK 200                                   MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL                                
REMARK 200  DATA SCALING SOFTWARE          : HKL                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 2647                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 90.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.1                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.18400                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR THE DATA SET  : 7.1520                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.08                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 84.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36100                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200  <I/SIGMA(I)> FOR SHELL         : 3.260                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; SINGLE WAVELENGTH           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: AN IDEALIZED BETA STRAND                             
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: 20% MPD, 0.1M SODIUM CITRATE PH          
REMARK 280  5.5, VAPOR DIFFUSION, HANGING DROP, 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       24.73900            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        2.41900            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       24.73900            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000        2.41900            
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 300 REMARK: THE BIOLOGICAL UNIT IS A                                     
REMARK 300 INDEFINITELY LONG PAIR OF SHEETS (A PROTOFIBRIL). ONE SHEET          
REMARK 300 FORMED BY CHAIN A AND CRYSTALLOGRAPHIC TRANSLATIONS                  
REMARK 300 ALONG THE B CELL DIMENSION (E.G. X,Y,Z AND X,Y+1,Z). THE             
REMARK 300 SECOND SHEET IS CONSTRUCTED FROM  1/2-X,1/2+Y,1-Z AND                
REMARK 300 CRYSTALLOGRAPHIC TRANSLATIONS ALONG THE B CELL DIMENSION             
REMARK 300 (E.G. 1/2-X,3/2+Y,1-Z).                                              
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: TETRAMERIC                        
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  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        4.83800            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -1.000000  0.000000  0.000000       22.48754            
REMARK 350   BIOMT2   3  0.000000  1.000000  0.000000        2.41900            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       19.31120            
REMARK 350   BIOMT1   4 -1.000000  0.000000  0.000000       22.48754            
REMARK 350   BIOMT2   4  0.000000  1.000000  0.000000        7.25700            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       19.31120            
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OMQ   RELATED DB: PDB                                   
REMARK 900 RESIDUES 12-17 FROM THE INSULIN B-CHAIN.                             
DBREF  3HYD A    1     7  UNP    P01308   INS_HUMAN       35     41             
SEQRES   1 A    7  LEU VAL GLU ALA LEU TYR LEU                                  
FORMUL   2  HOH   *3(H2 O)                                                      
CRYST1   49.478    4.838   19.442  90.00  96.65  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      0.020211  0.000000  0.002357        0.00000                         
SCALE2      0.000000  0.206697  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.051784        0.00000                         
ATOM      1  N   LEU A   1       1.149   1.920   3.550  1.00  5.65           N  
