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***  HYDROLASE(METALLOPROTEINASE) 01-SEP-93 8TLN  ***

elNémo ID: 20021021055064258

Job options:

ID        	=	 20021021055064258
JOBID     	=	 HYDROLASE(METALLOPROTEINASE) 01-SEP-93 8TLN
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 5
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 on

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    HYDROLASE(METALLOPROTEINASE)            01-SEP-93   8TLN              
TITLE     STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED NEUTRAL   
TITLE    2 PROTEASES UNDERGO HINGE-BENDING MOTION DURING CATALYSIS              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THERMOLYSIN;                                               
COMPND   3 CHAIN: E;                                                            
COMPND   4 EC: 3.4.24.27                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;                   
SOURCE   3 ORGANISM_TAXID: 1427                                                 
KEYWDS    HYDROLASE(METALLOPROTEINASE)                                          
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.TRONRUD,B.W.MATTHEWS                                                
REVDAT   4   29-NOV-17 8TLN    1       HELIX                                    
REVDAT   3   24-FEB-09 8TLN    1       VERSN                                    
REVDAT   2   01-APR-03 8TLN    1       JRNL                                     
REVDAT   1   30-APR-94 8TLN    0                                                
SPRSDE     30-APR-94 8TLN      3TLN                                             
JRNL        AUTH   D.R.HOLLAND,D.E.TRONRUD,H.W.PLEY,K.M.FLAHERTY,W.STARK,       
JRNL        AUTH 2 J.N.JANSONIUS,D.B.MCKAY,B.W.MATTHEWS                         
JRNL        TITL   STRUCTURAL COMPARISON SUGGESTS THAT THERMOLYSIN AND RELATED  
JRNL        TITL 2 NEUTRAL PROTEASES UNDERGO HINGE-BENDING MOTION DURING        
JRNL        TITL 3 CATALYSIS.                                                   
JRNL        REF    BIOCHEMISTRY                  V.  31 11310 1992              
JRNL        REFN                   ISSN 0006-2960                               
JRNL        PMID   1445869                                                      
JRNL        DOI    10.1021/BI00161A008                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.A.HOLMES,B.W.MATTHEWS                                      
REMARK   1  TITL   STRUCTURE OF THERMOLYSIN REFINED AT 1.6 ANGSTROMS RESOLUTION 
REMARK   1  REF    J.MOL.BIOL.                   V. 160   623 1982              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 2                                                          
REMARK   1  AUTH   A.F.MONZINGO,B.W.MATTHEWS                                    
REMARK   1  TITL   STRUCTURE OF A MERCAPTAN-THERMOLYSIN COMPLEX ILLUSTRATES     
REMARK   1  TITL 2 MODE OF INHIBITION OF ZINC PROTEASES BY SUBSTRATE-ANALOGUE   
REMARK   1  TITL 3 MERCAPTANS                                                   
REMARK   1  REF    BIOCHEMISTRY                  V.  21  3390 1982              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 3                                                          
REMARK   1  AUTH   M.A.HOLMES,B.W.MATTHEWS                                      
REMARK   1  TITL   BINDING OF HYDROXAMIC ACID INHIBITORS TO CRYSTALLINE         
REMARK   1  TITL 2 THERMOLYSIN SUGGESTS A PENTACOORDINATE ZINC INTERMEDIATE IN  
REMARK   1  TITL 3 CATALYSIS                                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  20  6912 1981              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 4                                                          
REMARK   1  AUTH   M.C.BOLOGNESI,B.W.MATTHEWS                                   
REMARK   1  TITL   BINDING OF THE BIPRODUCT ANALOG L-BENZYLSUCCINIC ACID TO     
REMARK   1  TITL 2 THERMOLYSIN DETERMINED BY X-RAY CRYSTALLOGRAPHY              
REMARK   1  REF    J.BIOL.CHEM.                  V. 254   634 1979              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 5                                                          
REMARK   1  AUTH   W.R.KESTER,B.W.MATTHEWS                                      
REMARK   1  TITL   COMPARISON OF THE STRUCTURES OF CARBOXYPEPTIDASE A AND       
REMARK   1  TITL 2 THERMOLYSIN                                                  
REMARK   1  REF    J.BIOL.CHEM.                  V. 252  7704 1977              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 6                                                          
REMARK   1  AUTH   L.H.WEAVER,W.R.KESTER,B.W.MATTHEWS                           
REMARK   1  TITL   A CRYSTALLOGRAPHIC STUDY OF THE COMPLEX OF PHOSPHORAMIDON    
REMARK   1  TITL 2 WITH THERMOLYSIN. A MODEL FOR THE PRESUMED CATALYTIC         
REMARK   1  TITL 3 TRANSITION STATE AND FOR THE BINDING OF EXTENDED SUBSTRATES  
REMARK   1  REF    J.MOL.BIOL.                   V. 114   119 1977              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 7                                                          
REMARK   1  AUTH   W.R.KESTER,B.W.MATTHEWS                                      
REMARK   1  TITL   CRYSTALLOGRAPHIC STUDY OF THE BINDING OF DIPEPTIDE           
REMARK   1  TITL 2 INHIBITORS TO THERMOLYSIN. IMPLICATIONS FOR THE MECHANISM OF 
REMARK   1  TITL 3 CATALYSIS                                                    
REMARK   1  REF    BIOCHEMISTRY                  V.  16  2506 1977              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 8                                                          
REMARK   1  AUTH   F.W.DAHLQUIST,J.W.LONG,W.L.BIGBEE                            
REMARK   1  TITL   ROLE OF CALCIUM IN THE THERMAL STABILITY OF THERMOLYSIN      
REMARK   1  REF    BIOCHEMISTRY                  V.  15  1103 1976              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 9                                                          
REMARK   1  AUTH   P.L.LEVY,M.K.PANGBURN,Y.BURSTEIN,L.H.ERICSSON,H.NEURATH,     
REMARK   1  AUTH 2 K.A.WALSH                                                    
REMARK   1  TITL   EVIDENCE OF HOMOLOGOUS RELATIONSHIP BETWEEN THERMOLYSIN AND  
REMARK   1  TITL 2 NEUTRAL PROTEASE A OF BACILLUS SUBTILIS                      
REMARK   1  REF    PROC.NATL.ACAD.SCI.USA        V.  72  4341 1975              
REMARK   1  REFN                   ISSN 0027-8424                               
REMARK   1 REFERENCE 10                                                         
REMARK   1  AUTH   B.W.MATTHEWS,L.H.WEAVER,W.R.KESTER                           
REMARK   1  TITL   THE CONFORMATION OF THERMOLYSIN                              
REMARK   1  REF    J.BIOL.CHEM.                  V. 249  8030 1974              
REMARK   1  REFN                   ISSN 0021-9258                               
REMARK   1 REFERENCE 11                                                         
REMARK   1  AUTH   B.W.MATTHEWS,L.H.WEAVER                                      
REMARK   1  TITL   BINDING OF LANTHANIDE IONS TO THERMOLYSIN                    
REMARK   1  REF    BIOCHEMISTRY                  V.  13  1719 1974              
REMARK   1  REFN                   ISSN 0006-2960                               
REMARK   1 REFERENCE 12                                                         
REMARK   1  AUTH   P.M.COLMAN,J.N.JANSONIUS,B.W.MATTHEWS                        
REMARK   1  TITL   THE STRUCTURE OF THERMOLYSIN,AN ELECTRON DENSITY MAP AT 2.3  
REMARK   1  TITL 2 ANGSTROMS RESOLUTION                                         
REMARK   1  REF    J.MOL.BIOL.                   V.  70   701 1972              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1 REFERENCE 13                                                         
REMARK   1  AUTH   K.TITANI,M.A.HERMODSON,L.H.ERICSSON,K.A.WALSH,H.NEURATH      
REMARK   1  TITL   AMINO-ACID SEQUENCE OF THERMOLYSIN                           
REMARK   1  REF    NATURE NEW BIOL.              V. 238    35 1972              
REMARK   1  REFN                   ISSN 0369-4887                               
REMARK   1 REFERENCE 14                                                         
REMARK   1  AUTH   B.W.MATTHEWS,J.N.JANSONIUS,P.M.COLMAN,B.P.SCHOENBORN,        
REMARK   1  AUTH 2 D.DUPORQUE                                                   
REMARK   1  TITL   THREE DIMENSIONAL STRUCTURE OF THERMOLYSIN                   
REMARK   1  REF    NATURE NEW BIOL.              V. 238    37 1972              
REMARK   1  REFN                   ISSN 0369-4887                               
REMARK   1 REFERENCE 15                                                         
REMARK   1  AUTH   B.W.MATTHEWS,P.M.COLMAN,J.N.JANSONIUS,K.TITANI,K.A.WALSH,    
REMARK   1  AUTH 2 H.NEURATH                                                    
REMARK   1  TITL   STRUCTURE OF THERMOLYSIN                                     
REMARK   1  REF    NATURE NEW BIOL.              V. 238    41 1972              
REMARK   1  REFN                   ISSN 0369-4887                               
REMARK   1 REFERENCE 16                                                         
REMARK   1  EDIT   M.O.DAYHOFF                                                  
REMARK   1  REF    ATLAS OF PROTEIN SEQUENCE     V.   5    98 1976              
REMARK   1  REF  2 AND STRUCTURE,SUPPLEMENT 2                                   
REMARK   1  PUBL   NATIONAL BIOMEDICAL RESEARCH FOUNDATION, SILVER SPRING,MD.   
REMARK   1  REFN                   ISSN 0-912466-05-7                           
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : TNT                                                  
REMARK   3   AUTHORS     : TRONRUD,TEN EYCK,MATTHEWS                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 20.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : NULL                           
REMARK   3   NUMBER OF REFLECTIONS             : NULL                           
REMARK   3                                                                      
REMARK   3  USING DATA ABOVE SIGMA CUTOFF.                                      
REMARK   3   CROSS-VALIDATION METHOD          : NULL                            
REMARK   3   FREE R VALUE TEST SET SELECTION  : NULL                            
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : NULL                            
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                                                                      
REMARK   3  USING ALL DATA, NO SIGMA CUTOFF.                                    
REMARK   3   R VALUE   (WORKING + TEST SET, NO CUTOFF) : NULL                   
REMARK   3   R VALUE          (WORKING SET, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE                  (NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET SIZE (%, NO CUTOFF) : NULL                   
REMARK   3   FREE R VALUE TEST SET COUNT   (NO CUTOFF) : NULL                   
REMARK   3   TOTAL NUMBER OF REFLECTIONS   (NO CUTOFF) : NULL                   
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2432                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 26                                      
REMARK   3   SOLVENT ATOMS            : 157                                     
REMARK   3                                                                      
REMARK   3  WILSON B VALUE (FROM FCALC, A**2) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.    RMS    WEIGHT  COUNT           
REMARK   3   BOND LENGTHS                 (A) : 0.022 ; NULL  ; NULL            
REMARK   3   BOND ANGLES            (DEGREES) : 3.143 ; NULL  ; NULL            
REMARK   3   TORSION ANGLES         (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   PSEUDOROTATION ANGLES  (DEGREES) : NULL  ; NULL  ; NULL            
REMARK   3   TRIGONAL CARBON PLANES       (A) : NULL  ; NULL  ; NULL            
REMARK   3   GENERAL PLANES               (A) : NULL  ; NULL  ; NULL            
REMARK   3   ISOTROPIC THERMAL FACTORS (A**2) : NULL  ; NULL  ; NULL            
REMARK   3   NON-BONDED CONTACTS          (A) : NULL  ; NULL  ; NULL            
REMARK   3                                                                      
REMARK   3  INCORRECT CHIRAL-CENTERS (COUNT) : NULL                             
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
REMARK   3                                                                      
REMARK   3  RESTRAINT LIBRARIES.                                                
REMARK   3   STEREOCHEMISTRY : NULL                                             
REMARK   3   ISOTROPIC THERMAL FACTOR RESTRAINTS : NULL                         
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 8TLN COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY BNL.                                
REMARK 100 THE DEPOSITION ID IS D_1000180022.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : NULL                               
REMARK 200  TEMPERATURE           (KELVIN) : NULL                               
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : NULL                               
REMARK 200  RADIATION SOURCE               : NULL                               
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : NULL                               
REMARK 200  WAVELENGTH OR RANGE        (A) : NULL                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : NULL                               
REMARK 200  DETECTOR MANUFACTURER          : NULL                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : NULL                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : NULL                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : NULL                               
REMARK 200  RESOLUTION RANGE LOW       (A) : NULL                               
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : NULL                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
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   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: NULL                                           
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 49.29                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.43                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: NULL                                     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       43.80000            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       87.60000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       65.70000            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      109.50000            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       21.90000            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       43.80000            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       87.60000            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      109.50000            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       65.70000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       21.90000            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: E                                     
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 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 E 619  LIES ON A SPECIAL POSITION.                          
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU E 160   CD    GLU E 160   OE2     0.071                       
REMARK 500    GLU E 177   CD    GLU E 177   OE2     0.086                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ASP E  16   CB  -  CG  -  OD1 ANGL. DEV. =   6.6 DEGREES          
REMARK 500    ASP E  16   CB  -  CG  -  OD2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TYR E  24   CG  -  CD1 -  CE1 ANGL. DEV. =   5.5 DEGREES          
REMARK 500    TYR E  24   CD1 -  CE1 -  CZ  ANGL. DEV. =  -6.1 DEGREES          
REMARK 500    TYR E  29   CB  -  CG  -  CD1 ANGL. DEV. =  -4.9 DEGREES          
REMARK 500    TYR E  29   CG  -  CD2 -  CE2 ANGL. DEV. =  -6.8 DEGREES          
REMARK 500    TYR E  29   CD1 -  CE1 -  CZ  ANGL. DEV. =  -5.4 DEGREES          
REMARK 500    TYR E  42   CB  -  CG  -  CD2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP E  57   CB  -  CG  -  OD1 ANGL. DEV. =   5.4 DEGREES          
REMARK 500    ASP E  59   CB  -  CG  -  OD1 ANGL. DEV. =   5.8 DEGREES          
REMARK 500    PHE E  62   CB  -  CG  -  CD1 ANGL. DEV. =   5.2 DEGREES          
REMARK 500    ASP E  72   CB  -  CG  -  OD2 ANGL. DEV. =   6.8 DEGREES          
REMARK 500    TYR E  75   CB  -  CG  -  CD2 ANGL. DEV. =  -5.2 DEGREES          
REMARK 500    TYR E  93   CB  -  CG  -  CD2 ANGL. DEV. =  -5.7 DEGREES          
REMARK 500    ARG E 101   NE  -  CZ  -  NH2 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    TYR E 110   CB  -  CG  -  CD2 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    MET E 120   CA  -  CB  -  CG  ANGL. DEV. = -10.7 DEGREES          
REMARK 500    ASN E 183   CB  -  CA  -  C   ANGL. DEV. = -15.4 DEGREES          
REMARK 500    ASP E 185   CB  -  CG  -  OD1 ANGL. DEV. =  -6.4 DEGREES          
REMARK 500    TYR E 193   CB  -  CG  -  CD1 ANGL. DEV. =  -4.1 DEGREES          
REMARK 500    ASP E 200   CB  -  CG  -  OD1 ANGL. DEV. =   7.2 DEGREES          
REMARK 500    ASP E 200   CB  -  CG  -  OD2 ANGL. DEV. = -12.3 DEGREES          
REMARK 500    ARG E 203   NE  -  CZ  -  NH1 ANGL. DEV. =   3.8 DEGREES          
REMARK 500    ASP E 207   CB  -  CG  -  OD1 ANGL. DEV. =   6.5 DEGREES          
REMARK 500    ASP E 207   CB  -  CG  -  OD2 ANGL. DEV. =  -5.8 DEGREES          
REMARK 500    TYR E 211   CG  -  CD2 -  CE2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ASP E 215   CB  -  CG  -  OD1 ANGL. DEV. =   6.2 DEGREES          
REMARK 500    ASP E 215   CB  -  CG  -  OD2 ANGL. DEV. =  -8.2 DEGREES          
REMARK 500    TYR E 217   CD1 -  CE1 -  CZ  ANGL. DEV. =  -6.0 DEGREES          
REMARK 500    ARG E 220   NE  -  CZ  -  NH1 ANGL. DEV. =   5.0 DEGREES          
REMARK 500    ARG E 220   NE  -  CZ  -  NH2 ANGL. DEV. =  -4.0 DEGREES          
REMARK 500    ASP E 226   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500    TYR E 274   CB  -  CG  -  CD2 ANGL. DEV. =   4.8 DEGREES          
REMARK 500    ARG E 285   NE  -  CZ  -  NH1 ANGL. DEV. =   3.0 DEGREES          
REMARK 500    THR E 299   CA  -  CB  -  CG2 ANGL. DEV. =  -9.0 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    SER E  25       81.26   -160.38                                   
REMARK 500    THR E  26      -63.47     80.12                                   
REMARK 500    SER E  92     -167.75     62.43                                   
REMARK 500    SER E 107     -162.43     61.62                                   
REMARK 500    THR E 152      -96.53   -120.91                                   
REMARK 500    ASN E 159     -147.48     53.06                                   
REMARK 500    ASN E 183       71.23     36.84                                   
REMARK 500    THR E 194       76.22     35.68                                   
REMARK 500    ASP E 207       82.81   -153.10                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 RESIDUES 1321 AND 1322 FORM A DIPEPTIDE (VAL-LYS) BOUND IN THE       
REMARK 600 ACTIVE SITE OF THE MOLECULE. IT IS PRESUMED THAT THE ORIGIN OF THIS  
REMARK 600 DIPEPTIDE IS THE C-TERMINAL TWO RESIDUES OF THE PROTEIN. SINCE THE   
REMARK 600 C-TERMINUS APPEARS AT FULL OCCUPANCY, MOLECULES NOT INCORPORATED     
REMARK 600 INTO THE CRYSTAL MUST HAVE BEEN SACRIFICED.                          
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 317  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 190   OE1                                                    
REMARK 620 2 ASP E 138   OD2  85.2                                              
REMARK 620 3 GLU E 177   OE1 129.4  77.0                                        
REMARK 620 4 GLU E 177   OE2 120.1 125.2  48.8                                  
REMARK 620 5 GLU E 187   O    76.4  84.2 145.6 145.0                            
REMARK 620 6 GLU E 190   OE2  53.9 100.7  83.2  69.1 129.0                      
REMARK 620 7 HOH E 346   O   152.5  98.0  77.6  80.3  76.8 149.4                
REMARK 620 8 ASP E 185   OD1  84.9 158.6 123.5  76.1  75.0  88.6  82.5          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 318  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU E 177   OE2                                                    
REMARK 620 2 GLU E 190   OE2  85.2                                              
REMARK 620 3 ASN E 183   O    90.3 174.7                                        
REMARK 620 4 ASP E 185   OD2  89.2  81.6  95.7                                  
REMARK 620 5 HOH E 353   O    86.2  92.5  89.9 172.8                            
REMARK 620 6 HOH E 475   O   168.8  91.5  93.4 100.9  83.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 319  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLN E  61   O                                                      
REMARK 620 2 ASP E  59   OD1  92.1                                              
REMARK 620 3 HOH E 503   O   173.9  81.9                                        
REMARK 620 4 ASP E  57   OD1  98.3 118.2  84.4                                  
REMARK 620 5 HOH E 419   O    84.9 158.6 100.9  83.1                            
REMARK 620 6 HOH E 482   O    92.3  80.8  87.1 157.6  78.1                      
REMARK 620 7 ASP E  57   OD2  92.7  65.5  84.5  53.3 135.7 146.1                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA E 320  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR E 194   O                                                      
REMARK 620 2 THR E 194   OG1  68.5                                              
REMARK 620 3 HOH E 354   O   153.6 125.5                                        
REMARK 620 4 HOH E 480   O    78.7 144.1  80.1                                  
REMARK 620 5 ILE E 197   O    77.6 106.9 113.5  79.1                            
REMARK 620 6 ASP E 200   OD1 132.9  79.9  73.5 135.3  79.3                      
REMARK 620 7 TYR E 193   O    79.3  76.3  82.9  83.6 153.4 126.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN E 321  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS E 146   NE2                                                    
REMARK 620 2 GLU E 166   OE2  85.6                                              
REMARK 620 3 HOH E 392   O   120.3  99.3                                        
REMARK 620 4 HIS E 142   NE2 103.9 132.2 114.2                                  
REMARK 620 N                    1     2     3                                   
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE VAL E 1322                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE LYS E 1323                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 317                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 318                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 319                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA E 320                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ZN E 321                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE DMS E 324                 
DBREF  8TLN E    1   316  UNP    P00800   THER_BACTH       1    316             
SEQRES   1 E  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL          
SEQRES   2 E  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR          
SEQRES   3 E  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASP GLY ILE          
SEQRES   4 E  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY          
SEQRES   5 E  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER          
SEQRES   6 E  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY          
SEQRES   7 E  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU          
SEQRES   8 E  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL          
SEQRES   9 E  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY          
SEQRES  10 E  316  SER GLU MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE          
SEQRES  11 E  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU          
SEQRES  12 E  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE          
SEQRES  13 E  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER          
SEQRES  14 E  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS          
SEQRES  15 E  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO          
SEQRES  16 E  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO          
SEQRES  17 E  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR          
SEQRES  18 E  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER          
SEQRES  19 E  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY          
SEQRES  20 E  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG          
SEQRES  21 E  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN          
SEQRES  22 E  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA          
SEQRES  23 E  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR          
SEQRES  24 E  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA          
SEQRES  25 E  316  VAL GLY VAL LYS                                              
HET    VAL  E1322       7                                                       
HET    LYS  E1323      10                                                       
HET     CA  E 317       1                                                       
HET     CA  E 318       1                                                       
HET     CA  E 319       1                                                       
HET     CA  E 320       1                                                       
HET     ZN  E 321       1                                                       
HET    DMS  E 324       4                                                       
HETNAM     VAL VALINE                                                           
HETNAM     LYS LYSINE                                                           
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     DMS DIMETHYL SULFOXIDE                                               
FORMUL   2  VAL    C5 H11 N O2                                                  
FORMUL   3  LYS    C6 H15 N2 O2 1+                                              
FORMUL   4   CA    4(CA 2+)                                                     
FORMUL   8   ZN    ZN 2+                                                        
FORMUL   9  DMS    C2 H6 O S                                                    
FORMUL  10  HOH   *157(H2 O)                                                    
HELIX    1  H1 SER E   65  VAL E   87  165,66 3/10 OR ALPHA-II CONFN      23    
HELIX    2  H2 LEU E  133  GLY E  135  5                                   3    
HELIX    3  H3 ILE E  137  ASP E  150  1151 IN ALPHA-II CONFORMATION      14    
HELIX    4  H4 GLU E  160  ALA E  180  1180 IN 3/10 CONFORMATION          21    
HELIX    5  H5 GLU E  190  VAL E  192  1192 IN 3/10 OR ALPHA-II CONFN      3    
HELIX    6  H6 PRO E  208  TYR E  211  5                                   4    
HELIX    7  H7 TYR E  217  LYS E  219  5                                   3    
HELIX    8  H8 ASP E  226  GLY E  229  6LEFT-HAND ALPHA HELIX              4    
HELIX    9  H9 ASN E  233  GLN E  246  1233,234 IN 3/10 CONFORMATION      14    
HELIX   10 H10 ARG E  260  TYR E  274  1262 IN ALPHA-II CONFORMATION      15    
HELIX   11 H11 PHE E  281  TYR E  296  1                                  16    
HELIX   12 H12 GLN E  301  VAL E  313  1313 IN 3/10 CONFORMATION          13    
SHEET    1  S1 5 GLN E  31  ASP E  32  0                                        
SHEET    2  S1 5 ILE E  39  ASP E  43 -1  N  ILE E  39   O  ASP E  32           
SHEET    3  S1 5 ILE E 100  TYR E 106  1  N  SER E 102   O  PHE E  40           
SHEET    4  S1 5 GLU E 119  TYR E 122  1  N  TYR E 122   O  SER E 103           
SHEET    5  S1 5 ASN E 112  TRP E 115 -1  N  PHE E 114   O  VAL E 121           
SHEET    1  S2 5 GLY E  52  LEU E  54  0                                        
SHEET    2  S2 5 ILE E  39  ASP E  43 -1  N  ASP E  43   O  SER E  53           
SHEET    3  S2 5 ILE E 100  TYR E 106  1  N  SER E 102   O  PHE E  40           
SHEET    4  S2 5 GLU E 119  TYR E 122  1  N  TYR E 122   O  SER E 103           
SHEET    5  S2 5 ASN E 112  TRP E 115 -1  N  PHE E 114   O  VAL E 121           
SHEET    1  S3 5 TRP E  55  ASP E  57  0                                        
SHEET    2  S3 5 TYR E  27  TYR E  29 -1  O  TYR E  28   N  ASP E  57           
SHEET    3  S3 5 ASP E  16  SER E  25 -1  O  THR E  23   N  TYR E  29           
SHEET    4  S3 5 THR E   2  ARG E  11 -1  O  THR E   6   N  THR E  22           
SHEET    5  S3 5 GLN E  61  PHE E  62  1  N  PHE E  62   O  VAL E   9           
LINK        CA    CA E 317                 OE1 GLU E 190     1555   1555  2.45  
LINK        CA    CA E 317                 OD2 ASP E 138     1555   1555  2.36  
LINK        CA    CA E 317                 OE1 GLU E 177     1555   1555  2.48  
LINK        CA    CA E 317                 OE2 GLU E 177     1555   1555  2.85  
LINK        CA    CA E 317                 O   GLU E 187     1555   1555  2.26  
LINK        CA    CA E 317                 OE2 GLU E 190     1555   1555  2.50  
LINK        CA    CA E 317                 O   HOH E 346     1555   1555  2.60  
LINK        CA    CA E 317                 OD1 ASP E 185     1555   1555  2.41  
LINK        CA    CA E 318                 OE2 GLU E 177     1555   1555  2.20  
LINK        CA    CA E 318                 OE2 GLU E 190     1555   1555  2.31  
LINK        CA    CA E 318                 O   ASN E 183     1555   1555  2.44  
LINK        CA    CA E 318                 OD2 ASP E 185     1555   1555  2.30  
LINK        CA    CA E 318                 O   HOH E 353     1555   1555  2.42  
LINK        CA    CA E 318                 O   HOH E 475     1555   1555  2.30  
LINK        CA    CA E 319                 O   GLN E  61     1555   1555  2.30  
LINK        CA    CA E 319                 OD1 ASP E  59     1555   1555  2.30  
LINK        CA    CA E 319                 O   HOH E 503     1555   1555  2.38  
LINK        CA    CA E 319                 OD1 ASP E  57     1555   1555  2.34  
LINK        CA    CA E 319                 O   HOH E 419     1555   1555  2.43  
LINK        CA    CA E 319                 O   HOH E 482     1555   1555  2.30  
LINK        CA    CA E 319                 OD2 ASP E  57     1555   1555  2.50  
LINK        CA    CA E 320                 O   THR E 194     1555   1555  2.31  
LINK        CA    CA E 320                 OG1 THR E 194     1555   1555  2.24  
LINK        CA    CA E 320                 O   HOH E 354     1555   1555  2.44  
LINK        CA    CA E 320                 O   HOH E 480     1555   1555  2.23  
LINK        CA    CA E 320                 O   ILE E 197     1555   1555  2.28  
LINK        CA    CA E 320                 OD1 ASP E 200     1555   1555  2.26  
LINK        CA    CA E 320                 O   TYR E 193     1555   1555  2.41  
LINK        ZN    ZN E 321                 NE2 HIS E 146     1555   1555  1.97  
LINK        ZN    ZN E 321                 OE2 GLU E 166     1555   1555  1.88  
LINK        ZN    ZN E 321                 O   HOH E 392     1555   1555  2.16  
LINK        ZN    ZN E 321                 NE2 HIS E 142     1555   1555  1.93  
LINK         C   VAL E1322                 N   LYS E1323     1555   1555  1.35  
CISPEP   1 LEU E   50    PRO E   51          0         4.68                     
SITE     1 AC1  7 ASN E 112  ALA E 113  GLU E 143  ARG E 203                    
SITE     2 AC1  7 HIS E 231  HOH E 392  LYS E1323                               
SITE     1 AC2  3 ASN E 111  ASN E 112  VAL E1322                               
SITE     1 AC3  6 ASP E 138  GLU E 177  ASP E 185  GLU E 187                    
SITE     2 AC3  6 GLU E 190  HOH E 346                                          
SITE     1 AC4  6 GLU E 177  ASN E 183  ASP E 185  GLU E 190                    
SITE     2 AC4  6 HOH E 353  HOH E 475                                          
SITE     1 AC5  6 ASP E  57  ASP E  59  GLN E  61  HOH E 419                    
SITE     2 AC5  6 HOH E 482  HOH E 503                                          
SITE     1 AC6  6 TYR E 193  THR E 194  ILE E 197  ASP E 200                    
SITE     2 AC6  6 HOH E 354  HOH E 480                                          
SITE     1 AC7  4 HIS E 142  HIS E 146  GLU E 166  HOH E 392                    
SITE     1 AC8  4 TYR E  66  SER E 218  TYR E 251  HOH E 506                    
CRYST1   94.100   94.100  131.400  90.00  90.00 120.00 P 61 2 2     12          
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      0.010627  0.006135  0.000000        0.00000                         
SCALE2      0.000000  0.012271  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007610        0.00000                         
ATOM      1  N   ILE E   1       9.246  51.879  -1.294  1.00 45.40           N  
ATOM      2  CA  ILE E   1       8.264  52.244  -0.248  1.00 35.87           C  
ATOM      3  C   ILE E   1       7.913  53.770   0.014  1.00 50.40           C  
ATOM      4  O   ILE E   1       8.734  54.647   0.069  1.00 37.01           O  
ATOM      5  CB  ILE E   1       8.686  51.693   1.085  1.00 40.05           C  
ATOM      6  CG1 ILE E   1       8.139  50.329   1.399  1.00 22.67           C  
ATOM      7  CG2 ILE E   1       8.201  52.622   2.190  1.00 46.54           C  
ATOM      8  CD1 ILE E   1       8.398  50.022   2.879  1.00100.00           C  
ATOM      9  N   THR E   2       6.673  54.156   0.337  1.00 33.08           N  
ATOM     10  CA  THR E   2       6.360  55.588   0.624  1.00 37.44           C  
ATOM     11  C   THR E   2       6.066  55.735   2.090  1.00 37.54           C  
ATOM     12  O   THR E   2       5.237  54.963   2.562  1.00 39.60           O  
ATOM     13  CB  THR E   2       5.036  55.979   0.011  1.00 49.97           C  
ATOM     14  OG1 THR E   2       5.128  55.786  -1.370  1.00 41.21           O  
ATOM     15  CG2 THR E   2       4.832  57.451   0.308  1.00 52.71           C  
ATOM     16  N   GLY E   3       6.681  56.674   2.817  1.00 17.50           N  
ATOM     17  CA  GLY E   3       6.433  56.795   4.229  1.00 14.05           C  
ATOM     18  C   GLY E   3       7.187  57.968   4.741  1.00 20.94           C  
ATOM     19  O   GLY E   3       7.558  58.889   3.999  1.00 27.69           O  
ATOM     20  N   THR E   4       7.346  57.962   6.015  1.00 16.12           N  
ATOM     21  CA  THR E   4       7.977  59.101   6.651  1.00 16.25           C  
ATOM     22  C   THR E   4       9.441  58.847   6.936  1.00 19.02           C  
ATOM     23  O   THR E   4       9.786  57.803   7.554  1.00 20.33           O  
ATOM     24  CB  THR E   4       7.203  59.227   8.023  1.00 21.57           C  
ATOM     25  OG1 THR E   4       5.837  59.412   7.706  1.00 38.00           O  
ATOM     26  CG2 THR E   4       7.674  60.452   8.730  1.00 32.90           C  
ATOM     27  N   SER E   5      10.271  59.838   6.621  1.00 16.25           N  
ATOM     28  CA  SER E   5      11.693  59.630   6.966  1.00 14.64           C  
ATOM     29  C   SER E   5      11.999  59.746   8.431  1.00 18.48           C  
ATOM     30  O   SER E   5      11.461  60.621   9.081  1.00 19.43           O  
ATOM     31  CB  SER E   5      12.489  60.642   6.233  1.00 23.02           C  
ATOM     32  OG  SER E   5      12.340  60.450   4.808  1.00 23.36           O  
ATOM     33  N   THR E   6      12.895  58.907   8.975  1.00  9.79           N  
ATOM     34  CA  THR E   6      13.200  58.984  10.349  1.00  9.44           C  
ATOM     35  C   THR E   6      14.617  58.466  10.586  1.00  9.73           C  
ATOM     36  O   THR E   6      15.281  58.186   9.563  1.00 13.60           O  
ATOM     37  CB  THR E   6      12.126  58.265  11.168  1.00 22.01           C  
ATOM     38  OG1 THR E   6      12.398  58.609  12.577  1.00 22.45           O  
ATOM     39  CG2 THR E   6      12.179  56.743  10.845  1.00 18.90           C  
ATOM     40  N   VAL E   7      15.021  58.402  11.816  1.00 12.10           N  
ATOM     41  CA  VAL E   7      16.368  57.923  12.037  1.00 14.37           C  
ATOM     42  C   VAL E   7      16.349  56.840  13.039  1.00 17.87           C  
ATOM     43  O   VAL E   7      15.789  57.026  14.128  1.00 20.62           O  
ATOM     44  CB  VAL E   7      17.203  59.040  12.618  1.00 21.53           C  
ATOM     45  CG1 VAL E   7      18.659  58.560  12.770  1.00 26.89           C  
ATOM     46  CG2 VAL E   7      17.180  60.183  11.632  1.00 20.19           C  
ATOM     47  N   GLY E   8      17.030  55.730  12.787  1.00 17.99           N  
ATOM     48  CA  GLY E   8      17.022  54.650  13.815  1.00 13.74           C  
ATOM     49  C   GLY E   8      18.450  54.430  14.332  1.00 14.73           C  
ATOM     50  O   GLY E   8      19.373  55.217  14.029  1.00 16.91           O  
ATOM     51  N   VAL E   9      18.619  53.466  15.237  1.00 15.99           N  
ATOM     52  CA  VAL E   9      19.968  53.305  15.761  1.00 18.56           C  
ATOM     53  C   VAL E   9      20.277  51.814  15.823  1.00 15.38           C  
ATOM     54  O   VAL E   9      19.346  50.923  15.943  1.00 17.95           O  
ATOM     55  CB  VAL E   9      20.064  53.959  17.173  1.00 23.59           C  
ATOM     56  CG1 VAL E   9      18.994  53.338  18.042  1.00 28.86           C  
ATOM     57  CG2 VAL E   9      21.460  53.727  17.842  1.00 23.96           C  
ATOM     58  N   GLY E  10      21.538  51.521  15.652  1.00 16.29           N  
ATOM     59  CA  GLY E  10      21.911  50.118  15.706  1.00 15.32           C  
ATOM     60  C   GLY E  10      23.399  49.953  15.935  1.00 24.09           C  
ATOM     61  O   GLY E  10      24.134  50.914  16.135  1.00 21.19           O  
ATOM     62  N   ARG E  11      23.853  48.706  15.813  1.00 13.73           N  
ATOM     63  CA  ARG E  11      25.244  48.370  16.033  1.00 13.46           C  
ATOM     64  C   ARG E  11      25.713  47.674  14.811  1.00 20.13           C  
ATOM     65  O   ARG E  11      24.993  46.802  14.307  1.00 16.35           O  
ATOM     66  CB  ARG E  11      25.293  47.361  17.179  1.00 23.50           C  
ATOM     67  CG  ARG E  11      26.233  47.661  18.320  1.00 42.16           C  
ATOM     68  CD AARG E  11      26.429  46.452  19.223  0.50 27.46           C  
ATOM     69  CD BARG E  11      26.157  46.617  19.467  0.50 19.84           C  
ATOM     70  NE AARG E  11      25.517  46.674  20.321  0.50 37.87           N  
ATOM     71  NE BARG E  11      25.317  46.936  20.640  0.50 62.69           N  
ATOM     72  CZ AARG E  11      25.627  47.738  21.127  0.50 36.74           C  
ATOM     73  CZ BARG E  11      24.471  46.059  21.207  0.50 31.65           C  
ATOM     74  NH1AARG E  11      26.642  48.600  21.018  0.50 34.81           N  
ATOM     75  NH1BARG E  11      24.317  44.829  20.723  0.50 32.17           N  
ATOM     76  NH2AARG E  11      24.721  47.935  22.086  0.50 27.59           N  
ATOM     77  NH2BARG E  11      23.762  46.423  22.277  0.50 23.37           N  
ATOM     78  N   GLY E  12      26.921  47.972  14.405  1.00 11.55           N  
ATOM     79  CA  GLY E  12      27.576  47.429  13.202  1.00 17.35           C  
ATOM     80  C   GLY E  12      28.346  46.111  13.492  1.00 10.37           C  
ATOM     81  O   GLY E  12      28.388  45.596  14.656  1.00 15.42           O  
ATOM     82  N   VAL E  13      28.914  45.595  12.420  1.00 11.07           N  
ATOM     83  CA  VAL E  13      29.645  44.334  12.569  1.00 16.77           C  
ATOM     84  C   VAL E  13      30.752  44.373  13.621  1.00 13.56           C  
ATOM     85  O   VAL E  13      31.034  43.368  14.238  1.00 21.40           O  
ATOM     86  CB  VAL E  13      30.254  43.979  11.208  1.00 21.23           C  
ATOM     87  CG1 VAL E  13      31.178  42.753  11.203  1.00 18.74           C  
ATOM     88  CG2 VAL E  13      29.127  43.809  10.200  1.00 19.64           C  
ATOM     89  N   LEU E  14      31.460  45.477  13.695  1.00 20.10           N  
ATOM     90  CA  LEU E  14      32.514  45.619  14.638  1.00 17.25           C  
ATOM     91  C   LEU E  14      31.948  46.002  15.954  1.00 42.66           C  
ATOM     92  O   LEU E  14      32.697  46.278  16.840  1.00 20.34           O  
ATOM     93  CB  LEU E  14      33.625  46.576  14.213  1.00 14.18           C  
ATOM     94  CG  LEU E  14      34.229  46.095  12.913  1.00 25.28           C  
ATOM     95  CD1 LEU E  14      35.395  46.962  12.628  1.00 30.93           C  
ATOM     96  CD2 LEU E  14      34.793  44.735  13.118  1.00 28.27           C  
ATOM     97  N   GLY E  15      30.643  46.009  16.148  1.00 24.54           N  
ATOM     98  CA  GLY E  15      30.212  46.318  17.517  1.00 18.90           C  
ATOM     99  C   GLY E  15      29.932  47.801  17.867  1.00 18.97           C  
ATOM    100  O   GLY E  15      29.596  48.161  19.001  1.00 24.85           O  
ATOM    101  N   ASP E  16      30.205  48.679  16.943  1.00 16.71           N  
ATOM    102  CA  ASP E  16      30.019  50.132  17.129  1.00 20.70           C  
ATOM    103  C   ASP E  16      28.551  50.553  16.846  1.00 23.83           C  
ATOM    104  O   ASP E  16      27.846  50.027  15.997  1.00 23.37           O  
ATOM    105  CB  ASP E  16      30.906  50.837  16.128  1.00 17.05           C  
ATOM    106  CG  ASP E  16      30.742  50.321  14.684  1.00 19.46           C  
ATOM    107  OD1 ASP E  16      30.684  49.097  14.353  1.00 28.50           O  
ATOM    108  OD2 ASP E  16      30.714  51.315  13.859  1.00 25.31           O  
ATOM    109  N   GLN E  17      28.112  51.494  17.618  1.00 17.14           N  
ATOM    110  CA  GLN E  17      26.779  52.040  17.507  1.00 13.64           C  
ATOM    111  C   GLN E  17      26.746  53.152  16.536  1.00 24.17           C  
ATOM    112  O   GLN E  17      27.633  53.999  16.514  1.00 24.69           O  
ATOM    113  CB  GLN E  17      26.331  52.476  18.917  1.00 17.73           C  
ATOM    114  CG  GLN E  17      24.882  52.941  18.893  1.00 26.08           C  
ATOM    115  CD  GLN E  17      24.386  53.403  20.242  1.00100.00           C  
ATOM    116  OE1 GLN E  17      24.225  52.596  21.148  1.00 43.16           O  
ATOM    117  NE2 GLN E  17      24.218  54.704  20.419  1.00 68.24           N  
ATOM    118  N   LYS E  18      25.728  53.201  15.688  1.00 17.25           N  
ATOM    119  CA  LYS E  18      25.625  54.331  14.772  1.00 24.00           C  
ATOM    120  C   LYS E  18      24.166  54.654  14.505  1.00 25.27           C  
ATOM    121  O   LYS E  18      23.363  53.758  14.693  1.00 17.44           O  
ATOM    122  CB  LYS E  18      26.348  54.141  13.458  1.00 23.59           C  
ATOM    123  CG  LYS E  18      25.909  52.945  12.711  1.00 22.74           C  
ATOM    124  CD  LYS E  18      27.099  51.991  12.554  1.00 23.88           C  
ATOM    125  CE  LYS E  18      28.165  52.388  11.595  1.00 31.66           C  
ATOM    126  NZ  LYS E  18      29.370  51.466  11.672  1.00 19.92           N  
ATOM    127  N   ASN E  19      23.809  55.853  13.978  1.00 15.92           N  
ATOM    128  CA  ASN E  19      22.420  56.193  13.605  1.00 11.75           C  
ATOM    129  C   ASN E  19      22.296  55.952  12.138  1.00 16.60           C  
ATOM    130  O   ASN E  19      23.265  56.147  11.420  1.00 18.67           O  
ATOM    131  CB  ASN E  19      22.233  57.730  13.838  1.00 17.60           C  
ATOM    132  CG  ASN E  19      22.222  58.095  15.343  1.00 26.17           C  
ATOM    133  OD1 ASN E  19      21.880  57.288  16.248  1.00 32.04           O  
ATOM    134  ND2 ASN E  19      22.516  59.338  15.598  1.00 57.84           N  
ATOM    135  N   ILE E  20      21.135  55.454  11.668  1.00 14.36           N  
ATOM    136  CA  ILE E  20      21.014  55.269  10.249  1.00 12.32           C  
ATOM    137  C   ILE E  20      19.652  55.887   9.871  1.00 14.21           C  
ATOM    138  O   ILE E  20      18.698  55.904  10.735  1.00 20.53           O  
ATOM    139  CB  ILE E  20      20.967  53.759   9.907  1.00 19.24           C  
ATOM    140  CG1 ILE E  20      20.137  53.166  11.001  1.00 17.05           C  
ATOM    141  CG2 ILE E  20      22.378  53.136  10.070  1.00 22.36           C  
ATOM    142  CD1 ILE E  20      20.229  51.651  11.109  1.00 31.47           C  
ATOM    143  N   ASN E  21      19.551  56.255   8.577  1.00 14.20           N  
ATOM    144  CA  ASN E  21      18.302  56.850   8.025  1.00 14.30           C  
ATOM    145  C   ASN E  21      17.355  55.751   7.567  1.00 21.96           C  
ATOM    146  O   ASN E  21      17.757  54.887   6.772  1.00 17.08           O  
ATOM    147  CB  ASN E  21      18.744  57.624   6.820  1.00 11.48           C  
ATOM    148  CG  ASN E  21      19.531  58.833   7.365  1.00 25.39           C  
ATOM    149  OD1 ASN E  21      20.551  59.164   6.888  1.00 31.28           O  
ATOM    150  ND2 ASN E  21      18.951  59.676   8.126  1.00 18.88           N  
ATOM    151  N   THR E  22      16.112  55.783   8.107  1.00 13.86           N  
ATOM    152  CA  THR E  22      15.108  54.779   7.815  1.00 15.62           C  
ATOM    153  C   THR E  22      13.832  55.454   7.324  1.00 28.21           C  
ATOM    154  O   THR E  22      13.778  56.665   7.252  1.00 15.08           O  
ATOM    155  CB  THR E  22      14.834  53.895   9.069  1.00 13.95           C  
ATOM    156  OG1 THR E  22      14.433  54.680  10.156  1.00 15.59           O  
ATOM    157  CG2 THR E  22      16.136  53.205   9.532  1.00 12.64           C  
ATOM    158  N   THR E  23      12.843  54.652   6.940  1.00 15.84           N  
ATOM    159  CA  THR E  23      11.560  55.139   6.466  1.00 14.08           C  
ATOM    160  C   THR E  23      10.536  54.403   7.189  1.00 18.20           C  
ATOM    161  O   THR E  23      10.595  53.178   7.335  1.00 19.32           O  
ATOM    162  CB  THR E  23      11.345  54.953   4.953  1.00 20.35           C  
ATOM    163  OG1 THR E  23      12.328  55.750   4.271  1.00 15.24           O  
ATOM    164  CG2 THR E  23       9.972  55.484   4.537  1.00 20.99           C  
ATOM    165  N   TYR E  24       9.529  55.130   7.594  1.00 15.96           N  
ATOM    166  CA  TYR E  24       8.473  54.468   8.353  1.00 14.45           C  
ATOM    167  C   TYR E  24       7.144  54.308   7.673  1.00 29.08           C  
ATOM    168  O   TYR E  24       6.560  55.305   7.237  1.00 18.94           O  
ATOM    169  CB  TYR E  24       8.268  55.156   9.724  1.00 11.77           C  
ATOM    170  CG  TYR E  24       7.116  54.601  10.496  1.00 24.30           C  
ATOM    171  CD1 TYR E  24       7.195  53.403  11.206  1.00 20.07           C  
ATOM    172  CD2 TYR E  24       5.983  55.365  10.712  1.00 36.69           C  
ATOM    173  CE1 TYR E  24       6.145  52.724  11.817  1.00 26.96           C  
ATOM    174  CE2 TYR E  24       4.964  54.794  11.481  1.00 42.36           C  
ATOM    175  CZ  TYR E  24       5.025  53.507  12.026  1.00 60.82           C  
ATOM    176  OH  TYR E  24       4.020  52.971  12.766  1.00 45.85           O  
ATOM    177  N   SER E  25       6.636  53.054   7.605  1.00 15.30           N  
ATOM    178  CA  SER E  25       5.346  52.842   7.001  1.00 15.61           C  
ATOM    179  C   SER E  25       4.848  51.499   7.499  1.00 26.03           C  
ATOM    180  O   SER E  25       5.138  50.480   6.839  1.00 23.60           O  
ATOM    181  CB  SER E  25       5.518  52.824   5.500  1.00 23.01           C  
ATOM    182  OG  SER E  25       4.191  52.998   4.996  1.00 40.54           O  
ATOM    183  N   THR E  26       4.281  51.447   8.707  1.00 19.98           N  
ATOM    184  CA  THR E  26       3.883  50.161   9.399  1.00 21.85           C  
ATOM    185  C   THR E  26       5.150  49.565  10.020  1.00 13.33           C  
ATOM    186  O   THR E  26       5.278  49.461  11.225  1.00 14.64           O  
ATOM    187  CB  THR E  26       3.144  49.133   8.519  1.00 20.71           C  
ATOM    188  OG1 THR E  26       2.001  49.743   7.973  1.00 27.48           O  
ATOM    189  CG2 THR E  26       2.667  47.987   9.353  1.00 26.93           C  
ATOM    190  N   TYR E  27       6.114  49.203   9.137  1.00 12.55           N  
ATOM    191  CA  TYR E  27       7.412  48.784   9.673  1.00 14.87           C  
ATOM    192  C   TYR E  27       8.387  49.990   9.463  1.00 13.35           C  
ATOM    193  O   TYR E  27       8.090  50.907   8.712  1.00 15.02           O  
ATOM    194  CB  TYR E  27       8.005  47.620   8.833  1.00 11.14           C  
ATOM    195  CG  TYR E  27       7.376  46.275   9.211  1.00 15.81           C  
ATOM    196  CD1 TYR E  27       7.782  45.602  10.364  1.00 18.59           C  
ATOM    197  CD2 TYR E  27       6.254  45.750   8.561  1.00 25.77           C  
ATOM    198  CE1 TYR E  27       7.271  44.354  10.740  1.00 16.90           C  
ATOM    199  CE2 TYR E  27       5.679  44.524   8.935  1.00 14.90           C  
ATOM    200  CZ  TYR E  27       6.178  43.837  10.044  1.00 20.44           C  
ATOM    201  OH  TYR E  27       5.652  42.632  10.491  1.00 21.64           O  
ATOM    202  N   TYR E  28       9.611  49.855  10.016  1.00 14.40           N  
ATOM    203  CA  TYR E  28      10.723  50.785   9.723  1.00 11.72           C  
ATOM    204  C   TYR E  28      11.564  50.058   8.713  1.00 17.95           C  
ATOM    205  O   TYR E  28      11.916  48.913   8.997  1.00 20.00           O  
ATOM    206  CB  TYR E  28      11.570  51.051  10.928  1.00 13.82           C  
ATOM    207  CG  TYR E  28      10.760  51.815  11.982  1.00 18.37           C  
ATOM    208  CD1 TYR E  28      10.654  53.205  11.897  1.00 18.79           C  
ATOM    209  CD2 TYR E  28      10.027  51.135  12.956  1.00 17.71           C  
ATOM    210  CE1 TYR E  28       9.922  53.913  12.862  1.00 18.79           C  
ATOM    211  CE2 TYR E  28       9.284  51.835  13.910  1.00 21.80           C  
ATOM    212  CZ  TYR E  28       9.170  53.223  13.815  1.00 27.99           C  
ATOM    213  OH  TYR E  28       8.495  53.919  14.801  1.00 26.86           O  
ATOM    214  N   TYR E  29      11.851  50.670   7.588  1.00 10.19           N  
ATOM    215  CA  TYR E  29      12.625  50.012   6.531  1.00 16.28           C  
ATOM    216  C   TYR E  29      14.019  50.650   6.403  1.00 27.63           C  
ATOM    217  O   TYR E  29      14.198  51.864   6.611  1.00 11.93           O  
ATOM    218  CB  TYR E  29      11.901  50.161   5.123  1.00 14.43           C  
ATOM    219  CG  TYR E  29      10.571  49.451   5.050  1.00 20.16           C  
ATOM    220  CD1 TYR E  29      10.616  48.090   4.713  1.00 22.70           C  
ATOM    221  CD2 TYR E  29       9.352  50.062   5.369  1.00 19.07           C  
ATOM    222  CE1 TYR E  29       9.506  47.236   4.654  1.00 24.84           C  
ATOM    223  CE2 TYR E  29       8.244  49.208   5.321  1.00 23.27           C  
ATOM    224  CZ  TYR E  29       8.287  47.855   4.939  1.00 37.84           C  
ATOM    225  OH  TYR E  29       7.122  47.084   4.924  1.00 35.52           O  
ATOM    226  N   LEU E  30      15.004  49.880   5.941  1.00 14.10           N  
ATOM    227  CA  LEU E  30      16.332  50.463   5.616  1.00 15.84           C  
ATOM    228  C   LEU E  30      16.252  51.092   4.224  1.00 13.53           C  
ATOM    229  O   LEU E  30      16.639  50.540   3.180  1.00 13.07           O  
ATOM    230  CB  LEU E  30      17.436  49.364   5.669  1.00  7.34           C  
ATOM    231  CG  LEU E  30      17.617  48.850   7.082  1.00 10.00           C  
ATOM    232  CD1 LEU E  30      18.817  47.823   7.026  1.00 11.32           C  
ATOM    233  CD2 LEU E  30      18.102  50.002   7.983  1.00 13.40           C  
ATOM    234  N   GLN E  31      15.666  52.336   4.198  1.00 10.41           N  
ATOM    235  CA  GLN E  31      15.500  53.098   3.010  1.00 10.54           C  
ATOM    236  C   GLN E  31      15.865  54.556   3.445  1.00 20.19           C  
ATOM    237  O   GLN E  31      15.224  55.102   4.344  1.00 14.32           O  
ATOM    238  CB  GLN E  31      14.035  53.065   2.536  1.00 13.12           C  
ATOM    239  CG  GLN E  31      13.831  53.908   1.263  1.00 14.06           C  
ATOM    240  CD  GLN E  31      12.375  53.927   0.884  1.00 24.45           C  
ATOM    241  OE1 GLN E  31      11.805  55.005   0.558  1.00 23.28           O  
ATOM    242  NE2 GLN E  31      11.887  52.718   0.752  1.00 13.07           N  
ATOM    243  N   ASP E  32      16.935  55.153   2.898  1.00 14.67           N  
ATOM    244  CA  ASP E  32      17.401  56.486   3.252  1.00 11.17           C  
ATOM    245  C   ASP E  32      16.994  57.380   2.152  1.00  9.99           C  
ATOM    246  O   ASP E  32      17.418  57.249   0.982  1.00 14.42           O  
ATOM    247  CB  ASP E  32      18.927  56.414   3.367  1.00 11.19           C  
ATOM    248  CG  ASP E  32      19.667  57.680   3.667  1.00 25.22           C  
ATOM    249  OD1 ASP E  32      18.946  58.740   3.692  1.00 15.09           O  
ATOM    250  OD2 ASP E  32      20.875  57.721   3.677  1.00 16.04           O  
ATOM    251  N   ASN E  33      15.981  58.275   2.551  1.00 12.42           N  
ATOM    252  CA  ASN E  33      15.496  59.148   1.490  1.00 13.14           C  
ATOM    253  C   ASN E  33      16.306  60.421   1.394  1.00 27.19           C  
ATOM    254  O   ASN E  33      16.046  61.240   0.537  1.00 23.35           O  
ATOM    255  CB  ASN E  33      14.049  59.595   1.752  1.00 16.41           C  
ATOM    256  CG  ASN E  33      13.146  58.391   1.833  1.00 17.05           C  
ATOM    257  OD1 ASN E  33      12.535  58.130   2.913  1.00 27.47           O  
ATOM    258  ND2 ASN E  33      13.251  57.561   0.809  1.00 14.95           N  
ATOM    259  N   THR E  34      17.287  60.588   2.285  1.00 18.00           N  
ATOM    260  CA  THR E  34      18.071  61.854   2.274  1.00 17.90           C  
ATOM    261  C   THR E  34      19.135  61.958   1.226  1.00 22.84           C  
ATOM    262  O   THR E  34      19.721  63.011   1.047  1.00 20.72           O  
ATOM    263  CB  THR E  34      18.670  62.167   3.594  1.00 13.87           C  
ATOM    264  OG1 THR E  34      19.752  61.273   3.836  1.00 21.13           O  
ATOM    265  CG2 THR E  34      17.636  61.902   4.660  1.00 16.13           C  
ATOM    266  N   ARG E  35      19.422  60.870   0.538  1.00 21.09           N  
ATOM    267  CA  ARG E  35      20.494  60.922  -0.453  1.00 13.76           C  
ATOM    268  C   ARG E  35      20.095  60.519  -1.822  1.00 15.16           C  
ATOM    269  O   ARG E  35      19.812  59.330  -2.069  1.00 21.13           O  
ATOM    270  CB  ARG E  35      21.696  60.071  -0.041  1.00 17.54           C  
ATOM    271  CG  ARG E  35      22.331  60.500   1.295  1.00 16.22           C  
ATOM    272  CD  ARG E  35      23.283  59.458   1.853  1.00 14.53           C  
ATOM    273  NE  ARG E  35      24.200  60.071   2.818  1.00 13.78           N  
ATOM    274  CZ  ARG E  35      24.040  59.830   4.104  1.00 23.15           C  
ATOM    275  NH1 ARG E  35      23.064  59.021   4.541  1.00 24.09           N  
ATOM    276  NH2 ARG E  35      24.886  60.368   4.986  1.00 20.51           N  
ATOM    277  N   GLY E  36      20.142  61.464  -2.792  1.00 17.77           N  
ATOM    278  CA  GLY E  36      19.761  61.198  -4.207  1.00 14.49           C  
ATOM    279  C   GLY E  36      18.372  60.532  -4.250  1.00 19.32           C  
ATOM    280  O   GLY E  36      17.490  60.909  -3.478  1.00 21.01           O  
ATOM    281  N   ASP E  37      18.193  59.592  -5.148  1.00 16.66           N  
ATOM    282  CA  ASP E  37      16.974  58.835  -5.223  1.00 16.05           C  
ATOM    283  C   ASP E  37      16.927  57.734  -4.148  1.00 23.43           C  
ATOM    284  O   ASP E  37      16.069  56.889  -4.227  1.00 19.56           O  
ATOM    285  CB  ASP E  37      16.780  58.202  -6.584  1.00 16.84           C  
ATOM    286  CG  ASP E  37      16.576  59.282  -7.609  1.00 43.82           C  
ATOM    287  OD1 ASP E  37      16.029  60.366  -7.148  1.00 41.28           O  
ATOM    288  OD2 ASP E  37      16.952  59.185  -8.743  1.00 42.42           O  
ATOM    289  N   GLY E  38      17.765  57.713  -3.123  1.00 15.34           N  
ATOM    290  CA  GLY E  38      17.579  56.733  -2.064  1.00 17.04           C  
ATOM    291  C   GLY E  38      18.696  55.684  -1.958  1.00 11.73           C  
ATOM    292  O   GLY E  38      19.310  55.344  -2.961  1.00 16.47           O  
ATOM    293  N   ILE E  39      18.912  55.229  -0.746  1.00 12.17           N  
ATOM    294  CA  ILE E  39      19.801  54.117  -0.528  1.00 14.60           C  
ATOM    295  C   ILE E  39      18.901  53.053   0.115  1.00 14.37           C  
ATOM    296  O   ILE E  39      18.194  53.316   1.072  1.00 13.45           O  
ATOM    297  CB  ILE E  39      20.958  54.491   0.387  1.00 14.05           C  
ATOM    298  CG1 ILE E  39      21.783  55.504  -0.421  1.00 16.77           C  
ATOM    299  CG2 ILE E  39      21.794  53.332   0.907  1.00 11.83           C  
ATOM    300  CD1 ILE E  39      22.765  56.212   0.434  1.00 19.10           C  
ATOM    301  N   PHE E  40      18.908  51.839  -0.406  1.00 16.43           N  
ATOM    302  CA  PHE E  40      18.028  50.761   0.039  1.00 10.86           C  
ATOM    303  C   PHE E  40      18.843  49.480   0.362  1.00 13.94           C  
ATOM    304  O   PHE E  40      19.633  49.065  -0.512  1.00 13.49           O  
ATOM    305  CB  PHE E  40      17.188  50.357  -1.251  1.00 10.17           C  
ATOM    306  CG  PHE E  40      16.327  51.486  -1.801  1.00 18.01           C  
ATOM    307  CD1 PHE E  40      16.857  52.453  -2.673  1.00 18.23           C  
ATOM    308  CD2 PHE E  40      15.002  51.613  -1.355  1.00 21.38           C  
ATOM    309  CE1 PHE E  40      16.078  53.537  -3.087  1.00 21.54           C  
ATOM    310  CE2 PHE E  40      14.194  52.687  -1.750  1.00 20.58           C  
ATOM    311  CZ  PHE E  40      14.745  53.595  -2.653  1.00 17.14           C  
ATOM    312  N   THR E  41      18.580  48.869   1.525  1.00 10.74           N  
ATOM    313  CA  THR E  41      19.315  47.671   1.847  1.00 12.08           C  
ATOM    314  C   THR E  41      18.305  46.534   1.970  1.00 13.03           C  
ATOM    315  O   THR E  41      17.214  46.730   2.566  1.00 14.09           O  
ATOM    316  CB  THR E  41      20.046  47.945   3.182  1.00 15.18           C  
ATOM    317  OG1 THR E  41      20.902  49.032   2.888  1.00 13.09           O  
ATOM    318  CG2 THR E  41      20.959  46.791   3.691  1.00 11.12           C  
ATOM    319  N   TYR E  42      18.718  45.375   1.448  1.00 10.96           N  
ATOM    320  CA  TYR E  42      17.867  44.168   1.376  1.00 11.15           C  
ATOM    321  C   TYR E  42      18.456  42.982   2.111  1.00 14.05           C  
ATOM    322  O   TYR E  42      19.665  42.878   2.295  1.00 12.18           O  
ATOM    323  CB  TYR E  42      17.765  43.765  -0.102  1.00 11.07           C  
ATOM    324  CG  TYR E  42      17.096  44.783  -0.970  1.00 15.50           C  
ATOM    325  CD1 TYR E  42      17.758  45.958  -1.341  1.00 19.22           C  
ATOM    326  CD2 TYR E  42      15.745  44.562  -1.287  1.00 11.83           C  
ATOM    327  CE1 TYR E  42      17.143  46.859  -2.199  1.00 13.15           C  
ATOM    328  CE2 TYR E  42      15.089  45.481  -2.096  1.00 13.39           C  
ATOM    329  CZ  TYR E  42      15.785  46.638  -2.481  1.00 27.04           C  
ATOM    330  OH  TYR E  42      15.162  47.521  -3.311  1.00 21.38           O  
ATOM    331  N   ASP E  43      17.574  42.104   2.509  1.00 12.05           N  
ATOM    332  CA  ASP E  43      17.979  40.866   3.183  1.00 15.02           C  
ATOM    333  C   ASP E  43      17.918  39.778   2.116  1.00 18.40           C  
ATOM    334  O   ASP E  43      16.800  39.539   1.614  1.00 12.21           O  
ATOM    335  CB  ASP E  43      16.978  40.501   4.320  1.00 15.69           C  
ATOM    336  CG  ASP E  43      17.377  39.301   5.141  1.00 15.51           C  
ATOM    337  OD1 ASP E  43      18.418  38.718   4.944  1.00 18.94           O  
ATOM    338  OD2 ASP E  43      16.524  39.009   6.070  1.00 16.15           O  
ATOM    339  N   ALA E  44      19.063  39.081   1.790  1.00 12.46           N  
ATOM    340  CA  ALA E  44      19.021  37.992   0.826  1.00 11.97           C  
ATOM    341  C   ALA E  44      18.720  36.627   1.519  1.00  8.13           C  
ATOM    342  O   ALA E  44      18.614  35.580   0.857  1.00 16.47           O  
ATOM    343  CB  ALA E  44      20.258  37.899  -0.029  1.00 12.72           C  
ATOM    344  N   LYS E  45      18.643  36.625   2.899  1.00 10.05           N  
ATOM    345  CA  LYS E  45      18.188  35.476   3.750  1.00 12.61           C  
ATOM    346  C   LYS E  45      18.937  34.196   3.465  1.00 25.56           C  
ATOM    347  O   LYS E  45      18.311  33.112   3.488  1.00 15.18           O  
ATOM    348  CB  LYS E  45      16.636  35.126   3.555  1.00 11.46           C  
ATOM    349  CG  LYS E  45      15.805  36.268   3.078  1.00 31.01           C  
ATOM    350  CD  LYS E  45      14.309  36.013   2.979  1.00 24.97           C  
ATOM    351  CE  LYS E  45      13.566  37.110   3.665  1.00 39.61           C  
ATOM    352  NZ  LYS E  45      12.219  37.314   3.112  1.00 22.81           N  
ATOM    353  N   TYR E  46      20.249  34.342   3.228  1.00 14.24           N  
ATOM    354  CA  TYR E  46      21.138  33.180   2.983  1.00  8.34           C  
ATOM    355  C   TYR E  46      20.878  32.574   1.677  1.00 14.38           C  
ATOM    356  O   TYR E  46      21.400  31.499   1.447  1.00 19.85           O  
ATOM    357  CB  TYR E  46      21.128  32.105   4.027  1.00  8.88           C  
ATOM    358  CG  TYR E  46      21.277  32.617   5.443  1.00 11.29           C  
ATOM    359  CD1 TYR E  46      22.335  33.474   5.735  1.00 17.62           C  
ATOM    360  CD2 TYR E  46      20.477  32.197   6.501  1.00 17.21           C  
ATOM    361  CE1 TYR E  46      22.570  33.880   7.042  1.00 20.61           C  
ATOM    362  CE2 TYR E  46      20.608  32.641   7.813  1.00 17.27           C  
ATOM    363  CZ  TYR E  46      21.704  33.456   8.048  1.00 16.23           C  
ATOM    364  OH  TYR E  46      21.857  33.808   9.333  1.00 21.28           O  
ATOM    365  N   ARG E  47      20.178  33.224   0.787  1.00 10.76           N  
ATOM    366  CA  ARG E  47      19.970  32.648  -0.506  1.00 11.10           C  
ATOM    367  C   ARG E  47      20.761  33.407  -1.541  1.00 11.86           C  
ATOM    368  O   ARG E  47      21.421  34.359  -1.152  1.00 13.10           O  
ATOM    369  CB  ARG E  47      18.431  32.602  -0.867  1.00 16.22           C  
ATOM    370  CG  ARG E  47      17.788  31.602   0.166  1.00 25.30           C  
ATOM    371  CD  ARG E  47      16.389  30.984   0.012  1.00 55.25           C  
ATOM    372  NE  ARG E  47      16.287  30.117  -1.158  1.00 41.78           N  
ATOM    373  CZ  ARG E  47      16.391  28.778  -1.257  1.00 49.12           C  
ATOM    374  NH1 ARG E  47      16.560  27.993  -0.176  1.00 35.32           N  
ATOM    375  NH2 ARG E  47      16.278  28.212  -2.461  1.00 27.08           N  
ATOM    376  N   THR E  48      20.687  32.989  -2.852  1.00 10.93           N  
ATOM    377  CA  THR E  48      21.426  33.664  -3.928  1.00 14.08           C  
ATOM    378  C   THR E  48      20.549  34.390  -4.872  1.00 15.94           C  
ATOM    379  O   THR E  48      20.989  34.960  -5.868  1.00 19.06           O  
ATOM    380  CB  THR E  48      22.361  32.740  -4.730  1.00 24.54           C  
ATOM    381  OG1 THR E  48      21.613  31.637  -5.160  1.00 24.20           O  
ATOM    382  CG2 THR E  48      23.382  32.164  -3.773  1.00 23.95           C  
ATOM    383  N   THR E  49      19.229  34.465  -4.556  1.00 16.03           N  
ATOM    384  CA  THR E  49      18.406  35.233  -5.470  1.00 18.49           C  
ATOM    385  C   THR E  49      18.432  36.682  -4.981  1.00 13.34           C  
ATOM    386  O   THR E  49      18.409  36.971  -3.770  1.00 19.48           O  
ATOM    387  CB  THR E  49      16.952  34.742  -5.586  1.00 31.34           C  
ATOM    388  OG1 THR E  49      16.612  34.516  -4.311  1.00 28.98           O  
ATOM    389  CG2 THR E  49      16.839  33.339  -6.104  1.00 28.62           C  
ATOM    390  N   LEU E  50      18.398  37.565  -5.939  1.00 10.41           N  
ATOM    391  CA  LEU E  50      18.557  38.942  -5.565  1.00 10.85           C  
ATOM    392  C   LEU E  50      17.494  39.808  -6.139  1.00 16.83           C  
ATOM    393  O   LEU E  50      16.906  39.519  -7.175  1.00 18.04           O  
ATOM    394  CB  LEU E  50      19.842  39.445  -6.197  1.00 17.27           C  
ATOM    395  CG  LEU E  50      21.139  38.928  -5.557  1.00 15.86           C  
ATOM    396  CD1 LEU E  50      22.293  39.261  -6.486  1.00 13.76           C  
ATOM    397  CD2 LEU E  50      21.362  39.392  -4.138  1.00 13.35           C  
ATOM    398  N   PRO E  51      17.250  40.942  -5.484  1.00 17.59           N  
ATOM    399  CA  PRO E  51      17.965  41.483  -4.322  1.00 16.48           C  
ATOM    400  C   PRO E  51      17.499  40.947  -3.017  1.00 14.02           C  
ATOM    401  O   PRO E  51      18.144  41.148  -1.965  1.00 13.47           O  
ATOM    402  CB  PRO E  51      17.531  42.975  -4.309  1.00 15.06           C  
ATOM    403  CG  PRO E  51      16.135  42.968  -4.937  1.00 30.81           C  
ATOM    404  CD  PRO E  51      16.226  41.885  -6.028  1.00 19.36           C  
ATOM    405  N   GLY E  52      16.338  40.241  -2.992  1.00 13.28           N  
ATOM    406  CA  GLY E  52      15.910  39.830  -1.661  1.00 12.31           C  
ATOM    407  C   GLY E  52      14.689  40.712  -1.172  1.00 11.54           C  
ATOM    408  O   GLY E  52      14.059  41.227  -2.037  1.00 17.44           O  
ATOM    409  N   SER E  53      14.407  40.857   0.127  1.00 12.22           N  
ATOM    410  CA  SER E  53      13.296  41.649   0.723  1.00 16.00           C  
ATOM    411  C   SER E  53      13.871  42.963   1.218  1.00 19.14           C  
ATOM    412  O   SER E  53      14.897  42.921   1.894  1.00 13.95           O  
ATOM    413  CB  SER E  53      12.771  40.918   2.020  1.00 14.53           C  
ATOM    414  OG  SER E  53      12.195  39.778   1.494  1.00 26.18           O  
ATOM    415  N   LEU E  54      13.215  44.086   0.978  1.00 13.43           N  
ATOM    416  CA  LEU E  54      13.706  45.317   1.499  1.00  9.92           C  
ATOM    417  C   LEU E  54      13.671  45.142   2.974  1.00 12.99           C  
ATOM    418  O   LEU E  54      12.723  44.647   3.607  1.00 14.38           O  
ATOM    419  CB  LEU E  54      12.815  46.492   1.018  1.00 11.43           C  
ATOM    420  CG  LEU E  54      13.261  47.853   1.533  1.00 13.86           C  
ATOM    421  CD1 LEU E  54      14.588  48.221   0.884  1.00 15.68           C  
ATOM    422  CD2 LEU E  54      12.141  48.855   1.131  1.00 17.10           C  
ATOM    423  N   TRP E  55      14.749  45.580   3.611  1.00 10.26           N  
ATOM    424  CA  TRP E  55      14.874  45.324   5.041  1.00  9.65           C  
ATOM    425  C   TRP E  55      13.791  46.013   5.926  1.00 13.44           C  
ATOM    426  O   TRP E  55      13.801  47.216   5.980  1.00 16.28           O  
ATOM    427  CB  TRP E  55      16.320  45.686   5.529  1.00  9.65           C  
ATOM    428  CG  TRP E  55      16.621  45.055   6.848  1.00  8.15           C  
ATOM    429  CD1 TRP E  55      16.124  45.386   8.069  1.00 10.44           C  
ATOM    430  CD2 TRP E  55      17.561  43.973   7.107  1.00 11.05           C  
ATOM    431  NE1 TRP E  55      16.663  44.609   9.071  1.00 11.88           N  
ATOM    432  CE2 TRP E  55      17.551  43.695   8.508  1.00 10.02           C  
ATOM    433  CE3 TRP E  55      18.354  43.266   6.234  1.00 12.83           C  
ATOM    434  CZ2 TRP E  55      18.347  42.669   9.083  1.00 14.98           C  
ATOM    435  CZ3 TRP E  55      19.146  42.235   6.771  1.00 12.05           C  
ATOM    436  CH2 TRP E  55      19.084  41.947   8.161  1.00 14.61           C  
ATOM    437  N   ALA E  56      13.064  45.256   6.765  1.00 14.39           N  
ATOM    438  CA  ALA E  56      12.013  45.777   7.587  1.00 15.74           C  
ATOM    439  C   ALA E  56      12.256  45.426   8.981  1.00 16.59           C  
ATOM    440  O   ALA E  56      12.668  44.295   9.295  1.00 14.41           O  
ATOM    441  CB  ALA E  56      10.614  45.214   7.143  1.00 18.48           C  
ATOM    442  N   ASP E  57      11.992  46.384   9.853  1.00 12.28           N  
ATOM    443  CA  ASP E  57      12.247  46.088  11.238  1.00 10.11           C  
ATOM    444  C   ASP E  57      11.083  46.631  12.025  1.00 21.19           C  
ATOM    445  O   ASP E  57      10.581  47.684  11.630  1.00 19.34           O  
ATOM    446  CB  ASP E  57      13.493  46.936  11.704  1.00  9.31           C  
ATOM    447  CG  ASP E  57      13.893  46.601  13.114  1.00 15.26           C  
ATOM    448  OD1 ASP E  57      14.607  45.618  13.419  1.00 16.35           O  
ATOM    449  OD2 ASP E  57      13.434  47.343  14.051  1.00 15.44           O  
ATOM    450  N   ALA E  58      10.751  46.049  13.171  1.00 12.69           N  
ATOM    451  CA  ALA E  58       9.621  46.544  13.884  1.00 20.26           C  
ATOM    452  C   ALA E  58       9.751  47.779  14.692  1.00 24.97           C  
ATOM    453  O   ALA E  58       8.779  48.484  14.864  1.00 17.69           O  
ATOM    454  CB  ALA E  58       8.857  45.477  14.675  1.00 17.15           C  
ATOM    455  N   ASP E  59      10.894  48.005  15.233  1.00 17.36           N  
ATOM    456  CA  ASP E  59      10.976  49.102  16.151  1.00 12.15           C  
ATOM    457  C   ASP E  59      12.070  50.171  15.931  1.00 15.01           C  
ATOM    458  O   ASP E  59      12.312  51.017  16.797  1.00 16.88           O  
ATOM    459  CB  ASP E  59      11.120  48.456  17.544  1.00 15.09           C  
ATOM    460  CG  ASP E  59      12.403  47.624  17.593  1.00 24.35           C  
ATOM    461  OD1 ASP E  59      13.158  47.465  16.636  1.00 18.91           O  
ATOM    462  OD2 ASP E  59      12.631  47.076  18.737  1.00 22.89           O  
ATOM    463  N   ASN E  60      12.654  50.192  14.741  1.00 18.42           N  
ATOM    464  CA  ASN E  60      13.646  51.194  14.465  1.00 17.22           C  
ATOM    465  C   ASN E  60      14.920  51.019  15.276  1.00 18.30           C  
ATOM    466  O   ASN E  60      15.754  51.909  15.334  1.00 18.56           O  
ATOM    467  CB  ASN E  60      13.097  52.613  14.658  1.00 17.81           C  
ATOM    468  CG  ASN E  60      13.647  53.517  13.573  1.00 24.93           C  
ATOM    469  OD1 ASN E  60      14.118  53.123  12.468  1.00 19.61           O  
ATOM    470  ND2 ASN E  60      13.501  54.817  13.801  1.00 20.62           N  
ATOM    471  N   GLN E  61      15.160  49.877  15.904  1.00 15.53           N  
ATOM    472  CA  GLN E  61      16.387  49.651  16.655  1.00 16.23           C  
ATOM    473  C   GLN E  61      17.047  48.415  16.045  1.00 25.33           C  
ATOM    474  O   GLN E  61      16.378  47.361  15.896  1.00 15.38           O  
ATOM    475  CB  GLN E  61      16.042  49.325  18.121  1.00 13.65           C  
ATOM    476  CG  GLN E  61      15.421  50.606  18.670  1.00 30.98           C  
ATOM    477  CD  GLN E  61      15.638  50.827  20.141  1.00 77.64           C  
ATOM    478  OE1 GLN E  61      16.716  51.252  20.594  1.00 87.63           O  
ATOM    479  NE2 GLN E  61      14.571  50.550  20.881  1.00 70.48           N  
ATOM    480  N   PHE E  62      18.316  48.487  15.715  1.00 14.97           N  
ATOM    481  CA  PHE E  62      18.940  47.332  15.080  1.00 15.00           C  
ATOM    482  C   PHE E  62      20.121  46.780  15.819  1.00 22.67           C  
ATOM    483  O   PHE E  62      21.248  46.906  15.371  1.00 14.83           O  
ATOM    484  CB  PHE E  62      19.366  47.826  13.702  1.00 14.10           C  
ATOM    485  CG  PHE E  62      18.220  48.401  12.866  1.00 17.26           C  
ATOM    486  CD1 PHE E  62      17.632  49.660  13.033  1.00 18.63           C  
ATOM    487  CD2 PHE E  62      17.722  47.636  11.802  1.00 19.59           C  
ATOM    488  CE1 PHE E  62      16.559  50.059  12.210  1.00 16.60           C  
ATOM    489  CE2 PHE E  62      16.644  48.034  11.004  1.00 16.35           C  
ATOM    490  CZ  PHE E  62      16.043  49.276  11.179  1.00 15.21           C  
ATOM    491  N   PHE E  63      19.874  46.137  16.928  1.00 13.33           N  
ATOM    492  CA  PHE E  63      20.933  45.568  17.725  1.00 18.21           C  
ATOM    493  C   PHE E  63      21.035  44.047  17.703  1.00 25.93           C  
ATOM    494  O   PHE E  63      21.797  43.479  18.448  1.00 21.15           O  
ATOM    495  CB  PHE E  63      20.733  46.069  19.154  1.00 18.79           C  
ATOM    496  CG  PHE E  63      21.024  47.575  19.340  1.00 20.61           C  
ATOM    497  CD1 PHE E  63      22.300  48.124  19.418  1.00 24.77           C  
ATOM    498  CD2 PHE E  63      20.002  48.522  19.391  1.00 34.98           C  
ATOM    499  CE1 PHE E  63      22.477  49.499  19.579  1.00 23.89           C  
ATOM    500  CE2 PHE E  63      20.151  49.906  19.568  1.00 27.50           C  
ATOM    501  CZ  PHE E  63      21.431  50.409  19.702  1.00 22.96           C  
ATOM    502  N   ALA E  64      20.265  43.376  16.888  1.00 19.84           N  
ATOM    503  CA  ALA E  64      20.361  41.933  16.797  1.00 17.32           C  
ATOM    504  C   ALA E  64      21.594  41.628  15.964  1.00 21.78           C  
ATOM    505  O   ALA E  64      21.990  42.324  14.991  1.00 15.25           O  
ATOM    506  CB  ALA E  64      19.203  41.381  16.008  1.00 17.46           C  
ATOM    507  N   SER E  65      22.157  40.478  16.262  1.00 16.57           N  
ATOM    508  CA  SER E  65      23.313  40.158  15.489  1.00 20.31           C  
ATOM    509  C   SER E  65      23.019  39.966  14.025  1.00 14.13           C  
ATOM    510  O   SER E  65      23.860  40.335  13.185  1.00 13.97           O  
ATOM    511  CB  SER E  65      24.289  39.174  16.148  1.00 32.79           C  
ATOM    512  OG  SER E  65      23.667  37.962  16.040  1.00 34.40           O  
ATOM    513  N   TYR E  66      21.842  39.466  13.676  1.00 12.90           N  
ATOM    514  CA  TYR E  66      21.587  39.340  12.256  1.00  8.58           C  
ATOM    515  C   TYR E  66      21.494  40.729  11.541  1.00  8.83           C  
ATOM    516  O   TYR E  66      21.588  40.819  10.323  1.00 12.25           O  
ATOM    517  CB  TYR E  66      20.209  38.627  12.245  1.00 10.59           C  
ATOM    518  CG  TYR E  66      19.796  38.259  10.869  1.00 20.45           C  
ATOM    519  CD1 TYR E  66      20.261  37.097  10.280  1.00 19.24           C  
ATOM    520  CD2 TYR E  66      18.824  38.926  10.141  1.00 19.90           C  
ATOM    521  CE1 TYR E  66      19.864  36.629   9.029  1.00 11.91           C  
ATOM    522  CE2 TYR E  66      18.472  38.533   8.850  1.00 14.45           C  
ATOM    523  CZ  TYR E  66      18.963  37.367   8.284  1.00 19.13           C  
ATOM    524  OH  TYR E  66      18.655  37.003   7.023  1.00 21.59           O  
ATOM    525  N   ASP E  67      21.257  41.788  12.346  1.00 11.57           N  
ATOM    526  CA  ASP E  67      21.077  43.169  11.816  1.00 13.91           C  
ATOM    527  C   ASP E  67      22.400  43.845  11.430  1.00 13.67           C  
ATOM    528  O   ASP E  67      22.428  44.718  10.569  1.00 14.18           O  
ATOM    529  CB  ASP E  67      20.520  44.124  12.914  1.00 11.12           C  
ATOM    530  CG  ASP E  67      19.074  43.771  13.303  1.00 18.32           C  
ATOM    531  OD1 ASP E  67      18.359  43.072  12.584  1.00 19.13           O  
ATOM    532  OD2 ASP E  67      18.719  44.112  14.515  1.00 17.34           O  
ATOM    533  N   ALA E  68      23.511  43.378  12.074  1.00 14.80           N  
ATOM    534  CA  ALA E  68      24.859  44.057  11.955  1.00 11.96           C  
ATOM    535  C   ALA E  68      25.318  44.435  10.545  1.00 11.32           C  
ATOM    536  O   ALA E  68      25.616  45.581  10.135  1.00 12.52           O  
ATOM    537  CB  ALA E  68      25.891  43.357  12.877  1.00 12.51           C  
ATOM    538  N   PRO E  69      25.333  43.441   9.676  1.00 13.40           N  
ATOM    539  CA  PRO E  69      25.792  43.658   8.322  1.00 10.87           C  
ATOM    540  C   PRO E  69      24.898  44.611   7.616  1.00 15.34           C  
ATOM    541  O   PRO E  69      25.368  45.259   6.725  1.00 12.26           O  
ATOM    542  CB  PRO E  69      25.728  42.309   7.590  1.00 14.40           C  
ATOM    543  CG  PRO E  69      25.524  41.281   8.704  1.00 17.79           C  
ATOM    544  CD  PRO E  69      24.973  42.017   9.927  1.00 17.75           C  
ATOM    545  N   ALA E  70      23.580  44.605   7.936  1.00 11.85           N  
ATOM    546  CA  ALA E  70      22.708  45.503   7.182  1.00 10.20           C  
ATOM    547  C   ALA E  70      22.933  46.956   7.624  1.00  7.27           C  
ATOM    548  O   ALA E  70      22.963  47.889   6.867  1.00 11.06           O  
ATOM    549  CB  ALA E  70      21.239  45.122   7.464  1.00 13.35           C  
ATOM    550  N   VAL E  71      23.090  47.074   8.898  1.00 10.21           N  
ATOM    551  CA  VAL E  71      23.369  48.424   9.399  1.00  9.97           C  
ATOM    552  C   VAL E  71      24.640  49.022   8.767  1.00 18.76           C  
ATOM    553  O   VAL E  71      24.640  50.192   8.310  1.00 13.21           O  
ATOM    554  CB  VAL E  71      23.558  48.352  10.931  1.00 12.31           C  
ATOM    555  CG1 VAL E  71      24.264  49.628  11.521  1.00 17.52           C  
ATOM    556  CG2 VAL E  71      22.340  47.921  11.783  1.00 10.34           C  
ATOM    557  N   ASP E  72      25.749  48.245   8.693  1.00 12.94           N  
ATOM    558  CA  ASP E  72      26.958  48.833   8.097  1.00 10.70           C  
ATOM    559  C   ASP E  72      26.889  48.950   6.601  1.00 10.65           C  
ATOM    560  O   ASP E  72      27.384  49.923   6.029  1.00 14.73           O  
ATOM    561  CB  ASP E  72      28.209  47.961   8.444  1.00 11.53           C  
ATOM    562  CG  ASP E  72      28.713  48.027   9.874  1.00 14.50           C  
ATOM    563  OD1 ASP E  72      28.450  49.146  10.452  1.00 17.41           O  
ATOM    564  OD2 ASP E  72      29.374  47.185  10.410  1.00 19.31           O  
ATOM    565  N   ALA E  73      26.215  48.032   5.898  1.00  7.51           N  
ATOM    566  CA  ALA E  73      26.161  48.241   4.418  1.00  5.74           C  
ATOM    567  C   ALA E  73      25.382  49.552   4.161  1.00 12.16           C  
ATOM    568  O   ALA E  73      25.690  50.292   3.209  1.00 12.12           O  
ATOM    569  CB  ALA E  73      25.370  47.072   3.794  1.00 12.34           C  
ATOM    570  N   HIS E  74      24.276  49.777   4.974  1.00 13.14           N  
ATOM    571  CA  HIS E  74      23.392  50.947   4.739  1.00  7.99           C  
ATOM    572  C   HIS E  74      24.148  52.238   5.068  1.00  7.63           C  
ATOM    573  O   HIS E  74      24.158  53.192   4.253  1.00 13.96           O  
ATOM    574  CB  HIS E  74      22.146  50.760   5.673  1.00  9.28           C  
ATOM    575  CG  HIS E  74      20.966  51.677   5.305  1.00 11.49           C  
ATOM    576  ND1 HIS E  74      20.338  51.620   4.082  1.00 11.80           N  
ATOM    577  CD2 HIS E  74      20.405  52.714   6.019  1.00  9.42           C  
ATOM    578  CE1 HIS E  74      19.316  52.541   4.099  1.00 13.20           C  
ATOM    579  NE2 HIS E  74      19.378  53.220   5.256  1.00 12.03           N  
ATOM    580  N   TYR E  75      24.785  52.246   6.258  1.00 11.83           N  
ATOM    581  CA  TYR E  75      25.560  53.442   6.690  1.00 15.19           C  
ATOM    582  C   TYR E  75      26.725  53.768   5.819  1.00 16.36           C  
ATOM    583  O   TYR E  75      26.911  54.905   5.403  1.00 15.12           O  
ATOM    584  CB  TYR E  75      26.012  53.167   8.091  1.00 12.40           C  
ATOM    585  CG  TYR E  75      26.607  54.387   8.645  1.00 18.98           C  
ATOM    586  CD1 TYR E  75      25.843  55.269   9.407  1.00 22.08           C  
ATOM    587  CD2 TYR E  75      27.996  54.455   8.606  1.00 18.91           C  
ATOM    588  CE1 TYR E  75      26.475  56.359   9.994  1.00 20.00           C  
ATOM    589  CE2 TYR E  75      28.628  55.536   9.203  1.00 19.37           C  
ATOM    590  CZ  TYR E  75      27.845  56.513   9.816  1.00 28.35           C  
ATOM    591  OH  TYR E  75      28.465  57.547  10.410  1.00 33.86           O  
ATOM    592  N   TYR E  76      27.508  52.710   5.444  1.00 10.17           N  
ATOM    593  CA  TYR E  76      28.730  52.971   4.630  1.00  9.99           C  
ATOM    594  C   TYR E  76      28.422  53.347   3.219  1.00 14.87           C  
ATOM    595  O   TYR E  76      29.153  54.071   2.542  1.00 15.55           O  
ATOM    596  CB  TYR E  76      29.778  51.826   4.738  1.00  9.36           C  
ATOM    597  CG  TYR E  76      30.365  51.674   6.127  1.00 12.10           C  
ATOM    598  CD1 TYR E  76      30.740  52.782   6.884  1.00 13.82           C  
ATOM    599  CD2 TYR E  76      30.718  50.401   6.572  1.00  9.31           C  
ATOM    600  CE1 TYR E  76      31.333  52.658   8.148  1.00 13.21           C  
ATOM    601  CE2 TYR E  76      31.243  50.262   7.861  1.00 10.73           C  
ATOM    602  CZ  TYR E  76      31.664  51.383   8.586  1.00 16.62           C  
ATOM    603  OH  TYR E  76      32.156  51.261   9.864  1.00 18.48           O  
ATOM    604  N   ALA E  77      27.276  52.879   2.740  1.00 10.25           N  
ATOM    605  CA  ALA E  77      26.906  53.324   1.407  1.00  8.70           C  
ATOM    606  C   ALA E  77      26.580  54.837   1.530  1.00 11.41           C  
ATOM    607  O   ALA E  77      26.935  55.525   0.588  1.00 14.84           O  
ATOM    608  CB  ALA E  77      25.712  52.570   0.923  1.00 11.48           C  
ATOM    609  N   GLY E  78      25.955  55.301   2.680  1.00 12.52           N  
ATOM    610  CA  GLY E  78      25.684  56.775   2.743  1.00 14.59           C  
ATOM    611  C   GLY E  78      27.020  57.580   2.752  1.00 19.58           C  
ATOM    612  O   GLY E  78      27.183  58.575   2.014  1.00 21.16           O  
ATOM    613  N   VAL E  79      27.934  57.126   3.609  1.00 12.58           N  
ATOM    614  CA  VAL E  79      29.250  57.767   3.679  1.00 15.52           C  
ATOM    615  C   VAL E  79      29.879  57.855   2.297  1.00 18.31           C  
ATOM    616  O   VAL E  79      30.406  58.890   1.917  1.00 15.79           O  
ATOM    617  CB  VAL E  79      30.198  57.096   4.698  1.00 19.69           C  
ATOM    618  CG1 VAL E  79      31.606  57.808   4.696  1.00 16.73           C  
ATOM    619  CG2 VAL E  79      29.524  57.049   6.076  1.00 16.90           C  
ATOM    620  N   THR E  80      29.932  56.766   1.562  1.00 12.30           N  
ATOM    621  CA  THR E  80      30.524  56.835   0.264  1.00  9.62           C  
ATOM    622  C   THR E  80      29.805  57.801  -0.649  1.00 20.93           C  
ATOM    623  O   THR E  80      30.416  58.417  -1.517  1.00 16.24           O  
ATOM    624  CB  THR E  80      30.538  55.419  -0.388  1.00 14.82           C  
ATOM    625  OG1 THR E  80      31.203  54.550   0.522  1.00 15.93           O  
ATOM    626  CG2 THR E  80      31.257  55.384  -1.717  1.00 12.28           C  
ATOM    627  N   TYR E  81      28.468  57.828  -0.566  1.00 15.12           N  
ATOM    628  CA  TYR E  81      27.704  58.757  -1.446  1.00 12.79           C  
ATOM    629  C   TYR E  81      28.131  60.198  -1.075  1.00  9.07           C  
ATOM    630  O   TYR E  81      28.402  61.026  -1.933  1.00 12.67           O  
ATOM    631  CB  TYR E  81      26.162  58.589  -1.132  1.00 12.59           C  
ATOM    632  CG  TYR E  81      25.309  59.664  -1.828  1.00 11.94           C  
ATOM    633  CD1 TYR E  81      25.145  60.919  -1.229  1.00 20.13           C  
ATOM    634  CD2 TYR E  81      24.721  59.422  -3.069  1.00 12.80           C  
ATOM    635  CE1 TYR E  81      24.433  61.900  -1.925  1.00 12.37           C  
ATOM    636  CE2 TYR E  81      23.924  60.359  -3.740  1.00 17.59           C  
ATOM    637  CZ  TYR E  81      23.764  61.591  -3.108  1.00 19.18           C  
ATOM    638  OH  TYR E  81      23.038  62.584  -3.711  1.00 20.02           O  
ATOM    639  N   ASP E  82      28.298  60.400   0.206  1.00 10.34           N  
ATOM    640  CA  ASP E  82      28.698  61.690   0.640  1.00 11.22           C  
ATOM    641  C   ASP E  82      30.050  62.036   0.134  1.00 20.24           C  
ATOM    642  O   ASP E  82      30.280  63.186  -0.219  1.00 21.56           O  
ATOM    643  CB  ASP E  82      28.644  61.844   2.207  1.00 10.48           C  
ATOM    644  CG  ASP E  82      27.241  61.782   2.764  1.00 11.63           C  
ATOM    645  OD1 ASP E  82      26.281  61.871   2.082  1.00 14.24           O  
ATOM    646  OD2 ASP E  82      27.197  61.765   4.035  1.00 13.51           O  
ATOM    647  N   TYR E  83      30.988  61.115   0.170  1.00 14.42           N  
ATOM    648  CA  TYR E  83      32.363  61.415  -0.296  1.00 13.16           C  
ATOM    649  C   TYR E  83      32.272  61.854  -1.716  1.00 17.46           C  
ATOM    650  O   TYR E  83      32.835  62.861  -2.127  1.00 21.17           O  
ATOM    651  CB  TYR E  83      33.235  60.062  -0.244  1.00 19.06           C  
ATOM    652  CG  TYR E  83      34.544  60.154  -1.009  1.00 12.04           C  
ATOM    653  CD1 TYR E  83      35.585  60.871  -0.419  1.00 17.36           C  
ATOM    654  CD2 TYR E  83      34.725  59.700  -2.310  1.00 10.82           C  
ATOM    655  CE1 TYR E  83      36.801  61.107  -1.068  1.00 15.84           C  
ATOM    656  CE2 TYR E  83      35.951  59.879  -2.971  1.00 15.74           C  
ATOM    657  CZ  TYR E  83      36.989  60.599  -2.357  1.00 18.35           C  
ATOM    658  OH  TYR E  83      38.199  60.783  -3.009  1.00 17.36           O  
ATOM    659  N   TYR E  84      31.570  61.112  -2.526  1.00 13.93           N  
ATOM    660  CA  TYR E  84      31.584  61.490  -3.938  1.00 10.99           C  
ATOM    661  C   TYR E  84      30.926  62.871  -4.265  1.00 12.07           C  
ATOM    662  O   TYR E  84      31.256  63.622  -5.238  1.00 14.10           O  
ATOM    663  CB  TYR E  84      30.950  60.433  -4.894  1.00 11.85           C  
ATOM    664  CG  TYR E  84      31.947  59.316  -5.191  1.00 19.48           C  
ATOM    665  CD1 TYR E  84      32.949  59.482  -6.139  1.00 18.67           C  
ATOM    666  CD2 TYR E  84      31.828  58.078  -4.595  1.00 14.91           C  
ATOM    667  CE1 TYR E  84      33.906  58.515  -6.446  1.00 14.15           C  
ATOM    668  CE2 TYR E  84      32.767  57.095  -4.901  1.00 12.92           C  
ATOM    669  CZ  TYR E  84      33.823  57.310  -5.790  1.00 25.53           C  
ATOM    670  OH  TYR E  84      34.800  56.358  -6.143  1.00 16.33           O  
ATOM    671  N   LYS E  85      29.956  63.145  -3.438  1.00 16.62           N  
ATOM    672  CA  LYS E  85      29.218  64.373  -3.722  1.00 18.86           C  
ATOM    673  C   LYS E  85      30.016  65.581  -3.237  1.00 17.18           C  
ATOM    674  O   LYS E  85      30.198  66.543  -3.970  1.00 24.51           O  
ATOM    675  CB  LYS E  85      27.931  64.340  -2.899  1.00 16.38           C  
ATOM    676  CG  LYS E  85      27.002  65.450  -3.279  1.00 35.41           C  
ATOM    677  CD  LYS E  85      25.960  65.651  -2.218  1.00 30.24           C  
ATOM    678  CE  LYS E  85      24.920  66.703  -2.533  1.00100.00           C  
ATOM    679  NZ  LYS E  85      24.473  67.401  -1.322  1.00100.00           N  
ATOM    680  N   ASN E  86      30.462  65.481  -1.980  1.00 14.74           N  
ATOM    681  CA  ASN E  86      31.188  66.574  -1.375  1.00 13.93           C  
ATOM    682  C   ASN E  86      32.520  66.859  -1.955  1.00 29.10           C  
ATOM    683  O   ASN E  86      32.970  67.990  -2.039  1.00 23.73           O  
ATOM    684  CB  ASN E  86      31.405  66.338   0.121  1.00 15.38           C  
ATOM    685  CG  ASN E  86      30.046  66.374   0.768  1.00 33.01           C  
ATOM    686  OD1 ASN E  86      29.196  67.123   0.317  1.00 31.30           O  
ATOM    687  ND2 ASN E  86      29.868  65.705   1.887  1.00 27.26           N  
ATOM    688  N   VAL E  87      33.229  65.807  -2.216  1.00 22.31           N  
ATOM    689  CA  VAL E  87      34.556  65.887  -2.720  1.00 18.54           C  
ATOM    690  C   VAL E  87      34.586  65.956  -4.252  1.00 17.22           C  
ATOM    691  O   VAL E  87      35.467  66.623  -4.816  1.00 26.27           O  
ATOM    692  CB  VAL E  87      35.495  64.752  -2.139  1.00 16.11           C  
ATOM    693  CG1 VAL E  87      36.914  64.797  -2.718  1.00 16.38           C  
ATOM    694  CG2 VAL E  87      35.517  64.777  -0.640  1.00 16.96           C  
ATOM    695  N   HIS E  88      33.771  65.276  -4.998  1.00 12.37           N  
ATOM    696  CA  HIS E  88      33.998  65.357  -6.435  1.00  7.64           C  
ATOM    697  C   HIS E  88      32.817  65.934  -7.177  1.00 10.15           C  
ATOM    698  O   HIS E  88      32.826  65.868  -8.424  1.00 17.72           O  
ATOM    699  CB  HIS E  88      34.306  63.903  -7.043  1.00 17.20           C  
ATOM    700  CG  HIS E  88      35.596  63.314  -6.462  1.00 25.75           C  
ATOM    701  ND1 HIS E  88      36.863  63.804  -6.838  1.00 20.99           N  
ATOM    702  CD2 HIS E  88      35.813  62.351  -5.504  1.00 17.08           C  
ATOM    703  CE1 HIS E  88      37.812  63.156  -6.112  1.00 24.27           C  
ATOM    704  NE2 HIS E  88      37.195  62.287  -5.260  1.00 19.89           N  
ATOM    705  N   ASN E  89      31.821  66.319  -6.380  1.00 16.28           N  
ATOM    706  CA  ASN E  89      30.671  66.871  -7.005  1.00 16.56           C  
ATOM    707  C   ASN E  89      29.975  65.913  -7.874  1.00 22.11           C  
ATOM    708  O   ASN E  89      29.421  66.291  -8.881  1.00 19.67           O  
ATOM    709  CB  ASN E  89      31.226  67.921  -7.956  1.00 25.67           C  
ATOM    710  CG  ASN E  89      30.659  69.183  -7.555  1.00100.00           C  
ATOM    711  OD1 ASN E  89      29.792  69.709  -8.292  1.00 76.36           O  
ATOM    712  ND2 ASN E  89      30.954  69.484  -6.277  1.00 43.77           N  
ATOM    713  N   ARG E  90      30.007  64.658  -7.529  1.00 20.49           N  
ATOM    714  CA  ARG E  90      29.341  63.646  -8.362  1.00 20.18           C  
ATOM    715  C   ARG E  90      28.083  63.141  -7.581  1.00 20.03           C  
ATOM    716  O   ARG E  90      28.193  62.879  -6.372  1.00 15.93           O  
ATOM    717  CB  ARG E  90      30.283  62.447  -8.535  1.00 15.93           C  
ATOM    718  CG  ARG E  90      29.740  61.488  -9.604  1.00 13.35           C  
ATOM    719  CD  ARG E  90      30.554  60.146  -9.747  1.00 10.76           C  
ATOM    720  NE  ARG E  90      29.948  59.368 -10.862  1.00 17.28           N  
ATOM    721  CZ  ARG E  90      30.046  59.672 -12.126  1.00 22.36           C  
ATOM    722  NH1 ARG E  90      30.848  60.687 -12.483  1.00 23.14           N  
ATOM    723  NH2 ARG E  90      29.421  58.906 -13.042  1.00 19.60           N  
ATOM    724  N   LEU E  91      26.882  63.116  -8.205  1.00 20.75           N  
ATOM    725  CA  LEU E  91      25.658  62.685  -7.520  1.00 14.27           C  
ATOM    726  C   LEU E  91      25.376  61.213  -7.871  1.00 12.10           C  
ATOM    727  O   LEU E  91      24.984  60.878  -9.041  1.00 16.03           O  
ATOM    728  CB  LEU E  91      24.530  63.525  -8.100  1.00 16.70           C  
ATOM    729  CG  LEU E  91      24.733  65.038  -7.909  1.00 24.93           C  
ATOM    730  CD1 LEU E  91      23.522  65.812  -8.445  1.00 22.75           C  
ATOM    731  CD2 LEU E  91      24.731  65.247  -6.421  1.00 26.16           C  
ATOM    732  N   SER E  92      25.702  60.388  -6.844  1.00 20.24           N  
ATOM    733  CA  SER E  92      25.616  58.915  -6.903  1.00 16.21           C  
ATOM    734  C   SER E  92      26.546  58.266  -7.964  1.00 20.14           C  
ATOM    735  O   SER E  92      27.283  58.947  -8.591  1.00 16.47           O  
ATOM    736  CB  SER E  92      24.186  58.523  -7.202  1.00 13.65           C  
ATOM    737  OG  SER E  92      24.033  57.114  -6.928  1.00 15.15           O  
ATOM    738  N   TYR E  93      26.439  56.972  -8.336  1.00 13.05           N  
ATOM    739  CA  TYR E  93      27.410  56.434  -9.260  1.00 12.01           C  
ATOM    740  C   TYR E  93      27.200  56.754 -10.652  1.00 19.87           C  
ATOM    741  O   TYR E  93      28.146  56.750 -11.426  1.00 20.61           O  
ATOM    742  CB  TYR E  93      27.445  54.942  -8.978  1.00 14.64           C  
ATOM    743  CG  TYR E  93      26.142  54.295  -9.232  1.00 14.10           C  
ATOM    744  CD1 TYR E  93      25.732  53.947 -10.516  1.00 12.92           C  
ATOM    745  CD2 TYR E  93      25.386  54.017  -8.098  1.00 17.68           C  
ATOM    746  CE1 TYR E  93      24.475  53.355 -10.631  1.00 19.46           C  
ATOM    747  CE2 TYR E  93      24.130  53.430  -8.183  1.00 22.22           C  
ATOM    748  CZ  TYR E  93      23.740  53.095  -9.471  1.00 19.07           C  
ATOM    749  OH  TYR E  93      22.557  52.487  -9.504  1.00 32.84           O  
ATOM    750  N   ASP E  94      25.998  57.149 -10.977  1.00 15.86           N  
ATOM    751  CA  ASP E  94      25.829  57.491 -12.377  1.00 14.85           C  
ATOM    752  C   ASP E  94      25.870  58.993 -12.655  1.00 18.23           C  
ATOM    753  O   ASP E  94      25.740  59.446 -13.787  1.00 20.18           O  
ATOM    754  CB  ASP E  94      24.481  56.951 -12.856  1.00 21.63           C  
ATOM    755  CG  ASP E  94      23.310  57.682 -12.234  1.00 16.04           C  
ATOM    756  OD1 ASP E  94      23.404  58.284 -11.066  1.00 18.04           O  
ATOM    757  OD2 ASP E  94      22.269  57.574 -12.781  1.00 24.80           O  
ATOM    758  N   GLY E  95      26.043  59.762 -11.654  1.00 15.52           N  
ATOM    759  CA  GLY E  95      26.107  61.210 -11.770  1.00 16.34           C  
ATOM    760  C   GLY E  95      24.726  61.850 -11.815  1.00 29.87           C  
ATOM    761  O   GLY E  95      24.555  63.059 -11.992  1.00 20.77           O  
ATOM    762  N   ASN E  96      23.732  61.041 -11.679  1.00 16.43           N  
ATOM    763  CA  ASN E  96      22.351  61.559 -11.775  1.00 15.27           C  
ATOM    764  C   ASN E  96      21.514  61.088 -10.656  1.00 25.58           C  
ATOM    765  O   ASN E  96      20.363  60.898 -10.816  1.00 22.95           O  
ATOM    766  CB  ASN E  96      21.707  61.266 -13.139  1.00 20.48           C  
ATOM    767  CG  ASN E  96      20.501  62.201 -13.366  1.00100.00           C  
ATOM    768  OD1 ASN E  96      20.284  63.324 -12.773  1.00 48.03           O  
ATOM    769  ND2 ASN E  96      19.587  61.641 -14.129  1.00 69.03           N  
ATOM    770  N   ASN E  97      22.144  60.862  -9.534  1.00 20.67           N  
ATOM    771  CA  ASN E  97      21.461  60.421  -8.350  1.00 13.96           C  
ATOM    772  C   ASN E  97      20.732  59.070  -8.368  1.00 21.38           C  
ATOM    773  O   ASN E  97      19.756  58.831  -7.609  1.00 18.23           O  
ATOM    774  CB  ASN E  97      20.509  61.519  -7.871  1.00 19.97           C  
ATOM    775  CG  ASN E  97      21.178  62.512  -6.975  1.00 27.74           C  
ATOM    776  OD1 ASN E  97      20.763  63.671  -6.871  1.00 28.19           O  
ATOM    777  ND2 ASN E  97      22.135  62.047  -6.206  1.00 14.91           N  
ATOM    778  N   ALA E  98      21.232  58.116  -9.141  1.00 17.98           N  
ATOM    779  CA  ALA E  98      20.667  56.721  -9.116  1.00 14.76           C  
ATOM    780  C   ALA E  98      20.573  56.109  -7.718  1.00 15.08           C  
ATOM    781  O   ALA E  98      21.410  56.288  -6.899  1.00 14.91           O  
ATOM    782  CB  ALA E  98      21.474  55.805 -10.011  1.00 18.41           C  
ATOM    783  N   ALA E  99      19.489  55.377  -7.400  1.00 12.09           N  
ATOM    784  CA  ALA E  99      19.350  54.745  -6.109  1.00 11.11           C  
ATOM    785  C   ALA E  99      20.466  53.667  -5.948  1.00  8.20           C  
ATOM    786  O   ALA E  99      20.901  52.975  -6.939  1.00 13.27           O  
ATOM    787  CB  ALA E  99      18.054  53.960  -6.097  1.00 13.96           C  
ATOM    788  N   ILE E 100      20.869  53.616  -4.741  1.00  9.40           N  
ATOM    789  CA  ILE E 100      21.946  52.658  -4.387  1.00 10.85           C  
ATOM    790  C   ILE E 100      21.333  51.489  -3.666  1.00 13.36           C  
ATOM    791  O   ILE E 100      20.669  51.663  -2.649  1.00 14.51           O  
ATOM    792  CB  ILE E 100      23.044  53.359  -3.577  1.00 14.90           C  
ATOM    793  CG1 ILE E 100      23.700  54.440  -4.491  1.00 16.26           C  
ATOM    794  CG2 ILE E 100      24.055  52.318  -3.084  1.00 16.88           C  
ATOM    795  CD1 ILE E 100      24.552  55.402  -3.648  1.00 17.72           C  
ATOM    796  N   ARG E 101      21.602  50.263  -4.191  1.00 11.55           N  
ATOM    797  CA  ARG E 101      21.040  49.132  -3.527  1.00 13.75           C  
ATOM    798  C   ARG E 101      22.099  48.126  -3.102  1.00 13.09           C  
ATOM    799  O   ARG E 101      22.973  47.929  -3.885  1.00 13.16           O  
ATOM    800  CB  ARG E 101      20.088  48.420  -4.534  1.00 16.88           C  
ATOM    801  CG  ARG E 101      18.821  49.209  -4.883  1.00 20.86           C  
ATOM    802  CD  ARG E 101      18.042  48.575  -6.027  1.00 26.47           C  
ATOM    803  NE  ARG E 101      17.356  49.636  -6.782  1.00 57.16           N  
ATOM    804  CZ  ARG E 101      16.269  50.249  -6.246  1.00100.00           C  
ATOM    805  NH1 ARG E 101      15.814  49.877  -5.055  1.00 45.96           N  
ATOM    806  NH2 ARG E 101      15.597  51.243  -6.866  1.00 50.99           N  
ATOM    807  N   SER E 102      21.889  47.504  -1.934  1.00 10.44           N  
ATOM    808  CA  SER E 102      22.810  46.479  -1.487  1.00  8.33           C  
ATOM    809  C   SER E 102      22.039  45.337  -0.904  1.00 22.24           C  
ATOM    810  O   SER E 102      21.050  45.600  -0.244  1.00 16.56           O  
ATOM    811  CB  SER E 102      23.660  46.994  -0.300  1.00 17.21           C  
ATOM    812  OG  SER E 102      24.265  48.264  -0.581  1.00 17.64           O  
ATOM    813  N   SER E 103      22.534  44.093  -0.994  1.00 10.46           N  
ATOM    814  CA  SER E 103      21.868  43.035  -0.264  1.00 12.05           C  
ATOM    815  C   SER E 103      22.902  42.402   0.656  1.00 17.71           C  
ATOM    816  O   SER E 103      24.057  42.321   0.218  1.00 14.99           O  
ATOM    817  CB  SER E 103      21.424  41.950  -1.246  1.00 13.62           C  
ATOM    818  OG  SER E 103      20.467  42.437  -2.159  1.00 15.20           O  
ATOM    819  N   VAL E 104      22.526  42.001   1.881  1.00 11.79           N  
ATOM    820  CA  VAL E 104      23.423  41.311   2.811  1.00 10.68           C  
ATOM    821  C   VAL E 104      22.901  39.899   3.065  1.00 13.15           C  
ATOM    822  O   VAL E 104      21.767  39.590   2.591  1.00 10.93           O  
ATOM    823  CB  VAL E 104      23.558  42.086   4.116  1.00 13.14           C  
ATOM    824  CG1 VAL E 104      24.169  43.402   3.726  1.00 10.81           C  
ATOM    825  CG2 VAL E 104      22.220  42.337   4.898  1.00 11.91           C  
ATOM    826  N   HIS E 105      23.700  39.041   3.795  1.00 11.88           N  
ATOM    827  CA  HIS E 105      23.394  37.642   4.084  1.00 14.30           C  
ATOM    828  C   HIS E 105      23.212  36.911   2.785  1.00 14.86           C  
ATOM    829  O   HIS E 105      22.313  36.111   2.648  1.00 13.99           O  
ATOM    830  CB  HIS E 105      22.137  37.468   4.896  1.00 13.28           C  
ATOM    831  CG  HIS E 105      22.263  38.075   6.247  1.00 13.15           C  
ATOM    832  ND1 HIS E 105      23.249  37.689   7.115  1.00 14.14           N  
ATOM    833  CD2 HIS E 105      21.503  39.020   6.912  1.00 15.36           C  
ATOM    834  CE1 HIS E 105      23.075  38.365   8.274  1.00 18.13           C  
ATOM    835  NE2 HIS E 105      22.012  39.192   8.190  1.00 18.38           N  
ATOM    836  N   TYR E 106      24.031  37.210   1.826  1.00 10.93           N  
ATOM    837  CA  TYR E 106      23.995  36.550   0.563  1.00  9.61           C  
ATOM    838  C   TYR E 106      24.652  35.190   0.679  1.00 17.80           C  
ATOM    839  O   TYR E 106      25.778  35.096   1.152  1.00 13.18           O  
ATOM    840  CB  TYR E 106      24.796  37.366  -0.406  1.00 14.72           C  
ATOM    841  CG  TYR E 106      24.921  36.683  -1.708  1.00 14.54           C  
ATOM    842  CD1 TYR E 106      23.915  36.766  -2.665  1.00 14.44           C  
ATOM    843  CD2 TYR E 106      26.094  36.039  -2.102  1.00 15.78           C  
ATOM    844  CE1 TYR E 106      23.990  36.184  -3.940  1.00 15.47           C  
ATOM    845  CE2 TYR E 106      26.204  35.494  -3.399  1.00 13.81           C  
ATOM    846  CZ  TYR E 106      25.167  35.530  -4.318  1.00 26.05           C  
ATOM    847  OH  TYR E 106      25.375  34.963  -5.558  1.00 26.36           O  
ATOM    848  N   SER E 107      23.888  34.146   0.329  1.00 17.64           N  
ATOM    849  CA  SER E 107      24.383  32.773   0.408  1.00 10.32           C  
ATOM    850  C   SER E 107      24.745  32.380   1.828  1.00 12.35           C  
ATOM    851  O   SER E 107      24.371  32.977   2.863  1.00 15.25           O  
ATOM    852  CB  SER E 107      25.616  32.626  -0.477  1.00 24.25           C  
ATOM    853  OG  SER E 107      25.790  31.241  -0.745  1.00 22.46           O  
ATOM    854  N   GLN E 108      25.550  31.276   1.892  1.00 11.28           N  
ATOM    855  CA  GLN E 108      25.996  30.777   3.227  1.00 12.85           C  
ATOM    856  C   GLN E 108      27.520  30.647   3.202  1.00 16.34           C  
ATOM    857  O   GLN E 108      28.096  30.029   2.289  1.00 21.65           O  
ATOM    858  CB  GLN E 108      25.533  29.314   3.493  1.00 16.55           C  
ATOM    859  CG  GLN E 108      24.012  29.243   3.589  1.00 21.26           C  
ATOM    860  CD  GLN E 108      23.480  27.924   4.106  1.00 43.19           C  
ATOM    861  OE1 GLN E 108      24.250  27.205   4.711  1.00 39.69           O  
ATOM    862  NE2 GLN E 108      22.211  27.556   3.792  1.00 21.88           N  
ATOM    863  N   GLY E 109      28.136  31.228   4.200  1.00 21.25           N  
ATOM    864  CA  GLY E 109      29.613  31.274   4.338  1.00 26.99           C  
ATOM    865  C   GLY E 109      30.320  31.867   3.126  1.00 30.37           C  
ATOM    866  O   GLY E 109      31.379  31.403   2.742  1.00 30.02           O  
ATOM    867  N   TYR E 110      29.755  32.904   2.513  1.00 12.80           N  
ATOM    868  CA  TYR E 110      30.314  33.392   1.318  1.00  8.71           C  
ATOM    869  C   TYR E 110      31.380  34.432   1.617  1.00 18.90           C  
ATOM    870  O   TYR E 110      31.109  35.442   2.224  1.00 15.17           O  
ATOM    871  CB  TYR E 110      29.170  33.984   0.584  1.00 12.59           C  
ATOM    872  CG  TYR E 110      29.589  34.323  -0.745  1.00 12.47           C  
ATOM    873  CD1 TYR E 110      29.860  33.379  -1.732  1.00 23.16           C  
ATOM    874  CD2 TYR E 110      29.671  35.679  -1.054  1.00  8.00           C  
ATOM    875  CE1 TYR E 110      30.259  33.741  -3.018  1.00 18.61           C  
ATOM    876  CE2 TYR E 110      30.059  36.065  -2.325  1.00 13.00           C  
ATOM    877  CZ  TYR E 110      30.443  35.102  -3.254  1.00 27.57           C  
ATOM    878  OH  TYR E 110      30.810  35.563  -4.492  1.00 27.18           O  
ATOM    879  N   ASN E 111      32.620  34.145   1.223  1.00 15.30           N  
ATOM    880  CA  ASN E 111      33.790  34.975   1.528  1.00 18.79           C  
ATOM    881  C   ASN E 111      34.043  36.008   0.509  1.00 21.53           C  
ATOM    882  O   ASN E 111      35.131  36.106  -0.040  1.00 16.90           O  
ATOM    883  CB  ASN E 111      35.046  34.057   1.604  1.00 19.45           C  
ATOM    884  CG  ASN E 111      35.021  33.316   2.920  1.00 20.33           C  
ATOM    885  OD1 ASN E 111      34.667  33.784   4.014  1.00 20.86           O  
ATOM    886  ND2 ASN E 111      35.351  32.063   2.831  1.00 25.19           N  
ATOM    887  N   ASN E 112      33.035  36.764   0.194  1.00 13.25           N  
ATOM    888  CA  ASN E 112      33.301  37.757  -0.777  1.00 11.93           C  
ATOM    889  C   ASN E 112      32.170  38.825  -0.810  1.00 16.64           C  
ATOM    890  O   ASN E 112      31.182  38.706  -0.071  1.00 13.37           O  
ATOM    891  CB  ASN E 112      33.471  37.162  -2.138  1.00 13.24           C  
ATOM    892  CG  ASN E 112      34.431  37.906  -3.109  1.00 50.43           C  
ATOM    893  OD1 ASN E 112      34.860  39.039  -2.979  1.00 20.84           O  
ATOM    894  ND2 ASN E 112      34.959  37.208  -4.073  1.00 46.07           N  
ATOM    895  N   ALA E 113      32.370  39.850  -1.639  1.00 13.63           N  
ATOM    896  CA  ALA E 113      31.414  40.982  -1.881  1.00 12.25           C  
ATOM    897  C   ALA E 113      31.608  41.439  -3.281  1.00 23.98           C  
ATOM    898  O   ALA E 113      32.667  41.228  -3.822  1.00 16.53           O  
ATOM    899  CB  ALA E 113      31.496  42.131  -0.914  1.00 15.03           C  
ATOM    900  N   PHE E 114      30.604  42.030  -3.927  1.00  9.81           N  
ATOM    901  CA  PHE E 114      30.768  42.427  -5.288  1.00  8.81           C  
ATOM    902  C   PHE E 114      29.643  43.380  -5.768  1.00 19.96           C  
ATOM    903  O   PHE E 114      28.588  43.473  -5.209  1.00 17.18           O  
ATOM    904  CB  PHE E 114      30.762  41.224  -6.236  1.00 13.66           C  
ATOM    905  CG  PHE E 114      29.547  40.225  -6.173  1.00 16.59           C  
ATOM    906  CD1 PHE E 114      29.529  39.203  -5.213  1.00 17.22           C  
ATOM    907  CD2 PHE E 114      28.508  40.249  -7.122  1.00 20.04           C  
ATOM    908  CE1 PHE E 114      28.463  38.282  -5.141  1.00 22.22           C  
ATOM    909  CE2 PHE E 114      27.404  39.392  -7.044  1.00 20.42           C  
ATOM    910  CZ  PHE E 114      27.404  38.409  -6.049  1.00 20.65           C  
ATOM    911  N   TRP E 115      29.939  44.053  -6.879  1.00 19.27           N  
ATOM    912  CA  TRP E 115      29.029  44.894  -7.644  1.00 14.92           C  
ATOM    913  C   TRP E 115      28.628  44.068  -8.830  1.00 25.48           C  
ATOM    914  O   TRP E 115      29.493  43.560  -9.518  1.00 19.48           O  
ATOM    915  CB  TRP E 115      29.672  46.185  -8.105  1.00 13.85           C  
ATOM    916  CG  TRP E 115      28.859  46.859  -9.153  1.00 19.00           C  
ATOM    917  CD1 TRP E 115      29.177  46.960 -10.477  1.00 22.97           C  
ATOM    918  CD2 TRP E 115      27.749  47.768  -8.934  1.00 14.75           C  
ATOM    919  NE1 TRP E 115      28.248  47.756 -11.142  1.00 18.30           N  
ATOM    920  CE2 TRP E 115      27.360  48.272 -10.213  1.00 18.99           C  
ATOM    921  CE3 TRP E 115      27.013  48.087  -7.806  1.00 13.45           C  
ATOM    922  CZ2 TRP E 115      26.219  49.109 -10.385  1.00 16.74           C  
ATOM    923  CZ3 TRP E 115      25.909  48.943  -7.964  1.00 11.14           C  
ATOM    924  CH2 TRP E 115      25.500  49.398  -9.246  1.00 13.11           C  
ATOM    925  N   ASN E 116      27.348  43.839  -9.020  1.00 16.25           N  
ATOM    926  CA  ASN E 116      26.982  42.959 -10.078  1.00 14.88           C  
ATOM    927  C   ASN E 116      26.524  43.626 -11.315  1.00 19.59           C  
ATOM    928  O   ASN E 116      25.890  42.977 -12.112  1.00 23.98           O  
ATOM    929  CB  ASN E 116      25.964  41.913  -9.618  1.00 14.55           C  
ATOM    930  CG  ASN E 116      24.546  42.465  -9.493  1.00 21.75           C  
ATOM    931  OD1 ASN E 116      24.333  43.666  -9.596  1.00 15.67           O  
ATOM    932  ND2 ASN E 116      23.580  41.632  -9.259  1.00 14.59           N  
ATOM    933  N   GLY E 117      26.757  44.932 -11.466  1.00 17.33           N  
ATOM    934  CA  GLY E 117      26.269  45.589 -12.671  1.00 14.81           C  
ATOM    935  C   GLY E 117      24.978  46.375 -12.292  1.00 22.76           C  
ATOM    936  O   GLY E 117      24.593  47.287 -13.015  1.00 15.30           O  
ATOM    937  N   SER E 118      24.319  46.037 -11.171  1.00 11.69           N  
ATOM    938  CA  SER E 118      23.081  46.740 -10.786  1.00 11.30           C  
ATOM    939  C   SER E 118      23.062  47.018  -9.334  1.00 13.10           C  
ATOM    940  O   SER E 118      22.284  47.855  -8.920  1.00 15.09           O  
ATOM    941  CB  SER E 118      21.798  45.841 -10.999  1.00 12.04           C  
ATOM    942  OG  SER E 118      21.802  45.416 -12.362  1.00 27.34           O  
ATOM    943  N   GLU E 119      23.771  46.310  -8.502  1.00  9.67           N  
ATOM    944  CA  GLU E 119      23.664  46.545  -7.049  1.00  8.95           C  
ATOM    945  C   GLU E 119      24.872  45.945  -6.339  1.00 12.98           C  
ATOM    946  O   GLU E 119      25.602  45.172  -6.939  1.00 12.35           O  
ATOM    947  CB  GLU E 119      22.387  45.851  -6.377  1.00  9.14           C  
ATOM    948  CG  GLU E 119      22.414  44.318  -6.584  1.00 14.30           C  
ATOM    949  CD  GLU E 119      21.422  43.611  -5.732  1.00 18.76           C  
ATOM    950  OE1 GLU E 119      21.665  43.584  -4.447  1.00 16.84           O  
ATOM    951  OE2 GLU E 119      20.397  43.178  -6.218  1.00 14.57           O  
ATOM    952  N   MET E 120      25.015  46.223  -5.072  1.00 10.64           N  
ATOM    953  CA  MET E 120      26.068  45.643  -4.286  1.00  9.35           C  
ATOM    954  C   MET E 120      25.553  44.389  -3.610  1.00 20.47           C  
ATOM    955  O   MET E 120      24.419  44.330  -3.258  1.00 15.53           O  
ATOM    956  CB  MET E 120      26.583  46.609  -3.187  1.00 13.50           C  
ATOM    957  CG  MET E 120      27.450  47.600  -3.989  1.00 17.34           C  
ATOM    958  SD  MET E 120      28.000  48.934  -2.925  1.00 33.85           S  
ATOM    959  CE  MET E 120      26.479  49.943  -2.630  1.00 24.77           C  
ATOM    960  N   VAL E 121      26.424  43.386  -3.355  1.00  8.72           N  
ATOM    961  CA  VAL E 121      26.090  42.158  -2.666  1.00 11.17           C  
ATOM    962  C   VAL E 121      27.175  41.797  -1.664  1.00 15.55           C  
ATOM    963  O   VAL E 121      28.387  41.908  -2.051  1.00 15.95           O  
ATOM    964  CB  VAL E 121      26.075  41.071  -3.767  1.00 15.00           C  
ATOM    965  CG1 VAL E 121      25.575  39.700  -3.164  1.00 16.17           C  
ATOM    966  CG2 VAL E 121      25.142  41.575  -4.919  1.00 13.34           C  
ATOM    967  N   TYR E 122      26.794  41.439  -0.430  1.00 10.00           N  
ATOM    968  CA  TYR E 122      27.846  41.095   0.575  1.00  9.47           C  
ATOM    969  C   TYR E 122      27.539  39.746   1.220  1.00 17.92           C  
ATOM    970  O   TYR E 122      26.422  39.497   1.690  1.00 14.36           O  
ATOM    971  CB  TYR E 122      27.787  42.047   1.801  1.00 16.11           C  
ATOM    972  CG  TYR E 122      28.047  43.481   1.345  1.00 14.78           C  
ATOM    973  CD1 TYR E 122      29.352  43.977   1.226  1.00 11.94           C  
ATOM    974  CD2 TYR E 122      27.018  44.357   0.977  1.00 12.04           C  
ATOM    975  CE1 TYR E 122      29.671  45.250   0.735  1.00 13.73           C  
ATOM    976  CE2 TYR E 122      27.344  45.620   0.470  1.00 14.40           C  
ATOM    977  CZ  TYR E 122      28.644  46.126   0.402  1.00 23.84           C  
ATOM    978  OH  TYR E 122      28.896  47.388  -0.085  1.00 22.34           O  
ATOM    979  N   GLY E 123      28.586  38.883   1.298  1.00 11.94           N  
ATOM    980  CA  GLY E 123      28.481  37.581   1.975  1.00 11.18           C  
ATOM    981  C   GLY E 123      28.718  37.842   3.458  1.00 11.80           C  
ATOM    982  O   GLY E 123      29.066  38.999   3.801  1.00 16.69           O  
ATOM    983  N   ASP E 124      28.466  36.871   4.339  1.00  6.76           N  
ATOM    984  CA  ASP E 124      28.714  37.056   5.744  1.00  6.06           C  
ATOM    985  C   ASP E 124      30.134  36.482   6.158  1.00  6.40           C  
ATOM    986  O   ASP E 124      30.561  36.587   7.339  1.00 13.98           O  
ATOM    987  CB  ASP E 124      27.734  36.192   6.549  1.00 10.30           C  
ATOM    988  CG  ASP E 124      26.321  36.764   6.521  1.00 20.90           C  
ATOM    989  OD1 ASP E 124      26.249  38.069   6.538  1.00 23.76           O  
ATOM    990  OD2 ASP E 124      25.364  36.045   6.469  1.00 23.75           O  
ATOM    991  N   GLY E 125      30.777  35.882   5.135  1.00 14.56           N  
ATOM    992  CA  GLY E 125      32.049  35.244   5.478  1.00 19.28           C  
ATOM    993  C   GLY E 125      31.786  33.873   6.174  1.00 22.44           C  
ATOM    994  O   GLY E 125      30.672  33.539   6.525  1.00 20.92           O  
ATOM    995  N   ASP E 126      32.845  33.043   6.338  1.00 21.13           N  
ATOM    996  CA  ASP E 126      32.770  31.730   6.974  1.00 24.29           C  
ATOM    997  C   ASP E 126      33.149  31.885   8.387  1.00 31.83           C  
ATOM    998  O   ASP E 126      33.106  30.984   9.179  1.00 27.50           O  
ATOM    999  CB  ASP E 126      33.715  30.742   6.386  1.00 20.93           C  
ATOM   1000  CG  ASP E 126      35.164  31.243   6.349  1.00 21.56           C  
ATOM   1001  OD1 ASP E 126      35.555  32.119   7.261  1.00 24.90           O  
ATOM   1002  OD2 ASP E 126      35.891  30.800   5.512  1.00 32.94           O  
ATOM   1003  N   GLY E 127      33.480  33.087   8.715  1.00 19.19           N  
ATOM   1004  CA  GLY E 127      33.758  33.310  10.095  1.00 17.66           C  
ATOM   1005  C   GLY E 127      35.195  33.126  10.454  1.00 40.93           C  
ATOM   1006  O   GLY E 127      35.544  33.403  11.585  1.00 36.21           O  
ATOM   1007  N   GLN E 128      36.031  32.676   9.536  1.00 25.20           N  
ATOM   1008  CA  GLN E 128      37.474  32.492   9.859  1.00 33.89           C  
ATOM   1009  C   GLN E 128      38.352  33.296   8.926  1.00 21.82           C  
ATOM   1010  O   GLN E 128      39.316  33.997   9.252  1.00 35.97           O  
ATOM   1011  CB  GLN E 128      37.817  31.090   9.398  1.00 42.54           C  
ATOM   1012  CG  GLN E 128      37.661  30.018  10.469  1.00100.00           C  
ATOM   1013  CD  GLN E 128      38.876  29.104  10.486  1.00100.00           C  
ATOM   1014  OE1 GLN E 128      39.155  28.397   9.495  1.00100.00           O  
ATOM   1015  NE2 GLN E 128      39.612  29.118  11.610  1.00100.00           N  
ATOM   1016  N   THR E 129      38.000  33.166   7.667  1.00 18.61           N  
ATOM   1017  CA  THR E 129      38.701  33.930   6.708  1.00 20.87           C  
ATOM   1018  C   THR E 129      38.112  35.338   6.732  1.00 30.61           C  
ATOM   1019  O   THR E 129      38.823  36.305   6.595  1.00 22.11           O  
ATOM   1020  CB  THR E 129      38.510  33.277   5.344  1.00 43.04           C  
ATOM   1021  OG1 THR E 129      38.688  31.870   5.437  1.00 46.77           O  
ATOM   1022  CG2 THR E 129      39.302  33.975   4.224  1.00 39.26           C  
ATOM   1023  N   PHE E 130      36.789  35.469   6.903  1.00 23.19           N  
ATOM   1024  CA  PHE E 130      36.212  36.814   6.932  1.00 17.63           C  
ATOM   1025  C   PHE E 130      35.058  36.841   7.864  1.00 19.79           C  
ATOM   1026  O   PHE E 130      34.443  35.799   8.060  1.00 18.97           O  
ATOM   1027  CB  PHE E 130      35.523  37.078   5.597  1.00 18.10           C  
ATOM   1028  CG  PHE E 130      36.395  37.591   4.488  1.00 21.61           C  
ATOM   1029  CD1 PHE E 130      36.825  38.918   4.500  1.00 18.30           C  
ATOM   1030  CD2 PHE E 130      36.749  36.812   3.374  1.00 30.33           C  
ATOM   1031  CE1 PHE E 130      37.645  39.380   3.470  1.00 24.30           C  
ATOM   1032  CE2 PHE E 130      37.581  37.246   2.334  1.00 28.24           C  
ATOM   1033  CZ  PHE E 130      38.017  38.567   2.392  1.00 17.24           C  
ATOM   1034  N   ILE E 131      34.724  38.026   8.345  1.00 17.04           N  
ATOM   1035  CA  ILE E 131      33.486  38.259   9.012  1.00 11.69           C  
ATOM   1036  C   ILE E 131      32.650  39.073   7.985  1.00 15.15           C  
ATOM   1037  O   ILE E 131      33.113  39.388   6.867  1.00 16.46           O  
ATOM   1038  CB  ILE E 131      33.614  38.982  10.254  1.00 19.86           C  
ATOM   1039  CG1 ILE E 131      34.374  40.288   9.994  1.00 15.10           C  
ATOM   1040  CG2 ILE E 131      34.353  38.098  11.246  1.00 28.46           C  
ATOM   1041  CD1 ILE E 131      34.552  40.954  11.373  1.00 18.99           C  
ATOM   1042  N   PRO E 132      31.356  39.348   8.258  1.00 14.55           N  
ATOM   1043  CA  PRO E 132      30.571  39.938   7.206  1.00  8.56           C  
ATOM   1044  C   PRO E 132      31.253  41.126   6.573  1.00 11.75           C  
ATOM   1045  O   PRO E 132      31.603  42.092   7.249  1.00 15.57           O  
ATOM   1046  CB  PRO E 132      29.258  40.277   7.866  1.00 12.60           C  
ATOM   1047  CG  PRO E 132      29.090  39.224   8.962  1.00 11.31           C  
ATOM   1048  CD  PRO E 132      30.567  39.068   9.454  1.00 13.13           C  
ATOM   1049  N   LEU E 133      31.346  41.049   5.256  1.00 11.49           N  
ATOM   1050  CA  LEU E 133      32.138  41.971   4.503  1.00  8.93           C  
ATOM   1051  C   LEU E 133      31.741  43.439   4.539  1.00 23.09           C  
ATOM   1052  O   LEU E 133      32.583  44.341   4.352  1.00 15.45           O  
ATOM   1053  CB  LEU E 133      32.287  41.449   3.080  1.00  9.55           C  
ATOM   1054  CG  LEU E 133      33.304  40.310   3.145  1.00 21.47           C  
ATOM   1055  CD1 LEU E 133      32.675  38.919   3.321  1.00 13.96           C  
ATOM   1056  CD2 LEU E 133      34.243  40.495   1.991  1.00 21.41           C  
ATOM   1057  N   SER E 134      30.454  43.751   4.774  1.00 13.37           N  
ATOM   1058  CA  SER E 134      30.085  45.187   4.794  1.00 11.71           C  
ATOM   1059  C   SER E 134      30.626  45.880   6.068  1.00 13.95           C  
ATOM   1060  O   SER E 134      30.440  47.061   6.232  1.00 16.15           O  
ATOM   1061  CB  SER E 134      28.542  45.280   4.731  1.00 10.99           C  
ATOM   1062  OG  SER E 134      28.081  44.523   5.852  1.00 15.15           O  
ATOM   1063  N   GLY E 135      31.339  45.172   7.013  1.00 13.96           N  
ATOM   1064  CA  GLY E 135      31.891  45.813   8.249  1.00 13.19           C  
ATOM   1065  C   GLY E 135      33.166  46.672   7.913  1.00 19.80           C  
ATOM   1066  O   GLY E 135      33.729  47.392   8.719  1.00 19.58           O  
ATOM   1067  N   GLY E 136      33.617  46.618   6.644  1.00 15.38           N  
ATOM   1068  CA  GLY E 136      34.788  47.357   6.209  1.00 15.73           C  
ATOM   1069  C   GLY E 136      34.446  48.497   5.292  1.00 14.62           C  
ATOM   1070  O   GLY E 136      33.966  48.286   4.144  1.00 15.47           O  
ATOM   1071  N   ILE E 137      34.720  49.740   5.743  1.00 15.94           N  
ATOM   1072  CA  ILE E 137      34.324  50.799   4.845  1.00 12.08           C  
ATOM   1073  C   ILE E 137      35.079  50.789   3.537  1.00 12.02           C  
ATOM   1074  O   ILE E 137      34.567  51.209   2.515  1.00 15.41           O  
ATOM   1075  CB  ILE E 137      34.314  52.077   5.645  1.00 13.66           C  
ATOM   1076  CG1 ILE E 137      33.855  53.220   4.773  1.00 19.20           C  
ATOM   1077  CG2 ILE E 137      35.716  52.325   6.138  1.00 19.49           C  
ATOM   1078  CD1 ILE E 137      33.934  54.473   5.658  1.00 20.43           C  
ATOM   1079  N   ASP E 138      36.370  50.279   3.540  1.00 14.07           N  
ATOM   1080  CA  ASP E 138      37.127  50.250   2.273  1.00 13.81           C  
ATOM   1081  C   ASP E 138      36.545  49.227   1.292  1.00 10.74           C  
ATOM   1082  O   ASP E 138      36.592  49.391   0.075  1.00 14.74           O  
ATOM   1083  CB  ASP E 138      38.658  50.079   2.454  1.00 11.13           C  
ATOM   1084  CG  ASP E 138      39.123  48.986   3.377  1.00 21.68           C  
ATOM   1085  OD1 ASP E 138      38.211  48.116   3.739  1.00 17.03           O  
ATOM   1086  OD2 ASP E 138      40.304  48.791   3.612  1.00 15.94           O  
ATOM   1087  N   VAL E 139      35.948  48.177   1.896  1.00 12.60           N  
ATOM   1088  CA  VAL E 139      35.322  47.159   1.032  1.00  8.69           C  
ATOM   1089  C   VAL E 139      34.066  47.776   0.370  1.00 10.71           C  
ATOM   1090  O   VAL E 139      33.892  47.684  -0.869  1.00 13.17           O  
ATOM   1091  CB  VAL E 139      34.907  45.928   1.873  1.00 16.59           C  
ATOM   1092  CG1 VAL E 139      34.078  44.922   1.063  1.00 17.83           C  
ATOM   1093  CG2 VAL E 139      36.161  45.251   2.447  1.00 18.20           C  
ATOM   1094  N   VAL E 140      33.220  48.426   1.226  1.00 11.81           N  
ATOM   1095  CA  VAL E 140      31.950  49.035   0.705  1.00 11.08           C  
ATOM   1096  C   VAL E 140      32.261  50.015  -0.391  1.00 12.18           C  
ATOM   1097  O   VAL E 140      31.709  50.032  -1.510  1.00 13.14           O  
ATOM   1098  CB  VAL E 140      31.139  49.705   1.831  1.00 14.29           C  
ATOM   1099  CG1 VAL E 140      29.980  50.451   1.129  1.00 15.67           C  
ATOM   1100  CG2 VAL E 140      30.608  48.588   2.786  1.00 12.83           C  
ATOM   1101  N   ALA E 141      33.248  50.878  -0.042  1.00 12.59           N  
ATOM   1102  CA  ALA E 141      33.580  51.888  -1.024  1.00 10.85           C  
ATOM   1103  C   ALA E 141      34.283  51.362  -2.241  1.00 14.69           C  
ATOM   1104  O   ALA E 141      34.153  51.903  -3.378  1.00 15.21           O  
ATOM   1105  CB  ALA E 141      34.497  52.914  -0.336  1.00 13.25           C  
ATOM   1106  N   HIS E 142      35.007  50.219  -2.075  1.00 16.97           N  
ATOM   1107  CA  HIS E 142      35.642  49.622  -3.265  1.00 12.02           C  
ATOM   1108  C   HIS E 142      34.547  49.120  -4.231  1.00  9.91           C  
ATOM   1109  O   HIS E 142      34.565  49.282  -5.449  1.00 10.62           O  
ATOM   1110  CB  HIS E 142      36.533  48.418  -2.742  1.00 11.59           C  
ATOM   1111  CG  HIS E 142      37.041  47.504  -3.848  1.00 14.86           C  
ATOM   1112  ND1 HIS E 142      38.408  47.362  -4.208  1.00 10.87           N  
ATOM   1113  CD2 HIS E 142      36.312  46.569  -4.590  1.00 20.58           C  
ATOM   1114  CE1 HIS E 142      38.446  46.498  -5.271  1.00 13.06           C  
ATOM   1115  NE2 HIS E 142      37.165  45.937  -5.499  1.00 16.12           N  
ATOM   1116  N   GLU E 143      33.520  48.468  -3.627  1.00  8.29           N  
ATOM   1117  CA  GLU E 143      32.452  47.959  -4.488  1.00 12.91           C  
ATOM   1118  C   GLU E 143      31.674  49.091  -5.193  1.00 11.01           C  
ATOM   1119  O   GLU E 143      31.371  49.012  -6.418  1.00 14.48           O  
ATOM   1120  CB  GLU E 143      31.445  47.099  -3.648  1.00 12.49           C  
ATOM   1121  CG  GLU E 143      32.075  45.783  -2.964  1.00 15.84           C  
ATOM   1122  CD  GLU E 143      32.988  44.926  -3.877  1.00 12.59           C  
ATOM   1123  OE1 GLU E 143      33.080  44.976  -5.110  1.00 14.89           O  
ATOM   1124  OE2 GLU E 143      33.727  44.162  -3.174  1.00 22.62           O  
ATOM   1125  N   LEU E 144      31.315  50.132  -4.391  1.00 14.56           N  
ATOM   1126  CA  LEU E 144      30.519  51.211  -5.015  1.00 11.53           C  
ATOM   1127  C   LEU E 144      31.312  51.876  -6.107  1.00 14.47           C  
ATOM   1128  O   LEU E 144      30.813  52.292  -7.139  1.00 15.45           O  
ATOM   1129  CB  LEU E 144      30.116  52.192  -3.921  1.00 12.23           C  
ATOM   1130  CG  LEU E 144      29.005  53.233  -4.266  1.00 26.93           C  
ATOM   1131  CD1 LEU E 144      27.880  52.508  -4.956  1.00 26.57           C  
ATOM   1132  CD2 LEU E 144      28.457  53.655  -2.898  1.00 30.67           C  
ATOM   1133  N   THR E 145      32.657  52.026  -5.956  1.00 13.55           N  
ATOM   1134  CA  THR E 145      33.422  52.644  -7.027  1.00 12.89           C  
ATOM   1135  C   THR E 145      33.385  51.805  -8.253  1.00  9.71           C  
ATOM   1136  O   THR E 145      33.500  52.335  -9.338  1.00 15.27           O  
ATOM   1137  CB  THR E 145      34.885  52.882  -6.517  1.00 16.37           C  
ATOM   1138  OG1 THR E 145      34.908  53.629  -5.351  1.00 11.86           O  
ATOM   1139  CG2 THR E 145      35.890  53.338  -7.533  1.00 11.72           C  
