CNRS Nantes University UFIP UFIP
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***  7awm_wt  ***

elNémo ID: 22031510354555331

Job options:

ID        	=	 22031510354555331
JOBID     	=	 7awm_wt
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 7awm_wt

HEADER    MEMBRANE PROTEIN                        08-NOV-20   7AWM              
TITLE     STRUCTURE OF THE THERMOSTABILIZED EAAT1 CRYST MUTANT IN COMPLEX WITH  
TITLE    2 L-ASP, THREE SODIUM IONS AND THE ALLOSTERIC INHIBITOR UCPH101        
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: EXCITATORY AMINO ACID TRANSPORTER 1,NEUTRAL AMINO ACID     
COMPND   3 TRANSPORTER B(0),EXCITATORY AMINO ACID TRANSPORTER 1;                
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: SODIUM-DEPENDENT GLUTAMATE/ASPARTATE TRANSPORTER 1,GLAST-1, 
COMPND   6 SOLUTE CARRIER FAMILY 1 MEMBER 3,ATB(0),BABOON M7 VIRUS RECEPTOR,    
COMPND   7 RD114/SIMIAN TYPE D RETROVIRUS RECEPTOR,SODIUM-DEPENDENT NEUTRAL     
COMPND   8 AMINO ACID TRANSPORTER TYPE 2,SOLUTE CARRIER FAMILY 1 MEMBER 5,      
COMPND   9 SODIUM-DEPENDENT GLUTAMATE/ASPARTATE TRANSPORTER 1,GLAST-1,SOLUTE    
COMPND  10 CARRIER FAMILY 1 MEMBER 3;                                           
COMPND  11 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: SLC1A3, EAAT1, GLAST, GLAST1, SLC1A5, ASCT2, M7V1, RDR, RDRC;  
SOURCE   6 EXPRESSION_SYSTEM: HOMO SAPIENS;                                     
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 9606;                                       
SOURCE   8 EXPRESSION_SYSTEM_CELL_LINE: HEK-293F;                               
SOURCE   9 EXPRESSION_SYSTEM_ATCC_NUMBER: CRL-1573;                             
SOURCE  10 EXPRESSION_SYSTEM_TISSUE: EMBRIONIC KIDNEY;                          
SOURCE  11 EXPRESSION_SYSTEM_CELL: EMBRIONIC;                                   
SOURCE  12 EXPRESSION_SYSTEM_VECTOR_TYPE: MAMMALIAN EXPRESION;                  
SOURCE  13 EXPRESSION_SYSTEM_PLASMID: PCDNA3.1                                  
KEYWDS    EXCITATORY AMINO ACID TRANSPORTER 1, HUMAN GLUTAMATE TRANSPORTER,     
KEYWDS   2 SLC1A3, ALLOSTERIC INHIBITOR UCPH101, MEMBRANE PROTEIN               
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.C.CANUL-TEC,P.LEGRAND,N.REYES                                       
REVDAT   3   12-JAN-22 7AWM    1       JRNL                                     
REVDAT   2   01-DEC-21 7AWM    1       JRNL                                     
REVDAT   1   13-OCT-21 7AWM    0                                                
JRNL        AUTH   J.C.CANUL-TEC,A.KUMAR,J.DHENIN,R.ASSAL,P.LEGRAND,M.REY,      
JRNL        AUTH 2 J.CHAMOT-ROOKE,N.REYES                                       
JRNL        TITL   THE ION-COUPLING MECHANISM OF HUMAN EXCITATORY AMINO ACID    
JRNL        TITL 2 TRANSPORTERS.                                                
JRNL        REF    EMBO J.                       V.  41       2022              
JRNL        REFN                   ESSN 1460-2075                               
JRNL        PMID   34747040                                                     
JRNL        DOI    10.15252/EMBJ.2021108341                                     
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.25 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : BUSTER 2.10.3                                        
REMARK   3   AUTHORS     : BRICOGNE,BLANC,BRANDL,FLENSBURG,KELLER,              
REMARK   3               : PACIOREK,ROVERSI,SHARFF,SMART,VONRHEIN,              
REMARK   3               : WOMACK,MATTHEWS,TEN EYCK,TRONRUD                     
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.25                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 23.31                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 78.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 9675                           
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD           : THROUGHOUT                     
REMARK   3   FREE R VALUE TEST SET SELECTION   : RANDOM                         
REMARK   3   R VALUE     (WORKING + TEST SET)  : 0.220                          
REMARK   3   R VALUE            (WORKING SET)  : 0.219                          
REMARK   3   FREE R VALUE                      : 0.238                          
REMARK   3   FREE R VALUE TEST SET SIZE   (%)  : 4.550                          
REMARK   3   FREE R VALUE TEST SET COUNT       : 440                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE   : NULL                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED               : 5                        
REMARK   3   BIN RESOLUTION RANGE HIGH   (ANGSTROMS) : 3.25                     
REMARK   3   BIN RESOLUTION RANGE LOW    (ANGSTROMS) : 3.63                     
REMARK   3   BIN COMPLETENESS (WORKING+TEST)     (%) : 35.23                    
REMARK   3   REFLECTIONS IN BIN (WORKING + TEST SET) : 1222                     
REMARK   3   BIN R VALUE        (WORKING + TEST SET) : 0.2170                   
REMARK   3   REFLECTIONS IN BIN        (WORKING SET) : 1166                     
REMARK   3   BIN R VALUE               (WORKING SET) : 0.2169                   
REMARK   3   BIN FREE R VALUE                        : 0.2183                   
REMARK   3   BIN FREE R VALUE TEST SET SIZE      (%) : 4.58                     
REMARK   3   BIN FREE R VALUE TEST SET COUNT         : 56                       
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE     : 0.000                    
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3135                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 45                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 145.0                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 135.4                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 4.68200                                              
REMARK   3    B22 (A**2) : 4.68200                                              
REMARK   3    B33 (A**2) : -9.36410                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT                    (A) : 0.480               
REMARK   3   DPI (BLOW EQ-10) BASED ON R VALUE        (A) : NULL                
REMARK   3   DPI (BLOW EQ-9) BASED ON FREE R VALUE    (A) : 0.458               
REMARK   3   DPI (CRUICKSHANK) BASED ON R VALUE       (A) : NULL                
REMARK   3   DPI (CRUICKSHANK) BASED ON FREE R VALUE  (A) : NULL                
REMARK   3                                                                      
REMARK   3   REFERENCES: BLOW, D. (2002) ACTA CRYST D58, 792-797                
REMARK   3               CRUICKSHANK, D.W.J. (1999) ACTA CRYST D55, 583-601     
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.912                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.894                         
REMARK   3                                                                      
REMARK   3   NUMBER OF GEOMETRIC FUNCTION TERMS DEFINED : 15                    
REMARK   3   TERM                          COUNT    WEIGHT   FUNCTION.          