ANISOU    1  N   LEU A   1      480    971    693    150     63     14       N  
ATOM      2  CA  LEU A   1       2.138   2.288   4.580  1.00  5.04           C  
ANISOU    2  CA  LEU A   1      636    614    665     33      4   -131       C  
ATOM      3  C   LEU A   1       3.461   1.638   4.282  1.00  3.88           C  
ANISOU    3  C   LEU A   1      385    511    576    -39    -35    -81       C  
ATOM      4  O   LEU A   1       3.527   0.405   4.165  1.00  4.79           O  
ANISOU    4  O   LEU A   1      463    508    848     23     10    -50       O  
ATOM      5  CB  LEU A   1       1.635   1.889   5.948  1.00  6.19           C  
ANISOU    5  CB  LEU A   1      698    982    671    137     81    -25       C  
ATOM      6  CG  LEU A   1       2.444   2.344   7.182  1.00 10.41           C  
ANISOU    6  CG  LEU A   1     1126   1967    863    136     67   -217       C  
ATOM      7  CD1 LEU A   1       1.603   2.227   8.438  1.00 18.81           C  
ANISOU    7  CD1 LEU A   1     2283   3608   1256    152    330   -519       C  
ATOM      8  CD2 LEU A   1       3.699   1.583   7.375  1.00 10.45           C  
ANISOU    8  CD2 LEU A   1     1204   1622   1142    -69     57    118       C  
ATOM      9  H1  LEU A   1       1.127   0.953   3.458  1.00  5.40           H  
ANISOU    9  H1  LEU A   1      568    822    662     61      8    -14       H  
ATOM     10  H2  LEU A   1       0.274   2.239   3.813  1.00  5.15           H  
ANISOU   10  H2  LEU A   1      540    761    653     63     13    -15       H  
ATOM     11  H3  LEU A   1       1.404   2.323   2.704  1.00  5.24           H  
ANISOU   11  H3  LEU A   1      562    769    657     54      9    -14       H  
ATOM     12  HA  LEU A   1       2.249   3.258   4.575  1.00  4.84           H  
ANISOU   12  HA  LEU A   1      557    657    623     31      2    -43       H  
ATOM     13  HB2 LEU A   1       0.742   2.251   6.048  1.00  6.49           H  
ANISOU   13  HB2 LEU A   1      747    990    726     66     15    -61       H  
ATOM     14  HB3 LEU A   1       1.585   0.920   5.978  1.00  6.58           H  
ANISOU   14  HB3 LEU A   1      780    989    729     55     12    -60       H  
ATOM     15  HG  LEU A   1       2.680   3.278   7.071  1.00 10.84           H  
ANISOU   15  HG  LEU A   1     1278   1792   1047     68     43   -115       H  
ATOM     16 HD11 LEU A   1       2.094   2.588   9.181  1.00 14.99           H  
ANISOU   16 HD11 LEU A   1     1834   2422   1440     60    116   -168       H  
ATOM     17 HD12 LEU A   1       1.404   1.298   8.594  1.00 15.61           H  
ANISOU   17 HD12 LEU A   1     1856   2646   1428    117     87   -214       H  
ATOM     18 HD13 LEU A   1       0.787   2.722   8.316  1.00 15.30           H  
ANISOU   18 HD13 LEU A   1     1927   2469   1416    -16    108   -189       H  
ATOM     19 HD21 LEU A   1       3.547   0.650   7.120  1.00 10.08           H  
ANISOU   19 HD21 LEU A   1     1199   1510   1119     13     21      2       H  
ATOM     20 HD22 LEU A   1       3.964   1.634   8.317  1.00 10.06           H  
ANISOU   20 HD22 LEU A   1     1199   1492   1129      8     24      0       H  
ATOM     21 HD23 LEU A   1       4.396   1.980   6.816  1.00  9.93           H  
ANISOU   21 HD23 LEU A   1     1184   1485   1104      2     28      1       H  
ATOM     22  N   VAL A   2       4.521   2.434   4.230  1.00  3.54           N  
ANISOU   22  N   VAL A   2      519    371    454     50    -60    -38       N  
ATOM     23  CA  VAL A   2       5.866   1.930   4.058  1.00  3.13           C  
ANISOU   23  CA  VAL A   2      365    412    412      0   -102    -63       C  
ATOM     24  C   VAL A   2       6.790   2.592   5.064  1.00  3.68           C  