ATOM   1140  N   HIS E 146      33.208  50.451  -8.177  1.00 10.90           N  
ATOM   1141  CA  HIS E 146      33.121  49.729  -9.451  1.00 10.30           C  
ATOM   1142  C   HIS E 146      31.911  50.247 -10.284  1.00 13.64           C  
ATOM   1143  O   HIS E 146      31.907  50.271 -11.545  1.00 15.84           O  
ATOM   1144  CB  HIS E 146      32.872  48.226  -9.174  1.00  9.84           C  
ATOM   1145  CG  HIS E 146      34.170  47.410  -8.928  1.00 15.99           C  
ATOM   1146  ND1 HIS E 146      35.290  47.502  -9.778  1.00 16.71           N  
ATOM   1147  CD2 HIS E 146      34.525  46.507  -7.952  1.00 17.30           C  
ATOM   1148  CE1 HIS E 146      36.252  46.647  -9.351  1.00 13.99           C  
ATOM   1149  NE2 HIS E 146      35.822  46.075  -8.254  1.00 14.83           N  
ATOM   1150  N   ALA E 147      30.884  50.703  -9.570  1.00 13.19           N  
ATOM   1151  CA  ALA E 147      29.706  51.267 -10.326  1.00 15.19           C  
ATOM   1152  C   ALA E 147      30.065  52.566 -10.984  1.00 14.43           C  
ATOM   1153  O   ALA E 147      29.702  52.850 -12.150  1.00 16.36           O  
ATOM   1154  CB  ALA E 147      28.580  51.567  -9.298  1.00 14.02           C  
ATOM   1155  N   VAL E 148      30.819  53.356 -10.177  1.00 12.91           N  
ATOM   1156  CA  VAL E 148      31.255  54.609 -10.773  1.00 15.48           C  
ATOM   1157  C   VAL E 148      32.070  54.319 -12.020  1.00 14.73           C  
ATOM   1158  O   VAL E 148      31.892  54.846 -13.120  1.00 14.61           O  
ATOM   1159  CB  VAL E 148      32.111  55.385  -9.785  1.00 16.28           C  
ATOM   1160  CG1 VAL E 148      32.702  56.660 -10.401  1.00 13.09           C  
ATOM   1161  CG2 VAL E 148      31.296  55.828  -8.584  1.00 15.07           C  
ATOM   1162  N   THR E 149      33.056  53.405 -11.954  1.00 11.79           N  
ATOM   1163  CA  THR E 149      33.831  53.098 -13.205  1.00 12.24           C  
ATOM   1164  C   THR E 149      32.987  52.608 -14.402  1.00 11.07           C  
ATOM   1165  O   THR E 149      33.242  52.889 -15.630  1.00 15.07           O  
ATOM   1166  CB  THR E 149      34.881  51.981 -12.755  1.00 16.14           C  
ATOM   1167  OG1 THR E 149      35.731  52.586 -11.813  1.00 14.77           O  
ATOM   1168  CG2 THR E 149      35.757  51.500 -13.890  1.00 19.12           C  
ATOM   1169  N   ASP E 150      31.980  51.714 -14.015  1.00 15.04           N  
ATOM   1170  CA  ASP E 150      31.132  51.197 -15.071  1.00 17.42           C  
ATOM   1171  C   ASP E 150      30.367  52.297 -15.863  1.00 14.97           C  
ATOM   1172  O   ASP E 150      30.133  52.135 -17.068  1.00 16.24           O  
ATOM   1173  CB  ASP E 150      29.950  50.357 -14.533  1.00 15.41           C  
ATOM   1174  CG  ASP E 150      30.254  48.914 -14.314  1.00 29.87           C  
ATOM   1175  OD1 ASP E 150      31.388  48.538 -14.460  1.00 41.55           O  
ATOM   1176  OD2 ASP E 150      29.320  48.194 -13.667  1.00 33.10           O  
ATOM   1177  N   TYR E 151      29.968  53.388 -15.149  1.00 15.10           N  
ATOM   1178  CA  TYR E 151      29.237  54.466 -15.769  1.00 17.33           C  
ATOM   1179  C   TYR E 151      30.121  55.460 -16.418  1.00 25.90           C  
ATOM   1180  O   TYR E 151      29.646  56.424 -17.052  1.00 24.90           O  
ATOM   1181  CB  TYR E 151      28.498  55.218 -14.735  1.00 18.77           C  
ATOM   1182  CG  TYR E 151      27.226  54.492 -14.676  1.00 24.11           C  
ATOM   1183  CD1 TYR E 151      26.158  54.864 -15.472  1.00 26.44           C  
ATOM   1184  CD2 TYR E 151      27.020  53.453 -13.778  1.00 18.80           C  
ATOM   1185  CE1 TYR E 151      24.977  54.121 -15.388  1.00 37.94           C  
ATOM   1186  CE2 TYR E 151      25.867  52.656 -13.732  1.00 19.90           C  
ATOM   1187  CZ  TYR E 151      24.773  53.079 -14.478  1.00 32.01           C  
ATOM   1188  OH  TYR E 151      23.556  52.439 -14.367  1.00 30.72           O  
ATOM   1189  N   THR E 152      31.465  55.311 -16.232  1.00 20.04           N  
ATOM   1190  CA  THR E 152      32.385  56.310 -16.807  1.00 20.75           C  
ATOM   1191  C   THR E 152      33.383  55.680 -17.785  1.00 21.02           C  
ATOM   1192  O   THR E 152      33.024  55.455 -18.901  1.00 18.51           O  
ATOM   1193  CB  THR E 152      33.120  57.112 -15.698  1.00 19.46           C  
ATOM   1194  OG1 THR E 152      33.815  56.249 -14.788  1.00 14.81           O  
ATOM   1195  CG2 THR E 152      32.156  57.890 -14.847  1.00 14.28           C  
ATOM   1196  N   ALA E 153      34.647  55.340 -17.330  1.00 16.61           N  
ATOM   1197  CA  ALA E 153      35.629  54.683 -18.193  1.00 12.26           C  
ATOM   1198  C   ALA E 153      35.105  53.347 -18.694  1.00 15.55           C  
ATOM   1199  O   ALA E 153      35.372  53.056 -19.868  1.00 18.32           O  
ATOM   1200  CB  ALA E 153      37.002  54.556 -17.508  1.00 13.16           C  
ATOM   1201  N   GLY E 154      34.374  52.594 -17.863  1.00 13.06           N  
ATOM   1202  CA  GLY E 154      33.847  51.363 -18.402  1.00 14.85           C  
ATOM   1203  C   GLY E 154      34.952  50.303 -18.634  1.00 24.19           C  
ATOM   1204  O   GLY E 154      34.864  49.448 -19.497  1.00 19.32           O  
ATOM   1205  N   LEU E 155      35.998  50.361 -17.839  1.00 14.58           N  
ATOM   1206  CA  LEU E 155      37.175  49.454 -17.976  1.00 15.93           C  
ATOM   1207  C   LEU E 155      36.780  47.978 -18.031  1.00 14.71           C  
ATOM   1208  O   LEU E 155      36.108  47.536 -17.104  1.00 17.51           O  
ATOM   1209  CB  LEU E 155      38.215  49.711 -16.863  1.00 14.85           C  
ATOM   1210  CG  LEU E 155      38.828  51.139 -16.882  1.00 15.40           C  
ATOM   1211  CD1 LEU E 155      39.272  51.507 -15.480  1.00 14.54           C  
ATOM   1212  CD2 LEU E 155      40.001  51.171 -17.869  1.00 22.98           C  
ATOM   1213  N   ILE E 156      37.107  47.274 -19.136  1.00 14.11           N  
ATOM   1214  CA  ILE E 156      36.713  45.851 -19.195  1.00 22.89           C  
ATOM   1215  C   ILE E 156      37.431  44.993 -18.086  1.00 29.66           C  
ATOM   1216  O   ILE E 156      38.579  45.234 -17.698  1.00 23.41           O  
ATOM   1217  CB  ILE E 156      36.533  45.259 -20.605  1.00 32.88           C  
ATOM   1218  CG1 ILE E 156      37.629  44.285 -20.885  1.00 37.15           C  
ATOM   1219  CG2 ILE E 156      36.514  46.296 -21.734  1.00 23.29           C  
ATOM   1220  CD1 ILE E 156      38.143  44.523 -22.286  1.00 66.78           C  
ATOM   1221  N   TYR E 157      36.746  44.053 -17.496  1.00 13.61           N  
ATOM   1222  CA  TYR E 157      37.264  43.337 -16.376  1.00 16.58           C  
ATOM   1223  C   TYR E 157      38.247  42.227 -16.697  1.00 20.41           C  
ATOM   1224  O   TYR E 157      38.023  41.071 -16.342  1.00 26.12           O  
ATOM   1225  CB  TYR E 157      36.103  42.797 -15.540  1.00 15.80           C  
ATOM   1226  CG  TYR E 157      36.483  42.686 -14.074  1.00 31.25           C  
ATOM   1227  CD1 TYR E 157      36.886  43.801 -13.326  1.00 37.96           C  
ATOM   1228  CD2 TYR E 157      36.489  41.470 -13.365  1.00 33.20           C  
ATOM   1229  CE1 TYR E 157      37.247  43.712 -11.968  1.00 31.69           C  
ATOM   1230  CE2 TYR E 157      36.755  41.372 -11.981  1.00 26.95           C  
ATOM   1231  CZ  TYR E 157      37.157  42.502 -11.252  1.00 34.82           C  
ATOM   1232  OH  TYR E 157      37.416  42.444  -9.877  1.00 31.04           O  
ATOM   1233  N   GLN E 158      39.300  42.530 -17.423  1.00 16.73           N  
ATOM   1234  CA  GLN E 158      40.262  41.484 -17.615  1.00 26.51           C  
ATOM   1235  C   GLN E 158      41.607  42.041 -17.985  1.00 22.55           C  
ATOM   1236  O   GLN E 158      41.671  43.176 -18.446  1.00 16.46           O  
ATOM   1237  CB  GLN E 158      39.788  40.465 -18.588  1.00 22.83           C  
ATOM   1238  CG  GLN E 158      39.867  40.915 -20.034  1.00 31.15           C  
ATOM   1239  CD  GLN E 158      39.156  39.805 -20.824  1.00100.00           C  
ATOM   1240  OE1 GLN E 158      38.768  38.778 -20.217  1.00100.00           O  
ATOM   1241  NE2 GLN E 158      38.930  40.001 -22.129  1.00 96.66           N  
ATOM   1242  N   ASN E 159      42.703  41.287 -17.786  1.00 18.25           N  
ATOM   1243  CA  ASN E 159      44.011  41.810 -18.181  1.00 11.36           C  
ATOM   1244  C   ASN E 159      44.333  43.187 -17.608  1.00 12.68           C  
ATOM   1245  O   ASN E 159      44.027  43.429 -16.447  1.00 17.53           O  
ATOM   1246  CB  ASN E 159      44.237  41.819 -19.686  1.00 16.76           C  
ATOM   1247  CG  ASN E 159      43.946  40.490 -20.330  1.00 73.30           C  
ATOM   1248  OD1 ASN E 159      44.210  39.522 -19.710  1.00 24.70           O  
ATOM   1249  ND2 ASN E 159      43.471  40.409 -21.572  1.00 40.11           N  
ATOM   1250  N   GLU E 160      45.098  44.042 -18.346  1.00 15.63           N  
ATOM   1251  CA  GLU E 160      45.495  45.361 -17.726  1.00 15.56           C  
ATOM   1252  C   GLU E 160      44.355  46.267 -17.401  1.00 15.15           C  
ATOM   1253  O   GLU E 160      44.395  46.979 -16.383  1.00 18.40           O  
ATOM   1254  CB  GLU E 160      46.546  46.118 -18.538  1.00 17.72           C  
ATOM   1255  CG  GLU E 160      47.930  45.481 -18.311  1.00 23.12           C  
ATOM   1256  CD  GLU E 160      49.080  46.168 -19.030  1.00 25.50           C  
ATOM   1257  OE1 GLU E 160      49.129  47.348 -19.338  1.00 20.48           O  
ATOM   1258  OE2 GLU E 160      50.125  45.371 -19.178  1.00 20.08           O  
ATOM   1259  N   SER E 161      43.359  46.262 -18.312  1.00 14.45           N  
ATOM   1260  CA  SER E 161      42.215  47.193 -18.106  1.00 15.10           C  
ATOM   1261  C   SER E 161      41.504  46.759 -16.877  1.00 16.75           C  
ATOM   1262  O   SER E 161      41.092  47.550 -16.044  1.00 15.12           O  
ATOM   1263  CB  SER E 161      41.422  47.396 -19.390  1.00 18.06           C  
ATOM   1264  OG ASER E 161      42.226  47.367 -20.550  0.20 18.32           O  
ATOM   1265  OG BSER E 161      40.837  46.166 -19.465  0.80 22.32           O  
ATOM   1266  N   GLY E 162      41.478  45.442 -16.649  1.00 13.10           N  
ATOM   1267  CA  GLY E 162      40.834  44.966 -15.461  1.00 10.69           C  
ATOM   1268  C   GLY E 162      41.649  45.256 -14.156  1.00 13.37           C  
ATOM   1269  O   GLY E 162      41.114  45.480 -13.075  1.00 13.82           O  
ATOM   1270  N   ALA E 163      42.995  45.264 -14.249  1.00 18.10           N  
ATOM   1271  CA  ALA E 163      43.756  45.522 -13.088  1.00 12.10           C  
ATOM   1272  C   ALA E 163      43.616  47.003 -12.774  1.00 10.68           C  
ATOM   1273  O   ALA E 163      43.647  47.352 -11.573  1.00 10.51           O  
ATOM   1274  CB  ALA E 163      45.225  45.214 -13.376  1.00 11.66           C  
ATOM   1275  N   ILE E 164      43.458  47.829 -13.775  1.00 13.28           N  
ATOM   1276  CA  ILE E 164      43.242  49.293 -13.491  1.00 13.97           C  
ATOM   1277  C   ILE E 164      41.868  49.487 -12.796  1.00 11.62           C  
ATOM   1278  O   ILE E 164      41.731  50.151 -11.773  1.00 12.32           O  
ATOM   1279  CB  ILE E 164      43.284  50.115 -14.798  1.00 15.95           C  
ATOM   1280  CG1 ILE E 164      44.720  50.230 -15.336  1.00 12.38           C  
ATOM   1281  CG2 ILE E 164      42.829  51.550 -14.434  1.00 14.75           C  
ATOM   1282  CD1 ILE E 164      44.715  50.250 -16.852  1.00 18.39           C  
ATOM   1283  N   ASN E 165      40.877  48.731 -13.270  1.00 12.18           N  
ATOM   1284  CA  ASN E 165      39.576  48.831 -12.681  1.00  7.40           C  
ATOM   1285  C   ASN E 165      39.642  48.521 -11.230  1.00  9.22           C  
ATOM   1286  O   ASN E 165      39.158  49.246 -10.330  1.00 14.36           O  
ATOM   1287  CB  ASN E 165      38.686  47.867 -13.494  1.00  8.17           C  
ATOM   1288  CG  ASN E 165      37.211  47.908 -13.039  1.00 13.99           C  
ATOM   1289  OD1 ASN E 165      36.868  48.093 -11.851  1.00 20.01           O  
ATOM   1290  ND2 ASN E 165      36.353  47.753 -14.020  1.00 12.64           N  
ATOM   1291  N   GLU E 166      40.349  47.392 -10.903  1.00 11.57           N  
ATOM   1292  CA  GLU E 166      40.506  47.001  -9.462  1.00 13.76           C  
ATOM   1293  C   GLU E 166      41.305  48.041  -8.592  1.00  7.45           C  
ATOM   1294  O   GLU E 166      40.900  48.343  -7.504  1.00 11.69           O  
ATOM   1295  CB  GLU E 166      41.232  45.574  -9.393  1.00 13.05           C  
ATOM   1296  CG  GLU E 166      40.224  44.382  -9.474  1.00  9.86           C  
ATOM   1297  CD  GLU E 166      39.155  44.532  -8.409  1.00 15.26           C  
ATOM   1298  OE1 GLU E 166      39.688  44.570  -7.209  1.00 22.55           O  
ATOM   1299  OE2 GLU E 166      37.996  44.672  -8.631  1.00 21.91           O  
ATOM   1300  N   ALA E 167      42.444  48.575  -9.136  1.00 13.85           N  
ATOM   1301  CA  ALA E 167      43.316  49.610  -8.467  1.00 11.62           C  
ATOM   1302  C   ALA E 167      42.446  50.869  -8.120  1.00 10.13           C  
ATOM   1303  O   ALA E 167      42.453  51.361  -6.947  1.00 14.22           O  
ATOM   1304  CB  ALA E 167      44.536  49.934  -9.333  1.00 12.12           C  
ATOM   1305  N   ILE E 168      41.634  51.265  -9.143  1.00 13.62           N  
ATOM   1306  CA  ILE E 168      40.683  52.403  -8.961  1.00 13.35           C  
ATOM   1307  C   ILE E 168      39.824  52.194  -7.740  1.00 12.02           C  
ATOM   1308  O   ILE E 168      39.757  53.040  -6.833  1.00 11.17           O  
ATOM   1309  CB  ILE E 168      39.898  52.735 -10.222  1.00 18.01           C  
ATOM   1310  CG1 ILE E 168      40.893  53.203 -11.305  1.00 20.56           C  
ATOM   1311  CG2 ILE E 168      38.816  53.832  -9.920  1.00 17.67           C  
ATOM   1312  CD1 ILE E 168      41.471  54.581 -11.151  1.00 26.06           C  
ATOM   1313  N   SER E 169      39.242  50.959  -7.678  1.00 12.26           N  
ATOM   1314  CA  SER E 169      38.424  50.625  -6.542  1.00  9.34           C  
ATOM   1315  C   SER E 169      39.196  50.641  -5.240  1.00 12.22           C  
ATOM   1316  O   SER E 169      38.734  51.047  -4.173  1.00 13.78           O  
ATOM   1317  CB  SER E 169      37.576  49.355  -6.688  1.00  9.42           C  
ATOM   1318  OG  SER E 169      36.506  49.604  -7.594  1.00 14.20           O  
ATOM   1319  N   ASP E 170      40.405  50.105  -5.186  1.00 15.88           N  
ATOM   1320  CA  ASP E 170      41.203  50.153  -3.896  1.00  7.85           C  
ATOM   1321  C   ASP E 170      41.611  51.642  -3.586  1.00  9.01           C  
ATOM   1322  O   ASP E 170      41.584  52.002  -2.400  1.00 13.17           O  
ATOM   1323  CB  ASP E 170      42.516  49.323  -4.170  1.00  9.45           C  
ATOM   1324  CG  ASP E 170      42.307  47.838  -4.028  1.00 20.31           C  
ATOM   1325  OD1 ASP E 170      41.091  47.437  -3.616  1.00 13.42           O  
ATOM   1326  OD2 ASP E 170      43.118  47.032  -4.404  1.00 16.91           O  
ATOM   1327  N   ILE E 171      42.022  52.370  -4.616  1.00 10.03           N  
ATOM   1328  CA  ILE E 171      42.425  53.775  -4.331  1.00 11.99           C  
ATOM   1329  C   ILE E 171      41.255  54.595  -3.707  1.00 13.94           C  
ATOM   1330  O   ILE E 171      41.381  55.157  -2.615  1.00 13.92           O  
ATOM   1331  CB  ILE E 171      42.952  54.400  -5.632  1.00 14.22           C  
ATOM   1332  CG1 ILE E 171      44.258  53.697  -6.138  1.00 13.57           C  
ATOM   1333  CG2 ILE E 171      43.088  55.923  -5.470  1.00 12.16           C  
ATOM   1334  CD1 ILE E 171      44.550  54.026  -7.602  1.00 13.90           C  
ATOM   1335  N   PHE E 172      40.082  54.620  -4.385  1.00 12.71           N  
ATOM   1336  CA  PHE E 172      38.926  55.309  -3.820  1.00  9.39           C  
ATOM   1337  C   PHE E 172      38.410  54.615  -2.578  1.00 12.82           C  
ATOM   1338  O   PHE E 172      37.974  55.236  -1.644  1.00 16.83           O  
ATOM   1339  CB  PHE E 172      37.861  55.495  -4.922  1.00 10.94           C  
ATOM   1340  CG  PHE E 172      38.349  56.601  -5.836  1.00 16.21           C  
ATOM   1341  CD1 PHE E 172      38.344  57.898  -5.322  1.00 23.26           C  
ATOM   1342  CD2 PHE E 172      38.893  56.348  -7.092  1.00 11.98           C  
ATOM   1343  CE1 PHE E 172      38.837  58.957  -6.082  1.00 14.88           C  
ATOM   1344  CE2 PHE E 172      39.384  57.398  -7.869  1.00 18.97           C  
ATOM   1345  CZ  PHE E 172      39.319  58.711  -7.372  1.00 14.05           C  
ATOM   1346  N   GLY E 173      38.496  53.280  -2.440  1.00 11.78           N  
ATOM   1347  CA  GLY E 173      38.024  52.855  -1.124  1.00 10.29           C  
ATOM   1348  C   GLY E 173      38.884  53.331   0.021  1.00 15.35           C  
ATOM   1349  O   GLY E 173      38.403  53.547   1.120  1.00 15.42           O  
ATOM   1350  N   THR E 174      40.196  53.423  -0.238  1.00 15.10           N  
ATOM   1351  CA  THR E 174      41.092  53.905   0.785  1.00  8.68           C  
ATOM   1352  C   THR E 174      40.825  55.444   1.002  1.00  8.91           C  
ATOM   1353  O   THR E 174      40.846  55.905   2.161  1.00 14.41           O  
ATOM   1354  CB  THR E 174      42.585  53.701   0.261  1.00 12.46           C  
ATOM   1355  OG1 THR E 174      42.864  52.300   0.443  1.00 16.75           O  
ATOM   1356  CG2 THR E 174      43.527  54.606   1.114  1.00 11.41           C  
ATOM   1357  N   LEU E 175      40.614  56.181  -0.068  1.00 11.05           N  
ATOM   1358  CA  LEU E 175      40.365  57.671   0.115  1.00 12.50           C  
ATOM   1359  C   LEU E 175      39.123  57.883   0.964  1.00 17.80           C  
ATOM   1360  O   LEU E 175      39.015  58.720   1.842  1.00 17.46           O  
ATOM   1361  CB  LEU E 175      40.289  58.418  -1.253  1.00 13.44           C  
ATOM   1362  CG  LEU E 175      41.683  58.401  -1.894  1.00 13.24           C  
ATOM   1363  CD1 LEU E 175      41.643  59.118  -3.241  1.00 15.88           C  
ATOM   1364  CD2 LEU E 175      42.607  59.063  -0.923  1.00 20.42           C  
ATOM   1365  N   VAL E 176      38.128  57.027   0.709  1.00 17.42           N  
ATOM   1366  CA  VAL E 176      36.921  57.079   1.509  1.00 10.72           C  
ATOM   1367  C   VAL E 176      37.186  56.697   2.954  1.00 18.99           C  
ATOM   1368  O   VAL E 176      36.661  57.317   3.855  1.00 15.64           O  
ATOM   1369  CB  VAL E 176      35.722  56.249   0.897  1.00 10.59           C  
ATOM   1370  CG1 VAL E 176      34.552  56.183   1.873  1.00 18.44           C  
ATOM   1371  CG2 VAL E 176      35.340  56.807  -0.504  1.00  9.63           C  
ATOM   1372  N   GLU E 177      38.011  55.676   3.235  1.00 13.99           N  
ATOM   1373  CA  GLU E 177      38.296  55.361   4.603  1.00 11.51           C  
ATOM   1374  C   GLU E 177      39.017  56.550   5.292  1.00 10.17           C  
ATOM   1375  O   GLU E 177      38.778  56.770   6.496  1.00 14.80           O  
ATOM   1376  CB  GLU E 177      39.179  54.109   4.521  1.00 13.67           C  
ATOM   1377  CG  GLU E 177      39.594  53.581   5.923  1.00 12.38           C  
ATOM   1378  CD  GLU E 177      40.332  52.227   5.906  1.00 18.69           C  
ATOM   1379  OE1 GLU E 177      39.903  51.305   5.232  1.00 15.75           O  
ATOM   1380  OE2 GLU E 177      41.409  52.073   6.684  1.00 15.74           O  
ATOM   1381  N   PHE E 178      39.870  57.270   4.518  1.00 15.61           N  
ATOM   1382  CA  PHE E 178      40.514  58.422   5.124  1.00 16.82           C  
ATOM   1383  C   PHE E 178      39.477  59.564   5.338  1.00 17.78           C  
ATOM   1384  O   PHE E 178      39.431  60.237   6.374  1.00 23.33           O  
ATOM   1385  CB  PHE E 178      41.596  59.023   4.222  1.00 18.01           C  
ATOM   1386  CG  PHE E 178      42.939  58.422   4.549  1.00 17.88           C  
ATOM   1387  CD1 PHE E 178      43.712  58.800   5.653  1.00 30.36           C  
ATOM   1388  CD2 PHE E 178      43.437  57.363   3.773  1.00 17.26           C  
ATOM   1389  CE1 PHE E 178      44.959  58.191   5.929  1.00 20.10           C  
ATOM   1390  CE2 PHE E 178      44.671  56.748   4.048  1.00 24.09           C  
ATOM   1391  CZ  PHE E 178      45.454  57.159   5.133  1.00 19.57           C  
ATOM   1392  N   TYR E 179      38.576  59.770   4.380  1.00 19.88           N  
ATOM   1393  CA  TYR E 179      37.532  60.796   4.550  1.00 17.06           C  
ATOM   1394  C   TYR E 179      36.673  60.609   5.780  1.00 24.58           C  
ATOM   1395  O   TYR E 179      36.270  61.536   6.455  1.00 25.50           O  
ATOM   1396  CB  TYR E 179      36.629  60.605   3.360  1.00 22.47           C  
ATOM   1397  CG  TYR E 179      35.426  61.519   3.358  1.00 36.36           C  
ATOM   1398  CD1 TYR E 179      35.572  62.892   3.129  1.00 33.86           C  
ATOM   1399  CD2 TYR E 179      34.139  61.001   3.524  1.00 25.41           C  
ATOM   1400  CE1 TYR E 179      34.470  63.743   3.030  1.00 20.55           C  
ATOM   1401  CE2 TYR E 179      33.027  61.848   3.440  1.00 37.33           C  
ATOM   1402  CZ  TYR E 179      33.190  63.226   3.221  1.00 28.81           C  
ATOM   1403  OH  TYR E 179      32.131  64.129   3.201  1.00 39.21           O  
ATOM   1404  N   ALA E 180      36.333  59.404   6.087  1.00 17.93           N  
ATOM   1405  CA  ALA E 180      35.513  59.184   7.238  1.00 17.67           C  
ATOM   1406  C   ALA E 180      36.360  59.068   8.452  1.00 22.60           C  
ATOM   1407  O   ALA E 180      35.826  59.009   9.517  1.00 25.75           O  
ATOM   1408  CB  ALA E 180      34.730  57.881   7.057  1.00 23.08           C  
ATOM   1409  N   ASN E 181      37.688  58.953   8.271  1.00 21.73           N  
ATOM   1410  CA  ASN E 181      38.536  58.911   9.389  1.00 22.51           C  
ATOM   1411  C   ASN E 181      38.304  57.752  10.329  1.00 24.60           C  
ATOM   1412  O   ASN E 181      38.471  57.775  11.525  1.00 24.24           O  
ATOM   1413  CB  ASN E 181      38.251  60.221  10.061  1.00 40.63           C  
ATOM   1414  CG  ASN E 181      39.484  60.659  10.744  1.00100.00           C  
ATOM   1415  OD1 ASN E 181      40.524  59.984  10.653  1.00 50.58           O  
ATOM   1416  ND2 ASN E 181      39.380  61.797  11.417  1.00100.00           N  
ATOM   1417  N   LYS E 182      37.955  56.664   9.738  1.00 47.72           N  
ATOM   1418  CA  LYS E 182      37.729  55.454  10.486  1.00 52.50           C  
ATOM   1419  C   LYS E 182      39.093  54.700  10.598  1.00 25.93           C  
ATOM   1420  O   LYS E 182      39.327  53.773   9.787  1.00 26.57           O  
ATOM   1421  CB  LYS E 182      36.747  54.648   9.585  1.00 43.54           C  
ATOM   1422  CG  LYS E 182      35.443  54.103  10.248  1.00 67.25           C  
ATOM   1423  CD  LYS E 182      35.147  52.565  10.226  1.00100.00           C  
ATOM   1424  CE  LYS E 182      35.457  51.751  11.528  1.00100.00           C  
ATOM   1425  NZ  LYS E 182      34.347  51.232  12.391  1.00 85.27           N  
ATOM   1426  N   ASN E 183      40.029  55.080  11.513  1.00 23.76           N  
ATOM   1427  CA  ASN E 183      41.398  54.458  11.576  1.00 16.47           C  
ATOM   1428  C   ASN E 183      41.924  54.143  10.182  1.00 21.81           C  
ATOM   1429  O   ASN E 183      42.046  52.977   9.785  1.00 22.57           O  
ATOM   1430  CB  ASN E 183      41.448  53.037  12.058  1.00 23.37           C  
ATOM   1431  CG  ASN E 183      41.088  52.854  13.448  1.00 51.38           C  
ATOM   1432  OD1 ASN E 183      41.653  53.442  14.352  1.00 67.10           O  
ATOM   1433  ND2 ASN E 183      40.092  52.041  13.626  1.00100.00           N  
ATOM   1434  N   PRO E 184      42.272  55.108   9.426  1.00 20.67           N  
ATOM   1435  CA  PRO E 184      42.637  54.867   8.026  1.00 17.75           C  
ATOM   1436  C   PRO E 184      44.005  54.316   7.839  1.00 30.11           C  
ATOM   1437  O   PRO E 184      44.827  54.553   8.698  1.00 24.27           O  
ATOM   1438  CB  PRO E 184      42.576  56.238   7.389  1.00 21.57           C  
ATOM   1439  CG  PRO E 184      42.569  57.246   8.546  1.00 21.06           C  
ATOM   1440  CD  PRO E 184      42.252  56.522   9.846  1.00 26.22           C  
ATOM   1441  N   ASP E 185      44.249  53.617   6.741  1.00 16.38           N  
ATOM   1442  CA  ASP E 185      45.552  53.070   6.429  1.00 16.67           C  
ATOM   1443  C   ASP E 185      45.567  52.853   4.972  1.00 18.25           C  
ATOM   1444  O   ASP E 185      44.610  53.197   4.280  1.00 19.51           O  
ATOM   1445  CB  ASP E 185      45.761  51.664   6.975  1.00 19.43           C  
ATOM   1446  CG  ASP E 185      44.440  50.855   6.952  1.00 17.59           C  
ATOM   1447  OD1 ASP E 185      44.109  50.504   5.749  1.00 15.09           O  
ATOM   1448  OD2 ASP E 185      43.842  50.549   7.996  1.00 15.49           O  
ATOM   1449  N   TRP E 186      46.649  52.250   4.480  1.00 15.47           N  
ATOM   1450  CA  TRP E 186      46.786  51.963   3.038  1.00 15.16           C  
ATOM   1451  C   TRP E 186      46.678  50.437   2.812  1.00 14.50           C  
ATOM   1452  O   TRP E 186      47.177  49.842   1.877  1.00 20.55           O  
ATOM   1453  CB  TRP E 186      48.139  52.569   2.508  1.00 17.22           C  
ATOM   1454  CG  TRP E 186      48.114  54.075   2.537  1.00 14.03           C  
ATOM   1455  CD1 TRP E 186      48.504  54.868   3.568  1.00 16.09           C  
ATOM   1456  CD2 TRP E 186      47.704  54.944   1.470  1.00 18.18           C  
ATOM   1457  NE1 TRP E 186      48.368  56.184   3.224  1.00 20.11           N  
ATOM   1458  CE2 TRP E 186      47.899  56.271   1.930  1.00 23.93           C  
ATOM   1459  CE3 TRP E 186      47.270  54.740   0.134  1.00 18.39           C  
ATOM   1460  CZ2 TRP E 186      47.575  57.363   1.112  1.00 23.72           C  
ATOM   1461  CZ3 TRP E 186      46.952  55.823  -0.670  1.00 24.61           C  
ATOM   1462  CH2 TRP E 186      47.156  57.136  -0.197  1.00 22.85           C  
ATOM   1463  N   GLU E 187      45.967  49.802   3.713  1.00 17.11           N  
ATOM   1464  CA  GLU E 187      45.759  48.397   3.533  1.00 13.02           C  
ATOM   1465  C   GLU E 187      44.269  48.258   3.099  1.00 22.96           C  
ATOM   1466  O   GLU E 187      43.384  49.050   3.414  1.00 14.66           O  
ATOM   1467  CB  GLU E 187      45.849  47.732   4.912  1.00 17.23           C  
ATOM   1468  CG  GLU E 187      47.217  48.060   5.544  1.00 29.45           C  
ATOM   1469  CD  GLU E 187      48.324  47.499   4.673  1.00 36.60           C  
ATOM   1470  OE1 GLU E 187      48.261  46.217   4.567  1.00 36.33           O  
ATOM   1471  OE2 GLU E 187      49.197  48.103   4.110  1.00 34.11           O  
ATOM   1472  N   ILE E 188      44.008  47.144   2.474  1.00 15.66           N  
ATOM   1473  CA  ILE E 188      42.644  46.805   2.005  1.00 12.50           C  
ATOM   1474  C   ILE E 188      41.985  45.629   2.787  1.00 22.16           C  
ATOM   1475  O   ILE E 188      42.476  44.487   2.742  1.00 18.11           O  
ATOM   1476  CB  ILE E 188      42.583  46.417   0.523  1.00 17.82           C  
ATOM   1477  CG1 ILE E 188      43.158  47.566  -0.297  1.00 16.86           C  
ATOM   1478  CG2 ILE E 188      41.099  46.107   0.146  1.00 12.93           C  
ATOM   1479  CD1 ILE E 188      42.268  48.807  -0.164  1.00 22.94           C  
ATOM   1480  N   GLY E 189      40.823  45.874   3.454  1.00 18.96           N  
ATOM   1481  CA  GLY E 189      40.045  44.767   4.058  1.00 14.24           C  
ATOM   1482  C   GLY E 189      40.441  44.389   5.464  1.00 23.42           C  
ATOM   1483  O   GLY E 189      39.956  43.428   6.047  1.00 14.06           O  
ATOM   1484  N   GLU E 190      41.337  45.168   6.011  1.00 13.61           N  
ATOM   1485  CA  GLU E 190      41.780  44.802   7.320  1.00 13.49           C  
ATOM   1486  C   GLU E 190      40.756  44.619   8.362  1.00 19.87           C  
ATOM   1487  O   GLU E 190      41.022  43.879   9.284  1.00 20.77           O  
ATOM   1488  CB  GLU E 190      42.873  45.785   7.877  1.00 13.13           C  
ATOM   1489  CG  GLU E 190      42.357  47.246   8.190  1.00 15.55           C  
ATOM   1490  CD  GLU E 190      42.010  47.993   6.927  1.00 15.35           C  
ATOM   1491  OE1 GLU E 190      42.439  47.677   5.807  1.00 13.83           O  
ATOM   1492  OE2 GLU E 190      41.350  49.067   7.199  1.00 16.92           O  
ATOM   1493  N   ASP E 191      39.673  45.397   8.365  1.00 14.67           N  
ATOM   1494  CA  ASP E 191      38.766  45.277   9.446  1.00 10.44           C  
ATOM   1495  C   ASP E 191      37.899  44.027   9.378  1.00 13.43           C  
ATOM   1496  O   ASP E 191      37.279  43.713  10.376  1.00 19.12           O  
ATOM   1497  CB  ASP E 191      37.791  46.496   9.410  1.00 14.12           C  
ATOM   1498  CG  ASP E 191      38.440  47.781   9.853  1.00 23.96           C  
ATOM   1499  OD1 ASP E 191      39.448  47.723  10.517  1.00 20.74           O  
ATOM   1500  OD2 ASP E 191      38.000  48.855   9.252  1.00 18.11           O  
ATOM   1501  N   VAL E 192      37.842  43.335   8.242  1.00 15.23           N  
ATOM   1502  CA  VAL E 192      36.959  42.148   8.158  1.00 14.77           C  
ATOM   1503  C   VAL E 192      37.660  40.886   7.796  1.00 17.72           C  
ATOM   1504  O   VAL E 192      37.030  39.818   7.727  1.00 21.74           O  
ATOM   1505  CB  VAL E 192      35.843  42.342   7.150  1.00 14.18           C  
ATOM   1506  CG1 VAL E 192      34.797  43.337   7.649  1.00 22.18           C  
ATOM   1507  CG2 VAL E 192      36.307  42.628   5.737  1.00  9.34           C  
ATOM   1508  N   TYR E 193      38.940  40.972   7.550  1.00 17.96           N  
ATOM   1509  CA  TYR E 193      39.729  39.760   7.194  1.00 19.12           C  
ATOM   1510  C   TYR E 193      40.384  39.037   8.382  1.00 23.74           C  
ATOM   1511  O   TYR E 193      40.867  39.723   9.265  1.00 18.05           O  
ATOM   1512  CB  TYR E 193      40.731  40.274   6.225  1.00 26.18           C  
ATOM   1513  CG  TYR E 193      41.567  39.234   5.661  1.00 20.82           C  
ATOM   1514  CD1 TYR E 193      40.958  38.338   4.803  1.00 21.47           C  
ATOM   1515  CD2 TYR E 193      42.959  39.315   5.775  1.00 21.89           C  
ATOM   1516  CE1 TYR E 193      41.740  37.350   4.209  1.00 36.06           C  
ATOM   1517  CE2 TYR E 193      43.743  38.309   5.218  1.00 25.78           C  
ATOM   1518  CZ  TYR E 193      43.126  37.392   4.373  1.00 39.15           C  
ATOM   1519  OH  TYR E 193      43.889  36.472   3.749  1.00 34.08           O  
ATOM   1520  N   THR E 194      40.307  37.677   8.458  1.00 20.04           N  
ATOM   1521  CA  THR E 194      40.941  36.902   9.561  1.00 16.34           C  
ATOM   1522  C   THR E 194      40.960  37.483  10.897  1.00 30.31           C  
ATOM   1523  O   THR E 194      41.956  37.961  11.447  1.00 17.86           O  
ATOM   1524  CB  THR E 194      42.405  36.664   9.264  1.00 18.96           C  
ATOM   1525  OG1 THR E 194      43.099  37.912   9.157  1.00 17.80           O  
ATOM   1526  CG2 THR E 194      42.487  35.930   7.954  1.00 16.64           C  
ATOM   1527  N   PRO E 195      39.806  37.360  11.378  1.00 22.32           N  
ATOM   1528  CA  PRO E 195      39.404  37.808  12.657  1.00 25.82           C  
ATOM   1529  C   PRO E 195      40.340  37.180  13.645  1.00 38.89           C  
ATOM   1530  O   PRO E 195      40.689  37.810  14.641  1.00 46.57           O  
ATOM   1531  CB  PRO E 195      37.953  37.337  12.791  1.00 32.06           C  
ATOM   1532  CG  PRO E 195      37.718  36.426  11.587  1.00 29.13           C  
ATOM   1533  CD  PRO E 195      38.771  36.727  10.548  1.00 26.11           C  
ATOM   1534  N   GLY E 196      40.811  35.977  13.348  1.00 31.09           N  
ATOM   1535  CA  GLY E 196      41.826  35.397  14.248  1.00 40.23           C  
ATOM   1536  C   GLY E 196      43.243  36.111  14.236  1.00 45.31           C  
ATOM   1537  O   GLY E 196      43.879  36.184  15.268  1.00 80.62           O  
ATOM   1538  N   ILE E 197      43.741  36.684  13.113  1.00 38.07           N  
ATOM   1539  CA  ILE E 197      45.053  37.326  13.083  1.00 26.52           C  
ATOM   1540  C   ILE E 197      45.016  38.818  13.037  1.00 44.21           C  
ATOM   1541  O   ILE E 197      44.312  39.400  12.235  1.00 31.37           O  
ATOM   1542  CB  ILE E 197      45.608  36.827  11.817  1.00 33.02           C  
ATOM   1543  CG1 ILE E 197      45.351  35.326  11.884  1.00 30.76           C  
ATOM   1544  CG2 ILE E 197      47.032  37.283  11.656  1.00 27.09           C  
ATOM   1545  CD1 ILE E 197      45.653  34.583  10.591  1.00 41.65           C  
ATOM   1546  N   SER E 198      45.791  39.450  13.882  1.00 34.87           N  
ATOM   1547  CA  SER E 198      45.848  40.898  13.882  1.00 39.43           C  
ATOM   1548  C   SER E 198      46.869  41.375  12.923  1.00 40.53           C  
ATOM   1549  O   SER E 198      47.813  40.704  12.601  1.00 36.83           O  
ATOM   1550  CB  SER E 198      46.328  41.420  15.200  1.00 47.77           C  
ATOM   1551  OG  SER E 198      45.331  41.055  16.114  1.00 82.05           O  
ATOM   1552  N   GLY E 199      46.741  42.578  12.504  1.00 30.52           N  
ATOM   1553  CA  GLY E 199      47.782  43.086  11.638  1.00 27.61           C  
ATOM   1554  C   GLY E 199      47.793  42.721  10.165  1.00 35.35           C  
ATOM   1555  O   GLY E 199      48.609  43.276   9.458  1.00 29.73           O  
ATOM   1556  N   ASP E 200      46.974  41.777   9.670  1.00 19.34           N  
ATOM   1557  CA  ASP E 200      47.116  41.501   8.248  1.00 12.58           C  
ATOM   1558  C   ASP E 200      45.956  42.143   7.439  1.00 12.56           C  
ATOM   1559  O   ASP E 200      45.112  42.831   8.025  1.00 19.82           O  
ATOM   1560  CB  ASP E 200      46.956  39.978   8.058  1.00 17.24           C  
ATOM   1561  CG  ASP E 200      45.667  39.488   8.631  1.00 19.88           C  
ATOM   1562  OD1 ASP E 200      45.027  40.041   9.503  1.00 21.10           O  
ATOM   1563  OD2 ASP E 200      45.577  38.256   8.294  1.00 22.56           O  
ATOM   1564  N   SER E 201      45.902  41.870   6.169  1.00 15.55           N  
ATOM   1565  CA  SER E 201      44.804  42.451   5.417  1.00 23.62           C  
ATOM   1566  C   SER E 201      44.785  41.686   4.167  1.00 22.23           C  
ATOM   1567  O   SER E 201      45.664  40.828   3.914  1.00 19.41           O  
ATOM   1568  CB  SER E 201      45.099  43.911   5.098  1.00 19.70           C  
ATOM   1569  OG  SER E 201      46.210  43.915   4.186  1.00 32.08           O  
ATOM   1570  N   LEU E 202      43.862  42.011   3.321  1.00 16.25           N  
ATOM   1571  CA  LEU E 202      43.780  41.313   2.028  1.00 12.47           C  
ATOM   1572  C   LEU E 202      44.872  41.704   1.017  1.00 21.82           C  
ATOM   1573  O   LEU E 202      45.392  40.862   0.297  1.00 21.21           O  
ATOM   1574  CB  LEU E 202      42.319  41.610   1.510  1.00 15.96           C  
ATOM   1575  CG  LEU E 202      41.860  40.787   0.409  1.00 24.16           C  
ATOM   1576  CD1 LEU E 202      41.721  39.448   1.095  1.00 26.29           C  
ATOM   1577  CD2 LEU E 202      40.435  41.220   0.039  1.00 29.97           C  
ATOM   1578  N   ARG E 203      45.107  42.996   0.872  1.00 15.57           N  
ATOM   1579  CA  ARG E 203      46.072  43.545  -0.072  1.00 15.58           C  
ATOM   1580  C   ARG E 203      46.681  44.732   0.628  1.00 14.24           C  
ATOM   1581  O   ARG E 203      46.044  45.275   1.525  1.00 18.59           O  
ATOM   1582  CB  ARG E 203      45.410  44.155  -1.304  1.00 17.81           C  
ATOM   1583  CG  ARG E 203      44.913  43.116  -2.277  1.00 22.14           C  
ATOM   1584  CD  ARG E 203      44.462  43.732  -3.606  1.00 13.87           C  
ATOM   1585  NE  ARG E 203      43.188  44.421  -3.480  1.00 16.45           N  
ATOM   1586  CZ  ARG E 203      42.034  43.745  -3.416  1.00 28.09           C  
ATOM   1587  NH1 ARG E 203      41.947  42.417  -3.386  1.00 17.67           N  
ATOM   1588  NH2 ARG E 203      40.898  44.390  -3.400  1.00 14.30           N  
ATOM   1589  N   SER E 204      47.904  45.105   0.219  1.00 15.19           N  
ATOM   1590  CA  SER E 204      48.586  46.267   0.787  1.00 11.96           C  
ATOM   1591  C   SER E 204      48.894  47.223  -0.350  1.00 20.80           C  
ATOM   1592  O   SER E 204      49.455  46.831  -1.380  1.00 19.74           O  
ATOM   1593  CB  SER E 204      49.981  45.967   1.454  1.00 20.78           C  
ATOM   1594  OG  SER E 204      50.549  47.184   1.977  1.00 21.94           O  
ATOM   1595  N   MET E 205      48.541  48.518  -0.179  1.00 16.48           N  
ATOM   1596  CA  MET E 205      48.904  49.424  -1.247  1.00 11.69           C  
ATOM   1597  C   MET E 205      50.360  49.982  -1.012  1.00 14.26           C  
ATOM   1598  O   MET E 205      51.058  50.340  -1.949  1.00 16.68           O  
ATOM   1599  CB  MET E 205      47.937  50.675  -1.348  1.00 13.03           C  
ATOM   1600  CG  MET E 205      46.468  50.195  -1.574  1.00 21.31           C  
ATOM   1601  SD  MET E 205      45.329  51.597  -1.541  1.00 21.49           S  
ATOM   1602  CE  MET E 205      45.852  52.373  -3.080  1.00 16.17           C  
ATOM   1603  N   SER E 206      50.703  50.075   0.278  1.00 14.35           N  
ATOM   1604  CA  SER E 206      52.025  50.631   0.649  1.00 19.48           C  
ATOM   1605  C   SER E 206      53.129  49.636   0.302  1.00 26.79           C  
ATOM   1606  O   SER E 206      54.196  50.010  -0.155  1.00 22.72           O  
ATOM   1607  CB  SER E 206      52.055  51.015   2.096  1.00 17.43           C  
ATOM   1608  OG  SER E 206      51.740  49.918   2.901  1.00 20.98           O  
ATOM   1609  N   ASP E 207      52.813  48.358   0.372  1.00 21.17           N  
ATOM   1610  CA  ASP E 207      53.783  47.347   0.003  1.00 18.32           C  
ATOM   1611  C   ASP E 207      53.094  46.088  -0.474  1.00 16.47           C  
ATOM   1612  O   ASP E 207      52.907  45.138   0.258  1.00 15.26           O  
ATOM   1613  CB  ASP E 207      54.583  46.912   1.270  1.00 15.97           C  
ATOM   1614  CG  ASP E 207      55.713  45.952   0.856  1.00 23.80           C  
ATOM   1615  OD1 ASP E 207      56.036  45.714  -0.294  1.00 25.76           O  
ATOM   1616  OD2 ASP E 207      56.269  45.370   1.876  1.00 31.27           O  
ATOM   1617  N   PRO E 208      52.717  46.078  -1.702  1.00 14.07           N  
ATOM   1618  CA  PRO E 208      51.919  44.988  -2.171  1.00  8.94           C  
ATOM   1619  C   PRO E 208      52.625  43.645  -2.015  1.00 20.34           C  
ATOM   1620  O   PRO E 208      52.021  42.585  -1.883  1.00 18.46           O  
ATOM   1621  CB  PRO E 208      51.751  45.298  -3.687  1.00 10.51           C  
ATOM   1622  CG  PRO E 208      51.948  46.784  -3.890  1.00 16.86           C  
ATOM   1623  CD  PRO E 208      52.765  47.215  -2.665  1.00 15.72           C  
ATOM   1624  N   ALA E 209      53.933  43.670  -2.084  1.00 15.55           N  
ATOM   1625  CA  ALA E 209      54.720  42.408  -2.085  1.00 18.61           C  
ATOM   1626  C   ALA E 209      54.612  41.679  -0.796  1.00 18.07           C  
ATOM   1627  O   ALA E 209      54.876  40.491  -0.656  1.00 24.37           O  
ATOM   1628  CB  ALA E 209      56.181  42.698  -2.347  1.00 18.49           C  
ATOM   1629  N   LYS E 210      54.162  42.394   0.173  1.00 18.21           N  
ATOM   1630  CA  LYS E 210      54.037  41.783   1.446  1.00 18.85           C  
ATOM   1631  C   LYS E 210      53.182  40.545   1.392  1.00 38.54           C  
ATOM   1632  O   LYS E 210      53.391  39.586   2.112  1.00 30.81           O  
ATOM   1633  CB  LYS E 210      53.452  42.854   2.299  1.00 20.51           C  
ATOM   1634  CG  LYS E 210      52.876  42.483   3.624  1.00 29.18           C  
ATOM   1635  CD  LYS E 210      52.218  43.715   4.220  1.00 39.92           C  
ATOM   1636  CE  LYS E 210      52.410  43.942   5.726  1.00100.00           C  
ATOM   1637  NZ  LYS E 210      51.569  45.030   6.295  1.00100.00           N  
ATOM   1638  N   TYR E 211      52.170  40.593   0.556  1.00 33.71           N  
ATOM   1639  CA  TYR E 211      51.279  39.472   0.412  1.00 34.39           C  
ATOM   1640  C   TYR E 211      51.555  38.848  -0.872  1.00 33.78           C  
ATOM   1641  O   TYR E 211      50.686  38.219  -1.417  1.00 32.70           O  
ATOM   1642  CB  TYR E 211      49.782  39.854   0.401  1.00 28.42           C  
ATOM   1643  CG  TYR E 211      49.516  40.519   1.719  1.00 19.88           C  
ATOM   1644  CD1 TYR E 211      49.685  39.808   2.893  1.00 25.60           C  
ATOM   1645  CD2 TYR E 211      49.202  41.873   1.851  1.00 24.27           C  
ATOM   1646  CE1 TYR E 211      49.357  40.440   4.088  1.00 24.84           C  
ATOM   1647  CE2 TYR E 211      48.992  42.556   3.049  1.00 19.52           C  
ATOM   1648  CZ  TYR E 211      49.045  41.788   4.204  1.00 33.50           C  
ATOM   1649  OH  TYR E 211      48.854  42.276   5.469  1.00 36.79           O  
ATOM   1650  N   GLY E 212      52.685  39.116  -1.454  1.00 25.78           N  
ATOM   1651  CA  GLY E 212      52.937  38.475  -2.735  1.00 22.60           C  
ATOM   1652  C   GLY E 212      52.445  39.087  -4.045  1.00 27.58           C  
ATOM   1653  O   GLY E 212      52.639  38.450  -5.094  1.00 23.10           O  
ATOM   1654  N   ASP E 213      51.871  40.305  -4.051  1.00 22.42           N  
ATOM   1655  CA  ASP E 213      51.437  40.908  -5.341  1.00 18.08           C  
ATOM   1656  C   ASP E 213      52.585  41.716  -5.875  1.00 19.61           C  
ATOM   1657  O   ASP E 213      53.396  42.203  -5.122  1.00 18.78           O  
ATOM   1658  CB  ASP E 213      50.258  41.878  -5.056  1.00 13.33           C  
ATOM   1659  CG  ASP E 213      49.097  41.027  -4.633  1.00 18.83           C  
ATOM   1660  OD1 ASP E 213      48.932  39.935  -5.092  1.00 22.56           O  
ATOM   1661  OD2 ASP E 213      48.322  41.534  -3.728  1.00 20.12           O  
ATOM   1662  N   PRO E 214      52.631  41.882  -7.115  1.00 11.44           N  
ATOM   1663  CA  PRO E 214      53.735  42.610  -7.683  1.00 14.77           C  
ATOM   1664  C   PRO E 214      53.780  44.110  -7.326  1.00 26.69           C  
ATOM   1665  O   PRO E 214      52.723  44.769  -7.250  1.00 16.65           O  
ATOM   1666  CB  PRO E 214      53.551  42.517  -9.205  1.00 11.05           C  
ATOM   1667  CG  PRO E 214      52.025  42.144  -9.312  1.00 17.39           C  
ATOM   1668  CD  PRO E 214      51.725  41.293  -8.100  1.00 13.27           C  
ATOM   1669  N   ASP E 215      55.030  44.666  -7.259  1.00 13.35           N  
ATOM   1670  CA  ASP E 215      55.154  46.087  -6.964  1.00 13.56           C  
ATOM   1671  C   ASP E 215      56.003  46.765  -8.028  1.00 23.01           C  
ATOM   1672  O   ASP E 215      56.505  47.888  -7.892  1.00 16.32           O  
ATOM   1673  CB  ASP E 215      55.688  46.308  -5.543  1.00 11.53           C  
ATOM   1674  CG  ASP E 215      57.116  45.648  -5.520  1.00 16.37           C  
ATOM   1675  OD1 ASP E 215      57.649  45.093  -6.492  1.00 18.61           O  
ATOM   1676  OD2 ASP E 215      57.640  45.771  -4.352  1.00 19.31           O  
ATOM   1677  N   HIS E 216      56.144  46.083  -9.124  1.00 17.53           N  
ATOM   1678  CA  HIS E 216      56.887  46.564 -10.278  1.00 17.61           C  
ATOM   1679  C   HIS E 216      56.379  45.833 -11.495  1.00 16.77           C  
ATOM   1680  O   HIS E 216      56.059  44.664 -11.430  1.00 19.13           O  
ATOM   1681  CB  HIS E 216      58.477  46.380 -10.083  1.00 21.81           C  
ATOM   1682  CG  HIS E 216      59.317  47.113 -11.089  1.00 18.71           C  
ATOM   1683  ND1 HIS E 216      59.528  46.590 -12.359  1.00 21.20           N  
ATOM   1684  CD2 HIS E 216      59.904  48.333 -11.030  1.00 13.72           C  
ATOM   1685  CE1 HIS E 216      60.229  47.451 -13.090  1.00 17.89           C  
ATOM   1686  NE2 HIS E 216      60.442  48.510 -12.299  1.00 21.30           N  
ATOM   1687  N   TYR E 217      56.407  46.551 -12.634  1.00 15.23           N  
ATOM   1688  CA  TYR E 217      55.905  46.034 -13.949  1.00 14.32           C  
ATOM   1689  C   TYR E 217      56.591  44.787 -14.434  1.00 29.70           C  
ATOM   1690  O   TYR E 217      55.968  43.914 -15.064  1.00 22.19           O  
ATOM   1691  CB  TYR E 217      55.858  47.131 -15.047  1.00 19.77           C  
ATOM   1692  CG  TYR E 217      55.030  46.800 -16.296  1.00 18.71           C  
ATOM   1693  CD1 TYR E 217      53.623  46.726 -16.202  1.00 17.86           C  
ATOM   1694  CD2 TYR E 217      55.641  46.575 -17.520  1.00 23.71           C  
ATOM   1695  CE1 TYR E 217      52.770  46.454 -17.265  1.00 16.87           C  
ATOM   1696  CE2 TYR E 217      54.818  46.314 -18.615  1.00 21.94           C  
ATOM   1697  CZ  TYR E 217      53.419  46.304 -18.476  1.00 24.43           C  
ATOM   1698  OH  TYR E 217      52.615  46.000 -19.513  1.00 24.11           O  
ATOM   1699  N   SER E 218      57.880  44.736 -14.110  1.00 16.52           N  
ATOM   1700  CA  SER E 218      58.683  43.586 -14.478  1.00 13.77           C  
ATOM   1701  C   SER E 218      58.199  42.315 -13.766  1.00 21.28           C  
ATOM   1702  O   SER E 218      58.472  41.195 -14.157  1.00 24.19           O  
ATOM   1703  CB  SER E 218      60.179  43.979 -14.147  1.00 13.02           C  
ATOM   1704  OG  SER E 218      60.404  43.915 -12.752  1.00 19.82           O  
ATOM   1705  N   LYS E 219      57.437  42.466 -12.723  1.00 12.31           N  
ATOM   1706  CA  LYS E 219      56.986  41.305 -12.020  1.00 18.00           C  
ATOM   1707  C   LYS E 219      55.533  41.005 -12.259  1.00 21.95           C  
ATOM   1708  O   LYS E 219      54.890  40.280 -11.479  1.00 20.68           O  
ATOM   1709  CB  LYS E 219      57.211  41.597 -10.565  1.00 22.83           C  
ATOM   1710  CG  LYS E 219      58.680  41.618 -10.172  1.00 23.93           C  
ATOM   1711  CD  LYS E 219      58.883  41.988  -8.691  1.00 25.69           C  
ATOM   1712  CE  LYS E 219      60.375  42.204  -8.330  1.00 34.03           C  
ATOM   1713  NZ  LYS E 219      60.774  41.892  -6.919  1.00 33.47           N  
ATOM   1714  N   ARG E 220      54.994  41.593 -13.313  1.00 18.35           N  
ATOM   1715  CA  ARG E 220      53.588  41.342 -13.496  1.00 21.83           C  
ATOM   1716  C   ARG E 220      53.246  39.923 -13.846  1.00 38.29           C  
ATOM   1717  O   ARG E 220      54.011  39.214 -14.454  1.00 20.42           O  
ATOM   1718  CB  ARG E 220      52.938  42.200 -14.506  1.00 16.70           C  
ATOM   1719  CG  ARG E 220      53.442  41.852 -15.862  1.00 16.78           C  
ATOM   1720  CD  ARG E 220      53.221  43.031 -16.784  1.00 27.86           C  
ATOM   1721  NE  ARG E 220      53.707  42.672 -18.100  1.00 34.13           N  
ATOM   1722  CZ  ARG E 220      54.982  42.721 -18.425  1.00 98.23           C  
ATOM   1723  NH1 ARG E 220      55.965  43.176 -17.636  1.00 47.20           N  
ATOM   1724  NH2 ARG E 220      55.285  42.330 -19.624  1.00 60.97           N  
ATOM   1725  N   TYR E 221      52.044  39.522 -13.479  1.00 22.50           N  
ATOM   1726  CA  TYR E 221      51.532  38.171 -13.731  1.00 26.13           C  
ATOM   1727  C   TYR E 221      50.992  38.123 -15.119  1.00 25.20           C  
ATOM   1728  O   TYR E 221      50.227  38.998 -15.508  1.00 22.74           O  
ATOM   1729  CB  TYR E 221      50.346  38.029 -12.792  1.00 22.92           C  
ATOM   1730  CG  TYR E 221      49.685  36.739 -13.024  1.00 24.70           C  
ATOM   1731  CD1 TYR E 221      50.395  35.559 -12.799  1.00 38.70           C  
ATOM   1732  CD2 TYR E 221      48.389  36.748 -13.519  1.00 23.19           C  
ATOM   1733  CE1 TYR E 221      49.765  34.349 -13.033  1.00 21.86           C  
ATOM   1734  CE2 TYR E 221      47.745  35.552 -13.781  1.00 24.59           C  
ATOM   1735  CZ  TYR E 221      48.455  34.383 -13.519  1.00100.00           C  
ATOM   1736  OH  TYR E 221      47.808  33.205 -13.715  1.00 39.65           O  
ATOM   1737  N   THR E 222      51.310  37.126 -15.908  1.00 16.84           N  
ATOM   1738  CA  THR E 222      50.884  37.112 -17.325  1.00 23.16           C  
ATOM   1739  C   THR E 222      50.044  35.913 -17.780  1.00 27.73           C  
ATOM   1740  O   THR E 222      49.703  35.710 -18.937  1.00 32.88           O  
ATOM   1741  CB  THR E 222      52.131  37.167 -18.230  1.00 48.87           C  
ATOM   1742  OG1 THR E 222      52.769  35.936 -18.057  1.00 51.90           O  
ATOM   1743  CG2 THR E 222      53.162  38.181 -17.746  1.00 57.55           C  
ATOM   1744  N   GLY E 223      49.739  35.136 -16.804  1.00 21.41           N  
ATOM   1745  CA  GLY E 223      48.859  34.018 -17.005  1.00 28.60           C  
ATOM   1746  C   GLY E 223      47.343  34.331 -17.066  1.00 34.08           C  
ATOM   1747  O   GLY E 223      46.903  35.446 -17.231  1.00 27.82           O  
ATOM   1748  N   THR E 224      46.552  33.286 -16.801  1.00 26.65           N  
ATOM   1749  CA  THR E 224      45.120  33.366 -16.909  1.00 22.98           C  
ATOM   1750  C   THR E 224      44.268  33.340 -15.693  1.00 35.22           C  
ATOM   1751  O   THR E 224      43.108  33.714 -15.738  1.00 30.41           O  
ATOM   1752  CB  THR E 224      44.552  32.446 -17.976  1.00100.00           C  
ATOM   1753  OG1 THR E 224      44.661  31.112 -17.541  1.00 34.03           O  
ATOM   1754  CG2 THR E 224      45.359  32.618 -19.239  1.00 31.92           C  
ATOM   1755  N   GLN E 225      44.746  32.913 -14.616  1.00 23.59           N  
ATOM   1756  CA  GLN E 225      43.795  32.986 -13.568  1.00 29.73           C  
ATOM   1757  C   GLN E 225      43.402  34.473 -13.279  1.00 21.27           C  
ATOM   1758  O   GLN E 225      44.093  35.447 -13.616  1.00 17.42           O  
ATOM   1759  CB  GLN E 225      44.607  32.603 -12.346  1.00 21.82           C  
ATOM   1760  CG  GLN E 225      44.831  31.180 -11.818  1.00100.00           C  
ATOM   1761  CD  GLN E 225      45.819  31.297 -10.613  1.00100.00           C  
ATOM   1762  OE1 GLN E 225      45.519  31.929  -9.553  1.00100.00           O  
ATOM   1763  NE2 GLN E 225      47.032  30.753 -10.794  1.00 90.63           N  
ATOM   1764  N   ASP E 226      42.369  34.559 -12.461  1.00 26.12           N  
ATOM   1765  CA  ASP E 226      41.853  35.818 -11.929  1.00 18.62           C  
ATOM   1766  C   ASP E 226      41.663  36.779 -12.987  1.00 16.90           C  
ATOM   1767  O   ASP E 226      42.074  37.907 -13.000  1.00 23.44           O  
ATOM   1768  CB  ASP E 226      42.855  36.354 -10.925  1.00 20.36           C  
ATOM   1769  CG  ASP E 226      42.368  37.566 -10.216  1.00 35.53           C  
ATOM   1770  OD1 ASP E 226      41.240  37.750  -9.911  1.00 23.64           O  
ATOM   1771  OD2 ASP E 226      43.302  38.341  -9.803  1.00 23.62           O  
ATOM   1772  N   ASN E 227      41.097  36.235 -13.959  1.00 15.88           N  
ATOM   1773  CA  ASN E 227      40.856  37.019 -15.118  1.00 16.75           C  
ATOM   1774  C   ASN E 227      42.101  37.656 -15.646  1.00 38.39           C  
ATOM   1775  O   ASN E 227      42.039  38.779 -16.188  1.00 23.48           O  
ATOM   1776  CB  ASN E 227      39.875  38.157 -14.705  1.00 22.18           C  
ATOM   1777  CG  ASN E 227      38.474  37.668 -14.544  1.00100.00           C  
ATOM   1778  OD1 ASN E 227      37.838  37.695 -13.501  1.00 48.28           O  
ATOM   1779  ND2 ASN E 227      37.974  37.220 -15.639  1.00 33.39           N  
ATOM   1780  N   GLY E 228      43.227  36.958 -15.570  1.00 32.36           N  
ATOM   1781  CA  GLY E 228      44.408  37.607 -16.145  1.00 20.86           C  
ATOM   1782  C   GLY E 228      45.092  38.472 -15.111  1.00 21.44           C  
ATOM   1783  O   GLY E 228      45.759  39.384 -15.455  1.00 22.83           O  
ATOM   1784  N   GLY E 229      44.844  38.135 -13.856  1.00 15.77           N  
ATOM   1785  CA  GLY E 229      45.388  38.705 -12.617  1.00 17.00           C  
ATOM   1786  C   GLY E 229      44.922  40.112 -12.210  1.00 26.50           C  
ATOM   1787  O   GLY E 229      45.736  40.982 -11.737  1.00 15.67           O  
ATOM   1788  N   VAL E 230      43.600  40.344 -12.341  1.00 15.70           N  
ATOM   1789  CA  VAL E 230      43.098  41.694 -12.081  1.00 13.91           C  
ATOM   1790  C   VAL E 230      43.268  42.062 -10.657  1.00 10.99           C  
ATOM   1791  O   VAL E 230      43.522  43.270 -10.357  1.00 16.63           O  
ATOM   1792  CB  VAL E 230      41.650  41.905 -12.597  1.00 17.55           C  
ATOM   1793  CG1 VAL E 230      41.518  41.481 -14.031  1.00 16.98           C  
ATOM   1794  CG2 VAL E 230      40.784  41.018 -11.738  1.00 16.90           C  
ATOM   1795  N   HIS E 231      43.230  41.054  -9.757  1.00  9.24           N  
ATOM   1796  CA  HIS E 231      43.435  41.318  -8.373  1.00 11.94           C  
ATOM   1797  C   HIS E 231      44.976  41.268  -8.032  1.00 15.29           C  
ATOM   1798  O   HIS E 231      45.312  41.593  -6.873  1.00 18.81           O  
ATOM   1799  CB  HIS E 231      42.685  40.498  -7.270  1.00 15.01           C  
ATOM   1800  CG  HIS E 231      41.219  40.672  -7.444  1.00 18.46           C  
ATOM   1801  ND1 HIS E 231      40.537  39.911  -8.393  1.00 21.74           N  
ATOM   1802  CD2 HIS E 231      40.327  41.525  -6.847  1.00 22.19           C  
ATOM   1803  CE1 HIS E 231      39.237  40.271  -8.338  1.00 19.84           C  
ATOM   1804  NE2 HIS E 231      39.098  41.245  -7.427  1.00 15.60           N  
ATOM   1805  N   ILE E 232      45.828  40.866  -8.979  1.00 15.77           N  
ATOM   1806  CA  ILE E 232      47.295  40.731  -8.648  1.00 15.97           C  
ATOM   1807  C   ILE E 232      48.084  41.936  -9.133  1.00  9.18           C  
ATOM   1808  O   ILE E 232      48.739  42.645  -8.360  1.00 18.18           O  
ATOM   1809  CB  ILE E 232      47.753  39.466  -9.376  1.00 17.43           C  
ATOM   1810  CG1 ILE E 232      46.991  38.304  -8.737  1.00 23.81           C  
ATOM   1811  CG2 ILE E 232      49.296  39.322  -9.209  1.00 19.22           C  
ATOM   1812  CD1 ILE E 232      47.103  36.976  -9.475  1.00 21.33           C  
ATOM   1813  N   ASN E 233      47.901  42.195 -10.406  1.00 12.24           N  
ATOM   1814  CA  ASN E 233      48.600  43.274 -11.020  1.00 10.96           C  
ATOM   1815  C   ASN E 233      48.056  44.618 -10.618  1.00 18.78           C  
ATOM   1816  O   ASN E 233      48.692  45.632 -10.928  1.00 16.29           O  
ATOM   1817  CB  ASN E 233      48.453  43.132 -12.531  1.00 11.99           C  
ATOM   1818  CG  ASN E 233      49.239  41.982 -13.044  1.00 17.28           C  
ATOM   1819  OD1 ASN E 233      50.222  41.630 -12.411  1.00 18.41           O  
ATOM   1820  ND2 ASN E 233      48.811  41.376 -14.142  1.00 17.57           N  
ATOM   1821  N   SER E 234      46.932  44.652  -9.906  1.00 14.61           N  
ATOM   1822  CA  SER E 234      46.473  45.948  -9.450  1.00 14.21           C  
ATOM   1823  C   SER E 234      47.527  46.433  -8.472  1.00 18.49           C  
ATOM   1824  O   SER E 234      47.647  47.635  -8.141  1.00 15.48           O  
ATOM   1825  CB  SER E 234      45.167  45.739  -8.714  1.00 15.02           C  
ATOM   1826  OG  SER E 234      45.339  44.808  -7.633  1.00 17.93           O  
ATOM   1827  N   GLY E 235      48.318  45.521  -7.919  1.00 16.53           N  
ATOM   1828  CA  GLY E 235      49.325  46.018  -6.947  1.00 14.19           C  
ATOM   1829  C   GLY E 235      50.362  47.017  -7.515  1.00 10.40           C  
ATOM   1830  O   GLY E 235      50.879  47.915  -6.789  1.00 16.91           O  
ATOM   1831  N   ILE E 236      50.622  46.947  -8.854  1.00 11.86           N  
ATOM   1832  CA  ILE E 236      51.635  47.851  -9.476  1.00 10.21           C  
ATOM   1833  C   ILE E 236      51.091  49.255  -9.462  1.00 15.02           C  
ATOM   1834  O   ILE E 236      51.765  50.237  -9.169  1.00 18.52           O  
ATOM   1835  CB  ILE E 236      51.830  47.402 -10.912  1.00  8.63           C  
ATOM   1836  CG1 ILE E 236      52.431  45.958 -10.855  1.00 11.56           C  
ATOM   1837  CG2 ILE E 236      52.684  48.363 -11.818  1.00 14.98           C  
ATOM   1838  CD1 ILE E 236      52.401  45.176 -12.154  1.00 12.23           C  
ATOM   1839  N   ILE E 237      49.785  49.366  -9.804  1.00 15.23           N  
ATOM   1840  CA  ILE E 237      49.113  50.707  -9.801  1.00 10.44           C  
ATOM   1841  C   ILE E 237      48.882  51.183  -8.422  1.00 12.94           C  
ATOM   1842  O   ILE E 237      48.995  52.393  -8.131  1.00 15.39           O  
ATOM   1843  CB  ILE E 237      47.738  50.608 -10.504  1.00 18.08           C  
ATOM   1844  CG1 ILE E 237      47.877  50.043 -11.924  1.00 14.72           C  
ATOM   1845  CG2 ILE E 237      47.057  51.992 -10.543  1.00 11.79           C  
ATOM   1846  CD1 ILE E 237      48.907  50.821 -12.695  1.00 23.48           C  
ATOM   1847  N   ASN E 238      48.506  50.285  -7.539  1.00 10.93           N  
ATOM   1848  CA  ASN E 238      48.278  50.684  -6.168  1.00  8.32           C  
ATOM   1849  C   ASN E 238      49.536  51.333  -5.580  1.00 15.49           C  
ATOM   1850  O   ASN E 238      49.463  52.225  -4.772  1.00 11.81           O  
ATOM   1851  CB  ASN E 238      47.834  49.531  -5.217  1.00 11.83           C  
ATOM   1852  CG  ASN E 238      46.367  49.113  -5.435  1.00 18.05           C  
ATOM   1853  OD1 ASN E 238      45.617  49.894  -6.047  1.00 15.66           O  
ATOM   1854  ND2 ASN E 238      45.936  47.983  -4.845  1.00 16.02           N  
ATOM   1855  N   LYS E 239      50.672  50.684  -5.844  1.00 18.20           N  
ATOM   1856  CA  LYS E 239      51.936  51.199  -5.345  1.00 14.38           C  
ATOM   1857  C   LYS E 239      52.221  52.589  -5.959  1.00 15.90           C  
ATOM   1858  O   LYS E 239      52.586  53.503  -5.263  1.00 17.94           O  
ATOM   1859  CB  LYS E 239      53.114  50.189  -5.693  1.00 18.06           C  
ATOM   1860  CG  LYS E 239      54.538  50.622  -5.165  1.00 10.79           C  
ATOM   1861  CD  LYS E 239      54.652  50.488  -3.634  1.00 12.79           C  
ATOM   1862  CE  LYS E 239      56.016  51.023  -3.147  1.00 16.00           C  
ATOM   1863  NZ  LYS E 239      56.097  50.928  -1.746  1.00 20.37           N  
ATOM   1864  N   ALA E 240      52.017  52.718  -7.278  1.00 11.20           N  
ATOM   1865  CA  ALA E 240      52.205  54.027  -7.868  1.00 13.18           C  
ATOM   1866  C   ALA E 240      51.384  55.093  -7.144  1.00 21.82           C  
ATOM   1867  O   ALA E 240      51.843  56.208  -6.855  1.00 17.44           O  
ATOM   1868  CB  ALA E 240      51.786  54.007  -9.323  1.00 15.91           C  
ATOM   1869  N   ALA E 241      50.097  54.778  -6.911  1.00 14.64           N  
ATOM   1870  CA  ALA E 241      49.209  55.713  -6.251  1.00 13.18           C  
ATOM   1871  C   ALA E 241      49.637  56.082  -4.809  1.00 14.89           C  
ATOM   1872  O   ALA E 241      49.614  57.244  -4.364  1.00 14.46           O  
ATOM   1873  CB  ALA E 241      47.806  55.165  -6.303  1.00 17.48           C  
ATOM   1874  N   TYR E 242      50.098  55.100  -4.052  1.00 13.22           N  
ATOM   1875  CA  TYR E 242      50.574  55.349  -2.687  1.00 10.61           C  
ATOM   1876  C   TYR E 242      51.848  56.305  -2.809  1.00 12.00           C  
ATOM   1877  O   TYR E 242      52.065  57.202  -1.965  1.00 17.09           O  
ATOM   1878  CB  TYR E 242      51.106  53.967  -2.126  1.00 12.71           C  
ATOM   1879  CG  TYR E 242      51.931  54.084  -0.863  1.00 18.12           C  
ATOM   1880  CD1 TYR E 242      51.323  54.312   0.375  1.00 17.62           C  
ATOM   1881  CD2 TYR E 242      53.322  54.083  -0.910  1.00 20.84           C  
ATOM   1882  CE1 TYR E 242      52.029  54.578   1.554  1.00 18.77           C  
ATOM   1883  CE2 TYR E 242      54.044  54.328   0.260  1.00 15.76           C  
ATOM   1884  CZ  TYR E 242      53.420  54.569   1.480  1.00 18.72           C  
ATOM   1885  OH  TYR E 242      54.177  54.804   2.607  1.00 31.89           O  
ATOM   1886  N   LEU E 243      52.675  56.095  -3.862  1.00 15.32           N  
ATOM   1887  CA  LEU E 243      53.886  56.901  -3.961  1.00 18.66           C  
ATOM   1888  C   LEU E 243      53.487  58.311  -4.326  1.00 24.39           C  
ATOM   1889  O   LEU E 243      54.011  59.292  -3.777  1.00 18.17           O  
ATOM   1890  CB  LEU E 243      54.928  56.352  -4.939  1.00 17.18           C  
ATOM   1891  CG  LEU E 243      55.602  55.077  -4.387  1.00 12.10           C  
ATOM   1892  CD1 LEU E 243      56.283  54.475  -5.579  1.00 14.55           C  
ATOM   1893  CD2 LEU E 243      56.635  55.348  -3.287  1.00 17.55           C  
ATOM   1894  N   ILE E 244      52.558  58.445  -5.251  1.00 19.13           N  
ATOM   1895  CA  ILE E 244      52.153  59.825  -5.593  1.00 19.21           C  
ATOM   1896  C   ILE E 244      51.701  60.596  -4.354  1.00 25.38           C  
ATOM   1897  O   ILE E 244      52.006  61.795  -4.103  1.00 20.26           O  
ATOM   1898  CB  ILE E 244      51.010  59.824  -6.597  1.00 16.86           C  
ATOM   1899  CG1 ILE E 244      51.581  59.376  -7.908  1.00 12.16           C  
ATOM   1900  CG2 ILE E 244      50.491  61.283  -6.834  1.00 16.93           C  
ATOM   1901  CD1 ILE E 244      50.563  59.052  -9.021  1.00 18.25           C  
ATOM   1902  N   SER E 245      50.898  59.912  -3.535  1.00 16.09           N  
ATOM   1903  CA  SER E 245      50.399  60.554  -2.335  1.00 15.67           C  
ATOM   1904  C   SER E 245      51.410  60.801  -1.240  1.00 27.62           C  
ATOM   1905  O   SER E 245      51.421  61.870  -0.627  1.00 23.90           O  
ATOM   1906  CB  SER E 245      49.191  59.792  -1.747  1.00 17.78           C  
ATOM   1907  OG  SER E 245      48.674  60.373  -0.540  1.00 21.57           O  
ATOM   1908  N   GLN E 246      52.153  59.735  -0.885  1.00 17.21           N  
ATOM   1909  CA  GLN E 246      53.023  59.727   0.282  1.00 17.72           C  
ATOM   1910  C   GLN E 246      54.487  59.980  -0.033  1.00 14.49           C  
ATOM   1911  O   GLN E 246      55.238  60.361   0.851  1.00 24.33           O  
ATOM   1912  CB  GLN E 246      52.919  58.354   1.030  1.00 22.24           C  
ATOM   1913  CG  GLN E 246      51.468  58.002   1.446  1.00 20.00           C  
ATOM   1914  CD  GLN E 246      50.881  59.080   2.330  1.00 39.00           C  
ATOM   1915  OE1 GLN E 246      50.065  59.968   1.970  1.00 27.36           O  
ATOM   1916  NE2 GLN E 246      51.260  59.008   3.575  1.00 35.45           N  
ATOM   1917  N   GLY E 247      54.916  59.661  -1.214  1.00 21.96           N  
ATOM   1918  CA  GLY E 247      56.309  59.823  -1.517  1.00 19.63           C  
ATOM   1919  C   GLY E 247      57.056  58.564  -1.091  1.00 18.75           C  
ATOM   1920  O   GLY E 247      56.575  57.714  -0.395  1.00 20.32           O  
ATOM   1921  N   GLY E 248      58.323  58.546  -1.448  1.00 22.50           N  
ATOM   1922  CA  GLY E 248      59.233  57.466  -1.033  1.00 13.11           C  
ATOM   1923  C   GLY E 248      60.188  57.200  -2.178  1.00 14.09           C  
ATOM   1924  O   GLY E 248      60.121  57.777  -3.319  1.00 20.18           O  
ATOM   1925  N   THR E 249      61.114  56.235  -1.861  1.00 21.31           N  
ATOM   1926  CA  THR E 249      62.112  55.768  -2.847  1.00 20.26           C  
ATOM   1927  C   THR E 249      61.778  54.302  -3.148  1.00 12.12           C  
ATOM   1928  O   THR E 249      61.634  53.494  -2.235  1.00 19.54           O  
ATOM   1929  CB  THR E 249      63.596  56.000  -2.327  1.00 17.75           C  
ATOM   1930  OG1 THR E 249      63.725  57.420  -2.393  1.00 22.25           O  
ATOM   1931  CG2 THR E 249      64.485  55.506  -3.425  1.00 18.72           C  
ATOM   1932  N   HIS E 250      61.613  53.988  -4.424  1.00 13.91           N  
ATOM   1933  CA  HIS E 250      61.209  52.615  -4.668  1.00 16.78           C  
ATOM   1934  C   HIS E 250      62.030  52.136  -5.800  1.00 14.57           C  
ATOM   1935  O   HIS E 250      62.080  52.820  -6.822  1.00 15.95           O  
ATOM   1936  CB  HIS E 250      59.659  52.592  -4.960  1.00 12.81           C  
ATOM   1937  CG  HIS E 250      59.099  51.207  -5.314  1.00 21.78           C  
ATOM   1938  ND1 HIS E 250      59.095  50.120  -4.406  1.00 23.55           N  
ATOM   1939  CD2 HIS E 250      58.522  50.730  -6.464  1.00 20.85           C  
ATOM   1940  CE1 HIS E 250      58.463  49.078  -4.983  1.00 14.79           C  
ATOM   1941  NE2 HIS E 250      58.151  49.408  -6.248  1.00 22.86           N  
ATOM   1942  N   TYR E 251      62.770  51.014  -5.615  1.00 19.18           N  
ATOM   1943  CA  TYR E 251      63.686  50.586  -6.673  1.00 20.49           C  
ATOM   1944  C   TYR E 251      64.670  51.708  -7.065  1.00 14.60           C  
ATOM   1945  O   TYR E 251      65.039  51.837  -8.229  1.00 23.18           O  
ATOM   1946  CB  TYR E 251      63.166  49.812  -7.894  1.00 22.95           C  
ATOM   1947  CG  TYR E 251      62.487  48.493  -7.580  1.00 28.27           C  
ATOM   1948  CD1 TYR E 251      63.191  47.292  -7.411  1.00 20.32           C  
ATOM   1949  CD2 TYR E 251      61.106  48.465  -7.447  1.00 25.31           C  
ATOM   1950  CE1 TYR E 251      62.590  46.065  -7.112  1.00 19.64           C  
ATOM   1951  CE2 TYR E 251      60.515  47.234  -7.156  1.00 23.81           C  
ATOM   1952  CZ  TYR E 251      61.206  46.035  -7.010  1.00 22.67           C  
ATOM   1953  OH  TYR E 251      60.536  44.900  -6.672  1.00 32.22           O  
ATOM   1954  N   GLY E 252      65.102  52.476  -6.089  1.00 23.52           N  
ATOM   1955  CA  GLY E 252      66.042  53.526  -6.444  1.00 19.96           C  
ATOM   1956  C   GLY E 252      65.453  54.776  -7.031  1.00 39.68           C  
ATOM   1957  O   GLY E 252      66.218  55.692  -7.278  1.00 25.97           O  
ATOM   1958  N   VAL E 253      64.135  54.829  -7.311  1.00 22.68           N  
ATOM   1959  CA  VAL E 253      63.531  56.072  -7.897  1.00 24.88           C  
ATOM   1960  C   VAL E 253      62.875  56.846  -6.804  1.00 23.57           C  
ATOM   1961  O   VAL E 253      62.128  56.242  -6.069  1.00 22.36           O  
ATOM   1962  CB  VAL E 253      62.490  55.795  -8.993  1.00 19.84           C  
ATOM   1963  CG1 VAL E 253      61.951  57.079  -9.549  1.00 17.54           C  
ATOM   1964  CG2 VAL E 253      63.117  55.030 -10.162  1.00 23.19           C  
ATOM   1965  N   SER E 254      63.128  58.157  -6.667  1.00 22.21           N  
ATOM   1966  CA  SER E 254      62.562  58.914  -5.540  1.00 16.94           C  
ATOM   1967  C   SER E 254      61.349  59.701  -5.942  1.00 19.65           C  
ATOM   1968  O   SER E 254      61.388  60.215  -7.020  1.00 26.86           O  
ATOM   1969  CB  SER E 254      63.662  59.820  -4.978  1.00 21.76           C  
ATOM   1970  OG  SER E 254      64.644  58.985  -4.322  1.00 32.47           O  
ATOM   1971  N   VAL E 255      60.295  59.749  -5.142  1.00 18.13           N  
ATOM   1972  CA  VAL E 255      59.056  60.441  -5.519  1.00 22.38           C  
ATOM   1973  C   VAL E 255      58.703  61.347  -4.410  1.00 14.20           C  
ATOM   1974  O   VAL E 255      58.657  60.987  -3.228  1.00 16.68           O  
ATOM   1975  CB  VAL E 255      57.869  59.425  -5.605  1.00 24.53           C  
ATOM   1976  CG1 VAL E 255      56.630  60.097  -6.196  1.00 18.38           C  
ATOM   1977  CG2 VAL E 255      58.289  58.316  -6.549  1.00 15.31           C  
ATOM   1978  N   VAL E 256      58.479  62.605  -4.737  1.00 20.75           N  
ATOM   1979  CA  VAL E 256      58.036  63.443  -3.639  1.00 15.37           C  
ATOM   1980  C   VAL E 256      56.502  63.315  -3.584  1.00 19.24           C  
ATOM   1981  O   VAL E 256      55.849  63.480  -4.645  1.00 21.66           O  
ATOM   1982  CB  VAL E 256      58.241  64.896  -4.101  1.00 32.70           C  
ATOM   1983  CG1 VAL E 256      57.783  65.913  -3.058  1.00 26.36           C  
ATOM   1984  CG2 VAL E 256      59.707  65.077  -4.373  1.00 47.42           C  
ATOM   1985  N   GLY E 257      55.998  63.155  -2.380  1.00 16.49           N  
ATOM   1986  CA  GLY E 257      54.555  63.011  -2.221  1.00 16.99           C  
ATOM   1987  C   GLY E 257      53.785  64.329  -2.393  1.00 27.76           C  
ATOM   1988  O   GLY E 257      54.285  65.345  -1.984  1.00 21.35           O  
ATOM   1989  N   ILE E 258      52.542  64.328  -2.956  1.00 15.32           N  
ATOM   1990  CA  ILE E 258      51.703  65.578  -3.092  1.00 12.61           C  
ATOM   1991  C   ILE E 258      50.431  65.498  -2.299  1.00 31.62           C  
ATOM   1992  O   ILE E 258      49.649  66.446  -2.305  1.00 22.45           O  
ATOM   1993  CB  ILE E 258      51.375  65.857  -4.494  1.00 22.20           C  
ATOM   1994  CG1 ILE E 258      50.524  64.694  -5.010  1.00 19.63           C  
ATOM   1995  CG2 ILE E 258      52.665  66.037  -5.327  1.00 17.91           C  
ATOM   1996  CD1 ILE E 258      50.217  64.996  -6.470  1.00 19.05           C  
ATOM   1997  N   GLY E 259      50.214  64.352  -1.596  1.00 19.46           N  
ATOM   1998  CA  GLY E 259      49.085  64.248  -0.659  1.00 19.36           C  
ATOM   1999  C   GLY E 259      47.832  63.544  -1.236  1.00 16.10           C  
ATOM   2000  O   GLY E 259      47.655  63.511  -2.443  1.00 15.45           O  
ATOM   2001  N   ARG E 260      46.926  63.142  -0.387  1.00 15.33           N  
ATOM   2002  CA  ARG E 260      45.713  62.421  -0.795  1.00 20.97           C  
ATOM   2003  C   ARG E 260      44.723  63.136  -1.592  1.00 18.78           C  
ATOM   2004  O   ARG E 260      44.094  62.554  -2.463  1.00 23.05           O  
ATOM   2005  CB  ARG E 260      44.929  62.086   0.404  1.00 27.49           C  
ATOM   2006  CG  ARG E 260      45.480  60.815   0.899  1.00 35.24           C  
ATOM   2007  CD  ARG E 260      45.047  60.464   2.315  1.00 49.83           C  
ATOM   2008  NE  ARG E 260      44.267  61.438   3.107  1.00 44.91           N  
ATOM   2009  CZ  ARG E 260      44.699  61.934   4.290  1.00 50.68           C  
ATOM   2010  NH1 ARG E 260      45.909  61.614   4.773  1.00100.00           N  
ATOM   2011  NH2 ARG E 260      43.925  62.776   4.976  1.00100.00           N  
ATOM   2012  N   ASP E 261      44.482  64.363  -1.210  1.00 20.12           N  
ATOM   2013  CA  ASP E 261      43.467  65.120  -1.921  1.00 13.38           C  
ATOM   2014  C   ASP E 261      43.774  65.256  -3.362  1.00 11.26           C  
ATOM   2015  O   ASP E 261      42.970  65.133  -4.285  1.00 20.33           O  
ATOM   2016  CB  ASP E 261      43.326  66.527  -1.301  1.00 31.74           C  
ATOM   2017  CG  ASP E 261      42.933  66.480   0.159  1.00 82.76           C  
ATOM   2018  OD1 ASP E 261      42.439  65.318   0.547  1.00 69.03           O  
ATOM   2019  OD2 ASP E 261      43.056  67.436   0.909  1.00100.00           O  
ATOM   2020  N   LYS E 262      45.048  65.636  -3.611  1.00 13.30           N  
ATOM   2021  CA  LYS E 262      45.461  65.797  -4.996  1.00 13.70           C  
ATOM   2022  C   LYS E 262      45.466  64.442  -5.752  1.00 11.62           C  
ATOM   2023  O   LYS E 262      45.151  64.408  -6.987  1.00 16.46           O  
ATOM   2024  CB  LYS E 262      46.805  66.616  -5.240  1.00 31.28           C  
ATOM   2025  CG  LYS E 262      46.952  68.002  -4.528  1.00 27.89           C  
ATOM   2026  CD  LYS E 262      48.298  68.726  -4.666  1.00 27.90           C  
ATOM   2027  CE  LYS E 262      48.208  70.206  -4.284  1.00 20.21           C  
ATOM   2028  NZ  LYS E 262      49.590  70.732  -4.258  1.00 25.62           N  
ATOM   2029  N   LEU E 263      45.881  63.369  -5.031  1.00 16.38           N  
ATOM   2030  CA  LEU E 263      45.884  62.008  -5.660  1.00 13.03           C  
ATOM   2031  C   LEU E 263      44.433  61.684  -6.164  1.00 13.16           C  
ATOM   2032  O   LEU E 263      44.238  61.334  -7.333  1.00 15.62           O  
ATOM   2033  CB  LEU E 263      46.238  60.954  -4.575  1.00 14.63           C  
ATOM   2034  CG  LEU E 263      45.982  59.484  -5.052  1.00 15.02           C  
ATOM   2035  CD1 LEU E 263      46.858  59.104  -6.223  1.00 14.92           C  
ATOM   2036  CD2 LEU E 263      46.062  58.520  -3.908  1.00 15.94           C  
ATOM   2037  N   GLY E 264      43.484  61.938  -5.287  1.00 15.77           N  
ATOM   2038  CA  GLY E 264      42.060  61.719  -5.591  1.00 14.33           C  
ATOM   2039  C   GLY E 264      41.620  62.631  -6.690  1.00 17.86           C  
ATOM   2040  O   GLY E 264      40.910  62.207  -7.566  1.00 14.90           O  
ATOM   2041  N   LYS E 265      42.057  63.922  -6.762  1.00 16.23           N  
ATOM   2042  CA  LYS E 265      41.576  64.734  -7.854  1.00 10.84           C  
ATOM   2043  C   LYS E 265      42.128  64.326  -9.179  1.00 13.40           C  
ATOM   2044  O   LYS E 265      41.467  64.355 -10.189  1.00 14.45           O  
ATOM   2045  CB  LYS E 265      42.108  66.088  -7.638  1.00 23.64           C  
ATOM   2046  CG  LYS E 265      41.049  66.783  -6.894  1.00 38.74           C  
ATOM   2047  CD  LYS E 265      41.304  68.239  -6.876  1.00 77.21           C  
ATOM   2048  CE  LYS E 265      41.044  68.745  -5.487  1.00100.00           C  
ATOM   2049  NZ  LYS E 265      39.654  69.187  -5.306  1.00100.00           N  
ATOM   2050  N   ILE E 266      43.434  63.924  -9.180  1.00 11.35           N  
ATOM   2051  CA  ILE E 266      44.016  63.477 -10.419  1.00 14.65           C  
ATOM   2052  C   ILE E 266      43.393  62.177 -10.916  1.00 10.48           C  
ATOM   2053  O   ILE E 266      43.196  62.093 -12.146  1.00 13.41           O  
ATOM   2054  CB  ILE E 266      45.508  63.227 -10.168  1.00 27.20           C  
ATOM   2055  CG1 ILE E 266      46.096  64.628 -10.069  1.00 22.00           C  
ATOM   2056  CG2 ILE E 266      46.183  62.447 -11.317  1.00 17.60           C  
ATOM   2057  CD1 ILE E 266      47.477  64.620  -9.458  1.00 22.09           C  
ATOM   2058  N   PHE E 267      43.213  61.204 -10.006  1.00 12.37           N  
ATOM   2059  CA  PHE E 267      42.648  59.933 -10.479  1.00 16.45           C  
ATOM   2060  C   PHE E 267      41.163  60.032 -10.938  1.00 16.08           C  
ATOM   2061  O   PHE E 267      40.752  59.397 -11.933  1.00 16.31           O  
ATOM   2062  CB  PHE E 267      42.964  58.798  -9.464  1.00 12.16           C  
ATOM   2063  CG  PHE E 267      44.326  58.143  -9.756  1.00 14.58           C  
ATOM   2064  CD1 PHE E 267      45.489  58.649  -9.174  1.00 37.16           C  
ATOM   2065  CD2 PHE E 267      44.435  56.960 -10.489  1.00 32.82           C  
ATOM   2066  CE1 PHE E 267      46.756  58.141  -9.446  1.00 50.93           C  
ATOM   2067  CE2 PHE E 267      45.689  56.413 -10.763  1.00 34.95           C  
ATOM   2068  CZ  PHE E 267      46.844  57.011 -10.257  1.00 25.87           C  
ATOM   2069  N   TYR E 268      40.421  60.857 -10.236  1.00 11.30           N  
ATOM   2070  CA  TYR E 268      39.011  61.027 -10.610  1.00 11.85           C  
ATOM   2071  C   TYR E 268      38.913  61.674 -12.008  1.00 21.50           C  
ATOM   2072  O   TYR E 268      38.065  61.344 -12.877  1.00 17.63           O  
ATOM   2073  CB  TYR E 268      38.362  61.902  -9.546  1.00 10.56           C  
ATOM   2074  CG  TYR E 268      36.912  62.141  -9.838  1.00 19.39           C  
ATOM   2075  CD1 TYR E 268      36.017  61.114  -9.549  1.00 23.52           C  
ATOM   2076  CD2 TYR E 268      36.481  63.247 -10.565  1.00 15.20           C  
ATOM   2077  CE1 TYR E 268      34.659  61.200  -9.860  1.00 20.87           C  
ATOM   2078  CE2 TYR E 268      35.127  63.350 -10.896  1.00 19.53           C  
ATOM   2079  CZ  TYR E 268      34.221  62.359 -10.478  1.00 19.34           C  
ATOM   2080  OH  TYR E 268      32.873  62.397 -10.791  1.00 18.80           O  
ATOM   2081  N   ARG E 269      39.820  62.652 -12.278  1.00 15.47           N  
ATOM   2082  CA  ARG E 269      39.796  63.240 -13.569  1.00 12.86           C  
ATOM   2083  C   ARG E 269      40.211  62.270 -14.622  1.00 15.50           C  
ATOM   2084  O   ARG E 269      39.672  62.206 -15.728  1.00 17.95           O  
ATOM   2085  CB  ARG E 269      40.642  64.504 -13.596  1.00 16.59           C  
ATOM   2086  CG  ARG E 269      40.524  65.222 -14.915  1.00 17.11           C  
ATOM   2087  CD  ARG E 269      41.140  66.608 -14.761  1.00 19.16           C  
ATOM   2088  NE  ARG E 269      41.157  67.148 -16.124  1.00 27.04           N  
ATOM   2089  CZ  ARG E 269      40.203  67.945 -16.603  1.00 36.27           C  
ATOM   2090  NH1 ARG E 269      39.225  68.406 -15.817  1.00 34.28           N  
ATOM   2091  NH2 ARG E 269      40.245  68.316 -17.884  1.00 39.28           N  
ATOM   2092  N   ALA E 270      41.250  61.463 -14.328  1.00 15.55           N  
ATOM   2093  CA  ALA E 270      41.652  60.537 -15.368  1.00 13.23           C  
ATOM   2094  C   ALA E 270      40.481  59.545 -15.710  1.00 12.56           C  
ATOM   2095  O   ALA E 270      40.169  59.199 -16.870  1.00 15.46           O  
ATOM   2096  CB  ALA E 270      42.847  59.727 -14.825  1.00 16.07           C  
ATOM   2097  N   LEU E 271      39.913  59.094 -14.613  1.00 13.76           N  
ATOM   2098  CA  LEU E 271      38.809  58.148 -14.771  1.00 17.19           C  
ATOM   2099  C   LEU E 271      37.611  58.637 -15.578  1.00 18.89           C  
ATOM   2100  O   LEU E 271      37.057  57.912 -16.437  1.00 21.27           O  
ATOM   2101  CB  LEU E 271      38.269  57.877 -13.353  1.00 20.31           C  
ATOM   2102  CG  LEU E 271      37.118  56.851 -13.285  1.00 18.84           C  
ATOM   2103  CD1 LEU E 271      37.559  55.474 -13.865  1.00 20.13           C  
ATOM   2104  CD2 LEU E 271      36.680  56.679 -11.830  1.00 16.92           C  
ATOM   2105  N   THR E 272      37.181  59.882 -15.234  1.00 17.32           N  
ATOM   2106  CA  THR E 272      35.994  60.454 -15.830  1.00 14.54           C  
ATOM   2107  C   THR E 272      36.251  61.094 -17.095  1.00 20.57           C  
ATOM   2108  O   THR E 272      35.348  61.252 -17.838  1.00 25.58           O  
ATOM   2109  CB  THR E 272      35.307  61.430 -14.896  1.00 17.86           C  
ATOM   2110  OG1 THR E 272      36.271  62.417 -14.536  1.00 22.05           O  
ATOM   2111  CG2 THR E 272      34.931  60.694 -13.651  1.00 20.47           C  
ATOM   2112  N   GLN E 273      37.441  61.536 -17.370  1.00 20.03           N  
ATOM   2113  CA  GLN E 273      37.616  62.207 -18.649  1.00 17.76           C  
ATOM   2114  C   GLN E 273      38.521  61.504 -19.664  1.00 29.29           C  
ATOM   2115  O   GLN E 273      38.393  61.806 -20.867  1.00 20.04           O  
ATOM   2116  CB  GLN E 273      38.175  63.675 -18.372  1.00 22.46           C  
ATOM   2117  CG  GLN E 273      37.249  64.573 -17.484  1.00 42.24           C  
ATOM   2118  CD  GLN E 273      36.209  65.238 -18.336  1.00 77.30           C  
ATOM   2119  OE1 GLN E 273      36.514  65.534 -19.504  1.00 67.51           O  
ATOM   2120  NE2 GLN E 273      34.964  65.284 -17.849  1.00 92.18           N  
ATOM   2121  N   TYR E 274      39.482  60.625 -19.220  1.00 21.27           N  
ATOM   2122  CA  TYR E 274      40.445  60.132 -20.166  1.00 21.37           C  
ATOM   2123  C   TYR E 274      40.524  58.659 -20.322  1.00 19.52           C  
ATOM   2124  O   TYR E 274      40.921  58.238 -21.383  1.00 21.51           O  
ATOM   2125  CB  TYR E 274      41.877  60.628 -19.826  1.00 18.42           C  
ATOM   2126  CG  TYR E 274      42.052  62.155 -19.910  1.00 21.00           C  
ATOM   2127  CD1 TYR E 274      41.863  62.849 -21.100  1.00 26.41           C  
ATOM   2128  CD2 TYR E 274      42.307  63.003 -18.841  1.00 16.57           C  
ATOM   2129  CE1 TYR E 274      42.027  64.235 -21.255  1.00 32.63           C  
ATOM   2130  CE2 TYR E 274      42.453  64.397 -18.967  1.00 20.43           C  
ATOM   2131  CZ  TYR E 274      42.382  65.055 -20.188  1.00 27.62           C  
ATOM   2132  OH  TYR E 274      42.477  66.462 -20.218  1.00 24.12           O  
ATOM   2133  N   LEU E 275      40.182  57.904 -19.358  1.00 16.50           N  
ATOM   2134  CA  LEU E 275      40.292  56.458 -19.614  1.00 15.17           C  
ATOM   2135  C   LEU E 275      39.141  55.910 -20.449  1.00 26.08           C  
ATOM   2136  O   LEU E 275      38.092  56.485 -20.455  1.00 18.37           O  
ATOM   2137  CB  LEU E 275      40.281  55.783 -18.228  1.00 13.90           C  
ATOM   2138  CG  LEU E 275      41.511  56.137 -17.355  1.00 15.75           C  
ATOM   2139  CD1 LEU E 275      41.388  55.486 -16.004  1.00 18.50           C  
ATOM   2140  CD2 LEU E 275      42.744  55.618 -18.053  1.00 19.79           C  
ATOM   2141  N   THR E 276      39.353  54.814 -21.119  1.00 14.11           N  
ATOM   2142  CA  THR E 276      38.413  54.142 -21.967  1.00 16.24           C  
ATOM   2143  C   THR E 276      38.304  52.667 -21.565  1.00 21.81           C  
ATOM   2144  O   THR E 276      39.086  52.183 -20.820  1.00 21.98           O  
ATOM   2145  CB  THR E 276      38.839  54.212 -23.433  1.00 20.30           C  
ATOM   2146  OG1 THR E 276      39.920  53.356 -23.655  1.00 21.59           O  
ATOM   2147  CG2 THR E 276      39.177  55.665 -23.738  1.00 22.42           C  
ATOM   2148  N   PRO E 277      37.324  51.943 -22.056  1.00 16.91           N  
ATOM   2149  CA  PRO E 277      37.176  50.552 -21.652  1.00 13.92           C  
ATOM   2150  C   PRO E 277      38.412  49.700 -21.866  1.00 16.56           C  
ATOM   2151  O   PRO E 277      38.559  48.710 -21.131  1.00 18.10           O  
ATOM   2152  CB  PRO E 277      36.087  49.971 -22.571  1.00 15.41           C  
ATOM   2153  CG  PRO E 277      35.230  51.188 -22.845  1.00 14.92           C  
ATOM   2154  CD  PRO E 277      36.214  52.345 -22.989  1.00 16.50           C  
ATOM   2155  N   THR E 278      39.282  50.015 -22.824  1.00 15.51           N  
ATOM   2156  CA  THR E 278      40.416  49.076 -23.056  1.00 19.20           C  
ATOM   2157  C   THR E 278      41.755  49.699 -22.738  1.00 24.52           C  
ATOM   2158  O   THR E 278      42.791  49.249 -23.159  1.00 20.81           O  
ATOM   2159  CB  THR E 278      40.412  48.489 -24.501  1.00 32.20           C  
ATOM   2160  OG1 THR E 278      40.559  49.605 -25.357  1.00 27.29           O  
ATOM   2161  CG2 THR E 278      39.095  47.768 -24.819  1.00 26.44           C  
ATOM   2162  N   SER E 279      41.744  50.739 -21.951  1.00 15.66           N  
ATOM   2163  CA  SER E 279      42.984  51.399 -21.596  1.00 17.26           C  
ATOM   2164  C   SER E 279      43.939  50.450 -20.914  1.00 22.16           C  
ATOM   2165  O   SER E 279      43.480  49.672 -20.082  1.00 20.89           O  
ATOM   2166  CB  SER E 279      42.729  52.442 -20.511  1.00 20.32           C  
ATOM   2167  OG  SER E 279      42.051  53.487 -21.150  1.00 18.90           O  
ATOM   2168  N   ASN E 280      45.267  50.567 -21.171  1.00 18.42           N  
ATOM   2169  CA  ASN E 280      46.260  49.680 -20.463  1.00 16.21           C  
ATOM   2170  C   ASN E 280      47.144  50.479 -19.543  1.00 19.71           C  
ATOM   2171  O   ASN E 280      46.908  51.703 -19.407  1.00 14.08           O  
ATOM   2172  CB  ASN E 280      47.101  48.950 -21.488  1.00 15.08           C  
ATOM   2173  CG  ASN E 280      47.875  49.961 -22.328  1.00 26.07           C  
ATOM   2174  OD1 ASN E 280      48.216  51.092 -21.953  1.00 26.98           O  
ATOM   2175  ND2 ASN E 280      48.124  49.543 -23.534  1.00 29.79           N  
ATOM   2176  N   PHE E 281      48.115  49.858 -18.893  1.00 14.06           N  
ATOM   2177  CA  PHE E 281      48.844  50.644 -17.877  1.00 15.58           C  
ATOM   2178  C   PHE E 281      49.512  51.874 -18.445  1.00 19.84           C  
ATOM   2179  O   PHE E 281      49.582  52.934 -17.869  1.00 17.53           O  
ATOM   2180  CB  PHE E 281      49.927  49.728 -17.310  1.00 23.81           C  
ATOM   2181  CG  PHE E 281      49.407  48.755 -16.306  1.00 17.89           C  
ATOM   2182  CD1 PHE E 281      48.025  48.540 -16.221  1.00 16.84           C  
ATOM   2183  CD2 PHE E 281      50.277  48.087 -15.430  1.00 18.39           C  
ATOM   2184  CE1 PHE E 281      47.542  47.693 -15.226  1.00 15.27           C  
ATOM   2185  CE2 PHE E 281      49.789  47.187 -14.478  1.00 27.08           C  
ATOM   2186  CZ  PHE E 281      48.404  47.006 -14.363  1.00 22.31           C  
ATOM   2187  N   SER E 282      50.012  51.700 -19.625  1.00 15.52           N  
ATOM   2188  CA  SER E 282      50.724  52.782 -20.230  1.00 15.27           C  
ATOM   2189  C   SER E 282      49.779  53.958 -20.599  1.00 25.43           C  
ATOM   2190  O   SER E 282      50.085  55.146 -20.481  1.00 22.25           O  
ATOM   2191  CB  SER E 282      51.544  52.211 -21.343  1.00 23.89           C  
ATOM   2192  OG  SER E 282      51.775  53.232 -22.250  1.00 50.30           O  
ATOM   2193  N   GLN E 283      48.565  53.645 -20.971  1.00 21.26           N  
ATOM   2194  CA  GLN E 283      47.612  54.683 -21.205  1.00 16.39           C  
ATOM   2195  C   GLN E 283      47.179  55.316 -19.906  1.00 16.53           C  
ATOM   2196  O   GLN E 283      46.951  56.545 -19.862  1.00 17.35           O  
ATOM   2197  CB  GLN E 283      46.426  54.064 -21.887  1.00 23.01           C  
ATOM   2198  CG  GLN E 283      46.802  54.027 -23.358  1.00 24.93           C  
ATOM   2199  CD  GLN E 283      46.005  52.992 -24.116  1.00 46.33           C  
ATOM   2200  OE1 GLN E 283      45.479  52.034 -23.595  1.00 29.96           O  
ATOM   2201  NE2 GLN E 283      45.966  53.135 -25.407  1.00 55.37           N  
ATOM   2202  N   LEU E 284      47.094  54.534 -18.833  1.00 12.13           N  
ATOM   2203  CA  LEU E 284      46.762  55.112 -17.562  1.00 12.33           C  
ATOM   2204  C   LEU E 284      47.812  56.211 -17.175  1.00 18.01           C  
ATOM   2205  O   LEU E 284      47.549  57.302 -16.633  1.00 18.15           O  
ATOM   2206  CB  LEU E 284      46.794  54.018 -16.483  1.00 13.82           C  
ATOM   2207  CG  LEU E 284      46.719  54.619 -15.109  1.00 15.80           C  
ATOM   2208  CD1 LEU E 284      45.377  55.387 -14.824  1.00 23.63           C  
ATOM   2209  CD2 LEU E 284      46.832  53.512 -14.088  1.00 20.73           C  
ATOM   2210  N   ARG E 285      49.059  55.902 -17.450  1.00 16.21           N  
ATOM   2211  CA  ARG E 285      50.047  56.892 -17.095  1.00 18.70           C  
ATOM   2212  C   ARG E 285      49.837  58.163 -17.907  1.00 13.60           C  
ATOM   2213  O   ARG E 285      49.979  59.236 -17.328  1.00 21.17           O  
ATOM   2214  CB  ARG E 285      51.472  56.331 -17.296  1.00 17.80           C  
ATOM   2215  CG  ARG E 285      52.518  57.401 -17.292  1.00 17.72           C  
ATOM   2216  CD  ARG E 285      53.883  56.806 -17.712  1.00 18.23           C  
ATOM   2217  NE  ARG E 285      54.912  57.897 -17.667  1.00 29.84           N  
ATOM   2218  CZ  ARG E 285      56.086  57.884 -17.018  1.00 32.86           C  
ATOM   2219  NH1 ARG E 285      56.519  56.868 -16.363  1.00 19.09           N  
ATOM   2220  NH2 ARG E 285      56.887  58.921 -17.065  1.00 20.62           N  
ATOM   2221  N   ALA E 286      49.533  58.074 -19.225  1.00 13.90           N  
ATOM   2222  CA  ALA E 286      49.347  59.300 -20.020  1.00 17.14           C  
ATOM   2223  C   ALA E 286      48.179  60.070 -19.520  1.00 27.30           C  
ATOM   2224  O   ALA E 286      48.141  61.269 -19.434  1.00 16.72           O  
ATOM   2225  CB  ALA E 286      49.071  58.830 -21.397  1.00 20.10           C  
ATOM   2226  N   ALA E 287      47.226  59.299 -19.083  1.00 18.27           N  
ATOM   2227  CA  ALA E 287      46.023  59.951 -18.593  1.00 16.55           C  
ATOM   2228  C   ALA E 287      46.268  60.689 -17.306  1.00 20.16           C  
ATOM   2229  O   ALA E 287      45.766  61.801 -17.046  1.00 22.34           O  
ATOM   2230  CB  ALA E 287      44.873  58.906 -18.433  1.00 19.30           C  
ATOM   2231  N   ALA E 288      46.991  60.021 -16.429  1.00 15.40           N  
ATOM   2232  CA  ALA E 288      47.223  60.648 -15.133  1.00 18.27           C  
ATOM   2233  C   ALA E 288      48.095  61.898 -15.290  1.00 21.02           C  
ATOM   2234  O   ALA E 288      47.955  62.910 -14.605  1.00 19.31           O  
ATOM   2235  CB  ALA E 288      47.866  59.675 -14.170  1.00 17.72           C  
ATOM   2236  N   VAL E 289      48.987  61.849 -16.216  1.00 20.17           N  
ATOM   2237  CA  VAL E 289      49.876  62.984 -16.450  1.00 16.28           C  
ATOM   2238  C   VAL E 289      49.066  64.126 -17.056  1.00 23.86           C  
ATOM   2239  O   VAL E 289      49.145  65.289 -16.660  1.00 23.02           O  
ATOM   2240  CB  VAL E 289      51.060  62.588 -17.380  1.00 19.91           C  
ATOM   2241  CG1 VAL E 289      51.806  63.847 -17.821  1.00 16.08           C  
ATOM   2242  CG2 VAL E 289      52.067  61.720 -16.580  1.00 23.30           C  
ATOM   2243  N   GLN E 290      48.243  63.779 -18.020  1.00 21.59           N  
ATOM   2244  CA  GLN E 290      47.400  64.821 -18.609  1.00 21.65           C  
ATOM   2245  C   GLN E 290      46.466  65.504 -17.626  1.00 25.63           C  
ATOM   2246  O   GLN E 290      46.206  66.730 -17.649  1.00 21.47           O  
ATOM   2247  CB  GLN E 290      46.714  64.251 -19.846  1.00 21.53           C  
ATOM   2248  CG  GLN E 290      45.693  65.228 -20.416  1.00 28.32           C  
ATOM   2249  CD  GLN E 290      46.463  66.377 -21.038  1.00 86.36           C  
ATOM   2250  OE1 GLN E 290      46.305  67.549 -20.723  1.00 39.02           O  
ATOM   2251  NE2 GLN E 290      47.458  66.051 -21.823  1.00 31.90           N  
ATOM   2252  N   SER E 291      45.967  64.683 -16.706  1.00 18.03           N  
ATOM   2253  CA  SER E 291      45.099  65.187 -15.631  1.00 23.27           C  
ATOM   2254  C   SER E 291      45.799  66.180 -14.714  1.00 23.90           C  
ATOM   2255  O   SER E 291      45.214  67.215 -14.386  1.00 20.56           O  
ATOM   2256  CB  SER E 291      44.452  64.124 -14.698  1.00 18.70           C  
ATOM   2257  OG  SER E 291      43.774  63.252 -15.590  1.00 26.37           O  
ATOM   2258  N   ALA E 292      46.982  65.812 -14.196  1.00 17.47           N  
ATOM   2259  CA  ALA E 292      47.699  66.694 -13.294  1.00 18.57           C  
ATOM   2260  C   ALA E 292      48.077  68.003 -14.048  1.00 18.94           C  
ATOM   2261  O   ALA E 292      48.144  69.129 -13.460  1.00 27.17           O  
ATOM   2262  CB  ALA E 292      48.977  65.942 -12.927  1.00 21.07           C  
ATOM   2263  N   THR E 293      48.381  67.780 -15.378  1.00 18.80           N  
ATOM   2264  CA  THR E 293      48.752  68.934 -16.246  1.00 24.21           C  
ATOM   2265  C   THR E 293      47.595  69.861 -16.301  1.00 40.25           C  
ATOM   2266  O   THR E 293      47.767  71.026 -16.073  1.00 27.01           O  
ATOM   2267  CB  THR E 293      49.049  68.606 -17.705  1.00 28.47           C  
ATOM   2268  OG1 THR E 293      50.276  67.890 -17.771  1.00 25.42           O  
ATOM   2269  CG2 THR E 293      49.288  69.937 -18.432  1.00 31.45           C  
ATOM   2270  N   ASP E 294      46.416  69.294 -16.610  1.00 23.39           N  
ATOM   2271  CA  ASP E 294      45.190  70.058 -16.682  1.00 15.56           C  
ATOM   2272  C   ASP E 294      45.003  70.830 -15.416  1.00 30.13           C  
ATOM   2273  O   ASP E 294      44.590  72.021 -15.345  1.00 27.45           O  
ATOM   2274  CB  ASP E 294      43.937  69.166 -16.779  1.00 14.95           C  
ATOM   2275  CG  ASP E 294      43.736  68.525 -18.085  1.00 21.29           C  
ATOM   2276  OD1 ASP E 294      44.402  68.879 -19.005  1.00 21.12           O  
ATOM   2277  OD2 ASP E 294      42.792  67.583 -18.164  1.00 28.53           O  
ATOM   2278  N   LEU E 295      45.204  70.140 -14.359  1.00 20.86           N  
ATOM   2279  CA  LEU E 295      44.889  70.787 -13.117  1.00 17.97           C  
ATOM   2280  C   LEU E 295      45.931  71.645 -12.509  1.00 30.14           C  
ATOM   2281  O   LEU E 295      45.614  72.459 -11.642  1.00 27.68           O  
ATOM   2282  CB  LEU E 295      44.571  69.793 -11.980  1.00 19.00           C  
ATOM   2283  CG  LEU E 295      43.343  68.898 -12.266  1.00 34.60           C  
ATOM   2284  CD1 LEU E 295      43.328  67.685 -11.335  1.00 32.21           C  
ATOM   2285  CD2 LEU E 295      41.951  69.587 -12.218  1.00 20.07           C  
ATOM   2286  N   TYR E 296      47.182  71.354 -12.759  1.00 23.55           N  
ATOM   2287  CA  TYR E 296      48.178  72.127 -11.976  1.00 21.18           C  
ATOM   2288  C   TYR E 296      49.262  72.691 -12.810  1.00 20.71           C  
ATOM   2289  O   TYR E 296      50.172  73.314 -12.278  1.00 29.12           O  
ATOM   2290  CB  TYR E 296      48.939  71.224 -11.041  1.00 27.83           C  
ATOM   2291  CG  TYR E 296      48.000  70.570 -10.154  1.00 30.39           C  
ATOM   2292  CD1 TYR E 296      47.371  71.356  -9.192  1.00 33.18           C  
ATOM   2293  CD2 TYR E 296      47.719  69.214 -10.261  1.00 35.90           C  
ATOM   2294  CE1 TYR E 296      46.503  70.821  -8.245  1.00 27.52           C  
ATOM   2295  CE2 TYR E 296      46.735  68.696  -9.415  1.00 33.56           C  
ATOM   2296  CZ  TYR E 296      46.116  69.496  -8.451  1.00 39.21           C  
ATOM   2297  OH  TYR E 296      45.271  68.913  -7.573  1.00 26.41           O  
ATOM   2298  N   GLY E 297      49.213  72.399 -14.080  1.00 20.95           N  
ATOM   2299  CA  GLY E 297      50.221  72.928 -14.944  1.00 27.26           C  
ATOM   2300  C   GLY E 297      51.404  71.991 -15.252  1.00 16.67           C  
ATOM   2301  O   GLY E 297      51.916  71.253 -14.417  1.00 28.89           O  
ATOM   2302  N   SER E 298      51.774  72.069 -16.524  1.00 21.84           N  
ATOM   2303  CA  SER E 298      52.847  71.233 -16.964  1.00 31.74           C  
ATOM   2304  C   SER E 298      54.200  71.294 -16.248  1.00 29.45           C  
ATOM   2305  O   SER E 298      54.934  70.316 -16.283  1.00 38.17           O  
ATOM   2306  CB  SER E 298      53.012  71.075 -18.441  1.00 70.16           C  
ATOM   2307  OG  SER E 298      53.353  72.327 -18.961  1.00 41.42           O  
ATOM   2308  N   THR E 299      54.520  72.356 -15.578  1.00 25.05           N  
ATOM   2309  CA  THR E 299      55.770  72.412 -14.940  1.00 26.55           C  
ATOM   2310  C   THR E 299      55.509  72.282 -13.532  1.00 29.38           C  
ATOM   2311  O   THR E 299      56.356  72.582 -12.716  1.00 35.48           O  
ATOM   2312  CB  THR E 299      56.447  73.725 -15.326  1.00 45.39           C  
ATOM   2313  OG1 THR E 299      55.653  74.846 -14.923  1.00 35.19           O  
ATOM   2314  CG2 THR E 299      56.502  73.659 -16.854  1.00 62.28           C  
ATOM   2315  N   SER E 300      54.327  71.807 -13.205  1.00 22.18           N  
ATOM   2316  CA  SER E 300      54.129  71.591 -11.747  1.00 20.64           C  
ATOM   2317  C   SER E 300      54.898  70.369 -11.141  1.00 17.26           C  
ATOM   2318  O   SER E 300      55.269  69.369 -11.764  1.00 26.36           O  
ATOM   2319  CB  SER E 300      52.661  71.313 -11.392  1.00 21.85           C  
ATOM   2320  OG  SER E 300      52.193  70.308 -12.260  1.00 25.19           O  
ATOM   2321  N   GLN E 301      55.065  70.458  -9.832  1.00 18.26           N  
ATOM   2322  CA  GLN E 301      55.630  69.385  -9.125  1.00 28.64           C  
ATOM   2323  C   GLN E 301      54.653  68.208  -9.158  1.00 35.29           C  
ATOM   2324  O   GLN E 301      55.044  67.078  -8.972  1.00 25.91           O  
ATOM   2325  CB  GLN E 301      55.656  69.828  -7.644  1.00 21.93           C  
ATOM   2326  CG  GLN E 301      56.028  68.669  -6.662  1.00 24.56           C  
ATOM   2327  CD  GLN E 301      57.475  68.172  -6.866  1.00 42.56           C  
ATOM   2328  OE1 GLN E 301      57.796  67.082  -7.456  1.00 36.65           O  
ATOM   2329  NE2 GLN E 301      58.387  68.948  -6.304  1.00 40.17           N  
ATOM   2330  N   GLU E 302      53.362  68.536  -9.235  1.00 24.81           N  
ATOM   2331  CA  GLU E 302      52.356  67.501  -9.241  1.00 20.75           C  
ATOM   2332  C   GLU E 302      52.608  66.664 -10.461  1.00 19.51           C  
ATOM   2333  O   GLU E 302      52.589  65.462 -10.432  1.00 20.70           O  
ATOM   2334  CB  GLU E 302      50.902  68.094  -9.279  1.00 20.52           C  
ATOM   2335  CG  GLU E 302      50.458  68.677  -7.907  1.00 18.98           C  
ATOM   2336  CD  GLU E 302      50.987  70.069  -7.660  1.00 29.06           C  
ATOM   2337  OE1 GLU E 302      51.694  70.646  -8.483  1.00 23.89           O  
ATOM   2338  OE2 GLU E 302      50.702  70.537  -6.480  1.00 31.68           O  
ATOM   2339  N   VAL E 303      52.812  67.306 -11.528  1.00 17.77           N  
ATOM   2340  CA  VAL E 303      53.044  66.522 -12.657  1.00 14.10           C  
ATOM   2341  C   VAL E 303      54.320  65.697 -12.519  1.00 27.89           C  
ATOM   2342  O   VAL E 303      54.464  64.550 -12.980  1.00 18.65           O  
ATOM   2343  CB  VAL E 303      53.186  67.424 -13.875  1.00 21.60           C  
ATOM   2344  CG1 VAL E 303      53.794  66.735 -15.088  1.00 18.53           C  
ATOM   2345  CG2 VAL E 303      51.817  67.886 -14.310  1.00 24.96           C  
ATOM   2346  N   ALA E 304      55.280  66.341 -11.947  1.00 17.98           N  
ATOM   2347  CA  ALA E 304      56.568  65.692 -11.826  1.00 24.13           C  
ATOM   2348  C   ALA E 304      56.411  64.475 -10.967  1.00 27.23           C  
ATOM   2349  O   ALA E 304      57.002  63.470 -11.331  1.00 26.90           O  
ATOM   2350  CB  ALA E 304      57.572  66.660 -11.204  1.00 23.98           C  
ATOM   2351  N   SER E 305      55.652  64.532  -9.872  1.00 17.66           N  
ATOM   2352  CA  SER E 305      55.505  63.334  -9.004  1.00 19.64           C  
ATOM   2353  C   SER E 305      54.745  62.217  -9.638  1.00 23.58           C  
ATOM   2354  O   SER E 305      55.092  61.056  -9.414  1.00 17.63           O  
ATOM   2355  CB  SER E 305      54.790  63.604  -7.743  1.00 21.42           C  
ATOM   2356  OG  SER E 305      55.611  64.480  -7.048  1.00 27.84           O  
ATOM   2357  N   VAL E 306      53.708  62.580 -10.403  1.00 20.37           N  
ATOM   2358  CA  VAL E 306      53.018  61.525 -11.098  1.00 17.76           C  
ATOM   2359  C   VAL E 306      54.035  60.818 -12.038  1.00 39.80           C  
ATOM   2360  O   VAL E 306      54.063  59.584 -12.153  1.00 19.98           O  
ATOM   2361  CB  VAL E 306      51.897  62.076 -11.936  1.00 17.84           C  
ATOM   2362  CG1 VAL E 306      51.360  61.088 -12.928  1.00 14.33           C  
ATOM   2363  CG2 VAL E 306      50.815  62.547 -10.993  1.00 18.87           C  
ATOM   2364  N   LYS E 307      54.900  61.536 -12.769  1.00 23.33           N  
ATOM   2365  CA  LYS E 307      55.884  60.820 -13.682  1.00 20.02           C  
ATOM   2366  C   LYS E 307      56.870  59.884 -12.963  1.00 17.08           C  
ATOM   2367  O   LYS E 307      57.179  58.749 -13.333  1.00 20.86           O  
ATOM   2368  CB  LYS E 307      56.686  61.864 -14.408  1.00 16.03           C  
ATOM   2369  CG  LYS E 307      55.951  62.280 -15.619  1.00 21.72           C  
ATOM   2370  CD  LYS E 307      56.505  63.586 -16.080  1.00 33.46           C  
ATOM   2371  CE  LYS E 307      56.069  63.825 -17.496  1.00100.00           C  
ATOM   2372  NZ  LYS E 307      56.364  65.181 -17.959  1.00100.00           N  
ATOM   2373  N   GLN E 308      57.402  60.417 -11.886  1.00 17.35           N  
ATOM   2374  CA  GLN E 308      58.345  59.645 -11.064  1.00 15.27           C  
ATOM   2375  C   GLN E 308      57.719  58.359 -10.507  1.00 24.60           C  
ATOM   2376  O   GLN E 308      58.407  57.358 -10.373  1.00 18.32           O  
ATOM   2377  CB  GLN E 308      58.675  60.371  -9.756  1.00 19.78           C  
ATOM   2378  CG  GLN E 308      59.831  61.391  -9.850  1.00100.00           C  
ATOM   2379  CD  GLN E 308      61.188  60.826 -10.270  1.00100.00           C  
ATOM   2380  OE1 GLN E 308      62.023  60.405  -9.442  1.00100.00           O  
ATOM   2381  NE2 GLN E 308      61.435  60.861 -11.574  1.00100.00           N  
ATOM   2382  N   ALA E 309      56.476  58.486 -10.003  1.00 19.22           N  
ATOM   2383  CA  ALA E 309      55.797  57.345  -9.416  1.00 17.40           C  
ATOM   2384  C   ALA E 309      55.590  56.326 -10.508  1.00 17.87           C  
ATOM   2385  O   ALA E 309      55.876  55.164 -10.382  1.00 17.22           O  
ATOM   2386  CB  ALA E 309      54.478  57.798  -8.895  1.00 16.08           C  
ATOM   2387  N   PHE E 310      55.160  56.679 -11.676  1.00 15.75           N  
ATOM   2388  CA  PHE E 310      55.068  55.567 -12.629  1.00 10.03           C  
ATOM   2389  C   PHE E 310      56.461  55.060 -13.061  1.00 23.36           C  
ATOM   2390  O   PHE E 310      56.664  53.913 -13.399  1.00 18.04           O  
ATOM   2391  CB  PHE E 310      54.301  55.992 -13.910  1.00 16.49           C  
ATOM   2392  CG  PHE E 310      52.784  55.973 -13.620  1.00 20.01           C  
ATOM   2393  CD1 PHE E 310      52.035  54.807 -13.779  1.00 20.57           C  
ATOM   2394  CD2 PHE E 310      52.120  57.080 -13.103  1.00 21.68           C  
ATOM   2395  CE1 PHE E 310      50.648  54.760 -13.562  1.00 21.81           C  
ATOM   2396  CE2 PHE E 310      50.758  57.024 -12.790  1.00 21.15           C  
ATOM   2397  CZ  PHE E 310      50.002  55.885 -13.067  1.00 20.41           C  
ATOM   2398  N   ASP E 311      57.429  55.937 -13.189  1.00 17.07           N  
ATOM   2399  CA  ASP E 311      58.737  55.414 -13.542  1.00 17.78           C  
ATOM   2400  C   ASP E 311      59.199  54.444 -12.423  1.00 14.47           C  
ATOM   2401  O   ASP E 311      59.773  53.366 -12.682  1.00 20.14           O  
ATOM   2402  CB  ASP E 311      59.811  56.550 -13.488  1.00 18.05           C  
ATOM   2403  CG  ASP E 311      59.790  57.396 -14.711  1.00 24.18           C  
ATOM   2404  OD1 ASP E 311      59.147  57.089 -15.677  1.00 27.09           O  
ATOM   2405  OD2 ASP E 311      60.493  58.504 -14.620  1.00 38.13           O  
ATOM   2406  N   ALA E 312      58.928  54.744 -11.140  1.00 13.27           N  
ATOM   2407  CA  ALA E 312      59.342  53.842 -10.135  1.00 13.28           C  
ATOM   2408  C   ALA E 312      58.720  52.451 -10.204  1.00 20.83           C  
ATOM   2409  O   ALA E 312      59.383  51.551  -9.752  1.00 19.21           O  
ATOM   2410  CB  ALA E 312      59.106  54.436  -8.776  1.00 14.44           C  
ATOM   2411  N   VAL E 313      57.502  52.225 -10.765  1.00 16.16           N  
ATOM   2412  CA  VAL E 313      56.927  50.891 -10.858  1.00 15.57           C  
ATOM   2413  C   VAL E 313      57.116  50.367 -12.241  1.00 17.42           C  
ATOM   2414  O   VAL E 313      56.629  49.290 -12.656  1.00 20.85           O  
ATOM   2415  CB  VAL E 313      55.455  50.904 -10.442  1.00 12.06           C  
ATOM   2416  CG1 VAL E 313      55.308  51.233  -8.982  1.00 14.80           C  
ATOM   2417  CG2 VAL E 313      54.540  51.757 -11.357  1.00 16.08           C  
ATOM   2418  N   GLY E 314      57.899  51.106 -13.008  1.00 16.61           N  
ATOM   2419  CA  GLY E 314      58.207  50.506 -14.258  1.00 14.00           C  
ATOM   2420  C   GLY E 314      57.223  50.640 -15.323  1.00 20.80           C  
ATOM   2421  O   GLY E 314      57.316  49.971 -16.362  1.00 18.53           O  
ATOM   2422  N   VAL E 315      56.348  51.642 -15.173  1.00 21.04           N  
ATOM   2423  CA  VAL E 315      55.383  51.877 -16.215  1.00 17.27           C  
ATOM   2424  C   VAL E 315      55.734  53.104 -17.084  1.00 19.91           C  
ATOM   2425  O   VAL E 315      55.685  54.272 -16.674  1.00 22.80           O  
ATOM   2426  CB  VAL E 315      53.976  52.029 -15.617  1.00 20.00           C  
ATOM   2427  CG1 VAL E 315      52.970  52.232 -16.737  1.00 20.79           C  
ATOM   2428  CG2 VAL E 315      53.566  50.717 -15.016  1.00 16.37           C  
ATOM   2429  N   LYS E 316      55.962  52.774 -18.334  1.00 20.06           N  
ATOM   2430  CA  LYS E 316      56.262  53.731 -19.301  1.00 34.69           C  
ATOM   2431  C   LYS E 316      55.120  53.968 -20.277  1.00 42.75           C  
ATOM   2432  O   LYS E 316      55.127  55.146 -20.735  1.00 40.40           O  
ATOM   2433  CB  LYS E 316      57.609  53.352 -19.817  1.00 49.26           C  
ATOM   2434  CG  LYS E 316      58.600  54.371 -19.209  1.00100.00           C  
ATOM   2435  CD  LYS E 316      59.423  54.189 -17.905  1.00 72.64           C  
ATOM   2436  CE  LYS E 316      60.240  55.506 -17.654  1.00100.00           C  
ATOM   2437  NZ  LYS E 316      61.738  55.495 -17.614  1.00100.00           N  
ATOM   2438  OXT LYS E 316      54.349  52.974 -20.478  1.00 49.75           O  
TER    2439      LYS E 316                                                      
HETATM 2440  N   VAL E1322      35.454  41.874  -3.978  1.00 24.29           N  
HETATM 2441  CA  VAL E1322      36.635  42.440  -3.303  1.00 27.04           C  
HETATM 2442  C   VAL E1322      37.884  41.618  -3.599  1.00 68.39           C  
HETATM 2443  O   VAL E1322      38.953  42.165  -3.667  1.00 21.34           O  
HETATM 2444  CB  VAL E1322      36.553  42.741  -1.798  1.00 26.94           C  
HETATM 2445  CG1 VAL E1322      36.660  41.454  -0.955  1.00 31.09           C  
HETATM 2446  CG2 VAL E1322      37.585  43.877  -1.388  1.00 18.44           C  
HETATM 2447  N   LYS E1323      37.771  40.284  -3.763  1.00 24.29           N  
HETATM 2448  CA  LYS E1323      38.936  39.307  -4.008  1.00 35.31           C  
HETATM 2449  C   LYS E1323      38.768  38.247  -5.148  1.00 31.13           C  
HETATM 2450  O   LYS E1323      37.580  38.233  -5.689  1.00 27.62           O  
HETATM 2451  CB  LYS E1323      39.396  38.642  -2.738  1.00 34.48           C  
HETATM 2452  CG  LYS E1323      38.307  37.936  -2.011  1.00 39.74           C  
HETATM 2453  CD  LYS E1323      38.970  36.886  -1.176  1.00 52.87           C  
HETATM 2454  CE  LYS E1323      38.645  35.509  -1.680  1.00 74.69           C  
HETATM 2455  NZ  LYS E1323      37.278  35.119  -1.325  1.00 65.28           N  
HETATM 2456  OXT LYS E1323      39.804  37.557  -5.482  1.00100.00           O  
HETATM 2457 CA    CA E 317      41.929  49.904   4.912  1.00 14.91          CA  
HETATM 2458 CA    CA E 318      41.643  50.919   8.542  1.00 16.44          CA  
HETATM 2459 CA    CA E 319      14.600  45.917  15.744  1.00 15.09          CA  
HETATM 2460 CA    CA E 320      42.980  39.755  10.425  1.00 20.58          CA  
HETATM 2461 ZN    ZN E 321      36.921  44.908  -7.111  1.00 16.45          ZN  
HETATM 2462  S   DMS E 324      63.493  46.221 -11.718  1.00 62.04           S  
HETATM 2463  O   DMS E 324      64.265  45.747 -12.880  1.00 57.40           O  
HETATM 2464  C1  DMS E 324      64.594  47.010 -10.655  1.00 40.80           C  
HETATM 2465  C2  DMS E 324      62.936  44.782 -10.848  1.00 56.27           C  
HETATM 2466  O   HOH E 331      50.895  48.828 -20.309  1.00 20.85           O  
HETATM 2467  O   HOH E 332      25.716  40.588 -12.651  1.00 30.00           O  
HETATM 2468  O   HOH E 334      36.637  50.614 -10.210  1.00 14.79           O  
HETATM 2469  O   HOH E 335      39.242  66.053 -10.444  1.00 19.52           O  
HETATM 2470  O   HOH E 337      20.581  42.207  -8.931  1.00 26.06           O  
HETATM 2471  O   HOH E 338      20.915  58.124  -4.657  1.00 25.57           O  
HETATM 2472  O   HOH E 339      27.469  60.816  -4.666  1.00 18.54           O  
HETATM 2473  O   HOH E 340      47.930  46.188  -3.742  1.00 19.16           O  
HETATM 2474  O   HOH E 341      19.294  30.259  -3.371  1.00 21.19           O  
HETATM 2475  O   HOH E 342      49.116  43.066  -1.660  1.00 17.57           O  
HETATM 2476  O   HOH E 343      17.270  36.119  -1.513  1.00 25.51           O  
HETATM 2477  O   HOH E 344      22.632  49.858   0.546  1.00 20.40           O  
HETATM 2478  O   HOH E 345      20.383  28.966   2.022  1.00 24.82           O  
HETATM 2479  O   HOH E 346      42.371  51.903   3.303  1.00 13.89           O  
HETATM 2480  O   HOH E 347      27.364  34.416   3.359  1.00 12.98           O  
HETATM 2481  O   HOH E 348      22.511  55.690   4.512  1.00 19.62           O  
HETATM 2482  O   HOH E 349      26.213  39.998   4.774  1.00 13.67           O  
HETATM 2483  O   HOH E 350      38.671  47.103   6.288  1.00 22.66           O  
HETATM 2484  O   HOH E 351      22.052  55.947   7.099  1.00 18.19           O  
HETATM 2485  O   HOH E 352      15.875  59.917   7.557  1.00 20.54           O  
HETATM 2486  O   HOH E 353      39.262  51.212   8.835  1.00 18.87           O  
HETATM 2487  O   HOH E 354      43.054  42.046   9.599  1.00 18.82           O  
HETATM 2488  O   HOH E 355      32.907  48.937  10.716  1.00 18.89           O  
HETATM 2489  O   HOH E 356      15.938  44.024  11.802  1.00 14.53           O  
HETATM 2490  O   HOH E 357      23.781  44.641  15.701  1.00 21.44           O  
HETATM 2491  O   HOH E 359      49.599  62.523 -21.741  1.00 46.01           O  
HETATM 2492  O   HOH E 361      56.504  47.051  -2.348  1.00 33.50           O  
HETATM 2493  O   HOH E 362      32.891  43.444  -7.919  1.00 29.21           O  
HETATM 2494  O   HOH E 366      37.423  66.037  -8.444  1.00 24.18           O  
HETATM 2495  O   HOH E 368      32.394  49.227 -20.885  1.00 28.54           O  
HETATM 2496  O   HOH E 371      53.244  49.751 -19.152  1.00 34.80           O  
HETATM 2497  O   HOH E 373      52.389  67.622 -19.573  1.00 45.20           O  
HETATM 2498  O   HOH E 374      36.636  58.226 -18.918  1.00 26.50           O  
HETATM 2499  O   HOH E 377      27.058  52.383 -18.552  1.00 46.91           O  
HETATM 2500  O   HOH E 379      33.313  48.794 -16.191  1.00 36.67           O  
HETATM 2501  O   HOH E 380      46.272  42.166 -15.079  1.00 35.05           O  
HETATM 2502  O   HOH E 381      52.742  34.830 -15.413  1.00 36.47           O  
HETATM 2503  O   HOH E 383      56.565  69.112 -14.080  1.00 36.11           O  
HETATM 2504  O   HOH E 384      61.758  50.989 -12.138  1.00 41.51           O  
HETATM 2505  O   HOH E 386      19.462  58.305 -12.137  1.00 38.57           O  
HETATM 2506  O   HOH E 387      38.573  37.877 -11.044  1.00 56.65           O  
HETATM 2507  O   HOH E 392      36.341  42.854  -6.770  1.00 20.72           O  
HETATM 2508  O   HOH E 393      22.222  50.179  -6.922  1.00 23.84           O  
HETATM 2509  O   HOH E 395      42.869  45.005  -6.375  1.00 18.41           O  
HETATM 2510  O   HOH E 397      27.193  32.354  -5.782  1.00 36.79           O  
HETATM 2511  O   HOH E 398      47.207  43.769  -5.364  1.00 20.29           O  
HETATM 2512  O   HOH E 403      40.446  64.675  -3.649  1.00 32.66           O  
HETATM 2513  O   HOH E 404      43.469  40.233  -3.222  1.00 34.28           O  
HETATM 2514  O   HOH E 405      39.927  62.417  -2.112  1.00 27.75           O  
HETATM 2515  O   HOH E 407      57.326  63.058  -0.079  1.00 32.70           O  
HETATM 2516  O   HOH E 408      26.520  49.048   0.725  1.00 22.27           O  
HETATM 2517  O   HOH E 410      10.221  43.835   3.030  1.00 36.61           O  
HETATM 2518  O   HOH E 412      11.442  38.916   5.145  1.00 33.89           O  
HETATM 2519  O   HOH E 413      49.044  51.989   6.140  1.00 30.06           O  
HETATM 2520  O   HOH E 414      25.577  33.598   5.281  1.00 27.13           O  
HETATM 2521  O   HOH E 415      12.772  42.070   5.274  1.00 29.97           O  
HETATM 2522  O   HOH E 419      16.295  44.180  15.680  1.00 15.61           O  
HETATM 2523  O   HOH E 420      27.601  43.280  16.026  1.00 61.06           O  
HETATM 2524  O   HOH E 422      10.109  52.304  18.012  1.00 51.32           O  
HETATM 2525  O   HOH E 423       9.398  40.630   5.473  1.00 38.43           O  
HETATM 2526  O   HOH E 424      50.639  73.820 -18.575  1.00 48.67           O  
HETATM 2527  O   HOH E 425      34.156  42.833 -18.377  1.00 26.69           O  
HETATM 2528  O   HOH E 426      55.185  68.232 -18.468  1.00 54.35           O  
HETATM 2529  O   HOH E 428      47.522  38.516 -17.666  1.00 47.44           O  
HETATM 2530  O   HOH E 434      28.475  43.678 -14.662  1.00 26.60           O  
HETATM 2531  O   HOH E 444      55.119  39.145  -7.176  1.00 41.51           O  
HETATM 2532  O   HOH E 450      50.238  36.547  -5.884  1.00 56.80           O  
HETATM 2533  O   HOH E 454      64.911  52.139  -3.430  1.00 22.71           O  
HETATM 2534  O   HOH E 455      63.196  49.881  -3.267  1.00 19.50           O  
HETATM 2535  O   HOH E 457      60.672  49.513  -2.159  1.00 22.96           O  
HETATM 2536  O   HOH E 463      56.201  65.757   0.312  1.00 46.51           O  
HETATM 2537  O   HOH E 464      40.442  61.110   1.633  1.00 33.65           O  
HETATM 2538  O   HOH E 468      15.125  58.350   5.304  1.00 16.83           O  
HETATM 2539  O   HOH E 469      37.955  49.633   6.306  1.00 59.88           O  
HETATM 2540  O   HOH E 470      25.658  57.418   6.421  1.00 29.96           O  
HETATM 2541  O   HOH E 475      41.447  49.645  10.445  1.00 20.62           O  
HETATM 2542  O   HOH E 476      38.544  41.320  11.836  1.00 47.69           O  
HETATM 2543  O   HOH E 477      13.716  42.403  11.604  1.00 28.69           O  
HETATM 2544  O   HOH E 478      15.038  39.884  11.598  1.00 34.75           O  
HETATM 2545  O   HOH E 479      40.943  34.094  11.585  1.00 34.93           O  
HETATM 2546  O   HOH E 480      41.803  40.776  12.023  1.00 32.17           O  
HETATM 2547  O   HOH E 481      31.186  47.965  12.255  1.00 17.59           O  
HETATM 2548  O   HOH E 482      14.764  45.335  17.961  1.00 21.45           O  
HETATM 2549  O   HOH E 483      25.552  43.095  17.648  1.00 61.65           O  
HETATM 2550  O   HOH E 484      17.573  45.319  18.190  1.00 32.57           O  
HETATM 2551  O   HOH E 487      30.569  35.175   9.575  1.00 31.39           O  
HETATM 2552  O   HOH E 491      52.597  63.723   1.307  1.00 35.49           O  
HETATM 2553  O   HOH E 493      58.853  44.890  -0.405  1.00 31.43           O  
HETATM 2554  O   HOH E 495      53.215  32.998 -13.154  1.00 45.82           O  
HETATM 2555  O   HOH E 496      35.817  65.356 -14.545  1.00 35.11           O  
HETATM 2556  O   HOH E 501      30.626  52.275  23.695  1.00 53.04           O  
HETATM 2557  O   HOH E 502      20.250  37.986  15.547  1.00 35.53           O  
HETATM 2558  O   HOH E 503      12.615  44.609  15.672  1.00 19.08           O  
HETATM 2559  O   HOH E 504       9.649  41.873  15.368  1.00 30.04           O  
HETATM 2560  O   HOH E 506      17.484  38.253  14.629  1.00 30.54           O  
HETATM 2561  O   HOH E 507      16.867  40.705  13.381  1.00 24.32           O  
HETATM 2562  O   HOH E 508      11.773  43.271  13.483  1.00 23.36           O  
HETATM 2563  O   HOH E 509      26.157  57.788  13.491  1.00 39.87           O  
HETATM 2564  O   HOH E 512       9.332  62.361   5.944  1.00 33.33           O  
HETATM 2565  O   HOH E 513      49.215  58.129   6.257  1.00 54.53           O  
HETATM 2566  O   HOH E 516      53.035  56.781   4.389  1.00 56.90           O  
HETATM 2567  O   HOH E 519      29.443  27.479   2.694  1.00 56.00           O  
HETATM 2568  O   HOH E 521      24.592  64.129   1.860  1.00 44.24           O  
HETATM 2569  O   HOH E 523      59.704  47.733  -0.296  1.00 49.59           O  
HETATM 2570  O   HOH E 524      57.979  52.834  -0.997  1.00 44.63           O  
HETATM 2571  O   HOH E 525      11.124  43.902  -1.014  1.00 37.09           O  
HETATM 2572  O   HOH E 527      46.752  39.413  -1.845  1.00 40.09           O  
HETATM 2573  O   HOH E 528      46.859  66.735  -1.382  1.00 26.46           O  
HETATM 2574  O   HOH E 531      17.128  63.126  -1.745  1.00 49.99           O  
HETATM 2575  O   HOH E 534      34.793  67.000  -9.902  1.00 34.49           O  
HETATM 2576  O   HOH E 535      17.617  60.347 -11.213  1.00 42.93           O  
HETATM 2577  O   HOH E 536      26.710  64.436 -10.800  1.00 27.40           O  
HETATM 2578  O   HOH E 537      31.715  65.130 -10.867  1.00 35.90           O  
HETATM 2579  O   HOH E 538      33.492  47.604 -12.761  1.00 35.92           O  
HETATM 2580  O   HOH E 539      23.325  49.791 -12.866  1.00 38.26           O  
HETATM 2581  O   HOH E 540      33.723  44.978 -15.093  1.00 41.01           O  
HETATM 2582  O   HOH E 542      51.351  42.869 -19.361  1.00 56.33           O  
HETATM 2583  O   HOH E 543      56.129  50.136 -19.501  1.00 46.31           O  
HETATM 2584  O   HOH E 600      31.351  56.530 -20.880  1.00 36.03           O  
HETATM 2585  O   HOH E 601      14.369  39.042  -4.886  1.00 28.13           O  
HETATM 2586  O   HOH E 602      20.887  38.888  18.469  1.00 29.59           O  
HETATM 2587  O   HOH E 603      50.710  69.090  -2.362  1.00 40.59           O  
HETATM 2588  O   HOH E 604      44.075  37.002  -7.057  1.00 53.44           O  
HETATM 2589  O   HOH E 605      65.023  59.504  -8.036  1.00 44.67           O  
HETATM 2590  O   HOH E 606      45.678  40.238  -4.796  1.00 48.28           O  
HETATM 2591  O   HOH E 607      38.438  67.398 -12.688  1.00 33.67           O  
HETATM 2592  O   HOH E 608      29.082  64.472 -12.520  1.00 46.33           O  
HETATM 2593  O   HOH E 609       9.094  57.579   1.081  1.00 49.45           O  
HETATM 2594  O   HOH E 610      31.516  62.046 -15.056  1.00 47.71           O  
HETATM 2595  O   HOH E 611      39.416  33.929 -14.185  1.00 53.07           O  
HETATM 2596  O   HOH E 612      12.425  47.877  -3.435  1.00 42.31           O  
HETATM 2597  O   HOH E 613      45.818  66.105   1.095  1.00 44.69           O  
HETATM 2598  O   HOH E 614      21.128  24.747   4.923  1.00 56.14           O  
HETATM 2599  O   HOH E 615      27.482  32.282  -8.856  1.00 58.96           O  
HETATM 2600  O   HOH E 619      27.228  38.612 -10.949  0.50 46.82           O  
HETATM 2601  O   HOH E 620      56.239  56.710   2.144  1.00 43.33           O  
HETATM 2602  O   HOH E 621      36.856  64.581   5.806  1.00 75.66           O  
HETATM 2603  O   HOH E 623      28.845  59.566 -15.702  1.00 46.79           O  
HETATM 2604  O   HOH E 624      57.208  54.926   0.816  1.00 57.99           O  
HETATM 2605  O   HOH E 626      55.446  60.721 -19.025  1.00 50.49           O  
HETATM 2606  O   HOH E 628      14.803  41.662  16.251  1.00 63.31           O  
HETATM 2607  O   HOH E 629      15.471  62.605   8.110  1.00 43.19           O  
HETATM 2608  O   HOH E 630      27.753  55.802 -19.266  1.00 56.31           O  
HETATM 2609  O   HOH E 650      35.630  49.727   8.584  1.00 24.89           O  
HETATM 2610  O   HOH E 651      30.131  45.416 -13.635  1.00 36.90           O  
HETATM 2611  O   HOH E 652      33.183  31.568  -0.051  1.00 37.52           O  
HETATM 2612  O   HOH E 653      52.427  56.623 -21.366  1.00 39.79           O  
HETATM 2613  O   HOH E 654      34.913  61.464 -20.527  1.00 50.51           O  
HETATM 2614  O   HOH E 655      17.403  55.712  -9.361  1.00 45.76           O  
HETATM 2615  O   HOH E 656      15.354  54.311  17.613  1.00 51.34           O  
HETATM 2616  O   HOH E 657      35.897  40.021 -17.815  1.00 73.10           O  
HETATM 2617  O   HOH E 658      49.578  50.291   4.666  1.00 39.11           O  
HETATM 2618  O   HOH E 659      59.887  48.153 -15.862  1.00100.00           O  
HETATM 2619  O   HOH E 660      59.711  60.275 -16.586  1.00 50.96           O  
HETATM 2620  O   HOH E 670      11.397  64.478   6.146  1.00 58.96           O  
HETATM 2621  O   HOH E 671      14.678  42.689  19.398  1.00 62.62           O  
HETATM 2622  O   HOH E 672      45.242  58.430 -22.282  1.00 67.71           O  
CONECT  448 2459                                                                
CONECT  449 2459                                                                
CONECT  461 2459                                                                
CONECT  474 2459                                                                
CONECT 1086 2457                                                                
CONECT 1115 2461                                                                
CONECT 1149 2461                                                                
CONECT 1299 2461                                                                
CONECT 1379 2457                                                                
CONECT 1380 2457 2458                                                           
CONECT 1429 2458                                                                
CONECT 1447 2457                                                                
CONECT 1448 2458                                                                
CONECT 1466 2457                                                                
CONECT 1491 2457                                                                
CONECT 1492 2457 2458                                                           
CONECT 1511 2460                                                                
CONECT 1523 2460                                                                
CONECT 1525 2460                                                                
CONECT 1541 2460                                                                
CONECT 1562 2460                                                                
CONECT 2442 2447                                                                
CONECT 2447 2442                                                                
CONECT 2457 1086 1379 1380 1447                                                 
CONECT 2457 1466 1491 1492 2479                                                 
CONECT 2458 1380 1429 1448 1492                                                 
CONECT 2458 2486 2541                                                           
CONECT 2459  448  449  461  474                                                 
CONECT 2459 2522 2548 2558                                                      
CONECT 2460 1511 1523 1525 1541                                                 
CONECT 2460 1562 2487 2546                                                      
CONECT 2461 1115 1149 1299 2507                                                 
CONECT 2462 2463 2464 2465                                                      
CONECT 2463 2462                                                                
CONECT 2464 2462                                                                
CONECT 2465 2462                                                                
CONECT 2479 2457                                                                
CONECT 2486 2458                                                                
CONECT 2487 2460                                                                
CONECT 2507 2461                                                                
CONECT 2522 2459                                                                
CONECT 2541 2458                                                                
CONECT 2546 2460                                                                
CONECT 2548 2459                                                                
CONECT 2558 2459                                                                
MASTER      512    0    8   12   15    0   13    6 2615    1   45   25          
END                                                                             


A second structure was input as follows:


HEADER    HYDROLASE                               20-NOV-18   6N4W              
TITLE     TETRAGONAL THERMOLYSIN (WITH 50% XYLOSE) CRYOCOOLED IN A NITROGEN GAS 
TITLE    2 STREAM TO 100 K                                                      
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: THERMOLYSIN;                                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: THERMOSTABLE NEUTRAL PROTEINASE;                            
COMPND   5 EC: 3.4.24.27;                                                       
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS THERMOPROTEOLYTICUS;                   
SOURCE   3 ORGANISM_TAXID: 1427;                                                
SOURCE   4 GENE: NPR;                                                           
SOURCE   5 EXPRESSION_SYSTEM: BACILLUS THERMOPROTEOLYTICUS;                     
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 1427                                        
KEYWDS    ZINC PROTEASE, HYDROLASE                                              
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    D.H.JUERS,K.HARRISON,B.WU                                             
REVDAT   3   01-JAN-20 6N4W    1       REMARK                                   
REVDAT   2   06-NOV-19 6N4W    1       JRNL                                     
REVDAT   1   02-OCT-19 6N4W    0                                                
JRNL        AUTH   K.HARRISON,Z.WU,D.H.JUERS                                    
JRNL        TITL   A COMPARISON OF GAS STREAM COOLING AND PLUNGE COOLING OF     
JRNL        TITL 2 MACROMOLECULAR CRYSTALS.                                     