REMARK   3    BOND LENGTHS              : 3227   ; 2.000  ; HARMONIC            
REMARK   3    BOND ANGLES               : 4382   ; 2.000  ; HARMONIC            
REMARK   3    TORSION ANGLES            : 1110   ; 2.000  ; SINUSOIDAL          
REMARK   3    TRIGONAL CARBON PLANES    : 56     ; 2.000  ; HARMONIC            
REMARK   3    GENERAL PLANES            : 493    ; 5.000  ; HARMONIC            
REMARK   3    ISOTROPIC THERMAL FACTORS : 3227   ; 20.000 ; HARMONIC            
REMARK   3    BAD NON-BONDED CONTACTS   : 2      ; 5.000  ; SEMIHARMONIC        
REMARK   3    IMPROPER TORSIONS         : NULL   ; NULL   ; NULL                
REMARK   3    PSEUDOROTATION ANGLES     : NULL   ; NULL   ; NULL                
REMARK   3    CHIRAL IMPROPER TORSION   : 448    ; 5.000  ; SEMIHARMONIC        
REMARK   3    SUM OF OCCUPANCIES        : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY DISTANCES         : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY ANGLES            : NULL   ; NULL   ; NULL                
REMARK   3    UTILITY TORSION           : NULL   ; NULL   ; NULL                
REMARK   3    IDEAL-DIST CONTACT TERM   : 4022   ; 4.000  ; SEMIHARMONIC        
REMARK   3                                                                      
REMARK   3   RMS DEVIATIONS FROM IDEAL VALUES.                                  
REMARK   3    BOND LENGTHS                       (A) : 0.010                    
REMARK   3    BOND ANGLES                  (DEGREES) : 1.17                     
REMARK   3    PEPTIDE OMEGA TORSION ANGLES (DEGREES) : 2.19                     
REMARK   3    OTHER TORSION ANGLES         (DEGREES) : 22.47                    
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: { A|* }                                                
REMARK   3    ORIGIN FOR THE GROUP (A):  -36.0755   30.1168    4.5558           
REMARK   3    T TENSOR                                                          
REMARK   3     T11:   -0.2676 T22:    0.1714                                    
REMARK   3     T33:   -0.3900 T12:    0.1246                                    
REMARK   3     T13:   -0.0020 T23:    0.0733                                    
REMARK   3    L TENSOR                                                          
REMARK   3     L11:    2.4757 L22:    1.7581                                    
REMARK   3     L33:    3.5616 L12:   -0.0831                                    
REMARK   3     L13:   -0.0382 L23:   -0.0988                                    
REMARK   3    S TENSOR                                                          
REMARK   3     S11:   -0.0792 S12:   -0.1292 S13:   -0.2980                     
REMARK   3     S21:    0.0956 S22:   -0.0713 S23:   -0.5971                     
REMARK   3     S31:    0.4311 S32:    1.2529 S33:    0.1505                     
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 7AWM COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE.                               
REMARK 100 THE DEPOSITION ID IS D_1292112208.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 23-SEP-16                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8-8.4                              
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SOLEIL                             
REMARK 200  BEAMLINE                       : PROXIMA 1                          
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.979                              
REMARK 200  MONOCHROMATOR                  : CHANNEL CUT MONOCHROMATOR          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS JUNE 31, 2020 BUILT=20200417   
REMARK 200  DATA SCALING SOFTWARE          : AIMLESS 0.5.32                     
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 12293                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.250                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.810                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 13.50                              
REMARK 200  R MERGE                    (I) : 0.14600                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.8000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.25                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.33                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 12.50                              
REMARK 200  R MERGE FOR SHELL          (I) : 7.92700                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER 2.7.17                                         
REMARK 200 STARTING MODEL: 5LLM                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 64.58                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 3.47                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 28% PEG400, 100MM TRIS PH 8.2, 50 MM     
REMARK 280  CALCIUM CHLORIDE, 50 MM BARIUM CHLORIDE, VAPOR DIFFUSION,           
REMARK 280  HANGING DROP, TEMPERATURE 277K                                      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 63                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z                                                
REMARK 290       3555   -X+Y,-X,Z                                               
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+1/2                                            
REMARK 290       6555   X-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 -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        0.00000            
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        0.00000            
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       45.01600            
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       45.01600            
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       45.01600            
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: TRIMERIC                          
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TRIMERIC                   
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 9220 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 52430 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -156.0 KCAL/MOL                       
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -0.500000 -0.866025  0.000000      -61.44100            
REMARK 350   BIOMT2   2  0.866025 -0.500000  0.000000      106.41893            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000     -122.88200            
REMARK 350   BIOMT2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     THR A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     SER A     4                                                      
REMARK 465     ASN A     5                                                      
REMARK 465     GLY A     6                                                      
REMARK 465     GLU A     7                                                      
REMARK 465     GLU A     8                                                      
REMARK 465     PRO A     9                                                      
REMARK 465     LYS A    10                                                      
REMARK 465     MET A    11                                                      
REMARK 465     GLY A    12                                                      
REMARK 465     GLY A    13                                                      