ANISOU   24  C   VAL A   2      394    369    635     83    122     29       C  
ATOM     25  O   VAL A   2       6.806   3.837   5.179  1.00  4.26           O  
ANISOU   25  O   VAL A   2      452    532    633     21   -112      7       O  
ATOM     26  CB  VAL A   2       6.425   2.168   2.650  1.00  3.78           C  
ANISOU   26  CB  VAL A   2      505    448    481     46     36    -68       C  
ATOM     27  CG1 VAL A   2       7.834   1.667   2.541  1.00  5.01           C  
ANISOU   27  CG1 VAL A   2      578    840    485     25    -26    -10       C  
ATOM     28  CG2 VAL A   2       5.522   1.554   1.584  1.00  5.05           C  
ANISOU   28  CG2 VAL A   2      560    876    483   -232   -103   -117       C  
ATOM     29  H   VAL A   2       4.482   3.290   4.290  1.00  3.28           H  
ANISOU   29  H   VAL A   2      423    378    442      2    -33    -29       H  
ATOM     30  HA  VAL A   2       5.875   0.967   4.219  1.00  3.38           H  
ANISOU   30  HA  VAL A   2      419    402    462     13    -11    -26       H  
ATOM     31  HB  VAL A   2       6.447   3.134   2.489  1.00  3.90           H  
ANISOU   31  HB  VAL A   2      487    517    475    -21    -18    -37       H  
ATOM     32 HG11 VAL A   2       8.026   1.465   1.622  1.00  4.53           H  
ANISOU   32 HG11 VAL A   2      549    651    520      5     -6    -15       H  
ATOM     33 HG12 VAL A   2       7.933   0.873   3.073  1.00  4.63           H  
ANISOU   33 HG12 VAL A   2      552    670    534      3     -5    -25       H  
ATOM     34 HG13 VAL A   2       8.436   2.348   2.851  1.00  4.60           H  
ANISOU   34 HG13 VAL A   2      559    662    526     12     -3    -10       H  
ATOM     35 HG21 VAL A   2       5.433   0.614   1.755  1.00  4.78           H  
ANISOU   35 HG21 VAL A   2      567    722    527    -79    -35    -62       H  
ATOM     36 HG22 VAL A   2       5.916   1.693   0.720  1.00  4.65           H  
ANISOU   36 HG22 VAL A   2      564    674    528    -82    -37    -55       H  
ATOM     37 HG23 VAL A   2       4.662   1.976   1.619  1.00  4.78           H  
ANISOU   37 HG23 VAL A   2      604    686    525    -97    -36    -54       H  
ATOM     38  N   GLU A   3       7.567   1.777   5.771  1.00  2.92           N  
ANISOU   38  N   GLU A   3      332    325    452    -21    -37    -42       N  
ATOM     39  CA AGLU A   3       8.674   2.248   6.587  0.50  3.42           C  
ANISOU   39  CA AGLU A   3      353    608    335    -56     83   -108       C  
ATOM     40  CA BGLU A   3       8.670   2.254   6.575  0.50  3.37           C  
ANISOU   40  CA BGLU A   3      350    600    328    -51     77   -105       C  
ATOM     41  C   GLU A   3       9.920   1.636   5.964  1.00  2.87           C  
ANISOU   41  C   GLU A   3      304    476    308    -83     19    -26       C  
ATOM     42  O   GLU A   3      10.041   0.405   5.901  1.00  3.28           O  
ANISOU   42  O   GLU A   3      447    346    452     31     51    -79       O  
ATOM     43  CB AGLU A   3       8.541   1.813   8.049  0.50  3.31           C  
ANISOU   43  CB AGLU A   3      408    470    380    -45    136    -75       C  
ATOM     44  CB BGLU A   3       8.513   1.848   8.037  0.50  3.20           C  
ANISOU   44  CB BGLU A   3      420    427    366    -23    133    -52       C  
ATOM     45  CG AGLU A   3       9.625   2.367   8.970  0.50  3.86           C  
ANISOU   45  CG AGLU A   3      511    687    266    -58     57     -1       C  
ATOM     46  CG BGLU A   3       9.663   2.264   8.926  0.50  4.43           C  
ANISOU   46  CG BGLU A   3      578    726    376      3     26    -84       C  