JRNL        REF    J.APPL.CRYSTALLOGR.           V.  52  1222 2019              
JRNL        REFN                   ISSN 0021-8898                               
JRNL        PMID   31636524                                                     
JRNL        DOI    10.1107/S1600576719010318                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX 1.14_3260                                     
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VINCENT CHEN,IAN            
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-KUNSTLEVE,           
REMARK   3               : LI-WEI HUNG,ROBERT IMMORMINO,TOM IOERGER,            
REMARK   3               : AIRLIE MCCOY,ERIK MCKEE,NIGEL MORIARTY,              
REMARK   3               : REETAL PAI,RANDY READ,JANE RICHARDSON,               
REMARK   3               : DAVID RICHARDSON,TOD ROMO,JIM SACCHETTINI,           
REMARK   3               : NICHOLAS SAUTER,JACOB SMITH,LAURENT                  
REMARK   3               : STORONI,TOM TERWILLIGER,PETER ZWART                  
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : NULL                                          
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.59                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.330                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.7                           
REMARK   3   NUMBER OF REFLECTIONS             : 99135                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.139                           
REMARK   3   R VALUE            (WORKING SET) : 0.138                           
REMARK   3   FREE R VALUE                     : 0.157                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.940                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 4893                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 30.6000 -  4.3500    1.00     3416   191  0.1691 0.1658        
REMARK   3     2  4.3500 -  3.4500    1.00     3267   159  0.1137 0.1171        
REMARK   3     3  3.4500 -  3.0200    1.00     3233   173  0.1232 0.1468        
REMARK   3     4  3.0200 -  2.7400    1.00     3177   186  0.1163 0.1396        
REMARK   3     5  2.7400 -  2.5400    1.00     3185   159  0.1087 0.1291        
REMARK   3     6  2.5400 -  2.3900    1.00     3182   174  0.1118 0.1251        
REMARK   3     7  2.3900 -  2.2700    1.00     3158   166  0.1048 0.1171        
REMARK   3     8  2.2700 -  2.1700    1.00     3144   181  0.1042 0.1311        
REMARK   3     9  2.1700 -  2.0900    1.00     3162   149  0.1094 0.1428        
REMARK   3    10  2.0900 -  2.0200    1.00     3128   177  0.1166 0.1409        
REMARK   3    11  2.0200 -  1.9600    1.00     3150   177  0.1164 0.1424        
REMARK   3    12  1.9600 -  1.9000    1.00     3120   154  0.1173 0.1489        
REMARK   3    13  1.9000 -  1.8500    1.00     3175   152  0.1192 0.1379        
REMARK   3    14  1.8500 -  1.8000    1.00     3141   132  0.1218 0.1438        
REMARK   3    15  1.8000 -  1.7600    1.00     3162   157  0.1280 0.1694        
REMARK   3    16  1.7600 -  1.7300    1.00     3114   155  0.1331 0.1636        
REMARK   3    17  1.7300 -  1.6900    1.00     3113   173  0.1480 0.1944        
REMARK   3    18  1.6900 -  1.6600    1.00     3098   206  0.1544 0.1855        
REMARK   3    19  1.6600 -  1.6300    1.00     3124   155  0.1628 0.1731        
REMARK   3    20  1.6300 -  1.6000    1.00     3116   145  0.1717 0.2143        
REMARK   3    21  1.6000 -  1.5800    1.00     3112   173  0.1816 0.2153        
REMARK   3    22  1.5800 -  1.5500    1.00     3104   173  0.1923 0.1917        
REMARK   3    23  1.5500 -  1.5300    1.00     3112   161  0.1993 0.2304        
REMARK   3    24  1.5300 -  1.5100    1.00     3111   159  0.2125 0.2448        
REMARK   3    25  1.5100 -  1.4900    0.99     3069   158  0.2309 0.2710        
REMARK   3    26  1.4900 -  1.4700    0.99     3109   142  0.2460 0.2984        
REMARK   3    27  1.4700 -  1.4500    0.99     3126   149  0.2671 0.2881        
REMARK   3    28  1.4500 -  1.4300    0.99     3068   154  0.2894 0.3071        
REMARK   3    29  1.4300 -  1.4200    0.98     3062   149  0.3127 0.3660        
REMARK   3    30  1.4200 -  1.4000    0.97     3004   154  0.3390 0.3781        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : NULL                                          
REMARK   3   SOLVENT RADIUS     : 1.11                                          
REMARK   3   SHRINKAGE RADIUS   : 0.90                                          
REMARK   3   K_SOL              : NULL                                          
REMARK   3   B_SOL              : NULL                                          
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.159            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 16.334           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 15.58                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 21.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.006           2865                                  
REMARK   3   ANGLE     :  0.899           3946                                  
REMARK   3   CHIRALITY :  0.076            448                                  
REMARK   3   PLANARITY :  0.006            509                                  
REMARK   3   DIHEDRAL  : 12.984           1027                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 6N4W COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 26-NOV-18.                  
REMARK 100 THE DEPOSITION ID IS D_1000238178.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 18-OCT-18                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : SEALED TUBE                        
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : OXFORD DIFFRACTION NOVA            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : OXFORD ONYX CCD                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : CRYSALISPRO 1.14_3260              
REMARK 200  DATA SCALING SOFTWARE          : CRYSALISPRO                        
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 99213                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.590                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 11.80                              
REMARK 200  R MERGE                    (I) : 0.07900                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.45                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.20                               
REMARK 200  R MERGE FOR SHELL          (I) : 2.62000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 0.790                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SAD                          
REMARK 200 SOFTWARE USED: PHENIX                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 66.05                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.62                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PROTEIN DROP: 75 MG/ML PROTEIN IN 45%    
REMARK 280  DMSO/0.5 M ZNCL2, WELL SOLUTION: 1 M AMMONIUM SULFATE, VAPOR        
REMARK 280  DIFFUSION, TEMPERATURE 295K                                         
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       53.21250            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       48.36950            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       48.36950            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       26.60625            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       48.36950            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       48.36950            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       79.81875            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       48.36950            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       48.36950            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       26.60625            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       48.36950            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       48.36950            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000       79.81875            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       53.21250            
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: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
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 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   HG   SER A   282     OXT  LYS A   316              1.55            
REMARK 500   HZ1  LYS A   239    ZN     ZN A   410              1.58            
REMARK 500   O    HOH A   644     O    HOH A   712              1.97            
REMARK 500   O    HOH A   756     O    HOH A   838              1.98            
REMARK 500   O    HOH A   711     O    HOH A   887              2.13            
REMARK 500   O    HOH A   747     O    HOH A   785              2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS                                             
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS THAT ARE RELATED BY CRYSTALLOGRAPHIC             
REMARK 500 SYMMETRY ARE IN CLOSE CONTACT.  AN ATOM LOCATED WITHIN 0.15          
REMARK 500 ANGSTROMS OF A SYMMETRY RELATED ATOM IS ASSUMED TO BE ON A           
REMARK 500 SPECIAL POSITION AND IS, THEREFORE, LISTED IN REMARK 375             
REMARK 500 INSTEAD OF REMARK 500.  ATOMS WITH NON-BLANK ALTERNATE               
REMARK 500 LOCATION INDICATORS ARE NOT INCLUDED IN THE CALCULATIONS.            
REMARK 500                                                                      
REMARK 500 DISTANCE CUTOFF:                                                     
REMARK 500 2.2 ANGSTROMS FOR CONTACTS NOT INVOLVING HYDROGEN ATOMS              
REMARK 500 1.6 ANGSTROMS FOR CONTACTS INVOLVING HYDROGEN ATOMS                  
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI  SSYMOP   DISTANCE          
REMARK 500   O    HOH A   848     O    HOH A   890     4464     1.96            
REMARK 500   O    HOH A   864     O    HOH A   877     6465     2.02            
REMARK 500   O    HOH A   824     O    HOH A   876     3655     2.16            
REMARK 500   O    HOH A   854     O    HOH A   874     3655     2.17            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  26      -56.12     70.76                                   
REMARK 500    SER A  92     -175.69     61.08                                   
REMARK 500    SER A 107     -159.73     59.92                                   
REMARK 500    ASN A 111       56.32    -93.32                                   
REMARK 500    THR A 152      -95.07   -125.60                                   
REMARK 500    ILE A 156     -175.90    -65.66                                   
REMARK 500    TYR A 157       36.99    -84.59                                   
REMARK 500    ASN A 159     -145.33     56.98                                   
REMARK 500    ASN A 183       58.21   -145.16                                   
REMARK 500    THR A 194       75.11     43.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 924        DISTANCE =  5.84 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 402  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  57   OD1                                                    
REMARK 620 2 ASP A  57   OD2  52.4                                              
REMARK 620 3 ASP A  59   OD1  70.2 122.4                                        
REMARK 620 4 GLN A  61   O    87.8  92.9  89.6                                  
REMARK 620 5 HOH A 577   O   147.3 157.8  77.5  97.4                            
REMARK 620 6 HOH A 646   O   134.4  83.5 153.5  83.0  78.3                      
REMARK 620 7 HOH A 814   O    89.1  86.3  87.9 176.5  84.5 100.3                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 401  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 138   OD2                                                    
REMARK 620 2 GLU A 177   OE1  79.0                                              
REMARK 620 3 GLU A 177   OE2 128.6  50.3                                        
REMARK 620 4 ASP A 185   OD1 157.8 122.4  72.2                                  
REMARK 620 5 GLU A 187   O    84.0 147.7 143.4  79.3                            
REMARK 620 6 GLU A 190   OE1  82.5 128.1 119.5  79.4  75.8                      
REMARK 620 7 GLU A 190   OE2  98.8  83.1  70.4  80.1 126.9  52.6                
REMARK 620 8 HOH A 645   O   101.3  80.6  80.8  88.8  76.0 150.9 151.1          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 404  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 142   NE2                                                    
REMARK 620 2 HIS A 146   NE2 104.5                                              
REMARK 620 3 GLU A 166   OE1  97.0 108.3                                        
REMARK 620 4 GLU A 166   OE2 119.4  98.9  22.5                                  
REMARK 620 5 HOH A 738   O   115.2 116.4 113.3 101.8                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 409  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 143   OE2                                                    
REMARK 620 2 HOH A 636   O   114.9                                              
REMARK 620 3 HOH A 738   O   105.4 131.3                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 406  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GLU A 177   OE2                                                    
REMARK 620 2 ASN A 183   O    94.3                                              
REMARK 620 3 ASN A 183   O    94.7   0.4                                        
REMARK 620 4 ASP A 185   OD2  91.3  88.1  88.0                                  
REMARK 620 5 GLU A 190   OE2  89.8 175.5 175.2  93.7                            
REMARK 620 6 HOH A 536   O    86.3  86.0  86.1 173.4  92.4                      
REMARK 620 7 HOH A 555   O   175.7  83.4  83.0  92.3  92.4  89.8                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A 403  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 193   O                                                      
REMARK 620 2 THR A 194   O    76.2                                              
REMARK 620 3 THR A 194   OG1  74.9  71.4                                        
REMARK 620 4 ILE A 197   O   154.6  80.3 106.5                                  
REMARK 620 5 ASP A 200   OD1 120.6 133.8  72.8  82.9                            
REMARK 620 6 HOH A 792   O    85.5  80.9 149.0  81.4 138.2                      
REMARK 620 7 HOH A 565   O    85.6 153.0 123.0 112.6  72.8  78.0                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 408  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A 226   OD1                                                    
REMARK 620 2 HIS A 231   ND1  89.8                                              
REMARK 620 N                    1                                               
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 407  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS A 231   NE2                                                    
REMARK 620 2 HOH A 840   O   124.1                                              
REMARK 620 3 HOH A 738   O   123.4 112.4                                        
REMARK 620 N                    1     2                                         
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              ZN A 410  ZN                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 LYS A 239   NZ                                                     
REMARK 620 2 HOH A 527   O   131.1                                              
REMARK 620 N                    1                                               
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 401                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 402                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue CA A 403                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 404                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 405                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 406                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 407                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 408                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 409                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue ZN A 410                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 412                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 413                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 414                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 415                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 416                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 417                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AD9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 418                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYP A 419                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYS A 420                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AE3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue XYS A 421                 
DBREF  6N4W A    1   316  UNP    P00800   THER_BACTH     233    548             
SEQRES   1 A  316  ILE THR GLY THR SER THR VAL GLY VAL GLY ARG GLY VAL          
SEQRES   2 A  316  LEU GLY ASP GLN LYS ASN ILE ASN THR THR TYR SER THR          
SEQRES   3 A  316  TYR TYR TYR LEU GLN ASP ASN THR ARG GLY ASN GLY ILE          
SEQRES   4 A  316  PHE THR TYR ASP ALA LYS TYR ARG THR THR LEU PRO GLY          
SEQRES   5 A  316  SER LEU TRP ALA ASP ALA ASP ASN GLN PHE PHE ALA SER          
SEQRES   6 A  316  TYR ASP ALA PRO ALA VAL ASP ALA HIS TYR TYR ALA GLY          
SEQRES   7 A  316  VAL THR TYR ASP TYR TYR LYS ASN VAL HIS ASN ARG LEU          
SEQRES   8 A  316  SER TYR ASP GLY ASN ASN ALA ALA ILE ARG SER SER VAL          
SEQRES   9 A  316  HIS TYR SER GLN GLY TYR ASN ASN ALA PHE TRP ASN GLY          
SEQRES  10 A  316  SER GLN MET VAL TYR GLY ASP GLY ASP GLY GLN THR PHE          
SEQRES  11 A  316  ILE PRO LEU SER GLY GLY ILE ASP VAL VAL ALA HIS GLU          
SEQRES  12 A  316  LEU THR HIS ALA VAL THR ASP TYR THR ALA GLY LEU ILE          
SEQRES  13 A  316  TYR GLN ASN GLU SER GLY ALA ILE ASN GLU ALA ILE SER          
SEQRES  14 A  316  ASP ILE PHE GLY THR LEU VAL GLU PHE TYR ALA ASN LYS          
SEQRES  15 A  316  ASN PRO ASP TRP GLU ILE GLY GLU ASP VAL TYR THR PRO          
SEQRES  16 A  316  GLY ILE SER GLY ASP SER LEU ARG SER MET SER ASP PRO          
SEQRES  17 A  316  ALA LYS TYR GLY ASP PRO ASP HIS TYR SER LYS ARG TYR          
SEQRES  18 A  316  THR GLY THR GLN ASP ASN GLY GLY VAL HIS ILE ASN SER          
SEQRES  19 A  316  GLY ILE ILE ASN LYS ALA ALA TYR LEU ILE SER GLN GLY          
SEQRES  20 A  316  GLY THR HIS TYR GLY VAL SER VAL VAL GLY ILE GLY ARG          
SEQRES  21 A  316  ASP LYS LEU GLY LYS ILE PHE TYR ARG ALA LEU THR GLN          
SEQRES  22 A  316  TYR LEU THR PRO THR SER ASN PHE SER GLN LEU ARG ALA          
SEQRES  23 A  316  ALA ALA VAL GLN SER ALA THR ASP LEU TYR GLY SER THR          
SEQRES  24 A  316  SER GLN GLU VAL ALA SER VAL LYS GLN ALA PHE ASP ALA          
SEQRES  25 A  316  VAL GLY VAL LYS                                              
HET     CA  A 401       1                                                       
HET     CA  A 402       1                                                       
HET     CA  A 403       1                                                       
HET     ZN  A 404       1                                                       
HET     ZN  A 405       1                                                       
HET     ZN  A 406       1                                                       
HET     ZN  A 407       1                                                       
HET     ZN  A 408       1                                                       
HET     ZN  A 409       1                                                       
HET     ZN  A 410       1                                                       
HET    XYP  A 411      20                                                       
HET    XYP  A 412      20                                                       
HET    XYP  A 413      20                                                       
HET    XYP  A 414      20                                                       
HET    XYP  A 415      20                                                       
HET    XYP  A 416      20                                                       
HET    XYP  A 417      20                                                       
HET    XYP  A 418      20                                                       
HET    XYP  A 419      20                                                       
HET    XYS  A 420      18                                                       
HET    XYS  A 421      18                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM      ZN ZINC ION                                                         
HETNAM     XYP BETA-D-XYLOPYRANOSE                                              
HETNAM     XYS XYLOPYRANOSE                                                     
FORMUL   2   CA    3(CA 2+)                                                     
FORMUL   5   ZN    7(ZN 2+)                                                     
FORMUL  12  XYP    9(C5 H10 O5)                                                 
FORMUL  21  XYS    2(C5 H10 O5)                                                 
FORMUL  23  HOH   *424(H2 O)                                                    
HELIX    1 AA1 ALA A   64  TYR A   66  5                                   3    
HELIX    2 AA2 ASP A   67  ASN A   89  1                                  23    
HELIX    3 AA3 PRO A  132  GLY A  135  5                                   4    
HELIX    4 AA4 GLY A  136  TYR A  151  1                                  16    
HELIX    5 AA5 GLN A  158  ASN A  181  1                                  24    
HELIX    6 AA6 ASP A  207  GLY A  212  5                                   6    
HELIX    7 AA7 HIS A  216  ARG A  220  5                                   5    
HELIX    8 AA8 THR A  224  GLY A  247  1                                  24    
HELIX    9 AA9 GLY A  259  TYR A  274  1                                  16    
HELIX   10 AB1 ASN A  280  GLY A  297  1                                  18    
HELIX   11 AB2 SER A  300  VAL A  313  1                                  14    
SHEET    1 AA1 5 ALA A  56  ASP A  57  0                                        
SHEET    2 AA1 5 TYR A  28  TYR A  29 -1  N  TYR A  28   O  ASP A  57           
SHEET    3 AA1 5 GLN A  17  TYR A  24 -1  N  THR A  23   O  TYR A  29           
SHEET    4 AA1 5 THR A   4  ARG A  11 -1  N  GLY A   8   O  ILE A  20           
SHEET    5 AA1 5 GLN A  61  PHE A  62  1  O  PHE A  62   N  VAL A   9           
SHEET    1 AA2 3 GLN A  31  ASP A  32  0                                        
SHEET    2 AA2 3 ILE A  39  ASP A  43 -1  O  ILE A  39   N  ASP A  32           
SHEET    3 AA2 3 SER A  53  LEU A  54 -1  O  SER A  53   N  ASP A  43           
SHEET    1 AA3 5 GLN A  31  ASP A  32  0                                        
SHEET    2 AA3 5 ILE A  39  ASP A  43 -1  O  ILE A  39   N  ASP A  32           
SHEET    3 AA3 5 ILE A 100  TYR A 106  1  O  SER A 102   N  TYR A  42           
SHEET    4 AA3 5 MET A 120  GLY A 123  1  O  MET A 120   N  ARG A 101           
SHEET    5 AA3 5 ALA A 113  TRP A 115 -1  N  PHE A 114   O  VAL A 121           
SHEET    1 AA4 2 GLU A 187  ILE A 188  0                                        
SHEET    2 AA4 2 ARG A 203  SER A 204 -1  O  ARG A 203   N  ILE A 188           
SHEET    1 AA5 2 GLY A 248  HIS A 250  0                                        
SHEET    2 AA5 2 VAL A 253  VAL A 255 -1  O  VAL A 255   N  GLY A 248           
LINK         OD1 ASP A  57                CA    CA A 402     1555   1555  2.57  
LINK         OD2 ASP A  57                CA    CA A 402     1555   1555  2.34  
LINK         OD1 ASP A  59                CA    CA A 402     1555   1555  2.35  
LINK         O   GLN A  61                CA    CA A 402     1555   1555  2.26  
LINK         OD2 ASP A 138                CA    CA A 401     1555   1555  2.36  
LINK         NE2 HIS A 142                ZN    ZN A 404     1555   1555  2.02  
LINK         OE2 GLU A 143                ZN    ZN A 409     1555   1555  1.76  
LINK         NE2 HIS A 146                ZN    ZN A 404     1555   1555  2.03  
LINK         OE1AGLU A 166                ZN    ZN A 404     1555   1555  1.98  
LINK         OE2BGLU A 166                ZN    ZN A 404     1555   1555  1.98  
LINK         OE1 GLU A 177                CA    CA A 401     1555   1555  2.42  
LINK         OE2 GLU A 177                CA    CA A 401     1555   1555  2.69  
LINK         OE2 GLU A 177                ZN    ZN A 406     1555   1555  2.14  
LINK         O  AASN A 183                ZN    ZN A 406     1555   1555  2.31  
LINK         O  BASN A 183                ZN    ZN A 406     1555   1555  2.32  
LINK         OD1 ASP A 185                CA    CA A 401     1555   1555  2.44  
LINK         OD2 ASP A 185                ZN    ZN A 406     1555   1555  2.00  
LINK         O   GLU A 187                CA    CA A 401     1555   1555  2.36  
LINK         OE1 GLU A 190                CA    CA A 401     1555   1555  2.52  
LINK         OE2 GLU A 190                CA    CA A 401     1555   1555  2.47  
LINK         OE2 GLU A 190                ZN    ZN A 406     1555   1555  2.09  
LINK         O   TYR A 193                CA    CA A 403     1555   1555  2.37  
LINK         O   THR A 194                CA    CA A 403     1555   1555  2.41  
LINK         OG1 THR A 194                CA    CA A 403     1555   1555  2.38  
LINK         O   ILE A 197                CA    CA A 403     1555   1555  2.27  
LINK         OD1 ASP A 200                CA    CA A 403     1555   1555  2.36  
LINK         OD1 ASP A 226                ZN    ZN A 408     1555   1555  2.34  
LINK         ND1 HIS A 231                ZN    ZN A 408     1555   1555  1.98  
LINK         NE2 HIS A 231                ZN    ZN A 407     1555   1555  1.93  
LINK         NZ  LYS A 239                ZN    ZN A 410     1555   1555  2.38  
LINK         ND1 HIS A 250                ZN    ZN A 405     1555   1555  2.50  
LINK        CA    CA A 401                 O   HOH A 645     1555   1555  2.41  
LINK        CA    CA A 402                 O   HOH A 577     1555   1555  2.39  
LINK        CA    CA A 402                 O   HOH A 646     1555   1555  2.40  
LINK        CA    CA A 402                 O   HOH A 814     1555   1555  2.30  
LINK        CA    CA A 403                 O   HOH A 792     1555   1555  2.43  
LINK        CA    CA A 403                 O   HOH A 565     1555   1555  2.40  
LINK        ZN    ZN A 404                 O   HOH A 738     1555   1555  1.85  
LINK        ZN    ZN A 406                 O  AHOH A 536     1555   1555  2.08  
LINK        ZN    ZN A 407                 O   HOH A 840     1555   1555  1.94  
LINK        ZN    ZN A 407                 O   HOH A 738     1555   1555  1.94  
LINK        ZN    ZN A 409                 O   HOH A 636     1555   1555  2.04  
LINK        ZN    ZN A 409                 O   HOH A 738     1555   1555  1.93  
LINK        ZN    ZN A 410                 O   HOH A 527     1555   1555  2.64  
LINK        ZN    ZN A 406                 O   HOH A 555     1555   4464  2.07  
CISPEP   1 LEU A   50    PRO A   51          0         0.58                     
SITE     1 AC1  7 ASP A 138  GLU A 177  ASP A 185  GLU A 187                    
SITE     2 AC1  7 GLU A 190   ZN A 406  HOH A 645                               
SITE     1 AC2  6 ASP A  57  ASP A  59  GLN A  61  HOH A 577                    
SITE     2 AC2  6 HOH A 646  HOH A 814                                          
SITE     1 AC3  6 TYR A 193  THR A 194  ILE A 197  ASP A 200                    
SITE     2 AC3  6 HOH A 565  HOH A 792                                          
SITE     1 AC4  7 HIS A 142  GLU A 143  HIS A 146  GLU A 166                    
SITE     2 AC4  7  ZN A 407   ZN A 409  HOH A 738                               
SITE     1 AC5  4 HIS A 250  HOH A 527  HOH A 573  HOH A 764                    
SITE     1 AC6  7 GLU A 177  ASN A 183  ASP A 185  GLU A 190                    
SITE     2 AC6  7  CA A 401  HOH A 536  HOH A 555                               
SITE     1 AC7  8 TYR A 157  GLU A 166  HIS A 231   ZN A 404                    
SITE     2 AC7  8  ZN A 409  HOH A 738  HOH A 747  HOH A 840                    
SITE     1 AC8  3 ASP A 226  HIS A 231  HOH A 873                               
SITE     1 AC9  7 GLU A 143   ZN A 404   ZN A 407  HOH A 636                    
SITE     2 AC9  7 HOH A 738  HOH A 767  HOH A 840                               
SITE     1 AD1  2 LYS A 239  HOH A 527                                          
SITE     1 AD2  8 TYR A  29  SER A  53  LEU A  54  ALA A 209                    
SITE     2 AD2  8 GLY A 212  XYS A 421  HOH A 516  HOH A 776                    
SITE     1 AD3 10 TYR A  66  SER A 218  TYR A 251  HOH A 518                    
SITE     2 AD3 10 HOH A 525  HOH A 526  HOH A 543  HOH A 685                    
SITE     3 AD3 10 HOH A 724  HOH A 849                                          
SITE     1 AD4  8 ARG A  11  VAL A  13  GLY A  15  PHE A  63                    
SITE     2 AD4  8 SER A  65  ALA A  68  HOH A 550  HOH A 728                    
SITE     1 AD5  8 ASN A 159  GLU A 160  ARG A 220  TYR A 221                    
SITE     2 AD5  8 THR A 222  GLY A 228  ASN A 233  HOH A 602                    
SITE     1 AD6 10 LEU A 175  PHE A 178  TYR A 179  ARG A 260                    
SITE     2 AD6 10 ASP A 261  GLN A 273  HOH A 512  HOH A 530                    
SITE     3 AD6 10 HOH A 611  HOH A 725                                          
SITE     1 AD7  7 ILE A   1  THR A   2  GLY A   3  GLN A  31                    
SITE     2 AD7  7 HOH A 501  HOH A 507  HOH A 692                               
SITE     1 AD8  7 TYR A 274  GLN A 283  ALA A 287  HOH A 612                    
SITE     2 AD8  7 HOH A 769  HOH A 787  HOH A 796                               
SITE     1 AD9  5 ASP A 294  LEU A 295  TYR A 296  GLY A 297                    
SITE     2 AD9  5 HOH A 678                                                     
SITE     1 AE1  3 ARG A  11  PHE A  63  HOH A 659                               
SITE     1 AE2 10 ASP A 150  TYR A 151  TRP A 186  SER A 206                    
SITE     2 AE2 10 TYR A 242  HOH A 510  HOH A 546  HOH A 682                    
SITE     3 AE2 10 HOH A 684  HOH A 700                                          
SITE     1 AE3  8 GLY A  52  SER A  53  ASP A 207  XYP A 411                    
SITE     2 AE3  8 HOH A 515  HOH A 652  HOH A 727  HOH A 776                    
CRYST1   96.739   96.739  106.425  90.00  90.00  90.00 P 41 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.010337  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.010337  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009396        0.00000                         
ATOM      1  N   ILE A   1      78.567  84.018  41.422  1.00 27.77           N  
ANISOU    1  N   ILE A   1     2228   3960   4361   -178   -488   -210       N  
ATOM      2  CA  ILE A   1      79.927  84.101  40.807  1.00 28.83           C  
ANISOU    2  CA  ILE A   1     2294   4181   4480   -244   -595   -493       C  
ATOM      3  C   ILE A   1      80.192  85.560  40.432  1.00 28.28           C  
ANISOU    3  C   ILE A   1     2139   4096   4509   -187   -463   -435       C  
ATOM      4  O   ILE A   1      79.255  86.340  40.267  1.00 27.57           O  
ANISOU    4  O   ILE A   1     1869   4023   4582    -77   -551   -431       O  
ATOM      5  CB  ILE A   1      80.048  83.136  39.608  1.00 31.65           C  
ANISOU    5  CB  ILE A   1     2604   4749   4672   -148   -473   -541       C  
ATOM      6  CG1 ILE A   1      81.518  82.886  39.276  1.00 35.03           C  
ANISOU    6  CG1 ILE A   1     3385   5053   4872     18   -523   -571       C  
ATOM      7  CG2 ILE A   1      79.320  83.684  38.390  1.00 30.91           C  
ANISOU    7  CG2 ILE A   1     2398   4764   4583   -297   -513   -706       C  
ATOM      8  CD1 ILE A   1      81.718  81.750  38.309  1.00 36.23           C  
ANISOU    8  CD1 ILE A   1     3696   5121   4948     88   -561   -635       C  
ATOM      9  H1  ILE A   1      78.349  83.164  41.547  1.00 33.33           H  
ATOM     10  H2  ILE A   1      78.569  84.441  42.205  1.00 33.33           H  
ATOM     11  H3  ILE A   1      77.973  84.399  40.881  1.00 33.33           H  
ATOM     12  HA  ILE A   1      80.611  83.824  41.436  1.00 34.61           H  
ATOM     13  HB  ILE A   1      79.632  82.296  39.858  1.00 37.99           H  
ATOM     14 HG12 ILE A   1      81.891  83.688  38.878  1.00 42.04           H  
ATOM     15 HG13 ILE A   1      81.993  82.670  40.094  1.00 42.04           H  
ATOM     16 HG21 ILE A   1      79.196  82.968  37.748  1.00 37.10           H  
ATOM     17 HG22 ILE A   1      78.459  84.033  38.667  1.00 37.10           H  
ATOM     18 HG23 ILE A   1      79.853  84.393  37.996  1.00 37.10           H  
ATOM     19 HD11 ILE A   1      82.669  81.607  38.184  1.00 43.48           H  
ATOM     20 HD12 ILE A   1      81.308  80.950  38.673  1.00 43.48           H  
ATOM     21 HD13 ILE A   1      81.304  81.980  37.463  1.00 43.48           H  
ATOM     22  N   THR A   2      81.464  85.940  40.335  1.00 29.44           N  
ANISOU   22  N   THR A   2     2537   4140   4509    -77   -308   -602       N  
ATOM     23  CA  THR A   2      81.837  87.277  39.894  1.00 29.45           C  
ANISOU   23  CA  THR A   2     2560   4166   4464   -200    -79   -658       C  
ATOM     24  C   THR A   2      82.042  87.264  38.384  1.00 28.31           C  
ANISOU   24  C   THR A   2     2557   3856   4344    300    325   -675       C  
ATOM     25  O   THR A   2      82.748  86.399  37.856  1.00 30.67           O  
ANISOU   25  O   THR A   2     3039   4095   4519    962    512   -637       O  
ATOM     26  CB  THR A   2      83.135  87.710  40.576  1.00 32.35           C  
ANISOU   26  CB  THR A   2     3007   4632   4653   -474   -133   -650       C  
ATOM     27  OG1 THR A   2      82.938  87.798  41.990  1.00 34.13           O  
ANISOU   27  OG1 THR A   2     3254   5014   4699   -486   -189   -716       O  
ATOM     28  CG2 THR A   2      83.590  89.064  40.054  1.00 33.29           C  
ANISOU   28  CG2 THR A   2     3077   4694   4878   -598   -101   -691       C  
ATOM     29  H   THR A   2      82.134  85.434  40.522  1.00 35.34           H  
ATOM     30  HA  THR A   2      81.135  87.908  40.117  1.00 35.35           H  
ATOM     31  HB  THR A   2      83.826  87.056  40.387  1.00 38.83           H  
ATOM     32  HG1 THR A   2      83.653  88.028  42.366  1.00 40.96           H  
ATOM     33 HG21 THR A   2      84.255  89.443  40.650  1.00 39.95           H  
ATOM     34 HG22 THR A   2      83.979  88.965  39.171  1.00 39.95           H  
ATOM     35 HG23 THR A   2      82.834  89.669  39.998  1.00 39.95           H  
ATOM     36  N   GLY A   3      81.430  88.218  37.698  1.00 26.59           N  
ANISOU   36  N   GLY A   3     2445   3474   4184    133    564   -566       N  
ATOM     37  CA  GLY A   3      81.554  88.293  36.255  1.00 25.46           C  
ANISOU   37  CA  GLY A   3     2451   3217   4008    171    671   -473       C  
ATOM     38  C   GLY A   3      80.787  89.482  35.723  1.00 25.41           C  
ANISOU   38  C   GLY A   3     2561   2944   4148    110    769   -351       C  
ATOM     39  O   GLY A   3      80.297  90.319  36.484  1.00 26.84           O  
ANISOU   39  O   GLY A   3     3022   3004   4170    229    641   -574       O  
ATOM     40  H   GLY A   3      80.938  88.833  38.043  1.00 31.92           H  
ATOM     41  HA2 GLY A   3      82.488  88.386  36.009  1.00 30.57           H  
ATOM     42  HA3 GLY A   3      81.201  87.485  35.852  1.00 30.57           H  
ATOM     43  N  ATHR A   4      80.682  89.532  34.397  0.54 25.10           N  
ANISOU   43  N  ATHR A   4     2477   2851   4209     26    809   -194       N  
ATOM     44  N  BTHR A   4      80.688  89.561  34.399  0.46 25.03           N  
ANISOU   44  N  BTHR A   4     2456   2821   4232     65    860   -225       N  
ATOM     45  CA ATHR A   4      79.988  90.609  33.706  0.54 24.55           C  
ANISOU   45  CA ATHR A   4     2502   2613   4214   -119    796    -58       C  
ATOM     46  CA BTHR A   4      79.993  90.673  33.766  0.46 24.42           C  
ANISOU   46  CA BTHR A   4     2450   2565   4264    -51    915   -107       C  
ATOM     47  C  ATHR A   4      78.509  90.273  33.600  0.54 22.83           C  
ANISOU   47  C  ATHR A   4     2312   2244   4120   -118    806    104       C  
ATOM     48  C  BTHR A   4      78.535  90.314  33.527  0.46 23.00           C  
ANISOU   48  C  BTHR A   4     2304   2300   4136   -115    893     68       C  
ATOM     49  O  ATHR A   4      78.140  89.122  33.353  0.54 22.66           O  
ANISOU   49  O  ATHR A   4     2363   2033   4216    -45    572    129       O  
ATOM     50  O  BTHR A   4      78.212  89.194  33.120  0.46 23.10           O  
ANISOU   50  O  BTHR A   4     2346   2246   4187   -116    762     91       O  
ATOM     51  CB ATHR A   4      80.550  90.758  32.292  0.54 26.11           C  
ANISOU   51  CB ATHR A   4     2646   2945   4331   -256    918    -67       C  
ATOM     52  CB BTHR A   4      80.634  91.043  32.429  0.46 25.63           C  
ANISOU   52  CB BTHR A   4     2527   2769   4442   -115   1119   -141       C  
ATOM     53  OG1ATHR A   4      81.975  90.897  32.345  0.54 27.50           O  
ANISOU   53  OG1ATHR A   4     2766   3244   4439   -349   1011    -26       O  
ATOM     54  OG1BTHR A   4      80.582  89.915  31.549  0.46 25.52           O  
ANISOU   54  OG1BTHR A   4     2472   2723   4500    -23   1289    -83       O  
ATOM     55  CG2ATHR A   4      79.942  91.972  31.594  0.54 26.11           C  
ANISOU   55  CG2ATHR A   4     2690   2938   4290   -160    970    -13       C  
ATOM     56  CG2BTHR A   4      82.076  91.496  32.628  0.46 26.24           C  
ANISOU   56  CG2BTHR A   4     2615   2851   4503   -311   1196   -159       C  
ATOM     57  H  ATHR A   4      81.013  88.940  33.868  0.54 30.13           H  
ATOM     58  H  BTHR A   4      81.014  88.984  33.851  0.46 30.04           H  
ATOM     59  HA ATHR A   4      80.100  91.440  34.193  0.54 29.47           H  
ATOM     60  HA BTHR A   4      80.045  91.443  34.354  0.46 29.31           H  
ATOM     61  HB ATHR A   4      80.326  89.969  31.774  0.54 31.34           H  
ATOM     62  HB BTHR A   4      80.150  91.781  32.025  0.46 30.76           H  
ATOM     63  HG1ATHR A   4      82.280  91.025  31.573  0.54 33.00           H  
ATOM     64  HG1BTHR A   4      80.947  90.105  30.817  0.46 30.63           H  
ATOM     65 HG21ATHR A   4      80.412  92.148  30.764  0.54 31.34           H  
ATOM     66 HG21BTHR A   4      82.462  91.755  31.777  0.46 31.49           H  
ATOM     67 HG22ATHR A   4      79.006  91.808  31.397  0.54 31.34           H  
ATOM     68 HG22BTHR A   4      82.105  92.255  33.231  0.46 31.49           H  
ATOM     69 HG23ATHR A   4      80.010  92.752  32.166  0.54 31.34           H  
ATOM     70 HG23BTHR A   4      82.601  90.773  33.006  0.46 31.49           H  
ATOM     71  N   SER A   5      77.659  91.279  33.772  1.00 22.59           N  
ANISOU   71  N   SER A   5     2284   2252   4046   -118    884     91       N  
ATOM     72  CA  SER A   5      76.236  91.087  33.538  1.00 22.37           C  
ANISOU   72  CA  SER A   5     2379   2300   3822   -262   1032    107       C  
ATOM     73  C   SER A   5      75.958  91.071  32.040  1.00 23.42           C  
ANISOU   73  C   SER A   5     2686   2288   3927   -337   1107    462       C  
ATOM     74  O   SER A   5      76.324  92.008  31.316  1.00 25.55           O  
ANISOU   74  O   SER A   5     3168   2430   4109   -310   1152    636       O  
ATOM     75  CB  SER A   5      75.447  92.206  34.204  1.00 22.13           C  
ANISOU   75  CB  SER A   5     2335   2324   3750   -138    953    124       C  
ATOM     76  OG  SER A   5      75.564  92.115  35.609  1.00 22.58           O  
ANISOU   76  OG  SER A   5     2458   2410   3712   -219    815    -86       O  
ATOM     77  H  ASER A   5      77.880  92.072  34.020  0.54 27.11           H  
ATOM     78  H  BSER A   5      77.863  92.057  34.074  0.46 27.11           H  
ATOM     79  HA  SER A   5      75.950  90.241  33.915  1.00 26.86           H  
ATOM     80  HB2 SER A   5      75.797  93.062  33.910  1.00 26.56           H  
ATOM     81  HB3 SER A   5      74.512  92.128  33.957  1.00 26.56           H  
ATOM     82  HG  SER A   5      76.369  92.190  35.836  1.00 27.10           H  
ATOM     83  N   THR A   6      75.297  90.010  31.584  1.00 22.21           N  
ANISOU   83  N   THR A   6     2597   2101   3740    -72    978    301       N  
ATOM     84  CA  THR A   6      75.023  89.786  30.176  1.00 20.60           C  
ANISOU   84  CA  THR A   6     2402   1936   3490    -46    960    278       C  
ATOM     85  C   THR A   6      73.547  89.446  30.009  1.00 20.63           C  
ANISOU   85  C   THR A   6     2519   2053   3268     85    778    374       C  
ATOM     86  O   THR A   6      72.815  89.223  30.982  1.00 20.47           O  
ANISOU   86  O   THR A   6     2452   2134   3192    -61    906    571       O  
ATOM     87  CB  THR A   6      75.960  88.703  29.613  1.00 21.82           C  
ANISOU   87  CB  THR A   6     2520   2189   3583     90   1089    342       C  
ATOM     88  OG1 THR A   6      75.974  87.549  30.467  1.00 22.49           O  
ANISOU   88  OG1 THR A   6     2604   2212   3730    169   1071    387       O  
ATOM     89  CG2 THR A   6      77.384  89.223  29.524  1.00 22.69           C  
ANISOU   89  CG2 THR A   6     2648   2340   3634    -11   1126    200       C  
ATOM     90  H   THR A   6      74.990  89.388  32.093  1.00 26.66           H  
ATOM     91  HA  THR A   6      75.177  90.590  29.655  1.00 24.73           H  
ATOM     92  HB  THR A   6      75.641  88.457  28.730  1.00 26.20           H  
ATOM     93  HG1 THR A   6      75.201  87.224  30.524  1.00 27.00           H  
ATOM     94 HG21 THR A   6      77.965  88.539  29.158  1.00 27.24           H  
ATOM     95 HG22 THR A   6      77.417  90.004  28.949  1.00 27.24           H  
ATOM     96 HG23 THR A   6      77.703  89.468  30.407  1.00 27.24           H  
ATOM     97  N   VAL A   7      73.099  89.432  28.757  1.00 20.66           N  
ANISOU   97  N   VAL A   7     2550   2244   3055    266    497    448       N  
ATOM     98  CA  VAL A   7      71.720  89.086  28.426  1.00 21.55           C  
ANISOU   98  CA  VAL A   7     2813   2451   2924    469    639    652       C  
ATOM     99  C   VAL A   7      71.762  87.964  27.408  1.00 20.31           C  
ANISOU   99  C   VAL A   7     2728   2374   2617    530    690    876       C  
ATOM    100  O   VAL A   7      72.228  88.162  26.275  1.00 21.91           O  
ANISOU  100  O   VAL A   7     3006   2606   2714    535    885   1016       O  
ATOM    101  CB  VAL A   7      70.932  90.280  27.882  1.00 24.11           C  
ANISOU  101  CB  VAL A   7     3247   2672   3240    539    645    442       C  
ATOM    102  CG1 VAL A   7      69.519  89.843  27.481  1.00 24.31           C  
ANISOU  102  CG1 VAL A   7     3282   2647   3309    594    609    388       C  
ATOM    103  CG2 VAL A   7      70.883  91.400  28.911  1.00 25.88           C  
ANISOU  103  CG2 VAL A   7     3533   2867   3433    525    694    317       C  
ATOM    104  H   VAL A   7      73.585  89.623  28.073  1.00 24.80           H  
ATOM    105  HA  VAL A   7      71.274  88.761  29.224  1.00 25.87           H  
ATOM    106  HB  VAL A   7      71.379  90.621  27.091  1.00 28.94           H  
ATOM    107 HG11 VAL A   7      68.970  90.632  27.349  1.00 29.18           H  
ATOM    108 HG12 VAL A   7      69.567  89.332  26.658  1.00 29.18           H  
ATOM    109 HG13 VAL A   7      69.145  89.294  28.189  1.00 29.18           H  
ATOM    110 HG21 VAL A   7      70.353  92.131  28.556  1.00 31.06           H  
ATOM    111 HG22 VAL A   7      70.479  91.063  29.725  1.00 31.06           H  
ATOM    112 HG23 VAL A   7      71.786  91.704  29.090  1.00 31.06           H  
ATOM    113  N   GLY A   8      71.290  86.782  27.808  1.00 19.21           N  
ANISOU  113  N   GLY A   8     2616   2228   2454    394    531    549       N  
ATOM    114  CA  GLY A   8      71.153  85.659  26.913  1.00 19.15           C  
ANISOU  114  CA  GLY A   8     2438   2429   2409    445    638    340       C  
ATOM    115  C   GLY A   8      69.737  85.548  26.377  1.00 19.08           C  
ANISOU  115  C   GLY A   8     2477   2462   2309    553    440    489       C  
ATOM    116  O   GLY A   8      68.858  86.356  26.668  1.00 18.65           O  
ANISOU  116  O   GLY A   8     2390   2423   2274    502    557    493       O  
ATOM    117  H   GLY A   8      71.040  86.613  28.613  1.00 23.06           H  
ATOM    118  HA2 GLY A   8      71.760  85.765  26.164  1.00 22.99           H  
ATOM    119  HA3 GLY A   8      71.372  84.840  27.384  1.00 22.99           H  
ATOM    120  N   VAL A   9      69.541  84.528  25.549  1.00 19.45           N  
ANISOU  120  N   VAL A   9     2582   2554   2255    606    299    536       N  
ATOM    121  CA AVAL A   9      68.254  84.270  24.916  0.72 19.86           C  
ANISOU  121  CA AVAL A   9     2685   2668   2191    596    208    626       C  
ATOM    122  CA BVAL A   9      68.258  84.270  24.907  0.28 19.55           C  
ANISOU  122  CA BVAL A   9     2658   2569   2200    524    208    544       C  
ATOM    123  C   VAL A   9      68.027  82.765  24.895  1.00 19.42           C  
ANISOU  123  C   VAL A   9     2617   2518   2245    483    145    550       C  
ATOM    124  O   VAL A   9      68.964  81.977  24.783  1.00 19.00           O  
ANISOU  124  O   VAL A   9     2486   2326   2407    509    157    548       O  
ATOM    125  CB AVAL A   9      68.209  84.879  23.497  0.72 21.00           C  
ANISOU  125  CB AVAL A   9     2966   2918   2096    640    219    788       C  
ATOM    126  CB BVAL A   9      68.199  84.813  23.462  0.28 19.93           C  
ANISOU  126  CB BVAL A   9     2824   2628   2119    467    185    540       C  
ATOM    127  CG1AVAL A   9      69.240  84.218  22.600  0.72 21.25           C  
ANISOU  127  CG1AVAL A   9     3116   2969   1988    678    379   1065       C  
ATOM    128  CG1BVAL A   9      66.755  84.838  22.961  0.28 20.23           C  
ANISOU  128  CG1BVAL A   9     2854   2708   2123    399    245    462       C  
ATOM    129  CG2AVAL A   9      66.798  84.777  22.907  0.72 21.59           C  
ANISOU  129  CG2AVAL A   9     2990   3112   2102    482    306    603       C  
ATOM    130  CG2BVAL A   9      68.826  86.188  23.378  0.28 19.79           C  
ANISOU  130  CG2BVAL A   9     2901   2587   2032    405    183    575       C  
ATOM    131  H  AVAL A   9      70.151  83.961  25.335  0.72 23.35           H  
ATOM    132  H  BVAL A   9      70.151  83.959  25.340  0.28 23.35           H  
ATOM    133  HA AVAL A   9      67.534  84.664  25.433  0.72 23.83           H  
ATOM    134  HA BVAL A   9      67.560  84.702  25.423  0.28 23.46           H  
ATOM    135  HB AVAL A   9      68.431  85.822  23.550  0.72 25.21           H  
ATOM    136  HB BVAL A   9      68.708  84.223  22.884  0.28 23.92           H  
ATOM    137 HG11AVAL A   9      69.285  84.703  21.761  0.72 25.50           H  
ATOM    138 HG11BVAL A   9      66.735  85.232  22.074  0.28 24.28           H  
ATOM    139 HG12AVAL A   9      70.103  84.241  23.042  0.72 25.50           H  
ATOM    140 HG12BVAL A   9      66.417  83.930  22.926  0.28 24.28           H  
ATOM    141 HG13AVAL A   9      68.975  83.300  22.438  0.72 25.50           H  
ATOM    142 HG13BVAL A   9      66.218  85.368  23.570  0.28 24.28           H  
ATOM    143 HG21AVAL A   9      66.782  85.226  22.047  0.72 25.92           H  
ATOM    144 HG21BVAL A   9      68.637  86.569  22.507  0.28 23.76           H  
ATOM    145 HG22AVAL A   9      66.568  83.842  22.796  0.72 25.92           H  
ATOM    146 HG22BVAL A   9      68.449  86.750  24.074  0.28 23.76           H  
ATOM    147 HG23AVAL A   9      66.171  85.202  23.513  0.72 25.92           H  
ATOM    148 HG23BVAL A   9      69.785  86.106  23.502  0.28 23.76           H  
ATOM    149  N   GLY A  10      66.772  82.368  25.010  1.00 18.68           N  
ANISOU  149  N   GLY A  10     2543   2342   2212    563     18    531       N  
ATOM    150  CA  GLY A  10      66.452  80.956  25.021  1.00 19.07           C  
ANISOU  150  CA  GLY A  10     2567   2450   2229    643   -100    476       C  
ATOM    151  C   GLY A  10      64.967  80.757  24.843  1.00 19.11           C  
ANISOU  151  C   GLY A  10     2514   2633   2116    382    -85    335       C  
ATOM    152  O   GLY A  10      64.229  81.700  24.554  1.00 19.84           O  
ANISOU  152  O   GLY A  10     2487   2692   2359    398    -23    320       O  
ATOM    153  H   GLY A  10      66.093  82.890  25.083  1.00 22.42           H  
ATOM    154  HA2 GLY A  10      66.919  80.506  24.299  1.00 22.90           H  
ATOM    155  HA3 GLY A  10      66.723  80.562  25.865  1.00 22.90           H  
ATOM    156  N  AARG A  11      64.544  79.503  24.986  0.49 18.66           N  
ANISOU  156  N  AARG A  11     2443   2638   2009    307   -139     62       N  
ATOM    157  N  BARG A  11      64.531  79.510  25.017  0.51 18.41           N  
ANISOU  157  N  BARG A  11     2528   2607   1861    291    -61    257       N  
ATOM    158  CA AARG A  11      63.139  79.136  24.914  0.49 18.94           C  
ANISOU  158  CA AARG A  11     2567   2756   1874    356   -267   -132       C  
ATOM    159  CA BARG A  11      63.121  79.162  24.906  0.51 18.42           C  
ANISOU  159  CA BARG A  11     2740   2680   1580    331   -139    260       C  
ATOM    160  C  AARG A  11      62.734  78.457  26.214  0.49 17.53           C  
ANISOU  160  C  AARG A  11     2294   2679   1687    328    -99    -58       C  
ATOM    161  C  BARG A  11      62.689  78.384  26.143  0.51 17.31           C  
ANISOU  161  C  BARG A  11     2434   2600   1542    341    -55    140       C  
ATOM    162  O  AARG A  11      63.514  77.700  26.806  0.49 17.36           O  
ANISOU  162  O  AARG A  11     2124   2730   1742    218   -178   -112       O  
ATOM    163  O  BARG A  11      63.410  77.504  26.628  0.51 17.31           O  
ANISOU  163  O  BARG A  11     2412   2562   1603    263   -116     59       O  
ATOM    164  CB AARG A  11      62.865  78.170  23.755  0.49 21.90           C  
ANISOU  164  CB AARG A  11     3037   3171   2112    392   -379   -463       C  
ATOM    165  CB BARG A  11      62.835  78.348  23.628  0.51 21.08           C  
ANISOU  165  CB BARG A  11     3364   3080   1565    280    -85    275       C  
ATOM    166  CG AARG A  11      62.609  78.842  22.409  0.49 24.82           C  
ANISOU  166  CG AARG A  11     3365   3616   2451    403   -541   -665       C  
ATOM    167  CG BARG A  11      62.876  79.183  22.338  0.51 23.58           C  
ANISOU  167  CG BARG A  11     3798   3517   1643    123   -112    317       C  
ATOM    168  CD AARG A  11      62.100  77.825  21.377  0.49 26.22           C  
ANISOU  168  CD AARG A  11     3520   3851   2592    391   -661   -843       C  
ATOM    169  CD BARG A  11      62.639  78.333  21.075  0.51 24.82           C  
ANISOU  169  CD BARG A  11     4155   3743   1534     58   -139    443       C  
ATOM    170  NE AARG A  11      62.964  76.653  21.317  0.49 28.35           N  
ANISOU  170  NE AARG A  11     3830   4135   2806    320   -514   -961       N  
ATOM    171  NE BARG A  11      62.771  79.132  19.855  0.51 27.37           N  
ANISOU  171  NE BARG A  11     4554   4091   1754     40   -256    387       N  
ATOM    172  CZ AARG A  11      63.869  76.422  20.367  0.49 29.69           C  
ANISOU  172  CZ AARG A  11     3908   4295   3079    303   -544   -860       C  
ATOM    173  CZ BARG A  11      61.824  79.931  19.372  0.51 29.28           C  
ANISOU  173  CZ BARG A  11     4876   4305   1944     54    -68    424       C  
ATOM    174  NH1AARG A  11      64.036  77.277  19.362  0.49 31.15           N  
ANISOU  174  NH1AARG A  11     4073   4583   3177    198   -714   -781       N  
ATOM    175  NH1BARG A  11      60.654  80.040  19.991  0.51 29.00           N  
ANISOU  175  NH1BARG A  11     4906   4306   1808    -58     51    429       N  
ATOM    176  NH2AARG A  11      64.604  75.322  20.420  0.49 28.43           N  
ANISOU  176  NH2AARG A  11     3700   3983   3120    557   -482  -1023       N  
ATOM    177  NH2BARG A  11      62.045  80.615  18.258  0.51 31.15           N  
ANISOU  177  NH2BARG A  11     5070   4482   2283     99     16    522       N  
ATOM    178  H  AARG A  11      65.069  78.836  25.129  0.49 22.40           H  
ATOM    179  H  BARG A  11      65.043  78.844  25.202  0.51 22.10           H  
ATOM    180  HA AARG A  11      62.609  79.938  24.781  0.49 22.74           H  
ATOM    181  HA BARG A  11      62.589  79.972  24.863  0.51 22.11           H  
ATOM    182  HB2AARG A  11      63.635  77.590  23.650  0.49 26.28           H  
ATOM    183  HB2BARG A  11      63.502  77.648  23.549  0.51 25.30           H  
ATOM    184  HB3AARG A  11      62.080  77.644  23.973  0.49 26.28           H  
ATOM    185  HB3BARG A  11      61.950  77.957  23.700  0.51 25.30           H  
ATOM    186  HG2AARG A  11      61.938  79.534  22.516  0.49 29.80           H  
ATOM    187  HG2BARG A  11      62.185  79.862  22.378  0.51 28.30           H  
ATOM    188  HG3AARG A  11      63.435  79.228  22.078  0.49 29.80           H  
ATOM    189  HG3BARG A  11      63.748  79.602  22.259  0.51 28.30           H  
ATOM    190  HD2AARG A  11      61.208  77.534  21.625  0.49 31.47           H  
ATOM    191  HD2BARG A  11      63.293  77.618  21.043  0.51 29.80           H  
ATOM    192  HD3AARG A  11      62.082  78.238  20.500  0.49 31.47           H  
ATOM    193  HD3BARG A  11      61.743  77.963  21.102  0.51 29.80           H  
ATOM    194  HE AARG A  11      62.885  76.067  21.941  0.49 34.03           H  
ATOM    195  HE BARG A  11      63.512  79.082  19.422  0.51 32.85           H  
ATOM    196 HH11AARG A  11      63.557  77.990  19.321  0.49 37.38           H  
ATOM    197 HH11BARG A  11      60.504  79.592  20.710  0.51 34.81           H  
ATOM    198 HH12AARG A  11      64.623  77.118  18.755  0.49 37.38           H  
ATOM    199 HH12BARG A  11      60.045  80.558  19.673  0.51 34.81           H  
ATOM    200 HH21AARG A  11      64.496  74.764  21.065  0.49 34.13           H  
ATOM    201 HH21BARG A  11      62.799  80.542  17.851  0.51 37.39           H  
ATOM    202 HH22AARG A  11      65.190  75.167  19.810  0.49 34.13           H  
ATOM    203 HH22BARG A  11      61.434  81.133  17.943  0.51 37.39           H  
ATOM    204  N   GLY A  12      61.512  78.726  26.651  1.00 16.97           N  
ANISOU  204  N   GLY A  12     2278   2571   1599    328    -11     30       N  
ATOM    205  CA  GLY A  12      60.969  78.102  27.831  1.00 16.44           C  
ANISOU  205  CA  GLY A  12     2337   2424   1486    215    -88    188       C  
ATOM    206  C   GLY A  12      60.274  76.789  27.526  1.00 16.75           C  
ANISOU  206  C   GLY A  12     2328   2479   1556    293   -177    -36       C  
ATOM    207  O   GLY A  12      60.288  76.267  26.408  1.00 17.79           O  
ANISOU  207  O   GLY A  12     2306   2769   1683    218   -261    -66       O  
ATOM    208  H  AGLY A  12      60.973  79.277  26.268  0.49 20.37           H  
ATOM    209  H  BGLY A  12      61.002  79.332  26.316  0.51 20.37           H  
ATOM    210  HA2 GLY A  12      61.686  77.929  28.461  1.00 19.74           H  
ATOM    211  HA3 GLY A  12      60.325  78.700  28.243  1.00 19.74           H  
ATOM    212  N   VAL A  13      59.662  76.243  28.577  1.00 16.75           N  
ANISOU  212  N   VAL A  13     2341   2386   1639    213   -294     -3       N  
ATOM    213  CA  VAL A  13      59.067  74.913  28.523  1.00 18.24           C  
ANISOU  213  CA  VAL A  13     2342   2746   1842     63   -493    -61       C  
ATOM    214  C   VAL A  13      58.008  74.828  27.429  1.00 19.81           C  
ANISOU  214  C   VAL A  13     2430   3165   1931    -57   -491   -182       C  
ATOM    215  O   VAL A  13      57.849  73.791  26.773  1.00 20.92           O  
ANISOU  215  O   VAL A  13     2568   3345   2035   -117   -602   -413       O  
ATOM    216  CB  VAL A  13      58.500  74.573  29.916  1.00 17.56           C  
ANISOU  216  CB  VAL A  13     2181   2658   1834    125   -539   -148       C  
ATOM    217  CG1 VAL A  13      57.690  73.282  29.875  1.00 20.16           C  
ANISOU  217  CG1 VAL A  13     2359   2917   2386    -37   -486   -126       C  
ATOM    218  CG2 VAL A  13      59.631  74.466  30.952  1.00 16.75           C  
ANISOU  218  CG2 VAL A  13     1947   2692   1726    107   -483   -180       C  
ATOM    219  H   VAL A  13      59.576  76.625  29.342  1.00 20.11           H  
ATOM    220  HA  VAL A  13      59.749  74.263  28.292  1.00 21.90           H  
ATOM    221  HB  VAL A  13      57.906  75.290  30.188  1.00 21.08           H  
ATOM    222 HG11 VAL A  13      57.544  72.971  30.782  1.00 24.21           H  
ATOM    223 HG12 VAL A  13      56.838  73.457  29.444  1.00 24.21           H  
ATOM    224 HG13 VAL A  13      58.184  72.615  29.372  1.00 24.21           H  
ATOM    225 HG21 VAL A  13      59.248  74.243  31.815  1.00 20.11           H  
ATOM    226 HG22 VAL A  13      60.248  73.771  30.675  1.00 20.11           H  
ATOM    227 HG23 VAL A  13      60.093  75.317  31.005  1.00 20.11           H  
ATOM    228  N   LEU A  14      57.245  75.896  27.234  1.00 20.47           N  
ANISOU  228  N   LEU A  14     2499   3431   1846    109   -835     46       N  
ATOM    229  CA ALEU A  14      56.185  75.913  26.233  0.58 21.80           C  
ANISOU  229  CA ALEU A  14     2558   3758   1969    167   -973     -9       C  
ATOM    230  CA BLEU A  14      56.181  75.937  26.240  0.42 21.96           C  
ANISOU  230  CA BLEU A  14     2652   3716   1976    101   -938     -3       C  
ATOM    231  C   LEU A  14      56.657  76.404  24.865  1.00 22.68           C  
ANISOU  231  C   LEU A  14     2690   3926   2000    121   -953      1       C  
ATOM    232  O   LEU A  14      55.822  76.665  23.986  1.00 25.32           O  
ANISOU  232  O   LEU A  14     3134   4526   1958    245   -927     31       O  
ATOM    233  CB ALEU A  14      55.001  76.738  26.739  0.58 23.14           C  
ANISOU  233  CB ALEU A  14     2540   4011   2243    237   -921    -58       C  
ATOM    234  CB BLEU A  14      55.040  76.827  26.743  0.42 23.32           C  
ANISOU  234  CB BLEU A  14     2795   3863   2203     48   -880    -40       C  
ATOM    235  CG ALEU A  14      54.133  76.091  27.829  0.58 25.17           C  
ANISOU  235  CG ALEU A  14     2773   4192   2599    313   -731   -213       C  
ATOM    236  CG BLEU A  14      53.971  76.161  27.617  0.42 24.96           C  
ANISOU  236  CG BLEU A  14     3084   3942   2459      0   -728   -129       C  
ATOM    237  CD1ALEU A  14      53.756  74.652  27.433  0.58 26.27           C  
ANISOU  237  CD1ALEU A  14     2889   4252   2841    201   -430   -322       C  
ATOM    238  CD1BLEU A  14      54.542  75.384  28.787  0.42 25.18           C  
ANISOU  238  CD1BLEU A  14     3120   3913   2535   -102   -695   -239       C  
ATOM    239  CD2ALEU A  14      54.781  76.116  29.199  0.58 26.18           C  
ANISOU  239  CD2ALEU A  14     2920   4313   2715    428   -496   -334       C  
ATOM    240  CD2BLEU A  14      52.989  77.216  28.114  0.42 25.63           C  
ANISOU  240  CD2BLEU A  14     3220   4029   2489     -2   -585   -187       C  
ATOM    241  H  ALEU A  14      57.323  76.631  27.674  0.58 24.57           H  
ATOM    242  H  BLEU A  14      57.327  76.628  27.677  0.42 24.57           H  
ATOM    243  HA ALEU A  14      55.866  75.006  26.103  0.58 26.17           H  
ATOM    244  HA BLEU A  14      55.830  75.040  26.125  0.42 26.36           H  
ATOM    245  HB2ALEU A  14      55.346  77.567  27.104  0.58 27.78           H  
ATOM    246  HB2BLEU A  14      55.429  77.543  27.269  0.42 27.99           H  
ATOM    247  HB3ALEU A  14      54.420  76.924  25.985  0.58 27.78           H  
ATOM    248  HB3BLEU A  14      54.584  77.194  25.969  0.42 27.99           H  
ATOM    249  HG ALEU A  14      53.324  76.620  27.905  0.58 30.21           H  
ATOM    250  HG BLEU A  14      53.511  75.509  27.066  0.42 29.97           H  
ATOM    251 HD11ALEU A  14      52.970  74.383  27.934  0.58 31.53           H  
ATOM    252 HD11BLEU A  14      53.811  75.034  29.320  0.42 30.23           H  
ATOM    253 HD12ALEU A  14      53.567  74.626  26.482  0.58 31.53           H  
ATOM    254 HD12BLEU A  14      55.083  74.654  28.448  0.42 30.23           H  
ATOM    255 HD13ALEU A  14      54.498  74.063  27.639  0.58 31.53           H  
ATOM    256 HD13BLEU A  14      55.088  75.979  29.325  0.42 30.23           H  
ATOM    257 HD21ALEU A  14      54.150  75.775  29.852  0.58 31.42           H  
ATOM    258 HD21BLEU A  14      52.211  76.772  28.485  0.42 30.76           H  
ATOM    259 HD22ALEU A  14      55.574  75.558  29.183  0.58 31.42           H  
ATOM    260 HD22BLEU A  14      53.421  77.753  28.796  0.42 30.76           H  
ATOM    261 HD23ALEU A  14      55.023  77.029  29.417  0.58 31.42           H  
ATOM    262 HD23BLEU A  14      52.725  77.778  27.369  0.42 30.76           H  
ATOM    263  N   GLY A  15      57.962  76.510  24.655  1.00 22.66           N  
ANISOU  263  N   GLY A  15     2797   3829   1983     50   -555    -68       N  
ATOM    264  CA  GLY A  15      58.507  76.831  23.347  1.00 23.41           C  
ANISOU  264  CA  GLY A  15     3073   3780   2042     58   -344    -32       C  
ATOM    265  C   GLY A  15      58.597  78.299  23.015  1.00 24.29           C  
ANISOU  265  C   GLY A  15     3214   3924   2090    275   -349    216       C  
ATOM    266  O   GLY A  15      58.904  78.641  21.866  1.00 26.04           O  
ANISOU  266  O   GLY A  15     3547   4138   2209    400   -372    195       O  
ATOM    267  H   GLY A  15      58.560  76.399  25.263  1.00 27.20           H  
ATOM    268  HA2 GLY A  15      59.402  76.463  23.289  1.00 28.10           H  
ATOM    269  HA3 GLY A  15      57.949  76.413  22.672  1.00 28.10           H  
ATOM    270  N   ASP A  16      58.358  79.177  23.984  1.00 22.77           N  
ANISOU  270  N   ASP A  16     2974   3628   2049    370   -569     77       N  
ATOM    271  CA  ASP A  16      58.372  80.613  23.764  1.00 22.16           C  
ANISOU  271  CA  ASP A  16     2820   3558   2043    636   -567    127       C  
ATOM    272  C   ASP A  16      59.767  81.179  24.004  1.00 21.21           C  
ANISOU  272  C   ASP A  16     2701   3374   1983    690   -291    498       C  
ATOM    273  O   ASP A  16      60.463  80.785  24.940  1.00 21.60           O  
ANISOU  273  O   ASP A  16     2738   3310   2157    785   -296    534       O  
ATOM    274  CB  ASP A  16      57.369  81.301  24.694  1.00 23.91           C  
ANISOU  274  CB  ASP A  16     2898   3868   2320    786   -466   -295       C  
ATOM    275  CG  ASP A  16      57.587  80.960  26.180  1.00 25.74           C  
ANISOU  275  CG  ASP A  16     3167   3947   2665   1005   -630   -504       C  
ATOM    276  OD1 ASP A  16      57.970  79.817  26.525  1.00 25.16           O  
ANISOU  276  OD1 ASP A  16     3044   3826   2691    581   -394   -353       O  
ATOM    277  OD2 ASP A  16      57.359  81.849  27.027  1.00 28.33           O  
ANISOU  277  OD2 ASP A  16     3736   4015   3012   1234   -811   -596       O  
ATOM    278  H   ASP A  16      58.181  78.956  24.797  1.00 27.33           H  
ATOM    279  HA  ASP A  16      58.124  80.799  22.845  1.00 26.60           H  
ATOM    280  HB2 ASP A  16      57.456  82.262  24.593  1.00 28.71           H  
ATOM    281  HB3 ASP A  16      56.473  81.021  24.452  1.00 28.71           H  
ATOM    282  N   GLN A  17      60.168  82.107  23.140  1.00 22.06           N  
ANISOU  282  N   GLN A  17     2826   3532   2023    647   -182    560       N  
ATOM    283  CA  GLN A  17      61.482  82.721  23.257  1.00 21.64           C  
ANISOU  283  CA  GLN A  17     2808   3403   2011    633    -10    641       C  
ATOM    284  C   GLN A  17      61.445  83.878  24.250  1.00 21.49           C  
ANISOU  284  C   GLN A  17     2653   3219   2294    903   -199    429       C  
ATOM    285  O   GLN A  17      60.488  84.657  24.295  1.00 23.12           O  
ANISOU  285  O   GLN A  17     2891   3329   2564    975   -515    199       O  
ATOM    286  CB  GLN A  17      61.946  83.218  21.889  1.00 24.37           C  
ANISOU  286  CB  GLN A  17     3174   3831   2253    721     95    819       C  
ATOM    287  CG  GLN A  17      63.360  83.746  21.907  1.00 27.22           C  
ANISOU  287  CG  GLN A  17     3559   4270   2511    575    412    967       C  
ATOM    288  CD  GLN A  17      63.899  83.990  20.516  1.00 30.60           C  
ANISOU  288  CD  GLN A  17     4094   4742   2792    374    420   1030       C  
ATOM    289  OE1 GLN A  17      63.868  83.104  19.665  1.00 31.87           O  
ANISOU  289  OE1 GLN A  17     4276   4990   2841    322    400    811       O  
ATOM    290  NE2 GLN A  17      64.382  85.202  20.275  1.00 32.60           N  
ANISOU  290  NE2 GLN A  17     4345   4992   3049    287    278   1200       N  
ATOM    291  H   GLN A  17      59.699  82.396  22.480  1.00 26.48           H  
ATOM    292  HA  GLN A  17      62.121  82.068  23.582  1.00 25.98           H  
ATOM    293  HB2 GLN A  17      61.908  82.483  21.258  1.00 29.25           H  
ATOM    294  HB3 GLN A  17      61.361  83.935  21.599  1.00 29.25           H  
ATOM    295  HG2 GLN A  17      63.379  84.587  22.389  1.00 32.67           H  
ATOM    296  HG3 GLN A  17      63.935  83.100  22.345  1.00 32.67           H  
ATOM    297 HE21 GLN A  17      64.377  85.799  20.894  1.00 39.13           H  
ATOM    298 HE22 GLN A  17      64.700  85.391  19.499  1.00 39.13           H  
ATOM    299  N   LYS A  18      62.508  83.992  25.044  1.00 20.41           N  
ANISOU  299  N   LYS A  18     2551   2938   2266    696   -134    433       N  
ATOM    300  CA  LYS A  18      62.635  85.094  25.984  1.00 20.51           C  
ANISOU  300  CA  LYS A  18     2631   2884   2280    511     84    518       C  
ATOM    301  C   LYS A  18      64.109  85.356  26.253  1.00 20.08           C  
ANISOU  301  C   LYS A  18     2572   2665   2392    689     71    621       C  
ATOM    302  O   LYS A  18      64.961  84.484  26.073  1.00 20.89           O  
ANISOU  302  O   LYS A  18     2606   2803   2529    579    318    531       O  
ATOM    303  CB  LYS A  18      61.871  84.824  27.287  1.00 20.55           C  
ANISOU  303  CB  LYS A  18     2578   2917   2314    659    128    578       C  
ATOM    304  CG  LYS A  18      62.319  83.598  28.037  1.00 19.62           C  
ANISOU  304  CG  LYS A  18     2524   2764   2167    625     99    381       C  
ATOM    305  CD  LYS A  18      61.204  83.080  29.005  1.00 18.71           C  
ANISOU  305  CD  LYS A  18     2242   2694   2173    430     26    291       C  
ATOM    306  CE  LYS A  18      60.096  82.348  28.262  1.00 20.46           C  
ANISOU  306  CE  LYS A  18     2464   3102   2209    345    -52    651       C  
ATOM    307  NZ  LYS A  18      58.931  82.046  29.168  1.00 19.31           N  
ANISOU  307  NZ  LYS A  18     2244   3119   1973    179     52    885       N  
ATOM    308  H   LYS A  18      63.169  83.442  25.054  1.00 24.50           H  
ATOM    309  HA  LYS A  18      62.263  85.897  25.586  1.00 24.62           H  
ATOM    310  HB2 LYS A  18      61.988  85.586  27.876  1.00 24.67           H  
ATOM    311  HB3 LYS A  18      60.931  84.710  27.075  1.00 24.67           H  
ATOM    312  HG2 LYS A  18      62.527  82.892  27.405  1.00 23.55           H  
ATOM    313  HG3 LYS A  18      63.105  83.813  28.564  1.00 23.55           H  
ATOM    314  HD2 LYS A  18      61.597  82.465  29.644  1.00 22.46           H  
ATOM    315  HD3 LYS A  18      60.809  83.834  29.469  1.00 22.46           H  
ATOM    316  HE2 LYS A  18      59.779  82.901  27.532  1.00 24.57           H  
ATOM    317  HE3 LYS A  18      60.440  81.509  27.918  1.00 24.57           H  
ATOM    318  HZ1 LYS A  18      58.288  81.637  28.709  1.00 23.18           H  
ATOM    319  HZ2 LYS A  18      59.193  81.517  29.834  1.00 23.18           H  
ATOM    320  HZ3 LYS A  18      58.608  82.802  29.509  1.00 23.18           H  
ATOM    321  N   ASN A  19      64.396  86.586  26.669  1.00 20.43           N  
ANISOU  321  N   ASN A  19     2634   2520   2609    508    119    511       N  
ATOM    322  CA  ASN A  19      65.724  86.974  27.110  1.00 20.56           C  
ANISOU  322  CA  ASN A  19     2697   2503   2612    578    240    535       C  
ATOM    323  C   ASN A  19      65.855  86.723  28.606  1.00 19.59           C  
ANISOU  323  C   ASN A  19     2350   2620   2472    424    320    255       C  
ATOM    324  O   ASN A  19      64.888  86.873  29.365  1.00 21.21           O  
ANISOU  324  O   ASN A  19     2454   2969   2638    547    167    425       O  
ATOM    325  CB  ASN A  19      65.961  88.465  26.830  1.00 22.57           C  
ANISOU  325  CB  ASN A  19     3207   2576   2793    696    501    687       C  
ATOM    326  CG  ASN A  19      65.977  88.795  25.344  1.00 26.51           C  
ANISOU  326  CG  ASN A  19     4020   2962   3090    768    517    804       C  
ATOM    327  OD1 ASN A  19      66.310  87.971  24.513  1.00 28.11           O  
ANISOU  327  OD1 ASN A  19     4484   3244   2953    481    540    855       O  
ATOM    328  ND2 ASN A  19      65.621  90.022  25.016  1.00 29.66           N  
ANISOU  328  ND2 ASN A  19     4550   3397   3322    828    446    932       N  
ATOM    329  H   ASN A  19      63.822  87.225  26.705  1.00 24.52           H  
ATOM    330  HA  ASN A  19      66.396  86.459  26.636  1.00 24.68           H  
ATOM    331  HB2 ASN A  19      65.250  88.980  27.243  1.00 27.10           H  
ATOM    332  HB3 ASN A  19      66.818  88.723  27.203  1.00 27.10           H  
ATOM    333 HD21 ASN A  19      65.613  90.262  24.190  1.00 35.60           H  
ATOM    334 HD22 ASN A  19      65.398  90.583  25.629  1.00 35.60           H  
ATOM    335  N   ILE A  20      67.063  86.336  29.026  1.00 18.21           N  
ANISOU  335  N   ILE A  20     2146   2351   2423    312    343    279       N  
ATOM    336  CA AILE A  20      67.354  86.091  30.433  0.42 18.40           C  
ANISOU  336  CA AILE A  20     2231   2308   2451    159    270    249       C  
ATOM    337  CA BILE A  20      67.364  86.072  30.429  0.58 18.45           C  
ANISOU  337  CA BILE A  20     2206   2370   2435    117    200    305       C  
ATOM    338  C   ILE A  20      68.650  86.784  30.818  1.00 17.70           C  
ANISOU  338  C   ILE A  20     2078   2270   2376    162    375    316       C  
ATOM    339  O   ILE A  20      69.599  86.851  30.030  1.00 18.65           O  
ANISOU  339  O   ILE A  20     2266   2445   2375   -111    408     77       O  
ATOM    340  CB AILE A  20      67.424  84.588  30.777  0.42 19.58           C  
ANISOU  340  CB AILE A  20     2372   2446   2621    136    250    105       C  
ATOM    341  CB BILE A  20      67.477  84.563  30.745  0.58 19.95           C  
ANISOU  341  CB BILE A  20     2273   2700   2608     31     88    246       C  
ATOM    342  CG1AILE A  20      68.237  83.845  29.725  0.42 19.80           C  
ANISOU  342  CG1AILE A  20     2300   2500   2723     86    230     40       C  
ATOM    343  CG1BILE A  20      68.371  83.859  29.725  0.58 19.92           C  
ANISOU  343  CG1BILE A  20     2041   2937   2590   -127     -2    210       C  
ATOM    344  CG2AILE A  20      66.027  84.023  30.907  0.42 19.88           C  
ANISOU  344  CG2AILE A  20     2446   2481   2626    264    298     53       C  
ATOM    345  CG2BILE A  20      66.098  83.951  30.822  0.58 20.75           C  
ANISOU  345  CG2BILE A  20     2406   2768   2710    184     96    269       C  
ATOM    346  CD1AILE A  20      68.431  82.388  30.044  0.42 19.99           C  
ANISOU  346  CD1AILE A  20     2337   2450   2809    136    129    158       C  
ATOM    347  CD1BILE A  20      67.639  83.209  28.552  0.58 19.83           C  
ANISOU  347  CD1BILE A  20     1949   3060   2527   -112   -166    442       C  
ATOM    348  H  AILE A  20      67.734  86.209  28.504  0.42 21.86           H  
ATOM    349  H  BILE A  20      67.735  86.219  28.502  0.58 21.86           H  
ATOM    350  HA AILE A  20      66.636  86.484  30.953  0.42 22.08           H  
ATOM    351  HA BILE A  20      66.638  86.439  30.957  0.58 22.15           H  
ATOM    352  HB AILE A  20      67.874  84.476  31.629  0.42 23.50           H  
ATOM    353  HB BILE A  20      67.900  84.449  31.610  0.58 23.95           H  
ATOM    354 HG12AILE A  20      67.777  83.906  28.873  0.42 23.76           H  
ATOM    355 HG12BILE A  20      68.986  84.512  29.356  0.58 23.91           H  
ATOM    356 HG13AILE A  20      69.114  84.255  29.659  0.42 23.76           H  
ATOM    357 HG13BILE A  20      68.864  83.160  30.182  0.58 23.91           H  
ATOM    358 HG21AILE A  20      66.084  83.114  31.241  0.42 23.86           H  
ATOM    359 HG21BILE A  20      66.184  82.988  30.898  0.58 24.91           H  
ATOM    360 HG22AILE A  20      65.521  84.572  31.525  0.42 23.86           H  
ATOM    361 HG22BILE A  20      65.638  84.305  31.599  0.58 24.91           H  
ATOM    362 HG23AILE A  20      65.602  84.028  30.035  0.42 23.86           H  
ATOM    363 HG23BILE A  20      65.607  84.177  30.016  0.58 24.91           H  
ATOM    364 HD11AILE A  20      69.365  82.160  29.920  0.42 24.00           H  
ATOM    365 HD11BILE A  20      68.287  82.961  27.874  0.58 23.81           H  
ATOM    366 HD12AILE A  20      68.170  82.229  30.965  0.42 24.00           H  
ATOM    367 HD12BILE A  20      67.173  82.420  28.869  0.58 23.81           H  
ATOM    368 HD13AILE A  20      67.879  81.859  29.448  0.42 24.00           H  
ATOM    369 HD13BILE A  20      67.004  83.844  28.185  0.58 23.81           H  
ATOM    370  N   ASN A  21      68.687  87.284  32.043  1.00 16.41           N  
ANISOU  370  N   ASN A  21     1979   2071   2183    147    491     83       N  
ATOM    371  CA  ASN A  21      69.856  87.962  32.575  1.00 16.24           C  
ANISOU  371  CA  ASN A  21     1927   1953   2292    322    495    165       C  
ATOM    372  C   ASN A  21      70.835  86.930  33.109  1.00 16.27           C  
ANISOU  372  C   ASN A  21     2096   1862   2225     76    608    244       C  
ATOM    373  O   ASN A  21      70.481  86.102  33.951  1.00 16.69           O  
ANISOU  373  O   ASN A  21     2381   1811   2151    147    462    328       O  
ATOM    374  CB  ASN A  21      69.412  88.893  33.699  1.00 18.47           C  
ANISOU  374  CB  ASN A  21     2077   2198   2744    570    628    215       C  
ATOM    375  CG  ASN A  21      68.565  90.043  33.204  1.00 21.27           C  
ANISOU  375  CG  ASN A  21     2252   2598   3231    778    759    498       C  
ATOM    376  OD1 ASN A  21      67.411  90.215  33.601  1.00 25.14           O  
ANISOU  376  OD1 ASN A  21     2689   3104   3757    799    793    420       O  
ATOM    377  ND2 ASN A  21      69.120  90.825  32.337  1.00 22.03           N  
ANISOU  377  ND2 ASN A  21     2329   2670   3370    947   1044    645       N  
ATOM    378  H   ASN A  21      68.033  87.242  32.600  1.00 19.70           H  
ATOM    379  HA  ASN A  21      70.299  88.481  31.885  1.00 19.50           H  
ATOM    380  HB2 ASN A  21      68.888  88.388  34.340  1.00 22.18           H  
ATOM    381  HB3 ASN A  21      70.198  89.264  34.132  1.00 22.18           H  
ATOM    382 HD21 ASN A  21      68.683  91.496  32.021  1.00 26.44           H  
ATOM    383 HD22 ASN A  21      69.926  90.675  32.075  1.00 26.44           H  
ATOM    384  N   THR A  22      72.072  86.991  32.625  1.00 16.63           N  
ANISOU  384  N   THR A  22     2066   1880   2371    219    710    336       N  
ATOM    385  CA  THR A  22      73.095  86.024  32.959  1.00 16.51           C  
ANISOU  385  CA  THR A  22     2048   1769   2455    220    567    180       C  
ATOM    386  C   THR A  22      74.335  86.758  33.453  1.00 16.29           C  
ANISOU  386  C   THR A  22     1844   1695   2650    255    562    136       C  
ATOM    387  O   THR A  22      74.398  87.990  33.442  1.00 17.26           O  
ANISOU  387  O   THR A  22     2069   1817   2672    132    514    126       O  
ATOM    388  CB  THR A  22      73.385  85.120  31.742  1.00 16.83           C  
ANISOU  388  CB  THR A  22     2326   1773   2298      1    611    207       C  
ATOM    389  OG1 THR A  22      73.753  85.923  30.605  1.00 18.05           O  
ANISOU  389  OG1 THR A  22     2543   1867   2446    270    760     70       O  
ATOM    390  CG2 THR A  22      72.150  84.279  31.419  1.00 17.30           C  
ANISOU  390  CG2 THR A  22     2522   1941   2112    -25    410     80       C  
ATOM    391  H   THR A  22      72.343  87.605  32.087  1.00 19.96           H  
ATOM    392  HA  THR A  22      72.811  85.450  33.687  1.00 19.82           H  
ATOM    393  HB  THR A  22      74.122  84.522  31.942  1.00 20.21           H  
ATOM    394  HG1 THR A  22      73.889  85.430  29.938  1.00 21.66           H  
ATOM    395 HG21 THR A  22      72.347  83.663  30.697  1.00 20.77           H  
ATOM    396 HG22 THR A  22      71.880  83.772  32.201  1.00 20.77           H  
ATOM    397 HG23 THR A  22      71.417  84.855  31.149  1.00 20.77           H  
ATOM    398  N   THR A  23      75.319  85.982  33.905  1.00 16.78           N  
ANISOU  398  N   THR A  23     1684   1907   2787    226    357     15       N  
ATOM    399  CA  THR A  23      76.608  86.501  34.345  1.00 17.59           C  
ANISOU  399  CA  THR A  23     1773   2031   2881     51    391   -212       C  
ATOM    400  C   THR A  23      77.688  85.701  33.634  1.00 17.43           C  
ANISOU  400  C   THR A  23     1771   1857   2995   -148    443   -326       C  
ATOM    401  O   THR A  23      77.651  84.466  33.627  1.00 18.26           O  
ANISOU  401  O   THR A  23     1983   1855   3098     26    496   -493       O  
ATOM    402  CB  THR A  23      76.766  86.360  35.865  1.00 17.80           C  
ANISOU  402  CB  THR A  23     1753   2169   2841    150    346   -228       C  
ATOM    403  OG1 THR A  23      75.786  87.148  36.537  1.00 17.88           O  
ANISOU  403  OG1 THR A  23     1847   2084   2864    163    728   -201       O  
ATOM    404  CG2 THR A  23      78.123  86.870  36.309  1.00 19.07           C  
ANISOU  404  CG2 THR A  23     1768   2471   3007     33    285   -380       C  
ATOM    405  H   THR A  23      75.258  85.126  33.965  1.00 20.15           H  
ATOM    406  HA  THR A  23      76.695  87.440  34.118  1.00 21.12           H  
ATOM    407  HB  THR A  23      76.669  85.423  36.095  1.00 21.37           H  
ATOM    408  HG1 THR A  23      75.015  86.898  36.314  1.00 21.47           H  
ATOM    409 HG21 THR A  23      78.152  86.937  37.276  1.00 22.89           H  
ATOM    410 HG22 THR A  23      78.818  86.261  36.015  1.00 22.89           H  
ATOM    411 HG23 THR A  23      78.290  87.746  35.927  1.00 22.89           H  
ATOM    412  N   TYR A  24      78.655  86.400  33.057  1.00 18.91           N  
ANISOU  412  N   TYR A  24     1907   2114   3164   -328    760   -268       N  
ATOM    413  CA  TYR A  24      79.684  85.774  32.237  1.00 20.17           C  
ANISOU  413  CA  TYR A  24     2084   2393   3189   -147   1068    -12       C  
ATOM    414  C   TYR A  24      81.011  85.723  32.984  1.00 20.35           C  
ANISOU  414  C   TYR A  24     2214   2307   3209    -24    718    -58       C  
ATOM    415  O   TYR A  24      81.561  86.761  33.373  1.00 20.93           O  
ANISOU  415  O   TYR A  24     2332   2397   3221     89    649   -106       O  
ATOM    416  CB  TYR A  24      79.872  86.530  30.919  1.00 22.27           C  
ANISOU  416  CB  TYR A  24     2427   2722   3311   -124   1398    108       C  
ATOM    417  CG  TYR A  24      80.993  85.967  30.072  1.00 24.35           C  
ANISOU  417  CG  TYR A  24     2472   3166   3614    -89   1713   -230       C  
ATOM    418  CD1 TYR A  24      80.928  84.671  29.571  1.00 24.22           C  
ANISOU  418  CD1 TYR A  24     2442   3163   3597    320   1590   -359       C  
ATOM    419  CD2 TYR A  24      82.123  86.717  29.795  1.00 27.32           C  
ANISOU  419  CD2 TYR A  24     2843   3666   3872   -145   1885   -612       C  
ATOM    420  CE1 TYR A  24      81.951  84.147  28.804  1.00 26.53           C  
ANISOU  420  CE1 TYR A  24     2679   3545   3855    216   1635   -338       C  
ATOM    421  CE2 TYR A  24      83.150  86.197  29.029  1.00 29.15           C  
ANISOU  421  CE2 TYR A  24     3038   3903   4135    -35   1978   -741       C  
ATOM    422  CZ  TYR A  24      83.056  84.913  28.542  1.00 29.67           C  
ANISOU  422  CZ  TYR A  24     3073   4029   4171     53   1964   -640       C  
ATOM    423  OH  TYR A  24      84.085  84.408  27.785  1.00 33.27           O  
ANISOU  423  OH  TYR A  24     3447   4708   4486   -110   1991   -658       O  
ATOM    424  H   TYR A  24      78.736  87.253  33.127  1.00 22.70           H  
ATOM    425  HA  TYR A  24      79.405  84.863  32.057  1.00 24.22           H  
ATOM    426  HB2 TYR A  24      79.051  86.475  30.404  1.00 26.73           H  
ATOM    427  HB3 TYR A  24      80.079  87.457  31.114  1.00 26.73           H  
ATOM    428  HD1 TYR A  24      80.181  84.147  29.754  1.00 29.07           H  
ATOM    429  HD2 TYR A  24      82.192  87.582  30.129  1.00 32.80           H  
ATOM    430  HE1 TYR A  24      81.890  83.282  28.468  1.00 31.84           H  
ATOM    431  HE2 TYR A  24      83.901  86.713  28.843  1.00 34.99           H  
ATOM    432  HH  TYR A  24      84.685  84.988  27.693  1.00 39.93           H  
ATOM    433  N   SER A  25      81.530  84.516  33.164  1.00 19.93           N  
ANISOU  433  N   SER A  25     1988   2351   3234    118    512    -63       N  
ATOM    434  CA  SER A  25      82.885  84.317  33.671  1.00 22.35           C  
ANISOU  434  CA  SER A  25     2244   2874   3375    255    346   -178       C  
ATOM    435  C   SER A  25      83.282  82.937  33.146  1.00 21.60           C  
ANISOU  435  C   SER A  25     2220   2651   3337    177    431    -80       C  
ATOM    436  O   SER A  25      82.994  81.917  33.780  1.00 21.29           O  
ANISOU  436  O   SER A  25     2094   2628   3370    186    436   -103       O  
ATOM    437  CB  SER A  25      82.962  84.388  35.177  1.00 25.03           C  
ANISOU  437  CB  SER A  25     2513   3384   3612    395     32   -246       C  
ATOM    438  OG  SER A  25      84.296  84.180  35.603  1.00 26.89           O  
ANISOU  438  OG  SER A  25     2871   3595   3753    337    -73   -187       O  
ATOM    439  H   SER A  25      81.114  83.782  32.999  1.00 23.93           H  
ATOM    440  HA  SER A  25      83.484  85.000  33.330  1.00 26.83           H  
ATOM    441  HB2 SER A  25      82.666  85.264  35.472  1.00 30.04           H  
ATOM    442  HB3 SER A  25      82.393  83.701  35.559  1.00 30.04           H  
ATOM    443  HG  SER A  25      84.334  84.183  36.442  1.00 32.28           H  
ATOM    444  N   THR A  26      83.901  82.931  31.961  1.00 21.07           N  
ANISOU  444  N   THR A  26     2089   2635   3282    180    739   -103       N  
ATOM    445  CA  THR A  26      84.234  81.742  31.188  1.00 21.38           C  
ANISOU  445  CA  THR A  26     2204   2703   3217    265    584     -4       C  
ATOM    446  C   THR A  26      82.986  81.089  30.606  1.00 20.23           C  
ANISOU  446  C   THR A  26     2259   2604   2822    262    582    -40       C  
ATOM    447  O   THR A  26      82.908  80.878  29.391  1.00 21.51           O  
ANISOU  447  O   THR A  26     2425   2853   2896    433    652    -14       O  
ATOM    448  CB  THR A  26      85.039  80.746  32.010  1.00 23.01           C  
ANISOU  448  CB  THR A  26     2055   3057   3629    356    571   -139       C  
ATOM    449  OG1 THR A  26      86.216  81.382  32.511  1.00 24.73           O  
ANISOU  449  OG1 THR A  26     2060   3295   4040    264    398   -250       O  
ATOM    450  CG2 THR A  26      85.454  79.583  31.115  1.00 24.30           C  
ANISOU  450  CG2 THR A  26     2150   3347   3734    401    865   -116       C  
ATOM    451  H   THR A  26      84.152  83.650  31.562  1.00 25.30           H  
ATOM    452  HA  THR A  26      84.795  82.014  30.445  1.00 25.67           H  
ATOM    453  HB  THR A  26      84.509  80.417  32.753  1.00 27.62           H  
ATOM    454  HG1 THR A  26      86.658  80.841  32.978  1.00 29.68           H  
ATOM    455 HG21 THR A  26      86.122  79.042  31.563  1.00 29.17           H  
ATOM    456 HG22 THR A  26      84.684  79.029  30.914  1.00 29.17           H  
ATOM    457 HG23 THR A  26      85.825  79.920  30.285  1.00 29.17           H  
ATOM    458  N   TYR A  27      82.028  80.749  31.467  1.00 18.22           N  
ANISOU  458  N   TYR A  27     1991   2343   2590    289    561     18       N  
ATOM    459  CA  TYR A  27      80.696  80.317  31.089  1.00 17.57           C  
ANISOU  459  CA  TYR A  27     2021   2134   2522    296    498    -15       C  
ATOM    460  C   TYR A  27      79.706  81.435  31.375  1.00 18.35           C  
ANISOU  460  C   TYR A  27     2117   2195   2662    257    422   -187       C  
ATOM    461  O   TYR A  27      80.002  82.388  32.116  1.00 18.70           O  
ANISOU  461  O   TYR A  27     2130   2279   2694    309    498   -355       O  
ATOM    462  CB  TYR A  27      80.293  79.053  31.859  1.00 16.81           C  
ANISOU  462  CB  TYR A  27     1909   2102   2377    226    400    -15       C  
ATOM    463  CG  TYR A  27      81.000  77.823  31.342  1.00 15.80           C  
ANISOU  463  CG  TYR A  27     1866   1904   2233    357    346    125       C  
ATOM    464  CD1 TYR A  27      82.270  77.480  31.797  1.00 16.54           C  
ANISOU  464  CD1 TYR A  27     2018   1872   2394    240    171    -80       C  
ATOM    465  CD2 TYR A  27      80.414  77.019  30.379  1.00 16.28           C  
ANISOU  465  CD2 TYR A  27     2048   1808   2332    286     97    190       C  
ATOM    466  CE1 TYR A  27      82.919  76.375  31.314  1.00 16.92           C  
ANISOU  466  CE1 TYR A  27     2041   1966   2423     60    253    -38       C  
ATOM    467  CE2 TYR A  27      81.065  75.901  29.890  1.00 16.60           C  
ANISOU  467  CE2 TYR A  27     2255   1842   2212    323     74    179       C  
ATOM    468  CZ  TYR A  27      82.321  75.600  30.347  1.00 16.14           C  
ANISOU  468  CZ  TYR A  27     1900   1803   2431     89    326    130       C  
ATOM    469  OH  TYR A  27      82.992  74.502  29.858  1.00 17.57           O  
ANISOU  469  OH  TYR A  27     1905   2034   2736    222    374    174       O  
ATOM    470  H   TYR A  27      82.140  80.763  32.320  1.00 21.88           H  
ATOM    471  HA  TYR A  27      80.671  80.110  30.142  1.00 21.10           H  
ATOM    472  HB2 TYR A  27      80.522  79.163  32.795  1.00 20.18           H  
ATOM    473  HB3 TYR A  27      79.337  78.915  31.766  1.00 20.18           H  
ATOM    474  HD1 TYR A  27      82.684  78.009  32.440  1.00 19.85           H  
ATOM    475  HD2 TYR A  27      79.568  77.234  30.057  1.00 19.55           H  
ATOM    476  HE1 TYR A  27      83.761  76.149  31.638  1.00 20.32           H  
ATOM    477  HE2 TYR A  27      80.654  75.359  29.256  1.00 19.93           H  
ATOM    478  HH  TYR A  27      82.555  74.153  29.232  1.00 21.09           H  
ATOM    479  N   TYR A  28      78.521  81.292  30.788  1.00 18.19           N  
ANISOU  479  N   TYR A  28     2190   2242   2479    344    538     40       N  
ATOM    480  CA  TYR A  28      77.380  82.150  31.077  1.00 17.27           C  
ANISOU  480  CA  TYR A  28     2237   2016   2308    316    516   -169       C  
ATOM    481  C   TYR A  28      76.515  81.439  32.105  1.00 16.66           C  
ANISOU  481  C   TYR A  28     2225   1916   2188     63    398   -221       C  
ATOM    482  O   TYR A  28      76.003  80.340  31.844  1.00 18.54           O  
ANISOU  482  O   TYR A  28     2663   2215   2167    -41    394   -258       O  
ATOM    483  CB  TYR A  28      76.574  82.452  29.818  1.00 17.87           C  
ANISOU  483  CB  TYR A  28     2274   2093   2423    502    586     61       C  
ATOM    484  CG  TYR A  28      77.354  83.244  28.804  1.00 18.78           C  
ANISOU  484  CG  TYR A  28     2317   2258   2561    548    548    397       C  
ATOM    485  CD1 TYR A  28      77.303  84.631  28.791  1.00 19.40           C  
ANISOU  485  CD1 TYR A  28     2335   2345   2690    567    561    477       C  
ATOM    486  CD2 TYR A  28      78.171  82.607  27.873  1.00 19.67           C  
ANISOU  486  CD2 TYR A  28     2537   2451   2488    498    683    575       C  
ATOM    487  CE1 TYR A  28      78.016  85.361  27.881  1.00 20.27           C  
ANISOU  487  CE1 TYR A  28     2568   2563   2572    555    862    505       C  
ATOM    488  CE2 TYR A  28      78.903  83.338  26.942  1.00 20.62           C  
ANISOU  488  CE2 TYR A  28     2602   2675   2558    448    950    734       C  
ATOM    489  CZ  TYR A  28      78.821  84.717  26.955  1.00 21.20           C  
ANISOU  489  CZ  TYR A  28     2626   2763   2666    394   1030    702       C  
ATOM    490  OH  TYR A  28      79.545  85.446  26.043  1.00 23.99           O  
ANISOU  490  OH  TYR A  28     2903   3218   2993    183    995    780       O  
ATOM    491  H   TYR A  28      78.352  80.686  30.201  1.00 21.84           H  
ATOM    492  HA  TYR A  28      77.687  82.996  31.438  1.00 20.73           H  
ATOM    493  HB2 TYR A  28      76.308  81.616  29.406  1.00 21.45           H  
ATOM    494  HB3 TYR A  28      75.789  82.967  30.062  1.00 21.45           H  
ATOM    495  HD1 TYR A  28      76.773  85.073  29.414  1.00 23.28           H  
ATOM    496  HD2 TYR A  28      78.228  81.679  27.873  1.00 23.62           H  
ATOM    497  HE1 TYR A  28      77.960  86.289  27.883  1.00 24.33           H  
ATOM    498  HE2 TYR A  28      79.440  82.904  26.319  1.00 24.75           H  
ATOM    499  HH  TYR A  28      80.014  84.933  25.572  1.00 28.79           H  
ATOM    500  N   TYR A  29      76.343  82.073  33.262  1.00 16.42           N  
ANISOU  500  N   TYR A  29     2009   2035   2196    147    164    -82       N  
ATOM    501  CA  TYR A  29      75.607  81.492  34.375  1.00 16.13           C  
ANISOU  501  CA  TYR A  29     1730   2130   2268    186    318   -110       C  
ATOM    502  C   TYR A  29      74.234  82.138  34.489  1.00 15.09           C  
ANISOU  502  C   TYR A  29     1727   1770   2236    264    247     21       C  
ATOM    503  O   TYR A  29      74.069  83.339  34.235  1.00 15.69           O  
ANISOU  503  O   TYR A  29     1926   1762   2272    125    205   -218       O  
ATOM    504  CB  TYR A  29      76.371  81.686  35.683  1.00 16.64           C  
ANISOU  504  CB  TYR A  29     1623   2401   2297    323    373   -147       C  
ATOM    505  CG  TYR A  29      77.625  80.831  35.755  1.00 17.29           C  
ANISOU  505  CG  TYR A  29     1632   2562   2376    409    315   -236       C  
ATOM    506  CD1 TYR A  29      78.835  81.287  35.250  1.00 18.76           C  
ANISOU  506  CD1 TYR A  29     1683   3021   2423    305    321   -277       C  
ATOM    507  CD2 TYR A  29      77.580  79.549  36.292  1.00 16.90           C  
ANISOU  507  CD2 TYR A  29     1633   2459   2328    372    330   -253       C  
ATOM    508  CE1 TYR A  29      79.984  80.488  35.292  1.00 18.52           C  
ANISOU  508  CE1 TYR A  29     1545   3077   2414    306    260   -112       C  
ATOM    509  CE2 TYR A  29      78.712  78.756  36.351  1.00 17.92           C  
ANISOU  509  CE2 TYR A  29     1708   2714   2386    295    246   -199       C  
ATOM    510  CZ  TYR A  29      79.911  79.217  35.845  1.00 18.68           C  
ANISOU  510  CZ  TYR A  29     1526   3119   2453    497    178   -170       C  
ATOM    511  OH  TYR A  29      81.038  78.414  35.903  1.00 20.95           O  
ANISOU  511  OH  TYR A  29     1893   3410   2658    580    259   -172       O  
ATOM    512  H   TYR A  29      76.652  82.858  33.426  1.00 19.71           H  
ATOM    513  HA  TYR A  29      75.488  80.541  34.225  1.00 19.36           H  
ATOM    514  HB2 TYR A  29      76.636  82.616  35.760  1.00 19.97           H  
ATOM    515  HB3 TYR A  29      75.797  81.442  36.425  1.00 19.97           H  
ATOM    516  HD1 TYR A  29      78.883  82.138  34.878  1.00 22.52           H  
ATOM    517  HD2 TYR A  29      76.774  79.219  36.618  1.00 20.28           H  
ATOM    518  HE1 TYR A  29      80.789  80.805  34.952  1.00 22.23           H  
ATOM    519  HE2 TYR A  29      78.665  77.909  36.732  1.00 21.51           H  
ATOM    520  HH  TYR A  29      80.818  77.621  36.071  1.00 25.15           H  
ATOM    521  N   LEU A  30      73.252  81.331  34.919  1.00 14.33           N  
ANISOU  521  N   LEU A  30     1600   1514   2330    174    216     41       N  
ATOM    522  CA  LEU A  30      71.922  81.858  35.233  1.00 14.00           C  
ANISOU  522  CA  LEU A  30     1591   1512   2215    173    156   -172       C  
ATOM    523  C   LEU A  30      71.993  82.580  36.576  1.00 14.71           C  
ANISOU  523  C   LEU A  30     1604   1792   2192    164    308    -66       C  
ATOM    524  O   LEU A  30      71.571  82.082  37.632  1.00 14.27           O  
ANISOU  524  O   LEU A  30     1485   1787   2150    188    108    -96       O  
ATOM    525  CB  LEU A  30      70.855  80.775  35.217  1.00 14.99           C  
ANISOU  525  CB  LEU A  30     1753   1738   2204    101    268    -11       C  
ATOM    526  CG  LEU A  30      70.583  80.156  33.841  1.00 15.03           C  
ANISOU  526  CG  LEU A  30     1676   1842   2193    112    151     78       C  
ATOM    527  CD1 LEU A  30      69.492  79.104  33.969  1.00 15.51           C  
ANISOU  527  CD1 LEU A  30     1513   1968   2410    -52    122     93       C  
ATOM    528  CD2 LEU A  30      70.173  81.218  32.837  1.00 16.33           C  
ANISOU  528  CD2 LEU A  30     2198   1823   2185    -23    273    223       C  
ATOM    529  H   LEU A  30      73.335  80.483  35.033  1.00 17.20           H  
ATOM    530  HA  LEU A  30      71.679  82.500  34.548  1.00 16.81           H  
ATOM    531  HB2 LEU A  30      71.135  80.059  35.808  1.00 17.99           H  
ATOM    532  HB3 LEU A  30      70.023  81.160  35.534  1.00 17.99           H  
ATOM    533  HG  LEU A  30      71.394  79.739  33.511  1.00 18.05           H  
ATOM    534 HD11 LEU A  30      69.336  78.704  33.099  1.00 18.61           H  
ATOM    535 HD12 LEU A  30      69.780  78.425  34.599  1.00 18.61           H  
ATOM    536 HD13 LEU A  30      68.680  79.529  34.288  1.00 18.61           H  
ATOM    537 HD21 LEU A  30      69.756  80.787  32.074  1.00 19.61           H  
ATOM    538 HD22 LEU A  30      69.545  81.826  33.258  1.00 19.61           H  
ATOM    539 HD23 LEU A  30      70.963  81.704  32.551  1.00 19.61           H  
ATOM    540  N   GLN A  31      72.554  83.784  36.510  1.00 15.38           N  
ANISOU  540  N   GLN A  31     1719   1820   2306     69    239   -144       N  
ATOM    541  CA  GLN A  31      72.699  84.677  37.653  1.00 15.07           C  
ANISOU  541  CA  GLN A  31     1664   1743   2317     66    466    -37       C  
ATOM    542  C   GLN A  31      72.326  86.060  37.143  1.00 15.93           C  
ANISOU  542  C   GLN A  31     1832   1942   2277     70    456    -35       C  
ATOM    543  O   GLN A  31      73.031  86.630  36.306  1.00 15.52           O  
ANISOU  543  O   GLN A  31     1620   1978   2298    -42    504     29       O  
ATOM    544  CB  GLN A  31      74.122  84.647  38.196  1.00 16.44           C  
ANISOU  544  CB  GLN A  31     1729   1962   2553    -89    167   -114       C  
ATOM    545  CG  GLN A  31      74.376  85.669  39.276  1.00 16.81           C  
ANISOU  545  CG  GLN A  31     1701   2013   2674   -104     11   -279       C  
ATOM    546  CD  GLN A  31      75.778  85.599  39.794  1.00 18.33           C  
ANISOU  546  CD  GLN A  31     1808   2284   2873    -28   -116   -289       C  
ATOM    547  OE1 GLN A  31      76.323  84.511  40.006  1.00 19.05           O  
ANISOU  547  OE1 GLN A  31     1756   2395   3088     73   -167   -272       O  
ATOM    548  NE2 GLN A  31      76.383  86.759  40.017  1.00 18.69           N  
ANISOU  548  NE2 GLN A  31     1745   2417   2938     81    -48   -346       N  
ATOM    549  H   GLN A  31      72.871  84.118  35.784  1.00 18.47           H  
ATOM    550  HA  GLN A  31      72.105  84.423  38.377  1.00 18.09           H  
ATOM    551  HB2 GLN A  31      74.295  83.770  38.571  1.00 19.73           H  
ATOM    552  HB3 GLN A  31      74.738  84.825  37.468  1.00 19.73           H  
ATOM    553  HG2 GLN A  31      74.230  86.557  38.916  1.00 20.18           H  
ATOM    554  HG3 GLN A  31      73.771  85.507  40.017  1.00 20.18           H  
ATOM    555 HE21 GLN A  31      75.968  87.496  39.863  1.00 22.43           H  
ATOM    556 HE22 GLN A  31      77.189  86.773  40.315  1.00 22.43           H  
ATOM    557  N   ASP A  32      71.207  86.569  37.644  1.00 15.88           N  
ANISOU  557  N   ASP A  32     1816   1873   2345    142    491     51       N  
ATOM    558  CA  ASP A  32      70.637  87.851  37.257  1.00 15.29           C  
ANISOU  558  CA  ASP A  32     1753   1813   2245    191    297   -141       C  
ATOM    559  C   ASP A  32      70.995  88.849  38.349  1.00 16.42           C  
ANISOU  559  C   ASP A  32     1808   1926   2505    -42    311   -138       C  
ATOM    560  O   ASP A  32      70.447  88.790  39.453  1.00 16.75           O  
ANISOU  560  O   ASP A  32     1865   1976   2521    -68    469   -174       O  
ATOM    561  CB  ASP A  32      69.123  87.668  37.146  1.00 15.55           C  
ANISOU  561  CB  ASP A  32     1677   1869   2363    315    175   -179       C  
ATOM    562  CG  ASP A  32      68.363  88.969  36.943  1.00 15.62           C  
ANISOU  562  CG  ASP A  32     1516   1851   2569    266    286    -97       C  
ATOM    563  OD1 ASP A  32      68.975  90.049  36.775  1.00 16.94           O  
ANISOU  563  OD1 ASP A  32     1842   1880   2716    127    278    -78       O  
ATOM    564  OD2 ASP A  32      67.115  88.885  36.944  1.00 17.45           O  
ANISOU  564  OD2 ASP A  32     1706   1926   2998    205    187    -84       O  
ATOM    565  H   ASP A  32      70.737  86.167  38.242  1.00 19.07           H  
ATOM    566  HA  ASP A  32      70.994  88.179  36.417  1.00 18.36           H  
ATOM    567  HB2 ASP A  32      68.933  87.093  36.388  1.00 18.67           H  
ATOM    568  HB3 ASP A  32      68.797  87.259  37.963  1.00 18.67           H  
ATOM    569  N   ASN A  33      71.928  89.745  38.049  1.00 17.03           N  
ANISOU  569  N   ASN A  33     1810   1906   2755   -139    471   -180       N  
ATOM    570  CA  ASN A  33      72.375  90.741  39.011  1.00 18.66           C  
ANISOU  570  CA  ASN A  33     1871   2057   3161   -159    381   -340       C  
ATOM    571  C   ASN A  33      71.513  91.993  39.017  1.00 19.51           C  
ANISOU  571  C   ASN A  33     1980   2056   3376    -35    490   -450       C  
ATOM    572  O   ASN A  33      71.824  92.933  39.763  1.00 20.66           O  
ANISOU  572  O   ASN A  33     2052   2219   3577    -79    536   -444       O  
ATOM    573  CB  ASN A  33      73.817  91.121  38.710  1.00 18.44           C  
ANISOU  573  CB  ASN A  33     1826   1980   3201   -125    364   -463       C  
ATOM    574  CG  ASN A  33      74.715  89.910  38.648  1.00 18.66           C  
ANISOU  574  CG  ASN A  33     1813   2090   3186   -135    424   -305       C  
ATOM    575  OD1 ASN A  33      74.750  89.106  39.580  1.00 19.23           O  
ANISOU  575  OD1 ASN A  33     1989   2157   3159   -366    375   -242       O  
ATOM    576  ND2 ASN A  33      75.420  89.747  37.534  1.00 19.20           N  
ANISOU  576  ND2 ASN A  33     1886   2190   3220   -112    319   -240       N  
ATOM    577  H   ASN A  33      72.321  89.794  37.285  1.00 20.44           H  
ATOM    578  HA  ASN A  33      72.336  90.357  39.901  1.00 22.40           H  
ATOM    579  HB2 ASN A  33      73.856  91.572  37.852  1.00 22.14           H  
ATOM    580  HB3 ASN A  33      74.146  91.707  39.409  1.00 22.14           H  
ATOM    581 HD21 ASN A  33      75.946  89.072  37.452  1.00 23.05           H  
ATOM    582 HD22 ASN A  33      75.350  90.318  36.894  1.00 23.05           H  
ATOM    583  N   THR A  34      70.443  92.033  38.214  1.00 18.34           N  
ANISOU  583  N   THR A  34     1786   1837   3346    -69    678   -282       N  
ATOM    584  CA  THR A  34      69.667  93.258  38.059  1.00 18.80           C  
ANISOU  584  CA  THR A  34     2073   1691   3379     92    674   -233       C  
ATOM    585  C   THR A  34      68.537  93.388  39.074  1.00 19.11           C  
ANISOU  585  C   THR A  34     2186   1761   3312    206    501   -440       C  
ATOM    586  O   THR A  34      67.895  94.449  39.131  1.00 20.49           O  
ANISOU  586  O   THR A  34     2530   1851   3404    286    324   -573       O  
ATOM    587  CB  THR A  34      69.053  93.366  36.656  1.00 20.49           C  
ANISOU  587  CB  THR A  34     2521   1731   3532     34    500     -7       C  
ATOM    588  OG1 THR A  34      67.947  92.458  36.512  1.00 19.66           O  
ANISOU  588  OG1 THR A  34     2456   1451   3564    102    518   -150       O  
ATOM    589  CG2 THR A  34      70.087  93.098  35.579  1.00 21.64           C  
ANISOU  589  CG2 THR A  34     2777   1940   3507    107    511    114       C  
ATOM    590  H   THR A  34      70.153  91.366  37.755  1.00 22.02           H  
ATOM    591  HA  THR A  34      70.284  93.998  38.173  1.00 22.57           H  
ATOM    592  HB  THR A  34      68.726  94.270  36.534  1.00 24.59           H  
ATOM    593  HG1 THR A  34      68.207  91.667  36.625  1.00 23.60           H  
ATOM    594 HG21 THR A  34      69.708  93.275  34.704  1.00 25.98           H  
ATOM    595 HG22 THR A  34      70.858  93.672  35.709  1.00 25.98           H  
ATOM    596 HG23 THR A  34      70.374  92.172  35.617  1.00 25.98           H  
ATOM    597  N   ARG A  35      68.293  92.356  39.881  1.00 18.63           N  
ANISOU  597  N   ARG A  35     2073   1900   3106    -93    280   -281       N  
ATOM    598  CA  ARG A  35      67.162  92.328  40.801  1.00 17.39           C  
ANISOU  598  CA  ARG A  35     1930   1825   2853   -120    468   -295       C  
ATOM    599  C   ARG A  35      67.640  91.988  42.207  1.00 18.07           C  
ANISOU  599  C   ARG A  35     2059   1934   2873    -56    172   -530       C  
ATOM    600  O   ARG A  35      68.005  90.840  42.490  1.00 19.15           O  
ANISOU  600  O   ARG A  35     2141   2134   3002    241     39   -758       O  
ATOM    601  CB  ARG A  35      66.103  91.332  40.317  1.00 17.37           C  
ANISOU  601  CB  ARG A  35     1980   1957   2662   -108    649   -198       C  
ATOM    602  CG  ARG A  35      65.438  91.781  39.016  1.00 16.53           C  
ANISOU  602  CG  ARG A  35     1866   1834   2582     96    335     10       C  
ATOM    603  CD  ARG A  35      64.525  90.722  38.462  1.00 16.41           C  
ANISOU  603  CD  ARG A  35     1924   1888   2423    191    273    245       C  
ATOM    604  NE  ARG A  35      63.715  91.187  37.347  1.00 16.85           N  
ANISOU  604  NE  ARG A  35     1926   2028   2448    211    434    280       N  
ATOM    605  CZ  ARG A  35      63.921  90.892  36.063  1.00 17.73           C  
ANISOU  605  CZ  ARG A  35     2170   2118   2450    584    590    309       C  
ATOM    606  NH1 ARG A  35      64.948  90.147  35.667  1.00 19.19           N  
ANISOU  606  NH1 ARG A  35     2442   2332   2518    775    559    258       N  
ATOM    607  NH2 ARG A  35      63.074  91.372  35.164  1.00 19.40           N  
ANISOU  607  NH2 ARG A  35     2594   2293   2486    671    415    157       N  
ATOM    608  H   ARG A  35      68.781  91.648  39.911  1.00 22.37           H  
ATOM    609  HA  ARG A  35      66.772  93.214  40.846  1.00 20.88           H  
ATOM    610  HB2 ARG A  35      66.524  90.472  40.160  1.00 20.85           H  
ATOM    611  HB3 ARG A  35      65.415  91.246  40.994  1.00 20.85           H  
ATOM    612  HG2 ARG A  35      64.912  92.578  39.183  1.00 19.85           H  
ATOM    613  HG3 ARG A  35      66.122  91.968  38.354  1.00 19.85           H  
ATOM    614  HD2 ARG A  35      65.061  89.976  38.149  1.00 19.70           H  
ATOM    615  HD3 ARG A  35      63.923  90.427  39.163  1.00 19.70           H  
ATOM    616  HE  ARG A  35      63.047  91.695  37.532  1.00 20.23           H  
ATOM    617 HH11 ARG A  35      65.505  89.839  36.246  1.00 23.04           H  
ATOM    618 HH12 ARG A  35      65.056  89.973  34.832  1.00 23.04           H  
ATOM    619 HH21 ARG A  35      62.412  91.860  35.415  1.00 23.29           H  
ATOM    620 HH22 ARG A  35      63.187  91.195  34.330  1.00 23.29           H  
ATOM    621  N   GLY A  36      67.605  92.981  43.092  1.00 18.35           N  
ANISOU  621  N   GLY A  36     2051   2226   2696   -237    350   -598       N  
ATOM    622  CA  GLY A  36      67.949  92.773  44.484  1.00 18.63           C  
ANISOU  622  CA  GLY A  36     2099   2335   2646   -339    330   -734       C  
ATOM    623  C   GLY A  36      69.326  92.181  44.654  1.00 18.46           C  
ANISOU  623  C   GLY A  36     1923   2612   2478   -587    388   -751       C  
ATOM    624  O   GLY A  36      70.291  92.570  43.990  1.00 21.02           O  
ANISOU  624  O   GLY A  36     2112   3036   2837   -641    202   -612       O  
ATOM    625  H   GLY A  36      67.383  93.792  42.909  1.00 22.03           H  
ATOM    626  HA2 GLY A  36      67.922  93.623  44.952  1.00 22.37           H  
ATOM    627  HA3 GLY A  36      67.305  92.170  44.887  1.00 22.37           H  
ATOM    628  N  AASN A  37      69.421  91.220  45.574  0.48 18.27           N  
ANISOU  628  N  AASN A  37     1798   2597   2546   -342    439   -726       N  
ATOM    629  N  BASN A  37      69.426  91.225  45.569  0.52 18.05           N  
ANISOU  629  N  BASN A  37     1870   2504   2484   -500    477   -730       N  
ATOM    630  CA AASN A  37      70.653  90.495  45.832  0.48 18.87           C  
ANISOU  630  CA AASN A  37     1796   2762   2612   -224    303   -633       C  
ATOM    631  CA BASN A  37      70.665  90.502  45.798  0.52 18.48           C  
ANISOU  631  CA BASN A  37     1949   2595   2479   -530    369   -650       C  
ATOM    632  C  AASN A  37      70.952  89.455  44.763  0.48 17.91           C  
ANISOU  632  C  AASN A  37     1704   2587   2514   -319    202   -648       C  
ATOM    633  C  BASN A  37      70.814  89.318  44.861  0.52 17.58           C  
ANISOU  633  C  BASN A  37     1850   2460   2369   -601    222   -555       C  
ATOM    634  O  AASN A  37      71.976  88.759  44.860  0.48 17.46           O  
ANISOU  634  O  AASN A  37     1613   2605   2416   -284    227   -683       O  
ATOM    635  O  BASN A  37      71.610  88.407  45.134  0.52 17.34           O  
ANISOU  635  O  BASN A  37     2026   2369   2192   -764    136   -463       O  
ATOM    636  CB AASN A  37      70.575  89.782  47.184  0.48 19.83           C  
ANISOU  636  CB AASN A  37     1831   2992   2710   -113    259   -644       C  
ATOM    637  CB BASN A  37      70.775  90.115  47.268  0.52 19.11           C  
ANISOU  637  CB BASN A  37     2063   2695   2503   -576    378   -817       C  
ATOM    638  CG AASN A  37      70.634  90.735  48.366  0.48 20.81           C  
ANISOU  638  CG AASN A  37     1937   3129   2842   -165    125   -699       C  
ATOM    639  CG BASN A  37      71.115  91.305  48.141  0.52 20.40           C  
ANISOU  639  CG BASN A  37     2259   2882   2608   -676    277   -891       C  
ATOM    640  OD1AASN A  37      70.640  91.958  48.210  0.48 20.95           O  
ANISOU  640  OD1AASN A  37     1888   3170   2901   -274     28   -842       O  
ATOM    641  OD1BASN A  37      72.012  92.071  47.816  0.52 21.91           O  
ANISOU  641  OD1BASN A  37     2377   3076   2873   -815    138  -1078       O  
ATOM    642  ND2AASN A  37      70.664  90.167  49.565  0.48 20.58           N  
ANISOU  642  ND2AASN A  37     2004   3029   2788    -95    -13   -640       N  
ATOM    643  ND2BASN A  37      70.380  91.484  49.230  0.52 19.81           N  
ANISOU  643  ND2BASN A  37     2289   2886   2351   -613    247   -924       N  
ATOM    644  H  AASN A  37      68.766  90.969  46.072  0.48 21.93           H  
ATOM    645  H  BASN A  37      68.777  90.977  46.076  0.52 21.67           H  
ATOM    646  HA AASN A  37      71.381  91.135  45.862  0.48 22.65           H  
ATOM    647  HA BASN A  37      71.423  91.081  45.621  0.52 22.19           H  
ATOM    648  HB2AASN A  37      69.738  89.295  47.236  0.48 23.80           H  
ATOM    649  HB2BASN A  37      69.927  89.752  47.568  0.52 22.94           H  
ATOM    650  HB3AASN A  37      71.322  89.167  47.260  0.48 23.80           H  
ATOM    651  HB3BASN A  37      71.476  89.452  47.372  0.52 22.94           H  
ATOM    652 HD21AASN A  37      70.698  90.656  50.272  0.48 24.71           H  
ATOM    653 HD21BASN A  37      70.541  92.148  49.752  0.52 23.78           H  
ATOM    654 HD22AASN A  37      70.649  89.310  49.636  0.48 24.71           H  
ATOM    655 HD22BASN A  37      69.743  90.937  49.414  0.52 23.78           H  
ATOM    656  N   GLY A  38      70.084  89.323  43.759  1.00 17.36           N  
ANISOU  656  N   GLY A  38     1690   2417   2490   -377    138   -567       N  
ATOM    657  CA  GLY A  38      70.317  88.406  42.671  1.00 16.33           C  
ANISOU  657  CA  GLY A  38     1779   2085   2340   -355    148   -434       C  
ATOM    658  C   GLY A  38      69.239  87.350  42.544  1.00 15.74           C  
ANISOU  658  C   GLY A  38     1711   2012   2258   -302    251   -405       C  
ATOM    659  O   GLY A  38      68.573  86.986  43.523  1.00 16.52           O  
ANISOU  659  O   GLY A  38     1659   2354   2263   -310     20   -412       O  
ATOM    660  H  AGLY A  38      69.347  89.762  43.693  0.48 20.85           H  
ATOM    661  H  BGLY A  38      69.431  89.864  43.618  0.52 20.85           H  
ATOM    662  HA2 GLY A  38      70.355  88.903  41.839  1.00 19.60           H  
ATOM    663  HA3 GLY A  38      71.166  87.958  42.810  1.00 19.60           H  
ATOM    664  N   ILE A  39      69.059  86.857  41.326  1.00 14.84           N  
ANISOU  664  N   ILE A  39     1896   1650   2091    -72    413   -284       N  
ATOM    665  CA  ILE A  39      68.265  85.668  41.047  1.00 13.88           C  
ANISOU  665  CA  ILE A  39     1721   1672   1881    -39    144   -225       C  
ATOM    666  C   ILE A  39      69.214  84.629  40.461  1.00 13.88           C  
ANISOU  666  C   ILE A  39     1738   1722   1814    -88     64   -220       C  
ATOM    667  O   ILE A  39      69.937  84.914  39.498  1.00 14.07           O  
ANISOU  667  O   ILE A  39     1704   1689   1952    -89     21   -293       O  
ATOM    668  CB  ILE A  39      67.080  85.991  40.121  1.00 14.71           C  
ANISOU  668  CB  ILE A  39     1727   1690   2173     38    121   -128       C  
ATOM    669  CG1 ILE A  39      66.170  87.009  40.846  1.00 17.15           C  
ANISOU  669  CG1 ILE A  39     1853   2090   2575     56     -6      1       C  
ATOM    670  CG2 ILE A  39      66.314  84.734  39.757  1.00 14.55           C  
ANISOU  670  CG2 ILE A  39     1876   1616   2036    -96     -8   -182       C  
ATOM    671  CD1 ILE A  39      64.979  87.451  40.049  1.00 18.84           C  
ANISOU  671  CD1 ILE A  39     1966   2465   2726    -98    -61   -181       C  
ATOM    672  H   ILE A  39      69.401  87.209  40.619  1.00 17.81           H  
ATOM    673  HA  ILE A  39      67.888  85.297  41.860  1.00 16.67           H  
ATOM    674  HB  ILE A  39      67.407  86.373  39.291  1.00 17.66           H  
ATOM    675 HG12 ILE A  39      65.841  86.603  41.663  1.00 20.59           H  
ATOM    676 HG13 ILE A  39      66.693  87.798  41.055  1.00 20.59           H  
ATOM    677 HG21 ILE A  39      65.574  84.972  39.175  1.00 17.46           H  
ATOM    678 HG22 ILE A  39      66.910  84.121  39.299  1.00 17.46           H  
ATOM    679 HG23 ILE A  39      65.977  84.323  40.568  1.00 17.46           H  
ATOM    680 HD11 ILE A  39      64.577  88.220  40.483  1.00 22.61           H  
ATOM    681 HD12 ILE A  39      65.269  87.690  39.155  1.00 22.61           H  
ATOM    682 HD13 ILE A  39      64.340  86.723  40.006  1.00 22.61           H  
ATOM    683  N   PHE A  40      69.239  83.449  41.076  1.00 13.41           N  
ANISOU  683  N   PHE A  40     1705   1733   1656     58    172   -221       N  
ATOM    684  CA  PHE A  40      70.207  82.408  40.777  1.00 13.48           C  
ANISOU  684  CA  PHE A  40     1656   1636   1828    177    -53   -201       C  
ATOM    685  C   PHE A  40      69.453  81.123  40.481  1.00 12.84           C  
ANISOU  685  C   PHE A  40     1496   1659   1722    148     28   -216       C  
ATOM    686  O   PHE A  40      68.624  80.705  41.286  1.00 13.05           O  
ANISOU  686  O   PHE A  40     1480   1636   1844     56     57   -112       O  
ATOM    687  CB  PHE A  40      71.103  82.137  41.988  1.00 14.36           C  
ANISOU  687  CB  PHE A  40     1614   1834   2006     92   -125   -390       C  
ATOM    688  CG  PHE A  40      71.882  83.338  42.480  1.00 15.27           C  
ANISOU  688  CG  PHE A  40     1707   1953   2140   -148   -114   -302       C  
ATOM    689  CD1 PHE A  40      71.281  84.305  43.279  1.00 16.13           C  
ANISOU  689  CD1 PHE A  40     1934   2008   2186   -210   -156   -185       C  
ATOM    690  CD2 PHE A  40      73.224  83.484  42.159  1.00 16.79           C  
ANISOU  690  CD2 PHE A  40     1880   2111   2388   -331    -72   -113       C  
ATOM    691  CE1 PHE A  40      72.014  85.394  43.742  1.00 16.67           C  
ANISOU  691  CE1 PHE A  40     2011   1911   2410   -204   -141   -208       C  
ATOM    692  CE2 PHE A  40      73.954  84.572  42.608  1.00 17.41           C  
ANISOU  692  CE2 PHE A  40     1999   2153   2463   -437    -21   -235       C  
ATOM    693  CZ  PHE A  40      73.347  85.521  43.402  1.00 17.40           C  
ANISOU  693  CZ  PHE A  40     2140   1984   2488   -503   -220   -354       C  
ATOM    694  H   PHE A  40      68.683  83.226  41.693  1.00 16.10           H  
ATOM    695  HA  PHE A  40      70.742  82.676  40.013  1.00 16.18           H  
ATOM    696  HB2 PHE A  40      70.547  81.831  42.721  1.00 17.23           H  
ATOM    697  HB3 PHE A  40      71.746  81.451  41.749  1.00 17.23           H  
ATOM    698  HD1 PHE A  40      70.383  84.223  43.506  1.00 19.36           H  
ATOM    699  HD2 PHE A  40      73.641  82.840  41.633  1.00 20.16           H  
ATOM    700  HE1 PHE A  40      71.607  86.035  44.279  1.00 20.01           H  
ATOM    701  HE2 PHE A  40      74.849  84.661  42.375  1.00 20.90           H  
ATOM    702  HZ  PHE A  40      73.837  86.249  43.710  1.00 20.89           H  
ATOM    703  N   THR A  41      69.754  80.482  39.354  1.00 12.33           N  
ANISOU  703  N   THR A  41     1442   1737   1507     59     50    -30       N  
ATOM    704  CA  THR A  41      69.073  79.256  38.954  1.00 13.11           C  
ANISOU  704  CA  THR A  41     1659   1594   1727    133     93   -163       C  
ATOM    705  C   THR A  41      70.097  78.148  38.775  1.00 12.69           C  
ANISOU  705  C   THR A  41     1519   1634   1669    108     84   -261       C  
ATOM    706  O   THR A  41      71.170  78.364  38.189  1.00 13.12           O  
ANISOU  706  O   THR A  41     1544   1690   1751    176     95   -208       O  
ATOM    707  CB  THR A  41      68.211  79.500  37.720  1.00 13.55           C  
ANISOU  707  CB  THR A  41     1795   1586   1765    115    123   -105       C  
ATOM    708  OG1 THR A  41      67.255  80.510  38.052  1.00 14.03           O  
ANISOU  708  OG1 THR A  41     1781   1641   1909    -66     -3   -252       O  
ATOM    709  CG2 THR A  41      67.454  78.260  37.286  1.00 12.65           C  
ANISOU  709  CG2 THR A  41     1538   1784   1485    329   -121     55       C  
ATOM    710  H   THR A  41      70.357  80.744  38.800  1.00 14.81           H  
ATOM    711  HA  THR A  41      68.471  78.947  39.649  1.00 15.74           H  
ATOM    712  HB  THR A  41      68.782  79.762  36.981  1.00 16.26           H  
ATOM    713  HG1 THR A  41      67.641  81.164  38.411  1.00 16.84           H  
ATOM    714 HG21 THR A  41      66.896  78.463  36.519  1.00 15.19           H  
ATOM    715 HG22 THR A  41      68.078  77.558  37.044  1.00 15.19           H  
ATOM    716 HG23 THR A  41      66.891  77.944  38.010  1.00 15.19           H  
ATOM    717  N   TYR A  42      69.770  76.983  39.325  1.00 12.82           N  
ANISOU  717  N   TYR A  42     1644   1454   1772    -38   -139    -61       N  
ATOM    718  CA  TYR A  42      70.678  75.865  39.499  1.00 13.24           C  
ANISOU  718  CA  TYR A  42     1507   1671   1851    -10    -51      2       C  
ATOM    719  C   TYR A  42      70.141  74.599  38.838  1.00 13.37           C  
ANISOU  719  C   TYR A  42     1462   1730   1889     17   -233     91       C  
ATOM    720  O   TYR A  42      68.927  74.409  38.699  1.00 12.48           O  
ANISOU  720  O   TYR A  42     1489   1453   1800    -36   -160     91       O  
ATOM    721  CB  TYR A  42      70.835  75.550  41.005  1.00 13.81           C  
ANISOU  721  CB  TYR A  42     1588   1833   1828    -78    -75     -2       C  
ATOM    722  CG  TYR A  42      71.398  76.668  41.853  1.00 13.19           C  
ANISOU  722  CG  TYR A  42     1467   1779   1766    127     83    -53       C  
ATOM    723  CD1 TYR A  42      70.595  77.713  42.277  1.00 12.83           C  
ANISOU  723  CD1 TYR A  42     1492   1664   1718    140    -27    -52       C  
ATOM    724  CD2 TYR A  42      72.732  76.667  42.245  1.00 14.34           C  
ANISOU  724  CD2 TYR A  42     1490   2092   1868    120    166     24       C  
ATOM    725  CE1 TYR A  42      71.101  78.738  43.047  1.00 13.89           C  
ANISOU  725  CE1 TYR A  42     1562   1989   1728     56    -89   -158       C  
ATOM    726  CE2 TYR A  42      73.239  77.680  43.008  1.00 14.98           C  
ANISOU  726  CE2 TYR A  42     1572   2168   1950      8     21    -82       C  
ATOM    727  CZ  TYR A  42      72.424  78.719  43.414  1.00 15.98           C  
ANISOU  727  CZ  TYR A  42     1738   2344   1992   -205   -115   -316       C  
ATOM    728  OH  TYR A  42      72.934  79.752  44.191  1.00 19.19           O  
ANISOU  728  OH  TYR A  42     2139   2789   2363   -315   -238   -616       O  
ATOM    729  H   TYR A  42      68.981  76.812  39.621  1.00 15.39           H  
ATOM    730  HA  TYR A  42      71.527  76.093  39.088  1.00 15.89           H  
ATOM    731  HB2 TYR A  42      69.960  75.330  41.363  1.00 16.59           H  
ATOM    732  HB3 TYR A  42      71.432  74.791  41.097  1.00 16.59           H  
ATOM    733  HD1 TYR A  42      69.696  77.723  42.038  1.00 15.40           H  
ATOM    734  HD2 TYR A  42      73.286  75.967  41.984  1.00 17.22           H  
ATOM    735  HE1 TYR A  42      70.551  79.439  43.315  1.00 16.68           H  
ATOM    736  HE2 TYR A  42      74.136  77.671  43.254  1.00 17.98           H  
ATOM    737  HH  TYR A  42      73.749  79.618  44.348  1.00 23.04           H  
ATOM    738  N   ASP A  43      71.062  73.719  38.450  1.00 13.55           N  
ANISOU  738  N   ASP A  43     1514   1780   1854    -64   -221    -29       N  
ATOM    739  CA  ASP A  43      70.730  72.406  37.915  1.00 13.75           C  
ANISOU  739  CA  ASP A  43     1591   1707   1924     18   -243    -81       C  
ATOM    740  C   ASP A  43      70.907  71.367  39.009  1.00 14.12           C  
ANISOU  740  C   ASP A  43     1544   1778   2044    -28   -140   -114       C  
ATOM    741  O   ASP A  43      72.027  71.183  39.513  1.00 14.48           O  
ANISOU  741  O   ASP A  43     1631   1938   1932   -118   -107   -136       O  
ATOM    742  CB  ASP A  43      71.673  72.047  36.772  1.00 14.79           C  
ANISOU  742  CB  ASP A  43     2192   1527   1902    157   -132    -35       C  
ATOM    743  CG  ASP A  43      71.191  70.865  35.977  1.00 16.89           C  
ANISOU  743  CG  ASP A  43     2752   1702   1962    254   -105    -58       C  
ATOM    744  OD1 ASP A  43      70.175  70.252  36.363  1.00 16.81           O  
ANISOU  744  OD1 ASP A  43     2749   1824   1816    190   -413    -52       O  
ATOM    745  OD2 ASP A  43      71.836  70.562  34.966  1.00 19.21           O  
ANISOU  745  OD2 ASP A  43     3436   1714   2147    532     46    -89       O  
ATOM    746  H   ASP A  43      71.908  73.867  38.490  1.00 16.27           H  
ATOM    747  HA  ASP A  43      69.810  72.414  37.606  1.00 16.50           H  
ATOM    748  HB2 ASP A  43      71.746  72.805  36.171  1.00 17.76           H  
ATOM    749  HB3 ASP A  43      72.545  71.828  37.137  1.00 17.76           H  
ATOM    750  N   ALA A  44      69.812  70.702  39.383  1.00 13.37           N  
ANISOU  750  N   ALA A  44     1374   1770   1935    289   -239     24       N  
ATOM    751  CA  ALA A  44      69.893  69.579  40.307  1.00 12.76           C  
ANISOU  751  CA  ALA A  44     1286   1730   1833    374   -163     82       C  
ATOM    752  C   ALA A  44      70.240  68.264  39.617  1.00 13.13           C  
ANISOU  752  C   ALA A  44     1460   1766   1763    488   -136     82       C  
ATOM    753  O   ALA A  44      70.476  67.273  40.315  1.00 14.54           O  
ANISOU  753  O   ALA A  44     1651   1847   2028    428      3    185       O  
ATOM    754  CB  ALA A  44      68.584  69.441  41.089  1.00 13.95           C  
ANISOU  754  CB  ALA A  44     1356   2052   1891    344     41    -14       C  
ATOM    755  H   ALA A  44      69.016  70.883  39.115  1.00 16.05           H  
ATOM    756  HA  ALA A  44      70.595  69.757  40.953  1.00 15.32           H  
ATOM    757  HB1 ALA A  44      68.657  68.689  41.698  1.00 16.74           H  
ATOM    758  HB2 ALA A  44      68.426  70.257  41.588  1.00 16.74           H  
ATOM    759  HB3 ALA A  44      67.857  69.290  40.464  1.00 16.74           H  
ATOM    760  N   LYS A  45      70.278  68.230  38.279  1.00 13.58           N  
ANISOU  760  N   LYS A  45     1585   1655   1921    292     10    179       N  
ATOM    761  CA  LYS A  45      70.856  67.107  37.529  1.00 13.86           C  
ANISOU  761  CA  LYS A  45     1459   1544   2262     66    127     43       C  
ATOM    762  C   LYS A  45      70.188  65.775  37.840  1.00 14.21           C  
ANISOU  762  C   LYS A  45     1426   1648   2325     80    120     68       C  
ATOM    763  O   LYS A  45      70.848  64.725  37.883  1.00 14.84           O  
ANISOU  763  O   LYS A  45     1511   1812   2314     50    176     28       O  
ATOM    764  CB  LYS A  45      72.373  67.026  37.729  1.00 14.47           C  
ANISOU  764  CB  LYS A  45     1416   1617   2466    -59    330   -110       C  
ATOM    765  CG  LYS A  45      73.062  68.350  37.435  1.00 15.77           C  
ANISOU  765  CG  LYS A  45     1280   1815   2896   -134    596    -99       C  
ATOM    766  CD  LYS A  45      74.593  68.273  37.511  1.00 17.56           C  
ANISOU  766  CD  LYS A  45     1462   1858   3350   -189    736   -492       C  
ATOM    767  CE  LYS A  45      75.166  69.627  37.104  1.00 19.78           C  
ANISOU  767  CE  LYS A  45     1632   2049   3833   -134    862   -487       C  
ATOM    768  NZ  LYS A  45      76.628  69.706  37.301  1.00 21.39           N  