REMARK 465     ARG A    14                                                      
REMARK 465     MET A    15                                                      
REMARK 465     GLU A    16                                                      
REMARK 465     ARG A    17                                                      
REMARK 465     PHE A    18                                                      
REMARK 465     GLN A    19                                                      
REMARK 465     GLN A    20                                                      
REMARK 465     GLY A    21                                                      
REMARK 465     VAL A    22                                                      
REMARK 465     SER A    23                                                      
REMARK 465     LYS A    24                                                      
REMARK 465     ARG A    25                                                      
REMARK 465     THR A    26                                                      
REMARK 465     LEU A    27                                                      
REMARK 465     LEU A    28                                                      
REMARK 465     GLY A   148                                                      
REMARK 465     ALA A   149                                                      
REMARK 465     ALA A   150                                                      
REMARK 465     SER A   151                                                      
REMARK 465     ALA A   152                                                      
REMARK 465     ALA A   153                                                      
REMARK 465     ILE A   154                                                      
REMARK 465     THR A   155                                                      
REMARK 465     ALA A   156                                                      
REMARK 465     SER A   157                                                      
REMARK 465     VAL A   158                                                      
REMARK 465     GLY A   159                                                      
REMARK 465     ALA A   160                                                      
REMARK 465     ALA A   161                                                      
REMARK 465     GLY A   162                                                      
REMARK 465     SER A   163                                                      
REMARK 465     ALA A   164                                                      
REMARK 465     GLU A   165                                                      
REMARK 465     ASN A   166                                                      
REMARK 465     ALA A   167                                                      
REMARK 465     PRO A   168                                                      
REMARK 465     SER A   169                                                      
REMARK 465     LYS A   170                                                      
REMARK 465     THR A   199                                                      
REMARK 465     TYR A   200                                                      
REMARK 465     GLU A   201                                                      
REMARK 465     GLU A   202                                                      
REMARK 465     ARG A   203                                                      
REMARK 465     THR A   204                                                      
REMARK 465     ILE A   205                                                      
REMARK 465     THR A   206                                                      
REMARK 465     GLY A   207                                                      
REMARK 465     THR A   208                                                      
REMARK 465     ARG A   209                                                      
REMARK 465     VAL A   210                                                      
REMARK 465     LYS A   211                                                      
REMARK 465     VAL A   212                                                      
REMARK 465     PRO A   213                                                      
REMARK 465     VAL A   214                                                      
REMARK 465     GLY A   215                                                      
REMARK 465     GLU A   283                                                      
REMARK 465     MET A   284                                                      
REMARK 465     GLU A   285                                                      
REMARK 465     ASP A   286                                                      
REMARK 465     LEU A   287                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     VAL A   289                                                      
REMARK 465     LEU A   290                                                      
REMARK 465     LEU A   489                                                      
REMARK 465     GLY A   490                                                      
REMARK 465     ASN A   491                                                      
REMARK 465     SER A   492                                                      
REMARK 465     VAL A   493                                                      
REMARK 465     ILE A   494                                                      
REMARK 465     GLU A   495                                                      
REMARK 465     GLU A   496                                                      
REMARK 465     ASN A   497                                                      
REMARK 465     GLU A   498                                                      
REMARK 465     MET A   499                                                      
REMARK 465     LYS A   500                                                      
REMARK 465     LYS A   501                                                      
REMARK 465     PRO A   502                                                      
REMARK 465     TYR A   503                                                      
REMARK 465     GLN A   504                                                      
REMARK 465     LEU A   505                                                      
REMARK 465     ILE A   506                                                      
REMARK 465     ALA A   507                                                      
REMARK 465     GLN A   508                                                      
REMARK 465     ASP A   509                                                      
REMARK 465     ASN A   510                                                      
REMARK 465     GLU A   511                                                      
REMARK 465     THR A   512                                                      
REMARK 465     GLU A   513                                                      
REMARK 465     LYS A   514                                                      
REMARK 465     PRO A   515                                                      
REMARK 465     ILE A   516                                                      
REMARK 465     ASP A   517                                                      
REMARK 465     SER A   518                                                      