ATOM     47  CD AGLU A   3       9.581   1.798  10.378  0.50  4.30           C  
ANISOU   47  CD AGLU A   3      464    534    635   -144     86   -220       C  
ATOM     48  CD BGLU A   3       9.372   2.079  10.393  0.50  7.27           C  
ANISOU   48  CD BGLU A   3      610   1296    855     14    -34    -37       C  
ATOM     49  OE1AGLU A   3       9.326   0.609  10.555  0.50  4.93           O  
ANISOU   49  OE1AGLU A   3      697    880    295    -83     70    110       O  
ATOM     50  OE1BGLU A   3       8.211   1.826  10.769  0.50  8.58           O  
ANISOU   50  OE1BGLU A   3     1133   1266    858    180    119     49       O  
ATOM     51  OE2AGLU A   3       9.823   2.595  11.317  0.50  5.24           O  
ANISOU   51  OE2AGLU A   3      669    896    423    107   -115   -177       O  
ATOM     52  OE2BGLU A   3      10.301   2.252  11.187  0.50  5.38           O  
ANISOU   52  OE2BGLU A   3      462    817    764    -60    -54     29       O  
ATOM     53  H   GLU A   3       7.465   0.924   5.796  1.00  3.13           H  
ANISOU   53  H   GLU A   3      368    389    432    -24     20    -37       H  
ATOM     54  HA AGLU A   3       8.739   3.223   6.557  0.50  3.34           H  
ANISOU   54  HA AGLU A   3      385    502    382    -39     32    -53       H  
ATOM     55  HA BGLU A   3       8.736   3.228   6.532  0.50  3.32           H  
ANISOU   55  HA BGLU A   3      386    494    380    -35     28    -49       H  
ATOM     56  HB2AGLU A   3       7.685   2.119   8.386  0.50  3.51           H  
ANISOU   56  HB2AGLU A   3      459    503    371    -29     49    -45       H  
ATOM     57  HB2BGLU A   3       7.707   2.257   8.388  0.50  3.63           H  
ANISOU   57  HB2BGLU A   3      479    497    402    -14     39    -47       H  
ATOM     58  HB3AGLU A   3       8.581   0.845   8.093  0.50  3.50           H  
ANISOU   58  HB3AGLU A   3      463    494    371    -29     49    -45       H  
ATOM     59  HB3BGLU A   3       8.438   0.883   8.085  0.50  3.60           H  
ANISOU   59  HB3BGLU A   3      485    479    401    -17     38    -46       H  
ATOM     60  HG2AGLU A   3      10.496   2.159   8.600  0.50  3.92           H  
ANISOU   60  HG2AGLU A   3      521    552    414    -47     32    -46       H  
ATOM     61  HG2BGLU A   3      10.441   1.727   8.712  0.50  4.83           H  
ANISOU   61  HG2BGLU A   3      597    699    537     -8      2    -44       H  
ATOM     62  HG3AGLU A   3       9.518   3.329   9.035  0.50  4.00           H  
ANISOU   62  HG3AGLU A   3      517    586    415    -49     35    -44       H  
ATOM     63  HG3BGLU A   3       9.855   3.203   8.775  0.50  4.81           H  
ANISOU   63  HG3BGLU A   3      591    697    536     -1      3    -47       H  
ATOM     64  N   ALA A   4      10.842   2.465   5.490  1.00  2.75           N  
ANISOU   64  N   ALA A   4      299    449    294     71      6    -49       N  
ATOM     65  CA  ALA A   4      12.006   2.016   4.750  1.00  3.09           C  
ANISOU   65  CA  ALA A   4      398    453    322    -24     92    -59       C  
ATOM     66  C   ALA A   4      13.270   2.689   5.248  1.00  2.94           C  
ANISOU   66  C   ALA A   4      351    426    339     44     55    -53       C  
ATOM     67  O   ALA A   4      13.284   3.899   5.529  1.00  3.58           O  
ANISOU   67  O   ALA A   4      435    501    421     -3    -19    -41       O  
ATOM     68  CB  ALA A   4      11.833   2.220   3.258  1.00  4.15           C  
ANISOU   68  CB  ALA A   4      507    762    308   -154     95   -109       C  
ATOM     69  H   ALA A   4      10.814   3.320   5.588  1.00  2.76           H  
ANISOU   69  H   ALA A   4      326    406    316     -1      8    -22       H  