ANISOU  768  NZ  LYS A  45     1759   2277   4091   -294    939   -552       N  
ATOM    769  H   LYS A  45      69.969  68.855  37.775  1.00 16.31           H  
ATOM    770  HA  LYS A  45      70.684  67.276  36.590  1.00 16.64           H  
ATOM    771  HB2 LYS A  45      72.560  66.784  38.650  1.00 17.37           H  
ATOM    772  HB3 LYS A  45      72.737  66.355  37.130  1.00 17.37           H  
ATOM    773  HG2 LYS A  45      72.824  68.636  36.539  1.00 18.93           H  
ATOM    774  HG3 LYS A  45      72.766  69.009  38.083  1.00 18.93           H  
ATOM    775  HD2 LYS A  45      74.871  68.070  38.417  1.00 21.07           H  
ATOM    776  HD3 LYS A  45      74.922  67.593  36.902  1.00 21.07           H  
ATOM    777  HE2 LYS A  45      74.981  69.781  36.164  1.00 23.74           H  
ATOM    778  HE3 LYS A  45      74.753  70.321  37.641  1.00 23.74           H  
ATOM    779  HZ1 LYS A  45      76.930  70.498  37.029  1.00 25.68           H  
ATOM    780  HZ2 LYS A  45      76.825  69.603  38.163  1.00 25.68           H  
ATOM    781  HZ3 LYS A  45      77.033  69.067  36.834  1.00 25.68           H  
ATOM    782  N   TYR A  46      68.871  65.811  38.046  1.00 14.78           N  
ANISOU  782  N   TYR A  46     1571   1677   2367     43    203    208       N  
ATOM    783  CA  TYR A  46      68.036  64.646  38.305  1.00 15.89           C  
ANISOU  783  CA  TYR A  46     1780   1876   2381     22    191    167       C  
ATOM    784  C   TYR A  46      68.278  64.023  39.671  1.00 16.32           C  
ANISOU  784  C   TYR A  46     1837   1957   2407    312    190    325       C  
ATOM    785  O   TYR A  46      67.821  62.896  39.923  1.00 16.95           O  
ANISOU  785  O   TYR A  46     1933   1993   2515    171    184    429       O  
ATOM    786  CB  TYR A  46      68.160  63.585  37.208  1.00 15.60           C  
ANISOU  786  CB  TYR A  46     1673   1832   2423    -10    270     28       C  
ATOM    787  CG  TYR A  46      67.820  64.074  35.818  1.00 16.30           C  
ANISOU  787  CG  TYR A  46     1761   2065   2368    279     14    184       C  
ATOM    788  CD1 TYR A  46      66.625  64.719  35.554  1.00 17.67           C  
ANISOU  788  CD1 TYR A  46     1947   2344   2422    181    -40    264       C  
ATOM    789  CD2 TYR A  46      68.703  63.905  34.762  1.00 18.50           C  
ANISOU  789  CD2 TYR A  46     1917   2590   2522    307    -72    289       C  
ATOM    790  CE1 TYR A  46      66.313  65.156  34.287  1.00 18.75           C  
ANISOU  790  CE1 TYR A  46     2169   2466   2491    166   -139    102       C  
ATOM    791  CE2 TYR A  46      68.394  64.337  33.490  1.00 18.89           C  
ANISOU  791  CE2 TYR A  46     2058   2674   2447    318     82    222       C  
ATOM    792  CZ  TYR A  46      67.194  64.966  33.261  1.00 19.26           C  
ANISOU  792  CZ  TYR A  46     2336   2516   2466      2   -239    282       C  
ATOM    793  OH  TYR A  46      66.869  65.397  31.994  1.00 20.80           O  
ANISOU  793  OH  TYR A  46     2742   2512   2650   -240   -298    256       O  
ATOM    794  H   TYR A  46      68.423  66.545  38.040  1.00 17.74           H  
ATOM    795  HA  TYR A  46      67.114  64.948  38.302  1.00 19.07           H  
ATOM    796  HB2 TYR A  46      69.076  63.266  37.190  1.00 18.73           H  
ATOM    797  HB3 TYR A  46      67.558  62.854  37.416  1.00 18.73           H  
ATOM    798  HD1 TYR A  46      66.020  64.860  36.247  1.00 21.21           H  
ATOM    799  HD2 TYR A  46      69.521  63.490  34.916  1.00 22.20           H  
ATOM    800  HE1 TYR A  46      65.501  65.582  34.129  1.00 22.51           H  
ATOM    801  HE2 TYR A  46      68.994  64.205  32.792  1.00 22.68           H  
ATOM    802  HH  TYR A  46      67.497  65.227  31.463  1.00 24.97           H  
ATOM    803  N   ARG A  47      68.995  64.710  40.543  1.00 16.28           N  
ANISOU  803  N   ARG A  47     2088   1973   2125    335    164    326       N  
ATOM    804  CA AARG A  47      69.230  64.281  41.911  0.66 17.63           C  
ANISOU  804  CA AARG A  47     2355   2275   2068    558     46    513       C  
ATOM    805  CA BARG A  47      69.235  64.284  41.912  0.34 17.54           C  
ANISOU  805  CA BARG A  47     2216   2295   2152    354     48    382       C  
ATOM    806  C   ARG A  47      68.373  65.127  42.849  1.00 17.40           C  
ANISOU  806  C   ARG A  47     2281   2200   2131    316     36    422       C  
ATOM    807  O   ARG A  47      67.636  66.003  42.421  1.00 15.97           O  
ANISOU  807  O   ARG A  47     1922   1904   2240    214   -135    190       O  
ATOM    808  CB AARG A  47      70.718  64.364  42.243  0.66 21.75           C  
ANISOU  808  CB AARG A  47     2858   3178   2229    864    220    616       C  
ATOM    809  CB BARG A  47      70.725  64.390  42.240  0.34 20.20           C  
ANISOU  809  CB BARG A  47     2360   2982   2332    371     96    331       C  
ATOM    810  CG AARG A  47      71.555  63.431  41.361  0.66 27.07           C  
ANISOU  810  CG AARG A  47     3443   4167   2677   1205    282    598       C  
ATOM    811  CG BARG A  47      71.590  63.494  41.350  0.34 23.49           C  
ANISOU  811  CG BARG A  47     2542   3715   2668    397    115    246       C  
ATOM    812  CD AARG A  47      73.042  63.465  41.699  0.66 32.63           C  
ANISOU  812  CD AARG A  47     4280   4929   3188   1275    321    592       C  
ATOM    813  CD BARG A  47      73.089  63.659  41.607  0.34 26.94           C  
ANISOU  813  CD BARG A  47     2914   4308   3015    268    134    188       C  
ATOM    814  NE AARG A  47      73.332  62.912  43.017  0.66 36.01           N  
ANISOU  814  NE AARG A  47     4917   5193   3570   1561    381    484       N  
ATOM    815  NE BARG A  47      73.471  63.308  42.972  0.34 28.95           N  
ANISOU  815  NE BARG A  47     3170   4578   3250    247    180     46       N  
ATOM    816  CZ AARG A  47      73.599  61.633  43.264  0.66 38.28           C  
ANISOU  816  CZ AARG A  47     5400   5407   3736   1554    438    363       C  
ATOM    817  CZ BARG A  47      73.882  64.177  43.896  0.34 29.74           C  
ANISOU  817  CZ BARG A  47     3256   4673   3372    174    214   -167       C  
ATOM    818  NH1AARG A  47      73.615  60.736  42.280  0.66 38.94           N  
ANISOU  818  NH1AARG A  47     5586   5423   3786   1698    526    264       N  
ATOM    819  NH1BARG A  47      73.978  65.470  43.618  0.34 30.90           N  
ANISOU  819  NH1BARG A  47     3413   4797   3532    119    295   -362       N  
ATOM    820  NH2AARG A  47      73.852  61.250  44.502  0.66 38.96           N  
ANISOU  820  NH2AARG A  47     5464   5572   3769   1500    388    381       N  
ATOM    821  NH2BARG A  47      74.197  63.746  45.107  0.34 29.67           N  
ANISOU  821  NH2BARG A  47     3209   4728   3338    267    139   -122       N  
ATOM    822  H  AARG A  47      69.370  65.461  40.356  0.66 19.54           H  
ATOM    823  H  BARG A  47      69.369  65.461  40.355  0.34 19.54           H  
ATOM    824  HA AARG A  47      68.966  63.355  42.023  0.66 21.16           H  
ATOM    825  HA BARG A  47      68.979  63.355  42.026  0.34 21.05           H  
ATOM    826  HB2AARG A  47      71.026  65.273  42.101  0.66 26.11           H  
ATOM    827  HB2BARG A  47      71.012  65.307  42.114  0.34 24.25           H  
ATOM    828  HB3AARG A  47      70.853  64.109  43.169  0.66 26.11           H  
ATOM    829  HB3BARG A  47      70.865  64.122  43.162  0.34 24.25           H  
ATOM    830  HG2AARG A  47      71.242  62.520  41.481  0.66 32.50           H  
ATOM    831  HG2BARG A  47      71.359  62.567  41.517  0.34 28.19           H  
ATOM    832  HG3AARG A  47      71.453  63.697  40.434  0.66 32.50           H  
ATOM    833  HG3BARG A  47      71.420  63.716  40.421  0.34 28.19           H  
ATOM    834  HD2AARG A  47      73.528  62.944  41.042  0.66 39.16           H  
ATOM    835  HD2BARG A  47      73.579  63.082  41.001  0.34 32.34           H  
ATOM    836  HD3AARG A  47      73.348  64.386  41.686  0.66 39.16           H  
ATOM    837  HD3BARG A  47      73.336  64.585  41.455  0.34 32.34           H  
ATOM    838  HE AARG A  47      73.331  63.454  43.685  0.66 43.21           H  
ATOM    839  HE BARG A  47      73.427  62.479  43.197  0.34 34.74           H  
ATOM    840 HH11AARG A  47      73.452  60.981  41.472  0.66 46.74           H  
ATOM    841 HH11BARG A  47      73.774  65.758  42.833  0.34 37.09           H  
ATOM    842 HH12AARG A  47      73.789  59.912  42.453  0.66 46.74           H  
ATOM    843 HH12BARG A  47      74.245  66.021  44.222  0.34 37.09           H  
ATOM    844 HH21AARG A  47      73.844  61.827  45.141  0.66 46.77           H  
ATOM    845 HH21BARG A  47      74.136  62.909  45.295  0.34 35.62           H  
ATOM    846 HH22AARG A  47      74.026  60.425  44.671  0.66 46.77           H  
ATOM    847 HH22BARG A  47      74.463  64.302  45.706  0.34 35.62           H  
ATOM    848  N   THR A  48      68.478  64.850  44.142  1.00 19.81           N  
ANISOU  848  N   THR A  48     2711   2560   2257    475    206    448       N  
ATOM    849  CA  THR A  48      67.731  65.608  45.138  1.00 21.11           C  
ANISOU  849  CA  THR A  48     2920   2811   2288    642    168    383       C  
ATOM    850  C   THR A  48      68.630  66.455  46.025  1.00 20.79           C  
ANISOU  850  C   THR A  48     2832   2814   2254    686    -28    372       C  
ATOM    851  O   THR A  48      68.140  67.068  46.978  1.00 21.66           O  
ANISOU  851  O   THR A  48     2964   3023   2242    568    -65    128       O  
ATOM    852  CB  THR A  48      66.853  64.683  45.980  1.00 23.18           C  
ANISOU  852  CB  THR A  48     3124   3245   2437    513    295    449       C  
ATOM    853  OG1 THR A  48      67.659  63.678  46.596  1.00 24.14           O  
ANISOU  853  OG1 THR A  48     3367   3257   2548    372    350    806       O  
ATOM    854  CG2 THR A  48      65.793  64.025  45.103  1.00 24.91           C  
ANISOU  854  CG2 THR A  48     3322   3388   2752    320    153    289       C  
ATOM    855  H   THR A  48      68.975  64.228  44.466  1.00 23.78           H  
ATOM    856  HA  THR A  48      67.134  66.213  44.670  1.00 25.34           H  
ATOM    857  HB  THR A  48      66.406  65.195  46.672  1.00 27.82           H  
ATOM    858  HG1 THR A  48      68.223  64.035  47.106  1.00 28.98           H  
ATOM    859 HG21 THR A  48      65.217  63.462  45.643  1.00 29.90           H  
ATOM    860 HG22 THR A  48      65.253  64.704  44.669  1.00 29.90           H  
ATOM    861 HG23 THR A  48      66.218  63.479  44.422  1.00 29.90           H  
ATOM    862  N   THR A  49      69.921  66.530  45.715  1.00 20.81           N  
ANISOU  862  N   THR A  49     2766   2708   2432    641   -211    425       N  
ATOM    863  CA  THR A  49      70.819  67.426  46.422  1.00 21.55           C  
ANISOU  863  CA  THR A  49     2739   2887   2562    741   -310    260       C  
ATOM    864  C   THR A  49      70.550  68.863  46.011  1.00 19.77           C  
ANISOU  864  C   THR A  49     2636   2725   2150    759   -137    192       C  
ATOM    865  O   THR A  49      70.472  69.174  44.817  1.00 21.24           O  
ANISOU  865  O   THR A  49     2904   2965   2199    853   -180    192       O  
ATOM    866  CB  THR A  49      72.268  67.077  46.088  1.00 24.40           C  
ANISOU  866  CB  THR A  49     2822   3099   3349    776   -391    384       C  
ATOM    867  OG1 THR A  49      72.539  65.753  46.548  1.00 26.97           O  
ANISOU  867  OG1 THR A  49     3204   3242   3800    729   -176    470       O  
ATOM    868  CG2 THR A  49      73.214  68.059  46.767  1.00 25.93           C  
ANISOU  868  CG2 THR A  49     2888   3426   3539    737   -301    323       C  
ATOM    869  H   THR A  49      70.302  66.070  45.096  1.00 24.98           H  
ATOM    870  HA  THR A  49      70.679  67.334  47.377  1.00 25.87           H  
ATOM    871  HB  THR A  49      72.416  67.127  45.131  1.00 29.29           H  
ATOM    872  HG1 THR A  49      73.362  65.592  46.491  1.00 32.37           H  
ATOM    873 HG21 THR A  49      74.117  67.705  46.766  1.00 31.12           H  
ATOM    874 HG22 THR A  49      73.208  68.906  46.295  1.00 31.12           H  
ATOM    875 HG23 THR A  49      72.936  68.208  47.685  1.00 31.12           H  
ATOM    876  N   LEU A  50      70.437  69.747  46.992  1.00 18.42           N  
ANISOU  876  N   LEU A  50     2167   2706   2124    714     94    331       N  
ATOM    877  CA  LEU A  50      70.094  71.124  46.681  1.00 16.60           C  
ANISOU  877  CA  LEU A  50     1887   2567   1854    492     49    380       C  
ATOM    878  C   LEU A  50      71.184  72.059  47.188  1.00 17.45           C  
ANISOU  878  C   LEU A  50     1840   2886   1905    398   -298    346       C  
ATOM    879  O   LEU A  50      71.802  71.793  48.225  1.00 19.27           O  
ANISOU  879  O   LEU A  50     2029   3257   2034    481   -483    412       O  
ATOM    880  CB  LEU A  50      68.772  71.501  47.356  1.00 15.62           C  
ANISOU  880  CB  LEU A  50     1813   2313   1808    436    108    286       C  
ATOM    881  CG  LEU A  50      67.542  70.803  46.794  1.00 16.86           C  
ANISOU  881  CG  LEU A  50     1900   2340   2168    331     81    251       C  
ATOM    882  CD1 LEU A  50      66.328  71.089  47.674  1.00 18.43           C  
ANISOU  882  CD1 LEU A  50     2100   2588   2314    350      8    637       C  
ATOM    883  CD2 LEU A  50      67.267  71.234  45.381  1.00 17.15           C  
ANISOU  883  CD2 LEU A  50     1819   2358   2341    358   -122     55       C  
ATOM    884  H   LEU A  50      70.551  69.574  47.827  1.00 22.11           H  
ATOM    885  HA  LEU A  50      70.007  71.239  45.722  1.00 19.93           H  
ATOM    886  HB2 LEU A  50      68.833  71.273  48.296  1.00 18.75           H  
ATOM    887  HB3 LEU A  50      68.638  72.456  47.254  1.00 18.75           H  
ATOM    888  HG  LEU A  50      67.707  69.848  46.784  1.00 20.25           H  
ATOM    889 HD11 LEU A  50      65.557  70.631  47.307  1.00 22.12           H  
ATOM    890 HD12 LEU A  50      66.507  70.768  48.572  1.00 22.12           H  
ATOM    891 HD13 LEU A  50      66.168  72.046  47.691  1.00 22.12           H  
ATOM    892 HD21 LEU A  50      66.409  70.876  45.104  1.00 20.59           H  
ATOM    893 HD22 LEU A  50      67.249  72.203  45.344  1.00 20.59           H  
ATOM    894 HD23 LEU A  50      67.969  70.893  44.805  1.00 20.59           H  
ATOM    895  N   PRO A  51      71.434  73.185  46.489  1.00 17.26           N  
ANISOU  895  N   PRO A  51     1821   2855   1882    288   -219    284       N  
ATOM    896  CA  PRO A  51      70.730  73.601  45.271  1.00 16.10           C  
ANISOU  896  CA  PRO A  51     1701   2646   1768    224    -68    437       C  
ATOM    897  C   PRO A  51      71.207  72.931  43.996  1.00 15.42           C  
ANISOU  897  C   PRO A  51     1556   2377   1926    327    -14    376       C  
ATOM    898  O   PRO A  51      70.521  73.014  42.990  1.00 15.53           O  
ANISOU  898  O   PRO A  51     1556   2500   1847    251      5    350       O  
ATOM    899  CB  PRO A  51      71.031  75.103  45.195  1.00 17.96           C  
ANISOU  899  CB  PRO A  51     1864   3025   1934    129   -259    284       C  
ATOM    900  CG  PRO A  51      72.388  75.228  45.848  1.00 18.00           C  
ANISOU  900  CG  PRO A  51     1875   3011   1952    244   -354    249       C  
ATOM    901  CD  PRO A  51      72.372  74.214  46.958  1.00 19.13           C  
ANISOU  901  CD  PRO A  51     2070   3073   2126    207   -375    301       C  
ATOM    902  HA  PRO A  51      69.782  73.429  45.381  1.00 19.32           H  
ATOM    903  HB2 PRO A  51      71.058  75.393  44.269  1.00 21.56           H  
ATOM    904  HB3 PRO A  51      70.358  75.605  45.681  1.00 21.56           H  
ATOM    905  HG2 PRO A  51      73.086  75.028  45.205  1.00 21.60           H  
ATOM    906  HG3 PRO A  51      72.506  76.124  46.199  1.00 21.60           H  
ATOM    907  HD2 PRO A  51      73.256  73.836  47.089  1.00 22.96           H  
ATOM    908  HD3 PRO A  51      72.056  74.614  47.783  1.00 22.96           H  
ATOM    909  N   GLY A  52      72.365  72.286  44.036  1.00 15.87           N  
ANISOU  909  N   GLY A  52     1681   2290   2058    288    103    367       N  
ATOM    910  CA  GLY A  52      72.974  71.807  42.816  1.00 15.00           C  
ANISOU  910  CA  GLY A  52     1633   2044   2023    272     12    164       C  
ATOM    911  C   GLY A  52      74.009  72.776  42.289  1.00 15.29           C  
ANISOU  911  C   GLY A  52     1680   2194   1936   -156     74    -79       C  
ATOM    912  O   GLY A  52      74.573  73.570  43.049  1.00 17.88           O  
ANISOU  912  O   GLY A  52     2054   2607   2130   -291    224   -188       O  
ATOM    913  H   GLY A  52      72.810  72.117  44.752  1.00 19.05           H  
ATOM    914  HA2 GLY A  52      73.406  70.954  42.983  1.00 18.01           H  
ATOM    915  HA3 GLY A  52      72.290  71.687  42.138  1.00 18.01           H  
ATOM    916  N   SER A  53      74.258  72.751  40.993  1.00 14.72           N  
ANISOU  916  N   SER A  53     1632   1961   2002     48     56     23       N  
ATOM    917  CA ASER A  53      75.279  73.585  40.377  0.78 13.90           C  
ANISOU  917  CA ASER A  53     1588   1813   1881    235    130    162       C  
ATOM    918  CA BSER A  53      75.283  73.599  40.404  0.22 14.37           C  
ANISOU  918  CA BSER A  53     1688   1858   1915     80    -22    114       C  
ATOM    919  C   SER A  53      74.643  74.836  39.787  1.00 13.80           C  
ANISOU  919  C   SER A  53     1670   1753   1820    160   -108     33       C  
ATOM    920  O   SER A  53      73.625  74.749  39.106  1.00 14.63           O  
ANISOU  920  O   SER A  53     1641   1874   2044   -150   -440    105       O  
ATOM    921  CB ASER A  53      75.967  72.828  39.243  0.78 15.29           C  
ANISOU  921  CB ASER A  53     1989   1858   1961    495    151    202       C  
ATOM    922  CB BSER A  53      76.065  72.832  39.339  0.22 15.12           C  
ANISOU  922  CB BSER A  53     1919   1871   1955     14    -92    220       C  
ATOM    923  OG ASER A  53      76.497  71.602  39.687  0.78 17.18           O  
ANISOU  923  OG ASER A  53     2403   1874   2250    586    326    258       O  
ATOM    924  OG BSER A  53      75.225  72.460  38.267  0.22 15.86           O  
ANISOU  924  OG BSER A  53     2110   1860   2056   -118   -152    318       O  
ATOM    925  H  ASER A  53      73.840  72.248  40.435  0.78 17.68           H  
ATOM    926  H  BSER A  53      73.845  72.249  40.430  0.22 17.68           H  
ATOM    927  HA ASER A  53      75.925  73.840  41.054  0.78 16.69           H  
ATOM    928  HA BSER A  53      75.903  73.889  41.092  0.22 17.26           H  
ATOM    929  HB2ASER A  53      75.317  72.654  38.544  0.78 18.35           H  
ATOM    930  HB2BSER A  53      76.776  73.399  39.000  0.22 18.15           H  
ATOM    931  HB3ASER A  53      76.689  73.374  38.896  0.78 18.35           H  
ATOM    932  HB3BSER A  53      76.441  72.032  39.738  0.22 18.15           H  
ATOM    933  HG ASER A  53      75.876  71.097  39.943  0.78 20.62           H  
ATOM    934  HG BSER A  53      75.687  72.182  37.623  0.22 19.04           H  
ATOM    935  N   LEU A  54      75.257  75.995  40.023  1.00 13.68           N  
ANISOU  935  N   LEU A  54     1676   1794   1727    211    -57     46       N  
ATOM    936  CA  LEU A  54      74.759  77.201  39.371  1.00 12.81           C  
ANISOU  936  CA  LEU A  54     1513   1669   1687    173    -11    -32       C  
ATOM    937  C   LEU A  54      74.797  76.946  37.874  1.00 12.36           C  
ANISOU  937  C   LEU A  54     1387   1601   1708     70    -93    -50       C  
ATOM    938  O   LEU A  54      75.803  76.466  37.352  1.00 14.13           O  
ANISOU  938  O   LEU A  54     1587   1864   1916    113    105    -37       O  
ATOM    939  CB  LEU A  54      75.630  78.396  39.742  1.00 13.70           C  
ANISOU  939  CB  LEU A  54     1575   1699   1930     60    112    -60       C  
ATOM    940  CG  LEU A  54      75.103  79.751  39.258  1.00 14.74           C  
ANISOU  940  CG  LEU A  54     1821   1600   2181    -58     45   -147       C  
ATOM    941  CD1 LEU A  54      73.780  80.123  39.909  1.00 14.99           C  
ANISOU  941  CD1 LEU A  54     1905   1548   2242     14    135   -339       C  
ATOM    942  CD2 LEU A  54      76.167  80.795  39.530  1.00 15.14           C  
ANISOU  942  CD2 LEU A  54     1937   1577   2237   -138    -48   -191       C  
ATOM    943  H   LEU A  54      75.937  76.106  40.538  1.00 16.42           H  
ATOM    944  HA  LEU A  54      73.856  77.414  39.653  1.00 15.38           H  
ATOM    945  HB2 LEU A  54      75.698  78.437  40.708  1.00 16.45           H  
ATOM    946  HB3 LEU A  54      76.509  78.268  39.352  1.00 16.45           H  
ATOM    947  HG  LEU A  54      74.919  79.710  38.306  1.00 17.70           H  
ATOM    948 HD11 LEU A  54      73.542  81.026  39.646  1.00 17.99           H  
ATOM    949 HD12 LEU A  54      73.097  79.501  39.614  1.00 17.99           H  
ATOM    950 HD13 LEU A  54      73.878  80.074  40.873  1.00 17.99           H  
ATOM    951 HD21 LEU A  54      75.846  81.659  39.228  1.00 18.17           H  
ATOM    952 HD22 LEU A  54      76.345  80.823  40.483  1.00 18.17           H  
ATOM    953 HD23 LEU A  54      76.974  80.555  39.049  1.00 18.17           H  
ATOM    954  N   TRP A  55      73.684  77.233  37.188  1.00 13.53           N  
ANISOU  954  N   TRP A  55     1536   1800   1807    316   -111     13       N  
ATOM    955  CA  TRP A  55      73.510  76.760  35.818  1.00 13.65           C  
ANISOU  955  CA  TRP A  55     1482   1843   1860     17     45     17       C  
ATOM    956  C   TRP A  55      74.532  77.418  34.890  1.00 13.75           C  
ANISOU  956  C   TRP A  55     1452   1793   1980    186    325   -128       C  
ATOM    957  O   TRP A  55      74.532  78.647  34.747  1.00 15.12           O  
ANISOU  957  O   TRP A  55     1669   1776   2301    229    117    -68       O  
ATOM    958  CB  TRP A  55      72.104  77.093  35.328  1.00 13.50           C  
ANISOU  958  CB  TRP A  55     1521   1807   1800     64    -11    -39       C  
ATOM    959  CG  TRP A  55      71.812  76.438  34.031  1.00 13.60           C  
ANISOU  959  CG  TRP A  55     1673   1812   1684     51    -97    -32       C  
ATOM    960  CD1 TRP A  55      72.293  76.786  32.804  1.00 14.42           C  
ANISOU  960  CD1 TRP A  55     1699   2023   1757    183     19   -123       C  
ATOM    961  CD2 TRP A  55      70.971  75.303  33.831  1.00 12.81           C  
ANISOU  961  CD2 TRP A  55     1735   1532   1598    181    -92    -30       C  
ATOM    962  NE1 TRP A  55      71.812  75.925  31.845  1.00 14.32           N  
ANISOU  962  NE1 TRP A  55     1894   2058   1490    156    134    -74       N  
ATOM    963  CE2 TRP A  55      71.001  74.996  32.450  1.00 14.04           C  
ANISOU  963  CE2 TRP A  55     1815   1828   1693     88     81     48       C  
ATOM    964  CE3 TRP A  55      70.220  74.494  34.692  1.00 14.59           C  
ANISOU  964  CE3 TRP A  55     2074   1720   1751    374   -204     86       C  
ATOM    965  CZ2 TRP A  55      70.279  73.939  31.909  1.00 14.46           C  
ANISOU  965  CZ2 TRP A  55     1828   1989   1677     56     32     -6       C  
ATOM    966  CZ3 TRP A  55      69.510  73.430  34.147  1.00 14.59           C  
ANISOU  966  CZ3 TRP A  55     1855   1827   1860    139    -68     35       C  
ATOM    967  CH2 TRP A  55      69.548  73.168  32.773  1.00 15.02           C  
ANISOU  967  CH2 TRP A  55     1882   1996   1828     46   -151    -32       C  
ATOM    968  H   TRP A  55      73.025  77.694  37.493  1.00 16.25           H  
ATOM    969  HA  TRP A  55      73.643  75.799  35.802  1.00 16.38           H  
ATOM    970  HB2 TRP A  55      71.456  76.784  35.980  1.00 16.20           H  
ATOM    971  HB3 TRP A  55      72.024  78.053  35.211  1.00 16.20           H  
ATOM    972  HD1 TRP A  55      72.864  77.502  32.639  1.00 17.31           H  
ATOM    973  HE1 TRP A  55      71.989  75.963  31.004  1.00 17.20           H  
ATOM    974  HE3 TRP A  55      70.196  74.665  35.606  1.00 17.52           H  
ATOM    975  HZ2 TRP A  55      70.292  73.763  30.996  1.00 17.36           H  
ATOM    976  HZ3 TRP A  55      69.002  72.885  34.704  1.00 17.51           H  
ATOM    977  HH2 TRP A  55      69.063  72.449  32.437  1.00 18.03           H  
ATOM    978  N   ALA A  56      75.348  76.608  34.229  1.00 14.57           N  
ANISOU  978  N   ALA A  56     1610   1918   2008    264    440   -239       N  
ATOM    979  CA  ALA A  56      76.387  77.097  33.340  1.00 14.78           C  
ANISOU  979  CA  ALA A  56     1600   2056   1961    179    270      1       C  
ATOM    980  C   ALA A  56      76.091  76.710  31.899  1.00 15.46           C  
ANISOU  980  C   ALA A  56     1856   2134   1884    140    290     55       C  
ATOM    981  O   ALA A  56      75.707  75.571  31.616  1.00 16.29           O  
ANISOU  981  O   ALA A  56     2155   2308   1729    117    265    113       O  
ATOM    982  CB  ALA A  56      77.746  76.503  33.709  1.00 16.62           C  
ANISOU  982  CB  ALA A  56     1895   2265   2153    213    119   -146       C  
ATOM    983  H   ALA A  56      75.315  75.750  34.283  1.00 17.49           H  
ATOM    984  HA  ALA A  56      76.415  78.064  33.411  1.00 17.75           H  
ATOM    985  HB1 ALA A  56      78.425  76.886  33.133  1.00 19.95           H  
ATOM    986  HB2 ALA A  56      77.941  76.713  34.636  1.00 19.95           H  
ATOM    987  HB3 ALA A  56      77.714  75.541  33.587  1.00 19.95           H  
ATOM    988  N   ASP A  57      76.307  77.662  30.990  1.00 16.16           N  
ANISOU  988  N   ASP A  57     2065   2178   1897    339    298    110       N  
ATOM    989  CA  ASP A  57      76.058  77.487  29.568  1.00 16.13           C  
ANISOU  989  CA  ASP A  57     2035   2226   1866    447    261    309       C  
ATOM    990  C   ASP A  57      77.200  78.106  28.772  1.00 16.80           C  
ANISOU  990  C   ASP A  57     2165   2316   1902    532    404      3       C  
ATOM    991  O   ASP A  57      77.672  79.202  29.086  1.00 17.76           O  
ANISOU  991  O   ASP A  57     2084   2501   2162    509    592     93       O  
ATOM    992  CB  ASP A  57      74.707  78.124  29.187  1.00 16.77           C  
ANISOU  992  CB  ASP A  57     1986   2586   1800    454    242    406       C  
ATOM    993  CG  ASP A  57      74.360  77.898  27.736  1.00 17.81           C  
ANISOU  993  CG  ASP A  57     2089   2786   1890    461    306    311       C  
ATOM    994  OD1 ASP A  57      74.755  78.714  26.893  1.00 19.97           O  
ANISOU  994  OD1 ASP A  57     2442   3014   2130    413    406    559       O  
ATOM    995  OD2 ASP A  57      73.733  76.867  27.430  1.00 18.74           O  
ANISOU  995  OD2 ASP A  57     2268   2866   1987    392     38     35       O  
ATOM    996  H   ASP A  57      76.608  78.443  31.184  1.00 19.40           H  
ATOM    997  HA  ASP A  57      76.031  76.545  29.335  1.00 19.36           H  
ATOM    998  HB2 ASP A  57      74.006  77.732  29.731  1.00 20.13           H  
ATOM    999  HB3 ASP A  57      74.752  79.081  29.342  1.00 20.13           H  
ATOM   1000  N   ALA A  58      77.638  77.408  27.723  1.00 17.54           N  
ANISOU 1000  N   ALA A  58     2324   2348   1994    490    606     50       N  
ATOM   1001  CA  ALA A  58      78.842  77.826  27.021  1.00 18.75           C  
ANISOU 1001  CA  ALA A  58     2575   2553   1994    638    721    119       C  
ATOM   1002  C   ALA A  58      78.644  79.080  26.178  1.00 19.43           C  
ANISOU 1002  C   ALA A  58     2520   2516   2347    554    689    182       C  
ATOM   1003  O   ALA A  58      79.604  79.836  25.983  1.00 21.43           O  
ANISOU 1003  O   ALA A  58     2591   2906   2647    447    464    221       O  
ATOM   1004  CB  ALA A  58      79.345  76.691  26.132  1.00 20.59           C  
ANISOU 1004  CB  ALA A  58     2822   2790   2209    798    821     59       C  
ATOM   1005  H   ALA A  58      77.264  76.702  27.405  1.00 21.06           H  
ATOM   1006  HA  ALA A  58      79.512  78.031  27.692  1.00 22.50           H  
ATOM   1007  HB1 ALA A  58      80.144  76.984  25.667  1.00 24.71           H  
ATOM   1008  HB2 ALA A  58      79.548  75.921  26.686  1.00 24.71           H  
ATOM   1009  HB3 ALA A  58      78.654  76.463  25.490  1.00 24.71           H  
ATOM   1010  N   ASP A  59      77.443  79.310  25.625  1.00 18.79           N  
ANISOU 1010  N   ASP A  59     2433   2394   2313    377    898    329       N  
ATOM   1011  CA  ASP A  59      77.293  80.330  24.590  1.00 19.38           C  
ANISOU 1011  CA  ASP A  59     2599   2470   2294    517    822    452       C  
ATOM   1012  C   ASP A  59      76.198  81.362  24.849  1.00 19.37           C  
ANISOU 1012  C   ASP A  59     2621   2404   2336    487    895    570       C  
ATOM   1013  O   ASP A  59      75.967  82.220  23.982  1.00 19.15           O  
ANISOU 1013  O   ASP A  59     2666   2233   2376    548    703    778       O  
ATOM   1014  CB  ASP A  59      77.097  79.689  23.199  1.00 19.93           C  
ANISOU 1014  CB  ASP A  59     2758   2606   2208    453    808    534       C  
ATOM   1015  CG  ASP A  59      75.818  78.883  23.092  1.00 20.35           C  
ANISOU 1015  CG  ASP A  59     2816   2712   2206    517    731     11       C  
ATOM   1016  OD1 ASP A  59      75.048  78.830  24.076  1.00 20.02           O  
ANISOU 1016  OD1 ASP A  59     2589   2664   2352    569    901   -108       O  
ATOM   1017  OD2 ASP A  59      75.600  78.303  22.007  1.00 22.61           O  
ANISOU 1017  OD2 ASP A  59     3182   3184   2226    452    625    -12       O  
ATOM   1018  H   ASP A  59      76.720  78.894  25.832  1.00 22.56           H  
ATOM   1019  HA  ASP A  59      78.125  80.829  24.580  1.00 23.26           H  
ATOM   1020  HB2 ASP A  59      77.064  80.391  22.531  1.00 23.92           H  
ATOM   1021  HB3 ASP A  59      77.841  79.093  23.019  1.00 23.92           H  
ATOM   1022  N   ASN A  60      75.545  81.339  26.015  1.00 19.03           N  
ANISOU 1022  N   ASN A  60     2576   2358   2296    531    688    249       N  
ATOM   1023  CA  ASN A  60      74.504  82.309  26.366  1.00 18.90           C  
ANISOU 1023  CA  ASN A  60     2421   2410   2349    543    411    291       C  
ATOM   1024  C   ASN A  60      73.239  82.124  25.532  1.00 18.43           C  
ANISOU 1024  C   ASN A  60     2293   2593   2119    534    554    224       C  
ATOM   1025  O   ASN A  60      72.397  83.023  25.468  1.00 19.54           O  
ANISOU 1025  O   ASN A  60     2497   2561   2368    511    251    274       O  
ATOM   1026  CB  ASN A  60      75.018  83.755  26.270  1.00 18.53           C  
ANISOU 1026  CB  ASN A  60     2366   2302   2373    508    427    248       C  
ATOM   1027  CG  ASN A  60      74.406  84.677  27.316  1.00 18.90           C  
ANISOU 1027  CG  ASN A  60     2377   2304   2499    428    681    328       C  
ATOM   1028  OD1 ASN A  60      73.899  84.239  28.366  1.00 19.10           O  
ANISOU 1028  OD1 ASN A  60     2395   2318   2545    471    791    367       O  
ATOM   1029  ND2 ASN A  60      74.477  85.978  27.045  1.00 20.11           N  
ANISOU 1029  ND2 ASN A  60     2538   2356   2746    463    673    189       N  
ATOM   1030  H   ASN A  60      75.693  80.757  26.630  1.00 22.84           H  
ATOM   1031  HA  ASN A  60      74.255  82.162  27.292  1.00 22.68           H  
ATOM   1032  HB2 ASN A  60      75.980  83.756  26.397  1.00 22.24           H  
ATOM   1033  HB3 ASN A  60      74.799  84.109  25.395  1.00 22.24           H  
ATOM   1034 HD21 ASN A  60      74.149  86.550  27.596  1.00 24.14           H  
ATOM   1035 HD22 ASN A  60      74.850  86.246  26.318  1.00 24.14           H  
ATOM   1036  N   GLN A  61      73.101  80.962  24.892  1.00 18.52           N  
ANISOU 1036  N   GLN A  61     2311   2786   1941    464    682    130       N  
ATOM   1037  CA AGLN A  61      71.908  80.600  24.138  0.70 19.02           C  
ANISOU 1037  CA AGLN A  61     2540   2824   1861    494    757    226       C  
ATOM   1038  CA BGLN A  61      71.909  80.601  24.135  0.30 19.04           C  
ANISOU 1038  CA BGLN A  61     2464   2799   1970    503    588    138       C  
ATOM   1039  C   GLN A  61      71.289  79.384  24.807  1.00 18.75           C  
ANISOU 1039  C   GLN A  61     2517   2714   1892    450    546    194       C  
ATOM   1040  O   GLN A  61      71.975  78.386  25.038  1.00 19.12           O  
ANISOU 1040  O   GLN A  61     2643   2590   2031    494    516    268       O  
ATOM   1041  CB AGLN A  61      72.265  80.250  22.692  0.70 21.58           C  
ANISOU 1041  CB AGLN A  61     3040   3307   1852    343    958    368       C  
ATOM   1042  CB BGLN A  61      72.272  80.266  22.684  0.30 20.74           C  
ANISOU 1042  CB BGLN A  61     2685   3068   2128    473    527    108       C  
ATOM   1043  CG AGLN A  61      72.878  81.398  21.927  0.70 24.87           C  
ANISOU 1043  CG AGLN A  61     3637   3823   1988    173   1000    275       C  
ATOM   1044  CG BGLN A  61      73.158  81.305  21.998  0.30 22.83           C  
ANISOU 1044  CG BGLN A  61     2980   3358   2337    424    464     39       C  
ATOM   1045  CD AGLN A  61      73.066  81.079  20.462  0.70 29.57           C  
ANISOU 1045  CD AGLN A  61     4366   4475   2394   -277    946    176       C  
ATOM   1046  CD BGLN A  61      72.489  82.655  21.849  0.30 25.44           C  
ANISOU 1046  CD BGLN A  61     3361   3712   2592    199    419    -32       C  
ATOM   1047  OE1AGLN A  61      72.299  80.310  19.876  0.70 31.79           O  
ANISOU 1047  OE1AGLN A  61     4803   4744   2533   -339    852    120       O  
ATOM   1048  OE1BGLN A  61      71.459  82.779  21.190  0.30 26.51           O  
ANISOU 1048  OE1BGLN A  61     3515   3862   2695    270    365    -50       O  
ATOM   1049  NE2AGLN A  61      74.093  81.658  19.865  0.70 31.55           N  
ANISOU 1049  NE2AGLN A  61     4552   4700   2736   -440    891     68       N  
ATOM   1050  NE2BGLN A  61      73.071  83.674  22.466  0.30 26.61           N  
ANISOU 1050  NE2BGLN A  61     3523   3874   2712    -53    449     92       N  
ATOM   1051  H  AGLN A  61      73.707  80.352  24.882  0.70 22.24           H  
ATOM   1052  H  BGLN A  61      73.706  80.351  24.884  0.30 22.24           H  
ATOM   1053  HA AGLN A  61      71.276  81.335  24.135  0.70 22.83           H  
ATOM   1054  HA BGLN A  61      71.271  81.331  24.129  0.30 22.85           H  
ATOM   1055  HB2AGLN A  61      72.904  79.520  22.696  0.70 25.90           H  
ATOM   1056  HB2BGLN A  61      72.748  79.420  22.672  0.30 24.90           H  
ATOM   1057  HB3AGLN A  61      71.457  79.981  22.227  0.70 25.90           H  
ATOM   1058  HB3BGLN A  61      71.453  80.193  22.169  0.30 24.90           H  
ATOM   1059  HG2AGLN A  61      72.297  82.172  21.995  0.70 29.85           H  
ATOM   1060  HG2BGLN A  61      73.964  81.428  22.524  0.30 27.41           H  
ATOM   1061  HG3AGLN A  61      73.748  81.603  22.305  0.70 29.85           H  
ATOM   1062  HG3BGLN A  61      73.388  80.986  21.111  0.30 27.41           H  
ATOM   1063 HE21AGLN A  61      74.610  82.182  20.310  0.70 37.87           H  
ATOM   1064 HE21BGLN A  61      73.790  83.548  22.921  0.30 31.94           H  
ATOM   1065 HE22AGLN A  61      74.245  81.510  19.032  0.70 37.87           H  
ATOM   1066 HE22BGLN A  61      72.729  84.462  22.412  0.30 31.94           H  
ATOM   1067  N   PHE A  62      70.004  79.473  25.127  1.00 18.15           N  
ANISOU 1067  N   PHE A  62     2644   2652   1602    456    485    150       N  
ATOM   1068  CA  PHE A  62      69.356  78.442  25.933  1.00 17.21           C  
ANISOU 1068  CA  PHE A  62     2520   2492   1527    418    335    202       C  
ATOM   1069  C   PHE A  62      68.149  77.846  25.216  1.00 17.08           C  
ANISOU 1069  C   PHE A  62     2620   2585   1284    200    283    259       C  
ATOM   1070  O   PHE A  62      67.012  77.963  25.689  1.00 17.26           O  
ANISOU 1070  O   PHE A  62     2542   2662   1354    204     -2    246       O  
ATOM   1071  CB  PHE A  62      68.939  79.045  27.275  1.00 16.37           C  
ANISOU 1071  CB  PHE A  62     2302   2277   1642    460    254    180       C  
ATOM   1072  CG  PHE A  62      70.088  79.587  28.100  1.00 15.64           C  
ANISOU 1072  CG  PHE A  62     2206   1946   1791    326    293     83       C  
ATOM   1073  CD1 PHE A  62      70.625  80.842  27.840  1.00 17.08           C  
ANISOU 1073  CD1 PHE A  62     2292   2208   1989    478    417     85       C  
ATOM   1074  CD2 PHE A  62      70.605  78.855  29.167  1.00 15.55           C  
ANISOU 1074  CD2 PHE A  62     2095   1954   1858    189    145     95       C  
ATOM   1075  CE1 PHE A  62      71.674  81.344  28.612  1.00 16.61           C  
ANISOU 1075  CE1 PHE A  62     2124   2173   2012    607    418    225       C  
ATOM   1076  CE2 PHE A  62      71.645  79.354  29.940  1.00 16.60           C  
ANISOU 1076  CE2 PHE A  62     2031   2124   2153    485    195    252       C  
ATOM   1077  CZ  PHE A  62      72.164  80.609  29.675  1.00 17.01           C  
ANISOU 1077  CZ  PHE A  62     2132   2136   2194    658    209    179       C  
ATOM   1078  H   PHE A  62      69.486  80.117  24.891  1.00 21.79           H  
ATOM   1079  HA  PHE A  62      69.978  77.715  26.091  1.00 20.66           H  
ATOM   1080  HB2 PHE A  62      68.326  79.777  27.108  1.00 19.65           H  
ATOM   1081  HB3 PHE A  62      68.500  78.357  27.800  1.00 19.65           H  
ATOM   1082  HD1 PHE A  62      70.282  81.354  27.143  1.00 20.50           H  
ATOM   1083  HD2 PHE A  62      70.248  78.019  29.364  1.00 18.66           H  
ATOM   1084  HE1 PHE A  62      72.044  82.173  28.411  1.00 19.93           H  
ATOM   1085  HE2 PHE A  62      71.993  78.844  30.636  1.00 19.93           H  
ATOM   1086  HZ  PHE A  62      72.841  80.956  30.210  1.00 20.42           H  
ATOM   1087  N   PHE A  63      68.388  77.219  24.060  1.00 18.49           N  
ANISOU 1087  N   PHE A  63     2948   2704   1375     40    194    158       N  
ATOM   1088  CA  PHE A  63      67.328  76.684  23.225  1.00 20.07           C  
ANISOU 1088  CA  PHE A  63     3111   2817   1696     86    191    142       C  
ATOM   1089  C   PHE A  63      67.219  75.168  23.280  1.00 20.08           C  
ANISOU 1089  C   PHE A  63     3008   2822   1799    268    -68    -61       C  
ATOM   1090  O   PHE A  63      66.366  74.595  22.591  1.00 21.18           O  
ANISOU 1090  O   PHE A  63     3157   2877   2014    333   -278   -240       O  
ATOM   1091  CB  PHE A  63      67.557  77.117  21.770  1.00 20.58           C  
ANISOU 1091  CB  PHE A  63     3145   2929   1744    266    261    101       C  
ATOM   1092  CG  PHE A  63      67.431  78.600  21.537  1.00 22.41           C  
ANISOU 1092  CG  PHE A  63     3305   3049   2162    464    249    312       C  
ATOM   1093  CD1 PHE A  63      68.554  79.406  21.466  1.00 23.79           C  
ANISOU 1093  CD1 PHE A  63     3470   3124   2445    510    392    464       C  
ATOM   1094  CD2 PHE A  63      66.190  79.185  21.394  1.00 24.08           C  
ANISOU 1094  CD2 PHE A  63     3513   3240   2398    560    302    392       C  
ATOM   1095  CE1 PHE A  63      68.438  80.774  21.250  1.00 24.85           C  
ANISOU 1095  CE1 PHE A  63     3546   3322   2572    499    424    513       C  
ATOM   1096  CE2 PHE A  63      66.064  80.556  21.170  1.00 24.52           C  
ANISOU 1096  CE2 PHE A  63     3597   3278   2441    622    422    372       C  
ATOM   1097  CZ  PHE A  63      67.192  81.351  21.099  1.00 23.95           C  
ANISOU 1097  CZ  PHE A  63     3515   3220   2367    544    449    508       C  
ATOM   1098  H   PHE A  63      69.175  77.092  23.739  1.00 22.20           H  
ATOM   1099  HA  PHE A  63      66.483  77.048  23.533  1.00 24.09           H  
ATOM   1100  HB2 PHE A  63      68.452  76.854  21.505  1.00 24.70           H  
ATOM   1101  HB3 PHE A  63      66.902  76.675  21.208  1.00 24.70           H  
ATOM   1102  HD1 PHE A  63      69.398  79.028  21.565  1.00 28.56           H  
ATOM   1103  HD2 PHE A  63      65.426  78.658  21.447  1.00 28.91           H  
ATOM   1104  HE1 PHE A  63      69.202  81.303  21.206  1.00 29.82           H  
ATOM   1105  HE2 PHE A  63      65.221  80.936  21.068  1.00 29.43           H  
ATOM   1106  HZ  PHE A  63      67.114  82.266  20.952  1.00 28.75           H  
ATOM   1107  N   ALA A  64      68.051  74.504  24.064  1.00 19.62           N  
ANISOU 1107  N   ALA A  64     2857   2705   1894    320     18   -112       N  
ATOM   1108  CA  ALA A  64      67.965  73.060  24.195  1.00 19.89           C  
ANISOU 1108  CA  ALA A  64     2957   2732   1868     85    -77   -275       C  
ATOM   1109  C   ALA A  64      66.793  72.685  25.095  1.00 19.15           C  
ANISOU 1109  C   ALA A  64     2960   2540   1777    196   -125   -383       C  
ATOM   1110  O   ALA A  64      66.427  73.422  26.008  1.00 19.13           O  
ANISOU 1110  O   ALA A  64     3026   2486   1757    301    -26   -380       O  
ATOM   1111  CB  ALA A  64      69.258  72.514  24.783  1.00 20.98           C  
ANISOU 1111  CB  ALA A  64     3120   2822   2028    160    -80   -328       C  
ATOM   1112  H   ALA A  64      68.676  74.865  24.531  1.00 23.55           H  
ATOM   1113  HA  ALA A  64      67.827  72.654  23.325  1.00 23.88           H  
ATOM   1114  HB1 ALA A  64      69.192  71.548  24.851  1.00 25.18           H  
ATOM   1115  HB2 ALA A  64      69.996  72.754  24.201  1.00 25.18           H  
ATOM   1116  HB3 ALA A  64      69.393  72.899  25.663  1.00 25.18           H  
ATOM   1117  N   SER A  65      66.192  71.527  24.822  1.00 19.76           N  
ANISOU 1117  N   SER A  65     3123   2486   1898     47   -145   -421       N  
ATOM   1118  CA ASER A  65      65.082  71.057  25.644  0.52 20.28           C  
ANISOU 1118  CA ASER A  65     3128   2485   2091    -34   -178   -399       C  
ATOM   1119  CA BSER A  65      65.070  71.097  25.647  0.48 20.47           C  
ANISOU 1119  CA BSER A  65     3131   2512   2133    117    -97   -398       C  
ATOM   1120  C   SER A  65      65.478  71.000  27.113  1.00 19.35           C  
ANISOU 1120  C   SER A  65     2913   2453   1988    166   -124   -319       C  
ATOM   1121  O   SER A  65      64.695  71.368  28.002  1.00 18.83           O  
ANISOU 1121  O   SER A  65     2818   2469   1867    293   -144   -364       O  
ATOM   1122  CB ASER A  65      64.653  69.674  25.150  0.52 22.50           C  
ANISOU 1122  CB ASER A  65     3359   2768   2421   -121   -267   -302       C  
ATOM   1123  CB BSER A  65      64.492  69.776  25.135  0.48 22.88           C  
ANISOU 1123  CB BSER A  65     3345   2818   2530    308    -26   -337       C  
ATOM   1124  OG ASER A  65      63.759  69.068  26.056  0.52 23.67           O  
ANISOU 1124  OG ASER A  65     3499   2936   2557   -416   -447   -330       O  
ATOM   1125  OG BSER A  65      65.350  68.701  25.418  0.48 24.05           O  
ANISOU 1125  OG BSER A  65     3478   2940   2718    491      4   -419       O  
ATOM   1126  H  ASER A  65      66.403  71.001  24.175  0.52 23.72           H  
ATOM   1127  H  BSER A  65      66.406  70.989  24.185  0.48 23.72           H  
ATOM   1128  HA ASER A  65      64.331  71.666  25.563  0.52 24.34           H  
ATOM   1129  HA BSER A  65      64.360  71.754  25.580  0.48 24.57           H  
ATOM   1130  HB2ASER A  65      64.214  69.769  24.291  0.52 27.01           H  
ATOM   1131  HB2BSER A  65      63.638  69.619  25.566  0.48 27.46           H  
ATOM   1132  HB3ASER A  65      65.439  69.113  25.061  0.52 27.01           H  
ATOM   1133  HB3BSER A  65      64.373  69.838  24.174  0.48 27.46           H  
ATOM   1134  HG ASER A  65      63.496  68.331  25.751  0.52 28.41           H  
ATOM   1135  HG BSER A  65      66.093  68.819  25.045  0.48 28.86           H  
ATOM   1136  N   TYR A  66      66.705  70.542  27.390  1.00 18.75           N  
ANISOU 1136  N   TYR A  66     2722   2450   1952    120   -105   -441       N  
ATOM   1137  CA  TYR A  66      67.187  70.452  28.764  1.00 16.56           C  
ANISOU 1137  CA  TYR A  66     2460   2129   1701    354     79   -379       C  
ATOM   1138  C   TYR A  66      67.272  71.825  29.425  1.00 15.87           C  
ANISOU 1138  C   TYR A  66     2293   2069   1669    345     81   -266       C  
ATOM   1139  O   TYR A  66      67.127  71.934  30.660  1.00 15.48           O  
ANISOU 1139  O   TYR A  66     2215   1999   1666    319    -42   -312       O  
ATOM   1140  CB  TYR A  66      68.554  69.745  28.784  1.00 16.88           C  
ANISOU 1140  CB  TYR A  66     2534   1962   1917    371    290   -336       C  
ATOM   1141  CG  TYR A  66      69.050  69.380  30.165  1.00 15.28           C  
ANISOU 1141  CG  TYR A  66     2163   1748   1895    221    160   -218       C  
ATOM   1142  CD1 TYR A  66      68.582  68.242  30.812  1.00 14.96           C  
ANISOU 1142  CD1 TYR A  66     2082   1817   1785    287    104   -111       C  
ATOM   1143  CD2 TYR A  66      70.000  70.157  30.813  1.00 16.38           C  
ANISOU 1143  CD2 TYR A  66     2102   2065   2058    -75    347    -78       C  
ATOM   1144  CE1 TYR A  66      69.045  67.900  32.076  1.00 15.11           C  
ANISOU 1144  CE1 TYR A  66     1962   1895   1884    354    -35   -225       C  
ATOM   1145  CE2 TYR A  66      70.457  69.841  32.072  1.00 16.49           C  
ANISOU 1145  CE2 TYR A  66     2003   2088   2173     47    166   -348       C  
ATOM   1146  CZ  TYR A  66      69.989  68.705  32.703  1.00 15.47           C  
ANISOU 1146  CZ  TYR A  66     1881   1926   2071    228    -10   -228       C  
ATOM   1147  OH  TYR A  66      70.432  68.385  33.959  1.00 16.12           O  
ANISOU 1147  OH  TYR A  66     1860   1961   2303      2   -350   -148       O  
ATOM   1148  H   TYR A  66      67.275  70.279  26.802  1.00 22.51           H  
ATOM   1149  HA  TYR A  66      66.566  69.921  29.287  1.00 19.87           H  
ATOM   1150  HB2 TYR A  66      68.485  68.925  28.271  1.00 20.26           H  
ATOM   1151  HB3 TYR A  66      69.212  70.333  28.382  1.00 20.26           H  
ATOM   1152  HD1 TYR A  66      67.951  67.703  30.392  1.00 17.96           H  
ATOM   1153  HD2 TYR A  66      70.337  70.910  30.385  1.00 19.67           H  
ATOM   1154  HE1 TYR A  66      68.725  67.137  32.500  1.00 18.14           H  
ATOM   1155  HE2 TYR A  66      71.077  70.389  32.495  1.00 19.79           H  
ATOM   1156  HH  TYR A  66      70.994  68.953  34.219  1.00 19.35           H  
ATOM   1157  N   ASP A  67      67.454  72.885  28.627  1.00 15.53           N  
ANISOU 1157  N   ASP A  67     2254   2062   1583    394    121   -135       N  
ATOM   1158  CA  ASP A  67      67.566  74.236  29.163  1.00 15.11           C  
ANISOU 1158  CA  ASP A  67     2139   2162   1440    353     35   -155       C  
ATOM   1159  C   ASP A  67      66.220  74.831  29.575  1.00 13.90           C  
ANISOU 1159  C   ASP A  67     1918   2055   1309    298   -312   -128       C  
ATOM   1160  O   ASP A  67      66.171  75.753  30.409  1.00 14.12           O  
ANISOU 1160  O   ASP A  67     1769   2164   1432    181   -244   -147       O  
ATOM   1161  CB  ASP A  67      68.137  75.199  28.119  1.00 14.94           C  
ANISOU 1161  CB  ASP A  67     1953   2231   1492    258    386    -20       C  
ATOM   1162  CG  ASP A  67      69.506  74.799  27.599  1.00 15.80           C  
ANISOU 1162  CG  ASP A  67     2137   2261   1603    289    296      9       C  
ATOM   1163  OD1 ASP A  67      70.239  74.031  28.267  1.00 16.21           O  
ANISOU 1163  OD1 ASP A  67     2098   2286   1777    543    117     95       O  
ATOM   1164  OD2 ASP A  67      69.845  75.282  26.502  1.00 16.83           O  
ANISOU 1164  OD2 ASP A  67     2549   2244   1600    412    308    102       O  
ATOM   1165  H   ASP A  67      67.516  72.845  27.770  1.00 18.64           H  
ATOM   1166  HA  ASP A  67      68.157  74.168  29.929  1.00 18.14           H  
ATOM   1167  HB2 ASP A  67      67.531  75.233  27.362  1.00 17.93           H  
ATOM   1168  HB3 ASP A  67      68.218  76.080  28.518  1.00 17.93           H  
ATOM   1169  N   ALA A  68      65.136  74.380  28.950  1.00 14.94           N  
ANISOU 1169  N   ALA A  68     2020   2230   1425    256   -284   -120       N  
ATOM   1170  CA  ALA A  68      63.869  75.093  29.063  1.00 16.02           C  
ANISOU 1170  CA  ALA A  68     2126   2411   1552    280   -118   -113       C  
ATOM   1171  C   ALA A  68      63.361  75.251  30.489  1.00 14.85           C  
ANISOU 1171  C   ALA A  68     2060   2041   1540    297    -40   -242       C  
ATOM   1172  O   ALA A  68      62.871  76.350  30.825  1.00 15.03           O  
ANISOU 1172  O   ALA A  68     2037   2109   1564    359   -100   -196       O  
ATOM   1173  CB  ALA A  68      62.819  74.408  28.179  1.00 17.96           C  
ANISOU 1173  CB  ALA A  68     2471   2586   1766    290   -163   -175       C  
ATOM   1174  H   ALA A  68      65.105  73.673  28.461  1.00 17.93           H  
ATOM   1175  HA  ALA A  68      64.019  75.991  28.728  1.00 19.24           H  
ATOM   1176  HB1 ALA A  68      61.958  74.831  28.326  1.00 21.55           H  
ATOM   1177  HB2 ALA A  68      63.079  74.502  27.250  1.00 21.55           H  
ATOM   1178  HB3 ALA A  68      62.771  73.469  28.416  1.00 21.55           H  
ATOM   1179  N   PRO A  69      63.425  74.250  31.359  1.00 13.91           N  
ANISOU 1179  N   PRO A  69     1883   1765   1635    251     16   -359       N  
ATOM   1180  CA  PRO A  69      62.942  74.480  32.728  1.00 13.32           C  
ANISOU 1180  CA  PRO A  69     1725   1795   1540    144    -40   -329       C  
ATOM   1181  C   PRO A  69      63.739  75.542  33.451  1.00 13.02           C  
ANISOU 1181  C   PRO A  69     1668   1780   1498    230   -153   -151       C  
ATOM   1182  O   PRO A  69      63.184  76.289  34.267  1.00 12.93           O  
ANISOU 1182  O   PRO A  69     1639   1721   1554    241   -108   -218       O  
ATOM   1183  CB  PRO A  69      63.068  73.106  33.389  1.00 14.11           C  
ANISOU 1183  CB  PRO A  69     1830   1834   1698      9   -216   -325       C  
ATOM   1184  CG  PRO A  69      63.033  72.149  32.248  1.00 14.85           C  
ANISOU 1184  CG  PRO A  69     1974   1865   1803    247   -106   -290       C  
ATOM   1185  CD  PRO A  69      63.769  72.829  31.136  1.00 13.89           C  
ANISOU 1185  CD  PRO A  69     1954   1700   1623    177    -98   -334       C  
ATOM   1186  HA  PRO A  69      62.004  74.727  32.721  1.00 15.99           H  
ATOM   1187  HB2 PRO A  69      63.906  73.043  33.873  1.00 16.94           H  
ATOM   1188  HB3 PRO A  69      62.324  72.957  33.994  1.00 16.94           H  
ATOM   1189  HG2 PRO A  69      63.473  71.322  32.498  1.00 17.83           H  
ATOM   1190  HG3 PRO A  69      62.113  71.972  31.995  1.00 17.83           H  
ATOM   1191  HD2 PRO A  69      64.725  72.684  31.210  1.00 16.68           H  
ATOM   1192  HD3 PRO A  69      63.453  72.525  30.271  1.00 16.68           H  
ATOM   1193  N   ALA A  70      65.039  75.620  33.189  1.00 12.76           N  
ANISOU 1193  N   ALA A  70     1564   1794   1491    311    -30   -225       N  
ATOM   1194  CA  ALA A  70      65.878  76.624  33.822  1.00 13.08           C  
ANISOU 1194  CA  ALA A  70     1630   1769   1572    136    -70   -103       C  
ATOM   1195  C   ALA A  70      65.555  78.018  33.302  1.00 12.78           C  
ANISOU 1195  C   ALA A  70     1544   1985   1327    234    -82    -12       C  
ATOM   1196  O   ALA A  70      65.484  78.968  34.084  1.00 13.83           O  
ANISOU 1196  O   ALA A  70     1694   2085   1475    349   -114    -34       O  
ATOM   1197  CB  ALA A  70      67.345  76.275  33.559  1.00 13.49           C  
ANISOU 1197  CB  ALA A  70     1759   1697   1669    135     26      2       C  
ATOM   1198  H   ALA A  70      65.462  75.103  32.647  1.00 15.32           H  
ATOM   1199  HA  ALA A  70      65.724  76.626  34.779  1.00 15.70           H  
ATOM   1200  HB1 ALA A  70      67.910  76.912  34.023  1.00 16.20           H  
ATOM   1201  HB2 ALA A  70      67.520  75.379  33.887  1.00 16.20           H  
ATOM   1202  HB3 ALA A  70      67.514  76.317  32.605  1.00 16.20           H  
ATOM   1203  N   VAL A  71      65.356  78.155  31.989  1.00 13.49           N  
ANISOU 1203  N   VAL A  71     1824   1989   1314    249    -13    147       N  
ATOM   1204  CA  VAL A  71      64.956  79.439  31.414  1.00 13.64           C  
ANISOU 1204  CA  VAL A  71     1884   1887   1412    279    102    -15       C  
ATOM   1205  C   VAL A  71      63.723  79.976  32.129  1.00 13.46           C  
ANISOU 1205  C   VAL A  71     1858   1777   1479    238     -3    -93       C  
ATOM   1206  O   VAL A  71      63.689  81.132  32.572  1.00 13.85           O  
ANISOU 1206  O   VAL A  71     1900   1905   1458     62   -106    -69       O  
ATOM   1207  CB  VAL A  71      64.714  79.285  29.901  1.00 14.54           C  
ANISOU 1207  CB  VAL A  71     2164   2018   1343    472    177    -64       C  
ATOM   1208  CG1 VAL A  71      64.029  80.521  29.341  1.00 15.38           C  
ANISOU 1208  CG1 VAL A  71     2312   2195   1337    336    -99    -93       C  
ATOM   1209  CG2 VAL A  71      66.027  78.995  29.184  1.00 15.10           C  
ANISOU 1209  CG2 VAL A  71     2315   2112   1311    763     99    -42       C  
ATOM   1210  H   VAL A  71      65.446  77.524  31.411  1.00 16.20           H  
ATOM   1211  HA  VAL A  71      65.673  80.079  31.542  1.00 16.38           H  
ATOM   1212  HB  VAL A  71      64.122  78.532  29.745  1.00 17.46           H  
ATOM   1213 HG11 VAL A  71      64.123  80.524  28.375  1.00 18.46           H  
ATOM   1214 HG12 VAL A  71      63.090  80.499  29.582  1.00 18.46           H  
ATOM   1215 HG13 VAL A  71      64.448  81.311  29.716  1.00 18.46           H  
ATOM   1216 HG21 VAL A  71      65.856  78.911  28.233  1.00 18.13           H  
ATOM   1217 HG22 VAL A  71      66.643  79.726  29.345  1.00 18.13           H  
ATOM   1218 HG23 VAL A  71      66.399  78.167  29.527  1.00 18.13           H  
ATOM   1219  N   ASP A  72      62.693  79.137  32.271  1.00 13.05           N  
ANISOU 1219  N   ASP A  72     1743   1744   1473    -32    -12    -66       N  
ATOM   1220  CA  ASP A  72      61.436  79.604  32.848  1.00 14.12           C  
ANISOU 1220  CA  ASP A  72     1771   1929   1667    110   -106      5       C  
ATOM   1221  C   ASP A  72      61.548  79.843  34.350  1.00 13.29           C  
ANISOU 1221  C   ASP A  72     1685   1798   1567    243   -149    -71       C  
ATOM   1222  O   ASP A  72      60.983  80.811  34.865  1.00 13.17           O  
ANISOU 1222  O   ASP A  72     1833   1614   1555    318     31   -127       O  
ATOM   1223  CB  ASP A  72      60.294  78.647  32.516  1.00 14.10           C  
ANISOU 1223  CB  ASP A  72     1674   2090   1595     99   -277    -54       C  
ATOM   1224  CG  ASP A  72      59.729  78.874  31.121  1.00 15.25           C  
ANISOU 1224  CG  ASP A  72     1827   2225   1742    218   -175     10       C  
ATOM   1225  OD1 ASP A  72      60.017  79.924  30.510  1.00 15.67           O  
ANISOU 1225  OD1 ASP A  72     2163   2225   1567    157   -414    112       O  
ATOM   1226  OD2 ASP A  72      58.994  77.992  30.630  1.00 16.77           O  
ANISOU 1226  OD2 ASP A  72     2151   2374   1846    127   -272   -132       O  
ATOM   1227  H   ASP A  72      62.696  78.307  32.045  1.00 15.67           H  
ATOM   1228  HA  ASP A  72      61.219  80.457  32.439  1.00 16.96           H  
ATOM   1229  HB2 ASP A  72      60.622  77.735  32.564  1.00 16.93           H  
ATOM   1230  HB3 ASP A  72      59.577  78.776  33.156  1.00 16.93           H  
ATOM   1231  N   ALA A  73      62.259  78.976  35.084  1.00 12.47           N  
ANISOU 1231  N   ALA A  73     1605   1633   1501    229   -192     17       N  
ATOM   1232  CA  ALA A  73      62.401  79.218  36.523  1.00 12.49           C  
ANISOU 1232  CA  ALA A  73     1769   1628   1348    218   -113     59       C  
ATOM   1233  C   ALA A  73      63.075  80.564  36.755  1.00 12.34           C  
ANISOU 1233  C   ALA A  73     1631   1682   1375    187     43    -79       C  
ATOM   1234  O   ALA A  73      62.666  81.352  37.627  1.00 12.55           O  
ANISOU 1234  O   ALA A  73     1616   1657   1496    265    -24    -70       O  
ATOM   1235  CB  ALA A  73      63.223  78.104  37.167  1.00 13.32           C  
ANISOU 1235  CB  ALA A  73     1968   1700   1394     53   -395     27       C  
ATOM   1236  H   ALA A  73      62.652  78.271  34.787  1.00 14.98           H  
ATOM   1237  HA  ALA A  73      61.525  79.220  36.939  1.00 15.00           H  
ATOM   1238  HB1 ALA A  73      63.310  78.284  38.116  1.00 15.99           H  
ATOM   1239  HB2 ALA A  73      62.769  77.257  37.032  1.00 15.99           H  
ATOM   1240  HB3 ALA A  73      64.100  78.078  36.753  1.00 15.99           H  
ATOM   1241  N   HIS A  74      64.103  80.846  35.957  1.00 12.74           N  
ANISOU 1241  N   HIS A  74     1636   1731   1471    177   -120      2       N  
ATOM   1242  CA  HIS A  74      64.882  82.067  36.108  1.00 13.10           C  
ANISOU 1242  CA  HIS A  74     1537   1800   1642    118    -51     85       C  
ATOM   1243  C   HIS A  74      64.059  83.278  35.694  1.00 13.38           C  
ANISOU 1243  C   HIS A  74     1703   1800   1580     95    -82     23       C  
ATOM   1244  O   HIS A  74      63.975  84.268  36.431  1.00 14.14           O  
ANISOU 1244  O   HIS A  74     1888   1922   1561    115     -9     14       O  
ATOM   1245  CB  HIS A  74      66.111  81.907  35.227  1.00 13.81           C  
ANISOU 1245  CB  HIS A  74     1560   1866   1820    174   -119    -83       C  
ATOM   1246  CG  HIS A  74      67.209  82.868  35.511  1.00 13.20           C  
ANISOU 1246  CG  HIS A  74     1535   1834   1644    -40     59   -164       C  
ATOM   1247  ND1 HIS A  74      67.921  82.847  36.690  1.00 13.13           N  
ANISOU 1247  ND1 HIS A  74     1515   1859   1616      6   -341   -375       N  
ATOM   1248  CD2 HIS A  74      67.766  83.836  34.745  1.00 14.06           C  
ANISOU 1248  CD2 HIS A  74     1898   1781   1664    152    104    -90       C  
ATOM   1249  CE1 HIS A  74      68.865  83.772  36.644  1.00 13.16           C  
ANISOU 1249  CE1 HIS A  74     1501   1879   1621     -1   -158   -220       C  
ATOM   1250  NE2 HIS A  74      68.795  84.385  35.468  1.00 13.60           N  
ANISOU 1250  NE2 HIS A  74     1796   1647   1724     16     86   -173       N  
ATOM   1251  H   HIS A  74      64.373  80.342  35.314  1.00 15.29           H  
ATOM   1252  HA  HIS A  74      65.153  82.210  37.029  1.00 15.73           H  
ATOM   1253  HB2 HIS A  74      66.466  81.013  35.352  1.00 16.58           H  
ATOM   1254  HB3 HIS A  74      65.846  82.032  34.302  1.00 16.58           H  
ATOM   1255  HD2 HIS A  74      67.501  84.083  33.888  1.00 16.88           H  
ATOM   1256  HE1 HIS A  74      69.474  83.961  37.321  1.00 15.80           H  
ATOM   1257  HE2 HIS A  74      69.310  85.021  35.204  1.00 16.33           H  
ATOM   1258  N   TYR A  75      63.414  83.198  34.535  1.00 13.34           N  
ANISOU 1258  N   TYR A  75     1725   1852   1492    267   -107     33       N  
ATOM   1259  CA  TYR A  75      62.670  84.336  34.002  1.00 13.67           C  
ANISOU 1259  CA  TYR A  75     1877   1749   1570    345   -153     11       C  
ATOM   1260  C   TYR A  75      61.441  84.643  34.851  1.00 13.50           C  
ANISOU 1260  C   TYR A  75     1904   1694   1533    404    -93     88       C  
ATOM   1261  O   TYR A  75      61.154  85.814  35.151  1.00 13.86           O  
ANISOU 1261  O   TYR A  75     1910   1545   1812    401     36    176       O  
ATOM   1262  CB  TYR A  75      62.273  84.035  32.557  1.00 15.14           C  
ANISOU 1262  CB  TYR A  75     2182   1981   1589    308   -340     70       C  
ATOM   1263  CG  TYR A  75      61.554  85.174  31.879  1.00 17.08           C  
ANISOU 1263  CG  TYR A  75     2553   2199   1737    467   -222    332       C  
ATOM   1264  CD1 TYR A  75      60.174  85.280  31.944  1.00 17.99           C  
ANISOU 1264  CD1 TYR A  75     2652   2388   1796    514     80    386       C  
ATOM   1265  CD2 TYR A  75      62.254  86.153  31.186  1.00 18.76           C  
ANISOU 1265  CD2 TYR A  75     2802   2290   2037    483   -215    532       C  
ATOM   1266  CE1 TYR A  75      59.515  86.330  31.360  1.00 20.21           C  
ANISOU 1266  CE1 TYR A  75     2927   2515   2236    638     65    475       C  
ATOM   1267  CE2 TYR A  75      61.592  87.209  30.581  1.00 21.13           C  
ANISOU 1267  CE2 TYR A  75     3190   2443   2396    475   -222    841       C  
ATOM   1268  CZ  TYR A  75      60.222  87.287  30.676  1.00 22.19           C  
ANISOU 1268  CZ  TYR A  75     3401   2473   2558    711   -186    787       C  
ATOM   1269  OH  TYR A  75      59.557  88.335  30.084  1.00 25.89           O  
ANISOU 1269  OH  TYR A  75     3953   2787   3096    948   -118    876       O  
ATOM   1270  H   TYR A  75      63.390  82.499  34.034  1.00 16.02           H  
ATOM   1271  HA  TYR A  75      63.233  85.126  34.011  1.00 16.42           H  
ATOM   1272  HB2 TYR A  75      63.076  83.845  32.046  1.00 18.17           H  
ATOM   1273  HB3 TYR A  75      61.684  83.265  32.548  1.00 18.17           H  
ATOM   1274  HD1 TYR A  75      59.687  84.627  32.392  1.00 21.60           H  
ATOM   1275  HD2 TYR A  75      63.180  86.098  31.126  1.00 22.52           H  
ATOM   1276  HE1 TYR A  75      58.589  86.393  31.427  1.00 24.26           H  
ATOM   1277  HE2 TYR A  75      62.068  87.858  30.115  1.00 25.36           H  
ATOM   1278  HH  TYR A  75      60.106  88.848  29.708  1.00 31.07           H  
ATOM   1279  N   TYR A  76      60.690  83.613  35.241  1.00 13.58           N  
ANISOU 1279  N   TYR A  76     1832   1683   1644    140   -168    -81       N  
ATOM   1280  CA  TYR A  76      59.481  83.842  36.024  1.00 13.08           C  
ANISOU 1280  CA  TYR A  76     1809   1601   1558    166   -135   -133       C  
ATOM   1281  C   TYR A  76      59.786  84.246  37.463  1.00 12.42           C  
ANISOU 1281  C   TYR A  76     1680   1569   1471    386   -283    117       C  
ATOM   1282  O   TYR A  76      58.975  84.939  38.081  1.00 13.77           O  
ANISOU 1282  O   TYR A  76     1773   1664   1795    238   -143    -76       O  
ATOM   1283  CB  TYR A  76      58.540  82.641  35.962  1.00 12.82           C  
ANISOU 1283  CB  TYR A  76     1779   1615   1478    245   -259    -42       C  
ATOM   1284  CG  TYR A  76      57.940  82.393  34.580  1.00 13.02           C  
ANISOU 1284  CG  TYR A  76     1624   1828   1494    328   -235    -18       C  
ATOM   1285  CD1 TYR A  76      57.561  83.446  33.758  1.00 14.88           C  
ANISOU 1285  CD1 TYR A  76     1902   1975   1778    399   -172     48       C  
ATOM   1286  CD2 TYR A  76      57.738  81.104  34.114  1.00 13.56           C  
ANISOU 1286  CD2 TYR A  76     1505   2024   1624    117   -315    -43       C  
ATOM   1287  CE1 TYR A  76      57.005  83.220  32.514  1.00 15.94           C  
ANISOU 1287  CE1 TYR A  76     2002   2117   1937    389   -124    145       C  
ATOM   1288  CE2 TYR A  76      57.190  80.872  32.866  1.00 14.99           C  
ANISOU 1288  CE2 TYR A  76     1780   2175   1741    146   -276   -190       C  
ATOM   1289  CZ  TYR A  76      56.827  81.945  32.068  1.00 15.75           C  
ANISOU 1289  CZ  TYR A  76     1956   2227   1802    122   -238   -173       C  
ATOM   1290  OH  TYR A  76      56.286  81.733  30.815  1.00 16.61           O  
ANISOU 1290  OH  TYR A  76     2242   2224   1847    206   -307   -315       O  
ATOM   1291  H   TYR A  76      60.855  82.786  35.068  1.00 16.30           H  
ATOM   1292  HA  TYR A  76      59.003  84.583  35.620  1.00 15.70           H  
ATOM   1293  HB2 TYR A  76      59.034  81.845  36.216  1.00 15.39           H  
ATOM   1294  HB3 TYR A  76      57.807  82.787  36.580  1.00 15.39           H  
ATOM   1295  HD1 TYR A  76      57.683  84.320  34.051  1.00 17.87           H  
ATOM   1296  HD2 TYR A  76      57.976  80.382  34.650  1.00 16.28           H  
ATOM   1297  HE1 TYR A  76      56.753  83.939  31.980  1.00 19.13           H  
ATOM   1298  HE2 TYR A  76      57.066  80.001  32.564  1.00 18.00           H  
ATOM   1299  HH  TYR A  76      56.250  80.909  30.653  1.00 19.95           H  
ATOM   1300  N   ALA A  77      60.942  83.843  38.021  1.00 12.06           N  
ANISOU 1300  N   ALA A  77     1765   1505   1313    230   -299    -32       N  
ATOM   1301  CA  ALA A  77      61.359  84.447  39.289  1.00 13.17           C  
ANISOU 1301  CA  ALA A  77     1826   1684   1494    270    -76     25       C  
ATOM   1302  C   ALA A  77      61.550  85.946  39.109  1.00 13.31           C  
ANISOU 1302  C   ALA A  77     1773   1680   1605    183   -113    -44       C  
ATOM   1303  O   ALA A  77      61.167  86.741  39.978  1.00 13.40           O  
ANISOU 1303  O   ALA A  77     1770   1700   1623    275    -41    -40       O  
ATOM   1304  CB  ALA A  77      62.638  83.794  39.816  1.00 13.31           C  
ANISOU 1304  CB  ALA A  77     1876   1702   1479    186    -68   -107       C  
ATOM   1305  H   ALA A  77      61.476  83.250  37.700  1.00 14.48           H  
ATOM   1306  HA  ALA A  77      60.674  84.291  39.958  1.00 15.81           H  
ATOM   1307  HB1 ALA A  77      62.891  84.222  40.648  1.00 15.98           H  
ATOM   1308  HB2 ALA A  77      62.471  82.850  39.967  1.00 15.98           H  
ATOM   1309  HB3 ALA A  77      63.343  83.905  39.159  1.00 15.98           H  
ATOM   1310  N   GLY A  78      62.122  86.350  37.972  1.00 12.91           N  
ANISOU 1310  N   GLY A  78     1753   1494   1656    108     93     31       N  
ATOM   1311  CA  GLY A  78      62.282  87.769  37.692  1.00 12.98           C  
ANISOU 1311  CA  GLY A  78     1634   1532   1765     62    245      2       C  
ATOM   1312  C   GLY A  78      60.963  88.505  37.564  1.00 13.35           C  
ANISOU 1312  C   GLY A  78     1710   1607   1754     73    307    117       C  
ATOM   1313  O   GLY A  78      60.818  89.620  38.070  1.00 13.66           O  
ANISOU 1313  O   GLY A  78     1704   1622   1864    120     59     68       O  
ATOM   1314  H   GLY A  78      62.421  85.830  37.355  1.00 15.50           H  
ATOM   1315  HA2 GLY A  78      62.789  88.180  38.411  1.00 15.58           H  
ATOM   1316  HA3 GLY A  78      62.770  87.877  36.861  1.00 15.58           H  
ATOM   1317  N   VAL A  79      59.981  87.895  36.886  1.00 13.27           N  
ANISOU 1317  N   VAL A  79     1672   1626   1745    166    -17    -17       N  
ATOM   1318  CA  VAL A  79      58.674  88.536  36.774  1.00 13.71           C  
ANISOU 1318  CA  VAL A  79     1631   1850   1727    204   -167     29       C  
ATOM   1319  C   VAL A  79      58.041  88.690  38.149  1.00 13.93           C  
ANISOU 1319  C   VAL A  79     1691   1831   1772    132    -83     33       C  
ATOM   1320  O   VAL A  79      57.425  89.721  38.462  1.00 13.74           O  
ANISOU 1320  O   VAL A  79     1833   1535   1853    136     -1    148       O  
ATOM   1321  CB  VAL A  79      57.742  87.770  35.825  1.00 14.83           C  
ANISOU 1321  CB  VAL A  79     1936   1960   1738    286   -239    109       C  
ATOM   1322  CG1 VAL A  79      56.381  88.473  35.775  1.00 15.60           C  
ANISOU 1322  CG1 VAL A  79     2057   1924   1947    102   -306    -36       C  
ATOM   1323  CG2 VAL A  79      58.335  87.679  34.423  1.00 16.26           C  
ANISOU 1323  CG2 VAL A  79     2047   2446   1686    392    -64    -19       C  
ATOM   1324  H   VAL A  79      60.047  87.133  36.494  1.00 15.94           H  
ATOM   1325  HA  VAL A  79      58.816  89.416  36.391  1.00 16.46           H  
ATOM   1326  HB  VAL A  79      57.630  86.865  36.157  1.00 17.80           H  
ATOM   1327 HG11 VAL A  79      56.023  88.403  34.876  1.00 18.73           H  
ATOM   1328 HG12 VAL A  79      55.780  88.043  36.404  1.00 18.73           H  
ATOM   1329 HG13 VAL A  79      56.498  89.406  36.013  1.00 18.73           H  
ATOM   1330 HG21 VAL A  79      57.722  87.190  33.853  1.00 19.52           H  
ATOM   1331 HG22 VAL A  79      58.465  88.576  34.077  1.00 19.52           H  
ATOM   1332 HG23 VAL A  79      59.185  87.215  34.470  1.00 19.52           H  
ATOM   1333  N   THR A  80      58.140  87.647  38.983  1.00 13.50           N  
ANISOU 1333  N   THR A  80     1814   1770   1545    152   -217    -58       N  
ATOM   1334  CA  THR A  80      57.547  87.695  40.308  1.00 12.97           C  
ANISOU 1334  CA  THR A  80     1753   1651   1523     41    -26    -42       C  
ATOM   1335  C   THR A  80      58.194  88.789  41.141  1.00 11.63           C  
ANISOU 1335  C   THR A  80     1555   1338   1527     32    139     -7       C  
ATOM   1336  O   THR A  80      57.501  89.531  41.847  1.00 12.71           O  
ANISOU 1336  O   THR A  80     1688   1615   1527    147    112     17       O  
ATOM   1337  CB  THR A  80      57.667  86.328  40.986  1.00 12.96           C  
ANISOU 1337  CB  THR A  80     1631   1823   1470    -89   -120    -67       C  
ATOM   1338  OG1 THR A  80      56.996  85.332  40.190  1.00 13.62           O  
ANISOU 1338  OG1 THR A  80     1708   1897   1572     13   -104   -169       O  
ATOM   1339  CG2 THR A  80      57.016  86.341  42.355  1.00 12.90           C  
ANISOU 1339  CG2 THR A  80     1833   1686   1382    107    -88     -4       C  
ATOM   1340  H   THR A  80      58.543  86.909  38.803  1.00 16.21           H  
ATOM   1341  HA  THR A  80      56.600  87.895  40.235  1.00 15.57           H  
ATOM   1342  HB  THR A  80      58.608  86.112  41.083  1.00 15.56           H  
ATOM   1343  HG1 THR A  80      57.340  85.297  39.424  1.00 16.35           H  
ATOM   1344 HG21 THR A  80      56.970  85.439  42.709  1.00 15.49           H  
ATOM   1345 HG22 THR A  80      57.533  86.892  42.963  1.00 15.49           H  
ATOM   1346 HG23 THR A  80      56.117  86.701  42.291  1.00 15.49           H  
ATOM   1347  N   TYR A  81      59.520  88.899  41.067  1.00 12.13           N  
ANISOU 1347  N   TYR A  81     1573   1328   1707    -34     84   -110       N  
ATOM   1348  CA  TYR A  81      60.232  89.983  41.724  1.00 12.83           C  
ANISOU 1348  CA  TYR A  81     1620   1479   1775   -190    200    -24       C  
ATOM   1349  C   TYR A  81      59.716  91.332  41.240  1.00 12.96           C  
ANISOU 1349  C   TYR A  81     1652   1526   1746      8     17   -115       C  
ATOM   1350  O   TYR A  81      59.441  92.227  42.049  1.00 13.14           O  
ANISOU 1350  O   TYR A  81     1753   1502   1736    -23     82    -90       O  
ATOM   1351  CB  TYR A  81      61.740  89.835  41.463  1.00 12.77           C  
ANISOU 1351  CB  TYR A  81     1606   1480   1768    -98    236     86       C  
ATOM   1352  CG  TYR A  81      62.551  90.921  42.115  1.00 13.19           C  
ANISOU 1352  CG  TYR A  81     1655   1556   1802   -114     71    -87       C  
ATOM   1353  CD1 TYR A  81      62.650  92.180  41.535  1.00 13.08           C  
ANISOU 1353  CD1 TYR A  81     1561   1678   1733   -241    -30     48       C  
ATOM   1354  CD2 TYR A  81      63.195  90.709  43.337  1.00 13.56           C  
ANISOU 1354  CD2 TYR A  81     1625   1576   1952      8     22   -286       C  
ATOM   1355  CE1 TYR A  81      63.355  93.189  42.146  1.00 13.54           C  
ANISOU 1355  CE1 TYR A  81     1640   1629   1873   -235     94    -54       C  
ATOM   1356  CE2 TYR A  81      63.908  91.727  43.957  1.00 14.05           C  
ANISOU 1356  CE2 TYR A  81     1653   1628   2058   -184    -98   -158       C  
ATOM   1357  CZ  TYR A  81      63.969  92.969  43.349  1.00 14.80           C  
ANISOU 1357  CZ  TYR A  81     1765   1688   2170   -403     12   -122       C  
ATOM   1358  OH  TYR A  81      64.657  94.009  43.932  1.00 16.05           O  
ANISOU 1358  OH  TYR A  81     2098   1681   2320   -353    113   -177       O  
ATOM   1359  H   TYR A  81      60.032  88.356  40.639  1.00 14.56           H  
ATOM   1360  HA  TYR A  81      60.090  89.938  42.682  1.00 15.40           H  
ATOM   1361  HB2 TYR A  81      62.040  88.983  41.816  1.00 15.34           H  
ATOM   1362  HB3 TYR A  81      61.901  89.873  40.507  1.00 15.34           H  
ATOM   1363  HD1 TYR A  81      62.232  92.342  40.720  1.00 15.71           H  
ATOM   1364  HD2 TYR A  81      63.144  89.873  43.742  1.00 16.28           H  
ATOM   1365  HE1 TYR A  81      63.415  94.023  41.741  1.00 16.25           H  
ATOM   1366  HE2 TYR A  81      64.337  91.577  44.768  1.00 16.87           H  
ATOM   1367  HH  TYR A  81      64.967  93.769  44.675  1.00 19.27           H  
ATOM   1368  N   ASP A  82      59.579  91.494  39.921  1.00 13.27           N  
ANISOU 1368  N   ASP A  82     1648   1582   1813    121     13     -7       N  
ATOM   1369  CA  ASP A  82      59.125  92.762  39.365  1.00 14.31           C  
ANISOU 1369  CA  ASP A  82     1704   1691   2043    146    100    103       C  
ATOM   1370  C   ASP A  82      57.711  93.089  39.836  1.00 14.37           C  
ANISOU 1370  C   ASP A  82     1785   1650   2023    152    300     -2       C  
ATOM   1371  O   ASP A  82      57.406  94.245  40.150  1.00 14.60           O  
ANISOU 1371  O   ASP A  82     1729   1623   2196    203    260    119       O  
ATOM   1372  CB  ASP A  82      59.146  92.713  37.837  1.00 14.50           C  
ANISOU 1372  CB  ASP A  82     1560   1896   2052    152    247     90       C  
ATOM   1373  CG  ASP A  82      60.546  92.737  37.247  1.00 15.63           C  
ANISOU 1373  CG  ASP A  82     1871   1944   2123    182    334    212       C  
ATOM   1374  OD1 ASP A  82      61.515  92.921  38.019  1.00 16.05           O  
ANISOU 1374  OD1 ASP A  82     1817   1953   2327     74    336     88       O  
ATOM   1375  OD2 ASP A  82      60.657  92.584  35.995  1.00 17.84           O  
ANISOU 1375  OD2 ASP A  82     2283   2292   2205    352    492    322       O  
ATOM   1376  H   ASP A  82      59.741  90.889  39.331  1.00 15.94           H  
ATOM   1377  HA  ASP A  82      59.732  93.458  39.662  1.00 17.18           H  
ATOM   1378  HB2 ASP A  82      58.714  91.896  37.544  1.00 17.40           H  
ATOM   1379  HB3 ASP A  82      58.666  93.483  37.493  1.00 17.40           H  
ATOM   1380  N   TYR A  83      56.826  92.083  39.886  1.00 14.16           N  
ANISOU 1380  N   TYR A  83     1870   1650   1862    139    241     27       N  
ATOM   1381  CA  TYR A  83      55.462  92.316  40.351  1.00 13.49           C  
ANISOU 1381  CA  TYR A  83     1946   1516   1663    220     21     66       C  
ATOM   1382  C   TYR A  83      55.468  92.853  41.777  1.00 13.11           C  
ANISOU 1382  C   TYR A  83     1751   1471   1759    179     29     20       C  
ATOM   1383  O   TYR A  83      54.891  93.907  42.071  1.00 13.28           O  
ANISOU 1383  O   TYR A  83     1789   1500   1756    130     66    100       O  
ATOM   1384  CB  TYR A  83      54.656  91.006  40.287  1.00 13.35           C  
ANISOU 1384  CB  TYR A  83     1746   1671   1655    197    -28     35       C  
ATOM   1385  CG  TYR A  83      53.317  91.146  40.979  1.00 11.82           C  
ANISOU 1385  CG  TYR A  83     1386   1538   1565    250    -17    199       C  
ATOM   1386  CD1 TYR A  83      52.238  91.736  40.335  1.00 12.63           C  
ANISOU 1386  CD1 TYR A  83     1533   1664   1602    376    -71    294       C  
ATOM   1387  CD2 TYR A  83      53.120  90.694  42.280  1.00 12.93           C  
ANISOU 1387  CD2 TYR A  83     1594   1592   1726    369   -129     39       C  
ATOM   1388  CE1 TYR A  83      51.019  91.884  40.959  1.00 13.42           C  
ANISOU 1388  CE1 TYR A  83     1657   1670   1774    175    -40    370       C  
ATOM   1389  CE2 TYR A  83      51.905  90.840  42.914  1.00 12.85           C  
ANISOU 1389  CE2 TYR A  83     1620   1418   1845    333    -20    111       C  
ATOM   1390  CZ  TYR A  83      50.847  91.433  42.248  1.00 13.04           C  
ANISOU 1390  CZ  TYR A  83     1605   1505   1844    280     84    263       C  
ATOM   1391  OH  TYR A  83      49.619  91.597  42.873  1.00 14.01           O  
ANISOU 1391  OH  TYR A  83     1645   1713   1966    201    311     80       O  
ATOM   1392  H   TYR A  83      56.990  91.270  39.660  1.00 17.01           H  
ATOM   1393  HA  TYR A  83      55.037  92.967  39.771  1.00 16.19           H  
ATOM   1394  HB2 TYR A  83      54.498  90.772  39.359  1.00 16.03           H  
ATOM   1395  HB3 TYR A  83      55.156  90.300  40.727  1.00 16.03           H  
ATOM   1396  HD1 TYR A  83      52.340  92.037  39.461  1.00 15.16           H  
ATOM   1397  HD2 TYR A  83      53.823  90.285  42.731  1.00 15.52           H  
ATOM   1398  HE1 TYR A  83      50.312  92.289  40.510  1.00 16.12           H  
ATOM   1399  HE2 TYR A  83      51.796  90.539  43.788  1.00 15.43           H  
ATOM   1400  HH  TYR A  83      49.655  91.302  43.659  1.00 16.82           H  
ATOM   1401  N   TYR A  84      56.144  92.149  42.682  1.00 13.17           N  
ANISOU 1401  N   TYR A  84     1509   1584   1910   -144    -29    100       N  
ATOM   1402  CA  TYR A  84      56.124  92.579  44.077  1.00 13.47           C  
ANISOU 1402  CA  TYR A  84     1679   1537   1902    -10    -19      1       C  
ATOM   1403  C   TYR A  84      56.769  93.943  44.249  1.00 13.38           C  
ANISOU 1403  C   TYR A  84     1619   1557   1908   -141    172     41       C  
ATOM   1404  O   TYR A  84      56.278  94.759  45.032  1.00 14.70           O  
ANISOU 1404  O   TYR A  84     1894   1653   2038    -81    333    -24       O  
ATOM   1405  CB  TYR A  84      56.734  91.517  44.982  1.00 12.32           C  
ANISOU 1405  CB  TYR A  84     1788   1374   1519    -27     61    -97       C  
ATOM   1406  CG  TYR A  84      55.723  90.450  45.350  1.00 11.74           C  
ANISOU 1406  CG  TYR A  84     1568   1379   1514   -160     60   -148       C  
ATOM   1407  CD1 TYR A  84      54.680  90.732  46.219  1.00 12.63           C  
ANISOU 1407  CD1 TYR A  84     1618   1429   1754   -268    116   -247       C  
ATOM   1408  CD2 TYR A  84      55.788  89.173  44.828  1.00 12.80           C  
ANISOU 1408  CD2 TYR A  84     1648   1492   1723    -43     66    -77       C  
ATOM   1409  CE1 TYR A  84      53.734  89.773  46.553  1.00 12.72           C  
ANISOU 1409  CE1 TYR A  84     1649   1340   1846   -191    -49   -187       C  
ATOM   1410  CE2 TYR A  84      54.846  88.190  45.176  1.00 12.19           C  
ANISOU 1410  CE2 TYR A  84     1587   1337   1710    -41     27   -212       C  
ATOM   1411  CZ  TYR A  84      53.820  88.512  46.034  1.00 12.40           C  
ANISOU 1411  CZ  TYR A  84     1552   1418   1741   -223     14   -119       C  
ATOM   1412  OH  TYR A  84      52.860  87.630  46.438  1.00 12.57           O  
ANISOU 1412  OH  TYR A  84     1742   1382   1652   -126     42   -211       O  
ATOM   1413  H   TYR A  84      56.606  91.442  42.523  1.00 15.81           H  
ATOM   1414  HA  TYR A  84      55.202  92.673  44.364  1.00 16.17           H  
ATOM   1415  HB2 TYR A  84      57.474  91.091  44.522  1.00 14.79           H  
ATOM   1416  HB3 TYR A  84      57.048  91.935  45.800  1.00 14.79           H  
ATOM   1417  HD1 TYR A  84      54.612  91.583  46.587  1.00 15.17           H  
ATOM   1418  HD2 TYR A  84      56.470  88.958  44.233  1.00 15.36           H  
ATOM   1419  HE1 TYR A  84      53.039  89.989  47.131  1.00 15.28           H  
ATOM   1420  HE2 TYR A  84      54.915  87.330  44.830  1.00 14.64           H  
ATOM   1421  HH  TYR A  84      52.986  86.883  46.075  1.00 15.09           H  
ATOM   1422  N   LYS A  85      57.862  94.221  43.528  1.00 13.40           N  
ANISOU 1422  N   LYS A  85     1670   1494   1927   -302    351    -17       N  
ATOM   1423  CA  LYS A  85      58.525  95.516  43.669  1.00 14.87           C  
ANISOU 1423  CA  LYS A  85     1853   1542   2256   -255    347    -46       C  
ATOM   1424  C   LYS A  85      57.691  96.639  43.058  1.00 15.31           C  
ANISOU 1424  C   LYS A  85     1964   1494   2360   -100    372   -105       C  
ATOM   1425  O   LYS A  85      57.443  97.675  43.700  1.00 16.58           O  
ANISOU 1425  O   LYS A  85     2190   1612   2497    -56    291    -99       O  
ATOM   1426  CB  LYS A  85      59.909  95.470  43.016  1.00 15.97           C  
ANISOU 1426  CB  LYS A  85     2061   1580   2429   -348    489   -126       C  
ATOM   1427  CG  LYS A  85      60.627  96.819  43.023  1.00 18.39           C  
ANISOU 1427  CG  LYS A  85     2313   1746   2929   -425    543   -265       C  
ATOM   1428  CD  LYS A  85      62.084  96.644  42.609  1.00 21.82           C  
ANISOU 1428  CD  LYS A  85     2820   2050   3421   -671    580   -291       C  
ATOM   1429  CE  LYS A  85      62.851  97.941  42.688  1.00 26.18           C  
ANISOU 1429  CE  LYS A  85     3560   2515   3874   -457    570    -40       C  
ATOM   1430  NZ  LYS A  85      62.505  98.826  41.558  1.00 29.28           N  
ANISOU 1430  NZ  LYS A  85     4035   2846   4246   -519    457    190       N  
ATOM   1431  H   LYS A  85      58.231  93.688  42.963  1.00 16.09           H  
ATOM   1432  HA  LYS A  85      58.637  95.703  44.614  1.00 17.86           H  
ATOM   1433  HB2 LYS A  85      60.462  94.835  43.499  1.00 19.18           H  
ATOM   1434  HB3 LYS A  85      59.811  95.189  42.093  1.00 19.18           H  
ATOM   1435  HG2 LYS A  85      60.196  97.421  42.396  1.00 22.08           H  
ATOM   1436  HG3 LYS A  85      60.602  97.197  43.916  1.00 22.08           H  
ATOM   1437  HD2 LYS A  85      62.510  96.004  43.200  1.00 26.19           H  
ATOM   1438  HD3 LYS A  85      62.121  96.326  41.693  1.00 26.19           H  
ATOM   1439  HE2 LYS A  85      62.630  98.398  43.515  1.00 31.43           H  
ATOM   1440  HE3 LYS A  85      63.803  97.757  42.654  1.00 31.43           H  
ATOM   1441  HZ1 LYS A  85      62.947  99.595  41.627  1.00 35.15           H  
ATOM   1442  HZ2 LYS A  85      62.723  98.436  40.788  1.00 35.15           H  
ATOM   1443  HZ3 LYS A  85      61.631  98.993  41.559  1.00 35.15           H  
ATOM   1444  N   ASN A  86      57.259  96.459  41.810  1.00 15.45           N  
ANISOU 1444  N   ASN A  86     1954   1440   2476   -104    340    119       N  
ATOM   1445  CA  ASN A  86      56.599  97.547  41.096  1.00 15.49           C  
ANISOU 1445  CA  ASN A  86     1999   1426   2462     15    366    332       C  
ATOM   1446  C   ASN A  86      55.175  97.784  41.585  1.00 15.74           C  
ANISOU 1446  C   ASN A  86     1896   1478   2605    208    408    353       C  
ATOM   1447  O   ASN A  86      54.707  98.927  41.620  1.00 18.07           O  
ANISOU 1447  O   ASN A  86     2169   1647   3047     17    490    444       O  
ATOM   1448  CB  ASN A  86      56.586  97.266  39.599  1.00 16.76           C  
ANISOU 1448  CB  ASN A  86     2094   1709   2564    -35    700    157       C  
ATOM   1449  CG  ASN A  86      57.977  97.265  39.003  1.00 19.12           C  
ANISOU 1449  CG  ASN A  86     2490   2042   2734   -337    796    187       C  
ATOM   1450  OD1 ASN A  86      58.899  97.904  39.517  1.00 22.09           O  
ANISOU 1450  OD1 ASN A  86     2731   2607   3055   -561    699    -68       O  
ATOM   1451  ND2 ASN A  86      58.136  96.556  37.909  1.00 20.68           N  
ANISOU 1451  ND2 ASN A  86     2788   2257   2812     86    724    123       N  
ATOM   1452  H   ASN A  86      57.334  95.730  41.360  1.00 18.55           H  
ATOM   1453  HA  ASN A  86      57.110  98.355  41.260  1.00 18.60           H  
ATOM   1454  HB2 ASN A  86      56.190  96.395  39.442  1.00 20.12           H  
ATOM   1455  HB3 ASN A  86      56.067  97.953  39.151  1.00 20.12           H  
ATOM   1456 HD21 ASN A  86      58.906  96.520  37.528  1.00 24.82           H  
ATOM   1457 HD22 ASN A  86      57.470  96.127  37.573  1.00 24.82           H  
ATOM   1458  N   VAL A  87      54.458  96.721  41.946  1.00 15.83           N  
ANISOU 1458  N   VAL A  87     1796   1655   2565    163    422    201       N  
ATOM   1459  CA  VAL A  87      53.062  96.858  42.339  1.00 15.54           C  
ANISOU 1459  CA  VAL A  87     1960   1656   2287    130    600    162       C  
ATOM   1460  C   VAL A  87      52.915  97.121  43.832  1.00 15.79           C  
ANISOU 1460  C   VAL A  87     2133   1700   2167    445    398    176       C  
ATOM   1461  O   VAL A  87      52.074  97.939  44.232  1.00 17.28           O  
ANISOU 1461  O   VAL A  87     2352   1877   2336    257    419    141       O  
ATOM   1462  CB  VAL A  87      52.264  95.612  41.897  1.00 16.06           C  
ANISOU 1462  CB  VAL A  87     1965   1782   2353    -55    570    376       C  
ATOM   1463  CG1 VAL A  87      50.811  95.727  42.334  1.00 16.92           C  
ANISOU 1463  CG1 VAL A  87     1993   2137   2301    -66    636    220       C  
ATOM   1464  CG2 VAL A  87      52.368  95.397  40.384  1.00 16.61           C  
ANISOU 1464  CG2 VAL A  87     1954   1809   2547    127    395    563       C  
ATOM   1465  H   VAL A  87      54.756  95.915  41.972  1.00 19.01           H  
ATOM   1466  HA  VAL A  87      52.692  97.626  41.876  1.00 18.65           H  
ATOM   1467  HB  VAL A  87      52.647  94.831  42.327  1.00 19.28           H  
ATOM   1468 HG11 VAL A  87      50.295  95.029  41.902  1.00 20.32           H  
ATOM   1469 HG12 VAL A  87      50.762  95.627  43.297  1.00 20.32           H  
ATOM   1470 HG13 VAL A  87      50.472  96.598  42.075  1.00 20.32           H  
ATOM   1471 HG21 VAL A  87      51.809  94.645  40.133  1.00 19.94           H  
ATOM   1472 HG22 VAL A  87      52.066  96.200  39.930  1.00 19.94           H  
ATOM   1473 HG23 VAL A  87      53.292  95.214  40.153  1.00 19.94           H  
ATOM   1474  N   HIS A  88      53.729  96.457  44.674  1.00 14.58           N  
ANISOU 1474  N   HIS A  88     1986   1552   2003    324    206    165       N  
ATOM   1475  CA  HIS A  88      53.556  96.530  46.116  1.00 14.44           C  
ANISOU 1475  CA  HIS A  88     1973   1372   2142    185    266    226       C  
ATOM   1476  C   HIS A  88      54.726  97.147  46.862  1.00 15.50           C  
ANISOU 1476  C   HIS A  88     2139   1470   2280    167    238   -100       C  
ATOM   1477  O   HIS A  88      54.690  97.199  48.096  1.00 16.16           O  
ANISOU 1477  O   HIS A  88     2265   1790   2086    -99    337   -207       O  
ATOM   1478  CB  HIS A  88      53.269  95.136  46.694  1.00 14.21           C  
ANISOU 1478  CB  HIS A  88     1864   1377   2157    194    185    136       C  
ATOM   1479  CG  HIS A  88      52.048  94.502  46.113  1.00 14.58           C  
ANISOU 1479  CG  HIS A  88     1780   1625   2133    222    301    159       C  
ATOM   1480  ND1 HIS A  88      50.787  95.019  46.303  1.00 15.58           N  
ANISOU 1480  ND1 HIS A  88     1846   1832   2242    243    435     89       N  
ATOM   1481  CD2 HIS A  88      51.899  93.429  45.301  1.00 14.48           C  
ANISOU 1481  CD2 HIS A  88     1708   1760   2035    231    382      8       C  
ATOM   1482  CE1 HIS A  88      49.909  94.273  45.656  1.00 15.93           C  
ANISOU 1482  CE1 HIS A  88     1774   2078   2200     56    487     26       C  
ATOM   1483  NE2 HIS A  88      50.561  93.300  45.038  1.00 15.24           N  
ANISOU 1483  NE2 HIS A  88     1718   2004   2069    315    692    125       N  
ATOM   1484  H   HIS A  88      54.386  95.962  44.423  1.00 17.51           H  
ATOM   1485  HA  HIS A  88      52.785  97.094  46.284  1.00 17.34           H  
ATOM   1486  HB2 HIS A  88      54.024  94.556  46.508  1.00 17.06           H  
ATOM   1487  HB3 HIS A  88      53.138  95.213  47.652  1.00 17.06           H  
ATOM   1488  HD1 HIS A  88      50.600  95.717  46.769  1.00 18.71           H  
ATOM   1489  HD2 HIS A  88      52.579  92.881  44.981  1.00 17.39           H  
ATOM   1490  HE1 HIS A  88      48.989  94.408  45.637  1.00 19.12           H  
ATOM   1491  N   ASN A  89      55.749  97.622  46.154  1.00 15.41           N  
ANISOU 1491  N   ASN A  89     1964   1300   2592     40    332    -96       N  
ATOM   1492  CA AASN A  89      56.939  98.194  46.786  0.57 16.17           C  
ANISOU 1492  CA AASN A  89     2172   1297   2674     63    324   -244       C  
ATOM   1493  CA BASN A  89      56.938  98.197  46.784  0.43 16.51           C  
ANISOU 1493  CA BASN A  89     2212   1347   2714    -96    335   -194       C  
ATOM   1494  C   ASN A  89      57.574  97.211  47.767  1.00 16.51           C  
ANISOU 1494  C   ASN A  89     2184   1537   2554   -127    392   -261       C  
ATOM   1495  O   ASN A  89      58.113  97.604  48.805  1.00 18.43           O  
ANISOU 1495  O   ASN A  89     2563   1798   2641   -261    223   -354       O  
ATOM   1496  CB AASN A  89      56.616  99.522  47.462  0.57 18.69           C  
ANISOU 1496  CB AASN A  89     2675   1425   3001    178    340   -296       C  
ATOM   1497  CB BASN A  89      56.645  99.536  47.463  0.43 19.16           C  
ANISOU 1497  CB BASN A  89     2721   1465   3095   -274    357   -168       C  
ATOM   1498  CG AASN A  89      56.018 100.511  46.503  0.57 21.95           C  
ANISOU 1498  CG AASN A  89     3124   1799   3415    355    439   -380       C  
ATOM   1499  CG BASN A  89      57.905 100.338  47.728  0.43 22.37           C  
ANISOU 1499  CG BASN A  89     3187   1760   3550   -441    443   -166       C  
ATOM   1500  OD1AASN A  89      56.567 100.754  45.430  0.57 23.03           O  
ANISOU 1500  OD1AASN A  89     3275   1975   3501    397    508   -434       O  
ATOM   1501  OD1BASN A  89      58.840 100.323  46.924  0.43 23.43           O  
ANISOU 1501  OD1BASN A  89     3279   1831   3791   -705    495   -168       O  
ATOM   1502  ND2AASN A  89      54.876 101.069  46.869  0.57 24.80           N  
ANISOU 1502  ND2AASN A  89     3442   2173   3808    510    503   -243       N  
ATOM   1503  ND2BASN A  89      57.945 101.029  48.864  0.43 24.32           N  
ANISOU 1503  ND2BASN A  89     3508   1990   3742   -587    442    -71       N  
ATOM   1504  H  AASN A  89      55.778  97.625  45.295  0.57 18.50           H  
ATOM   1505  H  BASN A  89      55.778  97.624  45.295  0.43 18.50           H  
ATOM   1506  HA AASN A  89      57.598  98.369  46.096  0.57 19.41           H  
ATOM   1507  HA BASN A  89      57.585  98.372  46.083  0.43 19.82           H  
ATOM   1508  HB2AASN A  89      55.979  99.370  48.177  0.57 22.43           H  
ATOM   1509  HB2BASN A  89      56.067 100.063  46.889  0.43 23.00           H  
ATOM   1510  HB3AASN A  89      57.433  99.904  47.821  0.57 22.43           H  
ATOM   1511  HB3BASN A  89      56.208  99.371  48.313  0.43 23.00           H  
ATOM   1512 HD21AASN A  89      54.493 101.642  46.354  0.57 29.77           H  
ATOM   1513 HD21BASN A  89      58.640 101.499  49.057  0.43 29.19           H  
ATOM   1514 HD22AASN A  89      54.516 100.860  47.621  0.57 29.77           H  
ATOM   1515 HD22BASN A  89      57.278 101.007  49.405  0.43 29.19           H  
ATOM   1516  N   ARG A  90      57.520  95.930  47.428  1.00 15.63           N  
ANISOU 1516  N   ARG A  90     2017   1523   2398    -81    510   -290       N  
ATOM   1517  CA  ARG A  90      58.135  94.874  48.225  1.00 14.62           C  
ANISOU 1517  CA  ARG A  90     1769   1621   2166    -27    270   -401       C  
ATOM   1518  C   ARG A  90      59.361  94.352  47.490  1.00 14.95           C  
ANISOU 1518  C   ARG A  90     1848   1735   2098    -47    174   -315       C  
ATOM   1519  O   ARG A  90      59.264  93.956  46.321  1.00 15.53           O  
ANISOU 1519  O   ARG A  90     2002   1868   2031     88    -34   -345       O  
ATOM   1520  CB  ARG A  90      57.156  93.732  48.492  1.00 15.41           C  
ANISOU 1520  CB  ARG A  90     1782   1785   2286    -59     37   -299       C  
ATOM   1521  CG  ARG A  90      57.724  92.661  49.395  1.00 14.95           C  
ANISOU 1521  CG  ARG A  90     1694   1850   2139   -182    142   -437       C  
ATOM   1522  CD  ARG A  90      56.792  91.439  49.509  1.00 15.03           C  
ANISOU 1522  CD  ARG A  90     1790   1756   2165    -78   -201   -622       C  
ATOM   1523  NE  ARG A  90      57.310  90.628  50.590  1.00 14.62           N  
ANISOU 1523  NE  ARG A  90     1831   1678   2047    215    -37   -393       N  
ATOM   1524  CZ  ARG A  90      57.079  90.874  51.875  1.00 14.48           C  
ANISOU 1524  CZ  ARG A  90     1989   1595   1917     75    -88   -344       C  
ATOM   1525  NH1 ARG A  90      56.238  91.849  52.215  1.00 14.86           N  
ANISOU 1525  NH1 ARG A  90     2058   1588   1999     64    -41   -191       N  
ATOM   1526  NH2 ARG A  90      57.655  90.119  52.810  1.00 14.49           N  
ANISOU 1526  NH2 ARG A  90     1873   1772   1861    -40     89   -148       N  
ATOM   1527  H   ARG A  90      57.121  95.641  46.723  1.00 18.76           H  
ATOM   1528  HA  ARG A  90      58.412  95.235  49.082  1.00 17.56           H  
ATOM   1529  HB2 ARG A  90      56.362  94.092  48.918  1.00 18.49           H  
ATOM   1530  HB3 ARG A  90      56.920  93.317  47.648  1.00 18.49           H  
ATOM   1531  HG2 ARG A  90      58.574  92.360  49.037  1.00 17.95           H  
ATOM   1532  HG3 ARG A  90      57.850  93.028  50.284  1.00 17.95           H  
ATOM   1533  HD2 ARG A  90      55.887  91.720  49.716  1.00 18.04           H  
ATOM   1534  HD3 ARG A  90      56.799  90.928  48.684  1.00 18.04           H  
ATOM   1535  HE  ARG A  90      57.795  89.947  50.388  1.00 17.56           H  
ATOM   1536 HH11 ARG A  90      55.850  92.314  51.605  1.00 17.84           H  
ATOM   1537 HH12 ARG A  90      56.084  92.014  53.045  1.00 17.84           H  
ATOM   1538 HH21 ARG A  90      58.175  89.474  52.581  1.00 17.40           H  
ATOM   1539 HH22 ARG A  90      57.506  90.277  53.642  1.00 17.40           H  
ATOM   1540  N   LEU A  91      60.507  94.358  48.171  1.00 14.75           N  
ANISOU 1540  N   LEU A  91     1653   1764   2187   -116    165   -278       N  
ATOM   1541  CA  LEU A  91      61.788  93.961  47.591  1.00 14.92           C  
ANISOU 1541  CA  LEU A  91     1629   1729   2309   -189    241   -355       C  
ATOM   1542  C   LEU A  91      62.059  92.492  47.917  1.00 14.47           C  
ANISOU 1542  C   LEU A  91     1647   1817   2032   -267    -16   -229       C  
ATOM   1543  O   LEU A  91      62.466  92.139  49.030  1.00 14.43           O  
ANISOU 1543  O   LEU A  91     1708   1792   1983   -241   -125   -284       O  
ATOM   1544  CB  LEU A  91      62.907  94.876  48.075  1.00 16.53           C  
ANISOU 1544  CB  LEU A  91     2044   1681   2557   -310    300   -380       C  
ATOM   1545  CG  LEU A  91      62.708  96.359  47.751  1.00 19.05           C  
ANISOU 1545  CG  LEU A  91     2435   1806   2998   -470    360   -338       C  
ATOM   1546  CD1 LEU A  91      63.839  97.194  48.318  1.00 19.85           C  
ANISOU 1546  CD1 LEU A  91     2479   1827   3238   -710    467   -270       C  
ATOM   1547  CD2 LEU A  91      62.609  96.568  46.258  1.00 20.15           C  
ANISOU 1547  CD2 LEU A  91     2655   1882   3118   -297    410   -214       C  
ATOM   1548  H   LEU A  91      60.567  94.595  48.995  1.00 17.71           H  
ATOM   1549  HA  LEU A  91      61.730  94.032  46.626  1.00 17.91           H  
ATOM   1550  HB2 LEU A  91      62.975  94.794  49.039  1.00 19.85           H  
ATOM   1551  HB3 LEU A  91      63.736  94.595  47.658  1.00 19.85           H  
ATOM   1552  HG  LEU A  91      61.879  96.655  48.160  1.00 22.87           H  
ATOM   1553 HD11 LEU A  91      63.675  98.128  48.114  1.00 23.83           H  
ATOM   1554 HD12 LEU A  91      63.875  97.066  49.279  1.00 23.83           H  
ATOM   1555 HD13 LEU A  91      64.674  96.908  47.915  1.00 23.83           H  
ATOM   1556 HD21 LEU A  91      62.701  97.514  46.064  1.00 24.19           H  
ATOM   1557 HD22 LEU A  91      63.318  96.071  45.821  1.00 24.19           H  
ATOM   1558 HD23 LEU A  91      61.745  96.250  45.951  1.00 24.19           H  
ATOM   1559  N   SER A  92      61.849  91.645  46.920  1.00 13.40           N  
ANISOU 1559  N   SER A  92     1743   1632   1718     10     -6   -411       N  
ATOM   1560  CA  SER A  92      61.940  90.195  47.045  1.00 13.51           C  
ANISOU 1560  CA  SER A  92     1774   1638   1721    167   -122   -282       C  
ATOM   1561  C   SER A  92      60.939  89.631  48.048  1.00 13.25           C  
ANISOU 1561  C   SER A  92     1654   1518   1862    120   -113   -319       C  
ATOM   1562  O   SER A  92      60.081  90.354  48.577  1.00 13.82           O  
ANISOU 1562  O   SER A  92     1681   1616   1955     39    140   -249       O  
ATOM   1563  CB  SER A  92      63.356  89.734  47.382  1.00 13.11           C  
ANISOU 1563  CB  SER A  92     1745   1586   1649     92    -75   -402       C  
ATOM   1564  OG  SER A  92      63.469  88.346  47.080  1.00 14.12           O  
ANISOU 1564  OG  SER A  92     1690   1693   1982     85    -54   -418       O  
ATOM   1565  H   SER A  92      61.643  91.894  46.123  1.00 16.09           H  
ATOM   1566  HA  SER A  92      61.715  89.826  46.177  1.00 16.22           H  
ATOM   1567  HB2 SER A  92      63.994  90.235  46.850  1.00 15.74           H  
ATOM   1568  HB3 SER A  92      63.527  89.875  48.326  1.00 15.74           H  
ATOM   1569  HG  SER A  92      64.259  88.088  47.206  1.00 16.95           H  
ATOM   1570  N   TYR A  93      61.017  88.321  48.289  1.00 13.86           N  
ANISOU 1570  N   TYR A  93     1741   1523   2004    -28    -44   -350       N  
ATOM   1571  CA  TYR A  93      59.973  87.676  49.072  1.00 14.39           C  
ANISOU 1571  CA  TYR A  93     1851   1545   2072   -140     82   -492       C  
ATOM   1572  C   TYR A  93      59.997  88.123  50.522  1.00 14.09           C  
ANISOU 1572  C   TYR A  93     1703   1673   1977   -400    241   -529       C  
ATOM   1573  O   TYR A  93      58.945  88.131  51.178  1.00 14.23           O  
ANISOU 1573  O   TYR A  93     1716   1836   1857   -283    284   -278       O  
ATOM   1574  CB  TYR A  93      60.056  86.152  48.961  1.00 14.98           C  
ANISOU 1574  CB  TYR A  93     1954   1509   2229     86    -10   -293       C  
ATOM   1575  CG  TYR A  93      61.383  85.557  49.349  1.00 15.09           C  
ANISOU 1575  CG  TYR A  93     1879   1649   2208     48   -147   -199       C  
ATOM   1576  CD1 TYR A  93      61.661  85.231  50.665  1.00 15.13           C  
ANISOU 1576  CD1 TYR A  93     1937   1668   2144     18   -185   -184       C  
ATOM   1577  CD2 TYR A  93      62.358  85.318  48.394  1.00 16.25           C  
ANISOU 1577  CD2 TYR A  93     1854   1858   2460     11   -158   -179       C  
ATOM   1578  CE1 TYR A  93      62.873  84.670  51.017  1.00 16.75           C  
ANISOU 1578  CE1 TYR A  93     1969   1871   2523     56   -345    -57       C  
ATOM   1579  CE2 TYR A  93      63.580  84.790  48.735  1.00 16.29           C  
ANISOU 1579  CE2 TYR A  93     1739   1745   2707     58   -242   -344       C  
ATOM   1580  CZ  TYR A  93      63.825  84.448  50.047  1.00 17.59           C  
ANISOU 1580  CZ  TYR A  93     1840   1878   2966    134   -453   -246       C  
ATOM   1581  OH  TYR A  93      65.033  83.892  50.379  1.00 21.21           O  
ANISOU 1581  OH  TYR A  93     2121   2361   3578    -31   -542   -213       O  
ATOM   1582  H   TYR A  93      61.645  87.800  48.017  1.00 16.65           H  
ATOM   1583  HA  TYR A  93      59.115  87.933  48.699  1.00 17.28           H  
ATOM   1584  HB2 TYR A  93      59.383  85.765  49.543  1.00 17.98           H  
ATOM   1585  HB3 TYR A  93      59.883  85.901  48.041  1.00 17.98           H  
ATOM   1586  HD1 TYR A  93      61.023  85.392  51.321  1.00 18.16           H  
ATOM   1587  HD2 TYR A  93      62.182  85.520  47.504  1.00 19.50           H  
ATOM   1588  HE1 TYR A  93      63.044  84.443  51.903  1.00 20.11           H  
ATOM   1589  HE2 TYR A  93      64.235  84.664  48.087  1.00 19.56           H  
ATOM   1590  HH  TYR A  93      65.515  83.822  49.695  1.00 25.46           H  
ATOM   1591  N   ASP A  94      61.170  88.488  51.039  1.00 14.07           N  
ANISOU 1591  N   ASP A  94     1687   1654   2006   -278    169   -483       N  
ATOM   1592  CA  ASP A  94      61.286  88.914  52.428  1.00 14.77           C  
ANISOU 1592  CA  ASP A  94     1777   1797   2040   -398     -3   -432       C  
ATOM   1593  C   ASP A  94      61.222  90.420  52.620  1.00 15.55           C  
ANISOU 1593  C   ASP A  94     1946   1910   2053   -321     88   -372       C  
ATOM   1594  O   ASP A  94      61.301  90.885  53.763  1.00 16.56           O  
ANISOU 1594  O   ASP A  94     2114   2016   2162   -315    206   -461       O  
ATOM   1595  CB  ASP A  94      62.546  88.334  53.086  1.00 15.46           C  
ANISOU 1595  CB  ASP A  94     1710   2074   2091   -305     -9   -260       C  
ATOM   1596  CG  ASP A  94      63.836  88.947  52.578  1.00 16.31           C  
ANISOU 1596  CG  ASP A  94     1994   2152   2050   -304   -198   -386       C  
ATOM   1597  OD1 ASP A  94      63.847  89.596  51.506  1.00 15.26           O  
ANISOU 1597  OD1 ASP A  94     1881   1987   1930   -216    -17   -251       O  
ATOM   1598  OD2 ASP A  94      64.860  88.769  53.296  1.00 17.61           O  
ANISOU 1598  OD2 ASP A  94     2217   2251   2223   -233   -319   -400       O  
ATOM   1599  H   ASP A  94      61.911  88.497  50.602  1.00 16.89           H  
ATOM   1600  HA  ASP A  94      60.529  88.543  52.907  1.00 17.74           H  
ATOM   1601  HB2 ASP A  94      62.499  88.491  54.042  1.00 18.56           H  
ATOM   1602  HB3 ASP A  94      62.581  87.381  52.907  1.00 18.56           H  
ATOM   1603  N   GLY A  95      61.035  91.187  51.552  1.00 14.79           N  
ANISOU 1603  N   GLY A  95     1857   1963   1798   -373    141   -391       N  
ATOM   1604  CA  GLY A  95      61.052  92.631  51.647  1.00 13.98           C  
ANISOU 1604  CA  GLY A  95     1554   1854   1906   -383     81   -453       C  
ATOM   1605  C   GLY A  95      62.407  93.244  51.876  1.00 14.77           C  
ANISOU 1605  C   GLY A  95     1732   1826   2056   -260    150   -683       C  
ATOM   1606  O   GLY A  95      62.503  94.475  51.983  1.00 15.90           O  
ANISOU 1606  O   GLY A  95     1882   1896   2264   -341    128   -696       O  
ATOM   1607  H   GLY A  95      60.895  90.888  50.758  1.00 17.75           H  
ATOM   1608  HA2 GLY A  95      60.698  92.999  50.822  1.00 16.79           H  
ATOM   1609  HA3 GLY A  95      60.480  92.899  52.383  1.00 16.79           H  
ATOM   1610  N   ASN A  96      63.455  92.435  51.945  1.00 15.56           N  
ANISOU 1610  N   ASN A  96     1917   1887   2107   -249    203   -526       N  
ATOM   1611  CA  ASN A  96      64.815  92.899  52.184  1.00 15.67           C  
ANISOU 1611  CA  ASN A  96     1955   2011   1988   -320     71   -621       C  
ATOM   1612  C   ASN A  96      65.753  92.431  51.080  1.00 15.63           C  
ANISOU 1612  C   ASN A  96     1839   2138   1961   -434    235   -626       C  
ATOM   1613  O   ASN A  96      66.956  92.258  51.300  1.00 16.93           O  
ANISOU 1613  O   ASN A  96     1987   2510   1937   -247     37   -636       O  
ATOM   1614  CB  ASN A  96      65.297  92.432  53.548  1.00 15.42           C  
ANISOU 1614  CB  ASN A  96     2021   2003   1835   -412     69   -480       C  
ATOM   1615  CG  ASN A  96      64.738  93.280  54.669  1.00 16.36           C  
ANISOU 1615  CG  ASN A  96     2435   1901   1879   -486     88   -644       C  
ATOM   1616  OD1 ASN A  96      64.787  94.513  54.617  1.00 17.69           O  
ANISOU 1616  OD1 ASN A  96     2721   1969   2031   -526    -54   -518       O  
ATOM   1617  ND2 ASN A  96      64.187  92.628  55.688  1.00 17.16           N  
ANISOU 1617  ND2 ASN A  96     2519   2078   1923   -547    274   -646       N  
ATOM   1618  H   ASN A  96      63.401  91.582  51.853  1.00 18.68           H  
ATOM   1619  HA  ASN A  96      64.828  93.869  52.184  1.00 18.81           H  
ATOM   1620  HB2 ASN A  96      65.012  91.516  53.691  1.00 18.51           H  
ATOM   1621  HB3 ASN A  96      66.265  92.488  53.580  1.00 18.51           H  
ATOM   1622 HD21 ASN A  96      63.855  93.066  56.350  1.00 20.60           H  
ATOM   1623 HD22 ASN A  96      64.162  91.768  55.686  1.00 20.60           H  
ATOM   1624  N   ASN A  97      65.199  92.207  49.890  1.00 15.37           N  
ANISOU 1624  N   ASN A  97     1829   2028   1984   -481    394   -645       N  
ATOM   1625  CA  ASN A  97      65.985  91.888  48.699  1.00 15.65           C  
ANISOU 1625  CA  ASN A  97     1821   2116   2008   -385    435   -465       C  
ATOM   1626  C   ASN A  97      66.741  90.559  48.814  1.00 16.09           C  
ANISOU 1626  C   ASN A  97     1884   2149   2081   -429    187   -459       C  
ATOM   1627  O   ASN A  97      67.804  90.387  48.233  1.00 16.65           O  
ANISOU 1627  O   ASN A  97     1936   2031   2361   -286    368   -432       O  
ATOM   1628  CB  ASN A  97      66.914  93.044  48.287  1.00 15.92           C  
ANISOU 1628  CB  ASN A  97     1779   2084   2186   -377    345   -488       C  
ATOM   1629  CG  ASN A  97      66.329  93.875  47.159  1.00 16.07           C  
ANISOU 1629  CG  ASN A  97     1764   1881   2462   -387    197   -379       C  
ATOM   1630  OD1 ASN A  97      65.474  93.406  46.415  1.00 16.69           O  
ANISOU 1630  OD1 ASN A  97     1815   2019   2507   -293    -32   -366       O  
ATOM   1631  ND2 ASN A  97      66.795  95.105  47.013  1.00 19.06           N  
ANISOU 1631  ND2 ASN A  97     2401   1990   2852   -428     15   -380       N  
ATOM   1632  H   ASN A  97      64.352  92.234  49.744  1.00 18.45           H  
ATOM   1633  HA  ASN A  97      65.357  91.766  47.970  1.00 18.78           H  
ATOM   1634  HB2 ASN A  97      67.054  93.627  49.050  1.00 19.11           H  
ATOM   1635  HB3 ASN A  97      67.761  92.680  47.986  1.00 19.11           H  
ATOM   1636 HD21 ASN A  97      66.490  95.609  46.386  1.00 22.89           H  
ATOM   1637 HD22 ASN A  97      67.402  95.401  47.546  1.00 22.89           H  
ATOM   1638  N   ALA A  98      66.187  89.580  49.519  1.00 15.48           N  
ANISOU 1638  N   ALA A  98     1911   2088   1882   -195      5   -494       N  
ATOM   1639  CA  ALA A  98      66.801  88.261  49.554  1.00 15.88           C  
ANISOU 1639  CA  ALA A  98     1885   2203   1947    -78     40   -676       C  
ATOM   1640  C   ALA A  98      67.004  87.716  48.150  1.00 15.48           C  
ANISOU 1640  C   ALA A  98     1678   2184   2019   -102    200   -462       C  
ATOM   1641  O   ALA A  98      66.146  87.868  47.270  1.00 15.43           O  
ANISOU 1641  O   ALA A  98     1556   2196   2113    -27    104   -230       O  
ATOM   1642  CB  ALA A  98      65.897  87.295  50.316  1.00 16.63           C  
ANISOU 1642  CB  ALA A  98     2178   2248   1892     26    217   -586       C  
ATOM   1643  H   ALA A  98      65.464  89.651  49.981  1.00 18.58           H  
ATOM   1644  HA  ALA A  98      67.661  88.330  49.996  1.00 19.07           H  
ATOM   1645  HB1 ALA A  98      66.278  86.404  50.271  1.00 19.96           H  
ATOM   1646  HB2 ALA A  98      65.837  87.582  51.241  1.00 19.96           H  
ATOM   1647  HB3 ALA A  98      65.016  87.300  49.911  1.00 19.96           H  
ATOM   1648  N   ALA A  99      68.138  87.044  47.951  1.00 16.11           N  
ANISOU 1648  N   ALA A  99     1862   2154   2106    -58     36   -348       N  
ATOM   1649  CA  ALA A  99      68.382  86.356  46.695  1.00 15.38           C  
ANISOU 1649  CA  ALA A  99     1693   2191   1960     34   -161   -479       C  
ATOM   1650  C   ALA A  99      67.298  85.317  46.466  1.00 14.64           C  
ANISOU 1650  C   ALA A  99     1759   2047   1756    159    -58   -292       C  
ATOM   1651  O   ALA A  99      66.859  84.643  47.402  1.00 14.99           O  
ANISOU 1651  O   ALA A  99     1851   2136   1710     -7   -209   -266       O  
ATOM   1652  CB  ALA A  99      69.742  85.666  46.752  1.00 16.98           C  
ANISOU 1652  CB  ALA A  99     1961   2250   2240    -69   -258   -602       C  
ATOM   1653  H   ALA A  99      68.776  86.974  48.524  1.00 19.34           H  
ATOM   1654  HA  ALA A  99      68.380  86.987  45.958  1.00 18.47           H  
ATOM   1655  HB1 ALA A  99      69.906  85.220  45.907  1.00 20.38           H  
ATOM   1656  HB2 ALA A  99      70.428  86.333  46.913  1.00 20.38           H  
ATOM   1657  HB3 ALA A  99      69.737  85.017  47.473  1.00 20.38           H  
ATOM   1658  N   ILE A 100      66.848  85.202  45.223  1.00 13.70           N  
ANISOU 1658  N   ILE A 100     1724   1972   1511    156    -63   -170       N  
ATOM   1659  CA  ILE A 100      65.874  84.183  44.845  1.00 13.08           C  
ANISOU 1659  CA  ILE A 100     1548   1790   1632     73    -73      5       C  
ATOM   1660  C   ILE A 100      66.619  83.057  44.134  1.00 13.75           C  
ANISOU 1660  C   ILE A 100     1562   2011   1652     34    -92   -185       C  
ATOM   1661  O   ILE A 100      67.134  83.235  43.027  1.00 14.49           O  
ANISOU 1661  O   ILE A 100     1759   1918   1829    147    167    -80       O  
ATOM   1662  CB  ILE A 100      64.749  84.747  43.971  1.00 13.52           C  
ANISOU 1662  CB  ILE A 100     1626   1828   1684     75   -260   -131       C  
ATOM   1663  CG1 ILE A 100      64.034  85.907  44.685  1.00 14.77           C  
ANISOU 1663  CG1 ILE A 100     1816   1910   1888    294    -18   -146       C  
ATOM   1664  CG2 ILE A 100      63.755  83.621  43.646  1.00 14.01           C  
ANISOU 1664  CG2 ILE A 100     1766   1870   1689    -30   -416   -164       C  
ATOM   1665  CD1 ILE A 100      62.974  86.602  43.836  1.00 15.26           C  
ANISOU 1665  CD1 ILE A 100     2008   1848   1944    241     56   -153       C  
ATOM   1666  H   ILE A 100      67.096  85.709  44.574  1.00 16.45           H  
ATOM   1667  HA  ILE A 100      65.475  83.825  45.653  1.00 15.70           H  
ATOM   1668  HB  ILE A 100      65.130  85.095  43.150  1.00 16.23           H  
ATOM   1669 HG12 ILE A 100      63.595  85.560  45.478  1.00 17.73           H  
ATOM   1670 HG13 ILE A 100      64.694  86.572  44.936  1.00 17.73           H  
ATOM   1671 HG21 ILE A 100      62.999  83.996  43.168  1.00 16.83           H  
ATOM   1672 HG22 ILE A 100      64.198  82.958  43.094  1.00 16.83           H  
ATOM   1673 HG23 ILE A 100      63.455  83.216  44.474  1.00 16.83           H  
ATOM   1674 HD11 ILE A 100      62.688  87.411  44.287  1.00 18.32           H  
ATOM   1675 HD12 ILE A 100      63.357  86.823  42.972  1.00 18.32           H  
ATOM   1676 HD13 ILE A 100      62.220  86.003  43.719  1.00 18.32           H  
ATOM   1677  N   ARG A 101      66.675  81.897  44.774  1.00 13.11           N  
ANISOU 1677  N   ARG A 101     1603   1863   1516    175     10   -164       N  
ATOM   1678  CA  ARG A 101      67.376  80.726  44.255  1.00 13.60           C  
ANISOU 1678  CA  ARG A 101     1662   1886   1621   -137   -252   -194       C  
ATOM   1679  C   ARG A 101      66.359  79.672  43.855  1.00 12.89           C  
ANISOU 1679  C   ARG A 101     1454   1844   1600    -20   -229     23       C  
ATOM   1680  O   ARG A 101      65.384  79.438  44.576  1.00 13.71           O  
ANISOU 1680  O   ARG A 101     1604   1992   1612    109    -65    -51       O  
ATOM   1681  CB  ARG A 101      68.322  80.169  45.319  1.00 15.46           C  
ANISOU 1681  CB  ARG A 101     1774   2209   1890   -142   -278    -51       C  
ATOM   1682  CG  ARG A 101      69.328  81.198  45.782  1.00 16.81           C  
ANISOU 1682  CG  ARG A 101     1964   2399   2026   -136   -426     30       C  
ATOM   1683  CD  ARG A 101      70.384  80.646  46.726  1.00 19.72           C  
ANISOU 1683  CD  ARG A 101     2116   2872   2506   -157   -755   -317       C  
ATOM   1684  NE  ARG A 101      71.052  81.756  47.421  1.00 23.11           N  
ANISOU 1684  NE  ARG A 101     2417   3376   2987   -129   -899   -424       N  
ATOM   1685  CZ  ARG A 101      72.078  82.449  46.937  1.00 24.44           C  
ANISOU 1685  CZ  ARG A 101     2553   3526   3209     28  -1064   -604       C  
ATOM   1686  NH1 ARG A 101      72.608  82.141  45.753  1.00 25.23           N  
ANISOU 1686  NH1 ARG A 101     2666   3428   3490    135   -870   -662       N  
ATOM   1687  NH2 ARG A 101      72.577  83.454  47.641  1.00 25.03           N  
ANISOU 1687  NH2 ARG A 101     2542   3716   3252    -14  -1128   -594       N  
ATOM   1688  H   ARG A 101      66.302  81.759  45.536  1.00 15.74           H  
ATOM   1689  HA  ARG A 101      67.896  80.959  43.471  1.00 16.33           H  
ATOM   1690  HB2 ARG A 101      67.803  79.885  46.088  1.00 18.56           H  
ATOM   1691  HB3 ARG A 101      68.807  79.416  44.950  1.00 18.56           H  
ATOM   1692  HG2 ARG A 101      69.785  81.559  45.006  1.00 20.18           H  
ATOM   1693  HG3 ARG A 101      68.857  81.907  46.249  1.00 20.18           H  
ATOM   1694  HD2 ARG A 101      69.967  80.069  47.385  1.00 23.68           H  
ATOM   1695  HD3 ARG A 101      71.047  80.148  46.221  1.00 23.68           H  
ATOM   1696  HE  ARG A 101      70.757  81.974  48.199  1.00 27.74           H  
ATOM   1697 HH11 ARG A 101      72.287  81.488  45.294  1.00 30.28           H  
ATOM   1698 HH12 ARG A 101      73.272  82.595  45.448  1.00 30.28           H  
ATOM   1699 HH21 ARG A 101      72.237  83.653  48.406  1.00 30.04           H  
ATOM   1700 HH22 ARG A 101      73.240  83.906  47.334  1.00 30.04           H  
ATOM   1701  N   SER A 102      66.586  79.051  42.694  1.00 12.41           N  
ANISOU 1701  N   SER A 102     1442   1802   1470     -4   -161      8       N  
ATOM   1702  CA  SER A 102      65.708  78.021  42.158  1.00 11.97           C  
ANISOU 1702  CA  SER A 102     1487   1688   1373     25   -144   -114       C  
ATOM   1703  C   SER A 102      66.546  76.875  41.613  1.00 12.52           C  
ANISOU 1703  C   SER A 102     1423   1671   1662     71     24    -20       C  
ATOM   1704  O   SER A 102      67.561  77.121  40.962  1.00 13.48           O  
ANISOU 1704  O   SER A 102     1402   1955   1766    141    139   -206       O  
ATOM   1705  CB  SER A 102      64.880  78.531  40.961  1.00 12.93           C  
ANISOU 1705  CB  SER A 102     1751   1628   1534     92   -121    -77       C  
ATOM   1706  OG  SER A 102      64.127  79.665  41.302  1.00 12.95           O  
ANISOU 1706  OG  SER A 102     1614   1574   1734     96    -14   -220       O  
ATOM   1707  H   SER A 102      67.263  79.217  42.189  1.00 14.90           H  
ATOM   1708  HA  SER A 102      65.128  77.726  42.877  1.00 14.37           H  
ATOM   1709  HB2 SER A 102      65.485  78.763  40.238  1.00 15.52           H  
ATOM   1710  HB3 SER A 102      64.276  77.828  40.675  1.00 15.52           H  
ATOM   1711  HG  SER A 102      64.638  80.297  41.513  1.00 15.55           H  
ATOM   1712  N   SER A 103      66.087  75.642  41.814  1.00 12.36           N  
ANISOU 1712  N   SER A 103     1406   1495   1797    120     75     48       N  
ATOM   1713  CA  SER A 103      66.714  74.461  41.242  1.00 12.26           C  
ANISOU 1713  CA  SER A 103     1524   1506   1627     52    -16   -166       C  
ATOM   1714  C   SER A 103      65.714  73.733  40.357  1.00 12.24           C  
ANISOU 1714  C   SER A 103     1432   1636   1584   -195     30     19       C  
ATOM   1715  O   SER A 103      64.555  73.541  40.754  1.00 13.65           O  
ANISOU 1715  O   SER A 103     1409   1970   1809   -220     21   -109       O  
ATOM   1716  CB  SER A 103      67.185  73.499  42.327  1.00 13.19           C  
ANISOU 1716  CB  SER A 103     1479   1819   1714    126    -14     33       C  
ATOM   1717  OG  SER A 103      68.128  74.116  43.174  1.00 15.12           O  
ANISOU 1717  OG  SER A 103     1441   2169   2134    185   -187    -36       O  
ATOM   1718  H   SER A 103      65.394  75.465  42.291  1.00 14.84           H  
ATOM   1719  HA  SER A 103      67.475  74.743  40.710  1.00 14.71           H  
ATOM   1720  HB2 SER A 103      66.421  73.221  42.856  1.00 15.84           H  
ATOM   1721  HB3 SER A 103      67.597  72.727  41.907  1.00 15.84           H  
ATOM   1722  HG  SER A 103      68.848  74.239  42.760  1.00 18.15           H  
ATOM   1723  N   VAL A 104      66.164  73.336  39.170  1.00 12.45           N  
ANISOU 1723  N   VAL A 104     1510   1574   1648     74     10    -32       N  
ATOM   1724  CA  VAL A 104      65.357  72.598  38.211  1.00 12.42           C  
ANISOU 1724  CA  VAL A 104     1475   1539   1706     93    -37    -42       C  
ATOM   1725  C   VAL A 104      65.977  71.217  37.980  1.00 13.14           C  
ANISOU 1725  C   VAL A 104     1390   1754   1848     27    -15   -101       C  
ATOM   1726  O   VAL A 104      67.077  70.905  38.448  1.00 13.29           O  
ANISOU 1726  O   VAL A 104     1348   1815   1886    162   -200     84       O  
ATOM   1727  CB  VAL A 104      65.147  73.365  36.891  1.00 13.00           C  
ANISOU 1727  CB  VAL A 104     1591   1645   1704    292    -20   -103       C  
ATOM   1728  CG1 VAL A 104      64.479  74.702  37.158  1.00 13.51           C  
ANISOU 1728  CG1 VAL A 104     1751   1802   1581    433     85    -38       C  
ATOM   1729  CG2 VAL A 104      66.455  73.562  36.170  1.00 13.74           C  
ANISOU 1729  CG2 VAL A 104     1724   1732   1764    121    -67     25       C  
ATOM   1730  H   VAL A 104      66.963  73.490  38.892  1.00 14.95           H  
ATOM   1731  HA  VAL A 104      64.479  72.451  38.599  1.00 14.91           H  
ATOM   1732  HB  VAL A 104      64.567  72.842  36.316  1.00 15.61           H  
ATOM   1733 HG11 VAL A 104      64.316  75.148  36.312  1.00 16.22           H  
ATOM   1734 HG12 VAL A 104      63.639  74.548  37.618  1.00 16.22           H  
ATOM   1735 HG13 VAL A 104      65.065  75.243  37.710  1.00 16.22           H  
ATOM   1736 HG21 VAL A 104      66.307  74.124  35.394  1.00 16.50           H  
ATOM   1737 HG22 VAL A 104      67.086  73.988  36.771  1.00 16.50           H  
ATOM   1738 HG23 VAL A 104      66.796  72.697  35.893  1.00 16.50           H  
ATOM   1739  N   HIS A 105      65.245  70.376  37.246  1.00 13.90           N  
ANISOU 1739  N   HIS A 105     1628   1741   1914     49    -18   -220       N  
ATOM   1740  CA  HIS A 105      65.628  68.975  37.076  1.00 13.19           C  
ANISOU 1740  CA  HIS A 105     1398   1820   1795    154     28     -9       C  
ATOM   1741  C   HIS A 105      65.809  68.298  38.430  1.00 13.42           C  
ANISOU 1741  C   HIS A 105     1380   1853   1866    261     77     20       C  
ATOM   1742  O   HIS A 105      66.722  67.494  38.633  1.00 14.17           O  
ANISOU 1742  O   HIS A 105     1515   1776   2092    206     25     -4       O  
ATOM   1743  CB  HIS A 105      66.870  68.804  36.208  1.00 13.35           C  
ANISOU 1743  CB  HIS A 105     1476   1657   1940     42    -50    -63       C  
ATOM   1744  CG  HIS A 105      66.708  69.318  34.817  1.00 13.23           C  
ANISOU 1744  CG  HIS A 105     1520   1886   1621     60     36   -207       C  
ATOM   1745  ND1 HIS A 105      65.673  68.923  33.996  1.00 14.13           N  
ANISOU 1745  ND1 HIS A 105     1751   1950   1669     50    -98   -123       N  
ATOM   1746  CD2 HIS A 105      67.443  70.195  34.096  1.00 14.00           C  
ANISOU 1746  CD2 HIS A 105     1664   1955   1700     67     54    -57       C  
ATOM   1747  CE1 HIS A 105      65.770  69.544  32.833  1.00 15.28           C  
ANISOU 1747  CE1 HIS A 105     1945   2048   1813    236    193   -203       C  
ATOM   1748  NE2 HIS A 105      66.842  70.314  32.861  1.00 14.87           N  
ANISOU 1748  NE2 HIS A 105     1989   1925   1737    180    236   -125       N  
ATOM   1749  H   HIS A 105      64.522  70.595  36.836  1.00 16.69           H  
ATOM   1750  HA  HIS A 105      64.903  68.531  36.609  1.00 15.84           H  
ATOM   1751  HB2 HIS A 105      67.605  69.286  36.618  1.00 16.03           H  
ATOM   1752  HB3 HIS A 105      67.083  67.860  36.152  1.00 16.03           H  
ATOM   1753  HD1 HIS A 105      65.059  68.360  34.207  1.00 16.97           H  
ATOM   1754  HD2 HIS A 105      68.210  70.637  34.381  1.00 16.81           H  
ATOM   1755  HE1 HIS A 105      65.184  69.454  32.117  1.00 18.35           H  
ATOM   1756  HE2 HIS A 105      67.120  70.809  32.214  1.00 17.86           H  
ATOM   1757  N   TYR A 106      64.913  68.610  39.364  1.00 13.50           N  
ANISOU 1757  N   TYR A 106     1370   1834   1925    235     86    160       N  
ATOM   1758  CA  TYR A 106      64.941  67.971  40.671  1.00 14.21           C  
ANISOU 1758  CA  TYR A 106     1636   1856   1907     40    111    -67       C  
ATOM   1759  C   TYR A 106      64.337  66.582  40.578  1.00 15.05           C  
ANISOU 1759  C   TYR A 106     1722   1740   2258     96    160     48       C  
ATOM   1760  O   TYR A 106      63.195  66.435  40.140  1.00 14.95           O  
ANISOU 1760  O   TYR A 106     1690   1665   2326    110    206    -50       O  
ATOM   1761  CB  TYR A 106      64.142  68.806  41.651  1.00 14.06           C  
ANISOU 1761  CB  TYR A 106     1757   1862   1723     81    192   -166       C  
ATOM   1762  CG  TYR A 106      64.039  68.238  43.040  1.00 15.64           C  
ANISOU 1762  CG  TYR A 106     1953   2069   1922    265    338     28       C  
ATOM   1763  CD1 TYR A 106      62.884  67.606  43.466  1.00 17.00           C  
ANISOU 1763  CD1 TYR A 106     2214   2184   2060    109    490    342       C  
ATOM   1764  CD2 TYR A 106      65.094  68.360  43.938  1.00 16.85           C  
ANISOU 1764  CD2 TYR A 106     2185   2216   2002    321     81    171       C  
ATOM   1765  CE1 TYR A 106      62.773  67.121  44.762  1.00 19.00           C  
ANISOU 1765  CE1 TYR A 106     2636   2387   2196     60    448    587       C  
ATOM   1766  CE2 TYR A 106      65.002  67.878  45.214  1.00 18.71           C  
ANISOU 1766  CE2 TYR A 106     2515   2547   2049    308    107    193       C  
ATOM   1767  CZ  TYR A 106      63.841  67.255  45.634  1.00 20.11           C  
ANISOU 1767  CZ  TYR A 106     2906   2652   2084    205    294    610       C  
ATOM   1768  OH  TYR A 106      63.750  66.781  46.925  1.00 23.60           O  
ANISOU 1768  OH  TYR A 106     3472   3121   2373    198    297    819       O  
ATOM   1769  H   TYR A 106      64.283  69.186  39.262  1.00 16.20           H  
ATOM   1770  HA  TYR A 106      65.859  67.893  40.976  1.00 17.06           H  
ATOM   1771  HB2 TYR A 106      64.561  69.678  41.724  1.00 16.88           H  
ATOM   1772  HB3 TYR A 106      63.239  68.900  41.309  1.00 16.88           H  
ATOM   1773  HD1 TYR A 106      62.172  67.506  42.876  1.00 20.40           H  
ATOM   1774  HD2 TYR A 106      65.879  68.778  43.664  1.00 20.23           H  
ATOM   1775  HE1 TYR A 106      61.988  66.710  45.043  1.00 22.81           H  
ATOM   1776  HE2 TYR A 106      65.719  67.970  45.800  1.00 22.47           H  
ATOM   1777  HH  TYR A 106      62.990  66.446  47.055  1.00 28.32           H  
ATOM   1778  N   SER A 107      65.110  65.569  40.991  1.00 15.73           N  
ANISOU 1778  N   SER A 107     1699   1842   2436    135     94    215       N  
ATOM   1779  CA  SER A 107      64.662  64.180  41.001  1.00 16.80           C  
ANISOU 1779  CA  SER A 107     1901   1773   2708     21     64    192       C  
ATOM   1780  C   SER A 107      64.292  63.740  39.593  1.00 16.64           C  
ANISOU 1780  C   SER A 107     1869   1560   2894    -20    116     -9       C  
ATOM   1781  O   SER A 107      64.749  64.342  38.619  1.00 16.15           O  
ANISOU 1781  O   SER A 107     1722   1588   2827    -36    157    -32       O  
ATOM   1782  CB  SER A 107      63.493  63.999  41.975  1.00 19.05           C  
ANISOU 1782  CB  SER A 107     2327   1895   3017   -376     40    522       C  
ATOM   1783  OG  SER A 107      63.235  62.611  42.201  1.00 21.77           O  
ANISOU 1783  OG  SER A 107     2759   2212   3299   -377    -17    607       O  
ATOM   1784  H   SER A 107      65.916  65.667  41.276  1.00 18.89           H  
ATOM   1785  HA  SER A 107      65.380  63.604  41.310  1.00 20.17           H  