REMARK 465     GLU A   519                                                      
REMARK 465     THR A   520                                                      
REMARK 465     LYS A   521                                                      
REMARK 465     MET A   522                                                      
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    ASN A  48       33.88    -86.84                                   
REMARK 500    PRO A  70      106.58    -55.83                                   
REMARK 500    PHE A 184       76.26   -118.75                                   
REMARK 500    ILE A 311      -53.92   -126.46                                   
REMARK 500    GLU A 358      -82.68    -95.26                                   
REMARK 500    MET A 379       78.71   -117.98                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
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                              NA A 602  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 TYR A 127   O                                                      
REMARK 620 2 THR A 130   OG1  82.3                                              
REMARK 620 3 THR A 131   OG1  80.4 131.2                                        
REMARK 620 4 ASN A 378   OD1 124.3 105.8 121.7                                  
REMARK 620 5 ASP A 380   OD1 133.7  78.6  81.4 101.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 601  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A 345   OG                                                     
REMARK 620 2 GLY A 374   O   163.5                                              
REMARK 620 3 ALA A 375   O    81.8  83.7                                        
REMARK 620 4 ASN A 378   O   132.8  63.1 127.0                                  
REMARK 620 5 ASP A 467   OD2 109.8  68.5 111.1  94.4                            
REMARK 620 N                    1     2     3     4                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A 603  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 THR A 376   O                                                      
REMARK 620 2 SER A 417   O   143.7                                              
REMARK 620 3 ILE A 418   O    73.9  81.2                                        
REMARK 620 4 ALA A 420   O    95.8 114.1  99.0                                  
REMARK 620 N                    1     2     3                                   
DBREF  7AWM A    1   148  UNP    P43003   EAA1_HUMAN       1    148             
DBREF  7AWM A  149   224  UNP    Q15758   AAAT_HUMAN     157    232             
DBREF  7AWM A  223   522  UNP    P43003   EAA1_HUMAN     243    542             
SEQADV 7AWM SER A   23  UNP  P43003    ARG    23 ENGINEERED MUTATION            
SEQADV 7AWM PHE A   44  UNP  P43003    TYR    44 ENGINEERED MUTATION            
SEQADV 7AWM ARG A   46  UNP  P43003    PHE    46 ENGINEERED MUTATION            
SEQADV 7AWM LEU A   50  UNP  P43003    PHE    50 ENGINEERED MUTATION            
SEQADV 7AWM LEU A   51  UNP  P43003    VAL    51 ENGINEERED MUTATION            
SEQADV 7AWM LEU A   56  UNP  P43003    THR    56 ENGINEERED MUTATION            
SEQADV 7AWM LEU A   60  UNP  P43003    VAL    60 ENGINEERED MUTATION            
SEQADV 7AWM VAL A   62  UNP  P43003    THR    62 ENGINEERED MUTATION            
SEQADV 7AWM VAL A   63  UNP  P43003    ILE    63 ENGINEERED MUTATION            
SEQADV 7AWM LEU A   67  UNP  P43003    THR    67 ENGINEERED MUTATION            
SEQADV 7AWM PRO A   72  UNP  P43003    ARG    72 ENGINEERED MUTATION            
SEQADV 7AWM LEU A   73  UNP  P43003    MET    73 ENGINEERED MUTATION            
SEQADV 7AWM PRO A   75  UNP  P43003    TYR    75 ENGINEERED MUTATION            
SEQADV 7AWM ALA A   82  UNP  P43003    SER    82 ENGINEERED MUTATION            
SEQADV 7AWM LYS A   93  UNP  P43003    GLN    93 ENGINEERED MUTATION            
SEQADV 7AWM ILE A   96  UNP  P43003    VAL    96 ENGINEERED MUTATION            
SEQADV 7AWM VAL A  101  UNP  P43003    ILE   101 ENGINEERED MUTATION            
SEQADV 7AWM ILE A  105  UNP  P43003    VAL   105 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  108  UNP  P43003    MET   108 ENGINEERED MUTATION            
SEQADV 7AWM SER A  110  UNP  P43003    ALA   110 ENGINEERED MUTATION            
SEQADV 7AWM ALA A  113  UNP  P43003    SER   113 ENGINEERED MUTATION            
SEQADV 7AWM ARG A  118  UNP  P43003    LYS   118 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  119  UNP  P43003    MET   119 ENGINEERED MUTATION            
SEQADV 7AWM SER A  129  UNP  P43003    THR   129 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  137  UNP  P43003    ILE   137 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  141  UNP  P43003    ILE   141 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  143  UNP  P43003    ILE   143 ENGINEERED MUTATION            
SEQADV 7AWM THR A  155  UNP  Q15758    ASN   163 ENGINEERED MUTATION            
SEQADV 7AWM CYS A  175  UNP  Q15758    SER   183 ENGINEERED MUTATION            
SEQADV 7AWM THR A  204  UNP  Q15758    ASN   212 ENGINEERED MUTATION            
SEQADV 7AWM VAL A  232  UNP  P43003    CYS   252 ENGINEERED MUTATION            
SEQADV 7AWM ALA A  236  UNP  P43003    VAL   256 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  237  UNP  P43003    ILE   257 ENGINEERED MUTATION            
SEQADV 7AWM LYS A  239  UNP  P43003    ASN   259 ENGINEERED MUTATION            
SEQADV 7AWM GLY A  241  UNP  P43003    LYS   261 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  246  UNP  P43003    ALA   266 ENGINEERED MUTATION            
SEQADV 7AWM VAL A  248  UNP  P43003    ARG   268 ENGINEERED MUTATION            
SEQADV 7AWM ASP A  249  UNP  P43003    GLU   269 ENGINEERED MUTATION            
SEQADV 7AWM ASN A  252  UNP  P43003    ASP   272 ENGINEERED MUTATION            
SEQADV 7AWM THR A  258  UNP  P43003    ILE   278 ENGINEERED MUTATION            
SEQADV 7AWM LYS A  260  UNP  P43003    ARG   280 ENGINEERED MUTATION            
SEQADV 7AWM ILE A  264  UNP  P43003    VAL   284 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  271  UNP  P43003    VAL   291 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  287  UNP  P43003    MET   307 ENGINEERED MUTATION            
SEQADV 7AWM GLU A  288  UNP  P43003    GLY   308 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  290  UNP  P43003    ILE   310 ENGINEERED MUTATION            
SEQADV 7AWM GLY A  295  UNP  P43003    ALA   315 ENGINEERED MUTATION            
SEQADV 7AWM MET A  298  UNP  P43003    THR   318 ENGINEERED MUTATION            
SEQADV 7AWM VAL A  306  UNP  P43003    LEU   326 ENGINEERED MUTATION            
SEQADV 7AWM GLY A  309  UNP  P43003    ALA   329 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  310  UNP  P43003    VAL   330 ENGINEERED MUTATION            
SEQADV 7AWM ILE A  316  UNP  P43003    LEU   336 ENGINEERED MUTATION            
SEQADV 7AWM ILE A  320  UNP  P43003    VAL   340 ENGINEERED MUTATION            
SEQADV 7AWM PHE A  326  UNP  P43003    TRP   346 ENGINEERED MUTATION            
SEQADV 7AWM ALA A  330  UNP  P43003    GLY   350 ENGINEERED MUTATION            
SEQADV 7AWM ILE A  332  UNP  P43003    LEU   352 ENGINEERED MUTATION            
SEQADV 7AWM ILE A  366  UNP  P43003    VAL   386 ENGINEERED MUTATION            
SEQADV 7AWM VAL A  388  UNP  P43003    LEU   408 ENGINEERED MUTATION            
SEQADV 7AWM TYR A  399  UNP  P43003    PHE   419 ENGINEERED MUTATION            