ATOM     70  HA  ALA A   4      12.112   1.056   4.889  1.00  3.11           H  
ANISOU   70  HA  ALA A   4      393    453    334    -22     35    -36       H  
ATOM     71  HB1 ALA A   4      11.060   1.734   2.964  1.00  3.79           H  
ANISOU   71  HB1 ALA A   4      482    586    370    -60     35    -38       H  
ATOM     72  HB2 ALA A   4      12.615   1.896   2.807  1.00  3.83           H  
ANISOU   72  HB2 ALA A   4      491    589    374    -62     31    -36       H  
ATOM     73  HB3 ALA A   4      11.717   3.157   3.082  1.00  3.98           H  
ANISOU   73  HB3 ALA A   4      491    642    378    -67     36    -47       H  
ATOM     74  N   LEU A   5      14.334   1.918   5.332  1.00  2.99           N  
ANISOU   74  N   LEU A   5      410    339    387    -65     95    -60       N  
ATOM     75  CA  LEU A   5      15.634   2.369   5.796  1.00  3.30           C  
ANISOU   75  CA  LEU A   5      396    562    295    -85     -7    -68       C  
ATOM     76  C   LEU A   5      16.689   1.821   4.849  1.00  3.28           C  
ANISOU   76  C   LEU A   5      421    540    283     -9    -53     50       C  
ATOM     77  O   LEU A   5      16.716   0.605   4.614  1.00  3.43           O  
ANISOU   77  O   LEU A   5      392    402    507      3    -28    -52       O  
ATOM     78  CB  LEU A   5      15.875   1.877   7.209  1.00  4.50           C  
ANISOU   78  CB  LEU A   5      682    722    306    -44     21    -52       C  
ATOM     79  CG  LEU A   5      17.250   2.151   7.852  1.00  9.40           C  
ANISOU   79  CG  LEU A   5     1638   1213    717   -149   -525    135       C  
ATOM     80  CD1 LEU A   5      17.789   3.495   7.677  1.00  9.16           C  
ANISOU   80  CD1 LEU A   5     1178   1398    903   -251   -359   -207       C  
ATOM     81  CD2 LEU A   5      17.128   1.821   9.337  1.00 11.72           C  
ANISOU   81  CD2 LEU A   5     2197   1444    811   -421   -588    204       C  
ATOM     82  H   LEU A   5      14.330   1.085   5.118  1.00  2.86           H  
ANISOU   82  H   LEU A   5      371    366    348    -36     40    -38       H  
ATOM     83  HA  LEU A   5      15.679   3.347   5.792  1.00  3.38           H  
ANISOU   83  HA  LEU A   5      430    516    337    -42      6    -28       H  
ATOM     84  HB2 LEU A   5      15.205   2.260   7.785  1.00  4.85           H  
ANISOU   84  HB2 LEU A   5      701    717    425    -33    -50    -25       H  
ATOM     85  HB3 LEU A   5      15.765   0.916   7.196  1.00  4.98           H  
ANISOU   85  HB3 LEU A   5      726    722    444    -43    -65    -16       H  
ATOM     86  HG  LEU A   5      17.893   1.532   7.474  1.00  8.68           H  
ANISOU   86  HG  LEU A   5     1339   1182    776   -151   -278     42       H  
ATOM     87 HD11 LEU A   5      18.580   3.588   8.214  1.00  8.30           H  
ANISOU   87 HD11 LEU A   5     1102   1166    884   -108   -234    -48       H  
ATOM     88 HD12 LEU A   5      17.128   4.128   7.958  1.00  8.71           H  
ANISOU   88 HD12 LEU A   5     1186   1201    920   -126   -226    -36       H  
ATOM     89 HD13 LEU A   5      18.004   3.632   6.753  1.00  8.61           H  
ANISOU   89 HD13 LEU A   5     1159   1176    935   -103   -219    -48       H  
ATOM     90 HD21 LEU A   5      16.648   2.528   9.774  1.00 10.72           H  
ANISOU   90 HD21 LEU A   5     1694   1405    974   -200   -294    122       H  
ATOM     91 HD22 LEU A   5      18.009   1.743   9.711  1.00 10.33           H  
ANISOU   91 HD22 LEU A   5     1670   1315    939   -152   -237     78       H  
ATOM     92 HD23 LEU A   5      16.655   0.991   9.440  1.00 10.20           H  
ANISOU   92 HD23 LEU A   5     1637   1310    926   -143   -263     78       H  