ATOM   1786  HB2 SER A 107      63.718  64.420  42.820  1.00 22.87           H  
ATOM   1787  HB3 SER A 107      62.701  64.412  41.599  1.00 22.87           H  
ATOM   1788  HG  SER A 107      63.920  62.237  42.511  1.00 26.13           H  
ATOM   1789  N   GLN A 108      63.493  62.680  39.478  1.00 18.27           N  
ANISOU 1789  N   GLN A 108     2045   1636   3261    -28    -17    -34       N  
ATOM   1790  CA  GLN A 108      63.052  62.154  38.191  1.00 19.87           C  
ANISOU 1790  CA  GLN A 108     2230   1586   3735    199    -10   -324       C  
ATOM   1791  C   GLN A 108      61.550  61.924  38.234  1.00 20.51           C  
ANISOU 1791  C   GLN A 108     2308   1679   3805    213    -51   -197       C  
ATOM   1792  O   GLN A 108      61.028  61.383  39.216  1.00 20.62           O  
ANISOU 1792  O   GLN A 108     2036   1803   3995     16    -79    148       O  
ATOM   1793  CB  GLN A 108      63.770  60.849  37.838  1.00 24.33           C  
ANISOU 1793  CB  GLN A 108     2449   2298   4498     30    271   -478       C  
ATOM   1794  CG  GLN A 108      65.196  61.141  37.371  1.00 28.78           C  
ANISOU 1794  CG  GLN A 108     2725   2944   5266    -92    662   -522       C  
ATOM   1795  CD  GLN A 108      65.984  59.922  37.056  1.00 34.70           C  
ANISOU 1795  CD  GLN A 108     3532   3839   5816   -132    658   -594       C  
ATOM   1796  OE1 GLN A 108      66.516  59.777  35.950  1.00 37.15           O  
ANISOU 1796  OE1 GLN A 108     3787   4308   6019    -44    616  -1009       O  
ATOM   1797  NE2 GLN A 108      66.103  59.037  38.031  1.00 36.00           N  
ANISOU 1797  NE2 GLN A 108     3772   3866   6042    128    680   -378       N  
ATOM   1798  H   GLN A 108      63.188  62.239  40.150  1.00 21.93           H  
ATOM   1799  HA  GLN A 108      63.247  62.805  37.499  1.00 23.86           H  
ATOM   1800  HB2 GLN A 108      63.810  60.278  38.621  1.00 29.20           H  
ATOM   1801  HB3 GLN A 108      63.294  60.399  37.122  1.00 29.20           H  
ATOM   1802  HG2 GLN A 108      65.157  61.683  36.567  1.00 34.54           H  
ATOM   1803  HG3 GLN A 108      65.662  61.622  38.072  1.00 34.54           H  
ATOM   1804 HE21 GLN A 108      65.733  59.185  38.794  1.00 43.21           H  
ATOM   1805 HE22 GLN A 108      66.549  58.313  37.903  1.00 43.21           H  
ATOM   1806  N   GLY A 109      60.862  62.367  37.183  1.00 20.86           N  
ANISOU 1806  N   GLY A 109     2587   1632   3706    323   -176   -357       N  
ATOM   1807  CA  GLY A 109      59.424  62.203  37.096  1.00 22.32           C  
ANISOU 1807  CA  GLY A 109     2633   2070   3778    106   -211   -290       C  
ATOM   1808  C   GLY A 109      58.653  62.852  38.221  1.00 21.60           C  
ANISOU 1808  C   GLY A 109     2409   2062   3737     -1   -210   -203       C  
ATOM   1809  O   GLY A 109      57.570  62.378  38.579  1.00 23.06           O  
ANISOU 1809  O   GLY A 109     2564   2170   4030   -126   -509   -351       O  
ATOM   1810  H   GLY A 109      61.209  62.769  36.506  1.00 25.04           H  
ATOM   1811  HA2 GLY A 109      59.115  62.589  36.261  1.00 26.80           H  
ATOM   1812  HA3 GLY A 109      59.217  61.255  37.101  1.00 26.80           H  
ATOM   1813  N   TYR A 110      59.178  63.936  38.783  1.00 19.44           N  
ANISOU 1813  N   TYR A 110     2116   1940   3332     76   -265   -178       N  
ATOM   1814  CA  TYR A 110      58.653  64.511  40.018  1.00 19.67           C  
ANISOU 1814  CA  TYR A 110     2262   2078   3132     78   -176    127       C  
ATOM   1815  C   TYR A 110      57.560  65.517  39.677  1.00 18.29           C  
ANISOU 1815  C   TYR A 110     1998   2108   2844     20    -42    -27       C  
ATOM   1816  O   TYR A 110      57.834  66.560  39.076  1.00 17.48           O  
ANISOU 1816  O   TYR A 110     1881   2178   2581   -150     -9      1       O  
ATOM   1817  CB  TYR A 110      59.788  65.166  40.796  1.00 20.22           C  
ANISOU 1817  CB  TYR A 110     2283   2324   3074      7   -311    394       C  
ATOM   1818  CG  TYR A 110      59.418  65.656  42.168  1.00 21.02           C  
ANISOU 1818  CG  TYR A 110     2513   2525   2947   -470   -127    500       C  
ATOM   1819  CD1 TYR A 110      59.131  64.760  43.184  1.00 24.73           C  
ANISOU 1819  CD1 TYR A 110     3381   3030   2987   -505     67    356       C  
ATOM   1820  CD2 TYR A 110      59.366  67.009  42.455  1.00 22.15           C  
ANISOU 1820  CD2 TYR A 110     2484   2911   3023   -800   -119    285       C  
ATOM   1821  CE1 TYR A 110      58.792  65.204  44.455  1.00 26.85           C  
ANISOU 1821  CE1 TYR A 110     3719   3447   3036   -576     82    370       C  
ATOM   1822  CE2 TYR A 110      59.045  67.462  43.713  1.00 24.30           C  
ANISOU 1822  CE2 TYR A 110     2965   3197   3070  -1000    -74    198       C  
ATOM   1823  CZ  TYR A 110      58.756  66.558  44.709  1.00 26.79           C  
ANISOU 1823  CZ  TYR A 110     3600   3541   3037   -865     56    130       C  
ATOM   1824  OH  TYR A 110      58.425  67.016  45.962  1.00 30.26           O  
ANISOU 1824  OH  TYR A 110     4048   4148   3300   -963    152    176       O  
ATOM   1825  H   TYR A 110      59.852  64.363  38.463  1.00 23.34           H  
ATOM   1826  HA  TYR A 110      58.253  63.816  40.563  1.00 23.61           H  
ATOM   1827  HB2 TYR A 110      60.502  64.518  40.901  1.00 24.27           H  
ATOM   1828  HB3 TYR A 110      60.106  65.930  40.290  1.00 24.27           H  
ATOM   1829  HD1 TYR A 110      59.165  63.846  43.013  1.00 29.69           H  
ATOM   1830  HD2 TYR A 110      59.552  67.625  41.784  1.00 26.59           H  
ATOM   1831  HE1 TYR A 110      58.592  64.595  45.128  1.00 32.23           H  
ATOM   1832  HE2 TYR A 110      59.024  68.374  43.890  1.00 29.16           H  
ATOM   1833  HH  TYR A 110      58.437  67.856  45.973  1.00 36.32           H  
ATOM   1834  N   ASN A 111      56.328  65.207  40.080  1.00 17.89           N  
ANISOU 1834  N   ASN A 111     1929   2021   2847   -134    -45   -133       N  
ATOM   1835  CA  ASN A 111      55.145  65.976  39.705  1.00 18.16           C  
ANISOU 1835  CA  ASN A 111     1876   2076   2948   -155    -97   -286       C  
ATOM   1836  C   ASN A 111      54.826  67.034  40.763  1.00 19.08           C  
ANISOU 1836  C   ASN A 111     1957   2248   3046   -210      1   -304       C  
ATOM   1837  O   ASN A 111      53.733  67.087  41.332  1.00 21.33           O  
ANISOU 1837  O   ASN A 111     2173   2432   3498   -469    140   -340       O  
ATOM   1838  CB  ASN A 111      53.951  65.039  39.539  1.00 19.25           C  
ANISOU 1838  CB  ASN A 111     1971   2164   3178   -390   -213   -386       C  
ATOM   1839  CG  ASN A 111      54.007  64.226  38.274  1.00 20.29           C  
ANISOU 1839  CG  ASN A 111     2091   2069   3551   -571   -312   -434       C  
ATOM   1840  OD1 ASN A 111      54.402  64.717  37.221  1.00 20.67           O  
ANISOU 1840  OD1 ASN A 111     2090   1947   3817   -255   -237   -440       O  
ATOM   1841  ND2 ASN A 111      53.545  62.976  38.359  1.00 22.59           N  
ANISOU 1841  ND2 ASN A 111     2609   2182   3793   -396   -212   -266       N  
ATOM   1842  H   ASN A 111      56.148  64.535  40.586  1.00 21.47           H  
ATOM   1843  HA  ASN A 111      55.329  66.421  38.863  1.00 21.80           H  
ATOM   1844  HB2 ASN A 111      53.928  64.424  40.288  1.00 23.10           H  
ATOM   1845  HB3 ASN A 111      53.138  65.567  39.518  1.00 23.10           H  
ATOM   1846 HD21 ASN A 111      53.553  62.466  37.667  1.00 27.12           H  
ATOM   1847 HD22 ASN A 111      53.240  62.680  39.107  1.00 27.12           H  
ATOM   1848  N   ASN A 112      55.800  67.889  41.042  1.00 17.66           N  
ANISOU 1848  N   ASN A 112     2029   1995   2686   -310    -71   -251       N  
ATOM   1849  CA  ASN A 112      55.592  68.904  42.062  1.00 19.87           C  
ANISOU 1849  CA  ASN A 112     2402   2420   2729   -378     78   -153       C  
ATOM   1850  C   ASN A 112      56.632  70.002  41.926  1.00 17.03           C  
ANISOU 1850  C   ASN A 112     1790   2274   2405   -111    -29   -144       C  
ATOM   1851  O   ASN A 112      57.656  69.841  41.261  1.00 16.28           O  
ANISOU 1851  O   ASN A 112     1755   2039   2393    -58      1   -198       O  
ATOM   1852  CB  ASN A 112      55.642  68.290  43.467  1.00 23.73           C  
ANISOU 1852  CB  ASN A 112     3014   2917   3084   -805    315   -189       C  
ATOM   1853  CG  ASN A 112      55.150  69.234  44.538  1.00 28.97           C  
ANISOU 1853  CG  ASN A 112     3565   3815   3628   -804    443   -392       C  
ATOM   1854  OD1 ASN A 112      54.170  69.971  44.353  1.00 29.91           O  
ANISOU 1854  OD1 ASN A 112     3572   4016   3776   -727    881   -783       O  
ATOM   1855  ND2 ASN A 112      55.829  69.215  45.680  1.00 32.50           N  
ANISOU 1855  ND2 ASN A 112     3818   4407   4123   -950    338   -406       N  
ATOM   1856  H   ASN A 112      56.572  67.901  40.663  1.00 21.20           H  
ATOM   1857  HA  ASN A 112      54.724  69.311  41.921  1.00 23.85           H  
ATOM   1858  HB2 ASN A 112      55.082  67.498  43.486  1.00 28.48           H  
ATOM   1859  HB3 ASN A 112      56.559  68.052  43.676  1.00 28.48           H  
ATOM   1860 HD21 ASN A 112      55.596  69.731  46.327  1.00 39.01           H  
ATOM   1861 HD22 ASN A 112      56.501  68.687  45.771  1.00 39.01           H  
ATOM   1862  N   ALA A 113      56.336  71.124  42.572  1.00 16.69           N  
ANISOU 1862  N   ALA A 113     1676   2344   2320   -212    -46   -208       N  
ATOM   1863  CA  ALA A 113      57.231  72.258  42.714  1.00 16.05           C  
ANISOU 1863  CA  ALA A 113     1826   2160   2114   -117     -6   -107       C  
ATOM   1864  C   ALA A 113      56.926  72.876  44.069  1.00 14.98           C  
ANISOU 1864  C   ALA A 113     1601   2104   1987     -8    158    -78       C  
ATOM   1865  O   ALA A 113      55.766  72.881  44.504  1.00 16.66           O  
ANISOU 1865  O   ALA A 113     1767   2281   2281    -97    368   -404       O  
ATOM   1866  CB  ALA A 113      57.001  73.293  41.615  1.00 17.17           C  
ANISOU 1866  CB  ALA A 113     2062   2279   2184    -87   -284    -17       C  
ATOM   1867  H   ALA A 113      55.579  71.257  42.957  1.00 20.03           H  
ATOM   1868  HA  ALA A 113      58.159  71.978  42.668  1.00 19.27           H  
ATOM   1869  HB1 ALA A 113      57.629  74.023  41.732  1.00 20.61           H  
ATOM   1870  HB2 ALA A 113      57.140  72.873  40.751  1.00 20.61           H  
ATOM   1871  HB3 ALA A 113      56.092  73.625  41.679  1.00 20.61           H  
ATOM   1872  N   PHE A 114      57.958  73.377  44.736  1.00 13.85           N  
ANISOU 1872  N   PHE A 114     1534   1856   1874     68      7    115       N  
ATOM   1873  CA  PHE A 114      57.732  73.903  46.071  1.00 13.80           C  
ANISOU 1873  CA  PHE A 114     1547   1763   1933     55    -33    157       C  
ATOM   1874  C   PHE A 114      58.802  74.898  46.471  1.00 13.68           C  
ANISOU 1874  C   PHE A 114     1564   1765   1871     47     26    125       C  
ATOM   1875  O   PHE A 114      59.958  74.791  46.074  1.00 13.62           O  
ANISOU 1875  O   PHE A 114     1592   1863   1722    201     36     90       O  
ATOM   1876  CB  PHE A 114      57.660  72.776  47.117  1.00 15.86           C  
ANISOU 1876  CB  PHE A 114     2014   1922   2090     10    -49     68       C  
ATOM   1877  CG  PHE A 114      58.879  71.881  47.174  1.00 16.54           C  
ANISOU 1877  CG  PHE A 114     2396   1768   2120     79   -107    208       C  
ATOM   1878  CD1 PHE A 114      59.021  70.804  46.309  1.00 16.79           C  
ANISOU 1878  CD1 PHE A 114     2270   1894   2218    202   -100    -49       C  
ATOM   1879  CD2 PHE A 114      59.851  72.063  48.149  1.00 17.75           C  
ANISOU 1879  CD2 PHE A 114     2583   1783   2379    234   -172    220       C  
ATOM   1880  CE1 PHE A 114      60.116  69.946  46.405  1.00 18.54           C  
ANISOU 1880  CE1 PHE A 114     2562   2028   2453    194   -213    148       C  
ATOM   1881  CE2 PHE A 114      60.941  71.209  48.241  1.00 18.68           C  
ANISOU 1881  CE2 PHE A 114     2842   1834   2423    397   -177    244       C  
ATOM   1882  CZ  PHE A 114      61.067  70.160  47.367  1.00 18.48           C  
ANISOU 1882  CZ  PHE A 114     2668   1899   2456    508   -212    345       C  
ATOM   1883  H   PHE A 114      58.766  73.421  44.447  1.00 16.63           H  
ATOM   1884  HA  PHE A 114      56.891  74.387  46.049  1.00 16.57           H  
ATOM   1885  HB2 PHE A 114      57.553  73.177  47.994  1.00 19.04           H  
ATOM   1886  HB3 PHE A 114      56.896  72.215  46.913  1.00 19.04           H  
ATOM   1887  HD1 PHE A 114      58.377  70.653  45.655  1.00 20.16           H  
ATOM   1888  HD2 PHE A 114      59.771  72.768  48.750  1.00 21.31           H  
ATOM   1889  HE1 PHE A 114      60.200  69.230  45.818  1.00 22.25           H  
ATOM   1890  HE2 PHE A 114      61.586  71.348  48.896  1.00 22.43           H  
ATOM   1891  HZ  PHE A 114      61.801  69.592  47.427  1.00 22.19           H  
ATOM   1892  N   TRP A 115      58.378  75.861  47.290  1.00 14.14           N  
ANISOU 1892  N   TRP A 115     1544   1929   1900    253    -70    -67       N  
ATOM   1893  CA  TRP A 115      59.275  76.656  48.107  1.00 14.35           C  
ANISOU 1893  CA  TRP A 115     1656   2035   1762    142    280     74       C  
ATOM   1894  C   TRP A 115      59.627  75.857  49.356  1.00 15.57           C  
ANISOU 1894  C   TRP A 115     2037   1930   1949    247    407    182       C  
ATOM   1895  O   TRP A 115      58.732  75.392  50.072  1.00 17.36           O  
ANISOU 1895  O   TRP A 115     2169   2074   2352    110    694    164       O  
ATOM   1896  CB  TRP A 115      58.566  77.940  48.526  1.00 13.79           C  
ANISOU 1896  CB  TRP A 115     1554   1974   1712    304    125    105       C  
ATOM   1897  CG  TRP A 115      59.380  78.790  49.437  1.00 14.49           C  
ANISOU 1897  CG  TRP A 115     1779   2041   1687    158    103   -139       C  
ATOM   1898  CD1 TRP A 115      59.203  78.969  50.777  1.00 15.62           C  
ANISOU 1898  CD1 TRP A 115     2030   2011   1893    168     73    -46       C  
ATOM   1899  CD2 TRP A 115      60.523  79.581  49.073  1.00 13.98           C  
ANISOU 1899  CD2 TRP A 115     1718   1947   1645    192    -51    -36       C  
ATOM   1900  NE1 TRP A 115      60.158  79.828  51.269  1.00 15.13           N  
ANISOU 1900  NE1 TRP A 115     1857   2153   1740     94     40     36       N  
ATOM   1901  CE2 TRP A 115      60.989  80.210  50.246  1.00 14.51           C  
ANISOU 1901  CE2 TRP A 115     1762   1969   1782     44     -9    -92       C  
ATOM   1902  CE3 TRP A 115      61.193  79.815  47.874  1.00 14.01           C  
ANISOU 1902  CE3 TRP A 115     1818   1835   1669    302    -36    -32       C  
ATOM   1903  CZ2 TRP A 115      62.087  81.070  50.246  1.00 14.20           C  
ANISOU 1903  CZ2 TRP A 115     1753   1858   1784    199   -310   -119       C  
ATOM   1904  CZ3 TRP A 115      62.265  80.666  47.880  1.00 15.16           C  
ANISOU 1904  CZ3 TRP A 115     1826   2004   1930    196    -27   -156       C  
ATOM   1905  CH2 TRP A 115      62.706  81.277  49.057  1.00 15.12           C  
ANISOU 1905  CH2 TRP A 115     1885   1814   2044    -54   -142   -224       C  
ATOM   1906  H   TRP A 115      57.551  76.075  47.389  1.00 16.98           H  
ATOM   1907  HA  TRP A 115      60.083  76.876  47.617  1.00 17.23           H  
ATOM   1908  HB2 TRP A 115      58.365  78.461  47.732  1.00 16.56           H  
ATOM   1909  HB3 TRP A 115      57.745  77.709  48.987  1.00 16.56           H  
ATOM   1910  HD1 TRP A 115      58.534  78.570  51.284  1.00 18.75           H  
ATOM   1911  HE1 TRP A 115      60.224  80.085  52.087  1.00 18.17           H  
ATOM   1912  HE3 TRP A 115      60.918  79.402  47.087  1.00 16.82           H  
ATOM   1913  HZ2 TRP A 115      62.380  81.484  51.026  1.00 17.05           H  
ATOM   1914  HZ3 TRP A 115      62.710  80.843  47.082  1.00 18.20           H  
ATOM   1915  HH2 TRP A 115      63.446  81.840  49.025  1.00 18.15           H  
ATOM   1916  N   ASN A 116      60.926  75.685  49.616  1.00 15.45           N  
ANISOU 1916  N   ASN A 116     2214   1895   1761    181    216    140       N  
ATOM   1917  CA  ASN A 116      61.357  74.825  50.713  1.00 16.81           C  
ANISOU 1917  CA  ASN A 116     2585   2152   1650    402     97    253       C  
ATOM   1918  C   ASN A 116      61.795  75.606  51.946  1.00 18.75           C  
ANISOU 1918  C   ASN A 116     2860   2474   1789    454     50    422       C  
ATOM   1919  O   ASN A 116      62.398  75.020  52.861  1.00 19.53           O  
ANISOU 1919  O   ASN A 116     2980   2643   1798    664     60    478       O  
ATOM   1920  CB  ASN A 116      62.456  73.855  50.262  1.00 17.00           C  
ANISOU 1920  CB  ASN A 116     2510   2296   1654    353    144    236       C  
ATOM   1921  CG  ASN A 116      63.839  74.488  50.241  1.00 17.19           C  
ANISOU 1921  CG  ASN A 116     2404   2271   1854    437      8    158       C  
ATOM   1922  OD1 ASN A 116      63.987  75.711  50.323  1.00 16.40           O  
ANISOU 1922  OD1 ASN A 116     2334   2159   1740    303   -186    151       O  
ATOM   1923  ND2 ASN A 116      64.858  73.654  50.099  1.00 18.66           N  
ANISOU 1923  ND2 ASN A 116     2656   2268   2166    514     89     14       N  
ATOM   1924  H   ASN A 116      61.565  76.054  49.174  1.00 18.55           H  
ATOM   1925  HA  ASN A 116      60.599  74.279  50.974  1.00 20.18           H  
ATOM   1926  HB2 ASN A 116      62.482  73.102  50.873  1.00 20.41           H  
ATOM   1927  HB3 ASN A 116      62.255  73.547  49.364  1.00 20.41           H  
ATOM   1928 HD21 ASN A 116      65.662  73.958  50.080  1.00 22.40           H  
ATOM   1929 HD22 ASN A 116      64.715  72.809  50.025  1.00 22.40           H  
ATOM   1930  N   GLY A 117      61.512  76.905  51.989  1.00 18.47           N  
ANISOU 1930  N   GLY A 117     2772   2412   1834    422    -23     71       N  
ATOM   1931  CA  GLY A 117      61.940  77.765  53.063  1.00 19.72           C  
ANISOU 1931  CA  GLY A 117     3204   2482   1806    355    -62     78       C  
ATOM   1932  C   GLY A 117      63.130  78.629  52.724  1.00 20.58           C  
ANISOU 1932  C   GLY A 117     3255   2694   1870    394   -486   -156       C  
ATOM   1933  O   GLY A 117      63.318  79.689  53.341  1.00 22.53           O  
ANISOU 1933  O   GLY A 117     3612   2920   2028    458   -663   -261       O  
ATOM   1934  H   GLY A 117      61.059  77.313  51.382  1.00 22.17           H  
ATOM   1935  HA2 GLY A 117      61.206  78.350  53.308  1.00 23.67           H  
ATOM   1936  HA3 GLY A 117      62.176  77.217  53.828  1.00 23.67           H  
ATOM   1937  N   SER A 118      63.932  78.199  51.747  1.00 18.87           N  
ANISOU 1937  N   SER A 118     2806   2541   1822    501   -456    -93       N  
ATOM   1938  CA ASER A 118      65.130  78.909  51.318  0.42 18.55           C  
ANISOU 1938  CA ASER A 118     2722   2530   1796    361   -492    -34       C  
ATOM   1939  CA BSER A 118      65.052  79.019  51.314  0.58 19.00           C  
ANISOU 1939  CA BSER A 118     2781   2502   1937    393   -473     49       C  
ATOM   1940  C   SER A 118      65.238  79.065  49.810  1.00 17.14           C  
ANISOU 1940  C   SER A 118     2561   2253   1700    221   -484    -86       C  
ATOM   1941  O   SER A 118      66.031  79.901  49.351  1.00 17.32           O  
ANISOU 1941  O   SER A 118     2580   2279   1722    170   -540   -221       O  
ATOM   1942  CB ASER A 118      66.390  78.160  51.787  0.42 20.48           C  
ANISOU 1942  CB ASER A 118     2933   2891   1958    310   -475     78       C  
ATOM   1943  CB BSER A 118      66.362  78.567  51.972  0.58 21.79           C  
ANISOU 1943  CB BSER A 118     3095   2798   2387    420   -412    263       C  
ATOM   1944  OG ASER A 118      66.315  77.807  53.156  0.42 22.05           O  
ANISOU 1944  OG ASER A 118     3033   3247   2098    189   -495    333       O  
ATOM   1945  OG BSER A 118      66.712  77.273  51.549  0.58 22.39           O  
ANISOU 1945  OG BSER A 118     3168   2675   2662    386   -456    347       O  
ATOM   1946  H  ASER A 118      63.796  77.474  51.305  0.42 22.65           H  
ATOM   1947  H  BSER A 118      63.847  77.452  51.331  0.58 22.65           H  
ATOM   1948  HA ASER A 118      65.123  79.790  51.723  0.42 22.27           H  
ATOM   1949  HA BSER A 118      64.893  79.927  51.615  0.58 22.81           H  
ATOM   1950  HB2ASER A 118      66.485  77.350  51.261  0.42 24.59           H  
ATOM   1951  HB2BSER A 118      67.069  79.182  51.723  0.58 26.16           H  
ATOM   1952  HB3ASER A 118      67.161  78.734  51.655  0.42 24.59           H  
ATOM   1953  HB3BSER A 118      66.247  78.564  52.935  0.58 26.16           H  
ATOM   1954  HG ASER A 118      65.639  77.327  53.292  0.42 26.47           H  
ATOM   1955  HG BSER A 118      66.106  76.729  51.757  0.58 26.87           H  
ATOM   1956  N   GLN A 119      64.535  78.244  49.029  1.00 14.88           N  
ANISOU 1956  N   GLN A 119     2074   2051   1530    124   -430    -49       N  
ATOM   1957  CA  GLN A 119      64.674  78.269  47.578  1.00 13.74           C  
ANISOU 1957  CA  GLN A 119     1706   1946   1570    211   -382    -62       C  
ATOM   1958  C   GLN A 119      63.475  77.584  46.942  1.00 13.42           C  
ANISOU 1958  C   GLN A 119     1609   1934   1557    267   -123    -71       C  
ATOM   1959  O   GLN A 119      62.725  76.859  47.602  1.00 13.70           O  
ANISOU 1959  O   GLN A 119     1621   2097   1488    176    -21     86       O  
ATOM   1960  CB  GLN A 119      65.972  77.554  47.140  1.00 14.16           C  
ANISOU 1960  CB  GLN A 119     1683   1945   1752    485   -337     17       C  
ATOM   1961  CG  GLN A 119      65.995  76.071  47.445  1.00 14.86           C  
ANISOU 1961  CG  GLN A 119     1752   2085   1807    377   -166     87       C  
ATOM   1962  CD  GLN A 119      67.042  75.357  46.641  1.00 14.15           C  
ANISOU 1962  CD  GLN A 119     1520   2151   1704    408   -182    194       C  
ATOM   1963  OE1 GLN A 119      68.121  75.019  47.139  1.00 15.35           O  
ANISOU 1963  OE1 GLN A 119     1712   2334   1784    402   -351    -36       O  
ATOM   1964  NE2 GLN A 119      66.758  75.169  45.361  1.00 14.89           N  
ANISOU 1964  NE2 GLN A 119     1416   2242   1998    196   -214    152       N  
ATOM   1965  H   GLN A 119      63.970  77.663  49.318  1.00 17.87           H  
ATOM   1966  HA  GLN A 119      64.692  79.191  47.278  1.00 16.50           H  
ATOM   1967  HB2 GLN A 119      66.076  77.659  46.181  1.00 17.00           H  
ATOM   1968  HB3 GLN A 119      66.722  77.961  47.602  1.00 17.00           H  
ATOM   1969  HG2 GLN A 119      66.193  75.940  48.386  1.00 17.83           H  
ATOM   1970  HG3 GLN A 119      65.131  75.686  47.231  1.00 17.83           H  
ATOM   1971 HE21 GLN A 119      66.011  75.450  45.041  1.00 17.87           H  
ATOM   1972 HE22 GLN A 119      67.321  74.765  44.851  1.00 17.87           H  
ATOM   1973  N   MET A 120      63.314  77.827  45.652  1.00 12.91           N  
ANISOU 1973  N   MET A 120     1489   1841   1577    214   -190    -48       N  
ATOM   1974  CA  MET A 120      62.350  77.107  44.837  1.00 12.76           C  
ANISOU 1974  CA  MET A 120     1460   1688   1699    104    -15    -22       C  
ATOM   1975  C   MET A 120      62.957  75.819  44.300  1.00 12.52           C  
ANISOU 1975  C   MET A 120     1295   1764   1700    125     -9     54       C  
ATOM   1976  O   MET A 120      64.139  75.779  43.930  1.00 12.41           O  
ANISOU 1976  O   MET A 120     1264   1722   1730    118     68    -66       O  
ATOM   1977  CB  MET A 120      61.947  77.972  43.644  1.00 12.96           C  
ANISOU 1977  CB  MET A 120     1585   1834   1505    111   -207   -193       C  
ATOM   1978  CG  MET A 120      60.918  79.027  43.969  1.00 13.39           C  
ANISOU 1978  CG  MET A 120     1662   1838   1586    180     78   -151       C  
ATOM   1979  SD  MET A 120      59.400  78.401  44.722  1.00 12.82           S  
ANISOU 1979  SD  MET A 120     1448   1743   1681    154    -79    -99       S  
ATOM   1980  CE  MET A 120      58.933  77.168  43.530  1.00 13.32           C  
ANISOU 1980  CE  MET A 120     1672   1576   1812     52     49    109       C  
ATOM   1981  H   MET A 120      63.762  78.417  45.215  1.00 15.50           H  
ATOM   1982  HA  MET A 120      61.572  76.900  45.378  1.00 15.32           H  
ATOM   1983  HB2 MET A 120      62.737  78.425  43.307  1.00 15.56           H  
ATOM   1984  HB3 MET A 120      61.575  77.399  42.955  1.00 15.56           H  
ATOM   1985  HG2 MET A 120      61.312  79.659  44.590  1.00 16.07           H  
ATOM   1986  HG3 MET A 120      60.670  79.479  43.147  1.00 16.07           H  
ATOM   1987  HE1 MET A 120      58.095  76.764  43.805  1.00 15.99           H  
ATOM   1988  HE2 MET A 120      58.828  77.591  42.663  1.00 15.99           H  
ATOM   1989  HE3 MET A 120      59.627  76.492  43.486  1.00 15.99           H  
ATOM   1990  N   VAL A 121      62.124  74.786  44.215  1.00 12.82           N  
ANISOU 1990  N   VAL A 121     1300   1822   1747    203    -87     56       N  
ATOM   1991  CA  VAL A 121      62.511  73.468  43.722  1.00 12.65           C  
ANISOU 1991  CA  VAL A 121     1382   1848   1577     48    -90    -34       C  
ATOM   1992  C   VAL A 121      61.458  73.026  42.708  1.00 12.49           C  
ANISOU 1992  C   VAL A 121     1441   1793   1511     25   -156   -107       C  
ATOM   1993  O   VAL A 121      60.266  73.010  43.025  1.00 13.63           O  
ANISOU 1993  O   VAL A 121     1491   1962   1724    108    -69   -113       O  
ATOM   1994  CB  VAL A 121      62.589  72.456  44.884  1.00 13.22           C  
ANISOU 1994  CB  VAL A 121     1549   1833   1640    269   -180    176       C  
ATOM   1995  CG1 VAL A 121      63.011  71.092  44.358  1.00 14.45           C  
ANISOU 1995  CG1 VAL A 121     1965   1716   1807    252    -18    301       C  
ATOM   1996  CG2 VAL A 121      63.541  72.957  45.983  1.00 14.78           C  
ANISOU 1996  CG2 VAL A 121     1842   2091   1683    244   -325    221       C  
ATOM   1997  H   VAL A 121      61.297  74.829  44.446  1.00 15.39           H  
ATOM   1998  HA  VAL A 121      63.372  73.511  43.278  1.00 15.19           H  
ATOM   1999  HB  VAL A 121      61.712  72.364  45.289  1.00 15.87           H  
ATOM   2000 HG11 VAL A 121      63.191  70.505  45.109  1.00 17.34           H  
ATOM   2001 HG12 VAL A 121      62.293  70.726  43.817  1.00 17.34           H  
ATOM   2002 HG13 VAL A 121      63.811  71.195  43.819  1.00 17.34           H  
ATOM   2003 HG21 VAL A 121      63.614  72.277  46.672  1.00 17.75           H  
ATOM   2004 HG22 VAL A 121      64.413  73.127  45.593  1.00 17.75           H  
ATOM   2005 HG23 VAL A 121      63.184  73.775  46.363  1.00 17.75           H  
ATOM   2006  N   TYR A 122      61.894  72.654  41.505  1.00 12.14           N  
ANISOU 2006  N   TYR A 122     1499   1752   1361    283   -132   -143       N  
ATOM   2007  CA  TYR A 122      60.977  72.279  40.428  1.00 12.82           C  
ANISOU 2007  CA  TYR A 122     1614   1749   1510    -73    -70   -109       C  
ATOM   2008  C   TYR A 122      61.270  70.880  39.904  1.00 13.35           C  
ANISOU 2008  C   TYR A 122     1564   1663   1844     91     14   -206       C  
ATOM   2009  O   TYR A 122      62.370  70.613  39.394  1.00 13.54           O  
ANISOU 2009  O   TYR A 122     1713   1556   1877    256     -8   -300       O  
ATOM   2010  CB  TYR A 122      61.083  73.238  39.243  1.00 12.49           C  
ANISOU 2010  CB  TYR A 122     1597   1801   1346     99   -202    -35       C  
ATOM   2011  CG  TYR A 122      60.719  74.650  39.568  1.00 11.75           C  
ANISOU 2011  CG  TYR A 122     1389   1583   1492     84   -161   -109       C  
ATOM   2012  CD1 TYR A 122      59.393  75.065  39.586  1.00 12.81           C  
ANISOU 2012  CD1 TYR A 122     1378   1797   1693    -20   -187   -110       C  
ATOM   2013  CD2 TYR A 122      61.695  75.581  39.868  1.00 11.67           C  
ANISOU 2013  CD2 TYR A 122     1377   1639   1420   -192   -269    -70       C  
ATOM   2014  CE1 TYR A 122      59.066  76.377  39.893  1.00 13.06           C  
ANISOU 2014  CE1 TYR A 122     1422   1849   1690    172   -397   -204       C  
ATOM   2015  CE2 TYR A 122      61.382  76.886  40.184  1.00 11.82           C  
ANISOU 2015  CE2 TYR A 122     1356   1508   1628   -182   -322   -139       C  
ATOM   2016  CZ  TYR A 122      60.058  77.280  40.194  1.00 12.19           C  
ANISOU 2016  CZ  TYR A 122     1270   1587   1774    176   -193    -44       C  
ATOM   2017  OH  TYR A 122      59.697  78.568  40.504  1.00 12.85           O  
ANISOU 2017  OH  TYR A 122     1282   1650   1949     61   -292   -118       O  
ATOM   2018  H   TYR A 122      62.725  72.611  41.288  1.00 14.57           H  
ATOM   2019  HA  TYR A 122      60.088  72.291  40.815  1.00 15.40           H  
ATOM   2020  HB2 TYR A 122      61.998  73.236  38.922  1.00 14.99           H  
ATOM   2021  HB3 TYR A 122      60.485  72.933  38.542  1.00 14.99           H  
ATOM   2022  HD1 TYR A 122      58.718  74.456  39.390  1.00 15.38           H  
ATOM   2023  HD2 TYR A 122      62.587  75.320  39.856  1.00 14.02           H  
ATOM   2024  HE1 TYR A 122      58.176  76.647  39.894  1.00 15.68           H  
ATOM   2025  HE2 TYR A 122      62.055  77.494  40.387  1.00 14.19           H  
ATOM   2026  HH  TYR A 122      60.383  79.046  40.589  1.00 15.42           H  
ATOM   2027  N   GLY A 123      60.274  70.005  39.976  1.00 14.12           N  
ANISOU 2027  N   GLY A 123     1617   1704   2044     56    -26   -169       N  
ATOM   2028  CA  GLY A 123      60.337  68.767  39.248  1.00 13.58           C  
ANISOU 2028  CA  GLY A 123     1512   1711   1936     48     17   -397       C  
ATOM   2029  C   GLY A 123      60.098  68.983  37.772  1.00 14.14           C  
ANISOU 2029  C   GLY A 123     1620   1658   2094     75     19   -124       C  
ATOM   2030  O   GLY A 123      59.598  70.020  37.334  1.00 15.37           O  
ANISOU 2030  O   GLY A 123     1975   1679   2188     27   -170   -166       O  
ATOM   2031  H   GLY A 123      59.557  70.111  40.439  1.00 16.95           H  
ATOM   2032  HA2 GLY A 123      61.213  68.366  39.365  1.00 16.30           H  
ATOM   2033  HA3 GLY A 123      59.663  68.157  39.585  1.00 16.30           H  
ATOM   2034  N   ASP A 124      60.464  67.971  36.985  1.00 14.75           N  
ANISOU 2034  N   ASP A 124     1622   1710   2274    180      2   -166       N  
ATOM   2035  CA  ASP A 124      60.218  67.985  35.556  1.00 15.55           C  
ANISOU 2035  CA  ASP A 124     1747   1842   2319   -102   -169   -234       C  
ATOM   2036  C   ASP A 124      58.873  67.385  35.182  1.00 15.47           C  
ANISOU 2036  C   ASP A 124     1733   1756   2388     74   -295   -329       C  
ATOM   2037  O   ASP A 124      58.498  67.419  34.002  1.00 16.66           O  
ANISOU 2037  O   ASP A 124     2028   1929   2372     38   -316   -328       O  
ATOM   2038  CB  ASP A 124      61.307  67.193  34.825  1.00 16.18           C  
ANISOU 2038  CB  ASP A 124     1927   1906   2313   -192   -138   -478       C  
ATOM   2039  CG  ASP A 124      62.633  67.917  34.790  1.00 18.14           C  
ANISOU 2039  CG  ASP A 124     2052   2170   2669    -30   -124   -435       C  
ATOM   2040  OD1 ASP A 124      62.667  69.154  34.826  1.00 19.89           O  
ANISOU 2040  OD1 ASP A 124     2300   2365   2891   -258    142   -378       O  
ATOM   2041  OD2 ASP A 124      63.654  67.241  34.697  1.00 20.29           O  
ANISOU 2041  OD2 ASP A 124     2104   2383   3223     92   -162   -598       O  
ATOM   2042  H   ASP A 124      60.860  67.261  37.264  1.00 17.71           H  
ATOM   2043  HA  ASP A 124      60.244  68.906  35.254  1.00 18.67           H  
ATOM   2044  HB2 ASP A 124      61.440  66.346  35.278  1.00 19.42           H  
ATOM   2045  HB3 ASP A 124      61.025  67.039  33.910  1.00 19.42           H  
ATOM   2046  N   GLY A 125      58.144  66.842  36.149  1.00 16.15           N  
ANISOU 2046  N   GLY A 125     1883   1727   2525    -68   -225   -489       N  
ATOM   2047  CA  GLY A 125      56.934  66.106  35.859  1.00 17.43           C  
ANISOU 2047  CA  GLY A 125     1885   1893   2844   -127   -186   -569       C  
ATOM   2048  C   GLY A 125      57.221  64.769  35.211  1.00 19.09           C  
ANISOU 2048  C   GLY A 125     2057   1832   3363   -103    -95   -536       C  
ATOM   2049  O   GLY A 125      58.364  64.472  34.837  1.00 19.40           O  
ANISOU 2049  O   GLY A 125     2190   1839   3341    -20    -26   -581       O  
ATOM   2050  H   GLY A 125      58.335  66.889  36.986  1.00 19.38           H  
ATOM   2051  HA2 GLY A 125      56.447  65.949  36.684  1.00 20.92           H  
ATOM   2052  HA3 GLY A 125      56.377  66.625  35.258  1.00 20.92           H  
ATOM   2053  N   ASP A 126      56.190  63.945  35.071  1.00 20.18           N  
ANISOU 2053  N   ASP A 126     2114   1879   3676   -265   -239   -879       N  
ATOM   2054  CA  ASP A 126      56.318  62.648  34.425  1.00 22.79           C  
ANISOU 2054  CA  ASP A 126     2550   2136   3974   -180   -131  -1010       C  
ATOM   2055  C   ASP A 126      55.942  62.679  32.949  1.00 23.35           C  
ANISOU 2055  C   ASP A 126     2699   2247   3928     54      8  -1196       C  
ATOM   2056  O   ASP A 126      55.961  61.625  32.292  1.00 24.08           O  
ANISOU 2056  O   ASP A 126     2943   2220   3986    -80     77  -1237       O  
ATOM   2057  CB  ASP A 126      55.492  61.595  35.164  1.00 24.26           C  
ANISOU 2057  CB  ASP A 126     2595   2403   4220   -318   -186   -850       C  
ATOM   2058  CG  ASP A 126      54.011  61.892  35.162  1.00 24.36           C  
ANISOU 2058  CG  ASP A 126     2536   2433   4287   -461   -262   -761       C  
ATOM   2059  OD1 ASP A 126      53.549  62.721  34.356  1.00 25.15           O  
ANISOU 2059  OD1 ASP A 126     2395   2716   4442   -361   -449   -409       O  
ATOM   2060  OD2 ASP A 126      53.311  61.284  35.989  1.00 25.91           O  
ANISOU 2060  OD2 ASP A 126     2962   2477   4405   -416   -152   -871       O  
ATOM   2061  H   ASP A 126      55.394  64.119  35.346  1.00 24.23           H  
ATOM   2062  HA  ASP A 126      57.246  62.368  34.480  1.00 27.36           H  
ATOM   2063  HB2 ASP A 126      55.623  60.735  34.736  1.00 29.12           H  
ATOM   2064  HB3 ASP A 126      55.787  61.556  36.087  1.00 29.12           H  
ATOM   2065  N   GLY A 127      55.619  63.857  32.413  1.00 24.22           N  
ANISOU 2065  N   GLY A 127     2738   2464   3999    170    -61  -1252       N  
ATOM   2066  CA  GLY A 127      55.265  63.990  31.018  1.00 25.74           C  
ANISOU 2066  CA  GLY A 127     2951   2677   4153    424   -225  -1207       C  
ATOM   2067  C   GLY A 127      53.821  63.703  30.697  1.00 27.36           C  
ANISOU 2067  C   GLY A 127     3225   2871   4300    393   -541  -1248       C  
ATOM   2068  O   GLY A 127      53.396  63.953  29.564  1.00 29.42           O  
ANISOU 2068  O   GLY A 127     3595   3327   4258    543   -402  -1265       O  
ATOM   2069  H   GLY A 127      55.599  64.598  32.850  1.00 29.07           H  
ATOM   2070  HA2 GLY A 127      55.455  64.899  30.736  1.00 30.90           H  
ATOM   2071  HA3 GLY A 127      55.810  63.378  30.501  1.00 30.90           H  
ATOM   2072  N   GLN A 128      53.046  63.214  31.658  1.00 26.94           N  
ANISOU 2072  N   GLN A 128     2976   2704   4557    106   -676  -1296       N  
ATOM   2073  CA  GLN A 128      51.627  62.946  31.475  1.00 29.74           C  
ANISOU 2073  CA  GLN A 128     3206   3166   4930     24   -659  -1293       C  
ATOM   2074  C   GLN A 128      50.771  63.771  32.418  1.00 27.17           C  
ANISOU 2074  C   GLN A 128     2828   2677   4818   -225   -615  -1036       C  
ATOM   2075  O   GLN A 128      49.846  64.461  31.968  1.00 27.51           O  
ANISOU 2075  O   GLN A 128     2819   2737   4895   -267   -738  -1028       O  
ATOM   2076  CB  GLN A 128      51.364  61.449  31.685  1.00 35.57           C  
ANISOU 2076  CB  GLN A 128     3945   4058   5513    268   -445  -1550       C  
ATOM   2077  CG  GLN A 128      52.069  60.565  30.661  1.00 42.61           C  
ANISOU 2077  CG  GLN A 128     4837   5221   6132    369   -342  -1549       C  
ATOM   2078  CD  GLN A 128      51.604  60.839  29.239  1.00 48.42           C  
ANISOU 2078  CD  GLN A 128     5576   6162   6659    536   -191  -1655       C  
ATOM   2079  OE1 GLN A 128      50.468  61.271  29.013  1.00 50.71           O  
ANISOU 2079  OE1 GLN A 128     5862   6480   6925    522   -255  -1675       O  
ATOM   2080  NE2 GLN A 128      52.483  60.595  28.274  1.00 50.38           N  
ANISOU 2080  NE2 GLN A 128     5823   6516   6803    519    -58  -1682       N  
ATOM   2081  H   GLN A 128      53.329  63.025  32.447  1.00 32.34           H  
ATOM   2082  HA  GLN A 128      51.364  63.172  30.569  1.00 35.70           H  
ATOM   2083  HB2 GLN A 128      51.681  61.195  32.566  1.00 42.69           H  
ATOM   2084  HB3 GLN A 128      50.411  61.284  31.614  1.00 42.69           H  
ATOM   2085  HG2 GLN A 128      53.024  60.731  30.703  1.00 51.14           H  
ATOM   2086  HG3 GLN A 128      51.885  59.635  30.865  1.00 51.14           H  
ATOM   2087 HE21 GLN A 128      53.266  60.299  28.471  1.00 60.47           H  
ATOM   2088 HE22 GLN A 128      52.269  60.733  27.453  1.00 60.47           H  
ATOM   2089  N   THR A 129      51.057  63.725  33.719  1.00 25.79           N  
ANISOU 2089  N   THR A 129     2778   2356   4664   -399   -331   -830       N  
ATOM   2090  CA  THR A 129      50.370  64.585  34.672  1.00 25.43           C  
ANISOU 2090  CA  THR A 129     2769   2383   4510   -449   -162   -585       C  
ATOM   2091  C   THR A 129      50.892  66.012  34.583  1.00 22.29           C  
ANISOU 2091  C   THR A 129     2059   2415   3995   -249   -129   -660       C  
ATOM   2092  O   THR A 129      50.102  66.965  34.613  1.00 22.04           O  
ANISOU 2092  O   THR A 129     2002   2664   3709     72    -70   -937       O  
ATOM   2093  CB  THR A 129      50.562  64.045  36.091  1.00 29.53           C  
ANISOU 2093  CB  THR A 129     3629   2705   4888   -737    -79   -348       C  
ATOM   2094  OG1 THR A 129      50.066  62.699  36.159  1.00 33.77           O  
ANISOU 2094  OG1 THR A 129     4337   3223   5272   -819   -135   -184       O  
ATOM   2095  CG2 THR A 129      49.817  64.887  37.097  1.00 31.29           C  
ANISOU 2095  CG2 THR A 129     3852   3102   4937   -648    100    -75       C  
ATOM   2096  H   THR A 129      51.643  63.205  34.074  1.00 30.95           H  
ATOM   2097  HA  THR A 129      49.420  64.588  34.477  1.00 30.52           H  
ATOM   2098  HB  THR A 129      51.506  64.066  36.313  1.00 35.45           H  
ATOM   2099  HG1 THR A 129      50.186  62.387  36.930  1.00 40.53           H  
ATOM   2100 HG21 THR A 129      49.843  64.462  37.969  1.00 37.56           H  
ATOM   2101 HG22 THR A 129      50.225  65.764  37.162  1.00 37.56           H  
ATOM   2102 HG23 THR A 129      48.892  64.989  36.825  1.00 37.56           H  
ATOM   2103  N   PHE A 130      52.218  66.169  34.479  1.00 19.93           N  
ANISOU 2103  N   PHE A 130     1695   2182   3696   -178   -181   -668       N  
ATOM   2104  CA  PHE A 130      52.820  67.481  34.364  1.00 18.61           C  
ANISOU 2104  CA  PHE A 130     1848   2090   3134   -139   -321   -481       C  
ATOM   2105  C   PHE A 130      53.980  67.433  33.383  1.00 17.78           C  
ANISOU 2105  C   PHE A 130     1920   1912   2924     54   -345   -557       C  
ATOM   2106  O   PHE A 130      54.638  66.397  33.222  1.00 18.56           O  
ANISOU 2106  O   PHE A 130     2124   1839   3089    155   -173   -459       O  
ATOM   2107  CB  PHE A 130      53.447  67.964  35.680  1.00 19.23           C  
ANISOU 2107  CB  PHE A 130     1942   2334   3032     26   -378   -213       C  
ATOM   2108  CG  PHE A 130      52.466  68.453  36.690  1.00 19.34           C  
ANISOU 2108  CG  PHE A 130     2023   2480   2843    238   -319   -308       C  
ATOM   2109  CD1 PHE A 130      51.892  69.707  36.577  1.00 18.67           C  
ANISOU 2109  CD1 PHE A 130     1773   2583   2737    178   -198   -466       C  
ATOM   2110  CD2 PHE A 130      52.151  67.676  37.781  1.00 22.55           C  
ANISOU 2110  CD2 PHE A 130     2234   2956   3376    741    115   -114       C  
ATOM   2111  CE1 PHE A 130      51.015  70.169  37.532  1.00 20.69           C  
ANISOU 2111  CE1 PHE A 130     2066   2801   2993    176   -188   -342       C  
ATOM   2112  CE2 PHE A 130      51.276  68.136  38.739  1.00 24.25           C  
ANISOU 2112  CE2 PHE A 130     2470   3228   3514    706    222   -186       C  
ATOM   2113  CZ  PHE A 130      50.696  69.377  38.599  1.00 22.84           C  
ANISOU 2113  CZ  PHE A 130     2293   3033   3350    581      6   -222       C  
ATOM   2114  H   PHE A 130      52.782  65.521  34.474  1.00 23.92           H  
ATOM   2115  HA  PHE A 130      52.120  68.084  34.067  1.00 22.34           H  
ATOM   2116  HB2 PHE A 130      53.934  67.226  36.079  1.00 23.09           H  
ATOM   2117  HB3 PHE A 130      54.054  68.694  35.484  1.00 23.09           H  
ATOM   2118  HD1 PHE A 130      52.102  70.244  35.847  1.00 22.41           H  
ATOM   2119  HD2 PHE A 130      52.531  66.833  37.872  1.00 27.06           H  
ATOM   2120  HE1 PHE A 130      50.640  71.017  37.452  1.00 24.83           H  
ATOM   2121  HE2 PHE A 130      51.077  67.610  39.479  1.00 29.10           H  
ATOM   2122  HZ  PHE A 130      50.085  69.677  39.232  1.00 27.41           H  
ATOM   2123  N   ILE A 131      54.230  68.574  32.747  1.00 17.27           N  
ANISOU 2123  N   ILE A 131     1955   1945   2661     42   -526   -534       N  
ATOM   2124  CA  ILE A 131      55.516  68.875  32.117  1.00 16.40           C  
ANISOU 2124  CA  ILE A 131     1769   1936   2527     43   -432   -590       C  
ATOM   2125  C   ILE A 131      56.285  69.745  33.107  1.00 15.81           C  
ANISOU 2125  C   ILE A 131     1732   2019   2255    244   -120   -515       C  
ATOM   2126  O   ILE A 131      55.750  70.072  34.174  1.00 15.79           O  
ANISOU 2126  O   ILE A 131     1698   2056   2244    -59   -103   -434       O  
ATOM   2127  CB  ILE A 131      55.329  69.546  30.750  1.00 17.64           C  
ANISOU 2127  CB  ILE A 131     2046   2014   2645    145   -359   -719       C  
ATOM   2128  CG1 ILE A 131      54.631  70.900  30.900  1.00 18.56           C  
ANISOU 2128  CG1 ILE A 131     2132   2170   2752    248   -324   -377       C  
ATOM   2129  CG2 ILE A 131      54.520  68.630  29.809  1.00 20.27           C  
ANISOU 2129  CG2 ILE A 131     2253   2514   2934    266   -344   -764       C  
ATOM   2130  CD1 ILE A 131      54.398  71.595  29.567  1.00 20.70           C  
ANISOU 2130  CD1 ILE A 131     2287   2621   2957    192   -170   -444       C  
ATOM   2131  H   ILE A 131      53.655  69.209  32.663  1.00 20.73           H  
ATOM   2132  HA  ILE A 131      56.024  68.066  31.950  1.00 19.69           H  
ATOM   2133  HB  ILE A 131      56.207  69.695  30.365  1.00 21.18           H  
ATOM   2134 HG12 ILE A 131      53.768  70.766  31.323  1.00 22.29           H  
ATOM   2135 HG13 ILE A 131      55.182  71.480  31.448  1.00 22.29           H  
ATOM   2136 HG21 ILE A 131      54.592  68.966  28.902  1.00 24.33           H  
ATOM   2137 HG22 ILE A 131      54.880  67.731  29.858  1.00 24.33           H  
ATOM   2138 HG23 ILE A 131      53.592  68.631  30.089  1.00 24.33           H  
ATOM   2139 HD11 ILE A 131      54.115  72.508  29.732  1.00 24.85           H  
ATOM   2140 HD12 ILE A 131      55.226  71.592  29.061  1.00 24.85           H  
ATOM   2141 HD13 ILE A 131      53.710  71.118  29.078  1.00 24.85           H  
ATOM   2142  N   PRO A 132      57.521  70.149  32.818  1.00 16.00           N  
ANISOU 2142  N   PRO A 132     1742   2123   2212    229   -110   -406       N  
ATOM   2143  CA  PRO A 132      58.313  70.801  33.870  1.00 14.59           C  
ANISOU 2143  CA  PRO A 132     1568   1935   2041     94   -302   -424       C  
ATOM   2144  C   PRO A 132      57.609  72.017  34.458  1.00 13.78           C  
ANISOU 2144  C   PRO A 132     1426   1943   1867    289   -267   -192       C  
ATOM   2145  O   PRO A 132      57.133  72.901  33.737  1.00 14.27           O  
ANISOU 2145  O   PRO A 132     1724   1894   1804    274   -300   -245       O  
ATOM   2146  CB  PRO A 132      59.634  71.143  33.166  1.00 14.92           C  
ANISOU 2146  CB  PRO A 132     1580   2030   2059     37   -234   -662       C  
ATOM   2147  CG  PRO A 132      59.785  70.013  32.173  1.00 15.95           C  
ANISOU 2147  CG  PRO A 132     1880   1986   2194     33    -67   -538       C  
ATOM   2148  CD  PRO A 132      58.363  69.758  31.672  1.00 16.94           C  
ANISOU 2148  CD  PRO A 132     2025   2118   2294    204   -128   -460       C  
ATOM   2149  HA  PRO A 132      58.494  70.180  34.593  1.00 17.52           H  
ATOM   2150  HB2 PRO A 132      59.569  72.001  32.720  1.00 17.91           H  
ATOM   2151  HB3 PRO A 132      60.365  71.155  33.804  1.00 17.91           H  
ATOM   2152  HG2 PRO A 132      60.368  70.284  31.446  1.00 19.15           H  
ATOM   2153  HG3 PRO A 132      60.146  69.228  32.613  1.00 19.15           H  
ATOM   2154  HD2 PRO A 132      58.167  70.307  30.897  1.00 20.34           H  
ATOM   2155  HD3 PRO A 132      58.237  68.821  31.456  1.00 20.34           H  
ATOM   2156  N   LEU A 133      57.491  72.030  35.787  1.00 13.91           N  
ANISOU 2156  N   LEU A 133     1335   1988   1961    201    -84   -247       N  
ATOM   2157  CA  LEU A 133      56.495  72.880  36.427  1.00 13.58           C  
ANISOU 2157  CA  LEU A 133     1534   1774   1851    119      0   -286       C  
ATOM   2158  C   LEU A 133      56.875  74.355  36.421  1.00 13.77           C  
ANISOU 2158  C   LEU A 133     1530   1944   1759     42    -37   -309       C  
ATOM   2159  O   LEU A 133      55.987  75.206  36.560  1.00 14.52           O  
ANISOU 2159  O   LEU A 133     1596   1985   1935    205    -49   -241       O  
ATOM   2160  CB  LEU A 133      56.192  72.393  37.847  1.00 15.85           C  
ANISOU 2160  CB  LEU A 133     1936   1843   2242     -6     85   -282       C  
ATOM   2161  CG  LEU A 133      55.268  71.163  37.877  1.00 17.61           C  
ANISOU 2161  CG  LEU A 133     2188   1871   2634     -5    178   -294       C  
ATOM   2162  CD1 LEU A 133      56.017  69.839  37.732  1.00 16.59           C  
ANISOU 2162  CD1 LEU A 133     1977   1748   2577    120    -32   -356       C  
ATOM   2163  CD2 LEU A 133      54.371  71.160  39.110  1.00 19.40           C  
ANISOU 2163  CD2 LEU A 133     2089   2257   3026    -18    243   -474       C  
ATOM   2164  H   LEU A 133      57.967  71.563  36.329  1.00 16.70           H  
ATOM   2165  HA  LEU A 133      55.669  72.804  35.924  1.00 16.30           H  
ATOM   2166  HB2 LEU A 133      57.025  72.153  38.281  1.00 19.03           H  
ATOM   2167  HB3 LEU A 133      55.756  73.108  38.337  1.00 19.03           H  
ATOM   2168  HG  LEU A 133      54.697  71.231  37.096  1.00 21.15           H  
ATOM   2169 HD11 LEU A 133      55.381  69.109  37.788  1.00 19.91           H  
ATOM   2170 HD12 LEU A 133      56.464  69.822  36.871  1.00 19.91           H  
ATOM   2171 HD13 LEU A 133      56.669  69.765  38.446  1.00 19.91           H  
ATOM   2172 HD21 LEU A 133      53.812  70.367  39.092  1.00 23.29           H  
ATOM   2173 HD22 LEU A 133      54.927  71.155  39.905  1.00 23.29           H  
ATOM   2174 HD23 LEU A 133      53.816  71.956  39.098  1.00 23.29           H  
ATOM   2175  N   SER A 134      58.154  74.683  36.234  1.00 12.97           N  
ANISOU 2175  N   SER A 134     1458   1894   1577    -81   -164   -194       N  
ATOM   2176  CA  SER A 134      58.535  76.078  36.094  1.00 13.35           C  
ANISOU 2176  CA  SER A 134     1506   1952   1616     66   -188   -218       C  
ATOM   2177  C   SER A 134      57.936  76.703  34.835  1.00 12.51           C  
ANISOU 2177  C   SER A 134     1593   1761   1398    120   -239   -180       C  
ATOM   2178  O   SER A 134      57.990  77.927  34.689  1.00 12.68           O  
ANISOU 2178  O   SER A 134     1704   1707   1408     84    -92   -186       O  
ATOM   2179  CB  SER A 134      60.053  76.203  36.096  1.00 12.89           C  
ANISOU 2179  CB  SER A 134     1383   1953   1561    319    -23   -233       C  
ATOM   2180  OG  SER A 134      60.610  75.526  34.989  1.00 13.87           O  
ANISOU 2180  OG  SER A 134     1471   2224   1573    190   -182   -358       O  
ATOM   2181  H   SER A 134      58.806  74.124  36.186  1.00 15.58           H  
ATOM   2182  HA  SER A 134      58.212  76.584  36.855  1.00 16.03           H  
ATOM   2183  HB2 SER A 134      60.294  77.141  36.047  1.00 15.47           H  
ATOM   2184  HB3 SER A 134      60.402  75.813  36.913  1.00 15.47           H  
ATOM   2185  HG  SER A 134      61.443  75.637  34.974  1.00 16.65           H  
ATOM   2186  N   GLY A 135      57.378  75.901  33.923  1.00 13.88           N  
ANISOU 2186  N   GLY A 135     1739   1859   1677    326   -406   -295       N  
ATOM   2187  CA  GLY A 135      56.668  76.446  32.785  1.00 13.96           C  
ANISOU 2187  CA  GLY A 135     1732   1921   1652    306   -347   -304       C  
ATOM   2188  C   GLY A 135      55.400  77.198  33.131  1.00 14.15           C  
ANISOU 2188  C   GLY A 135     1696   2092   1588    270   -262    -87       C  
ATOM   2189  O   GLY A 135      54.862  77.886  32.258  1.00 14.90           O  
ANISOU 2189  O   GLY A 135     1744   2322   1597    278   -412   -122       O  
ATOM   2190  H   GLY A 135      57.401  75.042  33.947  1.00 16.67           H  
ATOM   2191  HA2 GLY A 135      57.256  77.057  32.315  1.00 16.76           H  
ATOM   2192  HA3 GLY A 135      56.428  75.718  32.191  1.00 16.76           H  
ATOM   2193  N   GLY A 136      54.913  77.082  34.367  1.00 13.93           N  
ANISOU 2193  N   GLY A 136     1634   2078   1580    405   -164   -323       N  
ATOM   2194  CA  GLY A 136      53.703  77.773  34.782  1.00 13.27           C  
ANISOU 2194  CA  GLY A 136     1663   1776   1603    277   -381   -310       C  
ATOM   2195  C   GLY A 136      54.003  78.963  35.669  1.00 12.97           C  
ANISOU 2195  C   GLY A 136     1571   1884   1473    234   -333   -116       C  
ATOM   2196  O   GLY A 136      54.411  78.820  36.830  1.00 13.19           O  
ANISOU 2196  O   GLY A 136     1652   2022   1338    254   -295     33       O  
ATOM   2197  H   GLY A 136      55.271  76.604  34.986  1.00 16.72           H  
ATOM   2198  HA2 GLY A 136      53.227  78.087  33.997  1.00 15.93           H  
ATOM   2199  HA3 GLY A 136      53.134  77.159  35.272  1.00 15.93           H  
ATOM   2200  N   ILE A 137      53.810  80.157  35.112  1.00 13.11           N  
ANISOU 2200  N   ILE A 137     1567   1823   1591    181   -275    -44       N  
ATOM   2201  CA  ILE A 137      54.120  81.364  35.868  1.00 12.29           C  
ANISOU 2201  CA  ILE A 137     1455   1717   1497     69   -345     78       C  
ATOM   2202  C   ILE A 137      53.290  81.428  37.145  1.00 12.10           C  
ANISOU 2202  C   ILE A 137     1373   1726   1499    149   -305    -87       C  
ATOM   2203  O   ILE A 137      53.774  81.886  38.185  1.00 13.00           O  
ANISOU 2203  O   ILE A 137     1522   1727   1690    112   -257    -70       O  
ATOM   2204  CB  ILE A 137      54.001  82.628  34.995  1.00 13.94           C  
ANISOU 2204  CB  ILE A 137     1558   2030   1710    242   -219    141       C  
ATOM   2205  CG1 ILE A 137      54.589  83.811  35.759  1.00 13.87           C  
ANISOU 2205  CG1 ILE A 137     1689   1964   1617     25   -117    260       C  
ATOM   2206  CG2 ILE A 137      52.571  82.886  34.567  1.00 14.30           C  
ANISOU 2206  CG2 ILE A 137     1614   2222   1598    506   -217    197       C  
ATOM   2207  CD1 ILE A 137      54.602  85.101  34.956  1.00 16.16           C  
ANISOU 2207  CD1 ILE A 137     2216   2085   1839     39   -237    168       C  
ATOM   2208  H   ILE A 137      53.508  80.293  34.318  1.00 15.74           H  
ATOM   2209  HA  ILE A 137      55.050  81.319  36.139  1.00 14.75           H  
ATOM   2210  HB  ILE A 137      54.506  82.495  34.178  1.00 16.74           H  
ATOM   2211 HG12 ILE A 137      54.060  83.963  36.557  1.00 16.65           H  
ATOM   2212 HG13 ILE A 137      55.504  83.603  36.002  1.00 16.65           H  
ATOM   2213 HG21 ILE A 137      52.563  83.597  33.907  1.00 17.17           H  
ATOM   2214 HG22 ILE A 137      52.205  82.074  34.184  1.00 17.17           H  
ATOM   2215 HG23 ILE A 137      52.052  83.149  35.343  1.00 17.17           H  
ATOM   2216 HD11 ILE A 137      55.098  85.774  35.447  1.00 19.40           H  
ATOM   2217 HD12 ILE A 137      55.027  84.936  34.100  1.00 19.40           H  
ATOM   2218 HD13 ILE A 137      53.688  85.397  34.819  1.00 19.40           H  
ATOM   2219  N   ASP A 138      52.024  81.003  37.085  1.00 12.35           N  
ANISOU 2219  N   ASP A 138     1350   1815   1527    137   -338    -67       N  
ATOM   2220  CA  ASP A 138      51.200  80.994  38.288  1.00 11.78           C  
ANISOU 2220  CA  ASP A 138     1452   1599   1426    180   -277   -204       C  
ATOM   2221  C   ASP A 138      51.731  80.030  39.345  1.00 11.28           C  
ANISOU 2221  C   ASP A 138     1397   1622   1265    285   -320   -119       C  
ATOM   2222  O   ASP A 138      51.627  80.313  40.537  1.00 12.29           O  
ANISOU 2222  O   ASP A 138     1494   1784   1392     68   -197   -184       O  
ATOM   2223  CB  ASP A 138      49.713  80.777  37.988  1.00 11.85           C  
ANISOU 2223  CB  ASP A 138     1434   1626   1444    240    -71    -78       C  
ATOM   2224  CG  ASP A 138      49.400  79.529  37.154  1.00 12.75           C  
ANISOU 2224  CG  ASP A 138     1556   1838   1452    313   -273    -38       C  
ATOM   2225  OD1 ASP A 138      50.317  78.774  36.762  1.00 14.24           O  
ANISOU 2225  OD1 ASP A 138     1689   2113   1610    287   -481   -492       O  
ATOM   2226  OD2 ASP A 138      48.183  79.335  36.865  1.00 12.57           O  
ANISOU 2226  OD2 ASP A 138     1485   1935   1355    213   -327   -206       O  
ATOM   2227  H   ASP A 138      51.627  80.722  36.376  1.00 14.83           H  
ATOM   2228  HA  ASP A 138      51.242  81.884  38.671  1.00 14.15           H  
ATOM   2229  HB2 ASP A 138      49.238  80.692  38.830  1.00 14.23           H  
ATOM   2230  HB3 ASP A 138      49.382  81.546  37.498  1.00 14.23           H  
ATOM   2231  N   VAL A 139      52.312  78.892  38.930  1.00 12.00           N  
ANISOU 2231  N   VAL A 139     1462   1624   1474    230   -422   -240       N  
ATOM   2232  CA  VAL A 139      52.926  77.969  39.890  1.00 11.84           C  
ANISOU 2232  CA  VAL A 139     1422   1634   1442    160   -412    -98       C  
ATOM   2233  C   VAL A 139      54.143  78.610  40.551  1.00 12.07           C  
ANISOU 2233  C   VAL A 139     1431   1649   1505    116   -350    141       C  
ATOM   2234  O   VAL A 139      54.307  78.555  41.781  1.00 12.39           O  
ANISOU 2234  O   VAL A 139     1499   1657   1550    142   -375     66       O  
ATOM   2235  CB  VAL A 139      53.302  76.655  39.175  1.00 13.83           C  
ANISOU 2235  CB  VAL A 139     1798   1558   1900    222   -587   -162       C  
ATOM   2236  CG1 VAL A 139      54.092  75.726  40.109  1.00 14.44           C  
ANISOU 2236  CG1 VAL A 139     2104   1355   2028    113   -284   -205       C  
ATOM   2237  CG2 VAL A 139      52.069  75.933  38.631  1.00 16.05           C  
ANISOU 2237  CG2 VAL A 139     2241   1815   2042    -33   -642   -265       C  
ATOM   2238  H   VAL A 139      52.363  78.636  38.111  1.00 14.41           H  
ATOM   2239  HA  VAL A 139      52.283  77.772  40.589  1.00 14.21           H  
ATOM   2240  HB  VAL A 139      53.866  76.885  38.420  1.00 16.61           H  
ATOM   2241 HG11 VAL A 139      54.138  74.842  39.711  1.00 17.34           H  
ATOM   2242 HG12 VAL A 139      54.987  76.082  40.226  1.00 17.34           H  
ATOM   2243 HG13 VAL A 139      53.639  75.680  40.965  1.00 17.34           H  
ATOM   2244 HG21 VAL A 139      52.347  75.105  38.209  1.00 19.27           H  
ATOM   2245 HG22 VAL A 139      51.464  75.743  39.365  1.00 19.27           H  
ATOM   2246 HG23 VAL A 139      51.630  76.504  37.981  1.00 19.27           H  
ATOM   2247  N   VAL A 140      55.017  79.202  39.741  1.00 12.19           N  
ANISOU 2247  N   VAL A 140     1318   1635   1677     60   -309     69       N  
ATOM   2248  CA  VAL A 140      56.202  79.893  40.248  1.00 12.21           C  
ANISOU 2248  CA  VAL A 140     1409   1688   1542    206   -245    -64       C  
ATOM   2249  C   VAL A 140      55.789  80.949  41.274  1.00 11.93           C  
ANISOU 2249  C   VAL A 140     1328   1642   1562    116   -339   -178       C  
ATOM   2250  O   VAL A 140      56.319  81.003  42.397  1.00 12.03           O  
ANISOU 2250  O   VAL A 140     1359   1715   1497    104   -213   -149       O  
ATOM   2251  CB  VAL A 140      56.982  80.515  39.069  1.00 11.68           C  
ANISOU 2251  CB  VAL A 140     1392   1590   1457    174   -258   -217       C  
ATOM   2252  CG1 VAL A 140      58.090  81.447  39.597  1.00 12.44           C  
ANISOU 2252  CG1 VAL A 140     1561   1628   1536    -61   -222   -100       C  
ATOM   2253  CG2 VAL A 140      57.519  79.420  38.114  1.00 13.05           C  
ANISOU 2253  CG2 VAL A 140     1585   1705   1667    305    -60   -104       C  
ATOM   2254  H   VAL A 140      54.949  79.220  38.883  1.00 14.63           H  
ATOM   2255  HA  VAL A 140      56.783  79.258  40.695  1.00 14.66           H  
ATOM   2256  HB  VAL A 140      56.383  81.061  38.536  1.00 14.03           H  
ATOM   2257 HG11 VAL A 140      58.701  81.654  38.872  1.00 14.93           H  
ATOM   2258 HG12 VAL A 140      57.684  82.263  39.930  1.00 14.93           H  
ATOM   2259 HG13 VAL A 140      58.566  80.998  40.313  1.00 14.93           H  
ATOM   2260 HG21 VAL A 140      58.029  79.842  37.404  1.00 15.66           H  
ATOM   2261 HG22 VAL A 140      58.087  78.815  38.615  1.00 15.66           H  
ATOM   2262 HG23 VAL A 140      56.768  78.934  37.737  1.00 15.66           H  
ATOM   2263  N   ALA A 141      54.866  81.834  40.883  1.00 11.97           N  
ANISOU 2263  N   ALA A 141     1354   1470   1724    179   -254   -169       N  
ATOM   2264  CA  ALA A 141      54.465  82.924  41.766  1.00 11.88           C  
ANISOU 2264  CA  ALA A 141     1371   1515   1626     40   -195     45       C  
ATOM   2265  C   ALA A 141      53.638  82.431  42.954  1.00 10.82           C  
ANISOU 2265  C   ALA A 141     1132   1517   1462    -16   -162    104       C  
ATOM   2266  O   ALA A 141      53.734  83.010  44.045  1.00 12.18           O  
ANISOU 2266  O   ALA A 141     1430   1610   1587    102   -213   -148       O  
ATOM   2267  CB  ALA A 141      53.718  83.968  40.950  1.00 12.28           C  
ANISOU 2267  CB  ALA A 141     1473   1325   1868    148    -58     45       C  
ATOM   2268  H   ALA A 141      54.463  81.826  40.123  1.00 14.37           H  
ATOM   2269  HA  ALA A 141      55.252  83.347  42.144  1.00 14.26           H  
ATOM   2270  HB1 ALA A 141      53.338  84.627  41.552  1.00 14.75           H  
ATOM   2271  HB2 ALA A 141      54.339  84.396  40.340  1.00 14.75           H  
ATOM   2272  HB3 ALA A 141      53.011  83.530  40.450  1.00 14.75           H  
ATOM   2273  N   HIS A 142      52.836  81.373  42.773  1.00 10.95           N  
ANISOU 2273  N   HIS A 142     1263   1528   1370    -13   -122     19       N  
ATOM   2274  CA  HIS A 142      52.111  80.773  43.896  1.00 11.18           C  
ANISOU 2274  CA  HIS A 142     1342   1570   1337      0   -285   -132       C  
ATOM   2275  C   HIS A 142      53.100  80.341  44.983  1.00 11.65           C  
ANISOU 2275  C   HIS A 142     1407   1540   1478     31   -149    -87       C  
ATOM   2276  O   HIS A 142      52.954  80.687  46.164  1.00 11.44           O  
ANISOU 2276  O   HIS A 142     1378   1464   1504     90   -195    -34       O  
ATOM   2277  CB  HIS A 142      51.309  79.557  43.376  1.00 11.51           C  
ANISOU 2277  CB  HIS A 142     1335   1588   1451     77   -304   -210       C  
ATOM   2278  CG  HIS A 142      50.703  78.704  44.461  1.00 10.96           C  
ANISOU 2278  CG  HIS A 142     1278   1367   1518    -74   -233    -48       C  
ATOM   2279  ND1 HIS A 142      49.348  78.617  44.665  1.00 11.43           N  
ANISOU 2279  ND1 HIS A 142     1386   1374   1583   -146   -276     27       N  
ATOM   2280  CD2 HIS A 142      51.270  77.888  45.392  1.00 12.10           C  
ANISOU 2280  CD2 HIS A 142     1306   1560   1731     -7   -206   -144       C  
ATOM   2281  CE1 HIS A 142      49.098  77.801  45.674  1.00 12.43           C  
ANISOU 2281  CE1 HIS A 142     1452   1409   1861   -110   -198     78       C  
ATOM   2282  NE2 HIS A 142      50.250  77.358  46.151  1.00 11.99           N  
ANISOU 2282  NE2 HIS A 142     1421   1418   1715     38   -235   -143       N  
ATOM   2283  H   HIS A 142      52.696  80.987  42.017  1.00 13.15           H  
ATOM   2284  HA  HIS A 142      51.491  81.413  44.280  1.00 13.43           H  
ATOM   2285  HB2 HIS A 142      50.585  79.880  42.816  1.00 13.82           H  
ATOM   2286  HB3 HIS A 142      51.904  78.994  42.856  1.00 13.82           H  
ATOM   2287  HD1 HIS A 142      48.751  79.032  44.205  1.00 13.73           H  
ATOM   2288  HD2 HIS A 142      52.179  77.720  45.496  1.00 14.53           H  
ATOM   2289  HE1 HIS A 142      48.254  77.576  45.994  1.00 14.92           H  
ATOM   2290  N   GLU A 143      54.138  79.610  44.586  1.00 12.56           N  
ANISOU 2290  N   GLU A 143     1261   1773   1737    180   -115     26       N  
ATOM   2291  CA  GLU A 143      55.083  79.108  45.573  1.00 11.45           C  
ANISOU 2291  CA  GLU A 143     1123   1631   1595    200   -155    181       C  
ATOM   2292  C   GLU A 143      55.926  80.223  46.177  1.00 11.60           C  
ANISOU 2292  C   GLU A 143     1238   1715   1456     71   -166    145       C  
ATOM   2293  O   GLU A 143      56.160  80.225  47.390  1.00 11.95           O  
ANISOU 2293  O   GLU A 143     1243   1765   1533    -18   -174    134       O  
ATOM   2294  CB  GLU A 143      55.948  78.003  44.977  1.00 12.55           C  
ANISOU 2294  CB  GLU A 143     1318   1572   1878    224   -170    -51       C  
ATOM   2295  CG  GLU A 143      55.138  76.749  44.655  1.00 13.60           C  
ANISOU 2295  CG  GLU A 143     1551   1502   2116    118   -417    -39       C  
ATOM   2296  CD  GLU A 143      54.592  76.068  45.910  1.00 15.25           C  
ANISOU 2296  CD  GLU A 143     1487   1682   2626   -117   -214     96       C  
ATOM   2297  OE1 GLU A 143      55.260  76.095  46.964  1.00 15.01           O  
ANISOU 2297  OE1 GLU A 143     1791   1773   2139    -75    238    -67       O  
ATOM   2298  OE2 GLU A 143      53.491  75.507  45.842  1.00 18.54           O  
ANISOU 2298  OE2 GLU A 143     1690   1988   3368    -44   -301    496       O  
ATOM   2299  H   GLU A 143      54.314  79.395  43.772  1.00 15.07           H  
ATOM   2300  HA  GLU A 143      54.580  78.712  46.302  1.00 13.74           H  
ATOM   2301  HB2 GLU A 143      56.350  78.323  44.154  1.00 15.07           H  
ATOM   2302  HB3 GLU A 143      56.640  77.762  45.613  1.00 15.07           H  
ATOM   2303  HG2 GLU A 143      54.386  76.992  44.093  1.00 16.33           H  
ATOM   2304  HG3 GLU A 143      55.707  76.114  44.192  1.00 16.33           H  
ATOM   2305  N   LEU A 144      56.387  81.182  45.363  1.00 11.22           N  
ANISOU 2305  N   LEU A 144     1218   1702   1343   -126   -223     62       N  
ATOM   2306  CA  LEU A 144      57.130  82.299  45.952  1.00 11.51           C  
ANISOU 2306  CA  LEU A 144     1174   1686   1514   -192   -283    -83       C  
ATOM   2307  C   LEU A 144      56.259  83.100  46.908  1.00 12.14           C  
ANISOU 2307  C   LEU A 144     1324   1773   1515   -210   -197   -134       C  
ATOM   2308  O   LEU A 144      56.776  83.695  47.863  1.00 12.98           O  
ANISOU 2308  O   LEU A 144     1247   1901   1784    -98   -269   -391       O  
ATOM   2309  CB  LEU A 144      57.729  83.203  44.874  1.00 12.45           C  
ANISOU 2309  CB  LEU A 144     1234   1752   1746     14   -260     52       C  
ATOM   2310  CG  LEU A 144      58.955  82.606  44.161  1.00 12.41           C  
ANISOU 2310  CG  LEU A 144     1214   1818   1684     64   -136     15       C  
ATOM   2311  CD1 LEU A 144      59.307  83.348  42.909  1.00 13.95           C  
ANISOU 2311  CD1 LEU A 144     1583   1897   1822     73    -22     78       C  
ATOM   2312  CD2 LEU A 144      60.184  82.539  45.089  1.00 13.81           C  
ANISOU 2312  CD2 LEU A 144     1370   1932   1946   -139   -201    136       C  
ATOM   2313  H   LEU A 144      56.288  81.208  44.509  1.00 13.47           H  
ATOM   2314  HA  LEU A 144      57.877  81.936  46.453  1.00 13.82           H  
ATOM   2315  HB2 LEU A 144      57.051  83.373  44.201  1.00 14.95           H  
ATOM   2316  HB3 LEU A 144      58.004  84.037  45.286  1.00 14.95           H  
ATOM   2317  HG  LEU A 144      58.712  81.701  43.911  1.00 14.90           H  
ATOM   2318 HD11 LEU A 144      60.072  82.920  42.493  1.00 16.75           H  
ATOM   2319 HD12 LEU A 144      58.548  83.326  42.306  1.00 16.75           H  
ATOM   2320 HD13 LEU A 144      59.523  84.266  43.136  1.00 16.75           H  
ATOM   2321 HD21 LEU A 144      60.958  82.273  44.569  1.00 16.58           H  
ATOM   2322 HD22 LEU A 144      60.333  83.414  45.480  1.00 16.58           H  
ATOM   2323 HD23 LEU A 144      60.016  81.888  45.789  1.00 16.58           H  
ATOM   2324  N   THR A 145      54.945  83.139  46.660  1.00 11.98           N  
ANISOU 2324  N   THR A 145     1615   1618   1319    -63     63   -161       N  
ATOM   2325  CA  THR A 145      54.046  83.836  47.577  1.00 10.71           C  
ANISOU 2325  CA  THR A 145     1452   1325   1294    -85   -109   -215       C  
ATOM   2326  C   THR A 145      53.950  83.117  48.919  1.00 11.54           C  
ANISOU 2326  C   THR A 145     1502   1453   1428     39   -186    -36       C  
ATOM   2327  O   THR A 145      53.726  83.771  49.936  1.00 12.75           O  
ANISOU 2327  O   THR A 145     1549   1801   1494    132   -257    -48       O  
ATOM   2328  CB  THR A 145      52.692  84.043  46.909  1.00 11.30           C  
ANISOU 2328  CB  THR A 145     1402   1308   1583    -26   -167     33       C  
ATOM   2329  OG1 THR A 145      52.858  84.902  45.773  1.00 12.40           O  
ANISOU 2329  OG1 THR A 145     1608   1476   1626     -6    -58    -92       O  
ATOM   2330  CG2 THR A 145      51.682  84.692  47.839  1.00 11.66           C  
ANISOU 2330  CG2 THR A 145     1609   1218   1602      3   -195    -36       C  
ATOM   2331  H   THR A 145      54.557  82.778  45.983  1.00 14.39           H  
ATOM   2332  HA  THR A 145      54.388  84.722  47.774  1.00 12.87           H  
ATOM   2333  HB  THR A 145      52.348  83.174  46.650  1.00 13.57           H  
ATOM   2334  HG1 THR A 145      53.389  84.553  45.223  1.00 14.88           H  
ATOM   2335 HG21 THR A 145      50.879  84.925  47.346  1.00 14.00           H  
ATOM   2336 HG22 THR A 145      51.446  84.079  48.552  1.00 14.00           H  
ATOM   2337 HG23 THR A 145      52.058  85.498  48.227  1.00 14.00           H  
ATOM   2338  N   HIS A 146      54.143  81.796  48.963  1.00 11.13           N  
ANISOU 2338  N   HIS A 146     1337   1462   1429    -65   -256    116       N  
ATOM   2339  CA  HIS A 146      54.232  81.153  50.269  1.00 11.11           C  
ANISOU 2339  CA  HIS A 146     1436   1434   1350    -53   -276    139       C  
ATOM   2340  C   HIS A 146      55.365  81.755  51.092  1.00 12.18           C  
ANISOU 2340  C   HIS A 146     1558   1686   1384    -40   -287   -150       C  
ATOM   2341  O   HIS A 146      55.246  81.900  52.314  1.00 13.05           O  
ANISOU 2341  O   HIS A 146     1782   1763   1415     12   -281   -187       O  
ATOM   2342  CB  HIS A 146      54.430  79.634  50.163  1.00 11.87           C  
ANISOU 2342  CB  HIS A 146     1483   1504   1524    -30    -94    157       C  
ATOM   2343  CG  HIS A 146      53.183  78.877  49.835  1.00 12.07           C  
ANISOU 2343  CG  HIS A 146     1341   1586   1659     33   -146     43       C  
ATOM   2344  ND1 HIS A 146      52.016  78.998  50.558  1.00 12.28           N  
ANISOU 2344  ND1 HIS A 146     1265   1839   1562    -56   -230    121       N  
ATOM   2345  CD2 HIS A 146      52.935  77.948  48.879  1.00 12.41           C  
ANISOU 2345  CD2 HIS A 146     1478   1690   1548    162   -283    -43       C  
ATOM   2346  CE1 HIS A 146      51.093  78.201  50.046  1.00 12.20           C  
ANISOU 2346  CE1 HIS A 146     1343   1806   1486   -113   -172    145       C  
ATOM   2347  NE2 HIS A 146      51.632  77.536  49.037  1.00 12.17           N  
ANISOU 2347  NE2 HIS A 146     1373   1767   1484    -47   -216     25       N  
ATOM   2348  H   HIS A 146      54.223  81.275  48.284  1.00 13.36           H  
ATOM   2349  HA  HIS A 146      53.383  81.298  50.715  1.00 13.33           H  
ATOM   2350  HB2 HIS A 146      55.077  79.453  49.464  1.00 14.25           H  
ATOM   2351  HB3 HIS A 146      54.760  79.304  51.014  1.00 14.25           H  
ATOM   2352  HD1 HIS A 146      51.905  79.513  51.237  1.00 14.74           H  
ATOM   2353  HD2 HIS A 146      53.534  77.646  48.235  1.00 14.90           H  
ATOM   2354  HE1 HIS A 146      50.215  78.121  50.345  1.00 14.65           H  
ATOM   2355  N   ALA A 147      56.474  82.113  50.443  1.00 12.88           N  
ANISOU 2355  N   ALA A 147     1490   1768   1635     -3   -369   -404       N  
ATOM   2356  CA  ALA A 147      57.566  82.750  51.168  1.00 12.52           C  
ANISOU 2356  CA  ALA A 147     1489   1702   1566     42   -251   -271       C  
ATOM   2357  C   ALA A 147      57.140  84.124  51.683  1.00 12.89           C  
ANISOU 2357  C   ALA A 147     1590   1725   1582    130   -394   -195       C  
ATOM   2358  O   ALA A 147      57.452  84.485  52.827  1.00 13.95           O  
ANISOU 2358  O   ALA A 147     1793   1856   1652    -95   -513   -174       O  
ATOM   2359  CB  ALA A 147      58.807  82.831  50.285  1.00 13.30           C  
ANISOU 2359  CB  ALA A 147     1740   1706   1608    -87   -249   -428       C  
ATOM   2360  H   ALA A 147      56.616  82.002  49.603  1.00 15.46           H  
ATOM   2361  HA  ALA A 147      57.806  82.210  51.937  1.00 15.03           H  
ATOM   2362  HB1 ALA A 147      59.553  83.152  50.816  1.00 15.97           H  
ATOM   2363  HB2 ALA A 147      59.006  81.948  49.937  1.00 15.97           H  
ATOM   2364  HB3 ALA A 147      58.635  83.444  49.553  1.00 15.97           H  
ATOM   2365  N   VAL A 148      56.419  84.896  50.867  1.00 12.48           N  
ANISOU 2365  N   VAL A 148     1579   1588   1576    -83   -296   -142       N  
ATOM   2366  CA  VAL A 148      55.898  86.182  51.334  1.00 11.96           C  
ANISOU 2366  CA  VAL A 148     1679   1396   1469    -62   -309   -239       C  
ATOM   2367  C   VAL A 148      55.034  85.986  52.574  1.00 12.35           C  
ANISOU 2367  C   VAL A 148     1800   1426   1465   -133   -296   -254       C  
ATOM   2368  O   VAL A 148      55.167  86.700  53.577  1.00 13.92           O  
ANISOU 2368  O   VAL A 148     1896   1669   1723   -100   -313   -329       O  
ATOM   2369  CB  VAL A 148      55.108  86.872  50.205  1.00 12.41           C  
ANISOU 2369  CB  VAL A 148     1538   1609   1570    -38   -115   -101       C  
ATOM   2370  CG1 VAL A 148      54.439  88.158  50.711  1.00 13.47           C  
ANISOU 2370  CG1 VAL A 148     1880   1641   1597   -135    -23   -300       C  
ATOM   2371  CG2 VAL A 148      56.016  87.169  49.001  1.00 13.98           C  
ANISOU 2371  CG2 VAL A 148     1663   1840   1808      3      1   -340       C  
ATOM   2372  H   VAL A 148      56.219  84.703  50.054  1.00 14.99           H  
ATOM   2373  HA  VAL A 148      56.646  86.750  51.577  1.00 14.36           H  
ATOM   2374  HB  VAL A 148      54.410  86.267  49.911  1.00 14.91           H  
ATOM   2375 HG11 VAL A 148      54.101  88.657  49.951  1.00 16.17           H  
ATOM   2376 HG12 VAL A 148      53.708  87.922  51.303  1.00 16.17           H  
ATOM   2377 HG13 VAL A 148      55.095  88.688  51.189  1.00 16.17           H  
ATOM   2378 HG21 VAL A 148      55.500  87.636  48.325  1.00 16.78           H  
ATOM   2379 HG22 VAL A 148      56.757  87.722  49.293  1.00 16.78           H  
ATOM   2380 HG23 VAL A 148      56.349  86.331  48.642  1.00 16.78           H  
ATOM   2381  N   THR A 149      54.136  85.005  52.528  1.00 12.26           N  
ANISOU 2381  N   THR A 149     1691   1653   1316   -133   -192   -178       N  
ATOM   2382  CA  THR A 149      53.303  84.700  53.682  1.00 11.63           C  
ANISOU 2382  CA  THR A 149     1519   1524   1377    -33   -129    -80       C  
ATOM   2383  C   THR A 149      54.136  84.327  54.895  1.00 14.07           C  
ANISOU 2383  C   THR A 149     1879   1744   1723    -60   -352   -201       C  
ATOM   2384  O   THR A 149      53.892  84.827  56.001  1.00 14.06           O  
ANISOU 2384  O   THR A 149     1978   1604   1759    -79   -290    -12       O  
ATOM   2385  CB  THR A 149      52.300  83.606  53.307  1.00 12.91           C  
ANISOU 2385  CB  THR A 149     1597   1730   1578   -122    -54    -98       C  
ATOM   2386  OG1 THR A 149      51.417  84.156  52.319  1.00 13.06           O  
ANISOU 2386  OG1 THR A 149     1643   1646   1674    -98   -306   -128       O  
ATOM   2387  CG2 THR A 149      51.531  83.122  54.509  1.00 14.69           C  
ANISOU 2387  CG2 THR A 149     1793   1860   1928   -169     72   -286       C  
ATOM   2388  H   THR A 149      53.991  84.503  51.845  1.00 14.73           H  
ATOM   2389  HA  THR A 149      52.797  85.489  53.932  1.00 13.96           H  
ATOM   2390  HB  THR A 149      52.756  82.827  52.953  1.00 15.50           H  
ATOM   2391  HG1 THR A 149      50.875  83.569  52.060  1.00 15.68           H  
ATOM   2392 HG21 THR A 149      50.762  82.605  54.225  1.00 17.63           H  
ATOM   2393 HG22 THR A 149      52.099  82.564  55.063  1.00 17.63           H  
ATOM   2394 HG23 THR A 149      51.226  83.879  55.034  1.00 17.63           H  
ATOM   2395  N   ASP A 150      55.134  83.460  54.709  1.00 14.68           N  
ANISOU 2395  N   ASP A 150     1872   1931   1777    136   -360   -301       N  
ATOM   2396  CA  ASP A 150      55.975  83.035  55.825  1.00 15.11           C  
ANISOU 2396  CA  ASP A 150     2088   2008   1646    121   -519   -354       C  
ATOM   2397  C   ASP A 150      56.661  84.228  56.501  1.00 15.29           C  
ANISOU 2397  C   ASP A 150     2161   2060   1587    114   -305   -265       C  
ATOM   2398  O   ASP A 150      56.863  84.236  57.726  1.00 16.64           O  
ANISOU 2398  O   ASP A 150     2459   2237   1627   -122   -460   -236       O  
ATOM   2399  CB  ASP A 150      57.055  82.071  55.326  1.00 15.48           C  
ANISOU 2399  CB  ASP A 150     2214   1848   1820    427   -513   -538       C  
ATOM   2400  CG  ASP A 150      56.527  80.700  54.901  1.00 18.40           C  
ANISOU 2400  CG  ASP A 150     2530   2137   2325    407   -316   -473       C  
ATOM   2401  OD1 ASP A 150      55.335  80.376  55.136  1.00 20.24           O  
ANISOU 2401  OD1 ASP A 150     2698   2341   2652    183   -285   -247       O  
ATOM   2402  OD2 ASP A 150      57.342  79.945  54.320  1.00 19.68           O  
ANISOU 2402  OD2 ASP A 150     2841   2165   2472    244   -291   -431       O  
ATOM   2403  H   ASP A 150      55.344  83.105  53.954  1.00 17.63           H  
ATOM   2404  HA  ASP A 150      55.410  82.584  56.471  1.00 18.14           H  
ATOM   2405  HB2 ASP A 150      57.494  82.468  54.557  1.00 18.59           H  
ATOM   2406  HB3 ASP A 150      57.698  81.930  56.039  1.00 18.59           H  
ATOM   2407  N   TYR A 151      57.049  85.227  55.715  1.00 14.85           N  
ANISOU 2407  N   TYR A 151     2045   1899   1697    124   -220   -322       N  
ATOM   2408  CA  TYR A 151      57.766  86.395  56.218  1.00 15.57           C  
ANISOU 2408  CA  TYR A 151     2064   1901   1950    -70   -303   -328       C  
ATOM   2409  C   TYR A 151      56.849  87.509  56.692  1.00 16.36           C  
ANISOU 2409  C   TYR A 151     2183   1983   2051   -226   -326   -558       C  
ATOM   2410  O   TYR A 151      57.342  88.550  57.150  1.00 18.44           O  
ANISOU 2410  O   TYR A 151     2288   2256   2462   -298   -327   -848       O  
ATOM   2411  CB  TYR A 151      58.747  86.912  55.157  1.00 15.38           C  
ANISOU 2411  CB  TYR A 151     1864   1924   2057   -286   -476   -167       C  
ATOM   2412  CG  TYR A 151      60.039  86.139  55.136  1.00 15.59           C  
ANISOU 2412  CG  TYR A 151     1772   2104   2049   -246   -345   -222       C  
ATOM   2413  CD1 TYR A 151      60.164  84.956  54.419  1.00 15.42           C  
ANISOU 2413  CD1 TYR A 151     1598   2210   2050    -41   -440   -402       C  
ATOM   2414  CD2 TYR A 151      61.135  86.581  55.851  1.00 15.47           C  
ANISOU 2414  CD2 TYR A 151     1541   2315   2022   -214   -366   -309       C  
ATOM   2415  CE1 TYR A 151      61.356  84.240  54.412  1.00 17.33           C  
ANISOU 2415  CE1 TYR A 151     1759   2447   2380    -32   -623   -443       C  
ATOM   2416  CE2 TYR A 151      62.334  85.889  55.831  1.00 17.10           C  
ANISOU 2416  CE2 TYR A 151     1563   2577   2358    -50   -421   -296       C  
ATOM   2417  CZ  TYR A 151      62.435  84.713  55.121  1.00 18.37           C  
ANISOU 2417  CZ  TYR A 151     1803   2679   2498     67   -551   -367       C  
ATOM   2418  OH  TYR A 151      63.614  84.015  55.106  1.00 20.23           O  
ANISOU 2418  OH  TYR A 151     1968   2982   2735     75   -511   -631       O  
ATOM   2419  H   TYR A 151      56.906  85.251  54.868  1.00 17.82           H  
ATOM   2420  HA  TYR A 151      58.294  86.126  56.986  1.00 18.69           H  
ATOM   2421  HB2 TYR A 151      58.335  86.835  54.282  1.00 18.47           H  
ATOM   2422  HB3 TYR A 151      58.955  87.841  55.345  1.00 18.47           H  
ATOM   2423  HD1 TYR A 151      59.437  84.638  53.934  1.00 18.51           H  
ATOM   2424  HD2 TYR A 151      61.067  87.358  56.357  1.00 18.57           H  
ATOM   2425  HE1 TYR A 151      61.423  83.447  53.931  1.00 20.81           H  
ATOM   2426  HE2 TYR A 151      63.069  86.217  56.296  1.00 20.53           H  
ATOM   2427  HH  TYR A 151      64.172  84.381  55.616  1.00 24.28           H  
ATOM   2428  N   THR A 152      55.538  87.307  56.623  1.00 14.51           N  
ANISOU 2428  N   THR A 152     1967   1796   1749    -57   -237   -370       N  
ATOM   2429  CA  THR A 152      54.579  88.313  57.070  1.00 15.32           C  
ANISOU 2429  CA  THR A 152     2239   1753   1826    -52   -254   -342       C  
ATOM   2430  C   THR A 152      53.620  87.712  58.089  1.00 14.79           C  
ANISOU 2430  C   THR A 152     2117   1871   1630     14   -298   -347       C  
ATOM   2431  O   THR A 152      53.943  87.644  59.279  1.00 15.89           O  
ANISOU 2431  O   THR A 152     2317   1968   1751    187   -292   -220       O  
ATOM   2432  CB  THR A 152      53.852  88.966  55.889  1.00 15.83           C  
ANISOU 2432  CB  THR A 152     2389   1723   1901     18    -64   -161       C  
ATOM   2433  OG1 THR A 152      53.193  87.976  55.085  1.00 15.15           O  
ANISOU 2433  OG1 THR A 152     2112   1897   1749    197   -249   -192       O  
ATOM   2434  CG2 THR A 152      54.846  89.720  55.016  1.00 17.42           C  
ANISOU 2434  CG2 THR A 152     2725   1848   2045   -215   -104   -166       C  
ATOM   2435  H   THR A 152      55.174  86.590  56.318  1.00 17.41           H  
ATOM   2436  HA  THR A 152      55.053  89.035  57.511  1.00 18.39           H  
ATOM   2437  HB  THR A 152      53.189  89.584  56.234  1.00 19.00           H  
ATOM   2438  HG1 THR A 152      53.758  87.439  54.770  1.00 18.19           H  
ATOM   2439 HG21 THR A 152      54.411  90.022  54.203  1.00 20.91           H  
ATOM   2440 HG22 THR A 152      55.190  90.490  55.494  1.00 20.91           H  
ATOM   2441 HG23 THR A 152      55.587  89.139  54.780  1.00 20.91           H  
ATOM   2442  N   ALA A 153      52.454  87.253  57.639  1.00 14.68           N  
ANISOU 2442  N   ALA A 153     2136   1960   1481    -52   -370   -334       N  
ATOM   2443  CA  ALA A 153      51.429  86.783  58.571  1.00 14.79           C  
ANISOU 2443  CA  ALA A 153     2132   2037   1451    220   -395   -128       C  
ATOM   2444  C   ALA A 153      51.841  85.489  59.263  1.00 14.62           C  
ANISOU 2444  C   ALA A 153     2380   1925   1251    296   -231   -139       C  
ATOM   2445  O   ALA A 153      51.499  85.269  60.432  1.00 15.98           O  
ANISOU 2445  O   ALA A 153     2501   2037   1533    220   -190    -47       O  
ATOM   2446  CB  ALA A 153      50.120  86.572  57.825  1.00 14.94           C  
ANISOU 2446  CB  ALA A 153     2054   2065   1557    101   -243     22       C  
ATOM   2447  H   ALA A 153      52.230  87.201  56.810  1.00 17.62           H  
ATOM   2448  HA  ALA A 153      51.301  87.461  59.253  1.00 17.75           H  
ATOM   2449  HB1 ALA A 153      49.456  86.230  58.444  1.00 17.93           H  
ATOM   2450  HB2 ALA A 153      49.825  87.420  57.458  1.00 17.93           H  
ATOM   2451  HB3 ALA A 153      50.264  85.933  57.109  1.00 17.93           H  
ATOM   2452  N   GLY A 154      52.534  84.607  58.549  1.00 14.83           N  
ANISOU 2452  N   GLY A 154     2384   1869   1380    280   -213   -197       N  
ATOM   2453  CA  GLY A 154      52.912  83.332  59.111  1.00 16.00           C  
ANISOU 2453  CA  GLY A 154     2714   1768   1596    420   -348     20       C  
ATOM   2454  C   GLY A 154      51.782  82.325  59.184  1.00 17.22           C  
ANISOU 2454  C   GLY A 154     3244   1654   1648    302   -574    -64       C  
ATOM   2455  O   GLY A 154      51.793  81.441  60.049  1.00 18.19           O  
ANISOU 2455  O   GLY A 154     3603   1882   1426    230   -710    -21       O  
ATOM   2456  H   GLY A 154      52.794  84.728  57.738  1.00 17.80           H  
ATOM   2457  HA2 GLY A 154      53.619  82.949  58.569  1.00 19.20           H  
ATOM   2458  HA3 GLY A 154      53.245  83.473  60.011  1.00 19.20           H  
ATOM   2459  N   LEU A 155      50.802  82.434  58.296  1.00 16.72           N  
ANISOU 2459  N   LEU A 155     3219   1714   1421     53   -623   -160       N  
ATOM   2460  CA  LEU A 155      49.671  81.521  58.272  1.00 16.41           C  
ANISOU 2460  CA  LEU A 155     3266   1442   1526      9   -637    -71       C  
ATOM   2461  C   LEU A 155      50.156  80.087  58.337  1.00 19.55           C  
ANISOU 2461  C   LEU A 155     3603   1796   2029    218   -754     85       C  
ATOM   2462  O   LEU A 155      51.070  79.688  57.601  1.00 21.58           O  
ANISOU 2462  O   LEU A 155     4117   2071   2011    460   -427    100       O  
ATOM   2463  CB  LEU A 155      48.893  81.711  56.968  1.00 15.51           C  
ANISOU 2463  CB  LEU A 155     2891   1601   1403   -108   -410    151       C  
ATOM   2464  CG  LEU A 155      48.062  82.993  56.878  1.00 15.01           C  
ANISOU 2464  CG  LEU A 155     2510   1899   1292   -157    -41   -108       C  
ATOM   2465  CD1 LEU A 155      47.667  83.282  55.436  1.00 15.79           C  
ANISOU 2465  CD1 LEU A 155     2571   2107   1321    -14      9    -96       C  
ATOM   2466  CD2 LEU A 155      46.823  82.883  57.759  1.00 15.39           C  
ANISOU 2466  CD2 LEU A 155     2552   1975   1322   -466    146   -240       C  
ATOM   2467  H   LEU A 155      50.768  83.040  57.686  1.00 20.08           H  
ATOM   2468  HA  LEU A 155      49.092  81.704  59.029  1.00 19.70           H  
ATOM   2469  HB2 LEU A 155      49.528  81.725  56.235  1.00 18.62           H  
ATOM   2470  HB3 LEU A 155      48.284  80.963  56.865  1.00 18.62           H  
ATOM   2471  HG  LEU A 155      48.596  83.737  57.194  1.00 18.01           H  
ATOM   2472 HD11 LEU A 155      47.148  84.100  55.408  1.00 18.96           H  
ATOM   2473 HD12 LEU A 155      48.472  83.383  54.903  1.00 18.96           H  
ATOM   2474 HD13 LEU A 155      47.138  82.542  55.099  1.00 18.96           H  
ATOM   2475 HD21 LEU A 155      46.312  83.705  57.690  1.00 18.48           H  
ATOM   2476 HD22 LEU A 155      46.286  82.134  57.457  1.00 18.48           H  
ATOM   2477 HD23 LEU A 155      47.100  82.742  58.678  1.00 18.48           H  
ATOM   2478  N  AILE A 156      49.495  79.295  59.198  0.50 20.60           N  
ANISOU 2478  N  AILE A 156     3586   1773   2468    -24  -1232     53       N  
ATOM   2479  N  BILE A 156      49.578  79.310  59.236  0.50 18.73           N  
ANISOU 2479  N  BILE A 156     3393   1643   2080   -260   -898    130       N  
ATOM   2480  CA AILE A 156      49.819  77.887  59.376  0.50 21.98           C  
ANISOU 2480  CA AILE A 156     3624   1861   2867   -146  -1598    -15       C  
ATOM   2481  CA BILE A 156      49.978  77.917  59.311  0.50 18.17           C  
ANISOU 2481  CA BILE A 156     3178   1653   2073   -680   -948    160       C  
ATOM   2482  C  AILE A 156      49.099  77.051  58.327  0.50 21.37           C  
ANISOU 2482  C  AILE A 156     3376   1763   2979   -132  -1733     83       C  
ATOM   2483  C  BILE A 156      49.555  77.239  58.012  0.50 17.42           C  
ANISOU 2483  C  BILE A 156     2897   1626   2096   -646   -635    427       C  
ATOM   2484  O  AILE A 156      47.929  77.308  57.992  0.50 21.05           O  
ANISOU 2484  O  AILE A 156     3135   1686   3178   -243  -1636      7       O  
ATOM   2485  O  BILE A 156      49.034  77.879  57.076  0.50 15.06           O  
ANISOU 2485  O  BILE A 156     2426   1387   1908   -836    -15    526       O  
ATOM   2486  CB AILE A 156      49.462  77.413  60.794  0.50 25.11           C  
ANISOU 2486  CB AILE A 156     3911   2271   3359   -310  -1521   -116       C  
ATOM   2487  CB BILE A 156      49.383  77.225  60.544  0.50 19.42           C  
ANISOU 2487  CB BILE A 156     3280   1882   2216  -1160   -930    105       C  
ATOM   2488  CG1AILE A 156      47.955  77.384  61.017  0.50 27.33           C  
ANISOU 2488  CG1AILE A 156     4122   2624   3637   -154  -1317     48       C  
ATOM   2489  CG1BILE A 156      47.867  77.308  60.510  0.50 20.19           C  
ANISOU 2489  CG1BILE A 156     3458   2116   2098   -933   -678    254       C  
ATOM   2490  CG2AILE A 156      50.099  78.295  61.848  0.50 25.61           C  
ANISOU 2490  CG2AILE A 156     3922   2374   3433   -430  -1670   -198       C  
ATOM   2491  CG2BILE A 156      49.944  77.833  61.848  0.50 19.11           C  
ANISOU 2491  CG2BILE A 156     3121   1927   2214  -1198   -903    161       C  
ATOM   2492  CD1AILE A 156      47.569  76.439  62.156  0.50 28.66           C  
ANISOU 2492  CD1AILE A 156     4271   2813   3805   -193  -1279    238       C  
ATOM   2493  CD1BILE A 156      47.218  76.480  61.603  0.50 20.55           C  
ANISOU 2493  CD1BILE A 156     3592   2084   2130  -1242   -498    590       C  
ATOM   2494  H  AILE A 156      48.846  79.563  59.695  0.50 24.73           H  
ATOM   2495  H  BILE A 156      48.973  79.558  59.795  0.50 22.48           H  
ATOM   2496  HA AILE A 156      50.775  77.780  59.250  0.50 26.38           H  
ATOM   2497  HA BILE A 156      50.942  77.852  59.393  0.50 21.81           H  
ATOM   2498  HB AILE A 156      49.809  76.510  60.873  0.50 30.14           H  
ATOM   2499  HB BILE A 156      49.641  76.290  60.523  0.50 23.31           H  
ATOM   2500 HG12AILE A 156      47.648  78.276  61.244  0.50 32.80           H  
ATOM   2501 HG12BILE A 156      47.597  78.232  60.630  0.50 24.24           H  
ATOM   2502 HG13AILE A 156      47.517  77.079  60.207  0.50 32.80           H  
ATOM   2503 HG13BILE A 156      47.551  76.978  59.654  0.50 24.24           H  
ATOM   2504 HG21AILE A 156      49.920  77.920  62.724  0.50 30.74           H  
ATOM   2505 HG21BILE A 156      49.640  77.301  62.600  0.50 22.94           H  
ATOM   2506 HG22AILE A 156      51.056  78.330  61.693  0.50 30.74           H  
ATOM   2507 HG22BILE A 156      50.914  77.825  61.808  0.50 22.94           H  
ATOM   2508 HG23AILE A 156      49.721  79.186  61.785  0.50 30.74           H  
ATOM   2509 HG23BILE A 156      49.624  78.744  61.935  0.50 22.94           H  
ATOM   2510 HD11AILE A 156      46.603  76.430  62.245  0.50 34.40           H  
ATOM   2511 HD11BILE A 156      46.349  76.178  61.297  0.50 24.66           H  
ATOM   2512 HD12AILE A 156      47.891  75.548  61.949  0.50 34.40           H  
ATOM   2513 HD12BILE A 156      47.783  75.717  61.799  0.50 24.66           H  
ATOM   2514 HD13AILE A 156      47.975  76.755  62.979  0.50 34.40           H  
ATOM   2515 HD13BILE A 156      47.117  77.029  62.397  0.50 24.66           H  
ATOM   2516  N  ATYR A 157      49.782  76.016  57.859  0.50 21.61           N  
ANISOU 2516  N  ATYR A 157     3410   1812   2988     47  -1626     31       N  
ATOM   2517  N  BTYR A 157      49.770  75.938  57.944  0.50 19.12           N  
ANISOU 2517  N  BTYR A 157     3088   1791   2386   -528   -839    316       N  
ATOM   2518  CA ATYR A 157      49.440  75.266  56.644  0.50 21.54           C  
ANISOU 2518  CA ATYR A 157     3418   1833   2932    -44  -1577     57       C  
ATOM   2519  CA BTYR A 157      49.421  75.167  56.764  0.50 20.35           C  
ANISOU 2519  CA BTYR A 157     3212   1841   2680   -642  -1150    300       C  
ATOM   2520  C  ATYR A 157      48.398  74.167  56.880  0.50 21.26           C  
ANISOU 2520  C  ATYR A 157     3430   1768   2879   -112  -1593    220       C  
ATOM   2521  C  BTYR A 157      48.523  74.012  57.179  0.50 21.51           C  
ANISOU 2521  C  BTYR A 157     3376   1927   2871   -632  -1339    332       C  
ATOM   2522  O  ATYR A 157      48.468  73.120  56.216  0.50 21.03           O  
ANISOU 2522  O  ATYR A 157     3207   1790   2994    362  -1687    140       O  
ATOM   2523  O  BTYR A 157      48.819  72.831  57.009  0.50 23.13           O  
ANISOU 2523  O  BTYR A 157     3345   2126   3316   -533  -1244    554       O  
ATOM   2524  CB ATYR A 157      50.733  74.699  56.036  0.50 22.22           C  
ANISOU 2524  CB ATYR A 157     3567   1875   3001   -158  -1260      3       C  
ATOM   2525  CB BTYR A 157      50.655  74.704  56.027  0.50 20.82           C  
ANISOU 2525  CB BTYR A 157     3239   1857   2815   -830  -1004    367       C  
ATOM   2526  CG ATYR A 157      51.679  75.716  55.369  0.50 21.70           C  
ANISOU 2526  CG ATYR A 157     3356   1984   2905    -33  -1180     50       C  
ATOM   2527  CG BTYR A 157      50.373  74.455  54.576  0.50 20.26           C  
ANISOU 2527  CG BTYR A 157     2916   1988   2792   -792  -1067    479       C  
ATOM   2528  CD1ATYR A 157      52.525  76.526  56.130  0.50 21.29           C  
ANISOU 2528  CD1ATYR A 157     3134   2085   2869    169  -1212    274       C  
ATOM   2529  CD1BTYR A 157      50.090  75.505  53.707  0.50 19.93           C  
ANISOU 2529  CD1BTYR A 157     2740   2014   2818   -571  -1223    445       C  
ATOM   2530  CD2ATYR A 157      51.722  75.862  53.982  0.50 21.62           C  
ANISOU 2530  CD2ATYR A 157     3283   2036   2895   -156   -967    -58       C  
ATOM   2531  CD2BTYR A 157      50.403  73.179  54.066  0.50 20.56           C  
ANISOU 2531  CD2BTYR A 157     2883   1962   2965   -839  -1039    541       C  
ATOM   2532  CE1ATYR A 157      53.373  77.461  55.530  0.50 19.93           C  
ANISOU 2532  CE1ATYR A 157     2950   1921   2700    297  -1197    -52       C  
ATOM   2533  CE1BTYR A 157      49.830  75.269  52.377  0.50 19.60           C  
ANISOU 2533  CE1BTYR A 157     2668   1994   2784   -534  -1304    698       C  
ATOM   2534  CE2ATYR A 157      52.570  76.800  53.373  0.50 20.97           C  
ANISOU 2534  CE2ATYR A 157     3235   2053   2678     62   -939   -254       C  
ATOM   2535  CE2BTYR A 157      50.155  72.941  52.743  0.50 19.84           C  
ANISOU 2535  CE2BTYR A 157     2678   2056   2805   -709  -1402    644       C  
ATOM   2536  CZ ATYR A 157      53.396  77.586  54.151  0.50 20.18           C  
ANISOU 2536  CZ ATYR A 157     3020   2064   2585    113   -971   -154       C  
ATOM   2537  CZ BTYR A 157      49.881  73.989  51.904  0.50 19.87           C  
ANISOU 2537  CZ BTYR A 157     2700   2016   2833   -586  -1371    670       C  
ATOM   2538  OH ATYR A 157      54.223  78.512  53.540  0.50 20.50           O  
ANISOU 2538  OH ATYR A 157     3266   2200   2321    363   -993   -360       O  
ATOM   2539  OH BTYR A 157      49.646  73.740  50.588  0.50 20.94           O  
ANISOU 2539  OH BTYR A 157     3086   2054   2815   -502  -1260    892       O  
ATOM   2540  H  ATYR A 157      50.486  75.708  58.245  0.50 25.94           H  
ATOM   2541  H  BTYR A 157      50.120  75.474  58.577  0.50 22.95           H  
ATOM   2542  HA ATYR A 157      49.043  75.875  56.001  0.50 25.85           H  
ATOM   2543  HA BTYR A 157      48.914  75.724  56.152  0.50 24.43           H  
ATOM   2544  HB2ATYR A 157      51.234  74.266  56.745  0.50 26.67           H  
ATOM   2545  HB2BTYR A 157      51.341  75.387  56.092  0.50 25.00           H  
ATOM   2546  HB3ATYR A 157      50.489  74.050  55.358  0.50 26.67           H  
ATOM   2547  HB3BTYR A 157      50.972  73.877  56.423  0.50 25.00           H  
ATOM   2548  HD1ATYR A 157      52.524  76.441  57.056  0.50 25.55           H  
ATOM   2549  HD1BTYR A 157      50.077  76.377  54.030  0.50 23.92           H  
ATOM   2550  HD2ATYR A 157      51.177  75.328  53.451  0.50 25.95           H  
ATOM   2551  HD2BTYR A 157      50.596  72.465  54.631  0.50 24.68           H  
ATOM   2552  HE1ATYR A 157      53.922  77.998  56.056  0.50 23.92           H  
ATOM   2553  HE1BTYR A 157      49.621  75.973  51.806  0.50 23.52           H  
ATOM   2554  HE2ATYR A 157      52.576  76.891  52.447  0.50 25.17           H  
ATOM   2555  HE2BTYR A 157      50.172  72.072  52.414  0.50 23.82           H  
ATOM   2556  HH ATYR A 157      54.646  78.946  54.120  0.50 24.60           H  
ATOM   2557  HH BTYR A 157      49.516  74.462  50.178  0.50 25.13           H  
ATOM   2558  N   GLN A 158      47.390  74.376  57.749  1.00 22.36           N  
ANISOU 2558  N   GLN A 158     3888   1932   2676   -906  -1179    443       N  
ATOM   2559  CA AGLN A 158      46.368  73.390  58.052  0.48 24.07           C  
ANISOU 2559  CA AGLN A 158     4083   2267   2796   -925  -1146    671       C  
ATOM   2560  CA BGLN A 158      46.363  73.392  58.052  0.52 24.34           C  
ANISOU 2560  CA BGLN A 158     4273   2220   2754  -1003  -1079    741       C  
ATOM   2561  C   GLN A 158      45.032  74.095  58.263  1.00 22.77           C  
ANISOU 2561  C   GLN A 158     4068   2126   2457  -1138   -985    778       C  
ATOM   2562  O   GLN A 158      44.984  75.266  58.658  1.00 21.83           O  
ANISOU 2562  O   GLN A 158     4015   2146   2135  -1218   -801    684       O  
ATOM   2563  CB AGLN A 158      46.735  72.584  59.316  0.48 27.08           C  
ANISOU 2563  CB AGLN A 158     4352   2691   3247   -635  -1138    811       C  
ATOM   2564  CB BGLN A 158      46.715  72.554  59.288  0.52 27.85           C  
ANISOU 2564  CB BGLN A 158     4920   2547   3112   -874   -929   1010       C  
ATOM   2565  CG AGLN A 158      48.028  71.747  59.210  0.48 29.43           C  
ANISOU 2565  CG AGLN A 158     4549   3079   3555   -419  -1277    898       C  
ATOM   2566  CG BGLN A 158      46.616  73.303  60.603  0.52 30.67           C  
ANISOU 2566  CG BGLN A 158     5508   2847   3297   -821   -917   1210       C  
ATOM   2567  CD AGLN A 158      49.295  72.532  59.517  0.48 31.41           C  
ANISOU 2567  CD AGLN A 158     4808   3356   3769   -176  -1396    866       C  
ATOM   2568  CD BGLN A 158      47.045  72.467  61.792  0.52 33.45           C  
ANISOU 2568  CD BGLN A 158     6060   3120   3528   -685   -983   1319       C  
ATOM   2569  OE1AGLN A 158      49.281  73.476  60.307  0.48 32.42           O  
ANISOU 2569  OE1AGLN A 158     5005   3396   3917   -214  -1442    710       O  
ATOM   2570  OE1BGLN A 158      47.163  71.248  61.689  0.52 35.25           O  
ANISOU 2570  OE1BGLN A 158     6342   3314   3738   -487   -943   1468       O  
ATOM   2571  NE2AGLN A 158      50.406  72.130  58.896  0.48 31.63           N  
ANISOU 2571  NE2AGLN A 158     4693   3496   3830    -55  -1431   1054       N  
ATOM   2572  NE2BGLN A 158      47.286  73.122  62.930  0.52 33.66           N  
ANISOU 2572  NE2BGLN A 158     6207   3105   3479   -810  -1049   1352       N  
ATOM   2573  H  AGLN A 158      47.285  75.110  58.184  0.50 26.84           H  
ATOM   2574  H  BGLN A 158      47.190  75.182  57.971  0.50 26.84           H  
ATOM   2575  HA AGLN A 158      46.271  72.777  57.307  0.48 28.89           H  
ATOM   2576  HA BGLN A 158      46.276  72.795  57.292  0.52 29.21           H  
ATOM   2577  HB2AGLN A 158      46.851  73.205  60.051  0.48 32.51           H  
ATOM   2578  HB2BGLN A 158      46.107  71.800  59.334  0.52 33.42           H  
ATOM   2579  HB3AGLN A 158      46.008  71.972  59.510  0.48 32.51           H  
ATOM   2580  HB3BGLN A 158      47.628  72.238  59.198  0.52 33.42           H  
ATOM   2581  HG2AGLN A 158      47.975  71.012  59.841  0.48 35.33           H  
ATOM   2582  HG2BGLN A 158      47.189  74.085  60.565  0.52 36.81           H  
ATOM   2583  HG3AGLN A 158      48.104  71.403  58.306  0.48 35.33           H  
ATOM   2584  HG3BGLN A 158      45.695  73.573  60.744  0.52 36.81           H  
ATOM   2585 HE21AGLN A 158      50.379  71.461  58.357  0.48 37.97           H  
ATOM   2586 HE21BGLN A 158      47.196  73.977  62.961  0.52 40.40           H  
ATOM   2587 HE22AGLN A 158      51.149  72.541  59.036  0.48 37.97           H  
ATOM   2588 HE22BGLN A 158      47.532  72.690  63.631  0.52 40.40           H  
ATOM   2589  N   ASN A 159      43.950  73.371  57.981  1.00 22.28           N  
ANISOU 2589  N   ASN A 159     3951   2170   2345  -1183   -932    885       N  
ATOM   2590  CA  ASN A 159      42.582  73.820  58.281  1.00 24.06           C  
ANISOU 2590  CA  ASN A 159     4185   2684   2274  -1237   -766    801       C  
ATOM   2591  C   ASN A 159      42.291  75.165  57.615  1.00 20.03           C  
ANISOU 2591  C   ASN A 159     3257   2420   1935  -1163   -476    549       C  
ATOM   2592  O   ASN A 159      42.758  75.411  56.497  1.00 18.86           O  
ANISOU 2592  O   ASN A 159     3258   2151   1757   -978    -58    518       O  
ATOM   2593  CB  ASN A 159      42.400  73.743  59.772  1.00 29.01           C  
ANISOU 2593  CB  ASN A 159     5221   3302   2500   -930   -829   1143       C  
ATOM   2594  CG  ASN A 159      42.737  72.352  60.309  1.00 33.70           C  
ANISOU 2594  CG  ASN A 159     6070   3834   2900   -769   -959    982       C  
ATOM   2595  OD1 ASN A 159      43.459  72.199  61.305  1.00 37.79           O  
ANISOU 2595  OD1 ASN A 159     6514   4411   3435   -619  -1100    867       O  
ATOM   2596  ND2 ASN A 159      42.224  71.327  59.629  1.00 32.90           N  
ANISOU 2596  ND2 ASN A 159     6186   3636   2678   -938   -751    999       N  
ATOM   2597  H   ASN A 159      43.977  72.597  57.607  1.00 26.75           H  
ATOM   2598  HA  ASN A 159      41.949  73.223  57.853  1.00 28.88           H  
ATOM   2599  HB2 ASN A 159      42.988  74.385  60.201  1.00 34.82           H  
ATOM   2600  HB3 ASN A 159      41.477  73.940  59.993  1.00 34.82           H  
ATOM   2601 HD21 ASN A 159      42.379  70.521  59.885  1.00 39.49           H  
ATOM   2602 HD22 ASN A 159      41.737  71.472  58.935  1.00 39.49           H  
ATOM   2603  N   GLU A 160      41.500  76.046  58.245  1.00 19.45           N  
ANISOU 2603  N   GLU A 160     2859   2647   1885  -1329   -259    338       N  
ATOM   2604  CA  GLU A 160      41.080  77.256  57.537  1.00 18.58           C  
ANISOU 2604  CA  GLU A 160     2474   2665   1920   -827     30    164       C  
ATOM   2605  C   GLU A 160      42.263  78.168  57.259  1.00 15.74           C  
ANISOU 2605  C   GLU A 160     2019   2242   1720   -662   -144    302       C  
ATOM   2606  O   GLU A 160      42.346  78.773  56.183  1.00 15.31           O  
ANISOU 2606  O   GLU A 160     2051   2088   1676   -414     50     83       O  
ATOM   2607  CB  GLU A 160      39.978  78.036  58.277  1.00 19.17           C  
ANISOU 2607  CB  GLU A 160     2553   2761   1972   -874    104   -272       C  
ATOM   2608  CG  GLU A 160      38.615  77.448  58.076  1.00 21.35           C  
ANISOU 2608  CG  GLU A 160     2948   2748   2414   -499    -88    -92       C  
ATOM   2609  CD  GLU A 160      37.480  78.246  58.676  1.00 19.88           C  
ANISOU 2609  CD  GLU A 160     2872   2388   2292   -569    171    150       C  
ATOM   2610  OE1 GLU A 160      37.576  79.499  58.809  1.00 17.59           O  
ANISOU 2610  OE1 GLU A 160     2449   2178   2058   -328    249    148       O  
ATOM   2611  OE2 GLU A 160      36.454  77.603  58.984  1.00 21.97           O  
ANISOU 2611  OE2 GLU A 160     3379   2271   2697   -523    183    414       O  
ATOM   2612  H   GLU A 160      41.204  75.970  59.049  1.00 23.35           H  
ATOM   2613  HA  GLU A 160      40.689  76.964  56.699  1.00 22.30           H  
ATOM   2614  HB2 GLU A 160      40.170  78.029  59.228  1.00 23.02           H  
ATOM   2615  HB3 GLU A 160      39.962  78.949  57.949  1.00 23.02           H  
ATOM   2616  HG2 GLU A 160      38.448  77.378  57.123  1.00 25.62           H  
ATOM   2617  HG3 GLU A 160      38.597  76.567  58.481  1.00 25.62           H  
ATOM   2618  N   SER A 161      43.177  78.312  58.225  1.00 15.57           N  
ANISOU 2618  N   SER A 161     2007   2173   1736   -431   -170     34       N  
ATOM   2619  CA ASER A 161      44.350  79.157  58.004  0.74 14.56           C  
ANISOU 2619  CA ASER A 161     1760   2115   1656   -423   -169    -26       C  
ATOM   2620  CA BSER A 161      44.331  79.175  57.985  0.26 14.80           C  
ANISOU 2620  CA BSER A 161     1883   2010   1732   -320   -284     16       C  
ATOM   2621  C   SER A 161      45.159  78.661  56.819  1.00 14.28           C  
ANISOU 2621  C   SER A 161     1897   1828   1700   -273   -238    131       C  
ATOM   2622  O   SER A 161      45.668  79.456  56.019  1.00 13.45           O  
ANISOU 2622  O   SER A 161     1921   1543   1647   -169    -69     87       O  
ATOM   2623  CB ASER A 161      45.216  79.184  59.259  0.74 15.87           C  
ANISOU 2623  CB ASER A 161     2101   2421   1509   -560     43    -14       C  
ATOM   2624  CB BSER A 161      45.189  79.334  59.238  0.26 15.22           C  
ANISOU 2624  CB BSER A 161     1985   2066   1732   -248   -396    -39       C  
ATOM   2625  OG ASER A 161      44.459  79.643  60.356  0.74 18.02           O  
ANISOU 2625  OG ASER A 161     2571   2612   1666   -293    -66     49       O  
ATOM   2626  OG BSER A 161      45.302  78.122  59.938  0.26 15.65           O  
ANISOU 2626  OG BSER A 161     2118   2048   1781    -98   -577    -20       O  
ATOM   2627  H  ASER A 161      43.143  77.941  59.000  0.74 18.70           H  
ATOM   2628  H  BSER A 161      43.153  77.936  58.998  0.26 18.70           H  
ATOM   2629  HA ASER A 161      44.055  80.062  57.817  0.74 17.48           H  
ATOM   2630  HA BSER A 161      44.002  80.061  57.765  0.26 17.77           H  
ATOM   2631  HB2ASER A 161      45.537  78.288  59.444  0.74 19.06           H  
ATOM   2632  HB2BSER A 161      46.075  79.629  58.976  0.26 18.27           H  
ATOM   2633  HB3ASER A 161      45.966  79.782  59.116  0.74 19.06           H  
ATOM   2634  HB3BSER A 161      44.778  79.994  59.818  0.26 18.27           H  
ATOM   2635  HG ASER A 161      44.161  80.412  60.198  0.74 21.64           H  
ATOM   2636  HG BSER A 161      45.481  77.498  59.406  0.26 18.79           H  
ATOM   2637  N   GLY A 162      45.300  77.337  56.698  1.00 15.08           N  
ANISOU 2637  N   GLY A 162     2023   1824   1884   -546   -146    268       N  
ATOM   2638  CA  GLY A 162      46.023  76.769  55.578  1.00 14.03           C  
ANISOU 2638  CA  GLY A 162     1843   1775   1713   -292   -136    283       C  
ATOM   2639  C   GLY A 162      45.324  76.968  54.249  1.00 13.15           C  
ANISOU 2639  C   GLY A 162     1771   1520   1707   -200   -201     98       C  
ATOM   2640  O   GLY A 162      45.989  77.148  53.220  1.00 13.47           O  
ANISOU 2640  O   GLY A 162     1975   1452   1691   -122   -192   -111       O  
ATOM   2641  H   GLY A 162      44.986  76.755  57.248  1.00 18.11           H  
ATOM   2642  HA2 GLY A 162      46.898  77.182  55.524  1.00 16.85           H  
ATOM   2643  HA3 GLY A 162      46.132  75.816  55.722  1.00 16.85           H  
ATOM   2644  N   ALA A 163      43.994  76.943  54.247  1.00 13.25           N  
ANISOU 2644  N   ALA A 163     1754   1499   1781   -245   -105    127       N  
ATOM   2645  CA  ALA A 163      43.243  77.229  53.031  1.00 13.42           C  
ANISOU 2645  CA  ALA A 163     1972   1429   1698   -365   -186     -5       C  
ATOM   2646  C   ALA A 163      43.402  78.688  52.624  1.00 13.52           C  
ANISOU 2646  C   ALA A 163     1819   1622   1697   -286    -65    118       C  
ATOM   2647  O   ALA A 163      43.494  78.996  51.430  1.00 13.44           O  
ANISOU 2647  O   ALA A 163     1799   1690   1617   -188    -81    140       O  
ATOM   2648  CB  ALA A 163      41.772  76.868  53.227  1.00 15.70           C  
ANISOU 2648  CB  ALA A 163     2367   1776   1824   -288   -528      2       C  
ATOM   2649  H   ALA A 163      43.503  76.765  54.931  1.00 15.91           H  
ATOM   2650  HA  ALA A 163      43.583  76.679  52.307  1.00 16.11           H  
ATOM   2651  HB1 ALA A 163      41.285  77.074  52.414  1.00 18.85           H  
ATOM   2652  HB2 ALA A 163      41.703  75.920  53.422  1.00 18.85           H  
ATOM   2653  HB3 ALA A 163      41.416  77.384  53.967  1.00 18.85           H  
ATOM   2654  N   ILE A 164      43.449  79.597  53.600  1.00 13.08           N  
ANISOU 2654  N   ILE A 164     1708   1613   1647    -90    -26    177       N  
ATOM   2655  CA  ILE A 164      43.751  80.992  53.288  1.00 12.37           C  
ANISOU 2655  CA  ILE A 164     1752   1526   1424   -101    -61     62       C  
ATOM   2656  C   ILE A 164      45.152  81.108  52.705  1.00 11.78           C  
ANISOU 2656  C   ILE A 164     1568   1582   1324   -174   -188     34       C  
ATOM   2657  O   ILE A 164      45.371  81.825  51.726  1.00 12.41           O  
ANISOU 2657  O   ILE A 164     1707   1572   1435    -41    100    101       O  
ATOM   2658  CB  ILE A 164      43.600  81.887  54.528  1.00 13.40           C  
ANISOU 2658  CB  ILE A 164     1924   1504   1666   -191    -79     65       C  
ATOM   2659  CG1 ILE A 164      42.147  81.908  54.996  1.00 14.90           C  
ANISOU 2659  CG1 ILE A 164     2160   1685   1815   -118     45    137       C  
ATOM   2660  CG2 ILE A 164      44.113  83.297  54.208  1.00 13.16           C  
ANISOU 2660  CG2 ILE A 164     1915   1454   1631   -214   -346    -46       C  
ATOM   2661  CD1 ILE A 164      41.984  82.529  56.373  1.00 15.97           C  
ANISOU 2661  CD1 ILE A 164     2308   1913   1847     39    278    289       C  
ATOM   2662  H   ILE A 164      43.314  79.436  54.434  1.00 15.70           H  
ATOM   2663  HA  ILE A 164      43.107  81.292  52.627  1.00 14.86           H  
ATOM   2664  HB  ILE A 164      44.133  81.526  55.254  1.00 16.09           H  
ATOM   2665 HG12 ILE A 164      41.621  82.427  54.368  1.00 17.88           H  
ATOM   2666 HG13 ILE A 164      41.815  80.998  55.035  1.00 17.88           H  
ATOM   2667 HG21 ILE A 164      43.823  83.905  54.907  1.00 15.80           H  
ATOM   2668 HG22 ILE A 164      45.082  83.279  54.167  1.00 15.80           H  
ATOM   2669 HG23 ILE A 164      43.750  83.579  53.354  1.00 15.80           H  
ATOM   2670 HD11 ILE A 164      41.077  82.380  56.681  1.00 19.17           H  
ATOM   2671 HD12 ILE A 164      42.613  82.114  56.983  1.00 19.17           H  
ATOM   2672 HD13 ILE A 164      42.161  83.481  56.313  1.00 19.17           H  
ATOM   2673  N   ASN A 165      46.120  80.424  53.318  1.00 11.73           N  
ANISOU 2673  N   ASN A 165     1393   1562   1503   -186    -76     99       N  
ATOM   2674  CA  ASN A 165      47.500  80.428  52.840  1.00 11.59           C  
ANISOU 2674  CA  ASN A 165     1450   1432   1523   -146   -110      8       C  
ATOM   2675  C   ASN A 165      47.539  80.020  51.372  1.00 12.19           C  
ANISOU 2675  C   ASN A 165     1514   1476   1641   -175   -116   -124       C  
ATOM   2676  O   ASN A 165      48.131  80.711  50.530  1.00 11.83           O  
ANISOU 2676  O   ASN A 165     1553   1467   1474    -94   -155   -138       O  
ATOM   2677  CB  ASN A 165      48.297  79.471  53.742  1.00 12.84           C  
ANISOU 2677  CB  ASN A 165     1798   1648   1432    -44   -171    -10       C  
ATOM   2678  CG  ASN A 165      49.796  79.571  53.555  1.00 14.07           C  
ANISOU 2678  CG  ASN A 165     1893   1961   1492    132   -221    205       C  
ATOM   2679  OD1 ASN A 165      50.273  79.871  52.477  1.00 16.55           O  
ANISOU 2679  OD1 ASN A 165     1934   2687   1668    428   -126    427       O  
ATOM   2680  ND2 ASN A 165      50.537  79.303  54.615  1.00 13.79           N  
ANISOU 2680  ND2 ASN A 165     1687   1899   1654    -27   -348    102       N  
ATOM   2681  H   ASN A 165      46.003  79.943  54.021  1.00 14.09           H  
ATOM   2682  HA  ASN A 165      47.907  81.306  52.898  1.00 13.92           H  
ATOM   2683  HB2 ASN A 165      48.100  79.677  54.669  1.00 15.41           H  
ATOM   2684  HB3 ASN A 165      48.033  78.559  53.541  1.00 15.41           H  
ATOM   2685 HD21 ASN A 165      51.394  79.345  54.563  1.00 16.56           H  
ATOM   2686 HD22 ASN A 165      50.162  79.086  55.358  1.00 16.56           H  
ATOM   2687  N  AGLU A 166      46.864  78.922  51.028  0.46 11.88           N  
ANISOU 2687  N  AGLU A 166     1495   1430   1587   -199   -236    -21       N  
ATOM   2688  N  BGLU A 166      46.879  78.908  51.049  0.54 11.91           N  
ANISOU 2688  N  BGLU A 166     1521   1402   1601   -235   -231     32       N  
ATOM   2689  CA AGLU A 166      46.839  78.469  49.640  0.46 11.67           C  
ANISOU 2689  CA AGLU A 166     1529   1340   1566     24   -307    -82       C  
ATOM   2690  CA BGLU A 166      46.776  78.441  49.671  0.54 11.86           C  
ANISOU 2690  CA BGLU A 166     1626   1281   1598    -45   -270    -12       C  
ATOM   2691  C  AGLU A 166      46.097  79.449  48.730  0.46 11.63           C  
ANISOU 2691  C  AGLU A 166     1420   1357   1640     28   -247   -121       C  
ATOM   2692  C  BGLU A 166      46.122  79.483  48.771  0.54 12.10           C  
ANISOU 2692  C  BGLU A 166     1514   1399   1684      3   -160    -38       C  
ATOM   2693  O  AGLU A 166      46.519  79.679  47.592  0.46 11.78           O  
ANISOU 2693  O  AGLU A 166     1396   1474   1606    -41   -411   -194       O  
ATOM   2694  O  BGLU A 166      46.618  79.778  47.679  0.54 12.90           O  
ANISOU 2694  O  BGLU A 166     1562   1637   1701   -102   -161    -45       O  
ATOM   2695  CB AGLU A 166      46.230  77.070  49.546  0.46 12.46           C  
ANISOU 2695  CB AGLU A 166     1555   1558   1621    134   -348    -50       C  
ATOM   2696  CB BGLU A 166      45.966  77.144  49.645  0.54 12.78           C  
ANISOU 2696  CB BGLU A 166     1755   1408   1694     11   -310      5       C  
ATOM   2697  CG AGLU A 166      47.068  75.983  50.211  0.46 12.59           C  
ANISOU 2697  CG AGLU A 166     1591   1654   1539    -83   -325     32       C  
ATOM   2698  CG BGLU A 166      46.813  75.909  49.755  0.54 12.77           C  
ANISOU 2698  CG BGLU A 166     1755   1366   1730   -241   -188     48       C  
ATOM   2699  CD AGLU A 166      48.478  75.883  49.644  0.46 13.20           C  
ANISOU 2699  CD AGLU A 166     1455   1821   1742    147   -274     21       C  
ATOM   2700  CD BGLU A 166      47.871  75.892  48.686  0.54 12.41           C  
ANISOU 2700  CD BGLU A 166     1626   1398   1691    -76    -75      9       C  
ATOM   2701  OE1AGLU A 166      48.698  76.250  48.467  0.46 12.56           O  
ANISOU 2701  OE1AGLU A 166     1260   1683   1831    179   -234     73       O  
ATOM   2702  OE1BGLU A 166      47.501  75.945  47.490  0.54 12.39           O  
ANISOU 2702  OE1BGLU A 166     1634   1513   1560    -91     44    200       O  
ATOM   2703  OE2AGLU A 166      49.379  75.439  50.382  0.46 15.25           O  
ANISOU 2703  OE2AGLU A 166     1605   2252   1936     31      4    -20       O  
ATOM   2704  OE2BGLU A 166      49.066  75.895  49.048  0.54 11.45           O  
ANISOU 2704  OE2BGLU A 166     1193   1480   1679     81   -226     -4       O  
ATOM   2705  H  AGLU A 166      46.417  78.427  51.571  0.46 14.26           H  
ATOM   2706  H  BGLU A 166      46.477  78.400  51.615  0.54 14.30           H  
ATOM   2707  HA AGLU A 166      47.755  78.416  49.323  0.46 14.02           H  
ATOM   2708  HA BGLU A 166      47.669  78.273  49.330  0.54 14.23           H  
ATOM   2709  HB2AGLU A 166      45.362  77.080  49.979  0.46 14.96           H  
ATOM   2710  HB2BGLU A 166      45.345  77.148  50.391  0.54 15.35           H  
ATOM   2711  HB3AGLU A 166      46.131  76.836  48.610  0.46 14.96           H  
ATOM   2712  HB3BGLU A 166      45.478  77.097  48.808  0.54 15.35           H  
ATOM   2713  HG2AGLU A 166      47.141  76.178  51.159  0.46 15.12           H  
ATOM   2714  HG2BGLU A 166      47.250  75.893  50.621  0.54 15.33           H  
ATOM   2715  HG3AGLU A 166      46.633  75.126  50.081  0.46 15.12           H  
ATOM   2716  HG3BGLU A 166      46.255  75.123  49.650  0.54 15.33           H  
ATOM   2717  N   ALA A 167      44.981  80.021  49.189  1.00 12.13           N  
ANISOU 2717  N   ALA A 167     1405   1551   1655    -11    -68    139       N  
ATOM   2718  CA  ALA A 167      44.267  80.976  48.347  1.00 12.15           C  
ANISOU 2718  CA  ALA A 167     1306   1659   1653   -103   -138    143       C  
ATOM   2719  C   ALA A 167      45.093  82.227  48.094  1.00 11.48           C  
ANISOU 2719  C   ALA A 167     1320   1612   1430    -11     11     65       C  
ATOM   2720  O   ALA A 167      45.101  82.762  46.981  1.00 12.42           O  
ANISOU 2720  O   ALA A 167     1510   1739   1472     96    -17    281       O  
ATOM   2721  CB  ALA A 167      42.936  81.335  48.990  1.00 12.76           C  
ANISOU 2721  CB  ALA A 167     1444   1760   1643   -188     62    193       C  
ATOM   2722  H  AALA A 167      44.627  79.878  49.960  0.46 14.57           H  
ATOM   2723  H  BALA A 167      44.602  79.855  49.943  0.54 14.57           H  
ATOM   2724  HA  ALA A 167      44.090  80.563  47.487  1.00 14.59           H  
ATOM   2725  HB1 ALA A 167      42.473  81.971  48.424  1.00 15.32           H  
ATOM   2726  HB2 ALA A 167      42.404  80.529  49.085  1.00 15.32           H  
ATOM   2727  HB3 ALA A 167      43.102  81.727  49.862  1.00 15.32           H  
ATOM   2728  N   ILE A 168      45.785  82.731  49.111  1.00 11.35           N  
ANISOU 2728  N   ILE A 168     1493   1371   1448    -40    -43     92       N  
ATOM   2729  CA AILE A 168      46.679  83.873  48.934  0.74 11.68           C  
ANISOU 2729  CA AILE A 168     1491   1377   1571    -41     40    -56       C  
ATOM   2730  CA BILE A 168      46.639  83.888  48.887  0.26 11.15           C  
ANISOU 2730  CA BILE A 168     1465   1302   1471    -45     10     69       C  
ATOM   2731  C   ILE A 168      47.683  83.589  47.821  1.00 11.10           C  
ANISOU 2731  C   ILE A 168     1387   1318   1514      1   -123     80       C  
ATOM   2732  O   ILE A 168      47.936  84.417  46.941  1.00 11.82           O  
ANISOU 2732  O   ILE A 168     1511   1437   1541    -73   -187    122       O  
ATOM   2733  CB AILE A 168      47.382  84.186  50.269  0.74 12.48           C  
ANISOU 2733  CB AILE A 168     1627   1407   1707     -5    -12   -246       C  
ATOM   2734  CB BILE A 168      47.238  84.384  50.216  0.26 11.16           C  
ANISOU 2734  CB BILE A 168     1554   1230   1458    -10     84    123       C  
ATOM   2735  CG1AILE A 168      46.415  84.810  51.286  0.74 15.35           C  
ANISOU 2735  CG1AILE A 168     1841   1789   2204   -108    162   -327       C  
ATOM   2736  CG1BILE A 168      46.100  84.966  51.060  0.26 11.64           C  
ANISOU 2736  CG1BILE A 168     1720   1219   1483   -152     60    442       C  
ATOM   2737  CG2AILE A 168      48.645  85.029  50.087  0.74 13.11           C  
ANISOU 2737  CG2AILE A 168     1792   1348   1840    -70    -18    -94       C  
ATOM   2738  CG2BILE A 168      48.332  85.410  49.973  0.26 12.18           C  
ANISOU 2738  CG2BILE A 168     1623   1402   1604     47    218    -68       C  
ATOM   2739  CD1AILE A 168      45.927  86.195  50.945  0.74 16.64           C  
ANISOU 2739  CD1AILE A 168     2008   1972   2341     25     69   -376       C  
ATOM   2740  CD1BILE A 168      46.514  85.464  52.411  0.26 11.33           C  
ANISOU 2740  CD1BILE A 168     1754   1221   1330   -180   -179    669       C  
ATOM   2741  H  AILE A 168      45.758  82.431  49.917  0.74 13.63           H  
ATOM   2742  H  BILE A 168      45.779  82.430  49.917  0.26 13.63           H  
ATOM   2743  HA AILE A 168      46.161  84.649  48.669  0.74 14.03           H  
ATOM   2744  HA BILE A 168      46.097  84.615  48.542  0.26 13.39           H  
ATOM   2745  HB AILE A 168      47.673  83.334  50.632  0.74 14.98           H  
ATOM   2746  HB BILE A 168      47.651  83.645  50.689  0.26 13.40           H  
ATOM   2747 HG12AILE A 168      45.635  84.238  51.357  0.74 18.43           H  
ATOM   2748 HG12BILE A 168      45.712  85.714  50.579  0.26 13.97           H  
ATOM   2749 HG13AILE A 168      46.865  84.865  52.143  0.74 18.43           H  
ATOM   2750 HG13BILE A 168      45.432  84.276  51.195  0.26 13.97           H  
ATOM   2751 HG21AILE A 168      48.897  85.409  50.943  0.74 15.74           H  
ATOM   2752 HG21BILE A 168      48.605  85.788  50.824  0.26 14.63           H  
ATOM   2753 HG22AILE A 168      49.358  84.462  49.755  0.74 15.74           H  
ATOM   2754 HG22BILE A 168      49.086  84.973  49.547  0.26 14.63           H  
ATOM   2755 HG23AILE A 168      48.462  85.738  49.451  0.74 15.74           H  
ATOM   2756 HG23BILE A 168      47.986  86.110  49.397  0.26 14.63           H  
ATOM   2757 HD11AILE A 168      45.371  86.521  51.670  0.74 19.97           H  
ATOM   2758 HD11BILE A 168      45.738  85.484  52.992  0.26 13.60           H  
ATOM   2759 HD12AILE A 168      46.692  86.779  50.826  0.74 19.97           H  
ATOM   2760 HD12BILE A 168      47.185  84.866  52.776  0.26 13.60           H  
ATOM   2761 HD13AILE A 168      45.410  86.155  50.125  0.74 19.97           H  
ATOM   2762 HD13BILE A 168      46.882  86.357  52.320  0.26 13.60           H  
ATOM   2763  N   SER A 169      48.265  82.385  47.843  1.00 11.22           N  
ANISOU 2763  N   SER A 169     1356   1478   1429   -119   -130     85       N  
ATOM   2764  CA  SER A 169      49.215  82.002  46.797  1.00 10.70           C  
ANISOU 2764  CA  SER A 169     1147   1563   1355    -42   -205    201       C  
ATOM   2765  C   SER A 169      48.549  81.891  45.424  1.00 10.75           C  
ANISOU 2765  C   SER A 169     1161   1403   1522    131   -123     65       C  
ATOM   2766  O   SER A 169      49.171  82.234  44.415  1.00 11.13           O  
ANISOU 2766  O   SER A 169     1399   1598   1230    -11   -173     19       O  
ATOM   2767  CB  SER A 169      49.909  80.697  47.203  1.00 11.40           C  
ANISOU 2767  CB  SER A 169     1222   1710   1398   -114   -383     73       C  
ATOM   2768  OG  SER A 169      50.968  80.956  48.110  1.00 12.39           O  
ANISOU 2768  OG  SER A 169     1408   1757   1545   -122   -272    238       O  
ATOM   2769  H   SER A 169      48.131  81.781  48.440  1.00 13.47           H  
ATOM   2770  HA  SER A 169      49.893  82.691  46.713  1.00 12.85           H  
ATOM   2771  HB2 SER A 169      49.262  80.114  47.629  1.00 13.68           H  
ATOM   2772  HB3 SER A 169      50.269  80.270  46.410  1.00 13.68           H  
ATOM   2773  HG  SER A 169      51.555  81.429  47.739  1.00 14.88           H  
ATOM   2774  N   ASP A 170      47.307  81.393  45.347  1.00 11.55           N  
ANISOU 2774  N   ASP A 170     1253   1508   1628     14   -218      1       N  
ATOM   2775  CA  ASP A 170      46.609  81.340  44.064  1.00 11.37           C  
ANISOU 2775  CA  ASP A 170     1251   1429   1640     55   -396    144       C  
ATOM   2776  C   ASP A 170      46.252  82.744  43.568  1.00 11.44           C  
ANISOU 2776  C   ASP A 170     1243   1645   1458     82   -296    160       C  
ATOM   2777  O   ASP A 170      46.333  83.030  42.364  1.00 12.68           O  
ANISOU 2777  O   ASP A 170     1579   1767   1472     27   -208     33       O  
ATOM   2778  CB  ASP A 170      45.341  80.507  44.192  1.00 11.48           C  
ANISOU 2778  CB  ASP A 170     1305   1375   1682   -105   -504    158       C  
ATOM   2779  CG  ASP A 170      45.596  79.015  44.232  1.00 12.29           C  
ANISOU 2779  CG  ASP A 170     1210   1569   1890   -168   -393     64       C  
ATOM   2780  OD1 ASP A 170      46.729  78.578  43.923  1.00 12.63           O  
ANISOU 2780  OD1 ASP A 170     1255   1637   1908      0   -307    -66       O  
ATOM   2781  OD2 ASP A 170      44.642  78.276  44.575  1.00 13.73           O  
ANISOU 2781  OD2 ASP A 170     1346   1784   2088   -132   -381    102       O  
ATOM   2782  H   ASP A 170      46.856  81.085  46.012  1.00 13.87           H  
ATOM   2783  HA  ASP A 170      47.194  80.919  43.415  1.00 13.65           H  
ATOM   2784  HB2 ASP A 170      44.887  80.752  45.014  1.00 13.78           H  
ATOM   2785  HB3 ASP A 170      44.769  80.690  43.430  1.00 13.78           H  
ATOM   2786  N   ILE A 171      45.844  83.618  44.483  1.00 11.66           N  
ANISOU 2786  N   ILE A 171     1300   1612   1518    -23    -48     -6       N  
ATOM   2787  CA  ILE A 171      45.484  84.989  44.130  1.00 11.88           C  
ANISOU 2787  CA  ILE A 171     1387   1556   1571    107     15    142       C  
ATOM   2788  C   ILE A 171      46.693  85.719  43.557  1.00 11.75           C  
ANISOU 2788  C   ILE A 171     1344   1560   1562     52    -48     46       C  
ATOM   2789  O   ILE A 171      46.635  86.270  42.450  1.00 12.29           O  
ANISOU 2789  O   ILE A 171     1475   1581   1613    -58    -93    164       O  
ATOM   2790  CB  ILE A 171      44.893  85.727  45.346  1.00 12.71           C  
ANISOU 2790  CB  ILE A 171     1407   1561   1859    167     86    189       C  
ATOM   2791  CG1 ILE A 171      43.517  85.154  45.709  1.00 13.43           C  
ANISOU 2791  CG1 ILE A 171     1348   1922   1832    221     75    235       C  
ATOM   2792  CG2 ILE A 171      44.838  87.265  45.095  1.00 14.46           C  
ANISOU 2792  CG2 ILE A 171     1743   1626   2127     47    199    197       C  
ATOM   2793  CD1 ILE A 171      43.081  85.495  47.136  1.00 14.30           C  
ANISOU 2793  CD1 ILE A 171     1292   2205   1936    279    138    180       C  
ATOM   2794  H   ILE A 171      45.765  83.445  45.322  1.00 14.00           H  
ATOM   2795  HA  ILE A 171      44.799  84.961  43.443  1.00 14.27           H  
ATOM   2796  HB  ILE A 171      45.478  85.583  46.106  1.00 15.25           H  
ATOM   2797 HG12 ILE A 171      42.855  85.516  45.099  1.00 16.12           H  
ATOM   2798 HG13 ILE A 171      43.549  84.188  45.629  1.00 16.12           H  
ATOM   2799 HG21 ILE A 171      44.262  87.673  45.760  1.00 17.36           H  
ATOM   2800 HG22 ILE A 171      45.734  87.629  45.165  1.00 17.36           H  
ATOM   2801 HG23 ILE A 171      44.483  87.427  44.206  1.00 17.36           H  
ATOM   2802 HD11 ILE A 171      42.231  85.063  47.317  1.00 17.17           H  
ATOM   2803 HD12 ILE A 171      43.754  85.175  47.757  1.00 17.17           H  