SEQADV 7AWM ASP A  402  UNP  P43003    ASN   422 ENGINEERED MUTATION            
SEQADV 7AWM ALA A  437  UNP  P43003    SER   457 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  454  UNP  P43003    PHE   474 ENGINEERED MUTATION            
SEQADV 7AWM PHE A  458  UNP  P43003    LEU   478 ENGINEERED MUTATION            
SEQADV 7AWM MET A  461  UNP  P43003    THR   481 ENGINEERED MUTATION            
SEQADV 7AWM VAL A  462  UNP  P43003    THR   482 ENGINEERED MUTATION            
SEQADV 7AWM ALA A  468  UNP  P43003    SER   488 ENGINEERED MUTATION            
SEQADV 7AWM LYS A  480  UNP  P43003    HIS   500 ENGINEERED MUTATION            
SEQADV 7AWM GLU A  483  UNP  P43003    LYS   503 ENGINEERED MUTATION            
SEQADV 7AWM LYS A  484  UNP  P43003    ASN   504 ENGINEERED MUTATION            
SEQADV 7AWM GLN A  485  UNP  P43003    ARG   505 ENGINEERED MUTATION            
SEQADV 7AWM ALA A  487  UNP  P43003    VAL   507 ENGINEERED MUTATION            
SEQADV 7AWM LEU A  489  UNP  P43003    MET   509 ENGINEERED MUTATION            
SEQRES   1 A  522  MET THR LYS SER ASN GLY GLU GLU PRO LYS MET GLY GLY          
SEQRES   2 A  522  ARG MET GLU ARG PHE GLN GLN GLY VAL SER LYS ARG THR          
SEQRES   3 A  522  LEU LEU ALA LYS LYS LYS VAL GLN ASN ILE THR LYS GLU          
SEQRES   4 A  522  ASP VAL LYS SER PHE LEU ARG ARG ASN ALA LEU LEU LEU          
SEQRES   5 A  522  LEU THR VAL LEU ALA VAL ILE LEU GLY VAL VAL LEU GLY          
SEQRES   6 A  522  PHE LEU LEU ARG PRO TYR PRO LEU SER PRO ARG GLU VAL          
SEQRES   7 A  522  LYS TYR PHE ALA PHE PRO GLY GLU LEU LEU MET ARG MET          
SEQRES   8 A  522  LEU LYS MET LEU ILE LEU PRO LEU ILE VAL SER SER LEU          
SEQRES   9 A  522  ILE THR GLY LEU ALA SER LEU ASP ALA LYS ALA SER GLY          
SEQRES  10 A  522  ARG LEU GLY MET ARG ALA VAL VAL TYR TYR MET SER THR          
SEQRES  11 A  522  THR ILE ILE ALA VAL VAL LEU GLY ILE ILE LEU VAL LEU          
SEQRES  12 A  522  ILE ILE HIS PRO GLY ALA ALA SER ALA ALA ILE THR ALA          
SEQRES  13 A  522  SER VAL GLY ALA ALA GLY SER ALA GLU ASN ALA PRO SER          
SEQRES  14 A  522  LYS GLU VAL LEU ASP CYS PHE LEU ASP LEU ALA ARG ASN          
SEQRES  15 A  522  ILE PHE PRO SER ASN LEU VAL SER ALA ALA PHE ARG SER          
SEQRES  16 A  522  TYR SER THR THR TYR GLU GLU ARG THR ILE THR GLY THR          
SEQRES  17 A  522  ARG VAL LYS VAL PRO VAL GLY GLN GLU VAL GLU GLY MET          
SEQRES  18 A  522  ASN ILE LEU GLY LEU VAL VAL PHE SER MET VAL PHE GLY          
SEQRES  19 A  522  PHE ALA LEU GLY LYS MET GLY GLU GLN GLY GLN LEU LEU          
SEQRES  20 A  522  VAL ASP PHE PHE ASN SER LEU ASN GLU ALA THR MET LYS          
SEQRES  21 A  522  LEU VAL ALA ILE ILE MET TRP TYR ALA PRO LEU GLY ILE          
SEQRES  22 A  522  LEU PHE LEU ILE ALA GLY LYS ILE VAL GLU MET GLU ASP          
SEQRES  23 A  522  LEU GLU VAL LEU GLY GLY GLN LEU GLY MET TYR MET VAL          
SEQRES  24 A  522  THR VAL ILE VAL GLY LEU VAL ILE HIS GLY LEU ILE VAL          
SEQRES  25 A  522  LEU PRO LEU ILE TYR PHE LEU ILE THR ARG LYS ASN PRO          
SEQRES  26 A  522  PHE VAL PHE ILE ALA GLY ILE LEU GLN ALA LEU ILE THR          
SEQRES  27 A  522  ALA LEU GLY THR SER SER SER SER ALA THR LEU PRO ILE          
SEQRES  28 A  522  THR PHE LYS CYS LEU GLU GLU ASN ASN GLY VAL ASP LYS          
SEQRES  29 A  522  ARG ILE THR ARG PHE VAL LEU PRO VAL GLY ALA THR ILE          
SEQRES  30 A  522  ASN MET ASP GLY THR ALA LEU TYR GLU ALA VAL ALA ALA          
SEQRES  31 A  522  ILE PHE ILE ALA GLN VAL ASN ASN TYR GLU LEU ASP PHE          
SEQRES  32 A  522  GLY GLN ILE ILE THR ILE SER ILE THR ALA THR ALA ALA          
SEQRES  33 A  522  SER ILE GLY ALA ALA GLY ILE PRO GLN ALA GLY LEU VAL          
SEQRES  34 A  522  THR MET VAL ILE VAL LEU THR ALA VAL GLY LEU PRO THR          
SEQRES  35 A  522  ASP ASP ILE THR LEU ILE ILE ALA VAL ASP TRP LEU LEU          
SEQRES  36 A  522  ASP ARG PHE ARG THR MET VAL ASN VAL LEU GLY ASP ALA          
SEQRES  37 A  522  LEU GLY ALA GLY ILE VAL GLU HIS LEU SER ARG LYS GLU          
SEQRES  38 A  522  LEU GLU LYS GLN ASP ALA GLU LEU GLY ASN SER VAL ILE          
SEQRES  39 A  522  GLU GLU ASN GLU MET LYS LYS PRO TYR GLN LEU ILE ALA          
SEQRES  40 A  522  GLN ASP ASN GLU THR GLU LYS PRO ILE ASP SER GLU THR          
SEQRES  41 A  522  LYS MET                                                      
HET     NA  A 601       1                                                       
HET     NA  A 602       1                                                       
HET     NA  A 603       1                                                       
HET    ASP  A 604       9                                                       
HET    6Z6  A 605      32                                                       
HET     BA  A 606       1                                                       
HETNAM      NA SODIUM ION                                                       
HETNAM     ASP ASPARTIC ACID                                                    
HETNAM     6Z6 2-AMINO-5,6,7,8-TETRAHYDRO-4-(4-METHOXYPHENYL)-7-                
HETNAM   2 6Z6  (NAPHTHALEN-1-YL)-5-OXO-4H-CHROMENE-3-CARBONITRILE              
HETNAM      BA BARIUM ION                                                       
FORMUL   2   NA    3(NA 1+)                                                     
FORMUL   5  ASP    C4 H7 N O4                                                   
FORMUL   6  6Z6    C27 H22 N2 O3                                                
FORMUL   7   BA    BA 2+                                                        
HELIX    1 AA1 ALA A   29  ILE A   36  1                                   8    
HELIX    2 AA2 ASP A   40  ASN A   48  1                                   9    
HELIX    3 AA3 ASN A   48  ARG A   69  1                                  22    
HELIX    4 AA4 SER A   74  ALA A   82  1                                   9    
HELIX    5 AA5 ALA A   82  LEU A  111  1                                  30    
HELIX    6 AA6 ASP A  112  ILE A  145  1                                  34    
HELIX    7 AA7 VAL A  172  PHE A  184  1                                  13    
HELIX    8 AA8 ASN A  187  ALA A  192  1                                   6    
HELIX    9 AA9 ASN A  222  LYS A  239  1                                  18    
HELIX   10 AB1 GLY A  241  ILE A  281  1                                  41    
HELIX   11 AB2 GLY A  292  ILE A  311  1                                  20    
HELIX   12 AB3 ILE A  311  ARG A  322  1                                  12    
HELIX   13 AB4 ASN A  324  ILE A  332  1                                   9    
HELIX   14 AB5 ILE A  332  SER A  343  1                                  12    
HELIX   15 AB6 THR A  348  GLU A  358  1                                  11    
HELIX   16 AB7 ASP A  363  ASN A  378  1                                  16    
HELIX   17 AB8 MET A  379  ASN A  398  1                                  20    
HELIX   18 AB9 GLY A  404  ALA A  420  1                                  17    
HELIX   19 AC1 GLN A  425  THR A  430  1                                   6    
HELIX   20 AC2 THR A  430  GLY A  439  1                                  10    
HELIX   21 AC3 PRO A  441  LEU A  447  5                                   7    
HELIX   22 AC4 ILE A  448  SER A  478  1                                  31    
HELIX   23 AC5 SER A  478  GLN A  485  1                                   8    