ATOM     93  N   TYR A   6      17.519   2.699   4.281  1.00  3.06           N  
ANISOU   93  N   TYR A   6      361    383    419    -47      4     -5       N  
ATOM     94  CA  TYR A   6      18.548   2.342   3.321  1.00  3.08           C  
ANISOU   94  CA  TYR A   6      380    519    271   -138     47    -54       C  
ATOM     95  C   TYR A   6      19.876   2.878   3.804  1.00  3.48           C  
ANISOU   95  C   TYR A   6      491    516    313     43    -11      2       C  
ATOM     96  O   TYR A   6      20.024   4.082   3.994  1.00  4.60           O  
ANISOU   96  O   TYR A   6      528    524    695    -66    -86    -85       O  
ATOM     97  CB  TYR A   6      18.275   2.935   1.947  1.00  3.85           C  
ANISOU   97  CB  TYR A   6      394    702    364   -122     85    -23       C  
ATOM     98  CG  TYR A   6      16.873   2.775   1.400  1.00  3.42           C  
ANISOU   98  CG  TYR A   6      382    603    313     56     49     49       C  
ATOM     99  CD1 TYR A   6      15.855   3.614   1.819  1.00  3.67           C  
ANISOU   99  CD1 TYR A   6      565    505    324    -58    -28     -9       C  
ATOM    100  CD2 TYR A   6      16.556   1.796   0.450  1.00  3.75           C  
ANISOU  100  CD2 TYR A   6      416    559    447     80     48     51       C  
ATOM    101  CE1 TYR A   6      14.558   3.509   1.303  1.00  3.54           C  
ANISOU  101  CE1 TYR A   6      399    487    457    129    -35     69       C  
ATOM    102  CE2 TYR A   6      15.281   1.695  -0.071  1.00  3.30           C  
ANISOU  102  CE2 TYR A   6      331    626    295     41    -29    -27       C  
ATOM    103  CZ  TYR A   6      14.283   2.550   0.357  1.00  3.37           C  
ANISOU  103  CZ  TYR A   6      359    467    451    -97    -16     30       C  
ATOM    104  OH  TYR A   6      13.017   2.418  -0.175  1.00  3.64           O  
ANISOU  104  OH  TYR A   6      370    551    461      5    -86     19       O  
ATOM    105  H   TYR A   6      17.497   3.543   4.445  1.00  2.94           H  
ANISOU  105  H   TYR A   6      356    399    360    -31     -2     -7       H  
ATOM    106  HA  TYR A   6      18.611   1.369   3.230  1.00  3.22           H  
ANISOU  106  HA  TYR A   6      382    492    347    -52     20    -18       H  
ATOM    107  HB2 TYR A   6      18.454   3.887   1.978  1.00  3.50           H  
ANISOU  107  HB2 TYR A   6      388    586    356    -41     37     -8       H  
ATOM    108  HB3 TYR A   6      18.879   2.517   1.315  1.00  3.43           H  
ANISOU  108  HB3 TYR A   6      386    560    355    -48     34     -8       H  
ATOM    109  HD1 TYR A   6      16.041   4.275   2.443  1.00  3.43           H  
ANISOU  109  HD1 TYR A   6      460    483    360      3     -9     16       H  
ATOM    110  HD2 TYR A   6      17.223   1.227   0.139  1.00  3.37           H  
ANISOU  110  HD2 TYR A   6      377    515    387     40     22     22       H  
ATOM    111  HE1 TYR A   6      13.891   4.088   1.592  1.00  3.38           H  
ANISOU  111  HE1 TYR A   6      414    456    414     21    -13     29       H  
ATOM    112  HE2 TYR A   6      15.090   1.043  -0.705  1.00  3.24           H  
ANISOU  112  HE2 TYR A   6      352    501    375      9      0     14       H  
ATOM    113  HH  TYR A   6      12.808   3.103  -0.576  1.00  3.44           H  
ANISOU  113  HH  TYR A   6      378    481    448    -18    -25      3       H  
ATOM    114  N   LEU A   7      20.857   2.006   3.973  1.00  4.38           N  
ANISOU  114  N   LEU A   7      495    432    737    -29   -127    -96       N  
ATOM    115  CA  LEU A   7      22.208   2.473   4.312  1.00  6.08           C  