ATOM   2804 HD13 ILE A 171      42.987  86.457  47.216  1.00 17.17           H  
ATOM   2805  N   PHE A 172      47.822  85.695  44.274  1.00 11.37           N  
ANISOU 2805  N   PHE A 172     1409   1542   1369     -9   -107    237       N  
ATOM   2806  CA  PHE A 172      48.996  86.420  43.771  1.00 12.25           C  
ANISOU 2806  CA  PHE A 172     1528   1663   1465    178   -111    167       C  
ATOM   2807  C   PHE A 172      49.660  85.695  42.616  1.00 11.05           C  
ANISOU 2807  C   PHE A 172     1402   1520   1275    155    -83    166       C  
ATOM   2808  O   PHE A 172      50.212  86.344  41.719  1.00 12.41           O  
ANISOU 2808  O   PHE A 172     1588   1696   1431     79   -140    341       O  
ATOM   2809  CB  PHE A 172      49.934  86.795  44.918  1.00 11.91           C  
ANISOU 2809  CB  PHE A 172     1279   1604   1641    241   -208    157       C  
ATOM   2810  CG  PHE A 172      49.367  87.872  45.778  1.00 11.50           C  
ANISOU 2810  CG  PHE A 172     1288   1531   1552    122     25    138       C  
ATOM   2811  CD1 PHE A 172      49.212  89.139  45.270  1.00 12.09           C  
ANISOU 2811  CD1 PHE A 172     1348   1628   1620     13    -35     85       C  
ATOM   2812  CD2 PHE A 172      48.898  87.600  47.060  1.00 12.51           C  
ANISOU 2812  CD2 PHE A 172     1667   1437   1651    100    146    102       C  
ATOM   2813  CE1 PHE A 172      48.635  90.142  46.026  1.00 13.53           C  
ANISOU 2813  CE1 PHE A 172     1764   1488   1890   -113     10     52       C  
ATOM   2814  CE2 PHE A 172      48.314  88.582  47.813  1.00 13.81           C  
ANISOU 2814  CE2 PHE A 172     1816   1597   1834    -64    356     51       C  
ATOM   2815  CZ  PHE A 172      48.187  89.868  47.301  1.00 13.64           C  
ANISOU 2815  CZ  PHE A 172     1838   1375   1971   -255    310    -21       C  
ATOM   2816  H   PHE A 172      47.933  85.285  45.022  1.00 13.65           H  
ATOM   2817  HA  PHE A 172      48.728  87.277  43.403  1.00 14.71           H  
ATOM   2818  HB2 PHE A 172      50.086  86.014  45.473  1.00 14.30           H  
ATOM   2819  HB3 PHE A 172      50.775  87.110  44.552  1.00 14.30           H  
ATOM   2820  HD1 PHE A 172      49.499  89.324  44.405  1.00 14.52           H  
ATOM   2821  HD2 PHE A 172      48.983  86.742  47.408  1.00 15.02           H  
ATOM   2822  HE1 PHE A 172      48.549  91.000  45.675  1.00 16.25           H  
ATOM   2823  HE2 PHE A 172      48.002  88.389  48.668  1.00 16.58           H  
ATOM   2824  HZ  PHE A 172      47.802  90.540  47.816  1.00 16.38           H  
ATOM   2825  N   GLY A 173      49.578  84.361  42.575  1.00 11.30           N  
ANISOU 2825  N   GLY A 173     1466   1577   1252    -48   -151    133       N  
ATOM   2826  CA  GLY A 173      50.057  83.663  41.394  1.00 12.24           C  
ANISOU 2826  CA  GLY A 173     1427   1877   1348     33   -172    -33       C  
ATOM   2827  C   GLY A 173      49.311  84.118  40.155  1.00 12.54           C  
ANISOU 2827  C   GLY A 173     1440   1831   1495    170   -288   -109       C  
ATOM   2828  O   GLY A 173      49.912  84.362  39.109  1.00 12.70           O  
ANISOU 2828  O   GLY A 173     1509   1806   1511    236    -95    -86       O  
ATOM   2829  H   GLY A 173      49.261  83.858  43.196  1.00 13.57           H  
ATOM   2830  HA2 GLY A 173      51.003  83.839  41.271  1.00 14.70           H  
ATOM   2831  HA3 GLY A 173      49.925  82.708  41.504  1.00 14.70           H  
ATOM   2832  N   THR A 174      47.992  84.280  40.277  1.00 12.41           N  
ANISOU 2832  N   THR A 174     1373   1783   1558    397   -240    130       N  
ATOM   2833  CA  THR A 174      47.176  84.742  39.161  1.00 12.32           C  
ANISOU 2833  CA  THR A 174     1388   1761   1533    345    -83    100       C  
ATOM   2834  C   THR A 174      47.442  86.212  38.857  1.00 12.47           C  
ANISOU 2834  C   THR A 174     1576   1732   1431    312    -69    100       C  
ATOM   2835  O   THR A 174      47.487  86.608  37.687  1.00 13.25           O  
ANISOU 2835  O   THR A 174     1634   1868   1534    225   -118    182       O  
ATOM   2836  CB  THR A 174      45.711  84.479  39.511  1.00 11.88           C  
ANISOU 2836  CB  THR A 174     1293   1661   1557    282   -111    172       C  
ATOM   2837  OG1 THR A 174      45.494  83.051  39.496  1.00 12.98           O  
ANISOU 2837  OG1 THR A 174     1200   1808   1923    155   -111     66       O  
ATOM   2838  CG2 THR A 174      44.750  85.176  38.549  1.00 13.07           C  
ANISOU 2838  CG2 THR A 174     1460   1928   1577    160   -122    157       C  
ATOM   2839  H   THR A 174      47.545  84.130  40.997  1.00 14.90           H  
ATOM   2840  HA  THR A 174      47.389  84.254  38.351  1.00 14.80           H  
ATOM   2841  HB  THR A 174      45.515  84.841  40.389  1.00 14.26           H  
ATOM   2842  HG1 THR A 174      44.686  82.881  39.648  1.00 15.58           H  
ATOM   2843 HG21 THR A 174      43.856  84.814  38.653  1.00 15.69           H  
ATOM   2844 HG22 THR A 174      44.728  86.128  38.734  1.00 15.69           H  
ATOM   2845 HG23 THR A 174      45.040  85.039  37.634  1.00 15.69           H  
ATOM   2846  N   LEU A 175      47.613  87.039  39.878  1.00 12.18           N  
ANISOU 2846  N   LEU A 175     1562   1624   1441    158    -70    112       N  
ATOM   2847  CA  LEU A 175      47.883  88.443  39.606  1.00 11.87           C  
ANISOU 2847  CA  LEU A 175     1422   1555   1533    248   -114    125       C  
ATOM   2848  C   LEU A 175      49.249  88.627  38.943  1.00 12.16           C  
ANISOU 2848  C   LEU A 175     1497   1508   1617    412    -18    119       C  
ATOM   2849  O   LEU A 175      49.402  89.526  38.103  1.00 13.51           O  
ANISOU 2849  O   LEU A 175     1654   1671   1808    177    160    206       O  
ATOM   2850  CB  LEU A 175      47.715  89.273  40.876  1.00 12.42           C  
ANISOU 2850  CB  LEU A 175     1505   1614   1601    162   -194    208       C  
ATOM   2851  CG  LEU A 175      46.277  89.337  41.409  1.00 12.42           C  
ANISOU 2851  CG  LEU A 175     1496   1697   1525    333   -210    119       C  
ATOM   2852  CD1 LEU A 175      46.234  90.015  42.770  1.00 14.43           C  
ANISOU 2852  CD1 LEU A 175     1994   1742   1747     49    140    -80       C  
ATOM   2853  CD2 LEU A 175      45.388  90.089  40.399  1.00 13.87           C  
ANISOU 2853  CD2 LEU A 175     1568   2008   1693    339     49    376       C  
ATOM   2854  H   LEU A 175      47.579  86.824  40.710  1.00 14.62           H  
ATOM   2855  HA  LEU A 175      47.229  88.790  38.980  1.00 14.25           H  
ATOM   2856  HB2 LEU A 175      48.269  88.886  41.572  1.00 14.92           H  
ATOM   2857  HB3 LEU A 175      48.000  90.181  40.691  1.00 14.92           H  
ATOM   2858  HG  LEU A 175      45.931  88.438  41.522  1.00 14.91           H  
ATOM   2859 HD11 LEU A 175      45.313  90.063  43.071  1.00 17.33           H  
ATOM   2860 HD12 LEU A 175      46.761  89.497  43.398  1.00 17.33           H  
ATOM   2861 HD13 LEU A 175      46.602  90.909  42.689  1.00 17.33           H  
ATOM   2862 HD21 LEU A 175      44.539  90.297  40.819  1.00 16.65           H  
ATOM   2863 HD22 LEU A 175      45.835  90.908  40.133  1.00 16.65           H  
ATOM   2864 HD23 LEU A 175      45.244  89.524  39.624  1.00 16.65           H  
ATOM   2865  N   VAL A 176      50.233  87.787  39.278  1.00 12.48           N  
ANISOU 2865  N   VAL A 176     1541   1642   1559    269    146    138       N  
ATOM   2866  CA  VAL A 176      51.503  87.820  38.554  1.00 12.10           C  
ANISOU 2866  CA  VAL A 176     1412   1713   1472    352    244    114       C  
ATOM   2867  C   VAL A 176      51.303  87.377  37.113  1.00 12.48           C  
ANISOU 2867  C   VAL A 176     1458   1737   1546    152    121     67       C  
ATOM   2868  O   VAL A 176      51.848  87.986  36.182  1.00 13.45           O  
ANISOU 2868  O   VAL A 176     1552   1912   1646    192    144    174       O  
ATOM   2869  CB  VAL A 176      52.570  86.974  39.277  1.00 12.30           C  
ANISOU 2869  CB  VAL A 176     1480   1709   1484    282    200    186       C  
ATOM   2870  CG1 VAL A 176      53.798  86.824  38.418  1.00 13.71           C  
ANISOU 2870  CG1 VAL A 176     1866   1731   1612    310     95    281       C  
ATOM   2871  CG2 VAL A 176      52.913  87.623  40.589  1.00 12.90           C  
ANISOU 2871  CG2 VAL A 176     1612   1701   1587    151    297     28       C  
ATOM   2872  H   VAL A 176      50.192  87.201  39.906  1.00 14.98           H  
ATOM   2873  HA  VAL A 176      51.823  88.736  38.542  1.00 14.53           H  
ATOM   2874  HB  VAL A 176      52.221  86.085  39.448  1.00 14.76           H  
ATOM   2875 HG11 VAL A 176      54.536  86.525  38.971  1.00 16.46           H  
ATOM   2876 HG12 VAL A 176      53.620  86.171  37.723  1.00 16.46           H  
ATOM   2877 HG13 VAL A 176      54.010  87.683  38.019  1.00 16.46           H  
ATOM   2878 HG21 VAL A 176      53.479  87.023  41.100  1.00 15.48           H  
ATOM   2879 HG22 VAL A 176      53.383  88.454  40.417  1.00 15.48           H  
ATOM   2880 HG23 VAL A 176      52.094  87.801  41.078  1.00 15.48           H  
ATOM   2881  N   GLU A 177      50.490  86.337  36.898  1.00 12.06           N  
ANISOU 2881  N   GLU A 177     1490   1595   1498    123    -65    -66       N  
ATOM   2882  CA  GLU A 177      50.201  85.890  35.536  1.00 12.56           C  
ANISOU 2882  CA  GLU A 177     1488   1707   1577    286     15      1       C  
ATOM   2883  C   GLU A 177      49.572  87.012  34.718  1.00 13.58           C  
ANISOU 2883  C   GLU A 177     1624   1951   1585    147     61    206       C  
ATOM   2884  O   GLU A 177      49.946  87.228  33.560  1.00 14.11           O  
ANISOU 2884  O   GLU A 177     1673   2219   1470    299    -25    345       O  
ATOM   2885  CB  GLU A 177      49.325  84.634  35.592  1.00 12.94           C  
ANISOU 2885  CB  GLU A 177     1363   1950   1603    237   -199    114       C  
ATOM   2886  CG  GLU A 177      49.102  83.957  34.253  1.00 14.08           C  
ANISOU 2886  CG  GLU A 177     1642   1985   1725    180   -443    -49       C  
ATOM   2887  CD  GLU A 177      48.326  82.654  34.381  1.00 13.83           C  
ANISOU 2887  CD  GLU A 177     1650   2095   1508    146   -284   -139       C  
ATOM   2888  OE1 GLU A 177      48.743  81.804  35.175  1.00 13.64           O  
ANISOU 2888  OE1 GLU A 177     1572   2194   1417    214   -360     -1       O  
ATOM   2889  OE2 GLU A 177      47.287  82.469  33.684  1.00 14.00           O  
ANISOU 2889  OE2 GLU A 177     1655   2186   1478    203   -294   -199       O  
ATOM   2890  H   GLU A 177      50.099  85.879  37.512  1.00 14.48           H  
ATOM   2891  HA  GLU A 177      51.021  85.644  35.080  1.00 15.08           H  
ATOM   2892  HB2 GLU A 177      49.749  83.988  36.179  1.00 15.53           H  
ATOM   2893  HB3 GLU A 177      48.455  84.880  35.943  1.00 15.53           H  
ATOM   2894  HG2 GLU A 177      48.599  84.552  33.677  1.00 16.91           H  
ATOM   2895  HG3 GLU A 177      49.963  83.756  33.853  1.00 16.91           H  
ATOM   2896  N   PHE A 178      48.633  87.761  35.304  1.00 13.96           N  
ANISOU 2896  N   PHE A 178     1615   1949   1742    320    -70    317       N  
ATOM   2897  CA  PHE A 178      48.066  88.916  34.605  1.00 14.52           C  
ANISOU 2897  CA  PHE A 178     1751   2019   1746    381   -117    513       C  
ATOM   2898  C   PHE A 178      49.092  90.034  34.416  1.00 14.38           C  
ANISOU 2898  C   PHE A 178     1904   1946   1612    238   -160    470       C  
ATOM   2899  O   PHE A 178      49.100  90.703  33.377  1.00 16.65           O  
ANISOU 2899  O   PHE A 178     2373   2100   1852     67   -242    680       O  
ATOM   2900  CB  PHE A 178      46.826  89.454  35.335  1.00 14.59           C  
ANISOU 2900  CB  PHE A 178     1599   2149   1794    374    -53    426       C  
ATOM   2901  CG  PHE A 178      45.536  88.777  34.939  1.00 14.06           C  
ANISOU 2901  CG  PHE A 178     1587   2107   1650    409    -34    399       C  
ATOM   2902  CD1 PHE A 178      44.827  89.197  33.828  1.00 14.86           C  
ANISOU 2902  CD1 PHE A 178     1778   2187   1682    511    -77    406       C  
ATOM   2903  CD2 PHE A 178      45.028  87.720  35.682  1.00 14.61           C  
ANISOU 2903  CD2 PHE A 178     1636   2218   1697    360    -93    312       C  
ATOM   2904  CE1 PHE A 178      43.648  88.567  33.453  1.00 15.21           C  
ANISOU 2904  CE1 PHE A 178     1760   2304   1716    605    -65    396       C  
ATOM   2905  CE2 PHE A 178      43.845  87.090  35.316  1.00 15.52           C  
ANISOU 2905  CE2 PHE A 178     1844   2404   1650    386   -131    122       C  
ATOM   2906  CZ  PHE A 178      43.164  87.500  34.207  1.00 14.98           C  
ANISOU 2906  CZ  PHE A 178     1771   2371   1551    285   -155    200       C  
ATOM   2907  H   PHE A 178      48.311  87.627  36.090  1.00 16.76           H  
ATOM   2908  HA  PHE A 178      47.785  88.611  33.727  1.00 17.43           H  
ATOM   2909  HB2 PHE A 178      46.946  89.323  36.289  1.00 17.51           H  
ATOM   2910  HB3 PHE A 178      46.735  90.399  35.138  1.00 17.51           H  
ATOM   2911  HD1 PHE A 178      45.145  89.911  33.324  1.00 17.84           H  
ATOM   2912  HD2 PHE A 178      45.487  87.429  36.436  1.00 17.54           H  
ATOM   2913  HE1 PHE A 178      43.183  88.855  32.701  1.00 18.26           H  
ATOM   2914  HE2 PHE A 178      43.516  86.387  35.829  1.00 18.63           H  
ATOM   2915  HZ  PHE A 178      42.379  87.069  33.956  1.00 17.99           H  
ATOM   2916  N  ATYR A 179      49.950  90.255  35.410  0.39 15.11           N  
ANISOU 2916  N  ATYR A 179     2092   1904   1745    302   -108    256       N  
ATOM   2917  N  BTYR A 179      49.949  90.264  35.409  0.61 14.03           N  
ANISOU 2917  N  BTYR A 179     1863   1785   1684    269     24    269       N  
ATOM   2918  CA ATYR A 179      50.971  91.293  35.309  0.39 16.41           C  
ANISOU 2918  CA ATYR A 179     2362   1995   1877    322   -132    309       C  
ATOM   2919  CA BTYR A 179      50.992  91.281  35.294  0.61 14.78           C  
ANISOU 2919  CA BTYR A 179     1984   1862   1771    214     66    468       C  
ATOM   2920  C  ATYR A 179      51.883  91.055  34.110  0.39 16.50           C  
ANISOU 2920  C  ATYR A 179     2399   1927   1944    463   -154    308       C  
ATOM   2921  C  BTYR A 179      51.928  90.987  34.126  0.61 15.71           C  
ANISOU 2921  C  BTYR A 179     2212   2021   1735    119     54    511       C  
ATOM   2922  O  ATYR A 179      52.231  92.001  33.386  0.39 17.54           O  
ANISOU 2922  O  ATYR A 179     2605   2028   2033    305    -43    311       O  
ATOM   2923  O  BTYR A 179      52.282  91.888  33.348  0.61 16.89           O  
ANISOU 2923  O  BTYR A 179     2359   2207   1852      6    161    453       O  
ATOM   2924  CB ATYR A 179      51.767  91.333  36.614  0.39 17.47           C  
ANISOU 2924  CB ATYR A 179     2578   2145   1915     25   -105    167       C  
ATOM   2925  CB BTYR A 179      51.770  91.350  36.609  0.61 14.34           C  
ANISOU 2925  CB BTYR A 179     1841   1771   1838     -8    209    362       C  
ATOM   2926  CG ATYR A 179      52.730  92.484  36.715  0.39 18.72           C  
ANISOU 2926  CG ATYR A 179     2760   2306   2046   -148   -134    153       C  
ATOM   2927  CG BTYR A 179      53.002  92.222  36.566  0.61 14.19           C  
ANISOU 2927  CG BTYR A 179     1655   1699   2039     78    262    425       C  
ATOM   2928  CD1ATYR A 179      54.097  92.266  36.677  0.39 19.33           C  
ANISOU 2928  CD1ATYR A 179     2873   2358   2112   -273   -124    112       C  
ATOM   2929  CD1BTYR A 179      54.236  91.696  36.221  0.61 14.56           C  
ANISOU 2929  CD1BTYR A 179     1603   1575   2355    128    304    274       C  
ATOM   2930  CD2ATYR A 179      52.275  93.789  36.851  0.39 20.10           C  
ANISOU 2930  CD2ATYR A 179     2929   2498   2212   -228   -139     78       C  
ATOM   2931  CD2BTYR A 179      52.934  93.566  36.883  0.61 15.60           C  
ANISOU 2931  CD2BTYR A 179     1773   1959   2197     62    243    291       C  
ATOM   2932  CE1ATYR A 179      54.987  93.311  36.772  0.39 19.75           C  
ANISOU 2932  CE1ATYR A 179     2954   2373   2178   -401   -138    105       C  
ATOM   2933  CE1BTYR A 179      55.368  92.486  36.192  0.61 15.23           C  
ANISOU 2933  CE1BTYR A 179     1638   1695   2454    -20    272    285       C  
ATOM   2934  CE2ATYR A 179      53.160  94.844  36.946  0.39 20.69           C  
ANISOU 2934  CE2ATYR A 179     3070   2537   2256   -276    -82     41       C  
ATOM   2935  CE2BTYR A 179      54.056  94.362  36.863  0.61 15.67           C  
ANISOU 2935  CE2BTYR A 179     1650   1976   2330    -49    240    211       C  
ATOM   2936  CZ ATYR A 179      54.514  94.596  36.906  0.39 20.72           C  
ANISOU 2936  CZ ATYR A 179     3097   2469   2306   -380   -102    113       C  
ATOM   2937  CZ BTYR A 179      55.271  93.817  36.506  0.61 15.81           C  
ANISOU 2937  CZ BTYR A 179     1678   1849   2478   -122    118    176       C  
ATOM   2938  OH ATYR A 179      55.404  95.633  37.000  0.39 21.43           O  
ANISOU 2938  OH ATYR A 179     3330   2310   2503   -458     51    396       O  
ATOM   2939  OH BTYR A 179      56.408  94.597  36.468  0.61 16.27           O  
ANISOU 2939  OH BTYR A 179     1843   1807   2532   -317     40    208       O  
ATOM   2940  H  ATYR A 179      49.964  89.821  36.153  0.39 18.14           H  
ATOM   2941  H  BTYR A 179      49.951  89.846  36.161  0.61 16.85           H  
ATOM   2942  HA ATYR A 179      50.551  92.158  35.180  0.39 19.70           H  
ATOM   2943  HA BTYR A 179      50.582  92.145  35.129  0.61 17.74           H  
ATOM   2944  HB2ATYR A 179      51.144  91.405  37.354  0.39 20.97           H  
ATOM   2945  HB2BTYR A 179      51.185  91.704  37.296  0.61 17.22           H  
ATOM   2946  HB3ATYR A 179      52.279  90.513  36.690  0.39 20.97           H  
ATOM   2947  HB3BTYR A 179      52.055  90.453  36.846  0.61 17.22           H  
ATOM   2948  HD1ATYR A 179      54.419  91.399  36.586  0.39 23.20           H  
ATOM   2949  HD1BTYR A 179      54.303  90.794  36.005  0.61 17.48           H  
ATOM   2950  HD2ATYR A 179      51.360  93.955  36.878  0.39 24.13           H  
ATOM   2951  HD2BTYR A 179      52.114  93.939  37.115  0.61 18.73           H  
ATOM   2952  HE1ATYR A 179      55.903  93.150  36.744  0.39 23.71           H  
ATOM   2953  HE1BTYR A 179      56.190  92.118  35.961  0.61 18.28           H  
ATOM   2954  HE2ATYR A 179      52.845  95.714  37.036  0.39 24.84           H  
ATOM   2955  HE2BTYR A 179      53.995  95.262  37.089  0.61 18.82           H  
ATOM   2956  HH ATYR A 179      54.991  96.361  37.067  0.39 25.72           H  
ATOM   2957  HH BTYR A 179      56.198  95.408  36.408  0.61 19.53           H  
ATOM   2958  N  AALA A 180      52.289  89.800  33.884  0.41 15.54           N  
ANISOU 2958  N  AALA A 180     2139   1795   1970    642   -219    105       N  
ATOM   2959  N  BALA A 180      52.365  89.728  33.998  0.25 15.38           N  
ANISOU 2959  N  BALA A 180     2148   2028   1667     71     16    338       N  
ATOM   2960  N  CALA A 180      52.214  89.757  33.905  0.34 14.72           N  
ANISOU 2960  N  CALA A 180     2056   2446   1093    -60    626    278       N  
ATOM   2961  CA AALA A 180      52.986  89.459  32.647  0.41 15.46           C  
ANISOU 2961  CA AALA A 180     2140   1772   1963    792   -272    -10       C  
ATOM   2962  CA BALA A 180      53.185  89.342  32.854  0.25 15.82           C  
ANISOU 2962  CA BALA A 180     2277   2112   1623     -7    -22    164       C  
ATOM   2963  CA CALA A 180      53.177  89.299  32.909  0.34 15.12           C  
ANISOU 2963  CA CALA A 180     2205   2473   1068    -95    700    359       C  
ATOM   2964  C  AALA A 180      52.073  89.644  31.441  0.41 16.84           C  
ANISOU 2964  C  AALA A 180     2371   1899   2130   1024   -240     -3       C  
ATOM   2965  C  BALA A 180      52.453  89.585  31.542  0.25 16.74           C  
ANISOU 2965  C  BALA A 180     2433   2269   1659      7    -91    119       C  
ATOM   2966  C  CALA A 180      52.549  89.142  31.529  0.34 15.84           C  
ANISOU 2966  C  CALA A 180     2334   2533   1151     66    637    440       C  
ATOM   2967  O  AALA A 180      52.496  90.162  30.401  0.41 18.32           O  
ANISOU 2967  O  AALA A 180     2571   2117   2273   1007   -217     -7       O  
ATOM   2968  O  BALA A 180      53.083  89.911  30.529  0.25 16.80           O  
ANISOU 2968  O  BALA A 180     2394   2302   1689   -179   -156    127       O  
ATOM   2969  O  CALA A 180      53.263  89.046  30.527  0.34 16.01           O  
ANISOU 2969  O  CALA A 180     2288   2652   1144    119    718    421       O  
ATOM   2970  CB AALA A 180      53.483  88.014  32.711  0.41 15.07           C  
ANISOU 2970  CB AALA A 180     1956   1866   1903    778   -296    -88       C  
ATOM   2971  CB BALA A 180      53.578  87.868  32.972  0.25 15.71           C  
ANISOU 2971  CB BALA A 180     2220   2149   1601    -67    -15     67       C  
ATOM   2972  CB CALA A 180      53.778  87.971  33.346  0.34 15.28           C  
ANISOU 2972  CB CALA A 180     2180   2510   1114   -162    771    305       C  
ATOM   2973  H  AALA A 180      52.175  89.139  34.423  0.39 18.66           H  
ATOM   2974  H  BALA A 180      52.202  89.089  34.551  0.61 18.46           H  
ATOM   2975  HA AALA A 180      53.754  90.042  32.545  0.41 18.56           H  
ATOM   2976  HA BALA A 180      53.997  89.873  32.851  0.25 18.99           H  
ATOM   2977  HA CALA A 180      53.879  89.965  32.839  0.34 18.16           H  
ATOM   2978  HB1AALA A 180      53.937  87.799  31.882  0.41 18.09           H  
ATOM   2979  HB1BALA A 180      54.131  87.627  32.213  0.25 18.86           H  
ATOM   2980  HB1CALA A 180      54.570  87.793  32.814  0.34 18.34           H  
ATOM   2981  HB2AALA A 180      54.097  87.924  33.457  0.41 18.09           H  
ATOM   2982  HB2BALA A 180      54.072  87.739  33.797  0.25 18.86           H  
ATOM   2983  HB2CALA A 180      54.016  88.025  34.285  0.34 18.34           H  
ATOM   2984  HB3AALA A 180      52.723  87.424  32.835  0.41 18.09           H  
ATOM   2985  HB3BALA A 180      52.773  87.327  32.981  0.25 18.86           H  
ATOM   2986  HB3CALA A 180      53.124  87.268  33.210  0.34 18.34           H  
ATOM   2987  N  AASN A 181      50.818  89.221  31.568  0.55 18.31           N  
ANISOU 2987  N  AASN A 181     2537   2140   2280    967   -323     20       N  
ATOM   2988  N  BASN A 181      51.134  89.433  31.545  0.21 17.75           N  
ANISOU 2988  N  BASN A 181     2553   2500   1690     87   -174     91       N  
ATOM   2989  N  CASN A 181      51.219  89.102  31.490  0.24 16.81           N  
ANISOU 2989  N  CASN A 181     2397   2620   1368    247    341    413       N  
ATOM   2990  CA AASN A 181      49.772  89.470  30.569  0.55 19.86           C  
ANISOU 2990  CA AASN A 181     2592   2632   2322   1012   -267      5       C  
ATOM   2991  CA BASN A 181      50.285  89.699  30.388  0.21 19.31           C  
ANISOU 2991  CA BASN A 181     2724   2881   1732    287   -172     35       C  
ATOM   2992  CA CASN A 181      50.468  88.876  30.255  0.24 18.57           C  
ANISOU 2992  CA CASN A 181     2535   2856   1666    422    136    415       C  
ATOM   2993  C  AASN A 181      50.077  88.804  29.227  0.55 19.65           C  
ANISOU 2993  C  AASN A 181     2537   2794   2134   1020     45    130       C  
ATOM   2994  C  BASN A 181      50.753  88.922  29.159  0.21 18.85           C  
ANISOU 2994  C  BASN A 181     2568   3012   1580    304    -48    -93       C  
ATOM   2995  C  CASN A 181      50.894  87.576  29.570  0.24 17.89           C  
ANISOU 2995  C  CASN A 181     2291   2834   1672    494    108    382       C  
ATOM   2996  O  AASN A 181      49.742  89.326  28.155  0.55 20.15           O  
ANISOU 2996  O  AASN A 181     2636   2942   2080   1310    204    102       O  
ATOM   2997  O  BASN A 181      51.084  89.489  28.113  0.21 19.11           O  
ANISOU 2997  O  BASN A 181     2568   3028   1665    237     22      6       O  
ATOM   2998  O  CASN A 181      51.109  87.521  28.357  0.24 18.16           O  
ANISOU 2998  O  CASN A 181     2453   2691   1754    559    248    658       O  
ATOM   2999  CB AASN A 181      49.469  90.965  30.412  0.55 20.98           C  
ANISOU 2999  CB AASN A 181     2564   2848   2559   1132   -420   -334       C  
ATOM   3000  CB BASN A 181      50.189  91.197  30.083  0.21 21.14           C  
ANISOU 3000  CB BASN A 181     2997   3120   1916    388   -290     53       C  
ATOM   3001  CB CASN A 181      50.565  90.070  29.302  0.24 20.91           C  
ANISOU 3001  CB CASN A 181     2865   3129   1949    456     74    419       C  
ATOM   3002  CG AASN A 181      48.003  91.294  30.651  0.55 21.17           C  
ANISOU 3002  CG AASN A 181     2364   2986   2692   1043   -765   -250       C  
ATOM   3003  CG BASN A 181      48.988  91.535  29.219  0.21 22.37           C  
ANISOU 3003  CG BASN A 181     3213   3291   1995    505   -380    160       C  
ATOM   3004  CG CASN A 181      49.495  90.035  28.236  0.24 23.39           C  
ANISOU 3004  CG CASN A 181     3175   3438   2275    386    -13    520       C  
ATOM   3005  OD1AASN A 181      47.195  90.409  30.912  0.55 19.72           O  
ANISOU 3005  OD1AASN A 181     1972   2955   2566   1078   -677   -147       O  
ATOM   3006  OD1BASN A 181      47.874  91.081  29.481  0.21 22.89           O  
ANISOU 3006  OD1BASN A 181     3342   3384   1973    651   -318     91       O  
ATOM   3007  OD1CASN A 181      48.476  89.361  28.395  0.24 23.80           O  
ANISOU 3007  OD1CASN A 181     3229   3441   2373    423    -96    592       O  
ATOM   3008  ND2AASN A 181      47.660  92.571  30.577  0.55 23.70           N  
ANISOU 3008  ND2AASN A 181     2645   3341   3018    767   -866   -210       N  
ATOM   3009  ND2BASN A 181      49.213  92.316  28.172  0.21 23.35           N  
ANISOU 3009  ND2BASN A 181     3357   3383   2132    530   -547    186       N  
ATOM   3010  ND2CASN A 181      49.715  90.753  27.143  0.24 25.60           N  
ANISOU 3010  ND2CASN A 181     3403   3729   2593    303     10    378       N  
ATOM   3011  H  AASN A 181      50.536  88.772  32.245  0.41 21.98           H  
ATOM   3012  H  BASN A 181      50.691  89.166  32.233  0.25 21.30           H  
ATOM   3013  H  CASN A 181      50.718  89.204  32.181  0.34 20.17           H  
ATOM   3014  HA AASN A 181      48.960  89.053  30.896  0.55 23.84           H  
ATOM   3015  HA BASN A 181      49.395  89.387  30.612  0.21 23.18           H  
ATOM   3016  HA CASN A 181      49.532  88.780  30.494  0.24 22.29           H  
ATOM   3017  HB2AASN A 181      49.998  91.465  31.054  0.55 25.18           H  
ATOM   3018  HB2BASN A 181      50.108  91.686  30.917  0.21 25.38           H  
ATOM   3019  HB2CASN A 181      50.461  90.891  29.807  0.24 25.10           H  
ATOM   3020  HB3AASN A 181      49.695  91.241  29.510  0.55 25.18           H  
ATOM   3021  HB3BASN A 181      50.989  91.477  29.611  0.21 25.38           H  
ATOM   3022  HB3CASN A 181      51.430  90.057  28.863  0.24 25.10           H  
ATOM   3023 HD21AASN A 181      46.843  92.805  30.705  0.55 28.45           H  
ATOM   3024 HD21BASN A 181      48.564  92.536  27.653  0.21 28.03           H  
ATOM   3025 HD21CASN A 181      49.133  90.762  26.510  0.24 30.72           H  
ATOM   3026 HD22AASN A 181      48.255  93.166  30.401  0.55 28.45           H  
ATOM   3027 HD22BASN A 181      50.008  92.603  28.013  0.21 28.03           H  
ATOM   3028 HD22CASN A 181      50.440  91.209  27.067  0.24 30.72           H  
ATOM   3029  N  ALYS A 182      50.690  87.628  29.278  0.40 18.46           N  
ANISOU 3029  N  ALYS A 182     2322   2763   1930    966     82    138       N  
ATOM   3030  N  BLYS A 182      50.764  87.597  29.304  0.34 17.99           N  
ANISOU 3030  N  BLYS A 182     2358   3038   1440    372    -86   -276       N  
ATOM   3031  N  CLYS A 182      50.999  86.516  30.365  0.26 17.32           N  
ANISOU 3031  N  CLYS A 182     2024   2923   1633    439      7    276       N  
ATOM   3032  CA ALYS A 182      50.836  86.819  28.074  0.40 18.20           C  
ANISOU 3032  CA ALYS A 182     2234   2816   1866    823    -92    297       C  
ATOM   3033  CA BLYS A 182      51.033  86.695  28.189  0.34 18.07           C  
ANISOU 3033  CA BLYS A 182     2301   3089   1475    342   -254   -307       C  
ATOM   3034  CA CLYS A 182      51.396  85.202  29.863  0.26 17.46           C  
ANISOU 3034  CA CLYS A 182     1883   3091   1660    428   -172     30       C  
ATOM   3035  C  ALYS A 182      49.590  85.962  27.828  0.40 18.61           C  
ANISOU 3035  C  ALYS A 182     2294   2962   1816    724   -235    303       C  
ATOM   3036  C  BLYS A 182      49.827  85.822  27.863  0.34 18.01           C  
ANISOU 3036  C  BLYS A 182     2180   3194   1468    389   -433    -62       C  
ATOM   3037  C  CLYS A 182      50.179  84.287  29.847  0.26 16.55           C  
ANISOU 3037  C  CLYS A 182     1679   3130   1478    504   -295   -175       C  
ATOM   3038  O  ALYS A 182      48.927  86.119  26.797  0.40 19.14           O  
ANISOU 3038  O  ALYS A 182     2561   2994   1719    573   -343    386       O  
ATOM   3039  O  BLYS A 182      49.321  85.892  26.736  0.34 17.73           O  
ANISOU 3039  O  BLYS A 182     2311   3117   1307    410   -620     36       O  
ATOM   3040  O  CLYS A 182      49.830  83.688  30.864  0.26 15.73           O  
ANISOU 3040  O  CLYS A 182     1478   3193   1306    580   -442   -318       O  
ATOM   3041  CB ALYS A 182      52.083  85.934  28.167  0.40 18.47           C  
ANISOU 3041  CB ALYS A 182     2030   2962   2026    822   -321    500       C  
ATOM   3042  CB BLYS A 182      52.266  85.833  28.483  0.34 18.55           C  
ANISOU 3042  CB BLYS A 182     2257   3157   1635    451   -471   -389       C  
ATOM   3043  CB CLYS A 182      52.502  84.595  30.736  0.26 18.95           C  
ANISOU 3043  CB CLYS A 182     1978   3264   1960    298   -167     31       C  
ATOM   3044  CG ALYS A 182      52.392  85.209  26.873  0.40 20.80           C  
ANISOU 3044  CG ALYS A 182     2247   3273   2383    647   -267    425       C  
ATOM   3045  CG BLYS A 182      53.557  86.618  28.724  0.34 19.74           C  
ANISOU 3045  CG BLYS A 182     2445   3268   1788    524   -555   -403       C  
ATOM   3046  CG CLYS A 182      53.099  83.289  30.193  0.26 19.87           C  
ANISOU 3046  CG CLYS A 182     2106   3331   2112    284   -249    137       C  
ATOM   3047  CD ALYS A 182      52.912  83.808  27.117  0.40 23.59           C  
ANISOU 3047  CD ALYS A 182     2668   3616   2679    436   -101    397       C  
ATOM   3048  CD BLYS A 182      54.005  87.377  27.492  0.34 21.58           C  
ANISOU 3048  CD BLYS A 182     2665   3482   2053    501   -415   -390       C  
ATOM   3049  CD CLYS A 182      53.614  83.463  28.768  0.26 20.64           C  
ANISOU 3049  CD CLYS A 182     2168   3446   2227    430   -363    234       C  
ATOM   3050  CE ALYS A 182      53.260  83.124  25.809  0.40 25.97           C  
ANISOU 3050  CE ALYS A 182     3030   3909   2927    251     10    357       C  
ATOM   3051  CE BLYS A 182      55.357  88.026  27.700  0.34 23.03           C  
ANISOU 3051  CE BLYS A 182     2900   3625   2224    540   -385   -251       C  
ATOM   3052  CE CLYS A 182      54.490  82.300  28.319  0.26 19.56           C  
ANISOU 3052  CE CLYS A 182     1895   3376   2162    803   -563    496       C  
ATOM   3053  NZ ALYS A 182      54.304  83.885  25.069  0.40 27.37           N  
ANISOU 3053  NZ ALYS A 182     3157   4066   3175     74     74    425       N  
ATOM   3054  NZ BLYS A 182      55.746  88.854  26.525  0.34 24.76           N  
ANISOU 3054  NZ BLYS A 182     3121   3769   2516    468   -351   -142       N  
ATOM   3055  NZ CLYS A 182      53.801  80.970  28.306  0.26 19.55           N  
ANISOU 3055  NZ CLYS A 182     1897   3330   2202    861   -663    537       N  
ATOM   3056  H  ALYS A 182      51.027  87.280  29.989  0.55 22.16           H  
ATOM   3057  H  BLYS A 182      50.616  87.194  30.050  0.21 21.60           H  
ATOM   3058  H  CLYS A 182      50.844  86.530  31.211  0.24 20.79           H  
ATOM   3059  HA ALYS A 182      50.953  87.415  27.318  0.40 21.85           H  
ATOM   3060  HA BLYS A 182      51.230  87.231  27.405  0.34 21.69           H  
ATOM   3061  HA CLYS A 182      51.752  85.284  28.964  0.26 20.96           H  
ATOM   3062  HB2ALYS A 182      52.847  86.489  28.389  0.40 22.17           H  
ATOM   3063  HB2BLYS A 182      52.091  85.307  29.279  0.34 22.27           H  
ATOM   3064  HB2CLYS A 182      53.224  85.238  30.810  0.26 22.75           H  
ATOM   3065  HB3ALYS A 182      51.945  85.268  28.858  0.40 22.17           H  
ATOM   3066  HB3BLYS A 182      52.419  85.246  27.726  0.34 22.27           H  
ATOM   3067  HB3CLYS A 182      52.134  84.406  31.613  0.26 22.75           H  
ATOM   3068  HG2ALYS A 182      51.582  85.142  26.343  0.40 24.97           H  
ATOM   3069  HG2BLYS A 182      53.412  87.259  29.438  0.34 23.70           H  
ATOM   3070  HG2CLYS A 182      53.841  83.016  30.755  0.26 23.85           H  
ATOM   3071  HG3ALYS A 182      53.069  85.702  26.384  0.40 24.97           H  
ATOM   3072  HG3BLYS A 182      54.264  86.001  28.972  0.34 23.70           H  
ATOM   3073  HG3CLYS A 182      52.416  82.600  30.189  0.26 23.85           H  
ATOM   3074  HD2ALYS A 182      53.713  83.851  27.664  0.40 28.32           H  
ATOM   3075  HD2BLYS A 182      54.073  86.764  26.744  0.34 25.91           H  
ATOM   3076  HD2CLYS A 182      52.859  83.523  28.162  0.26 24.77           H  
ATOM   3077  HD3ALYS A 182      52.231  83.284  27.567  0.40 28.32           H  
ATOM   3078  HD3BLYS A 182      53.360  88.074  27.292  0.34 25.91           H  
ATOM   3079  HD3CLYS A 182      54.143  84.275  28.719  0.26 24.77           H  
ATOM   3080  HE2ALYS A 182      53.600  82.233  25.990  0.40 31.17           H  
ATOM   3081  HE2BLYS A 182      55.321  88.601  28.481  0.34 27.64           H  
ATOM   3082  HE2CLYS A 182      54.801  82.477  27.417  0.26 23.48           H  
ATOM   3083  HE3ALYS A 182      52.467  83.069  25.252  0.40 31.17           H  
ATOM   3084  HE3BLYS A 182      56.028  87.338  27.825  0.34 27.64           H  
ATOM   3085  HE3CLYS A 182      55.247  82.231  28.922  0.26 23.48           H  
ATOM   3086  HZ1ALYS A 182      54.582  83.415  24.366  0.40 32.85           H  
ATOM   3087  HZ1BLYS A 182      56.541  89.228  26.666  0.34 29.72           H  
ATOM   3088  HZ1CLYS A 182      54.369  80.334  28.050  0.26 23.47           H  
ATOM   3089  HZ2ALYS A 182      53.972  84.660  24.785  0.40 32.85           H  
ATOM   3090  HZ2BLYS A 182      55.792  88.346  25.796  0.34 29.72           H  
ATOM   3091  HZ2CLYS A 182      53.499  80.775  29.120  0.26 23.47           H  
ATOM   3092  HZ3ALYS A 182      54.999  84.045  25.602  0.40 32.85           H  
ATOM   3093  HZ3BLYS A 182      55.144  89.496  26.392  0.34 29.72           H  
ATOM   3094  HZ3CLYS A 182      53.114  80.988  27.740  0.26 23.47           H  
ATOM   3095  N  AASN A 183      49.281  85.041  28.757  0.70 18.79           N  
ANISOU 3095  N  AASN A 183     2204   3122   1813    688    -55    238       N  
ATOM   3096  N  BASN A 183      49.363  84.972  28.815  0.30 18.10           N  
ANISOU 3096  N  BASN A 183     2055   3264   1560    499   -297    101       N  
ATOM   3097  CA AASN A 183      48.115  84.163  28.626  0.70 17.81           C  
ANISOU 3097  CA AASN A 183     2009   2963   1795    688    -37    159       C  
ATOM   3098  CA BASN A 183      48.173  84.142  28.644  0.30 17.81           C  
ANISOU 3098  CA BASN A 183     1887   3236   1646    579   -222    204       C  
ATOM   3099  C  AASN A 183      47.408  83.987  29.971  0.70 16.48           C  
ANISOU 3099  C  AASN A 183     1889   2752   1620    786    -76     62       C  
ATOM   3100  C  BASN A 183      47.416  83.989  29.966  0.30 16.90           C  
ANISOU 3100  C  BASN A 183     1860   2946   1616    674   -134    118       C  
ATOM   3101  O  AASN A 183      47.207  82.866  30.452  0.70 15.90           O  
ANISOU 3101  O  AASN A 183     2065   2600   1375    715     33    -91       O  
ATOM   3102  O  BASN A 183      47.201  82.863  30.433  0.30 16.90           O  
ANISOU 3102  O  BASN A 183     1971   2899   1551    652    -71     55       O  
ATOM   3103  CB AASN A 183      48.493  82.812  28.022  0.70 16.70           C  
ANISOU 3103  CB AASN A 183     1729   2963   1654    729    -13    -54       C  
ATOM   3104  CB BASN A 183      48.534  82.739  28.146  0.30 17.88           C  
ANISOU 3104  CB BASN A 183     1687   3468   1638    599   -235    291       C  
ATOM   3105  CG AASN A 183      49.687  82.164  28.699  0.70 17.85           C  
ANISOU 3105  CG AASN A 183     2173   2823   1786    771   -167   -196       C  
ATOM   3106  CG BASN A 183      49.422  82.761  26.927  0.30 18.76           C  
ANISOU 3106  CG BASN A 183     1763   3647   1717    619   -262    457       C  
ATOM   3107  OD1AASN A 183      50.265  82.677  29.664  0.70 16.89           O  
ANISOU 3107  OD1AASN A 183     2220   2507   1690    480    -62   -190       O  
ATOM   3108  OD1BASN A 183      48.943  82.859  25.802  0.30 20.40           O  
ANISOU 3108  OD1BASN A 183     1872   3925   1954    526   -117    464       O  
ATOM   3109  ND2AASN A 183      50.066  81.015  28.177  0.70 19.57           N  
ANISOU 3109  ND2AASN A 183     2481   2851   2105    839   -414   -426       N  
ATOM   3110  ND2BASN A 183      50.720  82.635  27.143  0.30 18.07           N  
ANISOU 3110  ND2BASN A 183     1706   3414   1745    797   -372    596       N  
ATOM   3111  H  AASN A 183      49.738  84.910  29.474  0.40 22.55           H  
ATOM   3112  H  BASN A 183      49.738  84.866  29.581  0.34 21.73           H  
ATOM   3113  HA AASN A 183      47.492  84.602  28.026  0.70 21.38           H  
ATOM   3114  HA BASN A 183      47.607  84.586  27.993  0.30 21.38           H  
ATOM   3115  HB2AASN A 183      47.739  82.208  28.106  0.70 20.05           H  
ATOM   3116  HB2BASN A 183      49.004  82.265  28.851  0.30 21.46           H  
ATOM   3117  HB3AASN A 183      48.714  82.938  27.086  0.70 20.05           H  
ATOM   3118  HB3BASN A 183      47.720  82.266  27.915  0.30 21.46           H  
ATOM   3119 HD21AASN A 183      50.736  80.591  28.511  0.70 23.50           H  
ATOM   3120 HD21BASN A 183      51.268  82.641  26.481  0.30 21.69           H  
ATOM   3121 HD22AASN A 183      49.644  80.689  27.503  0.70 23.50           H  
ATOM   3122 HD22BASN A 183      51.015  82.545  27.946  0.30 21.69           H  
ATOM   3123  N   PRO A 184      46.987  85.080  30.585  1.00 16.02           N  
ANISOU 3123  N   PRO A 184     1799   2672   1615    707    -23     75       N  
ATOM   3124  CA  PRO A 184      46.367  84.993  31.910  1.00 15.16           C  
ANISOU 3124  CA  PRO A 184     1734   2584   1441    589   -244   -105       C  
ATOM   3125  C   PRO A 184      44.938  84.471  31.877  1.00 15.60           C  
ANISOU 3125  C   PRO A 184     1772   2739   1417    482   -246   -285       C  
ATOM   3126  O   PRO A 184      44.245  84.466  30.850  1.00 17.65           O  
ANISOU 3126  O   PRO A 184     2005   3091   1612    262   -542     60       O  
ATOM   3127  CB  PRO A 184      46.397  86.444  32.395  1.00 16.36           C  
ANISOU 3127  CB  PRO A 184     1888   2677   1652    730    -55     91       C  
ATOM   3128  CG  PRO A 184      46.246  87.224  31.118  1.00 17.09           C  
ANISOU 3128  CG  PRO A 184     1909   2807   1778    765     -2    204       C  
ATOM   3129  CD  PRO A 184      47.075  86.468  30.101  1.00 16.67           C  
ANISOU 3129  CD  PRO A 184     1819   2609   1904    837     88    307       C  
ATOM   3130  HA  PRO A 184      46.895  84.422  32.488  1.00 18.20           H  
ATOM   3131  HB2 PRO A 184      45.661  86.613  33.003  1.00 19.64           H  
ATOM   3132  HB3 PRO A 184      47.240  86.638  32.832  1.00 19.64           H  
ATOM   3133  HG2 PRO A 184      45.313  87.251  30.854  1.00 20.52           H  
ATOM   3134  HG3 PRO A 184      46.583  88.125  31.239  1.00 20.52           H  
ATOM   3135  HD2 PRO A 184      46.695  86.551  29.212  1.00 20.01           H  
ATOM   3136  HD3 PRO A 184      47.993  86.779  30.100  1.00 20.01           H  
ATOM   3137  N   ASP A 185      44.513  84.043  33.060  1.00 14.51           N  
ANISOU 3137  N   ASP A 185     1594   2401   1521    473   -197    -97       N  
ATOM   3138  CA  ASP A 185      43.227  83.403  33.299  1.00 14.80           C  
ANISOU 3138  CA  ASP A 185     1669   2442   1514    501   -353   -126       C  
ATOM   3139  C   ASP A 185      43.089  83.279  34.803  1.00 14.88           C  
ANISOU 3139  C   ASP A 185     1690   2346   1618    406   -299   -233       C  
ATOM   3140  O   ASP A 185      43.993  83.653  35.555  1.00 14.42           O  
ANISOU 3140  O   ASP A 185     1706   2250   1523    430   -152     -5       O  
ATOM   3141  CB  ASP A 185      43.212  82.027  32.643  1.00 14.90           C  
ANISOU 3141  CB  ASP A 185     1485   2524   1652    685   -255   -227       C  
ATOM   3142  CG  ASP A 185      44.487  81.281  32.917  1.00 15.21           C  
ANISOU 3142  CG  ASP A 185     1530   2510   1739    515   -344   -325       C  
ATOM   3143  OD1 ASP A 185      44.718  80.918  34.093  1.00 13.90           O  
ANISOU 3143  OD1 ASP A 185     1414   2325   1543    272   -263   -220       O  
ATOM   3144  OD2 ASP A 185      45.288  81.124  31.966  1.00 14.80           O  
ANISOU 3144  OD2 ASP A 185     1425   2653   1546    468   -302   -182       O  
ATOM   3145  H   ASP A 185      44.980  84.117  33.778  1.00 17.43           H  
ATOM   3146  HA  ASP A 185      42.498  83.939  32.950  1.00 17.77           H  
ATOM   3147  HB2 ASP A 185      42.472  81.509  32.998  1.00 17.89           H  
ATOM   3148  HB3 ASP A 185      43.117  82.128  31.683  1.00 17.89           H  
ATOM   3149  N   TRP A 186      41.946  82.751  35.236  1.00 14.53           N  
ANISOU 3149  N   TRP A 186     1588   2253   1682    290   -117   -154       N  
ATOM   3150  CA  TRP A 186      41.648  82.512  36.640  1.00 14.33           C  
ANISOU 3150  CA  TRP A 186     1563   2213   1671    277   -140   -197       C  
ATOM   3151  C   TRP A 186      41.715  81.028  36.986  1.00 14.21           C  
ANISOU 3151  C   TRP A 186     1566   2134   1699    379   -182   -103       C  
ATOM   3152  O   TRP A 186      41.043  80.560  37.907  1.00 16.29           O  
ANISOU 3152  O   TRP A 186     2015   2133   2042    176    -35   -159       O  
ATOM   3153  CB  TRP A 186      40.312  83.146  37.015  1.00 14.78           C  
ANISOU 3153  CB  TRP A 186     1644   2205   1766    169    -44     32       C  
ATOM   3154  CG  TRP A 186      40.344  84.631  36.913  1.00 15.38           C  
ANISOU 3154  CG  TRP A 186     1784   2271   1790    231    -14    143       C  
ATOM   3155  CD1 TRP A 186      40.093  85.381  35.801  1.00 15.83           C  
ANISOU 3155  CD1 TRP A 186     1953   2186   1876    332    -65    148       C  
ATOM   3156  CD2 TRP A 186      40.660  85.558  37.958  1.00 15.12           C  
ANISOU 3156  CD2 TRP A 186     1695   2162   1888    362     45    166       C  
ATOM   3157  NE1 TRP A 186      40.229  86.719  36.095  1.00 15.99           N  
ANISOU 3157  NE1 TRP A 186     1972   2177   1925    447    -34    232       N  
ATOM   3158  CE2 TRP A 186      40.573  86.856  37.415  1.00 15.20           C  
ANISOU 3158  CE2 TRP A 186     1702   2173   1902    347    179    260       C  
ATOM   3159  CE3 TRP A 186      40.991  85.415  39.313  1.00 14.86           C  
ANISOU 3159  CE3 TRP A 186     1586   2192   1868    365     68     71       C  
ATOM   3160  CZ2 TRP A 186      40.814  87.993  38.163  1.00 16.11           C  
ANISOU 3160  CZ2 TRP A 186     1777   2252   2093    229    334    360       C  
ATOM   3161  CZ3 TRP A 186      41.231  86.558  40.058  1.00 15.83           C  
ANISOU 3161  CZ3 TRP A 186     1681   2339   1994    411      7     61       C  
ATOM   3162  CH2 TRP A 186      41.137  87.829  39.485  1.00 16.12           C  
ANISOU 3162  CH2 TRP A 186     1665   2331   2130    125     -6     69       C  
ATOM   3163  H   TRP A 186      41.306  82.516  34.711  1.00 17.45           H  
ATOM   3164  HA  TRP A 186      42.317  82.945  37.192  1.00 17.21           H  
ATOM   3165  HB2 TRP A 186      39.624  82.817  36.416  1.00 17.74           H  
ATOM   3166  HB3 TRP A 186      40.095  82.911  37.931  1.00 17.74           H  
ATOM   3167  HD1 TRP A 186      39.863  85.039  34.967  1.00 19.01           H  
ATOM   3168  HE1 TRP A 186      40.116  87.366  35.540  1.00 19.19           H  
ATOM   3169  HE3 TRP A 186      41.049  84.573  39.703  1.00 17.84           H  
ATOM   3170  HZ2 TRP A 186      40.759  88.840  37.782  1.00 19.34           H  
ATOM   3171  HZ3 TRP A 186      41.459  86.478  40.956  1.00 19.00           H  
ATOM   3172  HH2 TRP A 186      41.296  88.579  40.012  1.00 19.36           H  
ATOM   3173  N   GLU A 187      42.521  80.280  36.247  1.00 14.98           N  
ANISOU 3173  N   GLU A 187     1630   2326   1737    474   -292     71       N  
ATOM   3174  CA AGLU A 187      42.817  78.881  36.490  0.62 14.71           C  
ANISOU 3174  CA AGLU A 187     1695   2134   1760    243   -471    -99       C  
ATOM   3175  CA BGLU A 187      42.789  78.887  36.561  0.38 14.71           C  
ANISOU 3175  CA BGLU A 187     1654   2207   1728    323   -463   -179       C  
ATOM   3176  C   GLU A 187      44.224  78.774  37.059  1.00 14.40           C  
ANISOU 3176  C   GLU A 187     1628   2123   1720    282   -398   -241       C  
ATOM   3177  O   GLU A 187      45.043  79.681  36.876  1.00 13.33           O  
ANISOU 3177  O   GLU A 187     1505   1906   1652    114   -106   -104       O  
ATOM   3178  CB AGLU A 187      42.771  78.100  35.168  0.62 16.65           C  
ANISOU 3178  CB AGLU A 187     1960   2468   1899    281   -633   -180       C  
ATOM   3179  CB BGLU A 187      42.554  77.966  35.352  0.38 16.02           C  
ANISOU 3179  CB BGLU A 187     1787   2511   1790    381   -636   -378       C  
ATOM   3180  CG AGLU A 187      41.462  78.225  34.402  0.62 19.10           C  
ANISOU 3180  CG AGLU A 187     2234   2805   2218    526   -524    -93       C  
ATOM   3181  CG BGLU A 187      41.120  78.020  34.770  0.38 17.44           C  
ANISOU 3181  CG BGLU A 187     1907   2780   1938    491   -585   -375       C  
ATOM   3182  CD AGLU A 187      40.312  77.623  35.170  0.62 19.78           C  
ANISOU 3182  CD AGLU A 187     2282   2860   2374    568   -349   -233       C  
ATOM   3183  CD BGLU A 187      40.472  76.645  34.549  0.38 17.48           C  
ANISOU 3183  CD BGLU A 187     1797   2877   1968    543   -520   -391       C  
ATOM   3184  OE1AGLU A 187      40.414  76.449  35.555  0.62 19.50           O  
ANISOU 3184  OE1AGLU A 187     2266   2772   2371    528   -137   -337       O  
ATOM   3185  OE1BGLU A 187      41.122  75.599  34.778  0.38 17.28           O  
ANISOU 3185  OE1BGLU A 187     1778   2877   1911    522   -161   -665       O  
ATOM   3186  OE2AGLU A 187      39.323  78.330  35.425  0.62 21.70           O  
ANISOU 3186  OE2AGLU A 187     2537   3050   2658    795   -297   -127       O  
ATOM   3187  OE2BGLU A 187      39.290  76.608  34.139  0.38 18.03           O  
ANISOU 3187  OE2BGLU A 187     1847   2928   2076    515   -739   -267       O  
ATOM   3188  H  AGLU A 187      42.933  80.583  35.555  0.62 17.99           H  
ATOM   3189  H  BGLU A 187      42.930  80.564  35.546  0.38 17.99           H  
ATOM   3190  HA AGLU A 187      42.176  78.502  37.112  0.62 17.66           H  
ATOM   3191  HA BGLU A 187      42.186  78.580  37.256  0.38 17.66           H  
ATOM   3192  HB2AGLU A 187      43.479  78.428  34.591  0.62 19.99           H  
ATOM   3193  HB2BGLU A 187      43.166  78.222  34.644  0.38 19.24           H  
ATOM   3194  HB3AGLU A 187      42.908  77.159  35.360  0.62 19.99           H  
ATOM   3195  HB3BGLU A 187      42.725  77.050  35.623  0.38 19.24           H  
ATOM   3196  HG2AGLU A 187      41.269  79.163  34.248  0.62 22.93           H  
ATOM   3197  HG2BGLU A 187      40.555  78.515  35.384  0.38 20.93           H  
ATOM   3198  HG3AGLU A 187      41.541  77.759  33.555  0.62 22.93           H  
ATOM   3199  HG3BGLU A 187      41.151  78.470  33.911  0.38 20.93           H  
ATOM   3200  N   ILE A 188      44.522  77.651  37.714  1.00 13.70           N  
ANISOU 3200  N   ILE A 188     1469   2082   1655     69   -447   -253       N  
ATOM   3201  CA  ILE A 188      45.844  77.437  38.313  1.00 13.26           C  
ANISOU 3201  CA  ILE A 188     1504   1922   1612      4   -460   -305       C  
ATOM   3202  C   ILE A 188      46.542  76.258  37.632  1.00 14.02           C  
ANISOU 3202  C   ILE A 188     1519   1940   1866    -22   -298   -381       C  
ATOM   3203  O   ILE A 188      46.039  75.121  37.657  1.00 15.26           O  
ANISOU 3203  O   ILE A 188     1692   1932   2174    -52   -184   -325       O  
ATOM   3204  CB  ILE A 188      45.768  77.208  39.831  1.00 14.01           C  
ANISOU 3204  CB  ILE A 188     1829   1910   1584    111   -393    -59       C  
ATOM   3205  CG1 ILE A 188      45.049  78.352  40.537  1.00 14.33           C  
ANISOU 3205  CG1 ILE A 188     1966   1831   1646     37   -173   -156       C  
ATOM   3206  CG2 ILE A 188      47.183  77.044  40.404  1.00 15.15           C  
ANISOU 3206  CG2 ILE A 188     2051   2071   1634    -54   -584   -120       C  
ATOM   3207  CD1 ILE A 188      45.735  79.728  40.404  1.00 15.48           C  
ANISOU 3207  CD1 ILE A 188     2251   1761   1869     -4     14     -4       C  
ATOM   3208  H   ILE A 188      43.973  76.999  37.825  1.00 16.45           H  
ATOM   3209  HA  ILE A 188      46.373  78.231  38.137  1.00 15.92           H  
ATOM   3210  HB  ILE A 188      45.256  76.398  39.984  1.00 16.82           H  
ATOM   3211 HG12 ILE A 188      44.158  78.433  40.162  1.00 17.20           H  
ATOM   3212 HG13 ILE A 188      44.994  78.144  41.483  1.00 17.20           H  
ATOM   3213 HG21 ILE A 188      47.166  77.247  41.352  1.00 18.19           H  
ATOM   3214 HG22 ILE A 188      47.475  76.129  40.267  1.00 18.19           H  
ATOM   3215 HG23 ILE A 188      47.782  77.654  39.946  1.00 18.19           H  
ATOM   3216 HD11 ILE A 188      45.208  80.391  40.877  1.00 18.58           H  
ATOM   3217 HD12 ILE A 188      46.624  79.677  40.788  1.00 18.58           H  
ATOM   3218 HD13 ILE A 188      45.794  79.962  39.464  1.00 18.58           H  
ATOM   3219  N   GLY A 189      47.722  76.521  37.075  1.00 13.60           N  
ANISOU 3219  N   GLY A 189     1339   2015   1812     83   -244   -269       N  
ATOM   3220  CA  GLY A 189      48.589  75.484  36.551  1.00 13.82           C  
ANISOU 3220  CA  GLY A 189     1475   1960   1817    130   -346   -457       C  
ATOM   3221  C   GLY A 189      48.255  74.989  35.164  1.00 14.42           C  
ANISOU 3221  C   GLY A 189     1586   2086   1805    301   -369   -658       C  
ATOM   3222  O   GLY A 189      48.805  73.969  34.731  1.00 15.64           O  
ANISOU 3222  O   GLY A 189     1817   2057   2071    242   -291   -514       O  
ATOM   3223  H   GLY A 189      48.046  77.312  36.990  1.00 16.32           H  
ATOM   3224  HA2 GLY A 189      49.496  75.826  36.529  1.00 16.60           H  
ATOM   3225  HA3 GLY A 189      48.553  74.722  37.150  1.00 16.60           H  
ATOM   3226  N   GLU A 190      47.384  75.698  34.438  1.00 14.68           N  
ANISOU 3226  N   GLU A 190     1691   2294   1594    367   -453   -624       N  
ATOM   3227  CA  GLU A 190      46.914  75.239  33.138  1.00 14.60           C  
ANISOU 3227  CA  GLU A 190     1615   2292   1641    192   -293   -676       C  
ATOM   3228  C   GLU A 190      48.043  75.044  32.131  1.00 15.39           C  
ANISOU 3228  C   GLU A 190     1587   2509   1750     86   -479   -626       C  
ATOM   3229  O   GLU A 190      47.904  74.223  31.210  1.00 17.54           O  
ANISOU 3229  O   GLU A 190     1857   2736   2072    104   -517  -1000       O  
ATOM   3230  CB  GLU A 190      45.882  76.234  32.586  1.00 15.64           C  
ANISOU 3230  CB  GLU A 190     1727   2405   1808    270   -440   -567       C  
ATOM   3231  CG  GLU A 190      46.412  77.644  32.248  1.00 14.88           C  
ANISOU 3231  CG  GLU A 190     1677   2437   1539    170   -349   -471       C  
ATOM   3232  CD  GLU A 190      46.702  78.513  33.454  1.00 14.18           C  
ANISOU 3232  CD  GLU A 190     1483   2293   1613    260   -323   -299       C  
ATOM   3233  OE1 GLU A 190      46.241  78.180  34.571  1.00 14.32           O  
ANISOU 3233  OE1 GLU A 190     1445   2245   1752    273   -374   -308       O  
ATOM   3234  OE2 GLU A 190      47.431  79.522  33.283  1.00 13.62           O  
ANISOU 3234  OE2 GLU A 190     1317   2166   1694    367   -334   -118       O  
ATOM   3235  H   GLU A 190      47.049  76.453  34.678  1.00 17.63           H  
ATOM   3236  HA  GLU A 190      46.491  74.375  33.260  1.00 17.53           H  
ATOM   3237  HB2 GLU A 190      45.511  75.864  31.769  1.00 18.77           H  
ATOM   3238  HB3 GLU A 190      45.181  76.342  33.248  1.00 18.77           H  
ATOM   3239  HG2 GLU A 190      47.238  77.552  31.748  1.00 17.86           H  
ATOM   3240  HG3 GLU A 190      45.748  78.103  31.710  1.00 17.86           H  
ATOM   3241  N   ASP A 191      49.141  75.791  32.266  1.00 15.55           N  
ANISOU 3241  N   ASP A 191     1529   2578   1802    327   -371   -401       N  
ATOM   3242  CA  ASP A 191      50.194  75.715  31.257  1.00 15.34           C  
ANISOU 3242  CA  ASP A 191     1770   2310   1748    421   -387   -616       C  
ATOM   3243  C   ASP A 191      51.006  74.439  31.364  1.00 15.80           C  
ANISOU 3243  C   ASP A 191     1843   2282   1878    326   -425   -576       C  
ATOM   3244  O   ASP A 191      51.589  74.009  30.369  1.00 17.34           O  
ANISOU 3244  O   ASP A 191     2287   2365   1934    460   -106   -421       O  
ATOM   3245  CB  ASP A 191      51.111  76.929  31.325  1.00 15.73           C  
ANISOU 3245  CB  ASP A 191     1651   2538   1788    436   -354   -349       C  
ATOM   3246  CG  ASP A 191      50.379  78.218  31.015  1.00 17.15           C  
ANISOU 3246  CG  ASP A 191     1838   2670   2008    734   -488   -506       C  
ATOM   3247  OD1 ASP A 191      49.440  78.197  30.181  1.00 17.95           O  
ANISOU 3247  OD1 ASP A 191     2281   2914   1624    858   -383   -311       O  
ATOM   3248  OD2 ASP A 191      50.712  79.234  31.649  1.00 20.00           O  
ANISOU 3248  OD2 ASP A 191     1872   2670   3057    867   -665   -265       O  
ATOM   3249  H   ASP A 191      49.298  76.334  32.914  1.00 18.67           H  
ATOM   3250  HA  ASP A 191      49.762  75.723  30.388  1.00 18.42           H  
ATOM   3251  HB2 ASP A 191      51.481  76.999  32.219  1.00 18.89           H  
ATOM   3252  HB3 ASP A 191      51.825  76.824  30.677  1.00 18.89           H  
ATOM   3253  N   VAL A 192      51.071  73.824  32.542  1.00 15.08           N  
ANISOU 3253  N   VAL A 192     1627   2170   1931    279   -401   -427       N  
ATOM   3254  CA  VAL A 192      51.947  72.680  32.760  1.00 15.66           C  
ANISOU 3254  CA  VAL A 192     1707   2116   2125    254   -449   -522       C  
ATOM   3255  C   VAL A 192      51.203  71.409  33.122  1.00 15.87           C  
ANISOU 3255  C   VAL A 192     1524   2185   2321    223   -304   -686       C  
ATOM   3256  O   VAL A 192      51.822  70.338  33.157  1.00 17.02           O  
ANISOU 3256  O   VAL A 192     1728   2259   2479    217   -242   -627       O  
ATOM   3257  CB  VAL A 192      53.036  72.982  33.809  1.00 17.18           C  
ANISOU 3257  CB  VAL A 192     1934   2298   2297    257   -538   -422       C  
ATOM   3258  CG1 VAL A 192      54.025  74.027  33.264  1.00 17.26           C  
ANISOU 3258  CG1 VAL A 192     1924   2127   2508    213   -361   -526       C  
ATOM   3259  CG2 VAL A 192      52.427  73.434  35.122  1.00 17.76           C  
ANISOU 3259  CG2 VAL A 192     2088   2550   2111    326   -795   -259       C  
ATOM   3260  H   VAL A 192      50.613  74.053  33.233  1.00 18.10           H  
ATOM   3261  HA  VAL A 192      52.404  72.500  31.924  1.00 18.80           H  
ATOM   3262  HB  VAL A 192      53.529  72.167  33.991  1.00 20.63           H  
ATOM   3263 HG11 VAL A 192      54.705  74.199  33.934  1.00 20.72           H  
ATOM   3264 HG12 VAL A 192      54.436  73.681  32.456  1.00 20.72           H  
ATOM   3265 HG13 VAL A 192      53.542  74.845  33.065  1.00 20.72           H  
ATOM   3266 HG21 VAL A 192      53.138  73.590  35.763  1.00 21.32           H  
ATOM   3267 HG22 VAL A 192      51.929  74.253  34.974  1.00 21.32           H  
ATOM   3268 HG23 VAL A 192      51.832  72.740  35.449  1.00 21.32           H  
ATOM   3269  N   TYR A 193      49.909  71.477  33.386  1.00 16.61           N  
ANISOU 3269  N   TYR A 193     1443   2266   2602    202   -210   -734       N  
ATOM   3270  CA  TYR A 193      49.137  70.313  33.777  1.00 17.76           C  
ANISOU 3270  CA  TYR A 193     1685   2229   2832      5   -193  -1026       C  
ATOM   3271  C   TYR A 193      48.597  69.593  32.547  1.00 18.95           C  
ANISOU 3271  C   TYR A 193     1882   2387   2930   -139   -451   -958       C  
ATOM   3272  O   TYR A 193      48.115  70.225  31.599  1.00 19.49           O  
ANISOU 3272  O   TYR A 193     2008   2381   3016    185   -531   -661       O  
ATOM   3273  CB  TYR A 193      47.965  70.793  34.635  1.00 19.69           C  
ANISOU 3273  CB  TYR A 193     1959   2447   3075     58   -177  -1208       C  
ATOM   3274  CG  TYR A 193      47.129  69.713  35.261  1.00 21.48           C  
ANISOU 3274  CG  TYR A 193     2070   2613   3479   -159    -53  -1117       C  
ATOM   3275  CD1 TYR A 193      47.686  68.772  36.118  1.00 23.12           C  
ANISOU 3275  CD1 TYR A 193     2387   2792   3604   -386     79   -856       C  
ATOM   3276  CD2 TYR A 193      45.765  69.653  35.021  1.00 22.15           C  
ANISOU 3276  CD2 TYR A 193     2072   2678   3665   -447    -56  -1135       C  
ATOM   3277  CE1 TYR A 193      46.908  67.785  36.693  1.00 25.17           C  
ANISOU 3277  CE1 TYR A 193     2523   3202   3840   -558    178   -933       C  
ATOM   3278  CE2 TYR A 193      44.984  68.683  35.603  1.00 24.02           C  
ANISOU 3278  CE2 TYR A 193     2222   3028   3876   -592    265  -1123       C  
ATOM   3279  CZ  TYR A 193      45.554  67.757  36.444  1.00 25.23           C  
ANISOU 3279  CZ  TYR A 193     2417   3201   3970   -916    329   -908       C  
ATOM   3280  OH  TYR A 193      44.742  66.799  37.010  1.00 28.99           O  
ANISOU 3280  OH  TYR A 193     2897   3871   4247  -1104    534   -787       O  
ATOM   3281  H   TYR A 193      49.447  72.201  33.344  1.00 19.94           H  
ATOM   3282  HA  TYR A 193      49.687  69.685  34.270  1.00 21.31           H  
ATOM   3283  HB2 TYR A 193      48.319  71.337  35.356  1.00 23.63           H  
ATOM   3284  HB3 TYR A 193      47.376  71.324  34.076  1.00 23.63           H  
ATOM   3285  HD1 TYR A 193      48.595  68.807  36.308  1.00 27.75           H  
ATOM   3286  HD2 TYR A 193      45.372  70.279  34.457  1.00 26.58           H  
ATOM   3287  HE1 TYR A 193      47.296  67.144  37.244  1.00 30.22           H  
ATOM   3288  HE2 TYR A 193      44.071  68.654  35.428  1.00 28.83           H  
ATOM   3289  HH  TYR A 193      43.946  66.921  36.772  1.00 34.80           H  
ATOM   3290  N   THR A 194      48.675  68.263  32.573  1.00 21.05           N  
ANISOU 3290  N   THR A 194     2062   2636   3302   -159   -554  -1150       N  
ATOM   3291  CA  THR A 194      48.104  67.361  31.570  1.00 22.51           C  
ANISOU 3291  CA  THR A 194     2096   2908   3547   -205   -663  -1291       C  
ATOM   3292  C   THR A 194      48.327  67.829  30.138  1.00 23.19           C  
ANISOU 3292  C   THR A 194     2147   3094   3570    178   -796  -1478       C  
ATOM   3293  O   THR A 194      47.400  68.305  29.472  1.00 24.22           O  
ANISOU 3293  O   THR A 194     2402   3255   3545     40   -807  -1563       O  
ATOM   3294  CB  THR A 194      46.601  67.124  31.810  1.00 23.83           C  
ANISOU 3294  CB  THR A 194     2166   3095   3794   -113   -525  -1288       C  
ATOM   3295  OG1 THR A 194      45.898  68.381  31.831  1.00 24.83           O  
ANISOU 3295  OG1 THR A 194     2148   3363   3924    158   -635  -1645       O  
ATOM   3296  CG2 THR A 194      46.401  66.389  33.117  1.00 24.24           C  
ANISOU 3296  CG2 THR A 194     2360   3058   3793   -238   -686  -1086       C  
ATOM   3297  H   THR A 194      49.077  67.831  33.199  1.00 25.27           H  
ATOM   3298  HA  THR A 194      48.581  66.522  31.666  1.00 27.02           H  
ATOM   3299  HB  THR A 194      46.232  66.582  31.095  1.00 28.60           H  
ATOM   3300 HG21 THR A 194      45.456  66.223  33.263  1.00 29.10           H  
ATOM   3301 HG22 THR A 194      46.870  65.540  33.095  1.00 29.10           H  
ATOM   3302 HG23 THR A 194      46.745  66.920  33.852  1.00 29.10           H  
ATOM   3303  N   PRO A 195      49.545  67.682  29.626  1.00 23.82           N  
ANISOU 3303  N   PRO A 195     2233   3211   3606    148   -578  -1464       N  
ATOM   3304  CA  PRO A 195      49.820  68.115  28.251  1.00 24.93           C  
ANISOU 3304  CA  PRO A 195     2382   3488   3600    183   -745  -1671       C  
ATOM   3305  C   PRO A 195      48.922  67.475  27.207  1.00 28.39           C  
ANISOU 3305  C   PRO A 195     2727   4122   3939    145   -713  -1846       C  
ATOM   3306  O   PRO A 195      48.723  68.069  26.141  1.00 30.20           O  
ANISOU 3306  O   PRO A 195     3111   4541   3820    272   -724  -1694       O  
ATOM   3307  CB  PRO A 195      51.293  67.740  28.057  1.00 25.07           C  
ANISOU 3307  CB  PRO A 195     2335   3564   3626    119   -590  -1452       C  
ATOM   3308  CG  PRO A 195      51.577  66.722  29.125  1.00 24.36           C  
ANISOU 3308  CG  PRO A 195     2165   3450   3640    256   -466  -1344       C  
ATOM   3309  CD  PRO A 195      50.752  67.157  30.290  1.00 23.78           C  
ANISOU 3309  CD  PRO A 195     2113   3310   3611    185   -525  -1424       C  
ATOM   3310  HA  PRO A 195      49.728  69.078  28.181  1.00 29.92           H  
ATOM   3311  HB2 PRO A 195      51.425  67.362  27.173  1.00 30.09           H  
ATOM   3312  HB3 PRO A 195      51.852  68.525  28.169  1.00 30.09           H  
ATOM   3313  HG2 PRO A 195      51.311  65.840  28.821  1.00 29.24           H  
ATOM   3314  HG3 PRO A 195      52.521  66.726  29.346  1.00 29.24           H  
ATOM   3315  HD2 PRO A 195      50.537  66.408  30.867  1.00 28.54           H  
ATOM   3316  HD3 PRO A 195      51.202  67.850  30.799  1.00 28.54           H  
ATOM   3317  N   GLY A 196      48.362  66.304  27.472  1.00 29.15           N  
ANISOU 3317  N   GLY A 196     2700   4197   4178    -18   -829  -2210       N  
ATOM   3318  CA  GLY A 196      47.484  65.683  26.499  1.00 30.17           C  
ANISOU 3318  CA  GLY A 196     2640   4510   4314     17   -873  -2273       C  
ATOM   3319  C   GLY A 196      46.040  66.135  26.535  1.00 31.82           C  
ANISOU 3319  C   GLY A 196     2869   4650   4571    -28  -1037  -2288       C  
ATOM   3320  O   GLY A 196      45.238  65.658  25.725  1.00 33.97           O  
ANISOU 3320  O   GLY A 196     3279   4808   4818    -68  -1147  -2280       O  
ATOM   3321  H   GLY A 196      48.474  65.857  28.198  1.00 34.99           H  
ATOM   3322  HA2 GLY A 196      47.827  65.872  25.611  1.00 36.21           H  
ATOM   3323  HA3 GLY A 196      47.493  64.724  26.644  1.00 36.21           H  
ATOM   3324  N   ILE A 197      45.683  67.039  27.448  1.00 30.80           N  
ANISOU 3324  N   ILE A 197     2817   4431   4455    -38   -889  -2316       N  
ATOM   3325  CA  ILE A 197      44.302  67.476  27.649  1.00 30.25           C  
ANISOU 3325  CA  ILE A 197     2756   4440   4297   -103   -828  -2147       C  
ATOM   3326  C   ILE A 197      44.276  68.998  27.612  1.00 30.07           C  
ANISOU 3326  C   ILE A 197     2906   4674   3844    152   -830  -2028       C  
ATOM   3327  O   ILE A 197      44.884  69.651  28.472  1.00 28.59           O  
ANISOU 3327  O   ILE A 197     2854   4465   3544     44   -853  -2067       O  
ATOM   3328  CB  ILE A 197      43.752  66.995  29.007  1.00 30.60           C  
ANISOU 3328  CB  ILE A 197     2653   4484   4492   -133   -628  -2030       C  
ATOM   3329  CG1 ILE A 197      43.819  65.470  29.120  1.00 32.05           C  
ANISOU 3329  CG1 ILE A 197     2912   4636   4629    -54   -602  -1864       C  
ATOM   3330  CG2 ILE A 197      42.318  67.504  29.223  1.00 30.91           C  
ANISOU 3330  CG2 ILE A 197     2551   4627   4567   -394   -818  -1985       C  
ATOM   3331  CD1 ILE A 197      43.378  64.939  30.475  1.00 32.86           C  
ANISOU 3331  CD1 ILE A 197     3118   4649   4716    -12   -553  -1813       C  
ATOM   3332  H   ILE A 197      46.242  67.423  27.978  1.00 36.97           H  
ATOM   3333  HA  ILE A 197      43.752  67.131  26.929  1.00 36.31           H  
ATOM   3334  HB  ILE A 197      44.313  67.367  29.705  1.00 36.73           H  
ATOM   3335 HG12 ILE A 197      43.241  65.081  28.446  1.00 38.47           H  
ATOM   3336 HG13 ILE A 197      44.736  65.186  28.975  1.00 38.47           H  
ATOM   3337 HG21 ILE A 197      41.974  67.137  30.052  1.00 37.10           H  
ATOM   3338 HG22 ILE A 197      42.330  68.473  29.271  1.00 37.10           H  
ATOM   3339 HG23 ILE A 197      41.765  67.217  28.480  1.00 37.10           H  
ATOM   3340 HD11 ILE A 197      43.663  64.016  30.561  1.00 39.43           H  
ATOM   3341 HD12 ILE A 197      43.784  65.477  31.173  1.00 39.43           H  
ATOM   3342 HD13 ILE A 197      42.411  64.994  30.536  1.00 39.43           H  
ATOM   3343  N   SER A 198      43.545  69.567  26.662  1.00 30.56           N  
ANISOU 3343  N   SER A 198     2959   4972   3681    407  -1009  -1733       N  
ATOM   3344  CA ASER A 198      43.398  71.012  26.585  0.39 31.45           C  
ANISOU 3344  CA ASER A 198     3057   5196   3698    476   -937  -1614       C  
ATOM   3345  CA BSER A 198      43.408  71.013  26.597  0.61 31.65           C  
ANISOU 3345  CA BSER A 198     3121   5234   3670    471  -1006  -1520       C  
ATOM   3346  C   SER A 198      42.230  71.477  27.447  1.00 31.06           C  
ANISOU 3346  C   SER A 198     3040   5189   3571    446   -993  -1553       C  
ATOM   3347  O   SER A 198      41.236  70.765  27.617  1.00 32.08           O  
ANISOU 3347  O   SER A 198     3284   5394   3511    360  -1031  -1311       O  
ATOM   3348  CB ASER A 198      43.151  71.454  25.139  0.39 32.35           C  
ANISOU 3348  CB ASER A 198     3129   5349   3813    542   -739  -1657       C  
ATOM   3349  CB BSER A 198      43.196  71.474  25.152  0.61 32.94           C  
ANISOU 3349  CB BSER A 198     3322   5442   3752    515   -896  -1414       C  
ATOM   3350  OG ASER A 198      44.326  71.331  24.356  0.39 33.27           O  
ANISOU 3350  OG ASER A 198     3267   5423   3950    615   -615  -1666       O  
ATOM   3351  OG BSER A 198      41.936  71.057  24.677  0.61 34.18           O  
ANISOU 3351  OG BSER A 198     3593   5525   3867    592   -923  -1260       O  
ATOM   3352  H  ASER A 198      43.124  69.134  26.049  0.39 36.68           H  
ATOM   3353  H  BSER A 198      43.122  69.137  26.048  0.61 36.68           H  
ATOM   3354  HA ASER A 198      44.212  71.430  26.906  0.39 37.75           H  
ATOM   3355  HA BSER A 198      44.218  71.423  26.936  0.61 37.99           H  
ATOM   3356  HB2ASER A 198      42.458  70.895  24.754  0.39 38.83           H  
ATOM   3357  HB2BSER A 198      43.242  72.442  25.118  0.61 39.53           H  
ATOM   3358  HB3ASER A 198      42.868  72.382  25.137  0.39 38.83           H  
ATOM   3359  HB3BSER A 198      43.888  71.089  24.592  0.61 39.53           H  
ATOM   3360  HG ASER A 198      44.167  71.558  23.563  0.39 39.93           H  
ATOM   3361  HG BSER A 198      41.833  71.305  23.882  0.61 41.02           H  
ATOM   3362  N   GLY A 199      42.358  72.679  27.988  1.00 30.07           N  
ANISOU 3362  N   GLY A 199     2930   5061   3434    582   -888  -1707       N  
ATOM   3363  CA  GLY A 199      41.254  73.331  28.656  1.00 29.10           C  
ANISOU 3363  CA  GLY A 199     2739   4864   3452    604   -841  -1570       C  
ATOM   3364  C   GLY A 199      41.045  72.991  30.110  1.00 28.82           C  
ANISOU 3364  C   GLY A 199     2703   4629   3619    411   -737  -1671       C  
ATOM   3365  O   GLY A 199      40.044  73.430  30.687  1.00 29.24           O  
ANISOU 3365  O   GLY A 199     2733   4593   3784    559   -777  -1705       O  
ATOM   3366  H   GLY A 199      43.084  73.141  27.978  1.00 36.09           H  
ATOM   3367  HA2 GLY A 199      41.390  74.290  28.601  1.00 34.92           H  
ATOM   3368  HA3 GLY A 199      40.437  73.100  28.186  1.00 34.92           H  
ATOM   3369  N   ASP A 200      41.935  72.217  30.719  1.00 25.61           N  
ANISOU 3369  N   ASP A 200     2247   4112   3373    219   -750  -1715       N  
ATOM   3370  CA  ASP A 200      41.819  71.871  32.130  1.00 24.07           C  
ANISOU 3370  CA  ASP A 200     2041   3740   3365    -83   -657  -1444       C  
ATOM   3371  C   ASP A 200      42.919  72.566  32.924  1.00 21.67           C  
ANISOU 3371  C   ASP A 200     1888   3344   3003    -20   -490  -1249       C  
ATOM   3372  O   ASP A 200      43.734  73.319  32.386  1.00 21.62           O  
ANISOU 3372  O   ASP A 200     1774   3370   3071     45   -571  -1196       O  
ATOM   3373  CB  ASP A 200      41.847  70.355  32.333  1.00 24.06           C  
ANISOU 3373  CB  ASP A 200     2010   3592   3540   -127   -692  -1425       C  
ATOM   3374  CG  ASP A 200      43.184  69.737  31.975  1.00 24.56           C  
ANISOU 3374  CG  ASP A 200     2177   3453   3700   -189   -552  -1416       C  
ATOM   3375  OD1 ASP A 200      44.019  70.408  31.316  1.00 23.32           O  
ANISOU 3375  OD1 ASP A 200     2158   3223   3482   -366   -686  -1529       O  
ATOM   3376  OD2 ASP A 200      43.402  68.571  32.379  1.00 24.80           O  
ANISOU 3376  OD2 ASP A 200     2165   3377   3882   -129   -361  -1288       O  
ATOM   3377  H   ASP A 200      42.621  71.877  30.328  1.00 30.74           H  
ATOM   3378  HA  ASP A 200      40.964  72.191  32.457  1.00 28.89           H  
ATOM   3379  HB2 ASP A 200      41.666  70.159  33.265  1.00 28.88           H  
ATOM   3380  HB3 ASP A 200      41.169  69.949  31.771  1.00 28.88           H  
ATOM   3381  N   SER A 201      42.908  72.324  34.232  1.00 19.43           N  
ANISOU 3381  N   SER A 201     1813   2932   2636   -224   -379   -950       N  
ATOM   3382  CA ASER A 201      43.842  72.950  35.162  0.59 18.27           C  
ANISOU 3382  CA ASER A 201     1697   2619   2625   -244   -174   -949       C  
ATOM   3383  CA BSER A 201      43.920  72.875  35.129  0.41 18.12           C  
ANISOU 3383  CA BSER A 201     1787   2523   2576   -118   -169   -872       C  
ATOM   3384  C   SER A 201      43.767  72.182  36.476  1.00 17.42           C  
ANISOU 3384  C   SER A 201     1660   2296   2664    -85    -88   -793       C  
ATOM   3385  O   SER A 201      42.951  71.267  36.634  1.00 19.30           O  
ANISOU 3385  O   SER A 201     1921   2446   2965   -163    106   -786       O  
ATOM   3386  CB ASER A 201      43.474  74.416  35.383  0.59 18.59           C  
ANISOU 3386  CB ASER A 201     1649   2693   2721   -274    119   -980       C  
ATOM   3387  CB BSER A 201      43.773  74.384  35.308  0.41 18.02           C  
ANISOU 3387  CB BSER A 201     1916   2384   2547     30     72   -782       C  
ATOM   3388  OG ASER A 201      42.170  74.533  35.939  0.59 19.50           O  
ANISOU 3388  OG ASER A 201     1712   2895   2801   -211    260   -924       O  
ATOM   3389  OG BSER A 201      42.908  74.669  36.397  0.41 17.72           O  
ANISOU 3389  OG BSER A 201     1998   2247   2489    197    228   -660       O  
ATOM   3390  H  ASER A 201      42.355  71.787  34.613  0.59 23.32           H  
ATOM   3391  H  BSER A 201      42.319  71.839  34.627  0.41 23.32           H  
ATOM   3392  HA ASER A 201      44.743  72.887  34.809  0.59 21.93           H  
ATOM   3393  HA BSER A 201      44.793  72.685  34.752  0.41 21.76           H  
ATOM   3394  HB2ASER A 201      44.114  74.814  35.994  0.59 22.32           H  
ATOM   3395  HB2BSER A 201      44.645  74.769  35.485  0.41 21.63           H  
ATOM   3396  HB3ASER A 201      43.496  74.879  34.531  0.59 22.32           H  
ATOM   3397  HB3BSER A 201      43.400  74.765  34.498  0.41 21.63           H  
ATOM   3398  HG ASER A 201      41.983  75.342  36.065  0.59 23.40           H  
ATOM   3399  HG BSER A 201      42.132  74.397  36.226  0.41 21.27           H  
ATOM   3400  N   LEU A 202      44.573  72.625  37.451  1.00 16.40           N  
ANISOU 3400  N   LEU A 202     1493   2126   2611     27   -203   -687       N  
ATOM   3401  CA  LEU A 202      44.518  72.014  38.771  1.00 16.34           C  
ANISOU 3401  CA  LEU A 202     1650   1948   2609    113   -330   -482       C  
ATOM   3402  C   LEU A 202      43.314  72.479  39.567  1.00 16.03           C  
ANISOU 3402  C   LEU A 202     1652   1851   2588    162   -318   -255       C  
ATOM   3403  O   LEU A 202      42.796  71.731  40.405  1.00 17.87           O  
ANISOU 3403  O   LEU A 202     1907   1888   2996     77   -270   -278       O  
ATOM   3404  CB  LEU A 202      45.745  72.404  39.586  1.00 17.19           C  
ANISOU 3404  CB  LEU A 202     1679   2010   2842    186   -381   -504       C  
ATOM   3405  CG  LEU A 202      47.078  71.918  39.041  1.00 20.17           C  
ANISOU 3405  CG  LEU A 202     2086   2254   3325    142   -220   -614       C  
ATOM   3406  CD1 LEU A 202      48.229  72.560  39.818  1.00 20.26           C  
ANISOU 3406  CD1 LEU A 202     1920   2378   3400    134   -218   -499       C  
ATOM   3407  CD2 LEU A 202      47.125  70.398  39.136  1.00 22.32           C  
ANISOU 3407  CD2 LEU A 202     2398   2496   3586    152   -302   -545       C  
ATOM   3408  H   LEU A 202      45.145  73.262  37.371  1.00 19.68           H  
ATOM   3409  HA  LEU A 202      44.488  71.054  38.641  1.00 19.61           H  
ATOM   3410  HB2 LEU A 202      45.787  73.372  39.629  1.00 20.64           H  
ATOM   3411  HB3 LEU A 202      45.647  72.036  40.478  1.00 20.64           H  
ATOM   3412  HG  LEU A 202      47.181  72.172  38.110  1.00 24.22           H  
ATOM   3413 HD11 LEU A 202      49.071  72.228  39.468  1.00 24.32           H  
ATOM   3414 HD12 LEU A 202      48.184  73.523  39.711  1.00 24.32           H  
ATOM   3415 HD13 LEU A 202      48.146  72.327  40.756  1.00 24.32           H  
ATOM   3416 HD21 LEU A 202      48.011  70.093  38.886  1.00 26.79           H  
ATOM   3417 HD22 LEU A 202      46.929  70.133  40.048  1.00 26.79           H  
ATOM   3418 HD23 LEU A 202      46.464  70.023  38.533  1.00 26.79           H  
ATOM   3419  N  AARG A 203      42.920  73.738  39.374  0.26 15.56           N  
ANISOU 3419  N  AARG A 203     1669   1784   2461    222   -333   -171       N  
ATOM   3420  N  BARG A 203      42.864  73.701  39.340  0.74 16.20           N  
ANISOU 3420  N  BARG A 203     1747   1967   2442    584   -353   -189       N  
ATOM   3421  CA AARG A 203      41.862  74.392  40.125  0.26 14.67           C  
ANISOU 3421  CA AARG A 203     1635   1643   2296    115   -328   -253       C  
ATOM   3422  CA BARG A 203      41.694  74.225  40.029  0.74 15.67           C  
ANISOU 3422  CA BARG A 203     1760   1934   2261    520   -327   -575       C  
ATOM   3423  C  AARG A 203      41.295  75.502  39.252  0.26 14.75           C  
ANISOU 3423  C  AARG A 203     1590   1764   2249    141   -350   -261       C  
ATOM   3424  C  BARG A 203      41.334  75.556  39.394  0.74 14.82           C  
ANISOU 3424  C  BARG A 203     1516   1970   2144    348   -420   -585       C  
ATOM   3425  O  AARG A 203      41.960  75.980  38.328  0.26 14.82           O  
ANISOU 3425  O  AARG A 203     1694   1693   2245    128   -375   -213       O  
ATOM   3426  O  BARG A 203      42.171  76.222  38.776  0.74 14.37           O  
ANISOU 3426  O  BARG A 203     1356   2089   2014    229   -646   -615       O  
ATOM   3427  CB AARG A 203      42.397  75.052  41.404  0.26 14.42           C  
ANISOU 3427  CB AARG A 203     1644   1531   2305    -40   -342   -169       C  
ATOM   3428  CB BARG A 203      41.934  74.375  41.528  0.74 17.11           C  
ANISOU 3428  CB BARG A 203     1827   2250   2424    436   -298   -471       C  
ATOM   3429  CG AARG A 203      42.928  74.087  42.446  0.26 14.07           C  
ANISOU 3429  CG AARG A 203     1686   1410   2250    -20   -408   -175       C  
ATOM   3430  CG BARG A 203      43.206  75.099  41.854  0.74 15.89           C  
ANISOU 3430  CG BARG A 203     1557   2196   2285      4   -289   -600       C  
ATOM   3431  CD AARG A 203      43.386  74.814  43.702  0.26 14.11           C  
ANISOU 3431  CD AARG A 203     1745   1330   2287   -114   -341      9       C  
ATOM   3432  CD BARG A 203      43.508  75.052  43.331  0.74 16.04           C  
ANISOU 3432  CD BARG A 203     1574   2193   2328   -131   -182   -350       C  
ATOM   3433  NE AARG A 203      44.653  75.520  43.519  0.26 13.87           N  
ANISOU 3433  NE AARG A 203     1775   1220   2276    -81   -316    186       N  
ATOM   3434  NE BARG A 203      44.799  75.672  43.614  0.74 14.85           N  
ANISOU 3434  NE BARG A 203     1435   2054   2153     73   -366   -250       N  
ATOM   3435  CZ AARG A 203      45.851  74.968  43.685  0.26 14.03           C  
ANISOU 3435  CZ AARG A 203     1852   1177   2300     -1   -141    350       C  
ATOM   3436  CZ BARG A 203      45.957  75.024  43.675  0.74 14.36           C  
ANISOU 3436  CZ BARG A 203     1623   1874   1958    203   -307   -382       C  
ATOM   3437  NH1AARG A 203      45.963  73.689  44.030  0.26 14.40           N  
ANISOU 3437  NH1AARG A 203     1988   1222   2263    -24    -82    417       N  
ATOM   3438  NH1BARG A 203      46.017  73.705  43.483  0.74 15.69           N  
ANISOU 3438  NH1BARG A 203     2032   1953   1975    335   -360   -434       N  
ATOM   3439  NH2AARG A 203      46.942  75.696  43.510  0.26 13.97           N  
ANISOU 3439  NH2AARG A 203     1816   1162   2329     94    -74    461       N  
ATOM   3440  NH2BARG A 203      47.063  75.701  43.964  0.74 12.90           N  
ANISOU 3440  NH2BARG A 203     1352   1873   1677    -32   -401   -463       N  
ATOM   3441  H  AARG A 203      43.270  74.255  38.783  0.26 18.69           H  
ATOM   3442  H  BARG A 203      43.221  74.253  38.785  0.74 19.45           H  
ATOM   3443  HA AARG A 203      41.184  73.736  40.351  0.26 17.61           H  
ATOM   3444  HA BARG A 203      40.946  73.619  39.913  0.74 18.82           H  
ATOM   3445  HB2AARG A 203      43.123  75.648  41.162  0.26 17.32           H  
ATOM   3446  HB2BARG A 203      41.198  74.876  41.915  0.74 20.54           H  
ATOM   3447  HB3AARG A 203      41.677  75.556  41.814  0.26 17.32           H  
ATOM   3448  HB3BARG A 203      41.981  73.493  41.928  0.74 20.54           H  
ATOM   3449  HG2AARG A 203      42.227  73.464  42.694  0.26 16.89           H  
ATOM   3450  HG2BARG A 203      43.942  74.682  41.380  0.74 19.08           H  
ATOM   3451  HG3AARG A 203      43.686  73.605  42.081  0.26 16.89           H  
ATOM   3452  HG3BARG A 203      43.124  76.028  41.589  0.74 19.08           H  
ATOM   3453  HD2AARG A 203      42.713  75.467  43.951  0.26 16.94           H  
ATOM   3454  HD2BARG A 203      42.821  75.534  43.817  0.74 19.26           H  
ATOM   3455  HD3AARG A 203      43.503  74.169  44.416  0.26 16.94           H  
ATOM   3456  HD3BARG A 203      43.537  74.129  43.627  0.74 19.26           H  
ATOM   3457  HE AARG A 203      44.622  76.348  43.290  0.26 16.66           H  
ATOM   3458  HE BARG A 203      44.811  76.521  43.752  0.74 17.83           H  
ATOM   3459 HH11AARG A 203      45.257  73.212  44.148  0.26 17.29           H  
ATOM   3460 HH11BARG A 203      45.299  73.261  43.316  0.74 18.83           H  
ATOM   3461 HH12AARG A 203      46.741  73.339  44.135  0.26 17.29           H  
ATOM   3462 HH12BARG A 203      46.773  73.298  43.525  0.74 18.83           H  
ATOM   3463 HH21AARG A 203      46.875  76.525  43.289  0.26 16.77           H  
ATOM   3464 HH21BARG A 203      47.023  76.548  44.109  0.74 15.49           H  
ATOM   3465 HH22AARG A 203      47.718  75.341  43.616  0.26 16.77           H  
ATOM   3466 HH22BARG A 203      47.818  75.293  44.007  0.74 15.49           H  
ATOM   3467  N   SER A 204      40.069  75.924  39.555  1.00 14.53           N  
ANISOU 3467  N   SER A 204     1427   1916   2177    120   -334   -253       N  
ATOM   3468  CA  SER A 204      39.515  77.134  38.973  1.00 14.42           C  
ANISOU 3468  CA  SER A 204     1345   2059   2074    192   -407   -129       C  
ATOM   3469  C   SER A 204      39.136  78.097  40.087  1.00 13.53           C  
ANISOU 3469  C   SER A 204     1349   1948   1845    144   -217   -155       C  
ATOM   3470  O   SER A 204      38.444  77.714  41.034  1.00 14.98           O  
ANISOU 3470  O   SER A 204     1673   2016   2002    -21    -76      0       O  
ATOM   3471  CB  SER A 204      38.268  76.820  38.156  1.00 15.11           C  
ANISOU 3471  CB  SER A 204     1393   2225   2124    282   -649   -141       C  
ATOM   3472  OG  SER A 204      37.660  78.023  37.716  1.00 16.41           O  
ANISOU 3472  OG  SER A 204     1508   2472   2255    358   -522   -110       O  
ATOM   3473  H  ASER A 204      39.542  75.520  40.101  0.26 17.44           H  
ATOM   3474  H  BSER A 204      39.499  75.473  40.013  0.74 17.44           H  
ATOM   3475  HA  SER A 204      40.182  77.545  38.402  1.00 17.31           H  
ATOM   3476  HB2 SER A 204      38.518  76.289  37.383  1.00 18.14           H  
ATOM   3477  HB3 SER A 204      37.640  76.329  38.708  1.00 18.14           H  
ATOM   3478  HG  SER A 204      38.199  78.463  37.245  1.00 19.70           H  
ATOM   3479  N   MET A 205      39.568  79.352  39.963  1.00 13.74           N  
ANISOU 3479  N   MET A 205     1362   2114   1743    104   -252   -248       N  
ATOM   3480  CA  MET A 205      39.132  80.368  40.905  1.00 13.12           C  
ANISOU 3480  CA  MET A 205     1315   1967   1703    213   -289   -220       C  
ATOM   3481  C   MET A 205      37.767  80.934  40.527  1.00 13.90           C  
ANISOU 3481  C   MET A 205     1416   1990   1878     36   -295   -299       C  
ATOM   3482  O   MET A 205      36.998  81.334  41.408  1.00 14.89           O  
ANISOU 3482  O   MET A 205     1676   1925   2058    134   -194   -209       O  
ATOM   3483  CB  MET A 205      40.133  81.516  40.950  1.00 12.96           C  
ANISOU 3483  CB  MET A 205     1327   1888   1709     69   -342   -170       C  
ATOM   3484  CG  MET A 205      41.571  81.102  41.305  1.00 13.07           C  
ANISOU 3484  CG  MET A 205     1348   1830   1788    -38   -441   -138       C  
ATOM   3485  SD  MET A 205      42.706  82.501  41.355  1.00 14.41           S  
ANISOU 3485  SD  MET A 205     1449   2139   1888   -150   -219     59       S  
ATOM   3486  CE  MET A 205      42.133  83.338  42.854  1.00 14.69           C  
ANISOU 3486  CE  MET A 205     1625   1969   1986   -204   -370   -256       C  
ATOM   3487  H   MET A 205      40.104  79.633  39.352  1.00 16.49           H  
ATOM   3488  HA  MET A 205      39.091  79.961  41.785  1.00 15.75           H  
ATOM   3489  HB2 MET A 205      40.158  81.938  40.076  1.00 15.56           H  
ATOM   3490  HB3 MET A 205      39.840  82.155  41.618  1.00 15.56           H  
ATOM   3491  HG2 MET A 205      41.573  80.683  42.180  1.00 15.69           H  
ATOM   3492  HG3 MET A 205      41.894  80.477  40.638  1.00 15.69           H  
ATOM   3493  HE1 MET A 205      42.700  84.107  43.023  1.00 17.63           H  
ATOM   3494  HE2 MET A 205      41.216  83.626  42.724  1.00 17.63           H  
ATOM   3495  HE3 MET A 205      42.183  82.720  43.600  1.00 17.63           H  
ATOM   3496  N   SER A 206      37.486  81.018  39.227  1.00 14.89           N  
ANISOU 3496  N   SER A 206     1527   2137   1994    106   -455   -277       N  
ATOM   3497  CA  SER A 206      36.214  81.563  38.767  1.00 15.01           C  
ANISOU 3497  CA  SER A 206     1522   2106   2077    113   -553   -112       C  
ATOM   3498  C   SER A 206      35.071  80.594  39.013  1.00 14.64           C  
ANISOU 3498  C   SER A 206     1388   1964   2210    174   -413     17       C  
ATOM   3499  O   SER A 206      33.925  81.023  39.212  1.00 15.57           O  
ANISOU 3499  O   SER A 206     1402   2045   2468    191   -285     -6       O  
ATOM   3500  CB  SER A 206      36.300  81.919  37.289  1.00 16.75           C  
ANISOU 3500  CB  SER A 206     1713   2425   2226     55   -440    -84       C  
ATOM   3501  OG  SER A 206      36.599  80.777  36.500  1.00 18.32           O  
ANISOU 3501  OG  SER A 206     2352   2497   2111     15   -571     10       O  
ATOM   3502  H   SER A 206      38.011  80.769  38.593  1.00 17.88           H  
ATOM   3503  HA  SER A 206      36.027  82.377  39.260  1.00 18.02           H  
ATOM   3504  HB2 SER A 206      35.447  82.283  37.004  1.00 20.11           H  
ATOM   3505  HB3 SER A 206      37.000  82.578  37.165  1.00 20.11           H  
ATOM   3506  HG  SER A 206      36.668  80.996  35.692  1.00 21.99           H  
ATOM   3507  N   ASP A 207      35.344  79.290  38.999  1.00 15.05           N  
ANISOU 3507  N   ASP A 207     1559   1905   2255     96   -518   -137       N  
ATOM   3508  CA  ASP A 207      34.306  78.282  39.248  1.00 15.76           C  
ANISOU 3508  CA  ASP A 207     1893   1824   2270   -128   -760    -50       C  
ATOM   3509  C   ASP A 207      34.948  77.076  39.905  1.00 14.56           C  
ANISOU 3509  C   ASP A 207     1645   1690   2198    -16   -543    -76       C  
ATOM   3510  O   ASP A 207      35.211  76.052  39.261  1.00 15.46           O  
ANISOU 3510  O   ASP A 207     1737   1896   2242    -64   -592    -80       O  
ATOM   3511  CB  ASP A 207      33.620  77.878  37.946  1.00 19.28           C  
ANISOU 3511  CB  ASP A 207     2279   2204   2843   -134  -1148    -40       C  
ATOM   3512  CG  ASP A 207      32.468  76.916  38.168  1.00 22.15           C  
ANISOU 3512  CG  ASP A 207     2319   2498   3600   -296  -1336   -308       C  
ATOM   3513  OD1 ASP A 207      32.060  76.723  39.333  1.00 23.79           O  
ANISOU 3513  OD1 ASP A 207     2156   2616   4269    -43   -744   -206       O  
ATOM   3514  OD2 ASP A 207      31.976  76.339  37.188  1.00 26.20           O  
ANISOU 3514  OD2 ASP A 207     2967   2772   4215   -464  -1465   -426       O  
ATOM   3515  H   ASP A 207      36.124  78.961  38.847  1.00 18.07           H  
ATOM   3516  HA  ASP A 207      33.641  78.646  39.853  1.00 18.92           H  
ATOM   3517  HB2 ASP A 207      33.270  78.672  37.513  1.00 23.15           H  
ATOM   3518  HB3 ASP A 207      34.267  77.443  37.369  1.00 23.15           H  
ATOM   3519  N   PRO A 208      35.211  77.153  41.203  1.00 14.67           N  
ANISOU 3519  N   PRO A 208     1728   1798   2050     66   -507   -269       N  
ATOM   3520  CA  PRO A 208      35.889  76.021  41.864  1.00 14.08           C  
ANISOU 3520  CA  PRO A 208     1670   1743   1935    184   -273    -50       C  
ATOM   3521  C   PRO A 208      35.173  74.693  41.661  1.00 14.39           C  
ANISOU 3521  C   PRO A 208     1337   1945   2188     40   -328    -81       C  
ATOM   3522  O   PRO A 208      35.828  73.631  41.579  1.00 15.37           O  
ANISOU 3522  O   PRO A 208     1552   1959   2328     51   -300   -179       O  
ATOM   3523  CB  PRO A 208      35.933  76.450  43.336  1.00 14.45           C  
ANISOU 3523  CB  PRO A 208     1692   1824   1976    171   -207   -200       C  
ATOM   3524  CG  PRO A 208      35.951  77.962  43.278  1.00 13.97           C  
ANISOU 3524  CG  PRO A 208     1611   1764   1934    161   -275   -365       C  
ATOM   3525  CD  PRO A 208      35.047  78.301  42.111  1.00 14.75           C  
ANISOU 3525  CD  PRO A 208     1704   1855   2044     93   -522   -418       C  
ATOM   3526  HA  PRO A 208      36.800  75.938  41.543  1.00 16.90           H  
ATOM   3527  HB2 PRO A 208      35.146  76.127  43.802  1.00 17.35           H  
ATOM   3528  HB3 PRO A 208      36.734  76.106  43.760  1.00 17.35           H  
ATOM   3529  HG2 PRO A 208      35.607  78.332  44.105  1.00 16.78           H  
ATOM   3530  HG3 PRO A 208      36.855  78.279  43.123  1.00 16.78           H  
ATOM   3531  HD2 PRO A 208      34.125  78.381  42.401  1.00 17.70           H  
ATOM   3532  HD3 PRO A 208      35.333  79.122  41.682  1.00 17.70           H  
ATOM   3533  N   ALA A 209      33.841  74.729  41.538  1.00 15.08           N  
ANISOU 3533  N   ALA A 209     1292   2152   2286   -104   -419   -121       N  
ATOM   3534  CA  ALA A 209      33.065  73.500  41.417  1.00 15.40           C  
ANISOU 3534  CA  ALA A 209     1469   2069   2315   -153   -319    -94       C  
ATOM   3535  C   ALA A 209      33.341  72.748  40.126  1.00 16.11           C  
ANISOU 3535  C   ALA A 209     1618   2013   2488   -334   -366   -193       C  
ATOM   3536  O   ALA A 209      33.006  71.563  40.038  1.00 17.27           O  
ANISOU 3536  O   ALA A 209     1977   1889   2696   -271   -406   -308       O  
ATOM   3537  CB  ALA A 209      31.584  73.846  41.550  1.00 16.30           C  
ANISOU 3537  CB  ALA A 209     1495   2378   2320   -141   -160    -39       C  
ATOM   3538  H   ALA A 209      33.369  75.448  41.522  1.00 18.10           H  
ATOM   3539  HA  ALA A 209      33.301  72.892  42.135  1.00 18.49           H  
ATOM   3540  HB1 ALA A 209      31.061  73.034  41.466  1.00 19.56           H  
ATOM   3541  HB2 ALA A 209      31.431  74.251  42.418  1.00 19.56           H  
ATOM   3542  HB3 ALA A 209      31.342  74.470  40.847  1.00 19.56           H  
ATOM   3543  N   LYS A 210      33.935  73.398  39.123  1.00 15.97           N  
ANISOU 3543  N   LYS A 210     1752   2010   2305   -278   -252   -242       N  
ATOM   3544  CA  LYS A 210      34.312  72.692  37.898  1.00 17.79           C  
ANISOU 3544  CA  LYS A 210     2099   2189   2472   -170      2   -388       C  
ATOM   3545  C   LYS A 210      35.161  71.463  38.194  1.00 18.23           C  
ANISOU 3545  C   LYS A 210     2186   2139   2600   -225   -315   -540       C  
ATOM   3546  O   LYS A 210      35.055  70.444  37.488  1.00 19.37           O  
ANISOU 3546  O   LYS A 210     2407   2194   2760   -158   -446   -616       O  
ATOM   3547  CB  LYS A 210      35.065  73.662  36.981  1.00 21.43           C  
ANISOU 3547  CB  LYS A 210     2866   2780   2495   -325    184   -341       C  
ATOM   3548  CG  LYS A 210      35.580  73.068  35.690  1.00 25.63           C  
ANISOU 3548  CG  LYS A 210     3382   3429   2926   -520    143   -138       C  
ATOM   3549  CD  LYS A 210      36.292  74.130  34.849  1.00 29.14           C  
ANISOU 3549  CD  LYS A 210     3922   4048   3102   -638    159    116       C  
ATOM   3550  CE  LYS A 210      36.812  73.541  33.546  1.00 32.68           C  
ANISOU 3550  CE  LYS A 210     4399   4617   3399   -713    114    220       C  
ATOM   3551  NZ  LYS A 210      37.603  74.529  32.748  1.00 35.08           N  
ANISOU 3551  NZ  LYS A 210     4748   5011   3570   -691     90    218       N  
ATOM   3552  H   LYS A 210      34.129  74.236  39.124  1.00 19.17           H  
ATOM   3553  HA  LYS A 210      33.514  72.386  37.438  1.00 21.36           H  
ATOM   3554  HB2 LYS A 210      34.466  74.388  36.747  1.00 25.72           H  
ATOM   3555  HB3 LYS A 210      35.831  74.007  37.466  1.00 25.72           H  
ATOM   3556  HG2 LYS A 210      36.211  72.359  35.889  1.00 30.76           H  
ATOM   3557  HG3 LYS A 210      34.836  72.716  35.177  1.00 30.76           H  
ATOM   3558  HD2 LYS A 210      35.669  74.843  34.636  1.00 34.98           H  
ATOM   3559  HD3 LYS A 210      37.044  74.484  35.347  1.00 34.98           H  
ATOM   3560  HE2 LYS A 210      37.388  72.787  33.747  1.00 39.22           H  
ATOM   3561  HE3 LYS A 210      36.060  73.251  33.007  1.00 39.22           H  
ATOM   3562  HZ1 LYS A 210      37.998  74.120  32.063  1.00 42.10           H  
ATOM   3563  HZ2 LYS A 210      37.066  75.165  32.433  1.00 42.10           H  
ATOM   3564  HZ3 LYS A 210      38.227  74.904  33.259  1.00 42.10           H  
ATOM   3565  N   TYR A 211      36.004  71.533  39.227  1.00 18.63           N  
ANISOU 3565  N   TYR A 211     2122   2232   2725     42   -422   -629       N  
ATOM   3566  CA  TYR A 211      36.869  70.432  39.628  1.00 18.42           C  
ANISOU 3566  CA  TYR A 211     2015   2156   2829    167   -446   -546       C  
ATOM   3567  C   TYR A 211      36.480  69.834  40.978  1.00 18.64           C  
ANISOU 3567  C   TYR A 211     2291   2119   2673    255   -641   -162       C  
ATOM   3568  O   TYR A 211      37.296  69.154  41.608  1.00 21.01           O  
ANISOU 3568  O   TYR A 211     2863   2360   2760    499   -514    130       O  
ATOM   3569  CB  TYR A 211      38.332  70.884  39.631  1.00 19.09           C  
ANISOU 3569  CB  TYR A 211     1834   2398   3021    345   -314   -593       C  
ATOM   3570  CG  TYR A 211      38.764  71.374  38.266  1.00 20.54           C  
ANISOU 3570  CG  TYR A 211     2008   2789   3009    187   -168   -505       C  
ATOM   3571  CD1 TYR A 211      38.900  70.493  37.204  1.00 21.98           C  
ANISOU 3571  CD1 TYR A 211     2283   3008   3060    -60    134   -566       C  
ATOM   3572  CD2 TYR A 211      39.004  72.712  38.032  1.00 22.02           C  
ANISOU 3572  CD2 TYR A 211     2113   3099   3156     11     75   -387       C  
ATOM   3573  CE1 TYR A 211      39.268  70.936  35.961  1.00 22.35           C  
ANISOU 3573  CE1 TYR A 211     2251   3299   2943     41    328   -645       C  
ATOM   3574  CE2 TYR A 211      39.377  73.161  36.788  1.00 24.00           C  
ANISOU 3574  CE2 TYR A 211     2277   3561   3279   -108    274   -369       C  
ATOM   3575  CZ  TYR A 211      39.513  72.263  35.760  1.00 24.12           C  
ANISOU 3575  CZ  TYR A 211     2338   3707   3118    -25    366   -364       C  
ATOM   3576  OH  TYR A 211      39.881  72.674  34.503  1.00 27.28           O  
ANISOU 3576  OH  TYR A 211     2705   4271   3390   -103    461   -214       O  
ATOM   3577  H   TYR A 211      36.090  72.230  39.723  1.00 22.37           H  
ATOM   3578  HA  TYR A 211      36.781  69.722  38.974  1.00 22.12           H  
ATOM   3579  HB2 TYR A 211      38.442  71.610  40.265  1.00 22.91           H  
ATOM   3580  HB3 TYR A 211      38.898  70.137  39.881  1.00 22.91           H  
ATOM   3581  HD1 TYR A 211      38.739  69.587  37.338  1.00 26.38           H  
ATOM   3582  HD2 TYR A 211      38.912  73.322  38.728  1.00 26.44           H  
ATOM   3583  HE1 TYR A 211      39.351  70.334  35.256  1.00 26.83           H  
ATOM   3584  HE2 TYR A 211      39.537  74.066  36.644  1.00 28.80           H  
ATOM   3585  HH  TYR A 211      40.013  73.504  34.500  1.00 32.75           H  
ATOM   3586  N   GLY A 212      35.247  70.071  41.427  1.00 17.54           N  
ANISOU 3586  N   GLY A 212     2322   1826   2516      9   -565   -190       N  
ATOM   3587  CA  GLY A 212      34.763  69.511  42.663  1.00 17.88           C  
ANISOU 3587  CA  GLY A 212     2375   1864   2554    -51   -474   -146       C  
ATOM   3588  C   GLY A 212      35.210  70.230  43.910  1.00 16.97           C  
ANISOU 3588  C   GLY A 212     2238   1908   2301   -204   -414      3       C  
ATOM   3589  O   GLY A 212      35.113  69.660  45.002  1.00 19.46           O  
ANISOU 3589  O   GLY A 212     2706   2425   2262   -331   -475     28       O  
ATOM   3590  H   GLY A 212      34.669  70.561  41.020  1.00 21.05           H  
ATOM   3591  HA2 GLY A 212      33.793  69.520  42.648  1.00 21.46           H  
ATOM   3592  HA3 GLY A 212      35.069  68.592  42.727  1.00 21.46           H  
ATOM   3593  N   ASP A 213      35.722  71.463  43.784  1.00 15.82           N  
ANISOU 3593  N   ASP A 213     1847   1791   2371   -139   -338    -37       N  
ATOM   3594  CA  ASP A 213      36.105  72.215  44.975  1.00 15.48           C  
ANISOU 3594  CA  ASP A 213     1553   1922   2406     29   -460    126       C  
ATOM   3595  C   ASP A 213      34.950  73.114  45.422  1.00 15.43           C  
ANISOU 3595  C   ASP A 213     1452   1992   2421    -94   -398      4       C  
ATOM   3596  O   ASP A 213      34.119  73.526  44.603  1.00 16.10           O  
ANISOU 3596  O   ASP A 213     1443   2144   2530    -96   -464   -155       O  
ATOM   3597  CB  ASP A 213      37.346  73.059  44.686  1.00 15.80           C  
ANISOU 3597  CB  ASP A 213     1656   1873   2473    104   -346    233       C  
ATOM   3598  CG  ASP A 213      38.588  72.214  44.486  1.00 17.29           C  
ANISOU 3598  CG  ASP A 213     1707   2174   2688     74   -313    254       C  
ATOM   3599  OD1 ASP A 213      38.696  71.138  45.121  1.00 17.51           O  
ANISOU 3599  OD1 ASP A 213     1748   2128   2777    321   -204    206       O  
ATOM   3600  OD2 ASP A 213      39.467  72.632  43.701  1.00 18.50           O  
ANISOU 3600  OD2 ASP A 213     1716   2455   2859    305   -230    306       O  
ATOM   3601  H   ASP A 213      35.854  71.872  43.039  1.00 18.99           H  
ATOM   3602  HA  ASP A 213      36.319  71.611  45.702  1.00 18.58           H  
ATOM   3603  HB2 ASP A 213      37.198  73.574  43.877  1.00 18.96           H  
ATOM   3604  HB3 ASP A 213      37.504  73.656  45.434  1.00 18.96           H  
ATOM   3605  N   PRO A 214      34.884  73.400  46.722  1.00 15.51           N  
ANISOU 3605  N   PRO A 214     1445   2073   2374    -59   -174   -133       N  
ATOM   3606  CA  PRO A 214      33.779  74.209  47.256  1.00 15.45           C  
ANISOU 3606  CA  PRO A 214     1578   1985   2309    -62   -220      6       C  
ATOM   3607  C   PRO A 214      33.844  75.659  46.817  1.00 14.93           C  
ANISOU 3607  C   PRO A 214     1436   1866   2371   -175   -354    114       C  
ATOM   3608  O   PRO A 214      34.924  76.258  46.711  1.00 15.05           O  
ANISOU 3608  O   PRO A 214     1501   1856   2361    -57   -219     24       O  
ATOM   3609  CB  PRO A 214      33.971  74.100  48.777  1.00 15.94           C  
ANISOU 3609  CB  PRO A 214     1555   2074   2426   -140    -87    -16       C  
ATOM   3610  CG  PRO A 214      35.440  73.825  48.941  1.00 16.34           C  
ANISOU 3610  CG  PRO A 214     1607   2179   2422   -175    -87   -112       C  
ATOM   3611  CD  PRO A 214      35.776  72.912  47.789  1.00 16.23           C  
ANISOU 3611  CD  PRO A 214     1651   2158   2358     22   -247   -100       C  
ATOM   3612  HA  PRO A 214      32.931  73.827  46.982  1.00 18.55           H  
ATOM   3613  HB2 PRO A 214      33.720  74.933  49.206  1.00 19.13           H  
ATOM   3614  HB3 PRO A 214      33.437  73.371  49.130  1.00 19.13           H  
ATOM   3615  HG2 PRO A 214      35.942  74.653  48.888  1.00 19.62           H  
ATOM   3616  HG3 PRO A 214      35.605  73.390  49.792  1.00 19.62           H  
ATOM   3617  HD2 PRO A 214      36.708  73.003  47.534  1.00 19.48           H  
ATOM   3618  HD3 PRO A 214      35.582  71.987  48.010  1.00 19.48           H  
ATOM   3619  N   ASP A 215      32.663  76.225  46.582  1.00 15.78           N  
ANISOU 3619  N   ASP A 215     1473   1811   2712     -9   -381    134       N  
ATOM   3620  CA  ASP A 215      32.511  77.628  46.224  1.00 15.64           C  
ANISOU 3620  CA  ASP A 215     1466   1784   2691    -11   -275     48       C  
ATOM   3621  C   ASP A 215      31.644  78.368  47.236  1.00 15.52           C  
ANISOU 3621  C   ASP A 215     1434   1762   2700    157   -247    109       C  
ATOM   3622  O   ASP A 215      31.145  79.463  46.945  1.00 15.42           O  
ANISOU 3622  O   ASP A 215     1448   1729   2681     85   -330    -61       O  
ATOM   3623  CB  ASP A 215      31.952  77.764  44.810  1.00 16.38           C  
ANISOU 3623  CB  ASP A 215     1429   1969   2825    -50   -429    -51       C  
ATOM   3624  CG  ASP A 215      30.580  77.156  44.668  1.00 16.15           C  
ANISOU 3624  CG  ASP A 215     1415   1921   2800   -147   -422     98       C  
ATOM   3625  OD1 ASP A 215      30.047  76.631  45.675  1.00 17.52           O  
ANISOU 3625  OD1 ASP A 215     1723   1913   3020   -166   -469     58       O  
ATOM   3626  OD2 ASP A 215      30.032  77.218  43.544  1.00 17.50           O  
ANISOU 3626  OD2 ASP A 215     1590   2153   2908    -69   -565     63       O  
ATOM   3627  H   ASP A 215      31.916  75.801  46.626  1.00 18.95           H  
ATOM   3628  HA  ASP A 215      33.383  78.053  46.223  1.00 18.77           H  
ATOM   3629  HB2 ASP A 215      31.888  78.705  44.584  1.00 19.66           H  
ATOM   3630  HB3 ASP A 215      32.546  77.313  44.190  1.00 19.66           H  
ATOM   3631  N   HIS A 216      31.510  77.807  48.436  1.00 15.95           N  
ANISOU 3631  N   HIS A 216     1624   1735   2702     36    -74    116       N  
ATOM   3632  CA  HIS A 216      30.681  78.360  49.491  1.00 16.00           C  
ANISOU 3632  CA  HIS A 216     1439   1816   2824    -75    -69    139       C  
ATOM   3633  C   HIS A 216      31.088  77.706  50.808  1.00 16.69           C  
ANISOU 3633  C   HIS A 216     1630   1758   2951    -35    -71    141       C  
ATOM   3634  O   HIS A 216      31.427  76.520  50.834  1.00 17.85           O  
ANISOU 3634  O   HIS A 216     1883   1782   3119   -118    142     79       O  
ATOM   3635  CB  HIS A 216      29.195  78.086  49.225  1.00 18.57           C  
ANISOU 3635  CB  HIS A 216     1623   2130   3301   -137   -172     35       C  
ATOM   3636  CG  HIS A 216      28.277  78.892  50.087  1.00 19.12           C  
ANISOU 3636  CG  HIS A 216     1534   2167   3563    -48     16   -151       C  
ATOM   3637  ND1 HIS A 216      27.900  78.493  51.354  1.00 19.36           N  
ANISOU 3637  ND1 HIS A 216     1469   2167   3720     88    116   -304       N  
ATOM   3638  CD2 HIS A 216      27.653  80.075  49.862  1.00 18.70           C  
ANISOU 3638  CD2 HIS A 216     1451   2048   3607    -67     22   -213       C  
ATOM   3639  CE1 HIS A 216      27.085  79.396  51.869  1.00 19.90           C  
ANISOU 3639  CE1 HIS A 216     1536   2316   3708      9    195   -277       C  
ATOM   3640  NE2 HIS A 216      26.921  80.368  50.986  1.00 19.98           N  
ANISOU 3640  NE2 HIS A 216     1538   2277   3775    -34    -43   -156       N  
ATOM   3641  H   HIS A 216      31.905  77.079  48.668  1.00 19.15           H  
ATOM   3642  HA  HIS A 216      30.819  79.319  49.550  1.00 19.21           H  
ATOM   3643  HB2 HIS A 216      28.998  78.300  48.300  1.00 22.29           H  
ATOM   3644  HB3 HIS A 216      29.015  77.148  49.394  1.00 22.29           H  
ATOM   3645  HD2 HIS A 216      27.710  80.591  49.091  1.00 22.45           H  
ATOM   3646  HE1 HIS A 216      26.691  79.354  52.711  1.00 23.89           H  
ATOM   3647  HE2 HIS A 216      26.436  81.069  51.098  1.00 23.98           H  
ATOM   3648  N   TYR A 217      31.040  78.481  51.889  1.00 17.90           N  
ANISOU 3648  N   TYR A 217     1972   1931   2898    -77     88    122       N  
ATOM   3649  CA  TYR A 217      31.458  77.984  53.196  1.00 18.02           C  
ANISOU 3649  CA  TYR A 217     2286   1796   2764   -271    280    250       C  
ATOM   3650  C   TYR A 217      30.678  76.748  53.613  1.00 18.28           C  
ANISOU 3650  C   TYR A 217     2186   1900   2862   -240    484    395       C  
ATOM   3651  O   TYR A 217      31.224  75.871  54.292  1.00 19.19           O  
ANISOU 3651  O   TYR A 217     2452   1898   2943    -97    387    513       O  
ATOM   3652  CB  TYR A 217      31.274  79.081  54.244  1.00 20.18           C  
ANISOU 3652  CB  TYR A 217     2805   1973   2888   -115    171    108       C  
ATOM   3653  CG  TYR A 217      31.969  78.824  55.558  1.00 22.26           C  
ANISOU 3653  CG  TYR A 217     3387   2182   2887   -241    198    236       C  
ATOM   3654  CD1 TYR A 217      33.350  78.800  55.626  1.00 23.11           C  
ANISOU 3654  CD1 TYR A 217     3684   2172   2925   -289    -92    268       C  
ATOM   3655  CD2 TYR A 217      31.254  78.635  56.728  1.00 25.06           C  
ANISOU 3655  CD2 TYR A 217     3867   2665   2990   -167    -18    273       C  
ATOM   3656  CE1 TYR A 217      34.003  78.586  56.810  1.00 24.78           C  
ANISOU 3656  CE1 TYR A 217     3974   2339   3103   -230    -69    192       C  
ATOM   3657  CE2 TYR A 217      31.906  78.413  57.926  1.00 25.63           C  
ANISOU 3657  CE2 TYR A 217     3936   2794   3009    -18   -112    281       C  
ATOM   3658  CZ  TYR A 217      33.286  78.399  57.957  1.00 25.20           C  
ANISOU 3658  CZ  TYR A 217     4009   2547   3020   -268     67    414       C  
ATOM   3659  OH  TYR A 217      33.966  78.192  59.153  1.00 27.66           O  
ANISOU 3659  OH  TYR A 217     4263   2914   3332   -234    161    516       O  
ATOM   3660  H   TYR A 217      30.771  79.298  51.895  1.00 21.49           H  
ATOM   3661  HA  TYR A 217      32.397  77.746  53.148  1.00 21.63           H  
ATOM   3662  HB2 TYR A 217      31.626  79.911  53.885  1.00 24.22           H  
ATOM   3663  HB3 TYR A 217      30.326  79.174  54.428  1.00 24.22           H  
ATOM   3664  HD1 TYR A 217      33.846  78.933  54.851  1.00 27.74           H  
ATOM   3665  HD2 TYR A 217      30.325  78.657  56.707  1.00 30.08           H  
ATOM   3666  HE1 TYR A 217      34.933  78.568  56.833  1.00 29.74           H  
ATOM   3667  HE2 TYR A 217      31.419  78.275  58.706  1.00 30.77           H  
ATOM   3668  HH  TYR A 217      34.795  78.208  59.018  1.00 33.20           H  
ATOM   3669  N   SER A 218      29.410  76.655  53.215  1.00 19.61           N  
ANISOU 3669  N   SER A 218     2204   2087   3159   -259    536    286       N  
ATOM   3670  CA  SER A 218      28.605  75.507  53.613  1.00 20.43           C  
ANISOU 3670  CA  SER A 218     2305   2002   3456   -306    563    281       C  
ATOM   3671  C   SER A 218      29.129  74.215  53.014  1.00 20.40           C  
ANISOU 3671  C   SER A 218     2401   1855   3493   -320    477    320       C  
ATOM   3672  O   SER A 218      28.772  73.129  53.493  1.00 21.80           O  
ANISOU 3672  O   SER A 218     2746   1839   3700   -287    505    118       O  
ATOM   3673  CB  SER A 218      27.148  75.687  53.180  1.00 22.16           C  
ANISOU 3673  CB  SER A 218     2321   2373   3725   -404    603     60       C  
ATOM   3674  OG  SER A 218      27.038  75.697  51.769  1.00 22.78           O  
ANISOU 3674  OG  SER A 218     2307   2564   3785   -454    538     90       O  
ATOM   3675  H   SER A 218      29.001  77.230  52.725  1.00 23.53           H  
ATOM   3676  HA  SER A 218      28.629  75.446  54.581  1.00 24.52           H  
ATOM   3677  HB2 SER A 218      26.621  74.953  53.532  1.00 26.60           H  
ATOM   3678  HB3 SER A 218      26.817  76.530  53.528  1.00 26.60           H  
ATOM   3679  HG  SER A 218      27.652  76.164  51.437  1.00 27.34           H  
ATOM   3680  N  ALYS A 219      29.965  74.306  51.983  0.73 18.84           N  
ANISOU 3680  N  ALYS A 219     2111   1693   3356   -118    406    417       N  
ATOM   3681  N  BLYS A 219      29.951  74.301  51.969  0.27 19.83           N  
ANISOU 3681  N  BLYS A 219     2306   1771   3458   -321    514    455       N  
ATOM   3682  CA ALYS A 219      30.514  73.144  51.305  0.73 19.38           C  
ANISOU 3682  CA ALYS A 219     2134   1873   3357   -138    332    386       C  
ATOM   3683  CA BLYS A 219      30.506  73.132  51.305  0.27 19.96           C  
ANISOU 3683  CA BLYS A 219     2306   1807   3471   -389    541    548       C  
ATOM   3684  C  ALYS A 219      31.942  72.847  51.716  0.73 19.28           C  
ANISOU 3684  C  ALYS A 219     2164   1793   3369   -224    233    457       C  
ATOM   3685  C  BLYS A 219      31.967  72.899  51.669  0.27 19.80           C  
ANISOU 3685  C  BLYS A 219     2273   1764   3488   -378    409    526       C  
ATOM   3686  O  ALYS A 219      32.585  71.994  51.103  0.73 20.50           O  
ANISOU 3686  O  ALYS A 219     2245   2036   3508     28    249    608       O  
ATOM   3687  O  BLYS A 219      32.662  72.157  50.968  0.27 20.61           O  
ANISOU 3687  O  BLYS A 219     2349   1867   3617   -402    434    548       O  
ATOM   3688  CB ALYS A 219      30.428  73.345  49.791  0.73 19.85           C  
ANISOU 3688  CB ALYS A 219     2026   2128   3389     23    127     19       C  
ATOM   3689  CB BLYS A 219      30.327  73.250  49.787  0.27 20.29           C  
ANISOU 3689  CB BLYS A 219     2308   1908   3493   -439    601    572       C  
ATOM   3690  CG ALYS A 219      29.006  73.228  49.286  0.73 20.55           C  
ANISOU 3690  CG ALYS A 219     2025   2352   3432   -126    -19   -163       C  
ATOM   3691  CG BLYS A 219      28.864  73.366  49.358  0.27 20.50           C  
ANISOU 3691  CG BLYS A 219     2280   2019   3488   -646    731    689       C  
ATOM   3692  CD ALYS A 219      28.833  73.834  47.920  0.73 20.46           C  
ANISOU 3692  CD ALYS A 219     1962   2480   3331    -44   -200   -197       C  
ATOM   3693  CD BLYS A 219      28.685  73.492  47.846  0.27 20.29           C  
ANISOU 3693  CD BLYS A 219     2354   2051   3304   -715    698    851       C  
ATOM   3694  CE ALYS A 219      27.581  73.328  47.292  0.73 20.68           C  
ANISOU 3694  CE ALYS A 219     2093   2685   3078     -8   -407   -588       C  
ATOM   3695  CE BLYS A 219      27.206  73.576  47.476  0.27 20.62           C  
ANISOU 3695  CE BLYS A 219     2504   2097   3233   -717    698    934       C  
ATOM   3696  NZ ALYS A 219      26.389  73.625  48.132  0.73 20.84           N  
ANISOU 3696  NZ ALYS A 219     1895   2836   3186     59   -297   -676       N  
ATOM   3697  NZ BLYS A 219      26.949  73.738  46.011  0.27 20.15           N  
ANISOU 3697  NZ BLYS A 219     2544   2042   3068   -624    603   1045       N  
ATOM   3698  H  ALYS A 219      30.234  75.053  51.653  0.73 22.62           H  
ATOM   3699  H  BLYS A 219      30.205  75.046  51.622  0.27 23.80           H  
ATOM   3700  HA ALYS A 219      29.982  72.367  51.535  0.73 23.27           H  
ATOM   3701  HA BLYS A 219      30.011  72.348  51.593  0.27 23.96           H  
ATOM   3702  HB2ALYS A 219      30.758  74.229  49.568  0.73 23.83           H  
ATOM   3703  HB2BLYS A 219      30.793  74.043  49.477  0.27 24.36           H  
ATOM   3704  HB3ALYS A 219      30.965  72.669  49.349  0.73 23.83           H  
ATOM   3705  HB3BLYS A 219      30.700  72.460  49.365  0.27 24.36           H  
ATOM   3706  HG2ALYS A 219      28.763  72.290  49.231  0.73 24.67           H  
ATOM   3707  HG2BLYS A 219      28.388  72.572  49.649  0.27 24.60           H  
ATOM   3708  HG3ALYS A 219      28.411  73.689  49.898  0.73 24.67           H  
ATOM   3709  HG3BLYS A 219      28.477  74.154  49.770  0.27 24.60           H  
ATOM   3710  HD2ALYS A 219      28.774  74.800  47.996  0.73 24.56           H  
ATOM   3711  HD2BLYS A 219      29.125  74.298  47.534  0.27 24.36           H  
ATOM   3712  HD3ALYS A 219      29.584  73.591  47.357  0.73 24.56           H  
ATOM   3713  HD3BLYS A 219      29.067  72.714  47.409  0.27 24.36           H  
ATOM   3714  HE2ALYS A 219      27.460  73.754  46.429  0.73 24.82           H  
ATOM   3715  HE2BLYS A 219      26.767  72.760  47.763  0.27 24.75           H  
ATOM   3716  HE3ALYS A 219      27.644  72.367  47.181  0.73 24.82           H  
ATOM   3717  HE3BLYS A 219      26.815  74.339  47.929  0.27 24.75           H  
ATOM   3718  HZ1ALYS A 219      25.648  73.384  47.703  0.73 25.01           H  
ATOM   3719  HZ1BLYS A 219      26.074  73.795  45.860  0.27 24.18           H  
ATOM   3720  HZ2ALYS A 219      26.438  73.176  48.899  0.73 25.01           H  
ATOM   3721  HZ2BLYS A 219      27.343  74.479  45.713  0.27 24.18           H  
ATOM   3722  HZ3ALYS A 219      26.351  74.496  48.309  0.73 25.01           H  
ATOM   3723  HZ3BLYS A 219      27.274  73.039  45.566  0.27 24.18           H  
ATOM   3724  N   ARG A 220      32.447  73.502  52.753  1.00 19.44           N  
ANISOU 3724  N   ARG A 220     2195   1755   3438   -255    301    489       N  
ATOM   3725  CA  ARG A 220      33.828  73.287  53.151  1.00 20.06           C  
ANISOU 3725  CA  ARG A 220     2266   1859   3495   -377    137    370       C  
ATOM   3726  C   ARG A 220      34.075  71.832  53.538  1.00 19.68           C  
ANISOU 3726  C   ARG A 220     2175   1939   3364   -428    208    463       C  
ATOM   3727  O   ARG A 220      33.224  71.158  54.134  1.00 21.37           O  
ANISOU 3727  O   ARG A 220     2568   2037   3512   -370    241    249       O  
ATOM   3728  CB  ARG A 220      34.189  74.198  54.313  1.00 20.99           C  
ANISOU 3728  CB  ARG A 220     2482   1939   3553   -366    -36    334       C  
ATOM   3729  CG  ARG A 220      33.556  73.863  55.623  1.00 21.78           C  
ANISOU 3729  CG  ARG A 220     2703   2049   3523   -497     -5    280       C  
ATOM   3730  CD  ARG A 220      33.752  75.042  56.571  1.00 24.15           C  
ANISOU 3730  CD  ARG A 220     3229   2372   3574   -393     74    244       C  
ATOM   3731  NE  ARG A 220      33.201  74.809  57.891  1.00 26.44           N  
ANISOU 3731  NE  ARG A 220     3660   2933   3452   -265     58    276       N  
ATOM   3732  CZ  ARG A 220      31.910  74.896  58.184  1.00 29.44           C  
ANISOU 3732  CZ  ARG A 220     4027   3713   3446   -281    152    429       C  
ATOM   3733  NH1 ARG A 220      31.039  75.223  57.244  1.00 29.89           N  
ANISOU 3733  NH1 ARG A 220     4089   3787   3479   -284     96    470       N  
ATOM   3734  NH2 ARG A 220      31.492  74.664  59.423  1.00 31.84           N  
ANISOU 3734  NH2 ARG A 220     4400   4169   3528   -343    134    512       N  
ATOM   3735  H  AARG A 220      32.018  74.069  53.237  0.73 23.34           H  
ATOM   3736  H  BARG A 220      32.002  74.031  53.264  0.27 23.34           H  
ATOM   3737  HA  ARG A 220      34.404  73.498  52.400  1.00 24.07           H  
ATOM   3738  HB2 ARG A 220      35.149  74.162  54.440  1.00 25.19           H  
ATOM   3739  HB3 ARG A 220      33.918  75.101  54.085  1.00 25.19           H  
ATOM   3740  HG2 ARG A 220      32.606  73.707  55.503  1.00 26.14           H  
ATOM   3741  HG3 ARG A 220      33.976  73.077  56.004  1.00 26.14           H  
ATOM   3742  HD2 ARG A 220      34.702  75.212  56.670  1.00 28.98           H  
ATOM   3743  HD3 ARG A 220      33.313  75.823  56.198  1.00 28.98           H  
ATOM   3744  HE  ARG A 220      33.745  74.602  58.524  1.00 31.73           H  
ATOM   3745 HH11 ARG A 220      31.309  75.380  56.443  1.00 35.87           H  
ATOM   3746 HH12 ARG A 220      30.202  75.278  57.434  1.00 35.87           H  
ATOM   3747 HH21 ARG A 220      32.058  74.458  60.037  1.00 38.21           H  
ATOM   3748 HH22 ARG A 220      30.655  74.720  59.612  1.00 38.21           H  
ATOM   3749  N   TYR A 221      35.254  71.350  53.168  1.00 19.21           N  
ANISOU 3749  N   TYR A 221     2117   1804   3376   -323    286    541       N  
ATOM   3750  CA  TYR A 221      35.719  70.024  53.540  1.00 19.43           C  
ANISOU 3750  CA  TYR A 221     2188   1903   3289   -336    153    389       C  
ATOM   3751  C   TYR A 221      36.216  70.042  54.977  1.00 21.48           C  
ANISOU 3751  C   TYR A 221     2705   2146   3312   -566    302    581       C  
ATOM   3752  O   TYR A 221      36.953  70.951  55.377  1.00 22.31           O  
ANISOU 3752  O   TYR A 221     3132   2264   3082   -630     53    742       O  
ATOM   3753  CB  TYR A 221      36.846  69.643  52.575  1.00 19.83           C  
ANISOU 3753  CB  TYR A 221     2065   2002   3468   -159    -31    228       C  
ATOM   3754  CG  TYR A 221      37.510  68.337  52.883  1.00 20.52           C  
ANISOU 3754  CG  TYR A 221     2301   1849   3646     26     21    299       C  
ATOM   3755  CD1 TYR A 221      36.942  67.136  52.505  1.00 22.69           C  
ANISOU 3755  CD1 TYR A 221     2464   2144   4014     49   -120    394       C  
ATOM   3756  CD2 TYR A 221      38.716  68.309  53.551  1.00 21.23           C  
ANISOU 3756  CD2 TYR A 221     2411   1956   3700    -39      1    232       C  
ATOM   3757  CE1 TYR A 221      37.568  65.938  52.799  1.00 23.77           C  
ANISOU 3757  CE1 TYR A 221     2673   2092   4266    -18   -137    374       C  
ATOM   3758  CE2 TYR A 221      39.337  67.129  53.849  1.00 22.98           C  
ANISOU 3758  CE2 TYR A 221     2670   2093   3968     16    -98    188       C  
ATOM   3759  CZ  TYR A 221      38.771  65.950  53.473  1.00 24.73           C  
ANISOU 3759  CZ  TYR A 221     3013   2127   4258     80   -130    448       C  
ATOM   3760  OH  TYR A 221      39.412  64.760  53.776  1.00 27.58           O  
ANISOU 3760  OH  TYR A 221     3521   2358   4602     91   -108    498       O  
ATOM   3761  H   TYR A 221      35.819  71.784  52.687  1.00 23.05           H  
ATOM   3762  HA  TYR A 221      35.010  69.364  53.488  1.00 23.32           H  
ATOM   3763  HB2 TYR A 221      36.478  69.581  51.679  1.00 23.80           H  
ATOM   3764  HB3 TYR A 221      37.527  70.333  52.607  1.00 23.80           H  
ATOM   3765  HD1 TYR A 221      36.132  67.133  52.049  1.00 27.24           H  
ATOM   3766  HD2 TYR A 221      39.116  69.110  53.803  1.00 25.48           H  
ATOM   3767  HE1 TYR A 221      37.182  65.132  52.544  1.00 28.53           H  
ATOM   3768  HE2 TYR A 221      40.146  67.132  54.308  1.00 27.58           H  
ATOM   3769  HH  TYR A 221      38.925  64.109  53.564  1.00 33.11           H  
ATOM   3770  N   THR A 222      35.803  69.048  55.761  1.00 23.10           N  
ANISOU 3770  N   THR A 222     3021   2294   3463   -478    517    668       N  
ATOM   3771  CA  THR A 222      36.145  68.978  57.175  1.00 26.97           C  
ANISOU 3771  CA  THR A 222     3686   2686   3875   -535    624    929       C  
ATOM   3772  C   THR A 222      36.892  67.698  57.525  1.00 27.81           C  
ANISOU 3772  C   THR A 222     3872   2781   3912   -336    252   1184       C  
ATOM   3773  O   THR A 222      37.033  67.390  58.715  1.00 30.68           O  
ANISOU 3773  O   THR A 222     4386   3201   4068   -278    324   1128       O  
ATOM   3774  CB  THR A 222      34.891  69.114  58.050  1.00 30.05           C  
ANISOU 3774  CB  THR A 222     4277   3083   4056   -442   1052    913       C  
ATOM   3775  OG1 THR A 222      33.996  68.033  57.784  1.00 31.73           O  
ANISOU 3775  OG1 THR A 222     4505   3260   4291   -481   1423   1060       O  
ATOM   3776  CG2 THR A 222      34.180  70.418  57.758  1.00 31.97           C  
ANISOU 3776  CG2 THR A 222     4541   3383   4224   -435   1277    799       C  
ATOM   3777  H   THR A 222      35.315  68.394  55.489  1.00 27.73           H  
ATOM   3778  HA  THR A 222      36.724  69.727  57.386  1.00 32.37           H  
ATOM   3779  HB  THR A 222      35.150  69.102  58.985  1.00 36.06           H  
ATOM   3780  HG1 THR A 222      34.361  67.303  57.981  1.00 38.08           H  
ATOM   3781 HG21 THR A 222      33.607  70.658  58.503  1.00 38.37           H  
ATOM   3782 HG22 THR A 222      34.829  71.126  57.619  1.00 38.37           H  
ATOM   3783 HG23 THR A 222      33.637  70.328  56.959  1.00 38.37           H  
ATOM   3784  N   GLY A 223      37.354  66.943  56.535  1.00 27.36           N  
ANISOU 3784  N   GLY A 223     3782   2632   3982   -202   -130   1196       N  
ATOM   3785  CA  GLY A 223      38.139  65.748  56.780  1.00 27.77           C  
ANISOU 3785  CA  GLY A 223     3854   2593   4104   -360   -350   1207       C  
ATOM   3786  C   GLY A 223      39.598  66.059  57.083  1.00 27.95           C  
ANISOU 3786  C   GLY A 223     3853   2589   4176   -562   -461   1177       C  
ATOM   3787  O   GLY A 223      40.007  67.214  57.222  1.00 27.47           O  
ANISOU 3787  O   GLY A 223     3660   2676   4101   -785   -398   1002       O  
ATOM   3788  H   GLY A 223      37.223  67.108  55.701  1.00 32.84           H  
ATOM   3789  HA2 GLY A 223      37.766  65.269  57.536  1.00 33.33           H  
ATOM   3790  HA3 GLY A 223      38.105  65.176  55.996  1.00 33.33           H  
ATOM   3791  N   THR A 224      40.396  64.994  57.184  1.00 28.87           N  
ANISOU 3791  N   THR A 224     3885   2643   4441   -537   -466   1156       N  
ATOM   3792  CA  THR A 224      41.796  65.133  57.567  1.00 30.09           C  
ANISOU 3792  CA  THR A 224     3984   2774   4675   -492   -387   1268       C  
ATOM   3793  C   THR A 224      42.761  65.125  56.389  1.00 30.33           C  
ANISOU 3793  C   THR A 224     3991   2716   4818   -519   -523    934       C  
ATOM   3794  O   THR A 224      43.927  65.499  56.568  1.00 30.79           O  
ANISOU 3794  O   THR A 224     3707   3082   4912   -512   -535    872       O  
ATOM   3795  CB  THR A 224      42.196  64.021  58.540  1.00 32.81           C  
ANISOU 3795  CB  THR A 224     4217   3260   4989   -409   -231   1354       C  
ATOM   3796  OG1 THR A 224      42.040  62.758  57.891  1.00 33.65           O  
ANISOU 3796  OG1 THR A 224     4370   3123   5293   -396   -146   1533       O  
ATOM   3797  CG2 THR A 224      41.329  64.066  59.765  1.00 34.99           C  
ANISOU 3797  CG2 THR A 224     4444   3803   5048   -364   -344   1218       C  
ATOM   3798  H   THR A 224      40.147  64.184  57.035  1.00 34.65           H  
ATOM   3799  HA  THR A 224      41.895  65.985  58.021  1.00 36.12           H  
ATOM   3800  HB  THR A 224      43.119  64.135  58.817  1.00 39.38           H  
ATOM   3801  HG1 THR A 224      41.238  62.648  57.665  1.00 40.39           H  
ATOM   3802 HG21 THR A 224      41.636  63.413  60.413  1.00 42.00           H  
ATOM   3803 HG22 THR A 224      41.366  64.949  60.166  1.00 42.00           H  
ATOM   3804 HG23 THR A 224      40.410  63.867  59.528  1.00 42.00           H  
ATOM   3805  N   GLN A 225      42.311  64.729  55.204  1.00 29.45           N  
ANISOU 3805  N   GLN A 225     4268   2198   4725   -623   -527    780       N  
ATOM   3806  CA  GLN A 225      43.189  64.687  54.048  1.00 30.21           C  
ANISOU 3806  CA  GLN A 225     4496   2188   4796   -409   -487    636       C  
ATOM   3807  C   GLN A 225      43.661  66.092  53.687  1.00 26.10           C  
ANISOU 3807  C   GLN A 225     3852   1882   4182   -240   -593    398       C  
ATOM   3808  O   GLN A 225      42.997  67.092  53.976  1.00 24.35           O  
ANISOU 3808  O   GLN A 225     3608   1668   3974    -12   -635    172       O  
ATOM   3809  CB  GLN A 225      42.434  64.104  52.853  1.00 34.99           C  
ANISOU 3809  CB  GLN A 225     5344   2528   5421   -448   -310    615       C  
ATOM   3810  CG  GLN A 225      41.900  62.702  53.100  1.00 40.59           C  
ANISOU 3810  CG  GLN A 225     6184   3150   6088   -249    -59    722       C  
ATOM   3811  CD  GLN A 225      43.010  61.717  53.407  1.00 45.74           C  
ANISOU 3811  CD  GLN A 225     6896   3899   6584   -101    245    910       C  
ATOM   3812  OE1 GLN A 225      43.853  61.428  52.554  1.00 48.25           O  
ANISOU 3812  OE1 GLN A 225     7229   4219   6884   -111    401    792       O  
ATOM   3813  NE2 GLN A 225      43.029  61.207  54.635  1.00 47.14           N  
ANISOU 3813  NE2 GLN A 225     7107   4126   6679     92    275   1151       N  
ATOM   3814  H   GLN A 225      41.503  64.480  55.043  1.00 35.35           H  
ATOM   3815  HA  GLN A 225      43.961  64.135  54.247  1.00 36.26           H  
ATOM   3816  HB2 GLN A 225      41.679  64.679  52.650  1.00 41.99           H  
ATOM   3817  HB3 GLN A 225      43.034  64.065  52.093  1.00 41.99           H  
ATOM   3818  HG2 GLN A 225      41.293  62.720  53.856  1.00 48.71           H  
ATOM   3819  HG3 GLN A 225      41.433  62.395  52.307  1.00 48.71           H  
ATOM   3820 HE21 GLN A 225      42.430  61.440  55.207  1.00 56.58           H  
ATOM   3821 HE22 GLN A 225      43.640  60.644  54.857  1.00 56.58           H  
ATOM   3822  N   ASP A 226      44.827  66.167  53.050  1.00 24.43           N  
ANISOU 3822  N   ASP A 226     3504   1856   3924   -139   -552    257       N  