SHEET    1 AA1 2 ARG A 194  TYR A 196  0                                        
SHEET    2 AA1 2 GLU A 217  GLU A 219 -1  O  VAL A 218   N  SER A 195           
LINK         O   TYR A 127                NA    NA A 602     1555   1555  2.25  
LINK         OG1 THR A 130                NA    NA A 602     1555   1555  2.40  
LINK         OG1 THR A 131                NA    NA A 602     1555   1555  2.45  
LINK         OG  SER A 345                NA    NA A 601     1555   1555  3.19  
LINK         O   GLY A 374                NA    NA A 601     1555   1555  2.74  
LINK         O   ALA A 375                NA    NA A 601     1555   1555  3.10  
LINK         O   THR A 376                NA    NA A 603     1555   1555  2.24  
LINK         O   ASN A 378                NA    NA A 601     1555   1555  3.18  
LINK         OD1 ASN A 378                NA    NA A 602     1555   1555  2.24  
LINK         OD1 ASP A 380                NA    NA A 602     1555   1555  2.56  
LINK         O   SER A 417                NA    NA A 603     1555   1555  2.25  
LINK         O   ILE A 418                NA    NA A 603     1555   1555  3.07  
LINK         O   ALA A 420                NA    NA A 603     1555   1555  2.24  
LINK         OD2 ASP A 467                NA    NA A 601     1555   1555  3.18  
CRYST1  122.882  122.882   90.032  90.00  90.00 120.00 P 63          6          
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      0.008138  0.004698  0.000000        0.00000                         
SCALE2      0.000000  0.009397  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011107        0.00000                         
ATOM      1  N   ALA A  29      -2.806  34.031  -5.460  1.00222.27           N  
ANISOU    1  N   ALA A  29    18679  35727  30047    826   2010    519       N  
ATOM      2  CA  ALA A  29      -1.889  35.119  -5.791  1.00223.92           C  
ANISOU    2  CA  ALA A  29    18644  35856  30578    503   2115    505       C  
ATOM      3  C   ALA A  29      -2.234  35.783  -7.131  1.00226.25           C  
ANISOU    3  C   ALA A  29    19223  35847  30894    243   2462    483       C  
ATOM      4  O   ALA A  29      -1.838  36.927  -7.363  1.00226.53           O  
ANISOU    4  O   ALA A  29    19181  35786  31102   -106   2511    506       O  
ATOM      5  CB  ALA A  29      -0.462  34.598  -5.817  1.00226.03           C  
ANISOU    5  CB  ALA A  29    18760  35666  31456    673   2189    355       C  
ATOM      6  N   LYS A  30      -2.965  35.060  -8.010  1.00222.87           N  
ANISOU    6  N   LYS A  30    18857  35792  30030    458   2705    527       N  
ATOM      7  CA  LYS A  30      -3.383  35.540  -9.332  1.00222.39           C  
ANISOU    7  CA  LYS A  30    18943  35773  29780    272   3038    565       C  
ATOM      8  C   LYS A  30      -4.619  36.428  -9.271  1.00222.74           C  
ANISOU    8  C   LYS A  30    19368  35708  29556     -4   2929    642       C  
ATOM      9  O   LYS A  30      -4.684  37.413 -10.007  1.00222.94           O  
ANISOU    9  O   LYS A  30    19445  35734  29530   -316   3102    707       O  
ATOM     10  CB  LYS A  30      -3.618  34.375 -10.294  1.00224.63           C  
ANISOU   10  CB  LYS A  30    19444  35878  30026    585   3337    458       C  
ATOM     11  CG  LYS A  30      -2.544  34.243 -11.370  1.00238.61           C  
ANISOU   11  CG  LYS A  30    21707  36205  32747    447   3685    166       C  
ATOM     12  CD  LYS A  30      -2.953  33.325 -12.518  1.00249.32           C  
ANISOU   12  CD  LYS A  30    23461  37111  34158    615   4003     16       C  
ATOM     13  CE  LYS A  30      -2.911  31.847 -12.197  1.00260.50           C  
ANISOU   13  CE  LYS A  30    25189  37806  35983    886   3933   -204       C  
ATOM     14  NZ  LYS A  30      -4.268  31.287 -11.977  1.00265.43           N  
ANISOU   14  NZ  LYS A  30    26511  37749  36593    905   3728   -298       N  
ATOM     15  N   LYS A  31      -5.597  36.087  -8.409  1.00218.18           N  
ANISOU   15  N   LYS A  31    18748  35631  28521    133   2654    741       N  
ATOM     16  CA  LYS A  31      -6.817  36.879  -8.234  1.00215.98           C  
ANISOU   16  CA  LYS A  31    18631  35618  27812   -113   2516    872       C  
ATOM     17  C   LYS A  31      -6.525  38.135  -7.402  1.00217.94           C  
ANISOU   17  C   LYS A  31    18880  35596  28331   -526   2288    884       C  
ATOM     18  O   LYS A  31      -7.189  39.160  -7.581  1.00216.72           O  
ANISOU   18  O   LYS A  31    18813  35597  27935   -875   2275    991       O  
ATOM     19  CB  LYS A  31      -7.947  36.039  -7.629  1.00216.14           C  
ANISOU   19  CB  LYS A  31    18897  35641  27584    181   2308    861       C  
ATOM     20  CG  LYS A  31      -8.504  35.032  -8.628  1.00223.94           C  
ANISOU   20  CG  LYS A  31    20699  35440  28947    440   2531    610       C  
ATOM     21  CD  LYS A  31      -8.082  33.611  -8.329  1.00230.46           C  
ANISOU   21  CD  LYS A  31    21843  35362  30357    760   2537    368       C  
ATOM     22  CE  LYS A  31      -8.376  32.692  -9.490  1.00235.60           C  
ANISOU   22  CE  LYS A  31    23000  35341  31175    890   2817    192       C  
ATOM     23  NZ  LYS A  31      -7.944  31.298  -9.211  1.00241.33           N  
ANISOU   23  NZ  LYS A  31    23991  35236  32469   1091   2831    -37       N  
ATOM     24  N   LYS A  32      -5.497  38.058  -6.527  1.00216.57           N  
ANISOU   24  N   LYS A  32    18327  35558  28400   -495   2108    863       N  
ATOM     25  CA  LYS A  32      -5.033  39.146  -5.661  1.00217.03           C  
ANISOU   25  CA  LYS A  32    18244  35546  28674   -845   1873    875       C  
ATOM     26  C   LYS A  32      -4.441  40.299  -6.484  1.00220.25           C  
ANISOU   26  C   LYS A  32    18741  35502  29444  -1195   2103    843       C  
ATOM     27  O   LYS A  32      -4.812  41.454  -6.263  1.00219.32           O  
ANISOU   27  O   LYS A  32    18671  35425  29237  -1575   2002    914       O  
ATOM     28  CB  LYS A  32      -3.995  38.629  -4.640  1.00220.19           C  
ANISOU   28  CB  LYS A  32    18516  35578  29566   -645   1651    742       C  
ATOM     29  CG  LYS A  32      -3.752  39.585  -3.467  1.00230.72           C  
ANISOU   29  CG  LYS A  32    20251  35901  31509   -862   1315    574       C  
ATOM     30  CD  LYS A  32      -2.295  40.076  -3.352  1.00236.78           C  
ANISOU   30  CD  LYS A  32    21221  35486  33259   -958   1349    341       C  
ATOM     31  CE  LYS A  32      -2.055  40.972  -2.153  1.00245.43           C  
ANISOU   31  CE  LYS A  32    22362  36305  34584  -1176   1022    287       C  
ATOM     32  NZ  LYS A  32      -2.640  42.331  -2.332  1.00250.73           N  
ANISOU   32  NZ  LYS A  32    23386  36676  35205  -1456   1060    295       N  
ATOM     33  N   VAL A  33      -3.531  39.982  -7.432  1.00219.00           N  
ANISOU   33  N   VAL A  33    18340  35437  29435  -1101   2416    829       N  
ATOM     34  CA  VAL A  33      -2.882  40.961  -8.319  1.00220.46           C  
ANISOU   34  CA  VAL A  33    18451  35476  29839  -1404   2688    853       C  
ATOM     35  C   VAL A  33      -3.911  41.517  -9.337  1.00222.05           C  
ANISOU   35  C   VAL A  33    19079  35499  29791  -1575   2896    920       C  
ATOM     36  O   VAL A  33      -3.756  42.635  -9.823  1.00222.62           O  
ANISOU   36  O   VAL A  33    19168  35473  29945  -1918   3024    986       O  