ANISOU  115  CA  LEU A   7      671   1003    633    117   -112   -193       C  
ATOM    116  C   LEU A   7      23.293   1.644   3.744  1.00  7.46           C  
ANISOU  116  C   LEU A   7      618   1275    940   -232     29   -339       C  
ATOM    117  O   LEU A   7      23.018   0.697   3.000  1.00 13.45           O  
ANISOU  117  O   LEU A   7     1190   2017   1903   -172    500   -892       O  
ATOM    118  CB  LEU A   7      22.356   2.753   5.793  1.00 11.09           C  
ANISOU  118  CB  LEU A   7     1127   1825   1260   -200      1   -154       C  
ATOM    119  CG  LEU A   7      22.263   1.578   6.717  1.00 11.34           C  
ANISOU  119  CG  LEU A   7     1206   1924   1176   -172   -422    265       C  
ATOM    120  CD1 LEU A   7      22.913   1.965   8.038  1.00 18.81           C  
ANISOU  120  CD1 LEU A   7     2128   3280   1736   -257   -694    -32       C  
ATOM    121  CD2 LEU A   7      20.853   1.118   7.009  1.00 11.10           C  
ANISOU  121  CD2 LEU A   7     1252   1967    996      9    -43     28       C  
ATOM    122  OXT LEU A   7      24.470   1.913   3.995  1.00  9.60           O  
ANISOU  122  OXT LEU A   7      754   1369   1524    124     23      9       O  
ATOM    123  H   LEU A   7      20.779   1.153   3.901  1.00  4.08           H  
ANISOU  123  H   LEU A   7      510    483    557      2    -52    -61       H  
ATOM    124  HA  LEU A   7      22.322   3.342   3.880  1.00  6.70           H  
ANISOU  124  HA  LEU A   7      742    997    804    -19    -44   -126       H  
ATOM    125  HB2 LEU A   7      23.219   3.171   5.933  1.00  9.43           H  
ANISOU  125  HB2 LEU A   7     1101   1432   1049    -45    -90    -38       H  
ATOM    126  HB3 LEU A   7      21.660   3.376   6.052  1.00  9.61           H  
ANISOU  126  HB3 LEU A   7     1132   1459   1058    -75   -102    -28       H  
ATOM    127  HG  LEU A   7      22.755   0.830   6.347  1.00 11.80           H  
ANISOU  127  HG  LEU A   7     1368   1901   1215   -100   -230     62       H  
ATOM    128 HD11 LEU A   7      23.845   2.140   7.890  1.00 14.43           H  
ANISOU  128 HD11 LEU A   7     1771   2250   1459    -82   -335     28       H  
ATOM    129 HD12 LEU A   7      22.815   1.242   8.663  1.00 14.59           H  
ANISOU  129 HD12 LEU A   7     1700   2317   1524    -87   -332    -33       H  
ATOM    130 HD13 LEU A   7      22.483   2.753   8.379  1.00 14.87           H  
ANISOU  130 HD13 LEU A   7     1752   2396   1499   -176   -353     90       H  
ATOM    131 HD21 LEU A   7      20.870   0.474   7.720  1.00 10.59           H  
ANISOU  131 HD21 LEU A   7     1234   1645   1142    -25    -76     29       H  
ATOM    132 HD22 LEU A   7      20.484   0.716   6.220  1.00 10.51           H  
ANISOU  132 HD22 LEU A   7     1230   1636   1123    -26    -78     36       H  
ATOM    133 HD23 LEU A   7      20.323   1.876   7.268  1.00 10.64           H  
ANISOU  133 HD23 LEU A   7     1247   1658   1135    -39    -80     46       H  
TER     134      LEU A   7                                                      
HETATM  135  O   HOH A   8       1.951   1.278   0.907  1.00 29.45           O  
ANISOU  135  O   HOH A   8     4097   4648   2444   -321     99    749       O  
HETATM  136  O   HOH A   9      21.018   0.402   1.001  1.00 28.03           O  
ANISOU  136  O   HOH A   9     3468   5153   2030   -297    567   -657       O  
HETATM  137  O   HOH A  10       2.557   3.706   1.400  1.00 27.04           O  
ANISOU  137  O   HOH A  10     3456   3400   3416    629    -82   -168       O  
MASTER      250    0    0    0    0    0    0    6  136    1    0    1          
END                                                                             