ATOM   3823  CA  ASP A 226      45.316  67.433  52.509  1.00 23.58           C  
ANISOU 3823  CA  ASP A 226     3325   1850   3782   -146   -457    183       C  
ATOM   3824  C   ASP A 226      45.448  68.483  53.609  1.00 22.59           C  
ANISOU 3824  C   ASP A 226     3147   1882   3554   -395   -670    325       C  
ATOM   3825  O   ASP A 226      45.108  69.648  53.420  1.00 21.14           O  
ANISOU 3825  O   ASP A 226     3030   1464   3537   -260   -577    311       O  
ATOM   3826  CB  ASP A 226      44.400  67.924  51.378  1.00 23.96           C  
ANISOU 3826  CB  ASP A 226     3427   1910   3767    -90   -433    135       C  
ATOM   3827  CG  ASP A 226      44.956  69.130  50.640  1.00 25.13           C  
ANISOU 3827  CG  ASP A 226     3572   2168   3808    -16   -249    218       C  
ATOM   3828  OD1 ASP A 226      46.186  69.313  50.641  1.00 27.01           O  
ANISOU 3828  OD1 ASP A 226     3647   2660   3954   -259    162    314       O  
ATOM   3829  OD2 ASP A 226      44.151  69.898  50.069  1.00 22.89           O  
ANISOU 3829  OD2 ASP A 226     3463   1657   3578    163   -315    317       O  
ATOM   3830  H   ASP A 226      45.352  65.499  52.920  1.00 29.33           H  
ATOM   3831  HA  ASP A 226      46.202  67.296  52.138  1.00 28.30           H  
ATOM   3832  HB2 ASP A 226      44.284  67.208  50.733  1.00 28.76           H  
ATOM   3833  HB3 ASP A 226      43.542  68.174  51.754  1.00 28.76           H  
ATOM   3834  N   ASN A 227      45.941  68.068  54.778  1.00 23.41           N  
ANISOU 3834  N   ASN A 227     3147   2138   3611   -255   -892    656       N  
ATOM   3835  CA  ASN A 227      46.071  68.973  55.924  1.00 25.24           C  
ANISOU 3835  CA  ASN A 227     3154   2677   3760   -497   -954    880       C  
ATOM   3836  C   ASN A 227      44.751  69.665  56.265  1.00 23.48           C  
ANISOU 3836  C   ASN A 227     3091   2287   3542   -474   -931    815       C  
ATOM   3837  O   ASN A 227      44.713  70.849  56.602  1.00 22.17           O  
ANISOU 3837  O   ASN A 227     3149   1992   3284   -689   -889    681       O  
ATOM   3838  CB  ASN A 227      47.181  70.002  55.701  1.00 28.24           C  
ANISOU 3838  CB  ASN A 227     3278   3436   4018   -323  -1147   1095       C  
ATOM   3839  CG  ASN A 227      48.545  69.391  55.823  1.00 33.39           C  
ANISOU 3839  CG  ASN A 227     3691   4520   4477    -33   -971   1025       C  
ATOM   3840  OD1 ASN A 227      48.938  68.952  56.901  1.00 36.20           O  
ANISOU 3840  OD1 ASN A 227     3970   5142   4642     65   -961    956       O  
ATOM   3841  ND2 ASN A 227      49.268  69.325  54.716  1.00 35.28           N  
ANISOU 3841  ND2 ASN A 227     3812   4876   4716     61   -866    962       N  
ATOM   3842  H   ASN A 227      46.208  67.265  54.932  1.00 28.10           H  
ATOM   3843  HA  ASN A 227      46.312  68.431  56.691  1.00 30.30           H  
ATOM   3844  HB2 ASN A 227      47.095  70.377  54.811  1.00 33.90           H  
ATOM   3845  HB3 ASN A 227      47.103  70.705  56.366  1.00 33.90           H  
ATOM   3846 HD21 ASN A 227      50.056  68.983  54.737  1.00 42.34           H  
ATOM   3847 HD22 ASN A 227      48.948  69.625  53.975  1.00 42.34           H  
ATOM   3848  N   GLY A 228      43.661  68.915  56.196  1.00 21.65           N  
ANISOU 3848  N   GLY A 228     2721   2156   3347   -525   -991    718       N  
ATOM   3849  CA  GLY A 228      42.363  69.508  56.433  1.00 21.21           C  
ANISOU 3849  CA  GLY A 228     2760   2132   3165   -315   -685    823       C  
ATOM   3850  C   GLY A 228      41.798  70.206  55.225  1.00 19.94           C  
ANISOU 3850  C   GLY A 228     2625   2106   2846   -134   -446    785       C  
ATOM   3851  O   GLY A 228      40.993  71.136  55.367  1.00 22.20           O  
ANISOU 3851  O   GLY A 228     3046   2440   2950    -77   -100    494       O  
ATOM   3852  H   GLY A 228      43.648  68.074  56.016  1.00 25.98           H  
ATOM   3853  HA2 GLY A 228      41.741  68.813  56.700  1.00 25.46           H  
ATOM   3854  HA3 GLY A 228      42.438  70.157  57.150  1.00 25.46           H  
ATOM   3855  N   GLY A 229      42.212  69.801  54.026  1.00 18.33           N  
ANISOU 3855  N   GLY A 229     2437   1982   2544   -126   -477    646       N  
ATOM   3856  CA  GLY A 229      41.643  70.336  52.806  1.00 17.43           C  
ANISOU 3856  CA  GLY A 229     2303   1941   2379   -186   -322    629       C  
ATOM   3857  C   GLY A 229      42.184  71.669  52.334  1.00 16.80           C  
ANISOU 3857  C   GLY A 229     1912   1940   2531   -390   -238    247       C  
ATOM   3858  O   GLY A 229      41.432  72.449  51.740  1.00 16.64           O  
ANISOU 3858  O   GLY A 229     1638   2191   2495   -258   -187    456       O  
ATOM   3859  H   GLY A 229      42.825  69.213  53.895  1.00 22.00           H  
ATOM   3860  HA2 GLY A 229      41.793  69.695  52.094  1.00 20.92           H  
ATOM   3861  HA3 GLY A 229      40.688  70.443  52.938  1.00 20.92           H  
ATOM   3862  N   VAL A 230      43.477  71.953  52.533  1.00 16.30           N  
ANISOU 3862  N   VAL A 230     1826   1801   2565   -279   -402     88       N  
ATOM   3863  CA  VAL A 230      43.959  73.304  52.260  1.00 15.67           C  
ANISOU 3863  CA  VAL A 230     1921   1741   2292   -282   -427    106       C  
ATOM   3864  C   VAL A 230      43.878  73.668  50.782  1.00 15.64           C  
ANISOU 3864  C   VAL A 230     2026   1635   2280    -27   -396    118       C  
ATOM   3865  O   VAL A 230      43.641  74.833  50.447  1.00 16.53           O  
ANISOU 3865  O   VAL A 230     2267   1728   2286     36   -449    141       O  
ATOM   3866  CB  VAL A 230      45.368  73.543  52.840  1.00 15.95           C  
ANISOU 3866  CB  VAL A 230     1998   1765   2297   -129   -459    207       C  
ATOM   3867  CG1 VAL A 230      45.358  73.326  54.340  1.00 16.50           C  
ANISOU 3867  CG1 VAL A 230     2329   1731   2209   -109   -641    407       C  
ATOM   3868  CG2 VAL A 230      46.414  72.641  52.160  1.00 16.68           C  
ANISOU 3868  CG2 VAL A 230     1890   1953   2495   -174   -336    243       C  
ATOM   3869  H   VAL A 230      44.073  71.401  52.816  1.00 19.57           H  
ATOM   3870  HA  VAL A 230      43.356  73.902  52.728  1.00 18.81           H  
ATOM   3871  HB  VAL A 230      45.625  74.461  52.665  1.00 19.15           H  
ATOM   3872 HG11 VAL A 230      46.238  73.528  54.694  1.00 19.81           H  
ATOM   3873 HG12 VAL A 230      44.698  73.913  54.739  1.00 19.81           H  
ATOM   3874 HG13 VAL A 230      45.132  72.400  54.524  1.00 19.81           H  
ATOM   3875 HG21 VAL A 230      47.269  72.759  52.603  1.00 20.03           H  
ATOM   3876 HG22 VAL A 230      46.129  71.717  52.232  1.00 20.03           H  
ATOM   3877 HG23 VAL A 230      46.488  72.892  51.226  1.00 20.03           H  
ATOM   3878  N   HIS A 231      44.078  72.707  49.870  1.00 15.47           N  
ANISOU 3878  N   HIS A 231     2086   1522   2269     56   -542     10       N  
ATOM   3879  CA  HIS A 231      43.946  73.009  48.445  1.00 15.81           C  
ANISOU 3879  CA  HIS A 231     2150   1637   2221     84   -532     48       C  
ATOM   3880  C   HIS A 231      42.513  72.873  47.934  1.00 16.75           C  
ANISOU 3880  C   HIS A 231     2055   2054   2254    -12   -764    351       C  
ATOM   3881  O   HIS A 231      42.249  73.159  46.759  1.00 19.90           O  
ANISOU 3881  O   HIS A 231     2192   2722   2645   -138   -794    592       O  
ATOM   3882  CB  HIS A 231      44.808  72.070  47.591  1.00 17.87           C  
ANISOU 3882  CB  HIS A 231     2293   2039   2456    192   -337   -307       C  
ATOM   3883  CG  HIS A 231      46.285  72.241  47.772  1.00 19.77           C  
ANISOU 3883  CG  HIS A 231     2516   2245   2750   -126   -536   -283       C  
ATOM   3884  ND1 HIS A 231      47.010  71.530  48.701  1.00 20.92           N  
ANISOU 3884  ND1 HIS A 231     2539   2059   3349     -6   -475   -302       N  
ATOM   3885  CD2 HIS A 231      47.172  73.045  47.144  1.00 21.69           C  
ANISOU 3885  CD2 HIS A 231     2560   2897   2784    -90   -461   -237       C  
ATOM   3886  CE1 HIS A 231      48.286  71.877  48.630  1.00 21.88           C  
ANISOU 3886  CE1 HIS A 231     2661   2360   3291     63   -255   -516       C  
ATOM   3887  NE2 HIS A 231      48.409  72.802  47.696  1.00 21.97           N  
ANISOU 3887  NE2 HIS A 231     2686   2770   2894    -99   -348   -417       N  
ATOM   3888  H   HIS A 231      44.285  71.892  50.051  1.00 18.57           H  
ATOM   3889  HA  HIS A 231      44.258  73.920  48.321  1.00 18.98           H  
ATOM   3890  HB2 HIS A 231      44.589  71.154  47.823  1.00 21.45           H  
ATOM   3891  HB3 HIS A 231      44.607  72.232  46.655  1.00 21.45           H  
ATOM   3892  HD1 HIS A 231      46.684  70.948  49.244  1.00 25.11           H  
ATOM   3893  HD2 HIS A 231      46.982  73.651  46.465  1.00 26.04           H  
ATOM   3894  HE1 HIS A 231      48.975  71.529  49.148  1.00 26.26           H  
ATOM   3895  N   ILE A 232      41.606  72.408  48.775  1.00 16.87           N  
ANISOU 3895  N   ILE A 232     1973   2156   2280   -216   -577    260       N  
ATOM   3896  CA  ILE A 232      40.193  72.219  48.454  1.00 15.70           C  
ANISOU 3896  CA  ILE A 232     1746   1857   2362   -146   -524    115       C  
ATOM   3897  C   ILE A 232      39.421  73.446  48.913  1.00 15.46           C  
ANISOU 3897  C   ILE A 232     1703   1944   2226   -242   -403    143       C  
ATOM   3898  O   ILE A 232      38.766  74.124  48.114  1.00 16.02           O  
ANISOU 3898  O   ILE A 232     1807   1969   2312   -152   -342     79       O  
ATOM   3899  CB  ILE A 232      39.681  70.946  49.152  1.00 17.50           C  
ANISOU 3899  CB  ILE A 232     1910   1868   2873   -111   -463    111       C  
ATOM   3900  CG1 ILE A 232      40.424  69.721  48.616  1.00 19.70           C  
ANISOU 3900  CG1 ILE A 232     2392   1809   3286   -289   -423     95       C  
ATOM   3901  CG2 ILE A 232      38.171  70.809  48.984  1.00 18.00           C  
ANISOU 3901  CG2 ILE A 232     1898   1863   3079    -63   -393    145       C  
ATOM   3902  CD1 ILE A 232      40.076  68.414  49.337  1.00 19.96           C  
ANISOU 3902  CD1 ILE A 232     2566   1532   3486     46   -550     63       C  
ATOM   3903  H   ILE A 232      41.789  72.179  49.584  1.00 20.25           H  
ATOM   3904  HA  ILE A 232      40.067  72.131  47.497  1.00 18.85           H  
ATOM   3905  HB  ILE A 232      39.863  71.015  50.103  1.00 21.01           H  
ATOM   3906 HG12 ILE A 232      40.201  69.608  47.679  1.00 23.65           H  
ATOM   3907 HG13 ILE A 232      41.377  69.867  48.716  1.00 23.65           H  
ATOM   3908 HG21 ILE A 232      37.895  69.937  49.309  1.00 21.61           H  
ATOM   3909 HG22 ILE A 232      37.732  71.506  49.496  1.00 21.61           H  
ATOM   3910 HG23 ILE A 232      37.949  70.898  48.045  1.00 21.61           H  
ATOM   3911 HD11 ILE A 232      40.742  67.745  49.116  1.00 23.96           H  
ATOM   3912 HD12 ILE A 232      40.072  68.573  50.294  1.00 23.96           H  
ATOM   3913 HD13 ILE A 232      39.199  68.117  49.047  1.00 23.96           H  
ATOM   3914  N   ASN A 233      39.511  73.751  50.204  1.00 15.74           N  
ANISOU 3914  N   ASN A 233     1909   1902   2170   -164   -483     96       N  
ATOM   3915  CA  ASN A 233      38.776  74.866  50.777  1.00 14.59           C  
ANISOU 3915  CA  ASN A 233     1745   1756   2041   -210   -302    254       C  
ATOM   3916  C   ASN A 233      39.310  76.208  50.318  1.00 14.29           C  
ANISOU 3916  C   ASN A 233     1754   1560   2114   -137   -301    141       C  
ATOM   3917  O   ASN A 233      38.625  77.221  50.481  1.00 14.70           O  
ANISOU 3917  O   ASN A 233     1740   1771   2076   -100   -222    269       O  
ATOM   3918  CB  ASN A 233      38.828  74.775  52.301  1.00 15.86           C  
ANISOU 3918  CB  ASN A 233     1939   2000   2088   -388   -119    402       C  
ATOM   3919  CG  ASN A 233      37.988  73.637  52.834  1.00 16.97           C  
ANISOU 3919  CG  ASN A 233     2014   2170   2264   -604   -233    524       C  
ATOM   3920  OD1 ASN A 233      36.997  73.246  52.212  1.00 18.13           O  
ANISOU 3920  OD1 ASN A 233     2125   2273   2490   -630   -182    346       O  
ATOM   3921  ND2 ASN A 233      38.386  73.093  53.982  1.00 18.43           N  
ANISOU 3921  ND2 ASN A 233     2430   2284   2290   -709   -333    804       N  
ATOM   3922  H   ASN A 233      39.994  73.323  50.772  1.00 18.90           H  
ATOM   3923  HA  ASN A 233      37.847  74.814  50.503  1.00 17.51           H  
ATOM   3924  HB2 ASN A 233      39.745  74.630  52.581  1.00 19.04           H  
ATOM   3925  HB3 ASN A 233      38.492  75.602  52.681  1.00 19.04           H  
ATOM   3926 HD21 ASN A 233      37.942  72.442  54.327  1.00 22.13           H  
ATOM   3927 HD22 ASN A 233      39.088  73.393  54.379  1.00 22.13           H  
ATOM   3928  N   SER A 234      40.506  76.242  49.727  1.00 13.55           N  
ANISOU 3928  N   SER A 234     1657   1387   2105     36   -345    103       N  
ATOM   3929  CA  SER A 234      40.962  77.469  49.088  1.00 12.87           C  
ANISOU 3929  CA  SER A 234     1587   1215   2088     60   -322    134       C  
ATOM   3930  C   SER A 234      39.966  77.958  48.043  1.00 12.46           C  
ANISOU 3930  C   SER A 234     1495   1243   1995    -35   -268     20       C  
ATOM   3931  O   SER A 234      39.919  79.156  47.750  1.00 12.71           O  
ANISOU 3931  O   SER A 234     1646   1239   1942    -92   -169    -86       O  
ATOM   3932  CB  SER A 234      42.324  77.241  48.437  1.00 15.19           C  
ANISOU 3932  CB  SER A 234     1702   1509   2561    -52   -111     20       C  
ATOM   3933  OG  SER A 234      42.226  76.178  47.501  1.00 16.10           O  
ANISOU 3933  OG  SER A 234     1705   1707   2705    106    -77    -95       O  
ATOM   3934  H   SER A 234      41.059  75.585  49.684  1.00 16.27           H  
ATOM   3935  HA  SER A 234      41.055  78.156  49.765  1.00 15.45           H  
ATOM   3936  HB2 SER A 234      42.601  78.049  47.978  1.00 18.24           H  
ATOM   3937  HB3 SER A 234      42.972  77.009  49.120  1.00 18.24           H  
ATOM   3938  HG  SER A 234      42.972  76.047  47.136  1.00 19.33           H  
ATOM   3939  N   GLY A 235      39.162  77.052  47.471  1.00 13.49           N  
ANISOU 3939  N   GLY A 235     1638   1434   2053    -52   -436    117       N  
ATOM   3940  CA  GLY A 235      38.177  77.461  46.479  1.00 13.45           C  
ANISOU 3940  CA  GLY A 235     1533   1519   2057    -62   -432     96       C  
ATOM   3941  C   GLY A 235      37.202  78.496  46.999  1.00 13.20           C  
ANISOU 3941  C   GLY A 235     1515   1556   1946    -15   -234    208       C  
ATOM   3942  O   GLY A 235      36.720  79.347  46.238  1.00 13.22           O  
ANISOU 3942  O   GLY A 235     1366   1713   1943    -91   -235    226       O  
ATOM   3943  H   GLY A 235      39.168  76.208  47.639  1.00 16.19           H  
ATOM   3944  HA2 GLY A 235      38.636  77.836  45.712  1.00 16.14           H  
ATOM   3945  HA3 GLY A 235      37.671  76.684  46.195  1.00 16.14           H  
ATOM   3946  N   ILE A 236      36.886  78.438  48.289  1.00 12.48           N  
ANISOU 3946  N   ILE A 236     1292   1598   1853   -106   -177    249       N  
ATOM   3947  CA  ILE A 236      35.926  79.374  48.852  1.00 13.87           C  
ANISOU 3947  CA  ILE A 236     1518   1718   2032    -57   -149    100       C  
ATOM   3948  C   ILE A 236      36.482  80.792  48.807  1.00 13.17           C  
ANISOU 3948  C   ILE A 236     1480   1634   1891     23   -161     86       C  
ATOM   3949  O   ILE A 236      35.780  81.743  48.431  1.00 13.88           O  
ANISOU 3949  O   ILE A 236     1574   1690   2008     -2     22    100       O  
ATOM   3950  CB  ILE A 236      35.567  78.930  50.279  1.00 14.87           C  
ANISOU 3950  CB  ILE A 236     1633   1899   2118   -113      2     83       C  
ATOM   3951  CG1 ILE A 236      34.863  77.559  50.247  1.00 15.85           C  
ANISOU 3951  CG1 ILE A 236     1986   1871   2167   -216     -6    -15       C  
ATOM   3952  CG2 ILE A 236      34.690  79.971  50.974  1.00 16.10           C  
ANISOU 3952  CG2 ILE A 236     1919   1992   2209     38     35    -39       C  
ATOM   3953  CD1 ILE A 236      34.926  76.797  51.548  1.00 16.05           C  
ANISOU 3953  CD1 ILE A 236     2058   1906   2136   -243    319   -322       C  
ATOM   3954  H   ILE A 236      37.208  77.874  48.853  1.00 14.99           H  
ATOM   3955  HA  ILE A 236      35.114  79.370  48.321  1.00 16.65           H  
ATOM   3956  HB  ILE A 236      36.390  78.846  50.785  1.00 17.85           H  
ATOM   3957 HG12 ILE A 236      33.927  77.696  50.032  1.00 19.03           H  
ATOM   3958 HG13 ILE A 236      35.283  77.011  49.566  1.00 19.03           H  
ATOM   3959 HG21 ILE A 236      34.304  79.577  51.772  1.00 19.33           H  
ATOM   3960 HG22 ILE A 236      35.236  80.736  51.213  1.00 19.33           H  
ATOM   3961 HG23 ILE A 236      33.984  80.245  50.367  1.00 19.33           H  
ATOM   3962 HD11 ILE A 236      34.467  75.950  51.440  1.00 19.27           H  
ATOM   3963 HD12 ILE A 236      35.855  76.643  51.779  1.00 19.27           H  
ATOM   3964 HD13 ILE A 236      34.495  77.321  52.242  1.00 19.27           H  
ATOM   3965  N   ILE A 237      37.752  80.952  49.184  1.00 12.35           N  
ANISOU 3965  N   ILE A 237     1352   1570   1769     79   -128     96       N  
ATOM   3966  CA  ILE A 237      38.394  82.260  49.162  1.00 12.39           C  
ANISOU 3966  CA  ILE A 237     1430   1503   1775     12   -178   -108       C  
ATOM   3967  C   ILE A 237      38.747  82.670  47.743  1.00 12.02           C  
ANISOU 3967  C   ILE A 237     1456   1339   1771     14   -164   -138       C  
ATOM   3968  O   ILE A 237      38.633  83.855  47.387  1.00 12.75           O  
ANISOU 3968  O   ILE A 237     1512   1441   1889      5   -183     96       O  
ATOM   3969  CB  ILE A 237      39.622  82.266  50.095  1.00 13.41           C  
ANISOU 3969  CB  ILE A 237     1489   1727   1879    -46    -65   -154       C  
ATOM   3970  CG1 ILE A 237      39.213  81.851  51.513  1.00 14.93           C  
ANISOU 3970  CG1 ILE A 237     1712   2122   1840    -96     10    -43       C  
ATOM   3971  CG2 ILE A 237      40.323  83.616  50.040  1.00 13.43           C  
ANISOU 3971  CG2 ILE A 237     1432   1667   2005   -106   -144   -142       C  
ATOM   3972  CD1 ILE A 237      38.090  82.632  52.111  1.00 15.97           C  
ANISOU 3972  CD1 ILE A 237     1967   2385   1717   -215    105    124       C  
ATOM   3973  H   ILE A 237      38.265  80.318  49.458  1.00 14.82           H  
ATOM   3974  HA  ILE A 237      37.765  82.916  49.501  1.00 14.88           H  
ATOM   3975  HB  ILE A 237      40.266  81.608  49.789  1.00 16.10           H  
ATOM   3976 HG12 ILE A 237      38.939  80.921  51.492  1.00 17.92           H  
ATOM   3977 HG13 ILE A 237      39.981  81.958  52.096  1.00 17.92           H  
ATOM   3978 HG21 ILE A 237      40.973  83.663  50.757  1.00 16.13           H  
ATOM   3979 HG22 ILE A 237      40.769  83.705  49.183  1.00 16.13           H  
ATOM   3980 HG23 ILE A 237      39.663  84.318  50.144  1.00 16.13           H  
ATOM   3981 HD11 ILE A 237      38.020  82.413  53.054  1.00 19.17           H  
ATOM   3982 HD12 ILE A 237      38.272  83.579  52.004  1.00 19.17           H  
ATOM   3983 HD13 ILE A 237      37.266  82.399  51.656  1.00 19.17           H  
ATOM   3984  N   ASN A 238      39.217  81.718  46.923  1.00 11.94           N  
ANISOU 3984  N   ASN A 238     1521   1392   1624    117   -201    -55       N  
ATOM   3985  CA  ASN A 238      39.520  82.031  45.531  1.00 11.79           C  
ANISOU 3985  CA  ASN A 238     1323   1498   1658    -49   -188      4       C  
ATOM   3986  C   ASN A 238      38.288  82.589  44.824  1.00 12.95           C  
ANISOU 3986  C   ASN A 238     1436   1675   1810     35   -285     72       C  
ATOM   3987  O   ASN A 238      38.388  83.555  44.060  1.00 12.15           O  
ANISOU 3987  O   ASN A 238     1396   1599   1621     43   -290    253       O  
ATOM   3988  CB  ASN A 238      40.022  80.790  44.790  1.00 11.49           C  
ANISOU 3988  CB  ASN A 238     1158   1453   1754     68   -230     64       C  
ATOM   3989  CG  ASN A 238      41.449  80.430  45.144  1.00 12.74           C  
ANISOU 3989  CG  ASN A 238     1367   1609   1865     14   -286   -106       C  
ATOM   3990  OD1 ASN A 238      42.185  81.226  45.755  1.00 13.25           O  
ANISOU 3990  OD1 ASN A 238     1464   1754   1818   -122   -208    -94       O  
ATOM   3991  ND2 ASN A 238      41.859  79.248  44.735  1.00 13.90           N  
ANISOU 3991  ND2 ASN A 238     1459   1792   2030    122   -377    -81       N  
ATOM   3992  H   ASN A 238      39.364  80.900  47.145  1.00 14.34           H  
ATOM   3993  HA  ASN A 238      40.227  82.695  45.515  1.00 14.16           H  
ATOM   3994  HB2 ASN A 238      39.457  80.035  45.020  1.00 13.79           H  
ATOM   3995  HB3 ASN A 238      39.982  80.954  43.835  1.00 13.79           H  
ATOM   3996 HD21 ASN A 238      42.661  78.989  44.906  1.00 16.68           H  
ATOM   3997 HD22 ASN A 238      41.326  78.736  44.296  1.00 16.68           H  
ATOM   3998  N   LYS A 239      37.116  82.004  45.082  1.00 12.63           N  
ANISOU 3998  N   LYS A 239     1251   1748   1800    -18   -153    -37       N  
ATOM   3999  CA  LYS A 239      35.892  82.493  44.462  1.00 12.30           C  
ANISOU 3999  CA  LYS A 239     1213   1737   1724   -118   -190     35       C  
ATOM   4000  C   LYS A 239      35.577  83.906  44.933  1.00 13.01           C  
ANISOU 4000  C   LYS A 239     1428   1755   1761    -89   -221    210       C  
ATOM   4001  O   LYS A 239      35.178  84.758  44.132  1.00 13.11           O  
ANISOU 4001  O   LYS A 239     1427   1808   1746     68     83    228       O  
ATOM   4002  CB  LYS A 239      34.734  81.553  44.801  1.00 13.51           C  
ANISOU 4002  CB  LYS A 239     1250   1878   2003   -132   -252     -1       C  
ATOM   4003  CG  LYS A 239      33.397  81.951  44.174  1.00 15.04           C  
ANISOU 4003  CG  LYS A 239     1413   2099   2203     -8   -488    -42       C  
ATOM   4004  CD  LYS A 239      33.355  81.738  42.679  1.00 15.96           C  
ANISOU 4004  CD  LYS A 239     1386   2425   2254    366   -566   -244       C  
ATOM   4005  CE  LYS A 239      32.142  82.415  42.094  1.00 17.03           C  
ANISOU 4005  CE  LYS A 239     1347   2868   2256    355   -693   -482       C  
ATOM   4006  NZ  LYS A 239      31.901  82.067  40.677  1.00 21.63           N  
ANISOU 4006  NZ  LYS A 239     1872   3735   2610    611   -764   -612       N  
ATOM   4007  H   LYS A 239      37.004  81.330  45.606  1.00 15.17           H  
ATOM   4008  HA  LYS A 239      36.004  82.507  43.499  1.00 14.77           H  
ATOM   4009  HB2 LYS A 239      34.955  80.663  44.484  1.00 16.22           H  
ATOM   4010  HB3 LYS A 239      34.616  81.542  45.764  1.00 16.22           H  
ATOM   4011  HG2 LYS A 239      32.691  81.416  44.571  1.00 18.06           H  
ATOM   4012  HG3 LYS A 239      33.236  82.892  44.345  1.00 18.06           H  
ATOM   4013  HD2 LYS A 239      34.150  82.118  42.273  1.00 19.16           H  
ATOM   4014  HD3 LYS A 239      33.306  80.789  42.486  1.00 19.16           H  
ATOM   4015  HE2 LYS A 239      31.359  82.150  42.602  1.00 20.45           H  
ATOM   4016  HE3 LYS A 239      32.262  83.376  42.147  1.00 20.45           H  
ATOM   4017  HZ1 LYS A 239      31.166  82.475  40.384  1.00 25.96           H  
ATOM   4018  HZ2 LYS A 239      32.592  82.323  40.179  1.00 25.96           H  
ATOM   4019  HZ3 LYS A 239      31.795  81.187  40.593  1.00 25.96           H  
ATOM   4020  N   ALA A 240      35.747  84.174  46.231  1.00 12.61           N  
ANISOU 4020  N   ALA A 240     1380   1647   1763    -17   -243    285       N  
ATOM   4021  CA  ALA A 240      35.536  85.522  46.743  1.00 13.04           C  
ANISOU 4021  CA  ALA A 240     1496   1598   1862     23   -249    119       C  
ATOM   4022  C   ALA A 240      36.452  86.519  46.046  1.00 11.33           C  
ANISOU 4022  C   ALA A 240     1439   1281   1584     86      5     67       C  
ATOM   4023  O   ALA A 240      36.028  87.609  45.674  1.00 12.61           O  
ANISOU 4023  O   ALA A 240     1637   1398   1757    157    -51     82       O  
ATOM   4024  CB  ALA A 240      35.752  85.570  48.252  1.00 13.22           C  
ANISOU 4024  CB  ALA A 240     1533   1623   1868   -218   -132     -7       C  
ATOM   4025  H   ALA A 240      35.981  83.600  46.827  1.00 15.14           H  
ATOM   4026  HA  ALA A 240      34.615  85.771  46.568  1.00 15.66           H  
ATOM   4027  HB1 ALA A 240      35.605  86.477  48.564  1.00 15.87           H  
ATOM   4028  HB2 ALA A 240      35.124  84.967  48.680  1.00 15.87           H  
ATOM   4029  HB3 ALA A 240      36.661  85.295  48.450  1.00 15.87           H  
ATOM   4030  N   ALA A 241      37.733  86.174  45.904  1.00 12.40           N  
ANISOU 4030  N   ALA A 241     1529   1416   1765    108   -222    216       N  
ATOM   4031  CA  ALA A 241      38.681  87.075  45.248  1.00 12.58           C  
ANISOU 4031  CA  ALA A 241     1419   1547   1815     45   -221    126       C  
ATOM   4032  C   ALA A 241      38.304  87.308  43.793  1.00 12.30           C  
ANISOU 4032  C   ALA A 241     1453   1408   1813    106   -221     90       C  
ATOM   4033  O   ALA A 241      38.348  88.450  43.306  1.00 12.86           O  
ANISOU 4033  O   ALA A 241     1587   1556   1745     97    -88    198       O  
ATOM   4034  CB  ALA A 241      40.099  86.496  45.347  1.00 13.51           C  
ANISOU 4034  CB  ALA A 241     1525   1752   1856    122   -297    312       C  
ATOM   4035  H   ALA A 241      38.077  85.434  46.174  1.00 14.88           H  
ATOM   4036  HA  ALA A 241      38.667  87.932  45.703  1.00 15.11           H  
ATOM   4037  HB1 ALA A 241      40.718  87.100  44.908  1.00 16.22           H  
ATOM   4038  HB2 ALA A 241      40.337  86.402  46.283  1.00 16.22           H  
ATOM   4039  HB3 ALA A 241      40.118  85.629  44.913  1.00 16.22           H  
ATOM   4040  N   TYR A 242      37.939  86.238  43.083  1.00 12.18           N  
ANISOU 4040  N   TYR A 242     1496   1385   1747     76   -238    237       N  
ATOM   4041  CA  TYR A 242      37.473  86.379  41.709  1.00 12.56           C  
ANISOU 4041  CA  TYR A 242     1482   1477   1814    107   -235    133       C  
ATOM   4042  C   TYR A 242      36.292  87.332  41.628  1.00 12.09           C  
ANISOU 4042  C   TYR A 242     1456   1535   1603    136   -143    152       C  
ATOM   4043  O   TYR A 242      36.252  88.204  40.748  1.00 13.11           O  
ANISOU 4043  O   TYR A 242     1667   1620   1696    246    -52    168       O  
ATOM   4044  CB  TYR A 242      37.088  85.003  41.164  1.00 13.12           C  
ANISOU 4044  CB  TYR A 242     1588   1666   1730    135   -211     50       C  
ATOM   4045  CG  TYR A 242      36.393  85.105  39.844  1.00 14.13           C  
ANISOU 4045  CG  TYR A 242     1751   1858   1761    196   -350   -162       C  
ATOM   4046  CD1 TYR A 242      37.116  85.266  38.675  1.00 15.94           C  
ANISOU 4046  CD1 TYR A 242     2239   1883   1936    352   -555   -376       C  
ATOM   4047  CD2 TYR A 242      35.012  85.091  39.770  1.00 15.95           C  
ANISOU 4047  CD2 TYR A 242     1897   2110   2052    260   -302   -159       C  
ATOM   4048  CE1 TYR A 242      36.494  85.377  37.479  1.00 18.48           C  
ANISOU 4048  CE1 TYR A 242     2708   2134   2180    300   -999   -256       C  
ATOM   4049  CE2 TYR A 242      34.371  85.211  38.570  1.00 18.79           C  
ANISOU 4049  CE2 TYR A 242     2416   2323   2400    426   -818   -441       C  
ATOM   4050  CZ  TYR A 242      35.110  85.357  37.425  1.00 20.45           C  
ANISOU 4050  CZ  TYR A 242     2918   2446   2405    418  -1323   -165       C  
ATOM   4051  OH  TYR A 242      34.436  85.464  36.231  1.00 25.36           O  
ANISOU 4051  OH  TYR A 242     3995   2892   2750    574  -1686    -29       O  
ATOM   4052  H   TYR A 242      37.951  85.428  43.371  1.00 14.62           H  
ATOM   4053  HA  TYR A 242      38.188  86.740  41.162  1.00 15.08           H  
ATOM   4054  HB2 TYR A 242      37.890  84.471  41.045  1.00 15.75           H  
ATOM   4055  HB3 TYR A 242      36.490  84.567  41.790  1.00 15.75           H  
ATOM   4056  HD1 TYR A 242      38.045  85.298  38.712  1.00 19.14           H  
ATOM   4057  HD2 TYR A 242      34.512  84.999  40.549  1.00 19.14           H  
ATOM   4058  HE1 TYR A 242      36.992  85.466  36.699  1.00 22.19           H  
ATOM   4059  HE2 TYR A 242      33.442  85.193  38.531  1.00 22.55           H  
ATOM   4060  HH  TYR A 242      33.607  85.440  36.366  1.00 30.44           H  
ATOM   4061  N   LEU A 243      35.337  87.203  42.550  1.00 12.80           N  
ANISOU 4061  N   LEU A 243     1486   1679   1698    131    -86    122       N  
ATOM   4062  CA  LEU A 243      34.166  88.074  42.527  1.00 13.39           C  
ANISOU 4062  CA  LEU A 243     1493   1701   1893    120   -152    402       C  
ATOM   4063  C   LEU A 243      34.536  89.519  42.825  1.00 13.12           C  
ANISOU 4063  C   LEU A 243     1505   1665   1814    123   -176    309       C  
ATOM   4064  O   LEU A 243      34.030  90.439  42.174  1.00 13.38           O  
ANISOU 4064  O   LEU A 243     1517   1694   1872    134    -67    351       O  
ATOM   4065  CB  LEU A 243      33.111  87.550  43.500  1.00 13.51           C  
ANISOU 4065  CB  LEU A 243     1439   1814   1880    255    -77    353       C  
ATOM   4066  CG  LEU A 243      32.374  86.278  43.059  1.00 13.99           C  
ANISOU 4066  CG  LEU A 243     1587   1896   1832    148   -177    264       C  
ATOM   4067  CD1 LEU A 243      31.610  85.693  44.254  1.00 14.18           C  
ANISOU 4067  CD1 LEU A 243     1536   1983   1870    209    -86    220       C  
ATOM   4068  CD2 LEU A 243      31.407  86.549  41.899  1.00 14.83           C  
ANISOU 4068  CD2 LEU A 243     1644   1972   2019    -22   -180    258       C  
ATOM   4069  H   LEU A 243      35.341  86.629  43.190  1.00 15.36           H  
ATOM   4070  HA  LEU A 243      33.777  88.060  41.638  1.00 16.08           H  
ATOM   4071  HB2 LEU A 243      33.547  87.353  44.344  1.00 16.22           H  
ATOM   4072  HB3 LEU A 243      32.443  88.242  43.626  1.00 16.22           H  
ATOM   4073  HG  LEU A 243      33.027  85.636  42.740  1.00 16.79           H  
ATOM   4074 HD11 LEU A 243      31.152  84.886  43.973  1.00 17.03           H  
ATOM   4075 HD12 LEU A 243      32.241  85.487  44.962  1.00 17.03           H  
ATOM   4076 HD13 LEU A 243      30.965  86.347  44.567  1.00 17.03           H  
ATOM   4077 HD21 LEU A 243      30.900  85.743  41.715  1.00 17.80           H  
ATOM   4078 HD22 LEU A 243      30.806  87.268  42.150  1.00 17.80           H  
ATOM   4079 HD23 LEU A 243      31.918  86.805  41.115  1.00 17.80           H  
ATOM   4080  N   ILE A 244      35.436  89.745  43.789  1.00 12.58           N  
ANISOU 4080  N   ILE A 244     1526   1596   1657    102    -87    241       N  
ATOM   4081  CA  ILE A 244      35.874  91.106  44.076  1.00 12.14           C  
ANISOU 4081  CA  ILE A 244     1632   1405   1575     93    -77    165       C  
ATOM   4082  C   ILE A 244      36.424  91.754  42.815  1.00 12.36           C  
ANISOU 4082  C   ILE A 244     1616   1451   1629    358     16     82       C  
ATOM   4083  O   ILE A 244      36.124  92.913  42.514  1.00 13.36           O  
ANISOU 4083  O   ILE A 244     1794   1555   1726    369    -46    130       O  
ATOM   4084  CB  ILE A 244      36.908  91.110  45.211  1.00 12.10           C  
ANISOU 4084  CB  ILE A 244     1722   1482   1393     17    -35    133       C  
ATOM   4085  CG1 ILE A 244      36.235  90.733  46.534  1.00 13.10           C  
ANISOU 4085  CG1 ILE A 244     1938   1511   1530     24      3    134       C  
ATOM   4086  CG2 ILE A 244      37.590  92.484  45.314  1.00 13.43           C  
ANISOU 4086  CG2 ILE A 244     1920   1566   1618     63    150    271       C  
ATOM   4087  CD1 ILE A 244      37.178  90.422  47.665  1.00 14.82           C  
ANISOU 4087  CD1 ILE A 244     2192   1665   1772    -30    -15    176       C  
ATOM   4088  H   ILE A 244      35.798  89.139  44.280  1.00 15.10           H  
ATOM   4089  HA  ILE A 244      35.108  91.621  44.373  1.00 14.57           H  
ATOM   4090  HB  ILE A 244      37.590  90.449  45.013  1.00 14.53           H  
ATOM   4091 HG12 ILE A 244      35.678  91.475  46.816  1.00 15.73           H  
ATOM   4092 HG13 ILE A 244      35.689  89.945  46.386  1.00 15.73           H  
ATOM   4093 HG21 ILE A 244      38.044  92.547  46.168  1.00 16.13           H  
ATOM   4094 HG22 ILE A 244      38.230  92.573  44.591  1.00 16.13           H  
ATOM   4095 HG23 ILE A 244      36.914  93.177  45.246  1.00 16.13           H  
ATOM   4096 HD11 ILE A 244      36.671  90.065  48.410  1.00 17.79           H  
ATOM   4097 HD12 ILE A 244      37.828  89.768  47.363  1.00 17.79           H  
ATOM   4098 HD13 ILE A 244      37.629  91.238  47.933  1.00 17.79           H  
ATOM   4099  N   SER A 245      37.250  91.020  42.064  1.00 12.31           N  
ANISOU 4099  N   SER A 245     1575   1516   1588    306     63    131       N  
ATOM   4100  CA  SER A 245      37.881  91.595  40.881  1.00 12.35           C  
ANISOU 4100  CA  SER A 245     1640   1550   1501    243     86    163       C  
ATOM   4101  C   SER A 245      36.890  91.728  39.734  1.00 12.61           C  
ANISOU 4101  C   SER A 245     1624   1588   1580    242   -132    225       C  
ATOM   4102  O   SER A 245      36.738  92.819  39.146  1.00 13.94           O  
ANISOU 4102  O   SER A 245     1930   1737   1629    222   -147    189       O  
ATOM   4103  CB  SER A 245      39.056  90.716  40.442  1.00 13.44           C  
ANISOU 4103  CB  SER A 245     1628   1910   1569    303    -17    196       C  
ATOM   4104  OG  SER A 245      39.689  91.275  39.312  1.00 14.47           O  
ANISOU 4104  OG  SER A 245     1670   2071   1758    253   -131    266       O  
ATOM   4105  H   SER A 245      37.459  90.200  42.216  1.00 14.79           H  
ATOM   4106  HA  SER A 245      38.212  92.478  41.109  1.00 14.82           H  
ATOM   4107  HB2 SER A 245      39.696  90.654  41.168  1.00 16.14           H  
ATOM   4108  HB3 SER A 245      38.725  89.832  40.216  1.00 16.14           H  
ATOM   4109  HG  SER A 245      39.175  91.244  38.649  1.00 17.38           H  
ATOM   4110  N   GLN A 246      36.230  90.620  39.368  1.00 12.40           N  
ANISOU 4110  N   GLN A 246     1671   1455   1586    120   -232    139       N  
ATOM   4111  CA  GLN A 246      35.475  90.551  38.122  1.00 13.89           C  
ANISOU 4111  CA  GLN A 246     1817   1749   1713    155   -308    119       C  
ATOM   4112  C   GLN A 246      33.976  90.764  38.283  1.00 14.99           C  
ANISOU 4112  C   GLN A 246     1851   1931   1912    161   -389    226       C  
ATOM   4113  O   GLN A 246      33.287  90.996  37.275  1.00 15.83           O  
ANISOU 4113  O   GLN A 246     1920   2070   2025     93   -568    404       O  
ATOM   4114  CB  GLN A 246      35.716  89.214  37.410  1.00 14.59           C  
ANISOU 4114  CB  GLN A 246     1844   1905   1796    296    -54    164       C  
ATOM   4115  CG  GLN A 246      37.176  88.944  37.082  1.00 15.00           C  
ANISOU 4115  CG  GLN A 246     1941   2019   1739    288   -140    298       C  
ATOM   4116  CD  GLN A 246      37.807  90.050  36.270  1.00 15.53           C  
ANISOU 4116  CD  GLN A 246     2058   2216   1626    338    -96    245       C  
ATOM   4117  OE1 GLN A 246      38.673  90.780  36.754  1.00 15.93           O  
ANISOU 4117  OE1 GLN A 246     2124   2246   1683    322   -228    235       O  
ATOM   4118  NE2 GLN A 246      37.377  90.177  35.029  1.00 16.97           N  
ANISOU 4118  NE2 GLN A 246     2386   2437   1625    240   -136    161       N  
ATOM   4119  H   GLN A 246      36.208  89.896  39.832  1.00 14.89           H  
ATOM   4120  HA  GLN A 246      35.807  91.260  37.548  1.00 16.68           H  
ATOM   4121  HB2 GLN A 246      35.404  88.496  37.983  1.00 17.52           H  
ATOM   4122  HB3 GLN A 246      35.220  89.212  36.576  1.00 17.52           H  
ATOM   4123  HG2 GLN A 246      37.675  88.857  37.909  1.00 18.01           H  
ATOM   4124  HG3 GLN A 246      37.238  88.123  36.569  1.00 18.01           H  
ATOM   4125 HE21 GLN A 246      36.772  89.647  34.727  1.00 20.37           H  
ATOM   4126 HE22 GLN A 246      37.703  90.791  34.522  1.00 20.37           H  
ATOM   4127  N   GLY A 247      33.462  90.701  39.506  1.00 14.38           N  
ANISOU 4127  N   GLY A 247     1588   1907   1970    213   -254    412       N  
ATOM   4128  CA  GLY A 247      32.039  90.832  39.736  1.00 14.92           C  
ANISOU 4128  CA  GLY A 247     1503   1992   2174    145   -389    -12       C  
ATOM   4129  C   GLY A 247      31.294  89.576  39.322  1.00 14.88           C  
ANISOU 4129  C   GLY A 247     1616   1856   2182    145   -374    -63       C  
ATOM   4130  O   GLY A 247      31.845  88.628  38.772  1.00 15.59           O  
ANISOU 4130  O   GLY A 247     1764   1888   2270    242   -188   -168       O  
ATOM   4131  H   GLY A 247      33.924  90.583  40.222  1.00 17.27           H  
ATOM   4132  HA2 GLY A 247      31.875  90.993  40.679  1.00 17.91           H  
ATOM   4133  HA3 GLY A 247      31.694  91.580  39.224  1.00 17.91           H  
ATOM   4134  N   GLY A 248      30.007  89.593  39.598  1.00 16.23           N  
ANISOU 4134  N   GLY A 248     1663   2079   2424   -130   -209   -134       N  
ATOM   4135  CA  GLY A 248      29.150  88.482  39.238  1.00 17.88           C  
ANISOU 4135  CA  GLY A 248     1826   2323   2646   -378   -232     15       C  
ATOM   4136  C   GLY A 248      28.054  88.309  40.272  1.00 18.78           C  
ANISOU 4136  C   GLY A 248     2110   2401   2623   -323   -269    -20       C  
ATOM   4137  O   GLY A 248      28.013  88.991  41.285  1.00 21.08           O  
ANISOU 4137  O   GLY A 248     2495   2531   2981   -668     37   -275       O  
ATOM   4138  H   GLY A 248      29.601  90.239  39.995  1.00 19.48           H  
ATOM   4139  HA2 GLY A 248      28.744  88.645  38.373  1.00 21.47           H  
ATOM   4140  HA3 GLY A 248      29.671  87.665  39.193  1.00 21.47           H  
ATOM   4141  N   THR A 249      27.164  87.366  39.983  1.00 18.21           N  
ANISOU 4141  N   THR A 249     2041   2400   2476   -131   -276    158       N  
ATOM   4142  CA  THR A 249      26.108  87.002  40.917  1.00 18.99           C  
ANISOU 4142  CA  THR A 249     2090   2528   2597   -276   -428    190       C  
ATOM   4143  C   THR A 249      26.300  85.543  41.262  1.00 18.66           C  
ANISOU 4143  C   THR A 249     2360   2227   2501   -280   -195    -33       C  
ATOM   4144  O   THR A 249      26.333  84.694  40.366  1.00 22.33           O  
ANISOU 4144  O   THR A 249     3534   2134   2816   -346   -328    -17       O  
ATOM   4145  CB  THR A 249      24.728  87.234  40.313  1.00 21.26           C  
ANISOU 4145  CB  THR A 249     1997   3009   3073   -278   -531    548       C  
ATOM   4146  OG1 THR A 249      24.613  88.617  39.952  1.00 23.81           O  
ANISOU 4146  OG1 THR A 249     2102   3351   3595     38   -631    903       O  
ATOM   4147  CG2 THR A 249      23.656  86.889  41.316  1.00 21.23           C  
ANISOU 4147  CG2 THR A 249     1985   3100   2981   -603   -461    389       C  
ATOM   4148  H   THR A 249      27.155  86.922  39.246  1.00 21.86           H  
ATOM   4149  HA  THR A 249      26.171  87.539  41.722  1.00 22.79           H  
ATOM   4150  HB  THR A 249      24.604  86.675  39.531  1.00 25.52           H  
ATOM   4151  HG1 THR A 249      23.844  88.773  39.651  1.00 28.58           H  
ATOM   4152 HG21 THR A 249      22.781  87.097  40.951  1.00 25.48           H  
ATOM   4153 HG22 THR A 249      23.691  85.943  41.527  1.00 25.48           H  
ATOM   4154 HG23 THR A 249      23.787  87.398  42.130  1.00 25.48           H  
ATOM   4155  N   HIS A 250      26.437  85.255  42.551  1.00 16.27           N  
ANISOU 4155  N   HIS A 250     1755   2098   2328   -134   -147    -46       N  
ATOM   4156  CA  HIS A 250      26.819  83.926  43.013  1.00 14.88           C  
ANISOU 4156  CA  HIS A 250     1503   1938   2213    -66   -217    -60       C  
ATOM   4157  C   HIS A 250      25.922  83.556  44.175  1.00 15.94           C  
ANISOU 4157  C   HIS A 250     1430   2286   2342    -28   -301     21       C  
ATOM   4158  O   HIS A 250      25.837  84.297  45.152  1.00 15.55           O  
ANISOU 4158  O   HIS A 250     1224   2372   2314    -14   -211    -26       O  
ATOM   4159  CB  HIS A 250      28.282  83.970  43.427  1.00 14.78           C  
ANISOU 4159  CB  HIS A 250     1398   1998   2218    135   -235    -84       C  
ATOM   4160  CG  HIS A 250      28.849  82.665  43.874  1.00 15.18           C  
ANISOU 4160  CG  HIS A 250     1351   2041   2377    166   -497   -247       C  
ATOM   4161  ND1 HIS A 250      28.799  81.524  43.101  1.00 16.06           N  
ANISOU 4161  ND1 HIS A 250     1546   2058   2499    101   -335   -139       N  
ATOM   4162  CD2 HIS A 250      29.522  82.330  45.002  1.00 15.59           C  
ANISOU 4162  CD2 HIS A 250     1417   2102   2405   -174   -391   -192       C  
ATOM   4163  CE1 HIS A 250      29.397  80.539  43.747  1.00 16.50           C  
ANISOU 4163  CE1 HIS A 250     1543   2143   2585    -56   -346   -281       C  
ATOM   4164  NE2 HIS A 250      29.861  81.006  44.895  1.00 16.33           N  
ANISOU 4164  NE2 HIS A 250     1475   2161   2569   -140   -215   -249       N  
ATOM   4165  H   HIS A 250      26.313  85.822  43.185  1.00 19.53           H  
ATOM   4166  HA  HIS A 250      26.694  83.249  42.330  1.00 17.87           H  
ATOM   4167  HB2 HIS A 250      28.807  84.270  42.668  1.00 17.74           H  
ATOM   4168  HB3 HIS A 250      28.375  84.596  44.162  1.00 17.74           H  
ATOM   4169  HD2 HIS A 250      29.718  82.893  45.715  1.00 18.72           H  
ATOM   4170  HE1 HIS A 250      29.479  79.663  43.445  1.00 19.81           H  
ATOM   4171  HE2 HIS A 250      30.303  80.553  45.477  1.00 19.60           H  
ATOM   4172  N   TYR A 251      25.232  82.424  44.054  1.00 17.23           N  
ANISOU 4172  N   TYR A 251     1726   2347   2476    -94   -364     66       N  
ATOM   4173  CA  TYR A 251      24.177  82.037  44.997  1.00 17.04           C  
ANISOU 4173  CA  TYR A 251     1779   2218   2476    -29   -206    245       C  
ATOM   4174  C   TYR A 251      23.230  83.197  45.305  1.00 17.36           C  
ANISOU 4174  C   TYR A 251     1650   2194   2754   -265   -145    269       C  
ATOM   4175  O   TYR A 251      22.817  83.404  46.446  1.00 19.10           O  
ANISOU 4175  O   TYR A 251     2008   2285   2963    -98   -144    -19       O  
ATOM   4176  CB  TYR A 251      24.754  81.442  46.281  1.00 16.60           C  
ANISOU 4176  CB  TYR A 251     1796   2113   2400   -145     -3    177       C  
ATOM   4177  CG  TYR A 251      25.447  80.103  46.115  1.00 16.40           C  
ANISOU 4177  CG  TYR A 251     1741   1988   2501   -328    -97     32       C  
ATOM   4178  CD1 TYR A 251      24.722  78.917  45.979  1.00 17.04           C  
ANISOU 4178  CD1 TYR A 251     1816   2172   2485   -350    -84    217       C  
ATOM   4179  CD2 TYR A 251      26.821  80.025  46.109  1.00 16.90           C  
ANISOU 4179  CD2 TYR A 251     1651   1924   2844   -308   -114    137       C  
ATOM   4180  CE1 TYR A 251      25.364  77.697  45.858  1.00 16.33           C  
ANISOU 4180  CE1 TYR A 251     1472   2179   2552   -394   -271    154       C  
ATOM   4181  CE2 TYR A 251      27.471  78.831  45.966  1.00 17.75           C  
ANISOU 4181  CE2 TYR A 251     1664   1936   3145   -160     -7     49       C  
ATOM   4182  CZ  TYR A 251      26.747  77.662  45.841  1.00 17.00           C  
ANISOU 4182  CZ  TYR A 251     1541   2013   2905   -194    -65    141       C  
ATOM   4183  OH  TYR A 251      27.377  76.439  45.727  1.00 18.34           O  
ANISOU 4183  OH  TYR A 251     1840   2137   2993     12     70    184       O  
ATOM   4184  H   TYR A 251      25.356  81.852  43.425  1.00 20.69           H  
ATOM   4185  HA  TYR A 251      23.649  81.347  44.566  1.00 20.45           H  
ATOM   4186  HB2 TYR A 251      25.406  82.063  46.641  1.00 19.93           H  
ATOM   4187  HB3 TYR A 251      24.030  81.317  46.914  1.00 19.93           H  
ATOM   4188  HD1 TYR A 251      23.793  78.947  45.971  1.00 20.45           H  
ATOM   4189  HD2 TYR A 251      27.320  80.804  46.204  1.00 20.28           H  
ATOM   4190  HE1 TYR A 251      24.872  76.911  45.788  1.00 19.60           H  
ATOM   4191  HE2 TYR A 251      28.401  78.806  45.953  1.00 21.31           H  
ATOM   4192  HH  TYR A 251      28.211  76.546  45.715  1.00 22.02           H  
ATOM   4193  N   GLY A 252      22.866  83.949  44.272  1.00 17.37           N  
ANISOU 4193  N   GLY A 252     1432   2218   2948    -95   -383    363       N  
ATOM   4194  CA  GLY A 252      21.902  85.021  44.407  1.00 18.31           C  
ANISOU 4194  CA  GLY A 252     1494   2245   3219    167   -348    366       C  
ATOM   4195  C   GLY A 252      22.446  86.322  44.954  1.00 19.52           C  
ANISOU 4195  C   GLY A 252     1623   2406   3386    218   -172    255       C  
ATOM   4196  O   GLY A 252      21.680  87.284  45.096  1.00 22.74           O  
ANISOU 4196  O   GLY A 252     1776   2842   4020    222   -314    195       O  
ATOM   4197  H   GLY A 252      23.171  83.853  43.473  1.00 20.85           H  
ATOM   4198  HA2 GLY A 252      21.523  85.206  43.534  1.00 21.98           H  
ATOM   4199  HA3 GLY A 252      21.195  84.725  45.002  1.00 21.98           H  
ATOM   4200  N   VAL A 253      23.734  86.397  45.257  1.00 17.55           N  
ANISOU 4200  N   VAL A 253     1524   2263   2882    128   -164    208       N  
ATOM   4201  CA  VAL A 253      24.341  87.592  45.822  1.00 17.60           C  
ANISOU 4201  CA  VAL A 253     1614   2354   2720     54     83    106       C  
ATOM   4202  C   VAL A 253      25.104  88.282  44.707  1.00 17.08           C  
ANISOU 4202  C   VAL A 253     1587   2248   2656    -42    -69     68       C  
ATOM   4203  O   VAL A 253      26.005  87.684  44.105  1.00 17.20           O  
ANISOU 4203  O   VAL A 253     1612   2270   2655    -42     96    -33       O  
ATOM   4204  CB  VAL A 253      25.289  87.244  46.982  1.00 18.95           C  
ANISOU 4204  CB  VAL A 253     1836   2537   2828    122    178     20       C  
ATOM   4205  CG1 VAL A 253      25.956  88.521  47.517  1.00 20.14           C  
ANISOU 4205  CG1 VAL A 253     2219   2505   2928    332    221   -185       C  
ATOM   4206  CG2 VAL A 253      24.535  86.526  48.083  1.00 19.75           C  
ANISOU 4206  CG2 VAL A 253     2024   2651   2829    259    245    197       C  
ATOM   4207  H   VAL A 253      24.289  85.750  45.140  1.00 21.07           H  
ATOM   4208  HA  VAL A 253      23.648  88.183  46.155  1.00 21.13           H  
ATOM   4209  HB  VAL A 253      25.985  86.649  46.660  1.00 22.75           H  
ATOM   4210 HG11 VAL A 253      26.387  88.322  48.363  1.00 24.18           H  
ATOM   4211 HG12 VAL A 253      26.615  88.827  46.874  1.00 24.18           H  
ATOM   4212 HG13 VAL A 253      25.277  89.202  47.645  1.00 24.18           H  
ATOM   4213 HG21 VAL A 253      25.140  86.361  48.823  1.00 23.71           H  
ATOM   4214 HG22 VAL A 253      23.798  87.084  48.376  1.00 23.71           H  
ATOM   4215 HG23 VAL A 253      24.197  85.685  47.738  1.00 23.71           H  
ATOM   4216  N   SER A 254      24.765  89.535  44.441  1.00 18.35           N  
ANISOU 4216  N   SER A 254     1629   2442   2900     69    -73    103       N  
ATOM   4217  CA ASER A 254      25.430  90.293  43.393  0.42 18.88           C  
ANISOU 4217  CA ASER A 254     1640   2543   2992    -21   -182    165       C  
ATOM   4218  CA BSER A 254      25.411  90.318  43.396  0.31 18.92           C  
ANISOU 4218  CA BSER A 254     1685   2578   2927    173    -61    201       C  
ATOM   4219  CA CSER A 254      25.416  90.309  43.394  0.27 18.94           C  
ANISOU 4219  CA CSER A 254     1687   2561   2950    132    -58     97       C  
ATOM   4220  C   SER A 254      26.661  90.989  43.947  1.00 18.37           C  
ANISOU 4220  C   SER A 254     1575   2585   2819     60    -32     -3       C  
ATOM   4221  O   SER A 254      26.634  91.566  45.040  1.00 20.91           O  
ANISOU 4221  O   SER A 254     1668   3043   3233   -140    199   -426       O  
ATOM   4222  CB ASER A 254      24.474  91.322  42.790  0.42 19.94           C  
ANISOU 4222  CB ASER A 254     1721   2672   3184   -348   -395    433       C  
ATOM   4223  CB BSER A 254      24.446  91.389  42.877  0.31 19.98           C  
ANISOU 4223  CB BSER A 254     1849   2733   3010    263    -32    537       C  
ATOM   4224  CB CSER A 254      24.451  91.367  42.859  0.27 20.05           C  
ANISOU 4224  CB CSER A 254     1846   2690   3082    146    -37    221       C  
ATOM   4225  OG ASER A 254      23.467  90.669  42.048  0.42 20.56           O  
ANISOU 4225  OG ASER A 254     1680   2857   3274   -520   -540    588       O  
ATOM   4226  OG BSER A 254      25.129  92.361  42.100  0.31 20.56           O  
ANISOU 4226  OG BSER A 254     1949   2864   2998    435     24    801       O  
ATOM   4227  OG CSER A 254      24.037  92.223  43.904  0.27 20.71           O  
ANISOU 4227  OG CSER A 254     1930   2809   3131    243     27    265       O  
ATOM   4228  H  ASER A 254      24.151  89.970  44.856  0.42 22.03           H  
ATOM   4229  H  BSER A 254      24.150  89.964  44.861  0.31 22.03           H  
ATOM   4230  H  CSER A 254      24.151  89.966  44.860  0.27 22.03           H  
ATOM   4231  HA ASER A 254      25.714  89.690  42.688  0.42 22.67           H  
ATOM   4232  HA BSER A 254      25.669  89.735  42.666  0.31 22.71           H  
ATOM   4233  HA CSER A 254      25.684  89.721  42.671  0.27 22.74           H  
ATOM   4234  HB2ASER A 254      24.063  91.832  43.505  0.42 23.94           H  
ATOM   4235  HB2BSER A 254      23.772  90.963  42.325  0.31 23.99           H  
ATOM   4236  HB2CSER A 254      24.899  91.891  42.176  0.27 24.06           H  
ATOM   4237  HB3ASER A 254      24.970  91.913  42.203  0.42 23.94           H  
ATOM   4238  HB3BSER A 254      24.027  91.828  43.634  0.31 23.99           H  
ATOM   4239  HB3CSER A 254      23.673  90.926  42.481  0.27 24.06           H  
ATOM   4240  HG ASER A 254      23.813  90.221  41.427  0.42 24.68           H  
ATOM   4241  HG BSER A 254      24.580  92.911  41.782  0.31 24.68           H  
ATOM   4242  HG CSER A 254      24.696  92.646  44.207  0.27 24.86           H  
ATOM   4243  N   VAL A 255      27.754  90.912  43.189  1.00 14.96           N  
ANISOU 4243  N   VAL A 255     1324   2096   2262    -15    -64    277       N  
ATOM   4244  CA  VAL A 255      29.013  91.545  43.556  1.00 14.46           C  
ANISOU 4244  CA  VAL A 255     1482   1924   2089    184    -58    292       C  
ATOM   4245  C   VAL A 255      29.417  92.475  42.421  1.00 14.75           C  
ANISOU 4245  C   VAL A 255     1589   1940   2077    204   -196    150       C  
ATOM   4246  O   VAL A 255      29.500  92.049  41.263  1.00 15.95           O  
ANISOU 4246  O   VAL A 255     1877   2120   2062    144   -138    176       O  
ATOM   4247  CB  VAL A 255      30.113  90.492  43.795  1.00 15.02           C  
ANISOU 4247  CB  VAL A 255     1638   1994   2076    405    -47    361       C  
ATOM   4248  CG1 VAL A 255      31.379  91.172  44.305  1.00 15.78           C  
ANISOU 4248  CG1 VAL A 255     1687   2040   2269    266   -126    117       C  
ATOM   4249  CG2 VAL A 255      29.650  89.397  44.756  1.00 16.01           C  
ANISOU 4249  CG2 VAL A 255     1816   2026   2241    242    -44    516       C  
ATOM   4250  H   VAL A 255      27.786  90.488  42.441  1.00 17.96           H  
ATOM   4251  HA  VAL A 255      28.893  92.068  44.365  1.00 17.36           H  
ATOM   4252  HB  VAL A 255      30.312  90.057  42.952  1.00 18.04           H  
ATOM   4253 HG11 VAL A 255      32.020  90.492  44.563  1.00 18.94           H  
ATOM   4254 HG12 VAL A 255      31.748  91.724  43.598  1.00 18.94           H  
ATOM   4255 HG13 VAL A 255      31.155  91.723  45.071  1.00 18.94           H  
ATOM   4256 HG21 VAL A 255      30.397  88.809  44.949  1.00 19.22           H  
ATOM   4257 HG22 VAL A 255      29.332  89.808  45.575  1.00 19.22           H  
ATOM   4258 HG23 VAL A 255      28.933  88.893  44.339  1.00 19.22           H  
ATOM   4259  N   VAL A 256      29.701  93.728  42.753  1.00 15.05           N  
ANISOU 4259  N   VAL A 256     1618   1957   2144    210     16    405       N  
ATOM   4260  CA  VAL A 256      30.195  94.700  41.787  1.00 14.80           C  
ANISOU 4260  CA  VAL A 256     1598   1899   2126    374    138    552       C  
ATOM   4261  C   VAL A 256      31.711  94.564  41.726  1.00 14.18           C  
ANISOU 4261  C   VAL A 256     1566   1918   1904    168    107    323       C  
ATOM   4262  O   VAL A 256      32.399  94.762  42.732  1.00 15.38           O  
ANISOU 4262  O   VAL A 256     1626   2248   1968    188     14    160       O  
ATOM   4263  CB  VAL A 256      29.790  96.122  42.192  1.00 15.37           C  
ANISOU 4263  CB  VAL A 256     1560   1923   2358    388    201    454       C  
ATOM   4264  CG1 VAL A 256      30.413  97.134  41.237  1.00 16.68           C  
ANISOU 4264  CG1 VAL A 256     1899   1856   2583    333    107    357       C  
ATOM   4265  CG2 VAL A 256      28.263  96.259  42.204  1.00 16.74           C  
ANISOU 4265  CG2 VAL A 256     1723   2045   2594    301    201    329       C  
ATOM   4266  H   VAL A 256      29.614  94.044  43.548  1.00 18.07           H  
ATOM   4267  HA  VAL A 256      29.828  94.512  40.909  1.00 17.77           H  
ATOM   4268  HB  VAL A 256      30.115  96.306  43.087  1.00 18.46           H  
ATOM   4269 HG11 VAL A 256      29.996  97.999  41.377  1.00 20.03           H  
ATOM   4270 HG12 VAL A 256      31.364  97.192  41.416  1.00 20.03           H  
ATOM   4271 HG13 VAL A 256      30.265  96.840  40.325  1.00 20.03           H  
ATOM   4272 HG21 VAL A 256      28.030  97.176  42.419  1.00 20.10           H  
ATOM   4273 HG22 VAL A 256      27.918  96.026  41.328  1.00 20.10           H  
ATOM   4274 HG23 VAL A 256      27.898  95.660  42.874  1.00 20.10           H  
ATOM   4275  N   GLY A 257      32.237  94.221  40.553  1.00 13.85           N  
ANISOU 4275  N   GLY A 257     1626   1844   1792    438     95     60       N  
ATOM   4276  CA  GLY A 257      33.670  94.009  40.433  1.00 13.57           C  
ANISOU 4276  CA  GLY A 257     1514   1670   1974    368    135    247       C  
ATOM   4277  C   GLY A 257      34.448  95.311  40.438  1.00 14.37           C  
ANISOU 4277  C   GLY A 257     1608   1662   2192    422    136    218       C  
ATOM   4278  O   GLY A 257      34.048  96.298  39.818  1.00 15.70           O  
ANISOU 4278  O   GLY A 257     1669   1956   2342    256    -31    355       O  
ATOM   4279  H   GLY A 257      31.794  94.108  39.825  1.00 16.63           H  
ATOM   4280  HA2 GLY A 257      33.979  93.466  41.176  1.00 16.30           H  
ATOM   4281  HA3 GLY A 257      33.858  93.544  39.603  1.00 16.30           H  
ATOM   4282  N   ILE A 258      35.604  95.288  41.111  1.00 13.66           N  
ANISOU 4282  N   ILE A 258     1660   1406   2124    438    311    305       N  
ATOM   4283  CA  ILE A 258      36.455  96.469  41.242  1.00 14.12           C  
ANISOU 4283  CA  ILE A 258     1785   1484   2094    213    337    323       C  
ATOM   4284  C   ILE A 258      37.785  96.334  40.515  1.00 14.59           C  
ANISOU 4284  C   ILE A 258     1722   1730   2090    210    113    513       C  
ATOM   4285  O   ILE A 258      38.573  97.292  40.499  1.00 14.62           O  
ANISOU 4285  O   ILE A 258     1578   1885   2091    177    295    354       O  
ATOM   4286  CB  ILE A 258      36.663  96.872  42.714  1.00 13.75           C  
ANISOU 4286  CB  ILE A 258     1890   1408   1927    197    399     91       C  
ATOM   4287  CG1 ILE A 258      37.469  95.807  43.454  1.00 14.36           C  
ANISOU 4287  CG1 ILE A 258     2054   1551   1853     96    255    169       C  
ATOM   4288  CG2 ILE A 258      35.301  97.157  43.382  1.00 15.69           C  
ANISOU 4288  CG2 ILE A 258     2049   1733   2178     92    321    -30       C  
ATOM   4289  CD1 ILE A 258      37.762  96.184  44.918  1.00 15.21           C  
ANISOU 4289  CD1 ILE A 258     2231   1624   1925     93    307     41       C  
ATOM   4290  H   ILE A 258      35.917  94.589  41.503  1.00 16.40           H  
ATOM   4291  HA  ILE A 258      35.990  97.206  40.816  1.00 16.95           H  
ATOM   4292  HB  ILE A 258      37.182  97.691  42.752  1.00 16.51           H  
ATOM   4293 HG12 ILE A 258      36.969  94.976  43.453  1.00 17.24           H  
ATOM   4294 HG13 ILE A 258      38.318  95.684  43.001  1.00 17.24           H  
ATOM   4295 HG21 ILE A 258      35.454  97.552  44.255  1.00 18.83           H  
ATOM   4296 HG22 ILE A 258      34.798  97.772  42.825  1.00 18.83           H  
ATOM   4297 HG23 ILE A 258      34.814  96.323  43.476  1.00 18.83           H  
ATOM   4298 HD11 ILE A 258      38.359  95.522  45.301  1.00 18.26           H  
ATOM   4299 HD12 ILE A 258      38.180  97.059  44.941  1.00 18.26           H  
ATOM   4300 HD13 ILE A 258      36.928  96.202  45.412  1.00 18.26           H  
ATOM   4301  N   GLY A 259      38.055  95.184  39.909  1.00 13.68           N  
ANISOU 4301  N   GLY A 259     1558   1669   1970    322     21    440       N  
ATOM   4302  CA  GLY A 259      39.250  94.994  39.122  1.00 12.73           C  
ANISOU 4302  CA  GLY A 259     1441   1706   1691    347     69    235       C  
ATOM   4303  C   GLY A 259      40.405  94.370  39.879  1.00 13.40           C  
ANISOU 4303  C   GLY A 259     1699   1611   1782    142    152    320       C  
ATOM   4304  O   GLY A 259      40.418  94.267  41.113  1.00 13.63           O  
ANISOU 4304  O   GLY A 259     1608   1844   1726    373    104    225       O  
ATOM   4305  H   GLY A 259      37.548  94.490  39.943  1.00 16.42           H  
ATOM   4306  HA2 GLY A 259      39.041  94.419  38.370  1.00 15.29           H  
ATOM   4307  HA3 GLY A 259      39.544  95.856  38.789  1.00 15.29           H  
ATOM   4308  N   ARG A 260      41.417  93.965  39.101  1.00 13.46           N  
ANISOU 4308  N   ARG A 260     1503   1809   1803    169     81    332       N  
ATOM   4309  CA  ARG A 260      42.515  93.154  39.615  1.00 12.27           C  
ANISOU 4309  CA  ARG A 260     1375   1518   1769    278    188    150       C  
ATOM   4310  C   ARG A 260      43.453  93.960  40.494  1.00 13.15           C  
ANISOU 4310  C   ARG A 260     1529   1624   1843    265    -50    265       C  
ATOM   4311  O   ARG A 260      43.955  93.451  41.510  1.00 13.92           O  
ANISOU 4311  O   ARG A 260     1778   1784   1727    238    -45    349       O  
ATOM   4312  CB  ARG A 260      43.288  92.513  38.457  1.00 13.78           C  
ANISOU 4312  CB  ARG A 260     1765   1633   1837    431    158     72       C  
ATOM   4313  CG  ARG A 260      42.497  91.526  37.633  1.00 15.68           C  
ANISOU 4313  CG  ARG A 260     2132   1774   2050    368    187     76       C  
ATOM   4314  CD  ARG A 260      43.339  90.901  36.505  1.00 16.77           C  
ANISOU 4314  CD  ARG A 260     2280   2011   2082    539     60     74       C  
ATOM   4315  NE  ARG A 260      43.899  91.945  35.652  1.00 16.35           N  
ANISOU 4315  NE  ARG A 260     2243   2005   1964    587    301    233       N  
ATOM   4316  CZ  ARG A 260      43.281  92.524  34.630  1.00 18.10           C  
ANISOU 4316  CZ  ARG A 260     2066   2472   2339    631     65     61       C  
ATOM   4317  NH1 ARG A 260      42.073  92.145  34.236  1.00 19.17           N  
ANISOU 4317  NH1 ARG A 260     2160   2497   2629    798   -281   -265       N  
ATOM   4318  NH2 ARG A 260      43.902  93.487  33.973  1.00 21.62           N  
ANISOU 4318  NH2 ARG A 260     2594   2845   2773    435   -188    504       N  
ATOM   4319  H   ARG A 260      41.491  94.150  38.264  1.00 16.16           H  
ATOM   4320  HA  ARG A 260      42.137  92.446  40.159  1.00 14.73           H  
ATOM   4321  HB2 ARG A 260      43.587  93.217  37.860  1.00 16.54           H  
ATOM   4322  HB3 ARG A 260      44.052  92.040  38.822  1.00 16.54           H  
ATOM   4323  HG2 ARG A 260      42.183  90.811  38.208  1.00 18.82           H  
ATOM   4324  HG3 ARG A 260      41.742  91.982  37.229  1.00 18.82           H  
ATOM   4325  HD2 ARG A 260      44.069  90.389  36.888  1.00 20.14           H  
ATOM   4326  HD3 ARG A 260      42.779  90.324  35.962  1.00 20.14           H  
ATOM   4327  HE  ARG A 260      44.698  92.209  35.827  1.00 19.63           H  
ATOM   4328 HH11 ARG A 260      41.668  91.507  34.646  1.00 23.02           H  
ATOM   4329 HH12 ARG A 260      41.695  92.537  33.571  1.00 23.02           H  
ATOM   4330 HH21 ARG A 260      44.693  93.728  34.211  1.00 25.95           H  
ATOM   4331 HH22 ARG A 260      43.516  93.873  33.309  1.00 25.95           H  
ATOM   4332  N   ASP A 261      43.743  95.204  40.115  1.00 13.66           N  
ANISOU 4332  N   ASP A 261     1668   1627   1895    168     23    155       N  
ATOM   4333  CA  ASP A 261      44.700  95.985  40.888  1.00 14.10           C  
ANISOU 4333  CA  ASP A 261     1718   1853   1786     -8    178    423       C  
ATOM   4334  C   ASP A 261      44.192  96.216  42.304  1.00 13.15           C  
ANISOU 4334  C   ASP A 261     1476   1799   1723     55    252    212       C  
ATOM   4335  O   ASP A 261      44.942  96.057  43.273  1.00 14.10           O  
ANISOU 4335  O   ASP A 261     1603   1875   1879    108    170    104       O  
ATOM   4336  CB  ASP A 261      44.978  97.318  40.206  1.00 14.92           C  
ANISOU 4336  CB  ASP A 261     1826   1878   1964     93    106    475       C  
ATOM   4337  CG  ASP A 261      46.083  98.088  40.884  1.00 18.96           C  
ANISOU 4337  CG  ASP A 261     2271   2235   2698     35    368    266       C  
ATOM   4338  OD1 ASP A 261      47.232  97.599  40.880  1.00 20.21           O  
ANISOU 4338  OD1 ASP A 261     2300   2406   2974    134    391    267       O  
ATOM   4339  OD2 ASP A 261      45.805  99.169  41.431  1.00 22.81           O  
ANISOU 4339  OD2 ASP A 261     2841   2600   3226   -169    305     24       O  
ATOM   4340  H   ASP A 261      43.410  95.608  39.433  1.00 16.40           H  
ATOM   4341  HA  ASP A 261      45.535  95.494  40.932  1.00 16.93           H  
ATOM   4342  HB2 ASP A 261      45.244  97.156  39.287  1.00 17.91           H  
ATOM   4343  HB3 ASP A 261      44.175  97.861  40.228  1.00 17.91           H  
ATOM   4344  N   LYS A 262      42.912  96.555  42.446  1.00 12.81           N  
ANISOU 4344  N   LYS A 262     1371   1728   1770     44    140    372       N  
ATOM   4345  CA  LYS A 262      42.377  96.791  43.780  1.00 12.78           C  
ANISOU 4345  CA  LYS A 262     1524   1610   1723     49     88    304       C  
ATOM   4346  C   LYS A 262      42.260  95.496  44.577  1.00 12.35           C  
ANISOU 4346  C   LYS A 262     1577   1487   1628      5    -54     64       C  
ATOM   4347  O   LYS A 262      42.508  95.486  45.789  1.00 13.06           O  
ANISOU 4347  O   LYS A 262     1838   1510   1616    238     -9     17       O  
ATOM   4348  CB  LYS A 262      41.050  97.530  43.694  1.00 13.85           C  
ANISOU 4348  CB  LYS A 262     1600   1754   1908     86    170    464       C  
ATOM   4349  CG  LYS A 262      41.231  98.955  43.165  1.00 15.11           C  
ANISOU 4349  CG  LYS A 262     1909   1651   2180    316    220    515       C  
ATOM   4350  CD  LYS A 262      39.911  99.660  42.960  1.00 17.30           C  
ANISOU 4350  CD  LYS A 262     2222   1832   2520    480    168    616       C  
ATOM   4351  CE  LYS A 262      40.131 101.101  42.509  1.00 19.23           C  
ANISOU 4351  CE  LYS A 262     2440   2061   2805    470    279    723       C  
ATOM   4352  NZ  LYS A 262      38.835 101.800  42.306  1.00 21.69           N  
ANISOU 4352  NZ  LYS A 262     3015   2157   3070    469      6    694       N  
ATOM   4353  H   LYS A 262      42.347  96.653  41.804  1.00 15.38           H  
ATOM   4354  HA  LYS A 262      42.990  97.365  44.266  1.00 15.35           H  
ATOM   4355  HB2 LYS A 262      40.457  97.054  43.092  1.00 16.63           H  
ATOM   4356  HB3 LYS A 262      40.654  97.581  44.578  1.00 16.63           H  
ATOM   4357  HG2 LYS A 262      41.752  99.468  43.802  1.00 18.14           H  
ATOM   4358  HG3 LYS A 262      41.691  98.921  42.311  1.00 18.14           H  
ATOM   4359  HD2 LYS A 262      39.400  99.198  42.278  1.00 20.77           H  
ATOM   4360  HD3 LYS A 262      39.417  99.671  43.795  1.00 20.77           H  
ATOM   4361  HE2 LYS A 262      40.634 101.579  43.187  1.00 23.08           H  
ATOM   4362  HE3 LYS A 262      40.617 101.106  41.669  1.00 23.08           H  
ATOM   4363  HZ1 LYS A 262      38.979 102.639  42.047  1.00 26.04           H  
ATOM   4364  HZ2 LYS A 262      38.359 101.382  41.681  1.00 26.04           H  
ATOM   4365  HZ3 LYS A 262      38.372 101.807  43.066  1.00 26.04           H  
ATOM   4366  N   LEU A 263      41.894  94.390  43.925  1.00 11.77           N  
ANISOU 4366  N   LEU A 263     1533   1332   1608     43    169    145       N  
ATOM   4367  CA  LEU A 263      41.930  93.102  44.615  1.00 12.54           C  
ANISOU 4367  CA  LEU A 263     1613   1466   1685     37    -48    209       C  
ATOM   4368  C   LEU A 263      43.314  92.867  45.215  1.00 12.25           C  
ANISOU 4368  C   LEU A 263     1500   1542   1614     21   -100    239       C  
ATOM   4369  O   LEU A 263      43.450  92.520  46.393  1.00 12.68           O  
ANISOU 4369  O   LEU A 263     1620   1571   1625     70    -30    298       O  
ATOM   4370  CB  LEU A 263      41.600  91.978  43.633  1.00 12.47           C  
ANISOU 4370  CB  LEU A 263     1686   1556   1497    208    -95    162       C  
ATOM   4371  CG  LEU A 263      41.832  90.555  44.159  1.00 12.43           C  
ANISOU 4371  CG  LEU A 263     1700   1526   1496    279    -60    217       C  
ATOM   4372  CD1 LEU A 263      40.839  90.193  45.270  1.00 13.10           C  
ANISOU 4372  CD1 LEU A 263     1772   1675   1532    -78     27     -5       C  
ATOM   4373  CD2 LEU A 263      41.819  89.501  43.061  1.00 12.93           C  
ANISOU 4373  CD2 LEU A 263     1812   1673   1426    190   -121    359       C  
ATOM   4374  H   LEU A 263      41.630  94.358  43.107  1.00 14.14           H  
ATOM   4375  HA  LEU A 263      41.266  93.099  45.322  1.00 15.05           H  
ATOM   4376  HB2 LEU A 263      40.663  92.049  43.392  1.00 14.97           H  
ATOM   4377  HB3 LEU A 263      42.155  92.090  42.844  1.00 14.97           H  
ATOM   4378  HG  LEU A 263      42.725  90.546  44.538  1.00 14.92           H  
ATOM   4379 HD11 LEU A 263      41.058  89.313  45.615  1.00 15.73           H  
ATOM   4380 HD12 LEU A 263      40.905  90.852  45.979  1.00 15.73           H  
ATOM   4381 HD13 LEU A 263      39.941  90.191  44.903  1.00 15.73           H  
ATOM   4382 HD21 LEU A 263      42.056  88.642  43.445  1.00 15.52           H  
ATOM   4383 HD22 LEU A 263      40.930  89.457  42.676  1.00 15.52           H  
ATOM   4384 HD23 LEU A 263      42.463  89.748  42.379  1.00 15.52           H  
ATOM   4385  N   GLY A 264      44.358  93.064  44.409  1.00 11.96           N  
ANISOU 4385  N   GLY A 264     1387   1559   1598     39     42    170       N  
ATOM   4386  CA  GLY A 264      45.702  92.821  44.892  1.00 12.94           C  
ANISOU 4386  CA  GLY A 264     1576   1610   1729     77     99    101       C  
ATOM   4387  C   GLY A 264      46.093  93.748  46.020  1.00 13.01           C  
ANISOU 4387  C   GLY A 264     1549   1600   1796    -30    -48     94       C  
ATOM   4388  O   GLY A 264      46.743  93.326  46.974  1.00 12.97           O  
ANISOU 4388  O   GLY A 264     1515   1741   1674     58   -142    115       O  
ATOM   4389  H   GLY A 264      44.313  93.333  43.594  1.00 14.36           H  
ATOM   4390  HA2 GLY A 264      45.766  91.908  45.212  1.00 15.53           H  
ATOM   4391  HA3 GLY A 264      46.331  92.945  44.164  1.00 15.53           H  
ATOM   4392  N   LYS A 265      45.690  95.022  45.944  1.00 13.28           N  
ANISOU 4392  N   LYS A 265     1667   1579   1799     11    -70     34       N  
ATOM   4393  CA ALYS A 265      46.044  95.960  47.003  0.55 13.75           C  
ANISOU 4393  CA ALYS A 265     1741   1637   1845    -48    -60     12       C  
ATOM   4394  CA BLYS A 265      46.047  95.956  47.005  0.45 13.96           C  
ANISOU 4394  CA BLYS A 265     1775   1656   1873     22     66    192       C  
ATOM   4395  C   LYS A 265      45.352  95.585  48.308  1.00 13.15           C  
ANISOU 4395  C   LYS A 265     1642   1602   1752     80     21     58       C  
ATOM   4396  O   LYS A 265      45.956  95.668  49.385  1.00 13.24           O  
ANISOU 4396  O   LYS A 265     1703   1551   1775    106   -116    149       O  
ATOM   4397  CB ALYS A 265      45.691  97.390  46.591  0.55 16.21           C  
ANISOU 4397  CB ALYS A 265     2024   1961   2175   -209   -211    -87       C  
ATOM   4398  CB BLYS A 265      45.708  97.389  46.597  0.45 16.55           C  
ANISOU 4398  CB BLYS A 265     2092   1976   2221    -13    158    413       C  
ATOM   4399  CG ALYS A 265      46.677  98.042  45.614  0.55 19.70           C  
ANISOU 4399  CG ALYS A 265     2535   2397   2551   -356   -370   -183       C  
ATOM   4400  CG BLYS A 265      46.485  97.879  45.382  0.45 19.87           C  
ANISOU 4400  CG BLYS A 265     2581   2412   2558    -34    254    601       C  
ATOM   4401  CD ALYS A 265      46.134  99.387  45.130  0.55 22.19           C  
ANISOU 4401  CD ALYS A 265     2876   2778   2778   -583   -532   -197       C  
ATOM   4402  CD BLYS A 265      47.986  97.746  45.593  0.45 21.93           C  
ANISOU 4402  CD BLYS A 265     2837   2717   2777    -45    385    826       C  
ATOM   4403  CE ALYS A 265      47.211 100.307  44.558  0.55 23.55           C  
ANISOU 4403  CE ALYS A 265     3153   2995   2800   -610   -395   -204       C  
ATOM   4404  CE BLYS A 265      48.773  98.150  44.350  0.45 23.69           C  
ANISOU 4404  CE BLYS A 265     3116   2958   2928   -108    689    917       C  
ATOM   4405  NZ ALYS A 265      47.355 100.223  43.087  0.55 23.03           N  
ANISOU 4405  NZ ALYS A 265     3195   2918   2639   -771   -514   -293       N  
ATOM   4406  NZ BLYS A 265      48.475  99.561  43.987  0.45 24.92           N  
ANISOU 4406  NZ BLYS A 265     3310   3139   3021    148    789   1002       N  
ATOM   4407  H  ALYS A 265      45.223  95.358  45.305  0.55 15.94           H  
ATOM   4408  H  BLYS A 265      45.223  95.359  45.306  0.45 15.94           H  
ATOM   4409  HA ALYS A 265      47.003  95.927  47.145  0.55 16.50           H  
ATOM   4410  HA BLYS A 265      47.005  95.916  47.148  0.45 16.76           H  
ATOM   4411  HB2ALYS A 265      44.820  97.381  46.164  0.55 19.46           H  
ATOM   4412  HB2BLYS A 265      44.763  97.437  46.383  0.45 19.87           H  
ATOM   4413  HB3ALYS A 265      45.663  97.941  47.389  0.55 19.46           H  
ATOM   4414  HB3BLYS A 265      45.911  97.981  47.338  0.45 19.87           H  
ATOM   4415  HG2ALYS A 265      47.526  98.193  46.059  0.55 23.64           H  
ATOM   4416  HG2BLYS A 265      46.238  97.352  44.607  0.45 23.85           H  
ATOM   4417  HG3ALYS A 265      46.804  97.465  44.845  0.55 23.64           H  
ATOM   4418  HG3BLYS A 265      46.281  98.815  45.226  0.45 23.85           H  
ATOM   4419  HD2ALYS A 265      45.478  99.229  44.433  0.55 26.64           H  
ATOM   4420  HD2BLYS A 265      48.258  98.321  46.325  0.45 26.32           H  
ATOM   4421  HD3ALYS A 265      45.719  99.846  45.878  0.55 26.64           H  
ATOM   4422  HD3BLYS A 265      48.199  96.823  45.800  0.45 26.32           H  
ATOM   4423  HE2ALYS A 265      46.988 101.224  44.780  0.55 28.27           H  
ATOM   4424  HE2BLYS A 265      49.723  98.069  44.526  0.45 28.44           H  
ATOM   4425  HE3ALYS A 265      48.065 100.068  44.951  0.55 28.27           H  
ATOM   4426  HE3BLYS A 265      48.523  97.579  43.607  0.45 28.44           H  
ATOM   4427  HZ1ALYS A 265      47.560  99.390  42.848  0.55 27.65           H  
ATOM   4428  HZ1BLYS A 265      48.978  99.809  43.296  0.45 29.91           H  
ATOM   4429  HZ2ALYS A 265      46.592 100.457  42.693  0.55 27.65           H  
ATOM   4430  HZ2BLYS A 265      47.617  99.643  43.764  0.45 29.91           H  
ATOM   4431  HZ3ALYS A 265      48.002 100.769  42.813  0.55 27.65           H  
ATOM   4432  HZ3BLYS A 265      48.647 100.096  44.677  0.45 29.91           H  
ATOM   4433  N   ILE A 266      44.085  95.196  48.224  1.00 12.78           N  
ANISOU 4433  N   ILE A 266     1573   1607   1677     50     51    -42       N  
ATOM   4434  CA  ILE A 266      43.328  94.848  49.419  1.00 12.77           C  
ANISOU 4434  CA  ILE A 266     1664   1789   1401    182     -9    120       C  
ATOM   4435  C   ILE A 266      43.906  93.602  50.074  1.00 12.34           C  
ANISOU 4435  C   ILE A 266     1786   1580   1323     -2     10     16       C  
ATOM   4436  O   ILE A 266      44.116  93.562  51.293  1.00 12.90           O  
ANISOU 4436  O   ILE A 266     1794   1785   1323    123      3    -52       O  
ATOM   4437  CB  ILE A 266      41.838  94.676  49.059  1.00 13.56           C  
ANISOU 4437  CB  ILE A 266     1762   1856   1534    259   -130    117       C  
ATOM   4438  CG1 ILE A 266      41.227  96.041  48.687  1.00 14.55           C  
ANISOU 4438  CG1 ILE A 266     1737   1977   1813    471   -147    133       C  
ATOM   4439  CG2 ILE A 266      41.073  93.983  50.178  1.00 14.18           C  
ANISOU 4439  CG2 ILE A 266     1960   2023   1404    161    -71    -96       C  
ATOM   4440  CD1 ILE A 266      39.931  95.929  47.950  1.00 16.15           C  
ANISOU 4440  CD1 ILE A 266     1938   2067   2130    666    -61    307       C  
ATOM   4441  H   ILE A 266      43.640  95.124  47.491  1.00 15.35           H  
ATOM   4442  HA  ILE A 266      43.401  95.570  50.063  1.00 15.34           H  
ATOM   4443  HB  ILE A 266      41.771  94.099  48.282  1.00 16.28           H  
ATOM   4444 HG12 ILE A 266      41.064  96.543  49.500  1.00 17.47           H  
ATOM   4445 HG13 ILE A 266      41.851  96.520  48.120  1.00 17.47           H  
ATOM   4446 HG21 ILE A 266      40.122  94.115  50.038  1.00 17.02           H  
ATOM   4447 HG22 ILE A 266      41.281  93.036  50.163  1.00 17.02           H  
ATOM   4448 HG23 ILE A 266      41.339  94.368  51.027  1.00 17.02           H  
ATOM   4449 HD11 ILE A 266      39.646  96.814  47.676  1.00 19.39           H  
ATOM   4450 HD12 ILE A 266      40.058  95.366  47.170  1.00 19.39           H  
ATOM   4451 HD13 ILE A 266      39.267  95.534  48.537  1.00 19.39           H  
ATOM   4452  N   PHE A 267      44.153  92.555  49.292  1.00 12.58           N  
ANISOU 4452  N   PHE A 267     1767   1615   1396    -53    -90    160       N  
ATOM   4453  CA  PHE A 267      44.669  91.327  49.881  1.00 11.76           C  
ANISOU 4453  CA  PHE A 267     1730   1385   1353   -131     76     98       C  
ATOM   4454  C   PHE A 267      46.116  91.456  50.324  1.00 11.84           C  
ANISOU 4454  C   PHE A 267     1687   1456   1356    -39      6    155       C  
ATOM   4455  O   PHE A 267      46.513  90.814  51.306  1.00 12.76           O  
ANISOU 4455  O   PHE A 267     1849   1577   1422    -37      3    211       O  
ATOM   4456  CB  PHE A 267      44.468  90.149  48.938  1.00 13.39           C  
ANISOU 4456  CB  PHE A 267     1993   1356   1737   -101     90    -41       C  
ATOM   4457  CG  PHE A 267      43.118  89.515  49.074  1.00 14.30           C  
ANISOU 4457  CG  PHE A 267     1969   1679   1786   -195     77    182       C  
ATOM   4458  CD1 PHE A 267      42.977  88.292  49.693  1.00 17.12           C  
ANISOU 4458  CD1 PHE A 267     2226   1973   2306   -482    190    200       C  
ATOM   4459  CD2 PHE A 267      41.987  90.164  48.635  1.00 17.65           C  
ANISOU 4459  CD2 PHE A 267     2298   2285   2121   -507   -344    394       C  
ATOM   4460  CE1 PHE A 267      41.728  87.716  49.841  1.00 18.68           C  
ANISOU 4460  CE1 PHE A 267     2465   2268   2364   -648   -155    270       C  
ATOM   4461  CE2 PHE A 267      40.736  89.574  48.787  1.00 18.75           C  
ANISOU 4461  CE2 PHE A 267     2361   2469   2295   -541   -420    652       C  
ATOM   4462  CZ  PHE A 267      40.620  88.354  49.384  1.00 19.02           C  
ANISOU 4462  CZ  PHE A 267     2489   2523   2214   -695   -372    424       C  
ATOM   4463  H   PHE A 267      44.034  92.528  48.440  1.00 15.10           H  
ATOM   4464  HA  PHE A 267      44.154  91.135  50.680  1.00 14.12           H  
ATOM   4465  HB2 PHE A 267      44.563  90.459  48.023  1.00 16.07           H  
ATOM   4466  HB3 PHE A 267      45.137  89.474  49.130  1.00 16.07           H  
ATOM   4467  HD1 PHE A 267      43.729  87.850  50.014  1.00 20.55           H  
ATOM   4468  HD2 PHE A 267      42.059  91.001  48.235  1.00 21.18           H  
ATOM   4469  HE1 PHE A 267      41.647  86.888  50.256  1.00 22.42           H  
ATOM   4470  HE2 PHE A 267      39.976  90.014  48.481  1.00 22.51           H  
ATOM   4471  HZ  PHE A 267      39.784  87.959  49.477  1.00 22.83           H  
ATOM   4472  N   TYR A 268      46.928  92.250  49.623  1.00 11.92           N  
ANISOU 4472  N   TYR A 268     1649   1406   1475    -91     94     60       N  
ATOM   4473  CA  TYR A 268      48.301  92.454  50.068  1.00 12.67           C  
ANISOU 4473  CA  TYR A 268     1678   1459   1676   -169    108     35       C  
ATOM   4474  C   TYR A 268      48.332  93.148  51.426  1.00 12.41           C  
ANISOU 4474  C   TYR A 268     1624   1487   1604    -55    130     66       C  
ATOM   4475  O   TYR A 268      49.080  92.758  52.330  1.00 13.33           O  
ANISOU 4475  O   TYR A 268     1527   1667   1870     22    -63    166       O  
ATOM   4476  CB  TYR A 268      49.117  93.212  49.016  1.00 12.32           C  
ANISOU 4476  CB  TYR A 268     1466   1331   1884    106    238   -107       C  
ATOM   4477  CG  TYR A 268      50.566  93.362  49.421  1.00 12.84           C  
ANISOU 4477  CG  TYR A 268     1389   1477   2013    -26    104    110       C  
ATOM   4478  CD1 TYR A 268      51.462  92.336  49.216  1.00 13.39           C  
ANISOU 4478  CD1 TYR A 268     1521   1524   2042   -106   -124    -25       C  
ATOM   4479  CD2 TYR A 268      51.027  94.512  50.045  1.00 13.47           C  
ANISOU 4479  CD2 TYR A 268     1479   1520   2121     91    133    205       C  
ATOM   4480  CE1 TYR A 268      52.773  92.441  49.608  1.00 13.97           C  
ANISOU 4480  CE1 TYR A 268     1628   1598   2081   -184    -82   -108       C  
ATOM   4481  CE2 TYR A 268      52.357  94.632  50.434  1.00 13.61           C  
ANISOU 4481  CE2 TYR A 268     1501   1575   2094    104    134     82       C  
ATOM   4482  CZ  TYR A 268      53.223  93.589  50.210  1.00 13.65           C  
ANISOU 4482  CZ  TYR A 268     1427   1638   2120   -100    -32   -331       C  
ATOM   4483  OH  TYR A 268      54.550  93.699  50.614  1.00 15.93           O  
ANISOU 4483  OH  TYR A 268     1476   2018   2560   -111   -197   -304       O  
ATOM   4484  H   TYR A 268      46.713  92.672  48.905  1.00 14.32           H  
ATOM   4485  HA  TYR A 268      48.728  91.588  50.167  1.00 15.21           H  
ATOM   4486  HB2 TYR A 268      49.086  92.726  48.177  1.00 14.79           H  
ATOM   4487  HB3 TYR A 268      48.741  94.099  48.900  1.00 14.79           H  
ATOM   4488  HD1 TYR A 268      51.171  91.555  48.804  1.00 16.07           H  
ATOM   4489  HD2 TYR A 268      50.438  95.214  50.206  1.00 16.18           H  
ATOM   4490  HE1 TYR A 268      53.359  91.732  49.465  1.00 16.77           H  
ATOM   4491  HE2 TYR A 268      52.657  95.412  50.842  1.00 16.33           H  
ATOM   4492  HH  TYR A 268      54.684  94.453  50.960  1.00 19.13           H  
ATOM   4493  N   ARG A 269      47.524  94.196  51.585  1.00 12.66           N  
ANISOU 4493  N   ARG A 269     1790   1528   1491     90    122     49       N  
ATOM   4494  CA  ARG A 269      47.436  94.867  52.878  1.00 13.04           C  
ANISOU 4494  CA  ARG A 269     1957   1432   1564     93     83   -138       C  
ATOM   4495  C   ARG A 269      46.897  93.929  53.951  1.00 13.60           C  
ANISOU 4495  C   ARG A 269     1901   1561   1704     -5     58   -194       C  
ATOM   4496  O   ARG A 269      47.428  93.874  55.063  1.00 14.35           O  
ANISOU 4496  O   ARG A 269     1927   1707   1818     46    -16   -128       O  
ATOM   4497  CB  ARG A 269      46.579  96.128  52.760  1.00 14.50           C  
ANISOU 4497  CB  ARG A 269     2086   1512   1909    156    105   -351       C  
ATOM   4498  CG  ARG A 269      46.550  96.926  54.034  1.00 15.77           C  
ANISOU 4498  CG  ARG A 269     2155   1705   2132    356    150   -302       C  
ATOM   4499  CD  ARG A 269      45.923  98.263  53.781  1.00 16.51           C  
ANISOU 4499  CD  ARG A 269     2143   1889   2242    133    385   -328       C  
ATOM   4500  NE  ARG A 269      45.977  99.123  54.942  1.00 19.32           N  
ANISOU 4500  NE  ARG A 269     2194   2427   2719    -68    316   -638       N  
ATOM   4501  CZ  ARG A 269      47.023  99.863  55.277  1.00 23.59           C  
ANISOU 4501  CZ  ARG A 269     2629   3219   3116   -462    559  -1233       C  
ATOM   4502  NH1 ARG A 269      48.127  99.834  54.541  1.00 25.91           N  
ANISOU 4502  NH1 ARG A 269     2723   3668   3452   -696    332  -1447       N  
ATOM   4503  NH2 ARG A 269      46.958 100.633  56.340  1.00 26.51           N  
ANISOU 4503  NH2 ARG A 269     3104   3544   3425   -553    400  -1474       N  
ATOM   4504  H   ARG A 269      47.025  94.535  50.972  1.00 15.20           H  
ATOM   4505  HA  ARG A 269      48.324  95.143  53.152  1.00 15.65           H  
ATOM   4506  HB2 ARG A 269      46.941  96.692  52.059  1.00 17.40           H  
ATOM   4507  HB3 ARG A 269      45.668  95.873  52.544  1.00 17.40           H  
ATOM   4508  HG2 ARG A 269      46.026  96.458  54.702  1.00 18.93           H  
ATOM   4509  HG3 ARG A 269      47.455  97.061  54.356  1.00 18.93           H  
ATOM   4510  HD2 ARG A 269      46.396  98.704  53.057  1.00 19.82           H  
ATOM   4511  HD3 ARG A 269      44.992  98.138  53.541  1.00 19.82           H  
ATOM   4512  HE  ARG A 269      45.283  99.157  55.449  1.00 23.19           H  
ATOM   4513 HH11 ARG A 269      48.165  99.332  53.844  1.00 31.09           H  
ATOM   4514 HH12 ARG A 269      48.804 100.316  54.763  1.00 31.09           H  
ATOM   4515 HH21 ARG A 269      46.240 100.654  56.813  1.00 31.82           H  
ATOM   4516 HH22 ARG A 269      47.634 101.116  56.563  1.00 31.82           H  
ATOM   4517  N   ALA A 270      45.878  93.136  53.624  1.00 12.63           N  
ANISOU 4517  N   ALA A 270     1748   1517   1534    -94     50   -102       N  
ATOM   4518  CA  ALA A 270      45.363  92.201  54.616  1.00 13.28           C  
ANISOU 4518  CA  ALA A 270     1888   1592   1564    156     25      4       C  
ATOM   4519  C   ALA A 270      46.466  91.266  55.080  1.00 13.03           C  
ANISOU 4519  C   ALA A 270     1908   1529   1513    119   -104     45       C  
ATOM   4520  O   ALA A 270      46.659  91.054  56.284  1.00 13.56           O  
ANISOU 4520  O   ALA A 270     2154   1525   1472    -56   -144     -2       O  
ATOM   4521  CB  ALA A 270      44.201  91.401  54.037  1.00 13.70           C  
ANISOU 4521  CB  ALA A 270     1931   1712   1564    126    108     61       C  
ATOM   4522  H   ALA A 270      45.481  93.120  52.861  1.00 15.16           H  
ATOM   4523  HA  ALA A 270      45.031  92.700  55.379  1.00 15.94           H  
ATOM   4524  HB1 ALA A 270      43.886  90.772  54.705  1.00 16.45           H  
ATOM   4525  HB2 ALA A 270      43.487  92.011  53.794  1.00 16.45           H  
ATOM   4526  HB3 ALA A 270      44.507  90.922  53.250  1.00 16.45           H  
ATOM   4527  N   LEU A 271      47.209  90.697  54.130  1.00 12.28           N  
ANISOU 4527  N   LEU A 271     1723   1500   1442     72   -136    126       N  
ATOM   4528  CA  LEU A 271      48.236  89.721  54.458  1.00 14.14           C  
ANISOU 4528  CA  LEU A 271     1948   1664   1760     52   -123    122       C  
ATOM   4529  C   LEU A 271      49.340  90.331  55.308  1.00 14.12           C  
ANISOU 4529  C   LEU A 271     1925   1722   1719    209    -54     27       C  
ATOM   4530  O   LEU A 271      49.790  89.717  56.281  1.00 15.20           O  
ANISOU 4530  O   LEU A 271     2126   1753   1897     32    -91    109       O  
ATOM   4531  CB  LEU A 271      48.829  89.169  53.157  1.00 13.62           C  
ANISOU 4531  CB  LEU A 271     1860   1659   1654     43   -177     33       C  
ATOM   4532  CG  LEU A 271      49.999  88.193  53.287  1.00 13.45           C  
ANISOU 4532  CG  LEU A 271     1811   1579   1722    -75    -90    106       C  
ATOM   4533  CD1 LEU A 271      49.531  86.899  53.939  1.00 14.32           C  
ANISOU 4533  CD1 LEU A 271     1923   1577   1943   -127    -69    134       C  
ATOM   4534  CD2 LEU A 271      50.618  87.920  51.928  1.00 14.00           C  
ANISOU 4534  CD2 LEU A 271     1753   1764   1801   -270    -57      8       C  
ATOM   4535  H   LEU A 271      47.136  90.859  53.288  1.00 14.74           H  
ATOM   4536  HA  LEU A 271      47.833  89.000  54.965  1.00 16.97           H  
ATOM   4537  HB2 LEU A 271      48.124  88.703  52.682  1.00 16.35           H  
ATOM   4538  HB3 LEU A 271      49.144  89.920  52.630  1.00 16.35           H  
ATOM   4539  HG  LEU A 271      50.685  88.586  53.849  1.00 16.15           H  
ATOM   4540 HD11 LEU A 271      50.298  86.326  54.090  1.00 17.20           H  
ATOM   4541 HD12 LEU A 271      49.103  87.109  54.784  1.00 17.20           H  
ATOM   4542 HD13 LEU A 271      48.900  86.459  53.350  1.00 17.20           H  
ATOM   4543 HD21 LEU A 271      51.320  87.258  52.028  1.00 16.80           H  
ATOM   4544 HD22 LEU A 271      49.932  87.587  51.329  1.00 16.80           H  
ATOM   4545 HD23 LEU A 271      50.990  88.745  51.579  1.00 16.80           H  
ATOM   4546  N   THR A 272      49.835  91.513  54.916  1.00 13.82           N  
ANISOU 4546  N   THR A 272     1735   1678   1839     27   -235     49       N  
ATOM   4547  CA  THR A 272      51.014  92.090  55.546  1.00 15.35           C  
ANISOU 4547  CA  THR A 272     1779   1991   2060   -109   -236    196       C  
ATOM   4548  C   THR A 272      50.709  92.845  56.830  1.00 15.57           C  
ANISOU 4548  C   THR A 272     1962   2005   1949   -427   -296    303       C  
ATOM   4549  O   THR A 272      51.610  92.991  57.676  1.00 16.54           O  
ANISOU 4549  O   THR A 272     2034   2284   1966   -393   -460    172       O  
ATOM   4550  CB  THR A 272      51.755  93.028  54.581  1.00 17.52           C  
ANISOU 4550  CB  THR A 272     1734   2633   2289   -174   -317    277       C  
ATOM   4551  OG1 THR A 272      50.893  94.089  54.144  1.00 18.44           O  
ANISOU 4551  OG1 THR A 272     1920   2582   2504   -354   -294    517       O  
ATOM   4552  CG2 THR A 272      52.295  92.245  53.393  1.00 19.38           C  
ANISOU 4552  CG2 THR A 272     1806   3220   2339   -104   -176    447       C  
ATOM   4553  H   THR A 272      49.503  91.996  54.287  1.00 16.59           H  
ATOM   4554  HA  THR A 272      51.607  91.355  55.764  1.00 18.42           H  
ATOM   4555  HB  THR A 272      52.508  93.431  55.039  1.00 21.03           H  
ATOM   4556  HG1 THR A 272      50.262  93.776  53.685  1.00 22.13           H  
ATOM   4557 HG21 THR A 272      52.915  92.794  52.888  1.00 23.27           H  
ATOM   4558 HG22 THR A 272      52.759  91.450  53.702  1.00 23.27           H  
ATOM   4559 HG23 THR A 272      51.566  91.977  52.812  1.00 23.27           H  
ATOM   4560  N   GLN A 273      49.481  93.331  57.006  1.00 15.53           N  
ANISOU 4560  N   GLN A 273     2182   1931   1788   -310   -273    153       N  
ATOM   4561  CA AGLN A 273      49.161  94.149  58.164  0.54 16.19           C  
ANISOU 4561  CA AGLN A 273     2481   1816   1855   -201   -389   -109       C  
ATOM   4562  CA BGLN A 273      49.144  94.159  58.154  0.46 16.58           C  
ANISOU 4562  CA BGLN A 273     2554   1904   1841   -329   -420     22       C  
ATOM   4563  C   GLN A 273      48.236  93.481  59.167  1.00 16.36           C  
ANISOU 4563  C   GLN A 273     2585   1866   1764   -273   -407   -200       C  
ATOM   4564  O   GLN A 273      48.368  93.752  60.366  1.00 18.18           O  
ANISOU 4564  O   GLN A 273     2848   2313   1748   -365   -398   -196       O  
ATOM   4565  CB AGLN A 273      48.544  95.487  57.723  0.54 17.64           C  
ANISOU 4565  CB AGLN A 273     2735   1864   2102     52   -359   -137       C  
ATOM   4566  CB BGLN A 273      48.458  95.455  57.692  0.46 18.52           C  
ANISOU 4566  CB BGLN A 273     2960   2049   2028   -365   -489    199       C  
ATOM   4567  CG AGLN A 273      48.271  96.452  58.861  0.54 20.37           C  
ANISOU 4567  CG AGLN A 273     3058   2189   2491    175   -387    105       C  
ATOM   4568  CG BGLN A 273      49.248  96.249  56.668  0.46 21.44           C  
ANISOU 4568  CG BGLN A 273     3463   2352   2331   -447   -464    542       C  
ATOM   4569  CD AGLN A 273      48.045  97.872  58.380  0.54 21.42           C  
ANISOU 4569  CD AGLN A 273     3018   2251   2871    -45   -560     90       C  
ATOM   4570  CD BGLN A 273      50.258  97.191  57.285  0.46 24.38           C  
ANISOU 4570  CD BGLN A 273     3893   2780   2592   -620   -510    823       C  
ATOM   4571  OE1AGLN A 273      48.475  98.247  57.287  0.54 21.41           O  
ANISOU 4571  OE1AGLN A 273     2928   2297   2908    -39   -796    342       O  
ATOM   4572  OE1BGLN A 273      50.629  97.056  58.454  0.46 26.59           O  
ANISOU 4572  OE1BGLN A 273     4200   3131   2772   -686   -681    762       O  
ATOM   4573  NE2AGLN A 273      47.375  98.675  59.202  0.54 21.41           N  
ANISOU 4573  NE2AGLN A 273     2790   2322   3022    -82   -591    -27       N  
ATOM   4574  NE2BGLN A 273      50.703  98.170  56.500  0.46 23.66           N  
ANISOU 4574  NE2BGLN A 273     3837   2442   2712   -856   -363    973       N  
ATOM   4575  H  AGLN A 273      48.824  93.199  56.467  0.54 18.65           H  
ATOM   4576  H  BGLN A 273      48.825  93.193  56.467  0.46 18.65           H  
ATOM   4577  HA AGLN A 273      49.988  94.346  58.632  0.54 19.44           H  
ATOM   4578  HA BGLN A 273      49.969  94.391  58.608  0.46 19.90           H  
ATOM   4579  HB2AGLN A 273      49.155  95.922  57.109  0.54 21.17           H  
ATOM   4580  HB2BGLN A 273      47.604  95.228  57.293  0.46 22.23           H  
ATOM   4581  HB3AGLN A 273      47.700  95.308  57.280  0.54 21.17           H  
ATOM   4582  HB3BGLN A 273      48.322  96.025  58.465  0.46 22.23           H  
ATOM   4583  HG2AGLN A 273      47.475  96.165  59.335  0.54 24.45           H  
ATOM   4584  HG2BGLN A 273      49.729  95.632  56.095  0.46 25.74           H  
ATOM   4585  HG3AGLN A 273      49.032  96.456  59.463  0.54 24.45           H  
ATOM   4586  HG3BGLN A 273      48.631  96.780  56.140  0.46 25.74           H  
ATOM   4587 HE21AGLN A 273      47.096  98.379  59.960  0.54 25.70           H  
ATOM   4588 HE21BGLN A 273      50.414  98.239  55.693  0.46 28.40           H  
ATOM   4589 HE22AGLN A 273      47.221  99.490  58.976  0.54 25.70           H  
ATOM   4590 HE22BGLN A 273      51.278  98.734  56.800  0.46 28.40           H  
ATOM   4591  N   TYR A 274      47.315  92.616  58.730  1.00 15.74           N  
ANISOU 4591  N   TYR A 274     2648   1701   1632   -326   -272    -82       N  
ATOM   4592  CA  TYR A 274      46.237  92.176  59.605  1.00 15.10           C  
ANISOU 4592  CA  TYR A 274     2544   1566   1628    -46   -126    141       C  
ATOM   4593  C   TYR A 274      46.172  90.679  59.879  1.00 15.29           C  
ANISOU 4593  C   TYR A 274     2590   1554   1664     -7     70    114       C  
ATOM   4594  O   TYR A 274      45.747  90.300  60.972  1.00 16.66           O  
ANISOU 4594  O   TYR A 274     2784   1807   1738    134     72    137       O  
ATOM   4595  CB  TYR A 274      44.881  92.662  59.060  1.00 15.43           C  
ANISOU 4595  CB  TYR A 274     2466   1638   1758   -137     30     35       C  
ATOM   4596  CG  TYR A 274      44.729  94.163  59.091  1.00 14.94           C  
ANISOU 4596  CG  TYR A 274     2307   1592   1778     39    -29     58       C  
ATOM   4597  CD1 TYR A 274      44.679  94.845  60.294  1.00 16.50           C  
ANISOU 4597  CD1 TYR A 274     2780   1627   1864     19    -23     84       C  
ATOM   4598  CD2 TYR A 274      44.638  94.898  57.927  1.00 15.80           C  
ANISOU 4598  CD2 TYR A 274     2622   1562   1818    107    140   -126       C  
ATOM   4599  CE1 TYR A 274      44.524  96.214  60.334  1.00 17.56           C  
ANISOU 4599  CE1 TYR A 274     3126   1609   1935    162   -218     85       C  
ATOM   4600  CE2 TYR A 274      44.491  96.284  57.954  1.00 16.64           C  
ANISOU 4600  CE2 TYR A 274     2895   1620   1807    117     68     11       C  
ATOM   4601  CZ  TYR A 274      44.451  96.931  59.165  1.00 17.37           C  
ANISOU 4601  CZ  TYR A 274     3020   1674   1906    125   -130    -71       C  
ATOM   4602  OH  TYR A 274      44.305  98.304  59.229  1.00 18.96           O  
ANISOU 4602  OH  TYR A 274     3158   1806   2238    -17   -259   -159       O  
ATOM   4603  H   TYR A 274      47.299  92.278  57.939  1.00 18.90           H  
ATOM   4604  HA  TYR A 274      46.379  92.588  60.471  1.00 18.13           H  
ATOM   4605  HB2 TYR A 274      44.791  92.372  58.138  1.00 18.52           H  
ATOM   4606  HB3 TYR A 274      44.171  92.279  59.599  1.00 18.52           H  
ATOM   4607  HD1 TYR A 274      44.752  94.371  61.090  1.00 19.81           H  
ATOM   4608  HD2 TYR A 274      44.676  94.460  57.108  1.00 18.96           H  
ATOM   4609  HE1 TYR A 274      44.469  96.652  61.152  1.00 21.07           H  
ATOM   4610  HE2 TYR A 274      44.421  96.765  57.161  1.00 19.98           H  
ATOM   4611  HH  TYR A 274      44.270  98.626  58.454  1.00 22.76           H  
ATOM   4612  N   LEU A 275      46.539  89.820  58.940  1.00 13.99           N  
ANISOU 4612  N   LEU A 275     2323   1444   1550   -120    -24     53       N  
ATOM   4613  CA  LEU A 275      46.423  88.395  59.195  1.00 13.89           C  
ANISOU 4613  CA  LEU A 275     2218   1559   1499   -152   -186     56       C  
ATOM   4614  C   LEU A 275      47.473  87.947  60.205  1.00 13.75           C  
ANISOU 4614  C   LEU A 275     2080   1553   1590   -148   -423      2       C  
ATOM   4615  O   LEU A 275      48.508  88.586  60.397  1.00 14.82           O  
ANISOU 4615  O   LEU A 275     2143   1761   1727   -214   -249    115       O  
ATOM   4616  CB  LEU A 275      46.562  87.599  57.901  1.00 13.34           C  
ANISOU 4616  CB  LEU A 275     2128   1705   1234   -290   -153     83       C  
ATOM   4617  CG  LEU A 275      45.442  87.814  56.873  1.00 13.76           C  
ANISOU 4617  CG  LEU A 275     2087   1765   1378   -268   -134     62       C  
ATOM   4618  CD1 LEU A 275      45.648  86.953  55.646  1.00 14.65           C  
ANISOU 4618  CD1 LEU A 275     2011   1818   1738   -390    -22    -46       C  
ATOM   4619  CD2 LEU A 275      44.052  87.567  57.441  1.00 15.69           C  
ANISOU 4619  CD2 LEU A 275     2342   2162   1458   -249     21     49       C  
ATOM   4620  H   LEU A 275      46.849  90.031  58.166  1.00 16.80           H  
ATOM   4621  HA  LEU A 275      45.547  88.207  59.565  1.00 16.67           H  
ATOM   4622  HB2 LEU A 275      47.398  87.851  57.476  1.00 16.01           H  
ATOM   4623  HB3 LEU A 275      46.574  86.655  58.123  1.00 16.01           H  
ATOM   4624  HG  LEU A 275      45.485  88.749  56.618  1.00 16.52           H  
ATOM   4625 HD11 LEU A 275      44.956  87.157  54.998  1.00 17.59           H  
ATOM   4626 HD12 LEU A 275      46.521  87.144  55.269  1.00 17.59           H  
ATOM   4627 HD13 LEU A 275      45.596  86.019  55.903  1.00 17.59           H  
ATOM   4628 HD21 LEU A 275      43.410  87.564  56.714  1.00 18.84           H  
ATOM   4629 HD22 LEU A 275      44.044  86.709  57.893  1.00 18.84           H  
ATOM   4630 HD23 LEU A 275      43.837  88.274  58.069  1.00 18.84           H  
ATOM   4631  N   THR A 276      47.159  86.837  60.890  1.00 14.71           N  
ANISOU 4631  N   THR A 276     2199   1724   1666   -330   -507    134       N  
ATOM   4632  CA  THR A 276      48.025  86.232  61.890  1.00 15.11           C  
ANISOU 4632  CA  THR A 276     2320   1752   1668   -399   -502    216       C  
ATOM   4633  C   THR A 276      48.151  84.744  61.563  1.00 16.27           C  
ANISOU 4633  C   THR A 276     2752   1682   1749   -259   -739     44       C  
ATOM   4634  O   THR A 276      47.480  84.253  60.636  1.00 17.25           O  
ANISOU 4634  O   THR A 276     3006   1854   1694   -330   -921    -97       O  
ATOM   4635  CB  THR A 276      47.420  86.362  63.287  1.00 15.54           C  
ANISOU 4635  CB  THR A 276     2275   1966   1664   -594   -435    276       C  
ATOM   4636  OG1 THR A 276      46.308  85.463  63.421  1.00 18.12           O  
ANISOU 4636  OG1 THR A 276     2744   2240   1900   -866   -286    342       O  
ATOM   4637  CG2 THR A 276      46.964  87.787  63.544  1.00 15.88           C  
ANISOU 4637  CG2 THR A 276     2081   2143   1808   -309   -351    190       C  
ATOM   4638  H   THR A 276      46.422  86.406  60.784  1.00 17.66           H  
ATOM   4639  HA  THR A 276      48.890  86.671  61.880  1.00 18.13           H  
ATOM   4640  HB  THR A 276      48.091  86.137  63.950  1.00 18.66           H  
ATOM   4641  HG1 THR A 276      46.585  84.676  63.514  1.00 21.75           H  
ATOM   4642 HG21 THR A 276      46.685  87.883  64.468  1.00 19.06           H  
ATOM   4643 HG22 THR A 276      47.691  88.404  63.369  1.00 19.06           H  
ATOM   4644 HG23 THR A 276      46.218  88.006  62.965  1.00 19.06           H  
ATOM   4645  N   PRO A 277      48.957  83.986  62.298  1.00 15.28           N  
ANISOU 4645  N   PRO A 277     2760   1444   1601   -201   -707   -195       N  
ATOM   4646  CA  PRO A 277      49.162  82.587  61.900  1.00 15.94           C  
ANISOU 4646  CA  PRO A 277     2837   1454   1766   -178   -752    -84       C  
ATOM   4647  C   PRO A 277      47.898  81.752  61.892  1.00 17.22           C  
ANISOU 4647  C   PRO A 277     3183   1610   1750   -365   -873     24       C  
ATOM   4648  O   PRO A 277      47.836  80.797  61.111  1.00 18.26           O  
ANISOU 4648  O   PRO A 277     3238   1895   1804   -352   -844    -40       O  
ATOM   4649  CB  PRO A 277      50.191  82.082  62.929  1.00 16.43           C  
ANISOU 4649  CB  PRO A 277     2863   1500   1879     94   -802    -80       C  
ATOM   4650  CG  PRO A 277      50.992  83.322  63.255  1.00 15.90           C  
ANISOU 4650  CG  PRO A 277     2783   1470   1788   -163   -622    -13       C  
ATOM   4651  CD  PRO A 277      49.936  84.412  63.320  1.00 15.62           C  
ANISOU 4651  CD  PRO A 277     2802   1559   1574   -227   -687   -116       C  
ATOM   4652  HA  PRO A 277      49.554  82.553  61.013  1.00 19.14           H  
ATOM   4653  HB2 PRO A 277      49.740  81.736  63.714  1.00 19.72           H  
ATOM   4654  HB3 PRO A 277      50.750  81.394  62.536  1.00 19.72           H  
ATOM   4655  HG2 PRO A 277      51.444  83.217  64.107  1.00 19.09           H  
ATOM   4656  HG3 PRO A 277      51.640  83.500  62.555  1.00 19.09           H  
ATOM   4657  HD2 PRO A 277      49.527  84.446  64.199  1.00 18.75           H  
ATOM   4658  HD3 PRO A 277      50.315  85.277  63.097  1.00 18.75           H  
ATOM   4659  N   THR A 278      46.897  82.069  62.727  1.00 18.73           N  
ANISOU 4659  N   THR A 278     3332   1867   1917   -327  -1009     48       N  
ATOM   4660  CA  THR A 278      45.697  81.252  62.843  1.00 20.38           C  
ANISOU 4660  CA  THR A 278     3564   2119   2062   -464   -578    394       C  
ATOM   4661  C   THR A 278      44.433  81.952  62.358  1.00 18.13           C  
ANISOU 4661  C   THR A 278     2912   2018   1961   -318   -169    267       C  
ATOM   4662  O   THR A 278      43.324  81.501  62.679  1.00 19.48           O  
ANISOU 4662  O   THR A 278     2996   2142   2264   -158    102    468       O  
ATOM   4663  CB  THR A 278      45.483  80.743  64.270  1.00 24.68           C  
ANISOU 4663  CB  THR A 278     4551   2563   2264   -934   -956    377       C  
ATOM   4664  OG1 THR A 278      45.249  81.859  65.144  1.00 29.46           O  
ANISOU 4664  OG1 THR A 278     5678   3287   2227   -751   -217    252       O  
ATOM   4665  CG2 THR A 278      46.704  79.932  64.728  1.00 26.00           C  
ANISOU 4665  CG2 THR A 278     4556   2716   2604  -1017  -1422    581       C  
ATOM   4666  H   THR A 278      46.899  82.761  63.237  1.00 22.48           H  
ATOM   4667  HA  THR A 278      45.847  80.481  62.273  1.00 24.47           H  
ATOM   4668  HB  THR A 278      44.711  80.157  64.311  1.00 29.63           H  
ATOM   4669  HG1 THR A 278      45.969  82.266  65.289  1.00 35.36           H  
ATOM   4670 HG21 THR A 278      46.540  79.551  65.605  1.00 31.20           H  
ATOM   4671 HG22 THR A 278      46.879  79.213  64.101  1.00 31.20           H  
ATOM   4672 HG23 THR A 278      47.485  80.505  64.775  1.00 31.20           H  
ATOM   4673  N   SER A 279      44.569  83.017  61.568  1.00 15.98           N  
ANISOU 4673  N   SER A 279     2452   1970   1650   -318    -53    314       N  
ATOM   4674  CA  SER A 279      43.389  83.669  61.007  1.00 15.63           C  
ANISOU 4674  CA  SER A 279     2183   2008   1746   -306    -73    288       C  
ATOM   4675  C   SER A 279      42.485  82.645  60.346  1.00 16.53           C  
ANISOU 4675  C   SER A 279     2132   2079   2069   -335     -3    320       C  
ATOM   4676  O   SER A 279      42.952  81.800  59.579  1.00 16.12           O  
ANISOU 4676  O   SER A 279     2072   2051   2002   -278   -168    -51       O  
ATOM   4677  CB  SER A 279      43.813  84.688  59.948  1.00 16.02           C  
ANISOU 4677  CB  SER A 279     2050   2206   1832   -210    -60    198       C  
ATOM   4678  OG  SER A 279      44.502  85.755  60.537  1.00 16.95           O  
ANISOU 4678  OG  SER A 279     2349   2077   2013   -287    167     47       O  
ATOM   4679  H   SER A 279      45.319  83.374  61.345  1.00 19.18           H  
ATOM   4680  HA  SER A 279      42.911  84.120  61.720  1.00 18.76           H  
ATOM   4681  HB2 SER A 279      44.393  84.253  59.305  1.00 19.24           H  
ATOM   4682  HB3 SER A 279      43.021  85.029  59.503  1.00 19.24           H  
ATOM   4683  HG  SER A 279      44.677  86.338  59.958  1.00 20.34           H  
ATOM   4684  N   ASN A 280      41.181  82.744  60.621  1.00 16.26           N  
ANISOU 4684  N   ASN A 280     1917   2063   2198   -202    -42    445       N  
ATOM   4685  CA  ASN A 280      40.176  81.922  59.963  1.00 15.55           C  
ANISOU 4685  CA  ASN A 280     1844   2028   2039   -317    153    288       C  
ATOM   4686  C   ASN A 280      39.481  82.734  58.865  1.00 15.13           C  
ANISOU 4686  C   ASN A 280     1783   2049   1916   -242    178    124       C  
ATOM   4687  O   ASN A 280      39.801  83.903  58.625  1.00 14.89           O  
ANISOU 4687  O   ASN A 280     1895   1798   1963   -207    206     46       O  
ATOM   4688  CB  ASN A 280      39.218  81.316  60.995  1.00 16.56           C  
ANISOU 4688  CB  ASN A 280     2095   2078   2122   -336    320    454       C  
ATOM   4689  CG  ASN A 280      38.392  82.351  61.721  1.00 18.21           C  
ANISOU 4689  CG  ASN A 280     2485   2387   2047   -294    422    590       C  
ATOM   4690  OD1 ASN A 280      38.135  83.429  61.213  1.00 18.35           O  
ANISOU 4690  OD1 ASN A 280     2529   2287   2158    -99    352    421       O  
ATOM   4691  ND2 ASN A 280      37.940  82.002  62.914  1.00 21.52           N  
ANISOU 4691  ND2 ASN A 280     3047   2936   2194   -138    631    906       N  
ATOM   4692  H   ASN A 280      40.854  83.292  61.197  1.00 19.52           H  
ATOM   4693  HA  ASN A 280      40.599  81.169  59.521  1.00 18.67           H  
ATOM   4694  HB2 ASN A 280      38.608  80.713  60.542  1.00 19.89           H  
ATOM   4695  HB3 ASN A 280      39.734  80.830  61.657  1.00 19.89           H  
ATOM   4696 HD21 ASN A 280      37.464  82.553  63.371  1.00 25.83           H  
ATOM   4697 HD22 ASN A 280      38.121  81.224  63.232  1.00 25.83           H  
ATOM   4698  N   PHE A 281      38.522  82.113  58.174  1.00 14.88           N  
ANISOU 4698  N   PHE A 281     1695   2054   1903   -124    124    203       N  
ATOM   4699  CA  PHE A 281      37.883  82.796  57.047  1.00 15.50           C  
ANISOU 4699  CA  PHE A 281     1791   2102   1996    -32    130     84       C  
ATOM   4700  C   PHE A 281      37.181  84.074  57.496  1.00 15.95           C  
ANISOU 4700  C   PHE A 281     1861   2089   2110   -204    226    130       C  
ATOM   4701  O   PHE A 281      37.237  85.097  56.810  1.00 15.47           O  
ANISOU 4701  O   PHE A 281     1832   1900   2148   -241    198    100       O  
ATOM   4702  CB  PHE A 281      36.873  81.876  56.371  1.00 15.16           C  
ANISOU 4702  CB  PHE A 281     1659   2050   2052     29     35    -78       C  
ATOM   4703  CG  PHE A 281      37.473  80.796  55.491  1.00 15.32           C  
ANISOU 4703  CG  PHE A 281     1771   1946   2103    -15     79   -113       C  
ATOM   4704  CD1 PHE A 281      38.823  80.571  55.402  1.00 16.04           C  
ANISOU 4704  CD1 PHE A 281     2013   2024   2060     66    156   -182       C  
ATOM   4705  CD2 PHE A 281      36.643  80.022  54.722  1.00 18.72           C  
ANISOU 4705  CD2 PHE A 281     2024   2466   2621    -46    146   -474       C  
ATOM   4706  CE1 PHE A 281      39.324  79.578  54.567  1.00 17.33           C  
ANISOU 4706  CE1 PHE A 281     2187   2219   2179    -51     89    -26       C  
ATOM   4707  CE2 PHE A 281      37.139  79.038  53.887  1.00 19.16           C  
ANISOU 4707  CE2 PHE A 281     2091   2555   2633     27    227   -530       C  
ATOM   4708  CZ  PHE A 281      38.472  78.812  53.825  1.00 17.58           C  
ANISOU 4708  CZ  PHE A 281     2024   2379   2275    281    402   -277       C  
ATOM   4709  H   PHE A 281      38.229  81.320  58.330  1.00 17.86           H  
ATOM   4710  HA  PHE A 281      38.573  83.025  56.405  1.00 18.61           H  
ATOM   4711  HB2 PHE A 281      36.352  81.433  57.060  1.00 18.20           H  
ATOM   4712  HB3 PHE A 281      36.292  82.416  55.812  1.00 18.20           H  
ATOM   4713  HD1 PHE A 281      39.410  81.088  55.905  1.00 19.26           H  
ATOM   4714  HD2 PHE A 281      35.725  80.163  54.763  1.00 22.47           H  
ATOM   4715  HE1 PHE A 281      40.241  79.436  54.513  1.00 20.80           H  
ATOM   4716  HE2 PHE A 281      36.557  78.531  53.367  1.00 22.99           H  
ATOM   4717  HZ  PHE A 281      38.807  78.137  53.280  1.00 21.10           H  
ATOM   4718  N   SER A 282      36.484  84.033  58.632  1.00 16.39           N  
ANISOU 4718  N   SER A 282     2087   2055   2086   -116    292    232       N  
ATOM   4719  CA ASER A 282      35.803  85.219  59.140  0.63 16.91           C  
ANISOU 4719  CA ASER A 282     2156   2212   2057     10    371    196       C  
ATOM   4720  CA BSER A 282      35.804  85.236  59.092  0.38 16.70           C  
ANISOU 4720  CA BSER A 282     2073   2162   2108   -152    426    214       C  
ATOM   4721  C   SER A 282      36.799  86.332  59.433  1.00 16.29           C  
ANISOU 4721  C   SER A 282     2094   2070   2023     81    391     61       C  
ATOM   4722  O   SER A 282      36.528  87.518  59.181  1.00 16.61           O  
ANISOU 4722  O   SER A 282     2147   2226   1938    124    374    225       O  
ATOM   4723  CB ASER A 282      35.028  84.841  60.403  0.63 18.32           C  
ANISOU 4723  CB ASER A 282     2433   2350   2178    127    439    -24       C  
ATOM   4724  CB BSER A 282      34.882  84.911  60.264  0.38 17.54           C  
ANISOU 4724  CB BSER A 282     2111   2271   2282   -350    612    167       C  
ATOM   4725  OG ASER A 282      34.316  85.942  60.916  0.63 19.81           O  
ANISOU 4725  OG ASER A 282     2829   2444   2254    333    318    -70       O  
ATOM   4726  OG BSER A 282      33.648  84.418  59.771  0.38 18.48           O  
ANISOU 4726  OG BSER A 282     2215   2388   2417   -447    654    189       O  
ATOM   4727  H  ASER A 282      36.389  83.335  59.126  0.63 19.68           H  
ATOM   4728  H  BSER A 282      36.392  83.344  59.139  0.38 19.68           H  
ATOM   4729  HA ASER A 282      35.176  85.549  58.477  0.63 20.30           H  
ATOM   4730  HA BSER A 282      35.235  85.576  58.384  0.38 20.04           H  
ATOM   4731  HB2ASER A 282      34.399  84.134  60.186  0.63 21.99           H  
ATOM   4732  HB2BSER A 282      35.298  84.236  60.822  0.38 21.05           H  
ATOM   4733  HB3ASER A 282      35.655  84.531  61.076  0.63 21.99           H  
ATOM   4734  HB3BSER A 282      34.723  85.717  60.780  0.38 21.05           H  
ATOM   4735  HG ASER A 282      33.773  86.226  60.342  0.63 23.78           H  
ATOM   4736  HG BSER A 282      33.056  85.011  59.831  0.38 22.18           H  
ATOM   4737  N   GLN A 283      37.962  85.968  59.970  1.00 15.97           N  
ANISOU 4737  N   GLN A 283     2265   1963   1841    -27    302     50       N  
ATOM   4738  CA  GLN A 283      38.984  86.971  60.248  1.00 15.79           C  
ANISOU 4738  CA  GLN A 283     2238   1961   1798    -22    343     87       C  
ATOM   4739  C   GLN A 283      39.611  87.500  58.967  1.00 15.70           C  
ANISOU 4739  C   GLN A 283     2241   1762   1962   -101     58     85       C  
ATOM   4740  O   GLN A 283      40.011  88.671  58.914  1.00 16.47           O  
ANISOU 4740  O   GLN A 283     2512   1657   2089    -22    -24    -66       O  
ATOM   4741  CB  GLN A 283      40.021  86.383  61.199  1.00 16.60           C  
ANISOU 4741  CB  GLN A 283     2521   2155   1631    156    353    163       C  
ATOM   4742  CG  GLN A 283      39.413  86.144  62.569  1.00 18.54           C  
ANISOU 4742  CG  GLN A 283     2852   2552   1641    340    345     83       C  
ATOM   4743  CD  GLN A 283      40.272  85.311  63.468  1.00 21.63           C  
ANISOU 4743  CD  GLN A 283     3196   3224   1798    394    352     21       C  
ATOM   4744  OE1 GLN A 283      40.895  84.346  63.038  1.00 21.79           O  
ANISOU 4744  OE1 GLN A 283     3066   3139   2075    321    352    199       O  
ATOM   4745  NE2 GLN A 283      40.309  85.682  64.751  1.00 25.00           N  
ANISOU 4745  NE2 GLN A 283     3646   3878   1974    692    208    -37       N  
ATOM   4746  H   GLN A 283      38.182  85.164  60.179  1.00 19.17           H  
ATOM   4747  HA  GLN A 283      38.587  87.736  60.695  1.00 18.95           H  
ATOM   4748  HB2 GLN A 283      40.338  85.536  60.849  1.00 19.93           H  
ATOM   4749  HB3 GLN A 283      40.763  87.001  61.293  1.00 19.93           H  
ATOM   4750  HG2 GLN A 283      39.271  87.000  63.002  1.00 22.26           H  
ATOM   4751  HG3 GLN A 283      38.566  85.684  62.459  1.00 22.26           H  
ATOM   4752 HE21 GLN A 283      39.856  86.363  65.014  1.00 30.01           H  
ATOM   4753 HE22 GLN A 283      40.787  85.240  65.313  1.00 30.01           H  
ATOM   4754  N   LEU A 284      39.699  86.674  57.929  1.00 14.29           N  
ANISOU 4754  N   LEU A 284     1875   1639   1916     52    127     80       N  
ATOM   4755  CA  LEU A 284      40.147  87.178  56.636  1.00 14.49           C  
ANISOU 4755  CA  LEU A 284     1848   1900   1758     41    163     -5       C  
ATOM   4756  C   LEU A 284      39.159  88.193  56.090  1.00 13.67           C  
ANISOU 4756  C   LEU A 284     1665   1860   1670   -130    145    141       C  
ATOM   4757  O   LEU A 284      39.562  89.232  55.549  1.00 14.72           O  
ANISOU 4757  O   LEU A 284     1854   1938   1799   -144    206    236       O  
ATOM   4758  CB  LEU A 284      40.337  86.041  55.642  1.00 13.75           C  
ANISOU 4758  CB  LEU A 284     1679   2028   1519    -10    214     14       C  
ATOM   4759  CG  LEU A 284      40.638  86.478  54.201  1.00 13.60           C  
ANISOU 4759  CG  LEU A 284     1672   1967   1527     31    236    -17       C  
ATOM   4760  CD1 LEU A 284      41.934  87.262  54.070  1.00 15.71           C  
ANISOU 4760  CD1 LEU A 284     1836   2367   1767   -228    198     23       C  
ATOM   4761  CD2 LEU A 284      40.640  85.278  53.272  1.00 14.64           C  
ANISOU 4761  CD2 LEU A 284     2044   1851   1667   -236    252   -121       C  
ATOM   4762  H   LEU A 284      39.510  85.836  57.943  1.00 17.16           H  
ATOM   4763  HA  LEU A 284      41.010  87.606  56.754  1.00 17.40           H  
ATOM   4764  HB2 LEU A 284      41.080  85.494  55.942  1.00 16.51           H  
ATOM   4765  HB3 LEU A 284      39.523  85.513  55.622  1.00 16.51           H  
ATOM   4766  HG  LEU A 284      39.931  87.085  53.931  1.00 16.32           H  
ATOM   4767 HD11 LEU A 284      42.072  87.490  53.138  1.00 18.86           H  
ATOM   4768 HD12 LEU A 284      41.869  88.071  54.602  1.00 18.86           H  
ATOM   4769 HD13 LEU A 284      42.668  86.714  54.390  1.00 18.86           H  
ATOM   4770 HD21 LEU A 284      40.809  85.580  52.365  1.00 17.57           H  
ATOM   4771 HD22 LEU A 284      41.337  84.663  53.550  1.00 17.57           H  
ATOM   4772 HD23 LEU A 284      39.775  84.841  53.319  1.00 17.57           H  
ATOM   4773  N   ARG A 285      37.861  87.902  56.189  1.00 14.43           N  
ANISOU 4773  N   ARG A 285     1820   1760   1902   -122    343     17       N  
ATOM   4774  CA  ARG A 285      36.876  88.883  55.749  1.00 14.71           C  
ANISOU 4774  CA  ARG A 285     1939   1762   1890   -116    133      1       C  
ATOM   4775  C   ARG A 285      37.096  90.204  56.469  1.00 14.24           C  
ANISOU 4775  C   ARG A 285     2046   1727   1638    -26    294      1       C  
ATOM   4776  O   ARG A 285      37.108  91.269  55.852  1.00 14.78           O  
ANISOU 4776  O   ARG A 285     2133   1867   1616      4    102     52       O  
ATOM   4777  CB  ARG A 285      35.452  88.374  55.982  1.00 15.39           C  
ANISOU 4777  CB  ARG A 285     1771   1910   2166    -17    231     18       C  
ATOM   4778  CG  ARG A 285      34.385  89.417  55.703  1.00 16.01           C  
ANISOU 4778  CG  ARG A 285     1677   2164   2243     29    306     62       C  
ATOM   4779  CD  ARG A 285      33.001  88.979  56.171  1.00 17.25           C  
ANISOU 4779  CD  ARG A 285     1727   2197   2629      3    302      9       C  
ATOM   4780  NE  ARG A 285      32.059  90.085  55.982  1.00 18.11           N  
ANISOU 4780  NE  ARG A 285     1780   2307   2793     59    190    -11       N  
ATOM   4781  CZ  ARG A 285      30.939  90.037  55.271  1.00 18.54           C  
ANISOU 4781  CZ  ARG A 285     2002   2410   2631    147    290   -209       C  
ATOM   4782  NH1 ARG A 285      30.534  88.910  54.708  1.00 19.09           N  
ANISOU 4782  NH1 ARG A 285     2080   2627   2546    190    118   -384       N  
ATOM   4783  NH2 ARG A 285      30.192  91.126  55.152  1.00 19.00           N  
ANISOU 4783  NH2 ARG A 285     2208   2343   2667     68    418   -177       N  
ATOM   4784  H   ARG A 285      37.535  87.168  56.496  1.00 17.32           H  
ATOM   4785  HA  ARG A 285      36.978  89.020  54.794  1.00 17.66           H  
ATOM   4786  HB2 ARG A 285      35.289  87.618  55.397  1.00 18.47           H  
ATOM   4787  HB3 ARG A 285      35.365  88.100  56.909  1.00 18.47           H  
ATOM   4788  HG2 ARG A 285      34.613  90.237  56.169  1.00 19.22           H  
ATOM   4789  HG3 ARG A 285      34.341  89.579  54.748  1.00 19.22           H  
ATOM   4790  HD2 ARG A 285      32.702  88.217  55.650  1.00 20.70           H  
ATOM   4791  HD3 ARG A 285      33.030  88.746  57.112  1.00 20.70           H  
ATOM   4792  HE  ARG A 285      32.248  90.831  56.366  1.00 21.74           H  
ATOM   4793 HH11 ARG A 285      30.998  88.192  54.799  1.00 22.91           H  
ATOM   4794 HH12 ARG A 285      29.806  88.896  54.250  1.00 22.91           H  
ATOM   4795 HH21 ARG A 285      30.433  91.857  55.535  1.00 22.80           H  
ATOM   4796 HH22 ARG A 285      29.465  91.101  54.693  1.00 22.80           H  
ATOM   4797  N   ALA A 286      37.235  90.146  57.795  1.00 15.16           N  
ANISOU 4797  N   ALA A 286     2084   1948   1728    -78    185     11       N  
ATOM   4798  CA  ALA A 286      37.429  91.362  58.573  1.00 15.25           C  
ANISOU 4798  CA  ALA A 286     2057   1845   1893   -149    440    -64       C  
ATOM   4799  C   ALA A 286      38.687  92.092  58.138  1.00 15.25           C  
ANISOU 4799  C   ALA A 286     2127   1742   1923    -68    483   -129       C  
ATOM   4800  O   ALA A 286      38.691  93.327  58.039  1.00 15.59           O  
ANISOU 4800  O   ALA A 286     2345   1673   1905   -152    181     14       O  
ATOM   4801  CB  ALA A 286      37.506  91.019  60.057  1.00 17.14           C  
ANISOU 4801  CB  ALA A 286     2242   2177   2095    -98    587   -188       C  
ATOM   4802  H   ALA A 286      37.220  89.424  58.262  1.00 18.20           H  
ATOM   4803  HA  ALA A 286      36.670  91.950  58.434  1.00 18.31           H  
ATOM   4804  HB1 ALA A 286      37.650  91.835  60.562  1.00 20.58           H  
ATOM   4805  HB2 ALA A 286      36.673  90.605  60.329  1.00 20.58           H  
ATOM   4806  HB3 ALA A 286      38.244  90.406  60.201  1.00 20.58           H  
ATOM   4807  N   ALA A 287      39.762  91.349  57.861  1.00 15.44           N  
ANISOU 4807  N   ALA A 287     2127   2007   1732    -36    389    -49       N  
ATOM   4808  CA  ALA A 287      41.004  91.966  57.440  1.00 14.94           C  
ANISOU 4808  CA  ALA A 287     2132   1859   1683   -160    149    -95       C  
ATOM   4809  C   ALA A 287      40.862  92.612  56.075  1.00 13.77           C  
ANISOU 4809  C   ALA A 287     1927   1545   1761   -127    -10     13       C  
ATOM   4810  O   ALA A 287      41.423  93.685  55.831  1.00 15.10           O  
ANISOU 4810  O   ALA A 287     2068   1478   2193     12    -40    -53       O  
ATOM   4811  CB  ALA A 287      42.107  90.914  57.396  1.00 15.60           C  
ANISOU 4811  CB  ALA A 287     2154   1955   1819   -165    205   -268       C  
ATOM   4812  H   ALA A 287      39.793  90.491  57.911  1.00 18.53           H  
ATOM   4813  HA  ALA A 287      41.245  92.652  58.082  1.00 17.93           H  
ATOM   4814  HB1 ALA A 287      42.922  91.325  57.068  1.00 18.73           H  
ATOM   4815  HB2 ALA A 287      42.249  90.568  58.291  1.00 18.73           H  
ATOM   4816  HB3 ALA A 287      41.836  90.197  56.803  1.00 18.73           H  
ATOM   4817  N   ALA A 288      40.142  91.961  55.166  1.00 14.81           N  
ANISOU 4817  N   ALA A 288     2130   1769   1726   -176    -34     35       N  
ATOM   4818  CA  ALA A 288      39.933  92.535  53.842  1.00 13.69           C  
ANISOU 4818  CA  ALA A 288     1985   1562   1656     80     74     16       C  
ATOM   4819  C   ALA A 288      39.048  93.771  53.915  1.00 14.23           C  
ANISOU 4819  C   ALA A 288     1991   1670   1746    149     -8    -35       C  
ATOM   4820  O   ALA A 288      39.309  94.762  53.229  1.00 14.18           O  
ANISOU 4820  O   ALA A 288     2060   1608   1719   -158    188   -129       O  
ATOM   4821  CB  ALA A 288      39.344  91.493  52.886  1.00 13.49           C  
ANISOU 4821  CB  ALA A 288     1958   1623   1546   -102     78    -30       C  
ATOM   4822  H   ALA A 288      39.767  91.196  55.286  1.00 17.78           H  
ATOM   4823  HA  ALA A 288      40.793  92.800  53.480  1.00 16.44           H  
ATOM   4824  HB1 ALA A 288      39.218  91.900  52.015  1.00 16.20           H  
ATOM   4825  HB2 ALA A 288      39.958  90.746  52.817  1.00 16.20           H  
ATOM   4826  HB3 ALA A 288      38.492  91.190  53.236  1.00 16.20           H  
ATOM   4827  N   VAL A 289      37.995  93.729  54.733  1.00 14.64           N  
ANISOU 4827  N   VAL A 289     2025   1688   1848     24     64    -78       N  
ATOM   4828  CA  VAL A 289      37.149  94.904  54.894  1.00 15.09           C  
ANISOU 4828  CA  VAL A 289     1987   1747   1998    117    157     59       C  
ATOM   4829  C   VAL A 289      37.950  96.054  55.485  1.00 14.78           C  
ANISOU 4829  C   VAL A 289     2035   1624   1957    -11    222    -95       C  
ATOM   4830  O   VAL A 289      37.854  97.197  55.030  1.00 15.60           O  
ANISOU 4830  O   VAL A 289     2149   1628   2149    -48    303     28       O  
ATOM   4831  CB  VAL A 289      35.910  94.570  55.746  1.00 15.89           C  
ANISOU 4831  CB  VAL A 289     2075   1829   2135    116    512     -9       C  
ATOM   4832  CG1 VAL A 289      35.171  95.847  56.156  1.00 16.83           C  
ANISOU 4832  CG1 VAL A 289     2067   1852   2477    146    548   -147       C  
ATOM   4833  CG2 VAL A 289      34.983  93.622  54.985  1.00 16.50           C  
ANISOU 4833  CG2 VAL A 289     2211   1832   2227    -23    488    -66       C  
ATOM   4834  H   VAL A 289      37.754  93.046  55.196  1.00 17.57           H  
ATOM   4835  HA  VAL A 289      36.835  95.179  54.019  1.00 18.11           H  
ATOM   4836  HB  VAL A 289      36.199  94.124  56.557  1.00 19.08           H  
ATOM   4837 HG11 VAL A 289      34.278  95.613  56.454  1.00 20.21           H  
ATOM   4838 HG12 VAL A 289      35.658  96.277  56.876  1.00 20.21           H  
ATOM   4839 HG13 VAL A 289      35.119  96.442  55.391  1.00 20.21           H  
ATOM   4840 HG21 VAL A 289      34.227  93.399  55.550  1.00 19.81           H  
ATOM   4841 HG22 VAL A 289      34.675  94.063  54.178  1.00 19.81           H  
ATOM   4842 HG23 VAL A 289      35.474  92.817  54.756  1.00 19.81           H  
ATOM   4843  N   GLN A 290      38.756  95.772  56.515  1.00 15.30           N  
ANISOU 4843  N   GLN A 290     2287   1622   1904     67    102   -173       N  
ATOM   4844  CA  GLN A 290      39.539  96.837  57.128  1.00 15.55           C  
ANISOU 4844  CA  GLN A 290     2288   1672   1949     98    233   -263       C  
ATOM   4845  C   GLN A 290      40.580  97.384  56.162  1.00 15.08           C  
ANISOU 4845  C   GLN A 290     2250   1485   1994     17    300   -262       C  
ATOM   4846  O   GLN A 290      40.804  98.600  56.116  1.00 15.67           O  
ANISOU 4846  O   GLN A 290     2262   1579   2111     -8    268   -190       O  
ATOM   4847  CB  GLN A 290      40.215  96.347  58.396  1.00 16.53           C  
ANISOU 4847  CB  GLN A 290     2548   1891   1840    -51    130   -336       C  
ATOM   4848  CG  GLN A 290      40.976  97.467  59.104  1.00 18.16           C  
ANISOU 4848  CG  GLN A 290     2810   2056   2034   -117    151   -403       C  
ATOM   4849  CD  GLN A 290      40.056  98.541  59.633  1.00 20.13           C  
ANISOU 4849  CD  GLN A 290     3058   2273   2320   -152    430   -457       C  
ATOM   4850  OE1 GLN A 290      39.110  98.256  60.378  1.00 20.96           O  
ANISOU 4850  OE1 GLN A 290     3042   2434   2488   -320    611   -501       O  
ATOM   4851  NE2 GLN A 290      40.322  99.783  59.256  1.00 21.66           N  
ANISOU 4851  NE2 GLN A 290     3241   2459   2530    162    392   -451       N  
ATOM   4852  H   GLN A 290      38.863  94.994  56.866  1.00 18.37           H  
ATOM   4853  HA  GLN A 290      38.933  97.554  57.370  1.00 18.67           H  
ATOM   4854  HB2 GLN A 290      39.542  96.005  59.004  1.00 19.84           H  
ATOM   4855  HB3 GLN A 290      40.846  95.646  58.170  1.00 19.84           H  
ATOM   4856  HG2 GLN A 290      41.466  97.093  59.853  1.00 21.80           H  
ATOM   4857  HG3 GLN A 290      41.592  97.879  58.478  1.00 21.80           H  
ATOM   4858 HE21 GLN A 290      40.989  99.941  58.737  1.00 26.00           H  