ATOM     37  CB  VAL A  33      -1.586  40.387  -8.977  1.00224.95           C  
ANISOU   37  CB  VAL A  33    19032  35421  31017  -1176   2982    678       C  
ATOM     38  CG1 VAL A  33      -0.938  41.388  -9.933  1.00226.14           C  
ANISOU   38  CG1 VAL A  33    19132  35250  31543  -1480   3217    675       C  
ATOM     39  CG2 VAL A  33      -0.576  39.959  -7.914  1.00225.66           C  
ANISOU   39  CG2 VAL A  33    18898  35372  31472   -926   2765    561       C  
ATOM     40  N   GLN A  34      -4.973  40.738  -9.618  1.00217.97           N  
ANISOU   40  N   GLN A  34    18607  35522  28691  -1385   2912   1009       N  
ATOM     41  CA  GLN A  34      -6.072  41.100 -10.510  1.00216.51           C  
ANISOU   41  CA  GLN A  34    18682  35504  28079  -1528   3065   1125       C  
ATOM     42  C   GLN A  34      -7.005  42.097  -9.810  1.00217.65           C  
ANISOU   42  C   GLN A  34    19076  35515  28104  -1842   2796   1187       C  
ATOM     43  O   GLN A  34      -7.535  42.994 -10.464  1.00217.14           O  
ANISOU   43  O   GLN A  34    19159  35504  27842  -2151   2908   1305       O  
ATOM     44  CB  GLN A  34      -6.852  39.844 -10.922  1.00216.31           C  
ANISOU   44  CB  GLN A  34    18856  35569  27762  -1118   3145   1080       C  
ATOM     45  CG  GLN A  34      -7.349  39.856 -12.358  1.00225.03           C  
ANISOU   45  CG  GLN A  34    20807  35472  29221  -1048   3485    906       C  
ATOM     46  CD  GLN A  34      -7.568  38.455 -12.866  1.00236.01           C  
ANISOU   46  CD  GLN A  34    23043  35400  31231   -607   3640    544       C  
ATOM     47  OE1 GLN A  34      -6.664  37.828 -13.422  1.00233.87           O  
ANISOU   47  OE1 GLN A  34    22557  35186  31116   -476   3870    481       O  
ATOM     48  NE2 GLN A  34      -8.772  37.933 -12.683  1.00228.20           N  
ANISOU   48  NE2 GLN A  34    21864  35342  29499   -461   3511    693       N  
ATOM     49  N   ASN A  35      -7.193  41.945  -8.482  1.00214.79           N  
ANISOU   49  N   ASN A  35    18482  35547  27582  -1846   2436   1215       N  
ATOM     50  CA  ASN A  35      -8.054  42.791  -7.647  1.00213.59           C  
ANISOU   50  CA  ASN A  35    18438  35509  27207  -2166   2146   1292       C  
ATOM     51  C   ASN A  35      -7.532  44.237  -7.481  1.00217.03           C  
ANISOU   51  C   ASN A  35    18984  35427  28050  -2582   2114   1263       C  
ATOM     52  O   ASN A  35      -8.322  45.145  -7.216  1.00216.15           O  
ANISOU   52  O   ASN A  35    19034  35360  27732  -2917   1975   1343       O  
ATOM     53  CB  ASN A  35      -8.265  42.121  -6.279  1.00213.51           C  
ANISOU   53  CB  ASN A  35    18398  35531  27195  -1936   1801   1218       C  
ATOM     54  CG  ASN A  35      -9.309  42.774  -5.405  1.00227.17           C  
ANISOU   54  CG  ASN A  35    21305  35348  29663  -1843   1551    903       C  
ATOM     55  OD1 ASN A  35     -10.515  42.691  -5.660  1.00221.78           O  
ANISOU   55  OD1 ASN A  35    20686  35148  28433  -1902   1546   1034       O  
ATOM     56  ND2 ASN A  35      -8.861  43.431  -4.347  1.00222.05           N  
ANISOU   56  ND2 ASN A  35    20274  35143  28954  -2127   1281    957       N  
ATOM     57  N   ILE A  36      -6.216  44.448  -7.656  1.00216.19           N  
ANISOU   57  N   ILE A  36    18518  35372  28251  -2669   2238   1251       N  
ATOM     58  CA  ILE A  36      -5.586  45.754  -7.473  1.00217.29           C  
ANISOU   58  CA  ILE A  36    18598  35273  28690  -3085   2208   1262       C  
ATOM     59  C   ILE A  36      -5.854  46.750  -8.640  1.00219.95           C  
ANISOU   59  C   ILE A  36    19258  35203  29111  -3313   2516   1326       C  
ATOM     60  O   ILE A  36      -5.534  47.931  -8.490  1.00220.38           O  
ANISOU   60  O   ILE A  36    19341  34976  29418  -3646   2499   1338       O  
ATOM     61  CB  ILE A  36      -4.063  45.591  -7.136  1.00221.54           C  
ANISOU   61  CB  ILE A  36    18927  35358  29891  -2937   2201   1092       C  
ATOM     62  CG1 ILE A  36      -3.560  46.711  -6.175  1.00223.10           C  
ANISOU   62  CG1 ILE A  36    19052  35300  30414  -3289   1982   1050       C  
ATOM     63  CG2 ILE A  36      -3.146  45.459  -8.356  1.00223.60           C  
ANISOU   63  CG2 ILE A  36    19064  35476  30417  -2818   2596   1075       C  
ATOM     64  CD1 ILE A  36      -4.003  46.633  -4.662  1.00226.63           C  
ANISOU   64  CD1 ILE A  36    19948  35252  30910  -3346   1630    952       C  
ATOM     65  N   THR A  37      -6.508  46.316  -9.741  1.00216.95           N  
ANISOU   65  N   THR A  37    18877  35324  28230  -3273   2753   1474       N  
ATOM     66  CA  THR A  37      -6.753  47.167 -10.916  1.00217.14           C  
ANISOU   66  CA  THR A  37    19093  35237  28174  -3506   3055   1596       C  
ATOM     67  C   THR A  37      -7.693  48.409 -10.718  1.00219.18           C  
ANISOU   67  C   THR A  37    19732  35146  28402  -3879   2955   1672       C  
ATOM     68  O   THR A  37      -7.711  49.252 -11.622  1.00219.69           O  
ANISOU   68  O   THR A  37    19949  34992  28532  -4072   3209   1764       O  
ATOM     69  CB  THR A  37      -7.226  46.349 -12.133  1.00222.15           C  
ANISOU   69  CB  THR A  37    20135  35522  28751  -3086   3334   1526       C  
ATOM     70  OG1 THR A  37      -8.183  45.361 -11.743  1.00219.58           O  
ANISOU   70  OG1 THR A  37    19894  35515  28022  -2885   3126   1528       O  
ATOM     71  CG2 THR A  37      -6.076  45.698 -12.867  1.00221.78           C  
ANISOU   71  CG2 THR A  37    19835  35534  28898  -2805   3600   1447       C  
ATOM     72  N   LYS A  38      -8.424  48.564  -9.566  1.00215.27           N  
ANISOU   72  N   LYS A  38    19172  35035  27587  -4138   2584   1731       N  
ATOM     73  CA  LYS A  38      -9.346  49.703  -9.241  1.00214.29           C  
ANISOU   73  CA  LYS A  38    19310  34788  27322  -4582   2437   1831       C  
ATOM     74  C   LYS A  38     -10.359  50.018 -10.377  1.00215.61           C  
ANISOU   74  C   LYS A  38    19876  34789  27257  -4642   2660   1960       C  
ATOM     75  O   LYS A  38     -10.762  51.167 -10.590  1.00215.62           O  
ANISOU   75  O   LYS A  38    20072  34517  27337  -4983   2734   2057       O  
ATOM     76  CB  LYS A  38      -8.562  50.972  -8.813  1.00217.67           C  
ANISOU   76  CB  LYS A  38    19757  34630  28316  -4821   2405   1746       C  
ATOM     77  CG  LYS A  38      -7.664  50.780  -7.597  1.00226.80           C  
ANISOU   77  CG  LYS A  38    21055  34832  30286  -4349   2195   1385       C  
ATOM     78  CD  LYS A  38      -6.862  52.037  -7.328  1.00234.89           C  
ANISOU   78  CD  LYS A  38    22274  34911  32063  -4380   2184   1217       C  
ATOM     79  CE  LYS A  38      -5.568  51.717  -6.647  1.00241.97           C  
ANISOU   79  CE  LYS A  38    23180  34934  33824  -3906   2124    903       C  
ATOM     80  NZ  LYS A  38      -4.721  52.926  -6.505  1.00251.31           N  
ANISOU   80  NZ  LYS A  38    24347  35589  35551  -4058   2079    808       N  
ATOM     81  N   GLU A  39     -10.753  48.965 -11.094  1.00211.92           N  
ANISOU   81  N   GLU A  39    19288  34992  26241  -4484   2733   2067       N  
ATOM     82  CA  GLU A  39     -11.617  49.040 -12.253  1.00210.93           C  
ANISOU   82  CA  GLU A  39    19419  34950  25776  -4537   2935   2216       C  