ATOM   4859 HE22 GLN A 290      39.827 100.431  59.530  1.00 26.00           H  
ATOM   4860  N   SER A 291      41.206  96.508  55.368  1.00 14.96           N  
ANISOU 4860  N   SER A 291     2372   1333   1980    -14    341    -40       N  
ATOM   4861  CA  SER A 291      42.188  96.941  54.384  1.00 14.44           C  
ANISOU 4861  CA  SER A 291     2146   1433   1909      2    192    -11       C  
ATOM   4862  C   SER A 291      41.550  97.837  53.329  1.00 13.94           C  
ANISOU 4862  C   SER A 291     2085   1276   1937   -103    184    -63       C  
ATOM   4863  O   SER A 291      42.100  98.881  52.972  1.00 15.17           O  
ANISOU 4863  O   SER A 291     2369   1364   2032   -252     98     21       O  
ATOM   4864  CB  SER A 291      42.833  95.723  53.726  1.00 14.73           C  
ANISOU 4864  CB  SER A 291     2122   1576   1899    -41    -65     32       C  
ATOM   4865  OG  SER A 291      43.619  95.000  54.645  1.00 15.17           O  
ANISOU 4865  OG  SER A 291     2145   1841   1779      8     85    -37       O  
ATOM   4866  H   SER A 291      41.078  95.657  55.381  1.00 17.97           H  
ATOM   4867  HA  SER A 291      42.880  97.450  54.836  1.00 17.34           H  
ATOM   4868  HB2 SER A 291      42.133  95.143  53.387  1.00 17.69           H  
ATOM   4869  HB3 SER A 291      43.398  96.022  52.997  1.00 17.69           H  
ATOM   4870  HG  SER A 291      43.133  94.681  55.251  1.00 18.21           H  
ATOM   4871  N   ALA A 292      40.399  97.424  52.793  1.00 14.72           N  
ANISOU 4871  N   ALA A 292     2024   1478   2091   -140     85     84       N  
ATOM   4872  CA  ALA A 292      39.687  98.262  51.834  1.00 14.19           C  
ANISOU 4872  CA  ALA A 292     1994   1477   1920    102      3    -23       C  
ATOM   4873  C   ALA A 292      39.253  99.579  52.475  1.00 15.20           C  
ANISOU 4873  C   ALA A 292     2254   1543   1979    164    -12    -27       C  
ATOM   4874  O   ALA A 292      39.250 100.632  51.820  1.00 15.85           O  
ANISOU 4874  O   ALA A 292     2268   1626   2127    191     32   -143       O  
ATOM   4875  CB  ALA A 292      38.492  97.513  51.251  1.00 14.48           C  
ANISOU 4875  CB  ALA A 292     2313   1344   1845    265    -43    -27       C  
ATOM   4876  H   ALA A 292      40.014  96.674  52.965  1.00 17.67           H  
ATOM   4877  HA  ALA A 292      40.281  98.471  51.096  1.00 17.03           H  
ATOM   4878  HB1 ALA A 292      38.030  98.092  50.625  1.00 17.39           H  
ATOM   4879  HB2 ALA A 292      38.810  96.718  50.795  1.00 17.39           H  
ATOM   4880  HB3 ALA A 292      37.894  97.262  51.973  1.00 17.39           H  
ATOM   4881  N   THR A 293      38.883  99.543  53.762  1.00 15.07           N  
ANISOU 4881  N   THR A 293     2343   1540   1845     54     11   -118       N  
ATOM   4882  CA  THR A 293      38.533 100.783  54.450  1.00 15.94           C  
ANISOU 4882  CA  THR A 293     2442   1652   1962     32    142   -224       C  
ATOM   4883  C   THR A 293      39.735 101.713  54.539  1.00 17.18           C  
ANISOU 4883  C   THR A 293     2603   1779   2145    -60    226   -166       C  
ATOM   4884  O   THR A 293      39.628 102.913  54.256  1.00 17.79           O  
ANISOU 4884  O   THR A 293     2615   1765   2380    247    120   -191       O  
ATOM   4885  CB  THR A 293      37.993 100.464  55.849  1.00 17.14           C  
ANISOU 4885  CB  THR A 293     2593   1809   2110    107    177   -498       C  
ATOM   4886  OG1 THR A 293      36.774  99.717  55.732  1.00 17.77           O  
ANISOU 4886  OG1 THR A 293     2516   1931   2305    142     10   -613       O  
ATOM   4887  CG2 THR A 293      37.712 101.726  56.640  1.00 18.43           C  
ANISOU 4887  CG2 THR A 293     2682   1895   2425    -13    359   -585       C  
ATOM   4888  H   THR A 293      38.828  98.833  54.244  1.00 18.10           H  
ATOM   4889  HA  THR A 293      37.836 101.237  53.952  1.00 19.14           H  
ATOM   4890  HB  THR A 293      38.661  99.949  56.328  1.00 20.58           H  
ATOM   4891  HG1 THR A 293      36.920  98.989  55.341  1.00 21.33           H  
ATOM   4892 HG21 THR A 293      37.169 101.517  57.416  1.00 22.12           H  
ATOM   4893 HG22 THR A 293      38.546 102.124  56.937  1.00 22.12           H  
ATOM   4894 HG23 THR A 293      37.238 102.366  56.087  1.00 22.12           H  
ATOM   4895  N   ASP A 294      40.891 101.175  54.929  1.00 16.65           N  
ANISOU 4895  N   ASP A 294     2497   1570   2259   -113     89   -223       N  
ATOM   4896  CA  ASP A 294      42.114 101.964  54.996  1.00 16.26           C  
ANISOU 4896  CA  ASP A 294     2373   1496   2308   -230    150   -308       C  
ATOM   4897  C   ASP A 294      42.429 102.620  53.653  1.00 17.38           C  
ANISOU 4897  C   ASP A 294     2570   1551   2483   -283      6    -75       C  
ATOM   4898  O   ASP A 294      42.813 103.798  53.600  1.00 18.58           O  
ANISOU 4898  O   ASP A 294     2744   1684   2630   -317    103     50       O  
ATOM   4899  CB  ASP A 294      43.304 101.072  55.349  1.00 16.27           C  
ANISOU 4899  CB  ASP A 294     2311   1466   2403    -60    196   -309       C  
ATOM   4900  CG  ASP A 294      43.251 100.471  56.731  1.00 17.10           C  
ANISOU 4900  CG  ASP A 294     2454   1604   2438     45    312   -105       C  
ATOM   4901  OD1 ASP A 294      42.476 100.928  57.612  1.00 17.82           O  
ANISOU 4901  OD1 ASP A 294     2678   1889   2205    172    209     58       O  
ATOM   4902  OD2 ASP A 294      44.060  99.527  56.938  1.00 18.54           O  
ANISOU 4902  OD2 ASP A 294     2630   1792   2621    116    325      9       O  
ATOM   4903  H   ASP A 294      40.995 100.353  55.161  1.00 19.99           H  
ATOM   4904  HA  ASP A 294      41.985 102.640  55.679  1.00 19.52           H  
ATOM   4905  HB2 ASP A 294      43.341 100.340  54.714  1.00 19.53           H  
ATOM   4906  HB3 ASP A 294      44.115 101.601  55.293  1.00 19.53           H  
ATOM   4907  N   LEU A 295      42.296 101.863  52.565  1.00 16.50           N  
ANISOU 4907  N   LEU A 295     2465   1541   2262   -206     26    -54       N  
ATOM   4908  CA  LEU A 295      42.735 102.314  51.256  1.00 17.03           C  
ANISOU 4908  CA  LEU A 295     2404   1675   2392   -138    -48     -7       C  
ATOM   4909  C   LEU A 295      41.716 103.196  50.555  1.00 17.54           C  
ANISOU 4909  C   LEU A 295     2525   1656   2482   -132     21     95       C  
ATOM   4910  O   LEU A 295      42.108 104.118  49.823  1.00 19.65           O  
ANISOU 4910  O   LEU A 295     2957   1907   2602   -207    -11    127       O  
ATOM   4911  CB  LEU A 295      43.038 101.093  50.378  1.00 17.72           C  
ANISOU 4911  CB  LEU A 295     2517   1768   2446    -74     61    172       C  
ATOM   4912  CG  LEU A 295      44.199 100.201  50.828  1.00 18.64           C  
ANISOU 4912  CG  LEU A 295     2398   2060   2623    -95    156    305       C  
ATOM   4913  CD1 LEU A 295      44.186  98.883  50.045  1.00 19.87           C  
ANISOU 4913  CD1 LEU A 295     2701   2168   2679    340    179    152       C  
ATOM   4914  CD2 LEU A 295      45.545 100.930  50.681  1.00 21.09           C  
ANISOU 4914  CD2 LEU A 295     2559   2511   2943    -70    118    539       C  
ATOM   4915  H   LEU A 295      41.950 101.075  52.560  1.00 19.80           H  
ATOM   4916  HA  LEU A 295      43.543 102.839  51.371  1.00 20.44           H  
ATOM   4917  HB2 LEU A 295      42.244 100.536  50.353  1.00 21.27           H  
ATOM   4918  HB3 LEU A 295      43.250 101.409  49.486  1.00 21.27           H  
ATOM   4919  HG  LEU A 295      44.095  99.990  51.769  1.00 22.37           H  
ATOM   4920 HD11 LEU A 295      44.932  98.335  50.336  1.00 23.85           H  
ATOM   4921 HD12 LEU A 295      43.350  98.422  50.218  1.00 23.85           H  
ATOM   4922 HD13 LEU A 295      44.267  99.077  49.098  1.00 23.85           H  
ATOM   4923 HD21 LEU A 295      46.262 100.321  50.917  1.00 25.32           H  
ATOM   4924 HD22 LEU A 295      45.648 101.221  49.761  1.00 25.32           H  
ATOM   4925 HD23 LEU A 295      45.555 101.698  51.274  1.00 25.32           H  
ATOM   4926  N   TYR A 296      40.420 102.952  50.755  1.00 17.18           N  
ANISOU 4926  N   TYR A 296     2300   1777   2452     44     66     78       N  
ATOM   4927  CA  TYR A 296      39.384 103.582  49.936  1.00 18.09           C  
ANISOU 4927  CA  TYR A 296     2588   1785   2500    192    -98     44       C  
ATOM   4928  C   TYR A 296      38.279 104.264  50.729  1.00 18.72           C  
ANISOU 4928  C   TYR A 296     2772   1723   2617    281    -44     48       C  
ATOM   4929  O   TYR A 296      37.494 105.009  50.129  1.00 20.22           O  
ANISOU 4929  O   TYR A 296     3082   1734   2866    298   -158    152       O  
ATOM   4930  CB  TYR A 296      38.751 102.549  48.980  1.00 18.58           C  
ANISOU 4930  CB  TYR A 296     2641   1854   2564    173    -31   -126       C  
ATOM   4931  CG  TYR A 296      39.809 101.847  48.161  1.00 17.50           C  
ANISOU 4931  CG  TYR A 296     2376   1644   2629    399    137    -61       C  
ATOM   4932  CD1 TYR A 296      40.505 102.530  47.193  1.00 18.55           C  
ANISOU 4932  CD1 TYR A 296     2613   1679   2757    318    275      7       C  
ATOM   4933  CD2 TYR A 296      40.144 100.519  48.387  1.00 18.00           C  
ANISOU 4933  CD2 TYR A 296     2367   1861   2611    336     42    138       C  
ATOM   4934  CE1 TYR A 296      41.499 101.933  46.474  1.00 19.33           C  
ANISOU 4934  CE1 TYR A 296     2784   1914   2646     17    513   -189       C  
ATOM   4935  CE2 TYR A 296      41.130  99.896  47.654  1.00 19.44           C  
ANISOU 4935  CE2 TYR A 296     2651   2054   2680    198     28    -20       C  
ATOM   4936  CZ  TYR A 296      41.819 100.607  46.701  1.00 19.78           C  
ANISOU 4936  CZ  TYR A 296     2698   2158   2658     97    207   -253       C  
ATOM   4937  OH  TYR A 296      42.828  99.998  45.970  1.00 22.01           O  
ANISOU 4937  OH  TYR A 296     2923   2582   2858    -50    -53   -562       O  
ATOM   4938  H   TYR A 296      40.115 102.424  51.361  1.00 20.63           H  
ATOM   4939  HA  TYR A 296      39.805 104.266  49.393  1.00 21.71           H  
ATOM   4940  HB2 TYR A 296      38.271 101.883  49.497  1.00 22.31           H  
ATOM   4941  HB3 TYR A 296      38.142 103.000  48.374  1.00 22.31           H  
ATOM   4942  HD1 TYR A 296      40.294 103.420  47.025  1.00 22.27           H  
ATOM   4943  HD2 TYR A 296      39.694 100.040  49.045  1.00 21.61           H  
ATOM   4944  HE1 TYR A 296      41.962 102.418  45.829  1.00 23.20           H  
ATOM   4945  HE2 TYR A 296      41.329  99.000  47.803  1.00 23.33           H  
ATOM   4946  HH  TYR A 296      42.914  99.198  46.211  1.00 26.42           H  
ATOM   4947  N   GLY A 297      38.209 104.068  52.036  1.00 19.38           N  
ANISOU 4947  N   GLY A 297     2935   1935   2493    446     20   -143       N  
ATOM   4948  CA  GLY A 297      37.202 104.712  52.862  1.00 19.82           C  
ANISOU 4948  CA  GLY A 297     3030   1932   2570    434    193   -103       C  
ATOM   4949  C   GLY A 297      36.055 103.774  53.189  1.00 20.65           C  
ANISOU 4949  C   GLY A 297     3068   2069   2709    464    327   -291       C  
ATOM   4950  O   GLY A 297      35.681 102.908  52.396  1.00 19.96           O  
ANISOU 4950  O   GLY A 297     2804   1966   2815    379    106   -507       O  
ATOM   4951  H   GLY A 297      38.742 103.558  52.477  1.00 23.26           H  
ATOM   4952  HA2 GLY A 297      37.606 105.006  53.693  1.00 23.80           H  
ATOM   4953  HA3 GLY A 297      36.845 105.483  52.394  1.00 23.80           H  
ATOM   4954  N   SER A 298      35.461 103.963  54.372  1.00 22.47           N  
ANISOU 4954  N   SER A 298     3401   2323   2812    453    422   -365       N  
ATOM   4955  CA  SER A 298      34.443 103.026  54.837  1.00 23.20           C  
ANISOU 4955  CA  SER A 298     3429   2595   2790    508    442   -492       C  
ATOM   4956  C   SER A 298      33.195 103.031  53.961  1.00 23.34           C  
ANISOU 4956  C   SER A 298     3287   2630   2950    504    488   -604       C  
ATOM   4957  O   SER A 298      32.496 102.020  53.891  1.00 23.40           O  
ANISOU 4957  O   SER A 298     3147   2822   2922    179    381   -641       O  
ATOM   4958  CB  SER A 298      34.073 103.328  56.287  1.00 25.09           C  
ANISOU 4958  CB  SER A 298     3655   2970   2908    680    520   -768       C  
ATOM   4959  OG  SER A 298      33.514 104.626  56.385  1.00 26.72           O  
ANISOU 4959  OG  SER A 298     3740   3415   2999    758    367   -969       O  
ATOM   4960  H   SER A 298      35.626 104.611  54.912  1.00 26.97           H  
ATOM   4961  HA  SER A 298      34.819 102.133  54.798  1.00 27.85           H  
ATOM   4962  HB2 SER A 298      33.422 102.677  56.592  1.00 30.11           H  
ATOM   4963  HB3 SER A 298      34.871 103.281  56.837  1.00 30.11           H  
ATOM   4964  HG  SER A 298      33.299 104.787  57.181  1.00 32.08           H  
ATOM   4965  N   THR A 299      32.896 104.144  53.283  1.00 23.54           N  
ANISOU 4965  N   THR A 299     3321   2531   3093    731    388   -766       N  
ATOM   4966  CA  THR A 299      31.694 104.246  52.458  1.00 24.97           C  
ANISOU 4966  CA  THR A 299     3421   2653   3412    796    361   -503       C  
ATOM   4967  C   THR A 299      31.952 103.899  50.995  1.00 23.36           C  
ANISOU 4967  C   THR A 299     3012   2527   3337    644    344   -265       C  
ATOM   4968  O   THR A 299      31.064 104.085  50.157  1.00 23.04           O  
ANISOU 4968  O   THR A 299     2754   2604   3394    734    292   -211       O  
ATOM   4969  CB  THR A 299      31.077 105.650  52.569  1.00 27.90           C  
ANISOU 4969  CB  THR A 299     3766   3007   3828    996    368   -535       C  
ATOM   4970  OG1 THR A 299      31.957 106.621  51.989  1.00 28.59           O  
ANISOU 4970  OG1 THR A 299     4063   2643   4157    985    194   -449       O  
ATOM   4971  CG2 THR A 299      30.822 106.002  54.016  1.00 29.63           C  
ANISOU 4971  CG2 THR A 299     3918   3347   3992   1213    274   -675       C  
ATOM   4972  H   THR A 299      33.380 104.856  53.288  1.00 28.26           H  
ATOM   4973  HA  THR A 299      31.039 103.618  52.799  1.00 29.97           H  
ATOM   4974  HB  THR A 299      30.232 105.666  52.094  1.00 33.49           H  
ATOM   4975  HG1 THR A 299      32.697 106.612  52.385  1.00 34.32           H  
ATOM   4976 HG21 THR A 299      30.329 106.835  54.072  1.00 35.56           H  
ATOM   4977 HG22 THR A 299      30.304 105.301  54.441  1.00 35.56           H  
ATOM   4978 HG23 THR A 299      31.664 106.101  54.487  1.00 35.56           H  
ATOM   4979  N   SER A 300      33.136 103.388  50.678  1.00 20.90           N  
ANISOU 4979  N   SER A 300     2718   2133   3090    539    429   -179       N  
ATOM   4980  CA  SER A 300      33.539 103.185  49.298  1.00 19.80           C  
ANISOU 4980  CA  SER A 300     2576   1934   3012    512    235   -125       C  
ATOM   4981  C   SER A 300      32.847 101.974  48.674  1.00 18.47           C  
ANISOU 4981  C   SER A 300     2305   1923   2790    548    166      6       C  
ATOM   4982  O   SER A 300      32.406 101.037  49.351  1.00 18.36           O  
ANISOU 4982  O   SER A 300     2245   1967   2766    441     51     15       O  
ATOM   4983  CB  SER A 300      35.057 103.012  49.220  1.00 18.78           C  
ANISOU 4983  CB  SER A 300     2477   1688   2971    465    231    -45       C  
ATOM   4984  OG  SER A 300      35.471 101.808  49.860  1.00 18.68           O  
ANISOU 4984  OG  SER A 300     2419   1738   2942    292    445     28       O  
ATOM   4985  H   SER A 300      33.730 103.149  51.251  1.00 25.09           H  
ATOM   4986  HA  SER A 300      33.278 103.962  48.779  1.00 23.76           H  
ATOM   4987  HB2 SER A 300      35.322 102.979  48.288  1.00 22.55           H  
ATOM   4988  HB3 SER A 300      35.482 103.764  49.660  1.00 22.55           H  
ATOM   4989  HG  SER A 300      35.263 101.829  50.674  1.00 22.43           H  
ATOM   4990  N   GLN A 301      32.762 102.009  47.338  1.00 18.05           N  
ANISOU 4990  N   GLN A 301     2235   1937   2686    380    -36    -14       N  
ATOM   4991  CA  GLN A 301      32.370 100.827  46.587  1.00 18.32           C  
ANISOU 4991  CA  GLN A 301     2259   1938   2762    471   -118    145       C  
ATOM   4992  C   GLN A 301      33.291  99.654  46.887  1.00 17.46           C  
ANISOU 4992  C   GLN A 301     1992   2119   2524    417     57    170       C  
ATOM   4993  O   GLN A 301      32.844  98.502  46.931  1.00 17.13           O  
ANISOU 4993  O   GLN A 301     1936   2061   2511    421     19    138       O  
ATOM   4994  CB  GLN A 301      32.422 101.135  45.090  1.00 19.27           C  
ANISOU 4994  CB  GLN A 301     2425   1983   2912    538      9     43       C  
ATOM   4995  CG  GLN A 301      32.030  99.975  44.216  1.00 20.27           C  
ANISOU 4995  CG  GLN A 301     2486   2206   3008    581   -176    163       C  
ATOM   4996  CD  GLN A 301      30.574  99.600  44.407  1.00 21.28           C  
ANISOU 4996  CD  GLN A 301     2498   2211   3377    836   -434     76       C  
ATOM   4997  OE1 GLN A 301      29.682 100.376  44.064  1.00 24.10           O  
ANISOU 4997  OE1 GLN A 301     2843   2426   3888    706   -798    156       O  
ATOM   4998  NE2 GLN A 301      30.330  98.417  44.970  1.00 21.23           N  
ANISOU 4998  NE2 GLN A 301     2516   2432   3118    877   -345     -3       N  
ATOM   4999  H   GLN A 301      32.926 102.699  46.851  1.00 21.67           H  
ATOM   5000  HA  GLN A 301      31.464 100.586  46.836  1.00 21.99           H  
ATOM   5001  HB2 GLN A 301      31.814 101.867  44.902  1.00 23.13           H  
ATOM   5002  HB3 GLN A 301      33.329 101.389  44.856  1.00 23.13           H  
ATOM   5003  HG2 GLN A 301      32.164 100.214  43.286  1.00 24.33           H  
ATOM   5004  HG3 GLN A 301      32.575  99.205  44.442  1.00 24.33           H  
ATOM   5005 HE21 GLN A 301      30.984  97.910  45.205  1.00 25.48           H  
ATOM   5006 HE22 GLN A 301      29.519  98.161  45.099  1.00 25.48           H  
ATOM   5007  N   GLU A 302      34.585  99.921  47.063  1.00 16.80           N  
ANISOU 5007  N   GLU A 302     2002   2029   2352    381     70    150       N  
ATOM   5008  CA  GLU A 302      35.534  98.838  47.285  1.00 15.41           C  
ANISOU 5008  CA  GLU A 302     1888   1852   2115    216    209     69       C  
ATOM   5009  C   GLU A 302      35.188  98.057  48.547  1.00 15.16           C  
ANISOU 5009  C   GLU A 302     1872   1789   2099    264    300     36       C  
ATOM   5010  O   GLU A 302      35.163  96.826  48.539  1.00 15.45           O  
ANISOU 5010  O   GLU A 302     1935   1858   2079    164    300     75       O  
ATOM   5011  CB  GLU A 302      36.950  99.403  47.325  1.00 15.00           C  
ANISOU 5011  CB  GLU A 302     1807   1824   2070    218    373     17       C  
ATOM   5012  CG  GLU A 302      37.461  99.910  45.973  1.00 16.14           C  
ANISOU 5012  CG  GLU A 302     2101   1927   2102     86    348    187       C  
ATOM   5013  CD  GLU A 302      37.050 101.346  45.633  1.00 18.34           C  
ANISOU 5013  CD  GLU A 302     2500   2153   2318    130    636    362       C  
ATOM   5014  OE1 GLU A 302      36.315 101.996  46.375  1.00 18.04           O  
ANISOU 5014  OE1 GLU A 302     2435   2100   2319    223    389    316       O  
ATOM   5015  OE2 GLU A 302      37.482 101.851  44.587  1.00 22.17           O  
ANISOU 5015  OE2 GLU A 302     3151   2600   2674    589    916    613       O  
ATOM   5016  H   GLU A 302      34.933 100.707  47.058  1.00 20.17           H  
ATOM   5017  HA  GLU A 302      35.494  98.210  46.547  1.00 18.50           H  
ATOM   5018  HB2 GLU A 302      36.969 100.148  47.946  1.00 18.01           H  
ATOM   5019  HB3 GLU A 302      37.553  98.706  47.626  1.00 18.01           H  
ATOM   5020  HG2 GLU A 302      38.431  99.877  45.977  1.00 19.37           H  
ATOM   5021  HG3 GLU A 302      37.113  99.334  45.275  1.00 19.37           H  
ATOM   5022  N   VAL A 303      34.896  98.760  49.643  1.00 15.19           N  
ANISOU 5022  N   VAL A 303     2069   1608   2095    302    336     65       N  
ATOM   5023  CA  VAL A 303      34.488  98.080  50.867  1.00 15.33           C  
ANISOU 5023  CA  VAL A 303     2012   1672   2140    282    332     23       C  
ATOM   5024  C   VAL A 303      33.205  97.292  50.634  1.00 15.25           C  
ANISOU 5024  C   VAL A 303     1942   1682   2172    178    151    -44       C  
ATOM   5025  O   VAL A 303      33.075  96.142  51.057  1.00 15.48           O  
ANISOU 5025  O   VAL A 303     1930   1692   2260    184    296     21       O  
ATOM   5026  CB  VAL A 303      34.324  99.099  52.008  1.00 16.64           C  
ANISOU 5026  CB  VAL A 303     2352   1786   2186    216    276   -148       C  
ATOM   5027  CG1 VAL A 303      33.581  98.472  53.165  1.00 16.32           C  
ANISOU 5027  CG1 VAL A 303     2467   1682   2052    190    333   -157       C  
ATOM   5028  CG2 VAL A 303      35.673  99.603  52.433  1.00 16.75           C  
ANISOU 5028  CG2 VAL A 303     2442   1669   2252    282    180   -422       C  
ATOM   5029  H   VAL A 303      34.925  99.618  49.703  1.00 18.24           H  
ATOM   5030  HA  VAL A 303      35.181  97.450  51.119  1.00 18.40           H  
ATOM   5031  HB  VAL A 303      33.801  99.856  51.702  1.00 19.98           H  
ATOM   5032 HG11 VAL A 303      33.722  99.010  53.960  1.00 19.59           H  
ATOM   5033 HG12 VAL A 303      32.635  98.438  52.952  1.00 19.59           H  
ATOM   5034 HG13 VAL A 303      33.920  97.575  53.309  1.00 19.59           H  
ATOM   5035 HG21 VAL A 303      35.558 100.251  53.145  1.00 20.10           H  
ATOM   5036 HG22 VAL A 303      36.205  98.856  52.747  1.00 20.10           H  
ATOM   5037 HG23 VAL A 303      36.107 100.021  51.673  1.00 20.10           H  
ATOM   5038  N   ALA A 304      32.231  97.912  49.970  1.00 16.06           N  
ANISOU 5038  N   ALA A 304     2037   1830   2234    228    223    -93       N  
ATOM   5039  CA  ALA A 304      30.959  97.242  49.749  1.00 16.37           C  
ANISOU 5039  CA  ALA A 304     1917   1890   2413    319    189      6       C  
ATOM   5040  C   ALA A 304      31.140  95.973  48.936  1.00 16.33           C  
ANISOU 5040  C   ALA A 304     2052   1930   2224    415    298     19       C  
ATOM   5041  O   ALA A 304      30.500  94.953  49.212  1.00 15.98           O  
ANISOU 5041  O   ALA A 304     2116   1905   2051    267    332      6       O  
ATOM   5042  CB  ALA A 304      29.999  98.180  49.026  1.00 17.06           C  
ANISOU 5042  CB  ALA A 304     1837   2113   2530    486    219    -90       C  
ATOM   5043  H   ALA A 304      32.280  98.706  49.644  1.00 19.27           H  
ATOM   5044  HA  ALA A 304      30.579  97.006  50.610  1.00 19.65           H  
ATOM   5045  HB1 ALA A 304      29.151  97.727  48.897  1.00 20.48           H  
ATOM   5046  HB2 ALA A 304      29.871  98.977  49.564  1.00 20.48           H  
ATOM   5047  HB3 ALA A 304      30.379  98.420  48.166  1.00 20.48           H  
ATOM   5048  N   SER A 305      32.021  96.009  47.935  1.00 16.20           N  
ANISOU 5048  N   SER A 305     1891   2000   2264    259    235    141       N  
ATOM   5049  CA  SER A 305      32.233  94.838  47.094  1.00 14.92           C  
ANISOU 5049  CA  SER A 305     1808   1834   2028    452    -12    -42       C  
ATOM   5050  C   SER A 305      32.936  93.716  47.844  1.00 14.26           C  
ANISOU 5050  C   SER A 305     1831   1669   1920    114     67    -12       C  
ATOM   5051  O   SER A 305      32.642  92.534  47.617  1.00 13.95           O  
ANISOU 5051  O   SER A 305     1741   1536   2023     15     39     67       O  
ATOM   5052  CB  SER A 305      33.040  95.225  45.857  1.00 15.73           C  
ANISOU 5052  CB  SER A 305     1901   2142   1934    427   -156   -181       C  
ATOM   5053  OG  SER A 305      32.247  96.050  44.999  1.00 17.05           O  
ANISOU 5053  OG  SER A 305     2094   2292   2092    395   -312    -53       O  
ATOM   5054  H   SER A 305      32.502  96.690  47.725  1.00 19.45           H  
ATOM   5055  HA  SER A 305      31.366  94.509  46.811  1.00 17.91           H  
ATOM   5056  HB2 SER A 305      33.830  95.715  46.132  1.00 18.89           H  
ATOM   5057  HB3 SER A 305      33.298  94.421  45.379  1.00 18.89           H  
ATOM   5058  HG  SER A 305      31.563  95.631  44.750  1.00 20.47           H  
ATOM   5059  N   VAL A 306      33.884  94.058  48.717  1.00 14.27           N  
ANISOU 5059  N   VAL A 306     1781   1738   1902    -50     95    127       N  
ATOM   5060  CA  VAL A 306      34.491  93.044  49.575  1.00 13.95           C  
ANISOU 5060  CA  VAL A 306     1646   1848   1805    -40     67    -28       C  
ATOM   5061  C   VAL A 306      33.417  92.339  50.390  1.00 13.93           C  
ANISOU 5061  C   VAL A 306     1658   1790   1844    165    149    -95       C  
ATOM   5062  O   VAL A 306      33.397  91.103  50.497  1.00 14.84           O  
ANISOU 5062  O   VAL A 306     1746   1812   2081    215   -104     27       O  
ATOM   5063  CB  VAL A 306      35.579  93.673  50.462  1.00 14.44           C  
ANISOU 5063  CB  VAL A 306     1776   1985   1727      9     20     -4       C  
ATOM   5064  CG1 VAL A 306      36.059  92.678  51.509  1.00 15.61           C  
ANISOU 5064  CG1 VAL A 306     2012   2051   1869    113      6    -52       C  
ATOM   5065  CG2 VAL A 306      36.752  94.141  49.584  1.00 14.48           C  
ANISOU 5065  CG2 VAL A 306     1655   1857   1989     68     49   -179       C  
ATOM   5066  H   VAL A 306      34.188  94.855  48.831  1.00 17.13           H  
ATOM   5067  HA  VAL A 306      34.922  92.376  49.019  1.00 16.74           H  
ATOM   5068  HB  VAL A 306      35.210  94.439  50.928  1.00 17.34           H  
ATOM   5069 HG11 VAL A 306      36.890  92.999  51.893  1.00 18.74           H  
ATOM   5070 HG12 VAL A 306      35.384  92.597  52.201  1.00 18.74           H  
ATOM   5071 HG13 VAL A 306      36.202  91.817  51.085  1.00 18.74           H  
ATOM   5072 HG21 VAL A 306      37.413  94.574  50.145  1.00 17.38           H  
ATOM   5073 HG22 VAL A 306      37.144  93.370  49.145  1.00 17.38           H  
ATOM   5074 HG23 VAL A 306      36.420  94.766  48.920  1.00 17.38           H  
ATOM   5075  N   LYS A 307      32.518  93.114  51.005  1.00 14.61           N  
ANISOU 5075  N   LYS A 307     1752   1822   1977    206    228    -70       N  
ATOM   5076  CA  LYS A 307      31.475  92.518  51.833  1.00 14.79           C  
ANISOU 5076  CA  LYS A 307     1873   1789   1956    166    241     72       C  
ATOM   5077  C   LYS A 307      30.550  91.644  51.004  1.00 14.56           C  
ANISOU 5077  C   LYS A 307     1819   1802   1910    244    210    -43       C  
ATOM   5078  O   LYS A 307      30.199  90.527  51.418  1.00 16.00           O  
ANISOU 5078  O   LYS A 307     1894   2037   2146    142    -12    -81       O  
ATOM   5079  CB  LYS A 307      30.671  93.611  52.537  1.00 15.30           C  
ANISOU 5079  CB  LYS A 307     2047   1742   2023    288    160    -45       C  
ATOM   5080  CG  LYS A 307      31.458  94.437  53.536  1.00 17.35           C  
ANISOU 5080  CG  LYS A 307     2401   1929   2262    342    242   -177       C  
ATOM   5081  CD  LYS A 307      30.588  95.506  54.169  1.00 19.26           C  
ANISOU 5081  CD  LYS A 307     2673   2126   2520    326    354   -500       C  
ATOM   5082  CE  LYS A 307      31.349  96.310  55.213  1.00 21.02           C  
ANISOU 5082  CE  LYS A 307     2798   2329   2861    377    562   -605       C  
ATOM   5083  NZ  LYS A 307      30.533  97.481  55.693  1.00 24.27           N  
ANISOU 5083  NZ  LYS A 307     3133   2779   3309    351    637   -543       N  
ATOM   5084  H   LYS A 307      32.492  93.972  50.961  1.00 17.54           H  
ATOM   5085  HA  LYS A 307      31.895  91.964  52.509  1.00 17.75           H  
ATOM   5086  HB2 LYS A 307      30.325  94.219  51.865  1.00 18.36           H  
ATOM   5087  HB3 LYS A 307      29.938  93.194  53.016  1.00 18.36           H  
ATOM   5088  HG2 LYS A 307      31.792  93.859  54.240  1.00 20.83           H  
ATOM   5089  HG3 LYS A 307      32.198  94.872  53.084  1.00 20.83           H  
ATOM   5090  HD2 LYS A 307      30.280  96.116  53.481  1.00 23.12           H  
ATOM   5091  HD3 LYS A 307      29.829  95.086  54.603  1.00 23.12           H  
ATOM   5092  HE2 LYS A 307      31.551  95.743  55.974  1.00 25.24           H  
ATOM   5093  HE3 LYS A 307      32.172  96.648  54.824  1.00 25.24           H  
ATOM   5094  HZ1 LYS A 307      30.998  97.953  56.286  1.00 29.13           H  
ATOM   5095  HZ2 LYS A 307      30.322  98.006  55.006  1.00 29.13           H  
ATOM   5096  HZ3 LYS A 307      29.784  97.192  56.077  1.00 29.13           H  
ATOM   5097  N   GLN A 308      30.176  92.118  49.811  1.00 15.18           N  
ANISOU 5097  N   GLN A 308     1849   1882   2037    131    219    -88       N  
ATOM   5098  CA AGLN A 308      29.302  91.346  48.933  0.65 14.86           C  
ANISOU 5098  CA AGLN A 308     1722   1827   2096     19    237   -128       C  
ATOM   5099  CA BGLN A 308      29.290  91.332  48.963  0.35 15.36           C  
ANISOU 5099  CA BGLN A 308     1857   1866   2113     45    268    -13       C  
ATOM   5100  C   GLN A 308      29.939  90.017  48.556  1.00 14.49           C  
ANISOU 5100  C   GLN A 308     1690   1749   2069     48    217    -27       C  
ATOM   5101  O   GLN A 308      29.279  88.976  48.547  1.00 15.07           O  
ANISOU 5101  O   GLN A 308     1771   1750   2205     42    138    110       O  
ATOM   5102  CB AGLN A 308      29.008  92.152  47.661  0.65 16.70           C  
ANISOU 5102  CB AGLN A 308     1909   2156   2281    328    302   -127       C  
ATOM   5103  CB BGLN A 308      28.869  92.136  47.734  0.35 17.49           C  
ANISOU 5103  CB BGLN A 308     2188   2154   2303    192    368    143       C  
ATOM   5104  CG AGLN A 308      28.216  93.447  47.881  0.65 18.12           C  
ANISOU 5104  CG AGLN A 308     2062   2212   2611    556    378    -32       C  
ATOM   5105  CG BGLN A 308      27.818  93.212  48.022  0.35 19.13           C  
ANISOU 5105  CG BGLN A 308     2435   2288   2545    239    467    350       C  
ATOM   5106  CD AGLN A 308      28.267  94.407  46.691  0.65 19.93           C  
ANISOU 5106  CD AGLN A 308     2226   2518   2829    756    446   -139       C  
ATOM   5107  CD BGLN A 308      26.527  92.648  48.627  0.35 20.06           C  
ANISOU 5107  CD BGLN A 308     2557   2483   2580    328    590    431       C  
ATOM   5108  OE1AGLN A 308      28.888  94.119  45.678  0.65 20.57           O  
ANISOU 5108  OE1AGLN A 308     2436   2641   2740    565     67   -124       O  
ATOM   5109  OE1BGLN A 308      26.305  92.736  49.833  0.35 21.86           O  
ANISOU 5109  OE1BGLN A 308     2723   2753   2828    339    617    558       O  
ATOM   5110  NE2AGLN A 308      27.597  95.557  46.819  0.65 21.51           N  
ANISOU 5110  NE2AGLN A 308     2195   2879   3097   1149    760   -281       N  
ATOM   5111  NE2BGLN A 308      25.671  92.075  47.784  0.35 19.20           N  
ANISOU 5111  NE2BGLN A 308     2516   2358   2420    228    575    458       N  
ATOM   5112  H  AGLN A 308      30.414  92.879  49.488  0.65 18.22           H  
ATOM   5113  H  BGLN A 308      30.417  92.874  49.478  0.35 18.22           H  
ATOM   5114  HA AGLN A 308      28.468  91.170  49.398  0.65 17.84           H  
ATOM   5115  HA BGLN A 308      28.486  91.126  49.465  0.35 18.44           H  
ATOM   5116  HB2AGLN A 308      29.852  92.395  47.249  0.65 20.05           H  
ATOM   5117  HB2BGLN A 308      29.652  92.579  47.370  0.35 20.99           H  
ATOM   5118  HB3AGLN A 308      28.492  91.596  47.057  0.65 20.05           H  
ATOM   5119  HB3BGLN A 308      28.497  91.528  47.077  0.35 20.99           H  
ATOM   5120  HG2AGLN A 308      27.286  93.221  48.040  0.65 21.75           H  
ATOM   5121  HG2BGLN A 308      28.187  93.852  48.650  0.35 22.96           H  
ATOM   5122  HG3AGLN A 308      28.582  93.910  48.651  0.65 21.75           H  
ATOM   5123  HG3BGLN A 308      27.588  93.657  47.191  0.35 22.96           H  
ATOM   5124 HE21AGLN A 308      27.167  95.725  47.544  0.65 25.81           H  
ATOM   5125 HE21BGLN A 308      25.856  92.035  46.945  0.35 23.05           H  
ATOM   5126 HE22AGLN A 308      27.597  96.128  46.176  0.65 25.81           H  
ATOM   5127 HE22BGLN A 308      24.934  91.745  48.077  0.35 23.05           H  
ATOM   5128  N   ALA A 309      31.233  90.038  48.226  1.00 13.41           N  
ANISOU 5128  N   ALA A 309     1532   1552   2012     71    174     47       N  
ATOM   5129  CA  ALA A 309      31.906  88.814  47.793  1.00 12.75           C  
ANISOU 5129  CA  ALA A 309     1571   1586   1688    168    367    121       C  
ATOM   5130  C   ALA A 309      31.973  87.780  48.904  1.00 13.89           C  
ANISOU 5130  C   ALA A 309     1693   1604   1979    -30    303   -109       C  
ATOM   5131  O   ALA A 309      31.753  86.579  48.662  1.00 15.09           O  
ANISOU 5131  O   ALA A 309     1703   1788   2244     36    162   -134       O  
ATOM   5132  CB  ALA A 309      33.312  89.143  47.298  1.00 13.62           C  
ANISOU 5132  CB  ALA A 309     1565   1806   1802    232    299    302       C  
ATOM   5133  H   ALA A 309      31.737  90.735  48.242  1.00 16.10           H  
ATOM   5134  HA  ALA A 309      31.398  88.430  47.061  1.00 15.31           H  
ATOM   5135  HB1 ALA A 309      33.748  88.323  47.017  1.00 16.35           H  
ATOM   5136  HB2 ALA A 309      33.247  89.757  46.549  1.00 16.35           H  
ATOM   5137  HB3 ALA A 309      33.813  89.554  48.019  1.00 16.35           H  
ATOM   5138  N   PHE A 310      32.329  88.211  50.118  1.00 14.04           N  
ANISOU 5138  N   PHE A 310     1810   1633   1892     23    204     89       N  
ATOM   5139  CA  PHE A 310      32.334  87.269  51.233  1.00 14.16           C  
ANISOU 5139  CA  PHE A 310     1817   1808   1754    -70    105    182       C  
ATOM   5140  C   PHE A 310      30.922  86.800  51.569  1.00 14.30           C  
ANISOU 5140  C   PHE A 310     1734   1715   1983    139     61    180       C  
ATOM   5141  O   PHE A 310      30.729  85.621  51.892  1.00 15.48           O  
ANISOU 5141  O   PHE A 310     2029   1589   2262    -10    198    199       O  
ATOM   5142  CB  PHE A 310      33.096  87.852  52.425  1.00 14.11           C  
ANISOU 5142  CB  PHE A 310     1875   1689   1795    -87    218     50       C  
ATOM   5143  CG  PHE A 310      34.599  87.768  52.264  1.00 13.75           C  
ANISOU 5143  CG  PHE A 310     1652   1637   1935   -121    197    107       C  
ATOM   5144  CD1 PHE A 310      35.272  86.613  52.623  1.00 15.11           C  
ANISOU 5144  CD1 PHE A 310     1719   1785   2238    -36    256    381       C  
ATOM   5145  CD2 PHE A 310      35.336  88.821  51.746  1.00 14.33           C  
ANISOU 5145  CD2 PHE A 310     1649   1778   2019     48    372     52       C  
ATOM   5146  CE1 PHE A 310      36.649  86.512  52.479  1.00 15.48           C  
ANISOU 5146  CE1 PHE A 310     1740   1848   2293     18     26    309       C  
ATOM   5147  CE2 PHE A 310      36.725  88.717  51.593  1.00 13.85           C  
ANISOU 5147  CE2 PHE A 310     1604   1623   2036    -28    166    122       C  
ATOM   5148  CZ  PHE A 310      37.368  87.566  51.960  1.00 14.31           C  
ANISOU 5148  CZ  PHE A 310     1449   1844   2145    -16     52    281       C  
ATOM   5149  H   PHE A 310      32.564  89.014  50.315  1.00 16.86           H  
ATOM   5150  HA  PHE A 310      32.824  86.470  50.986  1.00 17.00           H  
ATOM   5151  HB2 PHE A 310      32.857  88.787  52.524  1.00 16.93           H  
ATOM   5152  HB3 PHE A 310      32.852  87.361  53.225  1.00 16.93           H  
ATOM   5153  HD1 PHE A 310      34.795  85.893  52.967  1.00 18.14           H  
ATOM   5154  HD2 PHE A 310      34.903  89.606  51.498  1.00 17.21           H  
ATOM   5155  HE1 PHE A 310      37.087  85.731  52.732  1.00 18.58           H  
ATOM   5156  HE2 PHE A 310      37.210  89.430  51.242  1.00 16.63           H  
ATOM   5157  HZ  PHE A 310      38.290  87.496  51.860  1.00 17.18           H  
ATOM   5158  N   ASP A 311      29.915  87.684  51.465  1.00 14.78           N  
ANISOU 5158  N   ASP A 311     1645   1914   2058     69    228     43       N  
ATOM   5159  CA  ASP A 311      28.534  87.239  51.619  1.00 15.76           C  
ANISOU 5159  CA  ASP A 311     1646   1972   2370   -160    249    150       C  
ATOM   5160  C   ASP A 311      28.206  86.134  50.620  1.00 15.35           C  
ANISOU 5160  C   ASP A 311     1534   1951   2346   -229    145    268       C  
ATOM   5161  O   ASP A 311      27.552  85.139  50.965  1.00 16.14           O  
ANISOU 5161  O   ASP A 311     1633   2024   2475   -181    172    408       O  
ATOM   5162  CB  ASP A 311      27.560  88.396  51.378  1.00 17.36           C  
ANISOU 5162  CB  ASP A 311     1582   2227   2788    -52    132    130       C  
ATOM   5163  CG  ASP A 311      27.455  89.362  52.541  1.00 21.80           C  
ANISOU 5163  CG  ASP A 311     2157   2888   3237    389    -15     12       C  
ATOM   5164  OD1 ASP A 311      27.964  89.087  53.650  1.00 22.82           O  
ANISOU 5164  OD1 ASP A 311     2197   3267   3206     95     95   -202       O  
ATOM   5165  OD2 ASP A 311      26.843  90.431  52.329  1.00 24.93           O  
ANISOU 5165  OD2 ASP A 311     2696   3187   3590    808   -262   -224       O  
ATOM   5166  H   ASP A 311      30.006  88.525  51.310  1.00 17.75           H  
ATOM   5167  HA  ASP A 311      28.428  86.915  52.527  1.00 18.92           H  
ATOM   5168  HB2 ASP A 311      27.857  88.898  50.603  1.00 20.84           H  
ATOM   5169  HB3 ASP A 311      26.676  88.031  51.217  1.00 20.84           H  
ATOM   5170  N   ALA A 312      28.641  86.306  49.370  1.00 14.39           N  
ANISOU 5170  N   ALA A 312     1362   1786   2318     23     19    220       N  
ATOM   5171  CA  ALA A 312      28.268  85.377  48.313  1.00 14.92           C  
ANISOU 5171  CA  ALA A 312     1524   1748   2397    -38   -103    271       C  
ATOM   5172  C   ALA A 312      28.824  83.990  48.582  1.00 15.89           C  
ANISOU 5172  C   ALA A 312     1769   1759   2510     24   -208    182       C  
ATOM   5173  O   ALA A 312      28.203  82.986  48.214  1.00 16.71           O  
ANISOU 5173  O   ALA A 312     1800   1860   2689    -26   -250    -82       O  
ATOM   5174  CB  ALA A 312      28.789  85.881  46.969  1.00 16.78           C  
ANISOU 5174  CB  ALA A 312     1715   2095   2565     88     11    244       C  
ATOM   5175  H   ALA A 312      29.150  86.948  49.111  1.00 17.27           H  
ATOM   5176  HA  ALA A 312      27.301  85.324  48.269  1.00 17.91           H  
ATOM   5177  HB1 ALA A 312      28.549  85.243  46.278  1.00 20.14           H  
ATOM   5178  HB2 ALA A 312      28.386  86.742  46.778  1.00 20.14           H  
ATOM   5179  HB3 ALA A 312      29.753  85.969  47.017  1.00 20.14           H  
ATOM   5180  N   VAL A 313      29.998  83.903  49.208  1.00 15.79           N  
ANISOU 5180  N   VAL A 313     1663   1884   2453    -25   -168    156       N  
ATOM   5181  CA  VAL A 313      30.579  82.606  49.537  1.00 14.96           C  
ANISOU 5181  CA  VAL A 313     1620   1788   2278   -130    -57    175       C  
ATOM   5182  C   VAL A 313      30.267  82.175  50.968  1.00 15.63           C  
ANISOU 5182  C   VAL A 313     1617   1817   2504   -125    133     58       C  
ATOM   5183  O   VAL A 313      30.861  81.209  51.464  1.00 16.56           O  
ANISOU 5183  O   VAL A 313     1698   1861   2732    -60   -110    128       O  
ATOM   5184  CB  VAL A 313      32.087  82.547  49.228  1.00 14.74           C  
ANISOU 5184  CB  VAL A 313     1472   1834   2295    -61     -6     40       C  
ATOM   5185  CG1 VAL A 313      32.336  82.828  47.753  1.00 15.04           C  
ANISOU 5185  CG1 VAL A 313     1510   1966   2238    174     82    -99       C  
ATOM   5186  CG2 VAL A 313      32.886  83.500  50.101  1.00 15.07           C  
ANISOU 5186  CG2 VAL A 313     1401   1798   2529   -190    238     45       C  
ATOM   5187  H   VAL A 313      30.471  84.579  49.449  1.00 18.96           H  
ATOM   5188  HA  VAL A 313      30.160  81.948  48.959  1.00 17.96           H  
ATOM   5189  HB  VAL A 313      32.398  81.651  49.432  1.00 17.70           H  
ATOM   5190 HG11 VAL A 313      33.289  82.785  47.580  1.00 18.05           H  
ATOM   5191 HG12 VAL A 313      31.873  82.161  47.222  1.00 18.05           H  
ATOM   5192 HG13 VAL A 313      32.000  83.712  47.540  1.00 18.05           H  
ATOM   5193 HG21 VAL A 313      33.828  83.411  49.886  1.00 18.10           H  
ATOM   5194 HG22 VAL A 313      32.592  84.408  49.929  1.00 18.10           H  
ATOM   5195 HG23 VAL A 313      32.737  83.275  51.033  1.00 18.10           H  
ATOM   5196  N   GLY A 314      29.373  82.884  51.656  1.00 16.30           N  
ANISOU 5196  N   GLY A 314     1753   1978   2464   -132    257   -103       N  
ATOM   5197  CA  GLY A 314      28.895  82.427  52.941  1.00 17.07           C  
ANISOU 5197  CA  GLY A 314     1962   1953   2570   -223    320   -118       C  
ATOM   5198  C   GLY A 314      29.823  82.656  54.108  1.00 17.03           C  
ANISOU 5198  C   GLY A 314     2062   1970   2437   -184    267     72       C  
ATOM   5199  O   GLY A 314      29.698  81.969  55.130  1.00 17.75           O  
ANISOU 5199  O   GLY A 314     2220   2149   2376   -128    404    402       O  
ATOM   5200  H   GLY A 314      29.033  83.629  51.395  1.00 19.57           H  
ATOM   5201  HA2 GLY A 314      28.062  82.883  53.138  1.00 20.49           H  
ATOM   5202  HA3 GLY A 314      28.727  81.473  52.885  1.00 20.49           H  
ATOM   5203  N   VAL A 315      30.749  83.604  54.002  1.00 16.64           N  
ANISOU 5203  N   VAL A 315     2033   1969   2321   -121    288      8       N  
ATOM   5204  CA  VAL A 315      31.711  83.891  55.059  1.00 16.98           C  
ANISOU 5204  CA  VAL A 315     2111   2035   2306   -120    209    156       C  
ATOM   5205  C   VAL A 315      31.292  85.192  55.727  1.00 18.46           C  
ANISOU 5205  C   VAL A 315     2183   2304   2529   -151    288    170       C  
ATOM   5206  O   VAL A 315      31.343  86.257  55.104  1.00 18.74           O  
ANISOU 5206  O   VAL A 315     2338   2156   2625   -194    349    184       O  
ATOM   5207  CB  VAL A 315      33.130  83.981  54.497  1.00 16.77           C  
ANISOU 5207  CB  VAL A 315     2160   2085   2126    -10     49    315       C  
ATOM   5208  CG1 VAL A 315      34.099  84.454  55.560  1.00 17.56           C  
ANISOU 5208  CG1 VAL A 315     2278   2333   2063    -90     -1    361       C  
ATOM   5209  CG2 VAL A 315      33.548  82.631  53.945  1.00 16.71           C  
ANISOU 5209  CG2 VAL A 315     2124   2017   2206     18     43    437       C  
ATOM   5210  H   VAL A 315      30.840  84.104  53.308  1.00 19.98           H  
ATOM   5211  HA  VAL A 315      31.681  83.192  55.730  1.00 20.39           H  
ATOM   5212  HB  VAL A 315      33.150  84.628  53.775  1.00 20.13           H  
ATOM   5213 HG11 VAL A 315      35.005  84.293  55.256  1.00 21.09           H  
ATOM   5214 HG12 VAL A 315      33.963  85.402  55.711  1.00 21.09           H  
ATOM   5215 HG13 VAL A 315      33.933  83.962  56.380  1.00 21.09           H  
ATOM   5216 HG21 VAL A 315      34.456  82.695  53.609  1.00 20.06           H  
ATOM   5217 HG22 VAL A 315      33.504  81.972  54.655  1.00 20.06           H  
ATOM   5218 HG23 VAL A 315      32.946  82.384  53.225  1.00 20.06           H  
ATOM   5219  N   LYS A 316      30.861  85.110  56.984  1.00 21.82           N  
ANISOU 5219  N   LYS A 316     2583   2888   2821     19    660     13       N  
ATOM   5220  CA  LYS A 316      30.412  86.294  57.697  1.00 26.19           C  
ANISOU 5220  CA  LYS A 316     2967   3972   3014    -76    958   -327       C  
ATOM   5221  C   LYS A 316      31.481  86.813  58.626  1.00 27.73           C  
ANISOU 5221  C   LYS A 316     3296   4110   3131   -148   1036   -770       C  
ATOM   5222  O   LYS A 316      31.401  87.947  59.089  1.00 29.60           O  
ANISOU 5222  O   LYS A 316     3669   4138   3438   -163   1341   -847       O  
ATOM   5223  CB  LYS A 316      29.143  85.981  58.487  1.00 31.78           C  
ANISOU 5223  CB  LYS A 316     3467   4970   3638   -260    813   -279       C  
ATOM   5224  CG  LYS A 316      27.946  85.623  57.596  1.00 38.03           C  
ANISOU 5224  CG  LYS A 316     4276   5865   4308   -260    645    -63       C  
ATOM   5225  CD  LYS A 316      27.646  86.712  56.549  1.00 42.92           C  
ANISOU 5225  CD  LYS A 316     4941   6511   4857   -163    552    -46       C  
ATOM   5226  CE  LYS A 316      26.518  86.304  55.600  1.00 46.03           C  
ANISOU 5226  CE  LYS A 316     5402   6890   5196    -51    634   -153       C  
ATOM   5227  NZ  LYS A 316      26.873  85.142  54.729  1.00 47.57           N  
ANISOU 5227  NZ  LYS A 316     5575   7049   5449     71    920   -128       N  
ATOM   5228  OXT LYS A 316      32.441  86.106  58.920  1.00 28.90           O  
ANISOU 5228  OXT LYS A 316     3350   4522   3110   -248    494  -1073       O  
ATOM   5229  H   LYS A 316      30.820  84.382  57.440  1.00 26.20           H  
ATOM   5230  HA  LYS A 316      30.212  86.993  57.055  1.00 31.44           H  
ATOM   5231  HB2 LYS A 316      29.316  85.226  59.071  1.00 38.15           H  
ATOM   5232  HB3 LYS A 316      28.901  86.759  59.013  1.00 38.15           H  
ATOM   5233  HG2 LYS A 316      28.137  84.797  57.124  1.00 45.64           H  
ATOM   5234  HG3 LYS A 316      27.159  85.514  58.151  1.00 45.64           H  
ATOM   5235  HD2 LYS A 316      27.378  87.526  57.003  1.00 51.52           H  
ATOM   5236  HD3 LYS A 316      28.442  86.874  56.019  1.00 51.52           H  
ATOM   5237  HE2 LYS A 316      25.740  86.056  56.124  1.00 55.24           H  
ATOM   5238  HE3 LYS A 316      26.305  87.054  55.023  1.00 55.24           H  
ATOM   5239  HZ1 LYS A 316      26.203  84.964  54.170  1.00 57.09           H  
ATOM   5240  HZ2 LYS A 316      27.603  85.329  54.254  1.00 57.09           H  
ATOM   5241  HZ3 LYS A 316      27.031  84.423  55.229  1.00 57.09           H  
TER    5242      LYS A 316                                                      
HETATM 5243 CA    CA A 401      46.716  80.502  35.430  1.00 13.40          CA  
ANISOU 5243 CA    CA A 401     1534   2043   1515    313   -364   -203      CA  
HETATM 5244 CA    CA A 402      73.840  77.104  25.109  1.00 16.73          CA  
ANISOU 5244 CA    CA A 402     2356   2243   1756    680    453    115      CA  
HETATM 5245 CA    CA A 403      46.132  70.187  30.295  1.00 21.85          CA  
ANISOU 5245 CA    CA A 403     1984   3241   3078     28   -550  -1259      CA  
HETATM 5246 ZN    ZN A 404      50.579  76.286  47.835  1.00 14.20          ZN  
ANISOU 5246 ZN    ZN A 404     1873   1666   1858     82   -250    -15      ZN  
HETATM 5247 ZN    ZN A 405      27.823  80.897  40.885  0.63 50.20          ZN  
ANISOU 5247 ZN    ZN A 405    12133   3375   3565   1561    370     58      ZN  
HETATM 5248 ZN    ZN A 406      47.288  81.159  31.999  0.95 15.97          ZN  
ANISOU 5248 ZN    ZN A 406     1708   2746   1612    532   -315   -163      ZN  
HETATM 5249 ZN    ZN A 407      50.253  73.024  47.165  0.53 27.71          ZN  
ANISOU 5249 ZN    ZN A 407     2246   2364   5918   -255   1107  -1000      ZN  
HETATM 5250 ZN    ZN A 408      46.908  69.571  48.431  0.48 53.71          ZN  
ANISOU 5250 ZN    ZN A 408     5276   4436  10696   1436   3372   2710      ZN  
HETATM 5251 ZN    ZN A 409      52.759  74.029  46.448  0.43 25.96          ZN  
ANISOU 5251 ZN    ZN A 409     3527   2057   4278   -152    677    -82      ZN  
HETATM 5252 ZN    ZN A 410      30.451  83.228  39.188  0.75 80.09          ZN  
ANISOU 5252 ZN    ZN A 410     7001  12402  11027  -1313  -4239   3609      ZN  
HETATM 5253  O4A XYP A 411      80.860  79.395  41.502  0.81 36.75           O  
ANISOU 5253  O4A XYP A 411     3904   4573   5488   -762   -877    385       O  
HETATM 5254  C1B XYP A 411      80.717  78.099  41.080  0.81 33.75           C  
ANISOU 5254  C1B XYP A 411     3548   4214   5062   -846   -694    452       C  
HETATM 5255  C2B XYP A 411      79.399  77.555  41.576  0.81 32.79           C  
ANISOU 5255  C2B XYP A 411     3450   4290   4717   -664   -690    464       C  
HETATM 5256  C3B XYP A 411      79.148  76.196  41.030  0.81 28.93           C  
ANISOU 5256  C3B XYP A 411     2792   3912   4289   -703   -678    660       C  
HETATM 5257  C4B XYP A 411      79.266  76.172  39.552  0.81 29.08           C  
ANISOU 5257  C4B XYP A 411     2831   3823   4396   -546   -553    547       C  
HETATM 5258  C5B XYP A 411      80.549  76.771  39.022  0.81 30.00           C  
ANISOU 5258  C5B XYP A 411     2888   3920   4591   -527   -596    654       C  
HETATM 5259  O2B XYP A 411      79.392  77.469  43.010  0.81 34.98           O  
ANISOU 5259  O2B XYP A 411     3892   4643   4757   -473   -695    254       O  
HETATM 5260  O3B XYP A 411      77.794  75.810  41.403  0.81 25.61           O  
ANISOU 5260  O3B XYP A 411     2134   3740   3855   -562   -548   1128       O  
HETATM 5261  O4B XYP A 411      79.258  74.823  39.111  0.81 27.71           O  
ANISOU 5261  O4B XYP A 411     2737   3540   4252   -192   -556    159       O  
HETATM 5262  O5B XYP A 411      80.768  78.098  39.592  0.81 32.17           O  
ANISOU 5262  O5B XYP A 411     3268   3986   4969   -797   -545    672       O  
HETATM 5263 HO4A XYP A 411      81.718  79.624  41.468  0.81 44.11           H  
HETATM 5264  H1B XYP A 411      81.441  77.559  41.449  0.81 40.51           H  
HETATM 5265  H2B XYP A 411      78.692  78.172  41.309  0.81 39.35           H  
HETATM 5266  H3B XYP A 411      79.786  75.561  41.408  0.81 34.73           H  
HETATM 5267  H4B XYP A 411      78.504  76.673  39.206  0.81 34.90           H  
HETATM 5268 H5B1 XYP A 411      81.298  76.191  39.257  0.81 36.01           H  
HETATM 5269 H5B2 XYP A 411      80.495  76.841  38.050  0.81 36.01           H  
HETATM 5270 HO2B XYP A 411      78.808  78.052  43.339  0.81 41.99           H  
HETATM 5271 HO3B XYP A 411      77.818  75.047  41.857  0.81 30.73           H  
HETATM 5272 HO4B XYP A 411      78.495  74.654  38.690  0.81 33.26           H  
HETATM 5273  O4ABXYP A 412      22.268  80.744  49.544  0.83 36.91           O  
ANISOU 5273  O4ABXYP A 412     4050   6356   3619  -1352    442   -313       O  
HETATM 5274  C1BBXYP A 412      23.134  79.981  50.282  0.83 38.01           C  
ANISOU 5274  C1BBXYP A 412     4340   6402   3702  -1443    427   -335       C  
HETATM 5275  C2BBXYP A 412      22.466  79.547  51.567  0.83 40.31           C  
ANISOU 5275  C2BBXYP A 412     4858   6558   3901  -1179    403   -449       C  
HETATM 5276  C3BBXYP A 412      23.284  78.507  52.233  0.83 40.39           C  
ANISOU 5276  C3BBXYP A 412     4872   6501   3972  -1304    379   -366       C  
HETATM 5277  C4BBXYP A 412      23.422  77.348  51.313  0.83 41.05           C  
ANISOU 5277  C4BBXYP A 412     4878   6662   4058  -1181    352   -238       C  
HETATM 5278  C5BBXYP A 412      24.195  77.735  50.069  0.83 40.10           C  
ANISOU 5278  C5BBXYP A 412     4697   6623   3918  -1352    208   -290       C  
HETATM 5279  O2BBXYP A 412      22.341  80.678  52.447  0.83 42.27           O  
ANISOU 5279  O2BBXYP A 412     5276   6791   3992   -802    568   -462       O  
HETATM 5280  O3BBXYP A 412      22.669  78.081  53.468  0.83 40.92           O  
ANISOU 5280  O3BBXYP A 412     4945   6490   4111  -1311    313   -498       O  
HETATM 5281  O4BBXYP A 412      24.108  76.292  51.970  0.83 43.30           O  
ANISOU 5281  O4BBXYP A 412     5186   6880   4387   -930    268   -268       O  
HETATM 5282  O5BBXYP A 412      23.571  78.873  49.387  0.83 39.00           O  
ANISOU 5282  O5BBXYP A 412     4516   6510   3793  -1482    214   -265       O  
HETATM 5283 HO4ABXYP A 412      22.729  81.291  49.018  0.83 44.30           H  
HETATM 5284  H1BBXYP A 412      23.917  80.494  50.560  0.83 45.63           H  
HETATM 5285  H2BBXYP A 412      21.568  79.211  51.382  0.83 48.38           H  
HETATM 5286  H3BBXYP A 412      24.156  78.871  52.479  0.83 48.47           H  
HETATM 5287  H4BBXYP A 412      22.533  77.025  51.070  0.83 49.27           H  
HETATM 5288 H5B1BXYP A 412      24.223  76.973  49.460  0.83 48.13           H  
HETATM 5289 H5B2BXYP A 412      25.107  77.974  50.320  0.83 48.13           H  
HETATM 5290 HO2BBXYP A 412      21.481  80.874  52.557  0.83 50.73           H  
HETATM 5291 HO3BBXYP A 412      23.200  78.288  54.150  0.83 49.11           H  
HETATM 5292 HO4BBXYP A 412      23.681  75.527  51.827  0.83 51.97           H  
HETATM 5293  O4A XYP A 413      63.295  74.373  23.448  0.70 32.25           O  
ANISOU 5293  O4A XYP A 413     4723   4369   3161     10  -1066   -818       O  
HETATM 5294  C1B XYP A 413      62.154  74.014  24.114  0.70 32.43           C  
ANISOU 5294  C1B XYP A 413     4698   4338   3285     49  -1290   -698       C  
HETATM 5295  C2B XYP A 413      61.072  73.673  23.111  0.70 33.13           C  
ANISOU 5295  C2B XYP A 413     4777   4425   3386    274  -1149   -528       C  
HETATM 5296  C3B XYP A 413      59.836  73.230  23.804  0.70 33.40           C  
ANISOU 5296  C3B XYP A 413     4633   4451   3607    207  -1142   -634       C  
HETATM 5297  C4B XYP A 413      60.082  72.105  24.755  0.70 33.42           C  
ANISOU 5297  C4B XYP A 413     4656   4358   3686     96  -1080   -661       C  
HETATM 5298  C5B XYP A 413      61.239  72.395  25.700  0.70 32.91           C  
ANISOU 5298  C5B XYP A 413     4652   4260   3592     28  -1150   -749       C  
HETATM 5299  O2B XYP A 413      60.865  74.853  22.320  0.70 32.85           O  
ANISOU 5299  O2B XYP A 413     4885   4458   3140    498  -1084   -352       O  
HETATM 5300  O3B XYP A 413      58.896  72.787  22.790  0.70 33.87           O  
ANISOU 5300  O3B XYP A 413     4565   4619   3685    218  -1106   -900       O  
HETATM 5301  O4B XYP A 413      58.932  71.848  25.573  0.70 33.72           O  
ANISOU 5301  O4B XYP A 413     4729   4353   3732    -22  -1061   -725       O  
HETATM 5302  O5B XYP A 413      62.432  72.836  24.968  0.70 32.42           O  
ANISOU 5302  O5B XYP A 413     4662   4209   3446     57  -1285   -758       O  
HETATM 5303 HO4A XYP A 413      63.968  74.434  24.024  0.70 38.71           H  
HETATM 5304  H1B XYP A 413      61.882  74.774  24.663  0.70 38.92           H  
HETATM 5305  H2B XYP A 413      61.329  72.952  22.506  0.70 39.77           H  
HETATM 5306  H3B XYP A 413      59.461  73.978  24.306  0.70 40.09           H  
HETATM 5307  H4B XYP A 413      60.262  71.315  24.210  0.70 40.12           H  
HETATM 5308 H5B1 XYP A 413      60.972  73.094  26.327  0.70 39.50           H  
HETATM 5309 H5B2 XYP A 413      61.453  71.585  26.201  0.70 39.50           H  
HETATM 5310 HO2B XYP A 413      61.029  74.671  21.467  0.70 39.43           H  
HETATM 5311 HO3B XYP A 413      58.148  73.262  22.852  0.70 40.65           H  
HETATM 5312 HO4B XYP A 413      58.757  70.977  25.572  0.70 40.48           H  
HETATM 5313  O4A XYP A 414      35.994  75.026  58.919  0.78 31.71           O  
ANISOU 5313  O4A XYP A 414     4853   3194   4001  -1613   -104    411       O  
HETATM 5314  C1B XYP A 414      37.162  74.312  58.918  0.78 31.99           C  
ANISOU 5314  C1B XYP A 414     5137   3272   3745  -1531    170    405       C  
HETATM 5315  C2B XYP A 414      36.897  72.874  59.318  0.78 30.85           C  
ANISOU 5315  C2B XYP A 414     5015   3210   3497  -1294    499    696       C  
HETATM 5316  C3B XYP A 414      38.117  72.037  59.184  0.78 30.71           C  
ANISOU 5316  C3B XYP A 414     5041   3179   3450  -1270    620    666       C  
HETATM 5317  C4B XYP A 414      38.748  72.149  57.840  0.78 31.52           C  
ANISOU 5317  C4B XYP A 414     5150   3410   3416  -1225    442    310       C  
HETATM 5318  C5B XYP A 414      38.981  73.596  57.447  0.78 31.36           C  
ANISOU 5318  C5B XYP A 414     5162   3296   3456  -1449    244    199       C  
HETATM 5319  O2B XYP A 414      36.441  72.860  60.682  0.78 31.33           O  
ANISOU 5319  O2B XYP A 414     4833   3527   3543  -1029    654    672       O  
HETATM 5320  O3B XYP A 414      37.750  70.650  59.435  0.78 30.75           O  
ANISOU 5320  O3B XYP A 414     5114   2935   3633   -960    664    730       O  
HETATM 5321  O4B XYP A 414      40.025  71.500  57.846  0.78 31.59           O  
ANISOU 5321  O4B XYP A 414     5039   3574   3390  -1149    478     83       O  
HETATM 5322  O5B XYP A 414      37.747  74.390  57.559  0.78 32.67           O  
ANISOU 5322  O5B XYP A 414     5374   3425   3613  -1598    158    302       O  
HETATM 5323 HO4A XYP A 414      36.101  75.768  59.394  0.78 38.06           H  
HETATM 5324  H1B XYP A 414      37.765  74.708  59.574  0.78 38.39           H  
HETATM 5325  H2B XYP A 414      36.197  72.494  58.754  0.78 37.03           H  
HETATM 5326  H3B XYP A 414      38.774  72.322  59.848  0.78 36.86           H  
HETATM 5327  H4B XYP A 414      38.162  71.709  57.195  0.78 37.84           H  
HETATM 5328 H5B1 XYP A 414      39.662  73.980  58.031  0.78 37.64           H  
HETATM 5329 H5B2 XYP A 414      39.300  73.629  56.525  0.78 37.64           H  
HETATM 5330 HO2B XYP A 414      35.605  72.562  60.712  0.78 37.60           H  
HETATM 5331 HO3B XYP A 414      38.203  70.346  60.135  0.78 36.90           H  
HETATM 5332 HO4B XYP A 414      40.040  70.869  57.222  0.78 37.92           H  
HETATM 5333  O4A XYP A 415      53.361  96.186  64.578  0.88 29.05           O  
ANISOU 5333  O4A XYP A 415     2788   3631   4618  -1668   -205    126       O  
HETATM 5334  C1B XYP A 415      52.045  96.444  64.364  0.88 31.85           C  
ANISOU 5334  C1B XYP A 415     3031   3991   5081  -1034    -32   -229       C  
HETATM 5335  C2B XYP A 415      51.450  95.194  63.759  0.88 31.36           C  
ANISOU 5335  C2B XYP A 415     2830   3818   5267   -792     65   -294       C  
HETATM 5336  C3B XYP A 415      50.033  95.424  63.418  0.88 33.63           C  
ANISOU 5336  C3B XYP A 415     2965   4144   5668   -807   -111    -23       C  
HETATM 5337  C4B XYP A 415      49.234  95.830  64.602  0.88 36.38           C  
ANISOU 5337  C4B XYP A 415     3318   4593   5914   -604    165    -37       C  
HETATM 5338  C5B XYP A 415      49.876  96.970  65.378  0.88 36.75           C  
ANISOU 5338  C5B XYP A 415     3618   4741   5603   -469     21   -513       C  
HETATM 5339  O2B XYP A 415      52.212  94.824  62.608  0.88 28.04           O  
ANISOU 5339  O2B XYP A 415     2537   3260   4858   -581    484   -777       O  
HETATM 5340  O3B XYP A 415      49.534  94.149  62.964  0.88 32.22           O  
ANISOU 5340  O3B XYP A 415     2962   3550   5732  -1076   -385    365       O  
HETATM 5341  O4B XYP A 415      47.922  96.235  64.173  0.88 38.55           O  
ANISOU 5341  O4B XYP A 415     3582   4752   6313   -434    766    316       O  
HETATM 5342  O5B XYP A 415      51.317  96.775  65.619  0.88 34.74           O  
ANISOU 5342  O5B XYP A 415     3400   4579   5219   -809     60   -661       O  
HETATM 5343 HO4A XYP A 415      53.786  96.944  64.762  0.88 34.86           H  
HETATM 5344  H1B XYP A 415      51.997  97.223  63.777  0.88 38.23           H  
HETATM 5345  H2B XYP A 415      51.505  94.442  64.379  0.88 37.64           H  
HETATM 5346  H3B XYP A 415      49.949  96.115  62.733  0.88 40.36           H  
HETATM 5347  H4B XYP A 415      49.149  95.060  65.194  0.88 43.67           H  
HETATM 5348 H5B1 XYP A 415      49.754  97.797  64.874  0.88 44.10           H  
HETATM 5349 H5B2 XYP A 415      49.424  97.053  66.239  0.88 44.10           H  
HETATM 5350 HO2B XYP A 415      52.519  95.556  62.209  0.88 33.66           H  
HETATM 5351 HO3B XYP A 415      49.205  94.235  62.144  0.88 38.68           H  
HETATM 5352 HO4B XYP A 415      47.311  95.865  64.701  0.88 46.27           H  
HETATM 5353  O4A XYP A 416      79.469  89.756  39.416  0.84 55.99           O  
ANISOU 5353  O4A XYP A 416     5814   6800   8659    382    -57    215       O  
HETATM 5354  C1B XYP A 416      78.299  90.332  39.856  0.84 56.31           C  
ANISOU 5354  C1B XYP A 416     5861   6817   8717    130   -208    162       C  
HETATM 5355  C2B XYP A 416      78.289  90.334  41.371  0.84 56.28           C  
ANISOU 5355  C2B XYP A 416     5833   6834   8719     34   -201     77       C  
HETATM 5356  C3B XYP A 416      77.155  91.133  41.897  0.84 56.75           C  
ANISOU 5356  C3B XYP A 416     5826   6954   8783     40   -222     87       C  
HETATM 5357  C4B XYP A 416      77.243  92.529  41.396  0.84 56.85           C  
ANISOU 5357  C4B XYP A 416     5848   6933   8821     63   -248    111       C  
HETATM 5358  C5B XYP A 416      77.163  92.547  39.879  0.84 56.49           C  
ANISOU 5358  C5B XYP A 416     5836   6852   8776      7   -246    132       C  
HETATM 5359  O2B XYP A 416      78.172  88.991  41.866  0.84 55.80           O  
ANISOU 5359  O2B XYP A 416     5774   6764   8665    -74   -168      7       O  
HETATM 5360  O3B XYP A 416      77.187  91.119  43.345  0.84 57.32           O  
ANISOU 5360  O3B XYP A 416     5865   7079   8834     17   -195    136       O  
HETATM 5361  O4B XYP A 416      76.173  93.308  41.934  0.84 57.47           O  
ANISOU 5361  O4B XYP A 416     5912   7012   8910    107   -319    106       O  
HETATM 5362  O5B XYP A 416      78.200  91.702  39.262  0.84 56.69           O  
ANISOU 5362  O5B XYP A 416     5940   6836   8762     28   -285    170       O  
HETATM 5363 HO4A XYP A 416      79.350  88.881  39.320  0.84 67.20           H  
HETATM 5364  H1B XYP A 416      77.536  89.805  39.553  0.84 67.58           H  
HETATM 5365  H2B XYP A 416      79.135  90.701  41.689  0.84 67.55           H  
HETATM 5366  H3B XYP A 416      76.305  90.738  41.625  0.84 68.11           H  
HETATM 5367  H4B XYP A 416      78.078  92.934  41.698  0.84 68.23           H  
HETATM 5368 H5B1 XYP A 416      77.275  93.465  39.566  0.84 67.80           H  
HETATM 5369 H5B2 XYP A 416      76.285  92.223  39.603  0.84 67.80           H  
HETATM 5370 HO2B XYP A 416      78.921  88.765  42.287  0.84 66.97           H  
HETATM 5371 HO3B XYP A 416      76.434  90.764  43.654  0.84 68.79           H  
HETATM 5372 HO4B XYP A 416      76.484  94.098  42.194  0.84 68.97           H  
HETATM 5373  O4A XYP A 417      41.381  89.670  60.995  0.90 39.54           O  
ANISOU 5373  O4A XYP A 417     7637   5206   2180  -1855      2    220       O  
HETATM 5374  C1B XYP A 417      41.177  90.945  61.398  0.90 41.63           C  
ANISOU 5374  C1B XYP A 417     7751   5818   2248  -1819    334     96       C  
HETATM 5375  C2B XYP A 417      41.749  91.143  62.790  0.90 42.97           C  
ANISOU 5375  C2B XYP A 417     7836   6142   2349  -1942    394    231       C  
HETATM 5376  C3B XYP A 417      41.386  92.489  63.283  0.90 45.21           C  
ANISOU 5376  C3B XYP A 417     8094   6458   2626  -1909    510   -154       C  
HETATM 5377  C4B XYP A 417      41.797  93.582  62.361  0.90 45.42           C  
ANISOU 5377  C4B XYP A 417     8020   6412   2826  -1929    765   -393       C  
HETATM 5378  C5B XYP A 417      41.422  93.284  60.917  0.90 43.25           C  
ANISOU 5378  C5B XYP A 417     7773   6117   2542  -2032    713   -268       C  
HETATM 5379  O2B XYP A 417      41.238  90.095  63.615  0.90 43.50           O  
ANISOU 5379  O2B XYP A 417     7826   6281   2421  -1918    372    493       O  
HETATM 5380  O3B XYP A 417      42.043  92.644  64.568  0.90 47.13           O  
ANISOU 5380  O3B XYP A 417     8296   6716   2896  -1828    243   -338       O  
HETATM 5381  O4B XYP A 417      41.155  94.817  62.718  0.90 47.40           O  
ANISOU 5381  O4B XYP A 417     8083   6708   3219  -1856   1014   -620       O  
HETATM 5382  O5B XYP A 417      41.850  91.939  60.540  0.90 41.66           O  
ANISOU 5382  O5B XYP A 417     7654   5832   2342  -2074    563     -8       O  
HETATM 5383 HO4A XYP A 417      41.088  89.573  60.163  0.90 47.45           H  
HETATM 5384  H1B XYP A 417      40.208  91.046  61.350  0.90 49.96           H  
HETATM 5385  H2B XYP A 417      42.722  91.068  62.818  0.90 51.58           H  
HETATM 5386  H3B XYP A 417      40.418  92.563  63.386  0.90 54.26           H  
HETATM 5387  H4B XYP A 417      42.763  93.688  62.452  0.90 54.51           H  
HETATM 5388 H5B1 XYP A 417      40.454  93.355  60.814  0.90 51.91           H  
HETATM 5389 H5B2 XYP A 417      41.851  93.935  60.331  0.90 51.91           H  
HETATM 5390 HO2B XYP A 417      40.358  90.184  63.695  0.90 52.21           H  
HETATM 5391 HO3B XYP A 417      41.438  92.842  65.187  0.90 56.57           H  
HETATM 5392 HO4B XYP A 417      41.749  95.476  62.696  0.90 56.89           H  
HETATM 5393  O4A XYP A 418      42.646 107.915  50.876  0.80 65.92           O  
ANISOU 5393  O4A XYP A 418     8306   7402   9339   1003    464   -591       O  
HETATM 5394  C1B XYP A 418      41.652 107.027  51.218  0.80 66.01           C  
ANISOU 5394  C1B XYP A 418     8331   7393   9357   1003    412   -581       C  
HETATM 5395  C2B XYP A 418      41.150 107.365  52.606  0.80 66.21           C  
ANISOU 5395  C2B XYP A 418     8355   7439   9365    983    384   -542       C  
HETATM 5396  C3B XYP A 418      39.672 107.427  52.653  0.80 66.41           C  
ANISOU 5396  C3B XYP A 418     8328   7536   9370    858    379   -491       C  
HETATM 5397  C4B XYP A 418      39.154 108.462  51.720  0.80 66.58           C  
ANISOU 5397  C4B XYP A 418     8356   7575   9366    886    390   -473       C  
HETATM 5398  C5B XYP A 418      39.697 108.267  50.312  0.80 66.34           C  
ANISOU 5398  C5B XYP A 418     8334   7511   9362    921    386   -531       C  
HETATM 5399  O2B XYP A 418      41.607 106.364  53.530  0.80 66.11           O  
ANISOU 5399  O2B XYP A 418     8381   7366   9374   1046    329   -578       O  
HETATM 5400  O3B XYP A 418      39.263 107.746  54.010  0.80 66.77           O  
ANISOU 5400  O3B XYP A 418     8360   7621   9387    698    304   -469       O  
HETATM 5401  O4B XYP A 418      37.721 108.396  51.683  0.80 66.82           O  
ANISOU 5401  O4B XYP A 418     8422   7586   9380    914    394   -416       O  
HETATM 5402  O5B XYP A 418      40.577 107.087  50.186  0.80 66.03           O  
ANISOU 5402  O5B XYP A 418     8329   7393   9366    954    366   -580       O  
HETATM 5403 HO4A XYP A 418      43.284 107.488  50.429  0.80 79.12           H  
HETATM 5404  H1B XYP A 418      42.018 106.122  51.233  0.80 79.22           H  
HETATM 5405  H2B XYP A 418      41.517 108.228  52.876  0.80 79.46           H  
HETATM 5406  H3B XYP A 418      39.292 106.561  52.415  0.80 79.70           H  
HETATM 5407  H4B XYP A 418      39.413 109.345  52.047  0.80 79.90           H  
HETATM 5408 H5B1 XYP A 418      38.945 108.162  49.699  0.80 79.62           H  
HETATM 5409 H5B2 XYP A 418      40.204 109.062  50.059  0.80 79.62           H  
HETATM 5410 HO2B XYP A 418      42.249 106.703  54.041  0.80 79.34           H  
HETATM 5411 HO3B XYP A 418      38.843 107.049  54.364  0.80 80.13           H  
HETATM 5412 HO4B XYP A 418      37.384 109.200  51.852  0.80 80.19           H  
HETATM 5413  O4A XYP A 419      66.470  81.393  17.562  0.72 59.86           O  
ANISOU 5413  O4A XYP A 419     9614   8367   4762   -499   -586  -1621       O  
HETATM 5414  C1B XYP A 419      66.815  80.155  17.063  0.72 59.61           C  
ANISOU 5414  C1B XYP A 419     9585   8284   4780   -460   -537  -1739       C  
HETATM 5415  C2B XYP A 419      68.112  79.686  17.700  0.72 59.50           C  
ANISOU 5415  C2B XYP A 419     9559   8264   4786   -392   -414  -1744       C  
HETATM 5416  C3B XYP A 419      68.439  78.270  17.397  0.72 59.62           C  
ANISOU 5416  C3B XYP A 419     9503   8340   4810   -369   -409  -1743       C  
HETATM 5417  C4B XYP A 419      67.278  77.385  17.695  0.72 59.51           C  
ANISOU 5417  C4B XYP A 419     9509   8266   4837   -395   -490  -1784       C  
HETATM 5418  C5B XYP A 419      66.070  77.845  16.898  0.72 59.55           C  
ANISOU 5418  C5B XYP A 419     9530   8257   4838   -430   -529  -1792       C  
HETATM 5419  O2B XYP A 419      69.188  80.516  17.224  0.72 59.41           O  
ANISOU 5419  O2B XYP A 419     9584   8229   4759   -384   -301  -1739       O  
HETATM 5420  O3B XYP A 419      69.577  77.827  18.186  0.72 59.80           O  
ANISOU 5420  O3B XYP A 419     9453   8430   4837   -292   -296  -1684       O  
HETATM 5421  O4B XYP A 419      67.612  76.038  17.378  0.72 59.82           O  
ANISOU 5421  O4B XYP A 419     9519   8253   4957   -329   -483  -1712       O  
HETATM 5422  O5B XYP A 419      65.688  79.208  17.306  0.72 59.70           O  
ANISOU 5422  O5B XYP A 419     9574   8282   4826   -466   -560  -1773       O  
HETATM 5423 HO4A XYP A 419      65.863  81.767  17.033  0.72 71.84           H  
HETATM 5424  H1B XYP A 419      66.962  80.237  16.101  0.72 71.54           H  
HETATM 5425  H2B XYP A 419      68.024  79.780  18.668  0.72 71.41           H  
HETATM 5426  H3B XYP A 419      68.689  78.201  16.456  0.72 71.55           H  
HETATM 5427  H4B XYP A 419      67.066  77.398  18.648  0.72 71.42           H  
HETATM 5428 H5B1 XYP A 419      65.324  77.236  17.056  0.72 71.46           H  
HETATM 5429 H5B2 XYP A 419      66.287  77.839  15.946  0.72 71.46           H  
HETATM 5430 HO2B XYP A 419      69.510  80.999  17.897  0.72 71.30           H  
HETATM 5431 HO3B XYP A 419      70.249  77.617  17.646  0.72 71.76           H  
HETATM 5432 HO4B XYP A 419      67.302  75.498  18.011  0.72 71.79           H  
HETATM 5433  C1  XYS A 420      61.257  82.242  58.829  0.77 51.55           C  
ANISOU 5433  C1  XYS A 420     5538   8762   5288     90   -954   1484       C  
HETATM 5434  C2  XYS A 420      62.513  82.933  59.249  0.77 51.59           C  
ANISOU 5434  C2  XYS A 420     5582   8718   5302    172   -930   1451       C  
HETATM 5435  C3  XYS A 420      62.170  84.246  59.923  0.77 51.31           C  
ANISOU 5435  C3  XYS A 420     5618   8669   5209    159   -785   1583       C  
HETATM 5436  C4  XYS A 420      61.302  85.084  59.005  0.77 50.75           C  
ANISOU 5436  C4  XYS A 420     5649   8693   4940    110   -608   1609       C  
HETATM 5437  C5  XYS A 420      60.160  84.269  58.401  0.77 51.21           C  
ANISOU 5437  C5  XYS A 420     5565   8759   5132     13   -721   1538       C  
HETATM 5438  O1  XYS A 420      60.467  82.033  59.973  0.77 51.70           O  
ANISOU 5438  O1  XYS A 420     5530   8779   5333     21  -1028   1436       O  
HETATM 5439  O2  XYS A 420      63.163  82.107  60.189  0.77 52.18           O  
ANISOU 5439  O2  XYS A 420     5608   8743   5474    254   -979   1311       O  
HETATM 5440  O3  XYS A 420      63.359  84.942  60.213  0.77 51.94           O  
ANISOU 5440  O3  XYS A 420     5740   8630   5363    161   -728   1619       O  
HETATM 5441  O4  XYS A 420      60.784  86.200  59.694  0.77 49.65           O  
ANISOU 5441  O4  XYS A 420     5649   8630   4587    186   -353   1662       O  
HETATM 5442  O5  XYS A 420      60.553  82.985  57.950  0.77 51.99           O  
ANISOU 5442  O5  XYS A 420     5610   8850   5294    -58   -825   1416       O  
HETATM 5443  H2  XYS A 420      63.152  83.089  58.379  0.77 61.92           H  
HETATM 5444  H3  XYS A 420      61.638  84.029  60.849  0.77 61.58           H  
HETATM 5445  H4  XYS A 420      61.926  85.434  58.182  0.77 60.90           H  
HETATM 5446  H51 XYS A 420      59.740  84.822  57.561  0.77 61.46           H  
HETATM 5447  H52 XYS A 420      59.377  84.153  59.150  0.77 61.46           H  
HETATM 5448  HO2 XYS A 420      62.629  81.299  60.339  0.77 62.62           H  
HETATM 5449  HO3 XYS A 420      64.123  84.451  59.847  0.77 62.33           H  
HETATM 5450  HO4 XYS A 420      61.132  86.209  60.610  0.77 59.59           H  
HETATM 5451  C1 BXYS A 421      78.528  73.264  44.042  0.83 44.28           C  
ANISOU 5451  C1 BXYS A 421     6916   6151   3759   2063    300    149       C  
HETATM 5452  C2 BXYS A 421      77.515  72.325  44.641  0.83 44.55           C  
ANISOU 5452  C2 BXYS A 421     7031   6207   3688   2036    295    297       C  
HETATM 5453  C3 BXYS A 421      77.612  70.926  44.034  0.83 45.00           C  
ANISOU 5453  C3 BXYS A 421     7148   6078   3874   2163    163    480       C  
HETATM 5454  C4 BXYS A 421      77.635  71.001  42.513  0.83 45.35           C  
ANISOU 5454  C4 BXYS A 421     7083   6160   3988   2236    177    393       C  
HETATM 5455  C5 BXYS A 421      78.548  72.108  41.984  0.83 44.51           C  
ANISOU 5455  C5 BXYS A 421     6932   6167   3811   2136    278    375       C  
HETATM 5456  O1 BXYS A 421      79.836  72.878  44.415  0.83 44.74           O  
ANISOU 5456  O1 BXYS A 421     6851   6208   3940   2071    361    -70       O  
HETATM 5457  O2 BXYS A 421      77.769  72.256  46.028  0.83 44.43           O  
ANISOU 5457  O2 BXYS A 421     6997   6336   3549   1927    403    211       O  
HETATM 5458  O3 BXYS A 421      76.507  70.132  44.429  0.83 44.43           O  
ANISOU 5458  O3 BXYS A 421     7115   5830   3936   2311     91    590       O  
HETATM 5459  O4 BXYS A 421      78.027  69.757  41.963  0.83 45.96           O  
ANISOU 5459  O4 BXYS A 421     7003   6197   4262   2464     -5    513       O  
HETATM 5460  O5 BXYS A 421      78.437  73.335  42.689  0.83 43.35           O  
ANISOU 5460  O5 BXYS A 421     6810   6030   3633   2146    372    348       O  
HETATM 5461  H2 BXYS A 421      76.510  72.706  44.459  0.83 53.46           H  
HETATM 5462  H3 BXYS A 421      78.529  70.465  44.401  0.83 54.01           H  
HETATM 5463  H4 BXYS A 421      76.626  71.238  42.173  0.83 54.43           H  
HETATM 5464  H51BXYS A 421      78.310  72.286  40.935  0.83 53.41           H  
HETATM 5465  H52BXYS A 421      79.581  71.765  42.040  0.83 53.41           H  
HETATM 5466  HO2BXYS A 421      78.513  72.852  46.254  0.83 53.33           H  
HETATM 5467  HO3BXYS A 421      75.916  70.659  45.006  0.83 53.32           H  
HETATM 5468  HO4BXYS A 421      78.172  69.112  42.686  0.83 55.16           H  
HETATM 5469  O   HOH A 501      74.040  93.207  42.091  0.94 49.11           O  
HETATM 5470  O   HOH A 502      47.112  90.340  26.966  1.00 55.18           O  
HETATM 5471  O   HOH A 503      48.428  80.726  25.510  0.79 26.43           O  
HETATM 5472  O   HOH A 504      50.741  60.645  35.651  0.87 44.64           O  
HETATM 5473  O  AHOH A 505      32.088  77.104  41.536  0.48 18.32           O  
HETATM 5474  O   HOH A 506      48.442  94.072  26.988  0.83 34.15           O  
HETATM 5475  O   HOH A 507      78.171  91.958  36.951  0.83 34.30           O  
HETATM 5476  O   HOH A 508      46.695  83.737  65.266  0.79 22.92           O  
HETATM 5477  O  AHOH A 509      39.832  74.920  33.562  0.76 33.35           O  
HETATM 5478  O   HOH A 510      38.775  80.629  34.938  0.88 41.42           O  
HETATM 5479  O   HOH A 511      68.386  58.282  38.284  0.84 45.44           O  
HETATM 5480  O   HOH A 512      51.724  96.220  60.690  0.97 39.15           O  
HETATM 5481  O  BHOH A 513      37.326  77.811  34.889  1.00 50.23           O  
HETATM 5482  O   HOH A 514      74.310  67.527  42.374  1.00 45.73           O  
HETATM 5483  O   HOH A 515      77.498  68.792  39.777  0.87 28.11           O  
HETATM 5484  O  AHOH A 516      77.842  74.765  37.114  0.65 17.38           O  
HETATM 5485  O  BHOH A 516      76.430  74.299  35.780  0.35 19.62           O  
HETATM 5486  O   HOH A 517      61.049  99.987  47.946  0.99 48.07           O  
HETATM 5487  O   HOH A 518      22.745  75.343  53.806  0.91 26.22           O  
HETATM 5488  O   HOH A 519      38.555  62.670  52.726  0.98 39.36           O  
HETATM 5489  O   HOH A 520      47.185  87.091  25.269  0.87 22.91           O  
HETATM 5490  O   HOH A 521      29.965  90.008  58.962  1.00 46.14           O  
HETATM 5491  O   HOH A 522      65.233  75.580  53.605  1.00 36.20           O  
HETATM 5492  O   HOH A 523      72.885  72.384  33.570  0.83 16.14           O  
HETATM 5493  O  AHOH A 524      44.050  85.914  64.476  0.58 24.88           O  
HETATM 5494  O  BHOH A 524      43.394  84.618  64.982  0.42 35.81           O  
HETATM 5495  O   HOH A 525      23.274  83.046  49.206  0.97 22.89           O  
HETATM 5496  O   HOH A 526      19.760  80.571  49.888  1.00 29.10           O  
HETATM 5497  O   HOH A 527      27.820  83.187  38.938  0.76 28.91           O  
HETATM 5498  O   HOH A 528      27.525  92.125  54.124  0.90 26.52           O  
HETATM 5499  O   HOH A 529      66.863  67.394  49.181  0.92 36.36           O  
HETATM 5500  O   HOH A 530      47.877  93.114  41.720  1.00 17.85           O  
HETATM 5501  O   HOH A 531      55.522  96.071  50.943  0.98 25.36           O  
HETATM 5502  O   HOH A 532      71.301  67.621  42.920  1.00 24.10           O  
HETATM 5503  O   HOH A 533      57.382  78.372  28.639  0.92 18.03           O  
HETATM 5504  O   HOH A 534      51.850  94.565  33.362  0.97 32.84           O  
HETATM 5505  O   HOH A 535      85.883  82.183  34.957  0.78 33.50           O  
HETATM 5506  O  AHOH A 536      49.354  81.424  31.964  1.00 14.78           O  
HETATM 5507  O   HOH A 537      26.974  93.927  52.042  1.00 47.17           O  
HETATM 5508  O   HOH A 538      54.367 100.743  44.046  0.95 51.26           O  
HETATM 5509  O   HOH A 539      38.616  68.543  44.978  0.98 58.06           O  
HETATM 5510  O   HOH A 540      54.397  97.990  36.543  1.00 44.45           O  
HETATM 5511  O   HOH A 541      56.521  60.000  38.791  0.96 38.74           O  
HETATM 5512  O   HOH A 542      62.529  71.153  36.497  1.00 15.34           O  
HETATM 5513  O  AHOH A 543      24.957  74.407  50.869  0.44 15.45           O  
HETATM 5514  O  BHOH A 543      25.479  73.570  50.211  0.56 20.46           O  
HETATM 5515  O   HOH A 544      58.918  91.630  34.299  0.93 36.75           O  
HETATM 5516  O   HOH A 545      68.189  92.966  31.165  0.88 39.28           O  
HETATM 5517  O   HOH A 546      65.132  82.793  61.771  0.77 33.28           O  
HETATM 5518  O   HOH A 547      53.557  80.916  56.990  1.00 23.89           O  
HETATM 5519  O   HOH A 548      72.543  75.263  29.136  1.00 15.42           O  
HETATM 5520  O   HOH A 549      82.021  79.839  27.030  1.00 31.78           O  
HETATM 5521  O   HOH A 550      64.743  75.566  25.299  1.00 19.85           O  
HETATM 5522  O  BHOH A 551      31.657  92.336  35.692  0.40 15.62           O  
HETATM 5523  O   HOH A 552      34.407 106.745  52.960  0.86 29.03           O  
HETATM 5524  O  BHOH A 553      53.270  79.820  53.589  0.57 24.40           O  
HETATM 5525  O  AHOH A 554      25.032  92.057  47.083  0.79 27.51           O  
HETATM 5526  O   HOH A 555      65.148  95.789  56.923  1.00 15.65           O  
HETATM 5527  O   HOH A 556      68.077  81.352  50.240  0.90 30.44           O  
HETATM 5528  O   HOH A 557      49.284  99.273  40.611  1.00 39.69           O  
HETATM 5529  O   HOH A 558      49.643  92.818  25.464  0.98 36.18           O  
HETATM 5530  O   HOH A 559      41.719  66.840  33.515  1.00 32.30           O  
HETATM 5531  O   HOH A 560      73.763  87.820  46.606  0.87 31.50           O  
HETATM 5532  O   HOH A 561      76.011  75.485  44.227  0.94 33.14           O  
HETATM 5533  O  AHOH A 562      50.762  85.764  31.482  0.86 19.31           O  
HETATM 5534  O   HOH A 563      53.132  80.143  32.318  1.00 16.01           O  
HETATM 5535  O   HOH A 564      41.908  71.447  44.737  0.90 24.72           O  
HETATM 5536  O   HOH A 565      45.890  72.486  30.933  1.00 19.33           O  
HETATM 5537  O   HOH A 566      66.011  93.649  35.101  0.99 27.09           O  
HETATM 5538  O   HOH A 567      60.484  73.001  35.867  0.96 19.16           O  
HETATM 5539  O   HOH A 568      61.707  80.284  40.080  1.00 12.56           O  
HETATM 5540  O   HOH A 569      55.403  79.327  30.035  1.00 19.39           O  
HETATM 5541  O   HOH A 570      71.244  87.792  23.811  1.00 49.63           O  
HETATM 5542  O   HOH A 571      55.079  65.298  27.971  1.00 39.00           O  
HETATM 5543  O   HOH A 572      65.884  81.498  40.435  1.00 14.19           O  
HETATM 5544  O   HOH A 573      73.286  63.683  38.303  0.88 17.68           O  
HETATM 5545  O   HOH A 574      43.777 100.857  40.920  0.96 21.16           O  
HETATM 5546  O   HOH A 575      67.463  89.397  53.071  0.96 24.36           O  
HETATM 5547  O   HOH A 576      64.597  89.337  30.404  0.94 23.06           O  
HETATM 5548  O   HOH A 577      73.841  76.436  22.818  1.00 19.83           O  
HETATM 5549  O   HOH A 578      44.872  84.717  28.246  1.00 20.58           O  
HETATM 5550  O   HOH A 579      31.339  67.905  57.362  0.99 36.92           O  
HETATM 5551  O   HOH A 580      73.756  89.033  42.085  1.00 26.92           O  
HETATM 5552  O   HOH A 581      50.583  63.123  27.049  1.00 58.22           O  
HETATM 5553  O   HOH A 582      27.704  80.181  55.500  1.00 36.55           O  
HETATM 5554  O   HOH A 583      44.539  90.663  30.469  0.92 21.54           O  
HETATM 5555  O   HOH A 584      58.838 100.203  44.065  0.79 36.90           O  
HETATM 5556  O   HOH A 585      26.340  96.494  49.024  1.00 44.90           O  
HETATM 5557  O   HOH A 586      62.735  95.124  39.012  1.00 35.06           O  
HETATM 5558  O   HOH A 587      56.272  83.560  60.281  0.90 24.16           O  
HETATM 5559  O   HOH A 588      59.586 100.050  41.028  1.00 43.98           O  
HETATM 5560  O   HOH A 589      41.162  73.781  54.777  0.98 20.14           O  
HETATM 5561  O   HOH A 590      41.175  70.992  22.070  1.00 53.63           O  
HETATM 5562  O   HOH A 591      40.994 103.159  58.088  0.98 32.28           O  
HETATM 5563  O   HOH A 592      23.366  83.648  41.615  1.00 21.73           O  
HETATM 5564  O   HOH A 593      60.232  91.956  44.748  1.00 15.28           O  
HETATM 5565  O   HOH A 594      52.482  98.043  49.446  0.97 20.83           O  
HETATM 5566  O   HOH A 595      37.685 105.983  47.593  0.87 31.14           O  
HETATM 5567  O   HOH A 596      40.982  70.882  42.261  0.80 29.37           O  
HETATM 5568  O  BHOH A 597      29.319  94.531  45.332  0.42 15.60           O  
HETATM 5569  O   HOH A 598      51.002  99.978  42.765  1.00 37.95           O  
HETATM 5570  O   HOH A 599      71.883  72.039  27.379  1.00 20.92           O  
HETATM 5571  O   HOH A 600      48.429  64.555  29.635  1.00 30.21           O  
HETATM 5572  O   HOH A 601      61.676  65.545  38.051  1.00 16.55           O  
HETATM 5573  O   HOH A 602      39.904  68.971  59.349  0.97 39.28           O  
HETATM 5574  O   HOH A 603      31.110  86.230  37.686  0.97 32.78           O  
HETATM 5575  O   HOH A 604      40.717  89.923  35.067  0.88 37.85           O  
HETATM 5576  O   HOH A 605      34.526  99.942  57.271  0.95 29.61           O  
HETATM 5577  O   HOH A 606      49.674  77.470  27.556  1.00 43.65           O  
HETATM 5578  O   HOH A 607      31.073 100.868  51.733  1.00 21.36           O  
HETATM 5579  O   HOH A 608      50.071  77.583  34.311  1.00 15.76           O  
HETATM 5580  O   HOH A 609      64.466  82.338  53.117  0.80 30.34           O  
HETATM 5581  O   HOH A 610      61.580  97.546  39.084  0.90 27.73           O  
HETATM 5582  O   HOH A 611      47.534  97.867  62.007  1.00 51.12           O  
HETATM 5583  O  AHOH A 612      43.496  88.029  61.688  0.59 26.27           O  
HETATM 5584  O  BHOH A 612      43.425  86.678  62.999  0.41 23.50           O  
HETATM 5585  O   HOH A 613      36.549  67.382  45.513  0.79 33.64           O  
HETATM 5586  O   HOH A 614      48.567  69.434  51.994  0.88 33.86           O  
HETATM 5587  O   HOH A 615      42.993  77.144  61.052  1.00 32.34           O  
HETATM 5588  O   HOH A 616      47.613  95.481  43.016  1.00 19.48           O  
HETATM 5589  O   HOH A 617      36.810 104.611  45.703  1.00 43.85           O  
HETATM 5590  O   HOH A 618      39.812 105.194  55.776  1.00 43.87           O  
HETATM 5591  O   HOH A 619      63.427  64.878  36.080  0.95 25.21           O  
HETATM 5592  O   HOH A 620      50.778  82.056  50.666  1.00 12.63           O  
HETATM 5593  O   HOH A 621      37.534  99.835  40.420  1.00 21.22           O  
HETATM 5594  O   HOH A 622      64.221  68.279  49.181  0.80 34.10           O  
HETATM 5595  O   HOH A 623      42.062  68.948  37.813  1.00 30.92           O  
HETATM 5596  O   HOH A 624      44.804  76.210  46.542  0.96 15.24           O  
HETATM 5597  O   HOH A 625      41.655  84.074  30.011  0.93 19.84           O  
HETATM 5598  O   HOH A 626      68.065  84.013  49.793  0.97 23.58           O  
HETATM 5599  O   HOH A 627      57.687  98.861  51.215  0.90 38.85           O  
HETATM 5600  O   HOH A 628      61.842  94.830  34.932  0.99 51.99           O  
HETATM 5601  O   HOH A 629      58.092  93.761  34.455  1.00 47.50           O  
HETATM 5602  O   HOH A 630      36.771  97.414  59.190  0.94 27.34           O  
HETATM 5603  O   HOH A 631      43.622  68.217  47.951  0.86 28.43           O  
HETATM 5604  O   HOH A 632      83.548  79.500  35.560  0.96 35.91           O  
HETATM 5605  O   HOH A 633      55.301  74.936  49.466  1.00 51.84           O  
HETATM 5606  O   HOH A 634      45.026  66.821  58.725  1.00 39.58           O  
HETATM 5607  O   HOH A 635      66.154  61.144  33.581  1.00 55.33           O  
HETATM 5608  O   HOH A 636      54.029  72.443  46.605  0.93 29.02           O  
HETATM 5609  O   HOH A 637      38.918  93.342  35.742  1.00 15.94           O  
HETATM 5610  O   HOH A 638      31.884 100.327  55.991  0.85 34.53           O  
HETATM 5611  O   HOH A 639      30.622  71.591  54.967  0.90 30.41           O  
HETATM 5612  O   HOH A 640      65.767  81.932  47.491  1.00 14.50           O  
HETATM 5613  O   HOH A 641      69.271  90.759  51.883  0.89 40.27           O  
HETATM 5614  O  BHOH A 642      31.455  78.517  41.555  0.51 16.79           O  
HETATM 5615  O   HOH A 643      58.254  65.885  31.708  1.00 28.25           O  
HETATM 5616  O   HOH A 644      69.016  75.587  49.698  1.00 52.79           O  
HETATM 5617  O   HOH A 645      46.136  82.406  36.792  1.00 12.64           O  
HETATM 5618  O   HOH A 646      72.253  75.309  25.126  1.00 19.26           O  
HETATM 5619  O   HOH A 647      59.675  61.423  41.637  0.97 41.21           O  
HETATM 5620  O   HOH A 648      72.023  91.022  32.941  1.00 22.16           O  
HETATM 5621  O   HOH A 649      59.905  80.908  53.867  1.00 21.68           O  
HETATM 5622  O   HOH A 650      38.664  74.043  41.447  0.96 14.47           O  
HETATM 5623  O   HOH A 651      69.387  60.677  39.338  0.89 20.02           O  
HETATM 5624  O   HOH A 652      81.273  75.228  44.049  0.97 32.97           O  
HETATM 5625  O   HOH A 653      60.459  95.839  50.682  0.94 15.87           O  
HETATM 5626  O   HOH A 654      36.861  94.744  59.582  1.00 22.69           O  
HETATM 5627  O   HOH A 655      74.800  73.905  29.580  1.00 19.92           O  
HETATM 5628  O   HOH A 656      50.475  90.091  58.955  0.97 15.50           O  
HETATM 5629  O   HOH A 657      39.596 104.166  41.044  1.00 40.29           O  
HETATM 5630  O   HOH A 658      41.337  97.392  40.142  1.00 15.00           O  
HETATM 5631  O   HOH A 659      71.575  77.651  20.312  0.96 28.54           O  
HETATM 5632  O   HOH A 660      65.877  86.495  36.192  1.00 20.95           O  
HETATM 5633  O   HOH A 661      46.200  91.526  63.444  0.94 19.51           O  
HETATM 5634  O   HOH A 662      73.838  94.120  36.518  1.00 40.41           O  
HETATM 5635  O   HOH A 663      66.358  96.878  44.891  0.99 33.39           O  
HETATM 5636  O   HOH A 664      50.256  97.310  47.823  1.00 20.26           O  
HETATM 5637  O   HOH A 665      83.949  88.185  33.014  1.00 41.11           O  
HETATM 5638  O   HOH A 666      44.505 104.198  48.368  1.00 36.47           O  
HETATM 5639  O   HOH A 667      81.351  83.940  24.512  0.98 35.48           O  
HETATM 5640  O   HOH A 668      70.651  94.436  41.925  1.00 29.56           O  
HETATM 5641  O   HOH A 669      25.720  94.438  44.288  0.98 40.07           O  
HETATM 5642  O   HOH A 670      66.813  89.718  45.259  1.00 21.40           O  
HETATM 5643  O   HOH A 671      58.041  90.807  55.620  0.95 21.65           O  
HETATM 5644  O   HOH A 672      65.613  86.200  54.167  0.94 26.84           O  
HETATM 5645  O  AHOH A 673      25.434  91.356  50.073  1.00 34.98           O  
HETATM 5646  O   HOH A 674      27.127  72.804  55.755  1.00 27.77           O  
HETATM 5647  O   HOH A 675      61.973  88.320  34.154  0.98 19.06           O  
HETATM 5648  O   HOH A 676      34.339  66.803  54.887  0.97 21.85           O  
HETATM 5649  O  AHOH A 677      30.683  91.855  36.615  0.72 22.27           O  
HETATM 5650  O   HOH A 678      35.400 106.867  50.467  0.97 44.53           O  
HETATM 5651  O   HOH A 679      62.171  70.650  29.044  0.86 25.34           O  
HETATM 5652  O   HOH A 680      53.647  74.946  23.454  0.95 48.60           O  
HETATM 5653  O  AHOH A 681      52.916  82.261  30.547  0.84 23.37           O  
HETATM 5654  O   HOH A 682      58.170  85.507  60.523  0.97 36.83           O  
HETATM 5655  O   HOH A 683      74.061  69.497  40.525  0.84 24.59           O  
HETATM 5656  O   HOH A 684      59.836  88.664  58.665  0.95 23.80           O  
HETATM 5657  O   HOH A 685      26.394  76.352  48.910  0.79 22.32           O  
HETATM 5658  O   HOH A 686      34.054  88.830  59.634  1.00 21.75           O  
HETATM 5659  O   HOH A 687      35.648  81.348  59.769  1.00 20.01           O  
HETATM 5660  O   HOH A 688      27.171  92.354  39.668  0.98 39.80           O  
HETATM 5661  O   HOH A 689      66.304  86.935  33.552  1.00 19.02           O  
HETATM 5662  O  AHOH A 690      42.695  83.515  65.075  0.49 26.50           O  
HETATM 5663  O  BHOH A 690      42.062  82.579  64.824  0.51 38.57           O  
HETATM 5664  O   HOH A 691      43.882  99.539  61.760  1.00 49.95           O  
HETATM 5665  O   HOH A 692      75.967  88.203  43.488  0.91 32.94           O  
HETATM 5666  O   HOH A 693      48.191  97.419  49.630  1.00 18.52           O  
HETATM 5667  O   HOH A 694      27.533  98.131  45.436  0.94 27.23           O  
HETATM 5668  O   HOH A 695      64.127  89.734  55.880  0.84 26.45           O  
HETATM 5669  O   HOH A 696      39.901  77.431  43.471  0.98 14.48           O  
HETATM 5670  O   HOH A 697      39.214  70.101  29.523  1.00 39.20           O  
HETATM 5671  O   HOH A 698      28.368  96.152  57.001  0.97 47.15           O  
HETATM 5672  O   HOH A 699      68.782  96.950  38.060  0.81 38.55           O  
HETATM 5673  O   HOH A 700      39.849  82.037  33.423  0.87 26.17           O  
HETATM 5674  O   HOH A 701      60.997  63.488  34.299  0.98 47.70           O  
HETATM 5675  O  AHOH A 702      57.467  84.495  28.929  0.94 30.61           O  
HETATM 5676  O   HOH A 703      39.625  68.820  43.245  0.98 48.50           O  
HETATM 5677  O   HOH A 704      50.214  84.289  23.668  0.98 30.77           O  
HETATM 5678  O   HOH A 705      33.223  89.731  34.703  0.97 36.76           O  
HETATM 5679  O   HOH A 706      67.064  95.735  53.373  0.98 33.54           O  
HETATM 5680  O   HOH A 707      54.378  59.296  37.765  0.83 35.88           O  
HETATM 5681  O   HOH A 708      33.453 104.410  45.921  0.96 30.41           O  
HETATM 5682  O   HOH A 709      43.901 101.458  60.052  0.95 36.57           O  
HETATM 5683  O   HOH A 710      31.361  73.064  45.275  0.93 19.69           O  
HETATM 5684  O   HOH A 711      70.549  68.859  49.726  1.00 28.53           O  
HETATM 5685  O   HOH A 712      67.690  74.163  50.005  1.00 29.58           O  
HETATM 5686  O   HOH A 713      67.377  69.915  22.749  1.00 30.43           O  
HETATM 5687  O   HOH A 714      30.650  93.893  38.170  1.00 21.01           O  
HETATM 5688  O  AHOH A 715      52.541  79.613  28.651  0.63 29.37           O  
HETATM 5689  O   HOH A 716      52.071  75.141  59.492  1.00 36.02           O  
HETATM 5690  O   HOH A 717      28.212  70.553  52.311  1.00 18.94           O  
HETATM 5691  O   HOH A 718      26.269  90.603  38.663  0.83 33.76           O  
HETATM 5692  O   HOH A 719      80.025  88.236  26.645  0.98 39.35           O  
HETATM 5693  O   HOH A 720      70.984  84.017  49.991  0.98 41.27           O  
HETATM 5694  O   HOH A 721      42.034  67.908  24.829  0.96 39.41           O  
HETATM 5695  O   HOH A 722      22.709  90.870  46.097  1.00 30.34           O  
HETATM 5696  O   HOH A 723      78.692  93.927  34.377  1.00 36.84           O  
HETATM 5697  O   HOH A 724      19.831  78.709  53.439  1.00 41.75           O  
HETATM 5698  O   HOH A 725      48.896  91.489  63.950  1.00 19.92           O  
HETATM 5699  O   HOH A 726      85.483  85.261  31.238  0.94 37.62           O  
HETATM 5700  O   HOH A 727      74.431  71.511  45.931  0.96 23.02           O  
HETATM 5701  O   HOH A 728      64.163  71.980  22.008  0.99 38.77           O  
HETATM 5702  O   HOH A 729      44.079  71.520  43.313  0.94 23.09           O  
HETATM 5703  O   HOH A 730      25.749  82.930  50.188  1.00 23.69           O  
HETATM 5704  O   HOH A 731      64.394  88.894  33.079  0.92 21.37           O  
HETATM 5705  O   HOH A 732      39.051 102.270  60.134  1.00 36.88           O  
HETATM 5706  O   HOH A 733      70.266  87.120  49.963  0.99 26.24           O  
HETATM 5707  O   HOH A 734      83.492  84.136  41.443  0.84 39.67           O  
HETATM 5708  O   HOH A 735      74.972  90.356  26.698  1.00 32.25           O  
HETATM 5709  O   HOH A 736      36.829 105.536  56.435  1.00 30.04           O  
HETATM 5710  O   HOH A 737      27.253 100.191  42.430  0.89 44.99           O  
HETATM 5711  O   HOH A 738      51.294  74.605  47.569  0.97 15.03           O  
HETATM 5712  O   HOH A 739      72.769  91.477  42.853  0.96 30.94           O  
HETATM 5713  O   HOH A 740      70.795  76.350  22.618  0.97 23.38           O  
HETATM 5714  O   HOH A 741      76.078  59.153  42.547  0.92 39.06           O  
HETATM 5715  O   HOH A 742      78.385  81.311  42.557  1.00 37.83           O  
HETATM 5716  O   HOH A 743      46.277 101.419  59.092  0.96 35.76           O  
HETATM 5717  O   HOH A 744      68.382  69.045  25.483  0.97 25.11           O  
HETATM 5718  O   HOH A 745      72.881  89.782  35.259  1.00 19.64           O  
HETATM 5719  O   HOH A 746      38.879  62.493  56.797  1.00 33.96           O  
HETATM 5720  O   HOH A 747      49.435  74.043  44.567  1.00 30.85           O  
HETATM 5721  O   HOH A 748      77.372  72.194  35.887  0.95 19.07           O  
HETATM 5722  O   HOH A 749      55.805  62.843  41.782  1.00 30.95           O  
HETATM 5723  O   HOH A 750      58.330  82.970  20.985  0.89 30.44           O  
HETATM 5724  O   HOH A 751      47.203  65.521  55.611  0.90 38.60           O  
HETATM 5725  O   HOH A 752      50.706  69.786  24.761  0.91 56.80           O  
HETATM 5726  O   HOH A 753      55.689  93.097  54.847  0.96 24.10           O  
HETATM 5727  O   HOH A 754      52.862  61.832  41.010  1.00 54.58           O  
HETATM 5728  O   HOH A 755      35.243 102.966  42.978  1.00 39.42           O  
HETATM 5729  O   HOH A 756      70.152  62.586  45.105  1.00 38.26           O  
HETATM 5730  O   HOH A 757      43.579 101.785  43.710  0.97 31.62           O  
HETATM 5731  O   HOH A 758      40.224  75.614  60.903  1.00 33.85           O  
HETATM 5732  O   HOH A 759      75.487  86.801  24.361  1.00 37.21           O  
HETATM 5733  O   HOH A 760      48.988  98.582  51.974  0.98 24.18           O  
HETATM 5734  O   HOH A 761      60.496  96.847  36.104  1.00 41.33           O  
HETATM 5735  O   HOH A 762      65.427  92.257  32.705  1.00 31.14           O  
HETATM 5736  O   HOH A 763      40.296  75.154  45.072  0.99 16.42           O  
HETATM 5737  O   HOH A 764      30.218  79.648  40.160  1.00 34.32           O  
HETATM 5738  O   HOH A 765      47.093  70.578  26.093  0.84 39.05           O  
HETATM 5739  O   HOH A 766      59.280  87.504  27.219  1.00 45.40           O  
HETATM 5740  O   HOH A 767      51.638  74.337  43.790  1.00 44.52           O  
HETATM 5741  O   HOH A 768      62.104  88.518  26.907  1.00 27.13           O  
HETATM 5742  O   HOH A 769      38.339  89.461  63.117  0.97 40.27           O  
HETATM 5743  O  AHOH A 770      83.354  82.105  25.988  0.56 28.39           O  
HETATM 5744  O  BHOH A 770      84.316  82.248  27.370  0.45 22.35           O  
HETATM 5745  O   HOH A 771      27.912  95.602  50.610  1.00 32.70           O  
HETATM 5746  O   HOH A 772      61.407  62.188  44.558  1.00 52.75           O  
HETATM 5747  O  AHOH A 773      56.718  88.740  31.021  0.91 27.01           O  
HETATM 5748  O   HOH A 774      42.347  75.891  31.629  0.99 48.15           O  
HETATM 5749  O  BHOH A 775      54.679  82.791  28.069  0.90 50.21           O  
HETATM 5750  O  AHOH A 776      78.554  72.811  41.261  0.39 22.27           O  
HETATM 5751  O   HOH A 777      56.809  88.094  60.147  0.87 22.04           O  
HETATM 5752  O   HOH A 778      50.552  71.307  29.474  0.91 29.04           O  
HETATM 5753  O   HOH A 779      50.280  89.427  62.705  1.00 16.81           O  
HETATM 5754  O   HOH A 780      80.780  89.862  28.527  1.00 41.79           O  
HETATM 5755  O   HOH A 781      74.623  70.737  48.559  0.90 37.01           O  
HETATM 5756  O   HOH A 782      65.184  95.696  39.659  0.95 31.04           O  
HETATM 5757  O   HOH A 783      66.560  95.634  42.062  0.95 30.49           O  
HETATM 5758  O   HOH A 784      66.568  61.310  42.196  1.00 42.39           O  
HETATM 5759  O   HOH A 785      48.597  72.150  43.921  1.00 45.77           O  
HETATM 5760  O   HOH A 786      30.894  82.254  58.056  1.00 32.54           O  
HETATM 5761  O   HOH A 787      38.226  94.917  61.872  1.00 52.32           O  
HETATM 5762  O   HOH A 788      53.274  78.806  60.484  0.94 40.00           O  
HETATM 5763  O  AHOH A 789      48.638  75.564  53.347  0.41 17.85           O  
HETATM 5764  O   HOH A 790      64.059  70.725  50.477  0.93 24.24           O  
HETATM 5765  O   HOH A 791      68.767  64.661  49.278  0.97 51.17           O  
HETATM 5766  O   HOH A 792      47.453  71.323  28.602  1.00 23.84           O  
HETATM 5767  O   HOH A 793      46.334  69.027  59.739  1.00 53.29           O  
HETATM 5768  O   HOH A 794      80.247  75.463  35.497  0.92 32.43           O  
HETATM 5769  O   HOH A 795      52.109  92.642  26.691  1.00 48.87           O  
HETATM 5770  O   HOH A 796      43.268  88.468  65.270  1.00 31.74           O  
HETATM 5771  O   HOH A 797      32.563  98.046  57.948  1.00 42.31           O  
HETATM 5772  O   HOH A 798      62.048  80.857  55.901  0.98 48.98           O  
HETATM 5773  O   HOH A 799      29.910  98.729  52.938  0.99 25.86           O  
HETATM 5774  O  AHOH A 800      74.936  73.681  35.135  0.65 15.00           O  
HETATM 5775  O  BHOH A 800      74.169  74.270  33.076  0.35 29.31           O  
HETATM 5776  O   HOH A 801      33.481  81.891  57.986  0.91 26.98           O  
HETATM 5777  O   HOH A 802      68.874  96.162  49.061  0.88 37.62           O  
HETATM 5778  O   HOH A 803      45.654  94.171  63.672  0.95 29.75           O  
HETATM 5779  O   HOH A 804      55.073  92.720  32.235  1.00 43.14           O  
HETATM 5780  O   HOH A 805      58.248  93.893  53.455  0.92 28.53           O  
HETATM 5781  O   HOH A 806      86.759  85.009  29.285  1.00 59.34           O  
HETATM 5782  O   HOH A 807      62.851  91.880  32.087  0.99 35.66           O  
HETATM 5783  O   HOH A 808      25.160  82.064  52.938  0.93 33.36           O  
HETATM 5784  O   HOH A 809      63.812  87.280  22.738  0.91 43.48           O  
HETATM 5785  O   HOH A 810      51.255  74.562  62.517  1.00 50.20           O  
HETATM 5786  O   HOH A 811      50.188  99.712  46.637  1.00 37.50           O  
HETATM 5787  O   HOH A 812      75.635  83.018  45.400  1.00 45.64           O  
HETATM 5788  O  AHOH A 813      72.933  85.486  23.540  0.96 39.35           O  
HETATM 5789  O   HOH A 814      75.810  75.914  25.226  1.00 19.23           O  
HETATM 5790  O   HOH A 815      31.710  92.972  57.262  1.00 27.50           O  
HETATM 5791  O   HOH A 816      69.719  93.906  31.837  0.92 55.76           O  
HETATM 5792  O  AHOH A 817      49.771  72.240  53.454  0.41 28.36           O  
HETATM 5793  O   HOH A 818      36.179  84.179  64.418  1.00 43.56           O  
HETATM 5794  O   HOH A 819      50.127  74.612  27.611  0.93 41.52           O  
HETATM 5795  O   HOH A 820      57.658  84.923  26.250  1.00 50.61           O  
HETATM 5796  O   HOH A 821      77.483  85.939  43.720  1.00 50.50           O  
HETATM 5797  O   HOH A 822      33.653  91.348  58.438  1.00 29.56           O  
HETATM 5798  O   HOH A 823      38.980  88.439  65.663  0.91 47.18           O  
HETATM 5799  O   HOH A 824      62.963  80.221  62.786  1.00 63.67           O  
HETATM 5800  O   HOH A 825      36.363 103.190  40.775  1.00 41.81           O  
HETATM 5801  O   HOH A 826      73.831  93.679  30.108  1.00 50.77           O  
HETATM 5802  O   HOH A 827      55.999  76.487  51.432  1.00 45.12           O  
HETATM 5803  O   HOH A 828      63.728  94.824  36.547  1.00 49.56           O  
HETATM 5804  O   HOH A 829      39.464 104.663  43.821  1.00 54.16           O  
HETATM 5805  O   HOH A 830      44.964  74.591  27.313  1.00 60.42           O  
HETATM 5806  O   HOH A 831      63.860  66.499  31.196  1.00 52.40           O  
HETATM 5807  O   HOH A 832      66.961  90.597  29.848  0.85 34.76           O  
HETATM 5808  O   HOH A 833      81.573  80.557  23.409  1.00 67.30           O  
HETATM 5809  O   HOH A 834      46.628  99.214  64.942  1.00 59.55           O  
HETATM 5810  O   HOH A 835      50.004  98.163  61.554  1.00 46.90           O  
HETATM 5811  O   HOH A 836      44.308  75.092  62.773  1.00 47.52           O  
HETATM 5812  O   HOH A 837      60.503  90.274  32.711  0.79 29.84           O  
HETATM 5813  O   HOH A 838      68.984  61.475  43.959  1.00 46.64           O  
HETATM 5814  O   HOH A 839      69.901  77.475  48.718  1.00 56.34           O  
HETATM 5815  O   HOH A 840      51.235  71.750  46.082  1.00 34.94           O  
HETATM 5816  O   HOH A 841      74.600  91.785  45.563  1.00 52.15           O  
HETATM 5817  O   HOH A 842      69.191  96.742  41.362  1.00 54.53           O  
HETATM 5818  O   HOH A 843      32.317  70.836  46.660  0.89 24.28           O  
HETATM 5819  O   HOH A 844      35.367 100.485  42.212  1.00 39.24           O  
HETATM 5820  O   HOH A 845      65.236  59.532  41.370  0.92 49.76           O  
HETATM 5821  O   HOH A 846      84.028  79.309  39.296  1.00 62.59           O  
HETATM 5822  O   HOH A 847      70.115  73.986  21.295  1.00 32.40           O  
HETATM 5823  O   HOH A 848      47.031  76.384  28.399  1.00 54.83           O  
HETATM 5824  O  AHOH A 849      24.407  77.923  50.649  0.57 26.02           O  
HETATM 5825  O   HOH A 850      28.486 101.825  50.987  0.97 40.89           O  
HETATM 5826  O   HOH A 851      47.164  75.491  65.549  1.00 41.78           O  
HETATM 5827  O   HOH A 852      48.104 101.768  60.796  1.00 51.77           O  
HETATM 5828  O   HOH A 853      66.848  95.773  50.778  0.98 34.78           O  
HETATM 5829  O   HOH A 854      49.789 101.485  58.330  1.00 49.87           O  
HETATM 5830  O   HOH A 855      72.722  86.361  49.721  1.00 63.27           O  
HETATM 5831  O   HOH A 856      34.502  81.266  62.239  0.98 36.82           O  
HETATM 5832  O   HOH A 857      66.488  92.154  27.759  0.88 40.17           O  
HETATM 5833  O   HOH A 858      59.066  63.267  31.517  1.00 42.82           O  
HETATM 5834  O   HOH A 859      39.983  77.068  30.552  1.00 59.77           O  
HETATM 5835  O   HOH A 860      76.281  66.695  40.978  1.00 48.21           O  
HETATM 5836  O   HOH A 861      67.774  85.012  52.544  0.98 40.34           O  
HETATM 5837  O   HOH A 862      55.394  72.965  23.880  1.00 62.77           O  
HETATM 5838  O  AHOH A 863      75.671  65.454  44.620  1.00 79.42           O  
HETATM 5839  O   HOH A 864      19.510  84.718  47.436  1.00 62.20           O  
HETATM 5840  O   HOH A 865      41.326  68.745  42.019  1.00 40.59           O  
HETATM 5841  O   HOH A 866      20.459  86.687  48.597  1.00 51.89           O  
HETATM 5842  O   HOH A 867      21.699  89.539  48.108  1.00 52.77           O  
HETATM 5843  O   HOH A 868      62.544 100.344  46.073  0.85 49.83           O  
HETATM 5844  O   HOH A 869      55.263  80.195  58.964  1.00 35.73           O  
HETATM 5845  O   HOH A 870      57.933  69.191  28.199  0.88 36.37           O  
HETATM 5846  O   HOH A 871      66.962  74.016  53.720  1.00 66.73           O  
HETATM 5847  O   HOH A 872      62.558  90.518  28.919  0.94 39.52           O  
HETATM 5848  O   HOH A 873      47.705  69.390  45.503  1.00 60.27           O  
HETATM 5849  O   HOH A 874      54.923  95.405  32.919  1.00 56.95           O  
HETATM 5850  O   HOH A 875      27.861  91.875  37.177  1.00 56.56           O  
HETATM 5851  O   HOH A 876      30.534  80.765  37.182  1.00 56.91           O  
HETATM 5852  O   HOH A 877      67.164  61.589  30.922  1.00 53.51           O  
HETATM 5853  O   HOH A 878      61.957  88.268  23.513  1.00 52.82           O  
HETATM 5854  O   HOH A 879      69.345  96.428  44.198  1.00 69.69           O  
HETATM 5855  O   HOH A 880      63.334  68.736  30.688  1.00 37.82           O  
HETATM 5856  O   HOH A 881      61.560  63.449  46.389  1.00 54.82           O  
HETATM 5857  O   HOH A 882      77.519  75.021  23.337  0.98 25.83           O  
HETATM 5858  O   HOH A 883      70.971  74.798  50.813  1.00 57.67           O  
HETATM 5859  O  BHOH A 884      53.816  76.453  53.160  1.00 66.63           O  
HETATM 5860  O   HOH A 885      32.035  95.206  58.708  1.00 45.44           O  
HETATM 5861  O   HOH A 886      36.270 103.873  59.292  0.99 53.02           O  
HETATM 5862  O   HOH A 887      68.725  69.386  50.694  1.00 56.45           O  
HETATM 5863  O   HOH A 888      67.620  90.469  56.260  1.00 55.82           O  
HETATM 5864  O   HOH A 889      45.203  90.306  65.745  0.97 17.53           O  
HETATM 5865  O   HOH A 890      68.703  93.482  55.396  1.00 36.55           O  
HETATM 5866  O   HOH A 891      59.689  71.709  51.767  1.00 40.93           O  
HETATM 5867  O   HOH A 892      42.108  68.742  45.315  1.00 48.74           O  
HETATM 5868  O   HOH A 893      76.926  89.124  25.805  1.00 51.79           O  
HETATM 5869  O  AHOH A 894      53.354  84.774  31.536  0.74 20.14           O  
HETATM 5870  O   HOH A 895      73.188  95.300  34.247  0.98 44.61           O  
HETATM 5871  O   HOH A 896      72.307  93.590  32.299  1.00 33.25           O  
HETATM 5872  O   HOH A 897      72.406  77.924  48.676  1.00 50.07           O  
HETATM 5873  O  AHOH A 898      55.835  86.253  30.541  0.82 21.84           O  
HETATM 5874  O   HOH A 899      22.089  84.929  50.587  1.00 44.50           O  
HETATM 5875  O   HOH A 900      72.873  72.716  24.770  0.94 26.24           O  
HETATM 5876  O   HOH A 901      23.879  74.920  56.224  0.98 48.34           O  
HETATM 5877  O   HOH A 902      61.458  66.618  30.886  1.00 40.32           O  
HETATM 5878  O   HOH A 903      51.648  71.287  26.643  0.91 35.68           O  
HETATM 5879  O   HOH A 904      64.773  88.448  57.954  0.91 31.97           O  
HETATM 5880  O   HOH A 905      27.791  94.953  38.389  1.00 38.95           O  
HETATM 5881  O   HOH A 906      69.165  87.220  52.559  0.98 39.28           O  
HETATM 5882  O   HOH A 907      34.919 101.623  59.397  0.86 37.15           O  
HETATM 5883  O   HOH A 908      48.596 100.619  48.374  1.00 62.59           O  
HETATM 5884  O   HOH A 909      82.844  88.551  25.936  1.00 67.36           O  
HETATM 5885  O   HOH A 910      34.430  93.552  59.573  1.00 35.92           O  
HETATM 5886  O   HOH A 911      61.825  70.598  51.998  0.94 47.62           O  
HETATM 5887  O   HOH A 912      49.501 101.451  50.448  1.00 46.51           O  
HETATM 5888  O   HOH A 913      57.547  66.768  29.384  1.00 32.60           O  
HETATM 5889  O   HOH A 914      56.928  90.894  32.938  0.90 32.05           O  
HETATM 5890  O   HOH A 915      65.328  99.504  45.182  0.91 43.95           O  
HETATM 5891  O   HOH A 916      70.304  71.197  21.682  0.93 49.70           O  
HETATM 5892  O   HOH A 917      37.129  92.281  63.374  0.85 43.78           O  
HETATM 5893  O   HOH A 918      73.791  74.009  21.638  1.00 42.98           O  
HETATM 5894  O   HOH A 919      79.225  91.964  27.502  0.97 53.67           O  
HETATM 5895  O   HOH A 920      42.368  65.141  49.134  1.00 46.00           O  
HETATM 5896  O   HOH A 921      27.578  97.700  51.922  0.96 35.84           O  
HETATM 5897  O   HOH A 922      29.506  80.930  60.094  1.00 53.08           O  
HETATM 5898  O   HOH A 923      53.762  70.492  25.790  1.00 51.69           O  
HETATM 5899  O   HOH A 924      26.798  99.867  50.862  0.98 50.58           O  
CONECT  994 5244                                                                
CONECT  995 5244                                                                
CONECT 1016 5244                                                                
CONECT 1040 5244                                                                
CONECT 2226 5243                                                                
CONECT 2282 5246                                                                
CONECT 2298 5251                                                                
CONECT 2347 5246                                                                
CONECT 2701 5246                                                                
CONECT 2704 5246                                                                
CONECT 2888 5243                                                                
CONECT 2889 5243 5248                                                           
CONECT 3101 5248                                                                
CONECT 3102 5248                                                                
CONECT 3143 5243                                                                
CONECT 3144 5248                                                                
CONECT 3177 5243                                                                
CONECT 3233 5243                                                                
CONECT 3234 5243 5248                                                           
CONECT 3272 5245                                                                
CONECT 3293 5245                                                                
CONECT 3295 5245                                                                
CONECT 3327 5245                                                                
CONECT 3375 5245                                                                
CONECT 3828 5250                                                                
CONECT 3884 5250                                                                
CONECT 3887 5249                                                                
CONECT 4006 5252                                                                
CONECT 4161 5247                                                                
CONECT 5243 2226 2888 2889 3143                                                 
CONECT 5243 3177 3233 3234 5617                                                 
CONECT 5244  994  995 1016 1040                                                 
CONECT 5244 5548 5618 5789                                                      
CONECT 5245 3272 3293 3295 3327                                                 
CONECT 5245 3375 5536 5766                                                      
CONECT 5246 2282 2347 2701 2704                                                 
CONECT 5246 5711                                                                
CONECT 5247 4161                                                                
CONECT 5248 2889 3101 3102 3144                                                 
CONECT 5248 3234 5506                                                           
CONECT 5249 3887 5711 5815                                                      
CONECT 5250 3828 3884                                                           
CONECT 5251 2298 5608 5711                                                      
CONECT 5252 4006 5497                                                           
CONECT 5253 5254 5263                                                           
CONECT 5254 5253 5255 5262 5264                                                 
CONECT 5255 5254 5256 5259 5265                                                 
CONECT 5256 5255 5257 5260 5266                                                 
CONECT 5257 5256 5258 5261 5267                                                 
CONECT 5258 5257 5262 5268 5269                                                 
CONECT 5259 5255 5270                                                           
CONECT 5260 5256 5271                                                           
CONECT 5261 5257 5272                                                           
CONECT 5262 5254 5258                                                           
CONECT 5263 5253                                                                
CONECT 5264 5254                                                                
CONECT 5265 5255                                                                
CONECT 5266 5256                                                                
CONECT 5267 5257                                                                
CONECT 5268 5258                                                                
CONECT 5269 5258                                                                
CONECT 5270 5259                                                                
CONECT 5271 5260                                                                
CONECT 5272 5261                                                                
CONECT 5273 5274 5283                                                           
CONECT 5274 5273 5275 5282 5284                                                 
CONECT 5275 5274 5276 5279 5285                                                 
CONECT 5276 5275 5277 5280 5286                                                 
CONECT 5277 5276 5278 5281 5287                                                 
CONECT 5278 5277 5282 5288 5289                                                 
CONECT 5279 5275 5290                                                           
CONECT 5280 5276 5291                                                           
CONECT 5281 5277 5292                                                           
CONECT 5282 5274 5278                                                           
CONECT 5283 5273                                                                
CONECT 5284 5274                                                                
CONECT 5285 5275                                                                
CONECT 5286 5276                                                                
CONECT 5287 5277                                                                
CONECT 5288 5278                                                                
CONECT 5289 5278                                                                
CONECT 5290 5279                                                                
CONECT 5291 5280                                                                
CONECT 5292 5281                                                                
CONECT 5293 5294 5303                                                           
CONECT 5294 5293 5295 5302 5304                                                 
CONECT 5295 5294 5296 5299 5305                                                 
CONECT 5296 5295 5297 5300 5306                                                 
CONECT 5297 5296 5298 5301 5307                                                 
CONECT 5298 5297 5302 5308 5309                                                 
CONECT 5299 5295 5310                                                           
CONECT 5300 5296 5311                                                           
CONECT 5301 5297 5312                                                           
CONECT 5302 5294 5298                                                           
CONECT 5303 5293                                                                
CONECT 5304 5294                                                                
CONECT 5305 5295                                                                
CONECT 5306 5296                                                                
CONECT 5307 5297                                                                
CONECT 5308 5298                                                                
CONECT 5309 5298                                                                
CONECT 5310 5299                                                                
CONECT 5311 5300                                                                
CONECT 5312 5301                                                                
CONECT 5313 5314 5323                                                           
CONECT 5314 5313 5315 5322 5324                                                 
CONECT 5315 5314 5316 5319 5325                                                 
CONECT 5316 5315 5317 5320 5326                                                 
CONECT 5317 5316 5318 5321 5327                                                 
CONECT 5318 5317 5322 5328 5329                                                 
CONECT 5319 5315 5330                                                           
CONECT 5320 5316 5331                                                           
CONECT 5321 5317 5332                                                           
CONECT 5322 5314 5318                                                           
CONECT 5323 5313                                                                
CONECT 5324 5314                                                                
CONECT 5325 5315                                                                
CONECT 5326 5316                                                                
CONECT 5327 5317                                                                
CONECT 5328 5318                                                                
CONECT 5329 5318                                                                
CONECT 5330 5319                                                                
CONECT 5331 5320                                                                
CONECT 5332 5321                                                                
CONECT 5333 5334 5343                                                           
CONECT 5334 5333 5335 5342 5344                                                 
CONECT 5335 5334 5336 5339 5345                                                 
CONECT 5336 5335 5337 5340 5346                                                 
CONECT 5337 5336 5338 5341 5347                                                 
CONECT 5338 5337 5342 5348 5349                                                 
CONECT 5339 5335 5350                                                           
CONECT 5340 5336 5351                                                           
CONECT 5341 5337 5352                                                           
CONECT 5342 5334 5338                                                           
CONECT 5343 5333                                                                
CONECT 5344 5334                                                                
CONECT 5345 5335                                                                
CONECT 5346 5336                                                                
CONECT 5347 5337                                                                
CONECT 5348 5338                                                                
CONECT 5349 5338                                                                
CONECT 5350 5339                                                                
CONECT 5351 5340                                                                
CONECT 5352 5341                                                                
CONECT 5353 5354 5363                                                           
CONECT 5354 5353 5355 5362 5364                                                 
CONECT 5355 5354 5356 5359 5365                                                 
CONECT 5356 5355 5357 5360 5366                                                 
CONECT 5357 5356 5358 5361 5367                                                 
CONECT 5358 5357 5362 5368 5369                                                 
CONECT 5359 5355 5370                                                           
CONECT 5360 5356 5371                                                           
CONECT 5361 5357 5372                                                           
CONECT 5362 5354 5358                                                           
CONECT 5363 5353                                                                
CONECT 5364 5354                                                                
CONECT 5365 5355                                                                
CONECT 5366 5356                                                                
CONECT 5367 5357                                                                
CONECT 5368 5358                                                                
CONECT 5369 5358                                                                
CONECT 5370 5359                                                                
CONECT 5371 5360                                                                
CONECT 5372 5361                                                                
CONECT 5373 5374 5383                                                           
CONECT 5374 5373 5375 5382 5384                                                 
CONECT 5375 5374 5376 5379 5385                                                 
CONECT 5376 5375 5377 5380 5386                                                 
CONECT 5377 5376 5378 5381 5387                                                 
CONECT 5378 5377 5382 5388 5389                                                 
CONECT 5379 5375 5390                                                           
CONECT 5380 5376 5391                                                           
CONECT 5381 5377 5392                                                           
CONECT 5382 5374 5378                                                           
CONECT 5383 5373                                                                
CONECT 5384 5374                                                                
CONECT 5385 5375                                                                
CONECT 5386 5376                                                                
CONECT 5387 5377                                                                
CONECT 5388 5378                                                                
CONECT 5389 5378                                                                
CONECT 5390 5379                                                                
CONECT 5391 5380                                                                
CONECT 5392 5381                                                                
CONECT 5393 5394 5403                                                           
CONECT 5394 5393 5395 5402 5404                                                 
CONECT 5395 5394 5396 5399 5405                                                 
CONECT 5396 5395 5397 5400 5406                                                 
CONECT 5397 5396 5398 5401 5407                                                 
CONECT 5398 5397 5402 5408 5409                                                 
CON