ATOM     83  C   GLU A  39     -13.084  48.806 -11.931  1.00210.93           C  
ANISOU   83  C   GLU A  39    19754  34948  25443  -4478   2737   2227       C  
ATOM     84  O   GLU A  39     -13.428  47.872 -11.203  1.00210.04           O  
ANISOU   84  O   GLU A  39    19494  35184  25129  -4259   2541   2162       O  
ATOM     85  CB  GLU A  39     -11.129  48.035 -13.308  1.00212.39           C  
ANISOU   85  CB  GLU A  39    19534  35175  25989  -4108   3261   2160       C  
ATOM     86  CG  GLU A  39     -11.864  48.128 -14.636  1.00218.51           C  
ANISOU   86  CG  GLU A  39    20904  35321  26797  -3876   3535   2139       C  
ATOM     87  CD  GLU A  39     -11.865  46.896 -15.520  1.00230.32           C  
ANISOU   87  CD  GLU A  39    22958  35787  28766  -3102   3819   1810       C  
ATOM     88  OE1 GLU A  39     -12.811  46.756 -16.329  1.00222.23           O  
ANISOU   88  OE1 GLU A  39    21803  35635  27001  -3263   3886   2047       O  
ATOM     89  OE2 GLU A  39     -10.900  46.101 -15.451  1.00228.01           O  
ANISOU   89  OE2 GLU A  39    22203  35939  28492  -2988   3889   1774       O  
ATOM     90  N   ASP A  40     -13.950  49.668 -12.507  1.00207.99           N  
ANISOU   90  N   ASP A  40    19566  34752  24706  -4891   2771   2449       N  
ATOM     91  CA  ASP A  40     -15.413  49.636 -12.503  1.00206.17           C  
ANISOU   91  CA  ASP A  40    19572  34753  24010  -5006   2617   2556       C  
ATOM     92  C   ASP A  40     -16.099  49.723 -11.130  1.00206.71           C  
ANISOU   92  C   ASP A  40    19715  34788  24035  -5136   2247   2482       C  
ATOM     93  O   ASP A  40     -17.154  49.085 -10.982  1.00203.96           O  
ANISOU   93  O   ASP A  40    19489  34626  23380  -4992   2119   2476       O  
ATOM     94  CB  ASP A  40     -15.956  48.388 -13.261  1.00206.70           C  
ANISOU   94  CB  ASP A  40    19673  35045  23819  -4513   2763   2512       C  
ATOM     95  CG  ASP A  40     -15.602  48.210 -14.732  1.00215.10           C  
ANISOU   95  CG  ASP A  40    21145  35293  25289  -4043   3174   2375       C  
ATOM     96  OD1 ASP A  40     -15.049  49.159 -15.343  1.00216.69           O  
ANISOU   96  OD1 ASP A  40    21474  35143  25716  -4255   3363   2451       O  
ATOM     97  OD2 ASP A  40     -15.909  47.137 -15.283  1.00218.77           O  
ANISOU   97  OD2 ASP A  40    21784  35563  25775  -3528   3303   2219       O  
ATOM     98  N   VAL A  41     -15.628  50.558 -10.170  1.00203.90           N  
ANISOU   98  N   VAL A  41    19189  34456  23830  -5544   2059   2486       N  
ATOM     99  CA  VAL A  41     -16.419  50.627  -8.929  1.00202.31           C  
ANISOU   99  CA  VAL A  41    19061  34294  23515  -5736   1704   2426       C  
ATOM    100  C   VAL A  41     -17.604  51.632  -9.064  1.00203.61           C  
ANISOU  100  C   VAL A  41    19747  34031  23584  -6079   1609   2504       C  
ATOM    101  O   VAL A  41     -18.625  51.433  -8.405  1.00200.78           O  
ANISOU  101  O   VAL A  41    19623  33598  23067  -6027   1405   2444       O  
ATOM    102  CB  VAL A  41     -15.625  50.808  -7.605  1.00206.22           C  
ANISOU  102  CB  VAL A  41    19440  34397  24518  -5672   1543   2216       C  
ATOM    103  CG1 VAL A  41     -15.429  52.279  -7.237  1.00206.75           C  
ANISOU  103  CG1 VAL A  41    19739  34080  24737  -6171   1365   2214       C  
ATOM    104  CG2 VAL A  41     -16.308  50.049  -6.465  1.00205.21           C  
ANISOU  104  CG2 VAL A  41    19096  34598  24278  -5364   1320   2091       C  
ATOM    105  N   LYS A  42     -17.484  52.664  -9.927  1.00201.25           N  
ANISOU  105  N   LYS A  42    19563  33629  23274  -6503   1755   2690       N  
ATOM    106  CA  LYS A  42     -18.545  53.663 -10.142  1.00199.76           C  
ANISOU  106  CA  LYS A  42    19851  33080  22969  -6886   1679   2812       C  
ATOM    107  C   LYS A  42     -19.784  53.048 -10.830  1.00198.11           C  
ANISOU  107  C   LYS A  42    20026  32645  22603  -6479   1758   2808       C  
ATOM    108  O   LYS A  42     -20.916  53.446 -10.537  1.00194.69           O  
ANISOU  108  O   LYS A  42    20082  31672  22220  -6440   1620   2748       O  
ATOM    109  CB  LYS A  42     -17.994  54.869 -10.929  1.00203.49           C  
ANISOU  109  CB  LYS A  42    20499  33032  23785  -7072   1896   2899       C  
ATOM    110  CG  LYS A  42     -18.938  56.067 -11.008  1.00215.41           C  
ANISOU  110  CG  LYS A  42    22750  33395  25699  -6918   1918   2830       C  
ATOM    111  CD  LYS A  42     -18.550  56.979 -12.148  1.00223.19           C  
ANISOU  111  CD  LYS A  42    23989  33590  27223  -6618   2286   2832       C  
ATOM    112  CE  LYS A  42     -19.636  57.977 -12.442  1.00229.81           C  
ANISOU  112  CE  LYS A  42    25427  33594  28295  -6467   2361   2857       C  
ATOM    113  NZ  LYS A  42     -19.242  58.901 -13.531  1.00236.93           N  
ANISOU  113  NZ  LYS A  42    26490  33794  29740  -6159   2737   2858       N  
ATOM    114  N   SER A  43     -19.557  52.064 -11.725  1.00193.76           N  
ANISOU  114  N   SER A  43    19269  32445  21905  -6119   1988   2839       N  
ATOM    115  CA  SER A  43     -20.605  51.323 -12.431  1.00189.37           C  
ANISOU  115  CA  SER A  43    19043  31677  21234  -5660   2083   2794       C  
ATOM    116  C   SER A  43     -21.308  50.390 -11.438  1.00187.90           C  
ANISOU  116  C   SER A  43    18983  31300  21109  -5212   1885   2559       C  
ATOM    117  O   SER A  43     -22.521  50.209 -11.534  1.00184.42           O  
ANISOU  117  O   SER A  43    18975  30446  20652  -4976   1832   2492       O  
ATOM    118  CB  SER A  43     -20.010  50.516 -13.579  1.00194.49           C  
ANISOU  118  CB  SER A  43    19396  32798  21705  -5424   2379   2867       C  
ATOM    119  OG  SER A  43     -19.025  49.609 -13.111  1.00203.03           O  
ANISOU  119  OG  SER A  43    19990  34333  22818  -5183   2397   2760       O  
ATOM    120  N   PHE A  44     -20.542  49.819 -10.477  1.00183.51           N  
ANISOU  120  N   PHE A  44    18050  31054  20623  -5106   1772   2444       N  
ATOM    121  CA  PHE A  44     -21.026  48.929  -9.420  1.00179.44           C  
ANISOU  121  CA  PHE A  44    17607  30406  20165  -4708   1579   2241       C  
ATOM    122  C   PHE A  44     -21.922  49.695  -8.443  1.00179.01           C  
ANISOU  122  C   PHE A  44    17954  29833  20227  -4886   1321   2160       C  
ATOM    123  O   PHE A  44     -22.991  49.194  -8.107  1.00174.87           O  
ANISOU  123  O   PHE A  44    17763  28971  19709  -4567   1230   2040       O  
ATOM    124  CB  PHE A  44     -19.846  48.257  -8.683  1.00183.71           C  
ANISOU  124  CB  PHE A  44    17614  31449  20739  -4588   1524   2178       C  
ATOM    125  CG  PHE A  44     -20.229  47.326  -7.556  1.00182.43           C  
ANISOU  125  CG  PHE A  44    17504  31184  20627  -4183   1326   1996       C  
ATOM    126  CD1 PHE A  44     -20.666  46.035  -7.817  1.00183.16           C  
ANISOU  126  CD1 PHE A  44    17669  31271  20653  -3639   1410   1908       C  
ATOM    127  CD2 PHE A  44     -20.130  47.735  -6.230  1.00184.48           C  
ANISOU  127  CD2 PHE A  44    17745  31359  20991  -4357   1057   1913       C  
ATOM    128  CE1 PHE A  44     -21.024  45.177  -6.774  1.00181.83           C  
ANISOU  128  CE1 PHE A  44    17564  30992  20531  -3282   1234   1762       C  
ATOM    129  CE2 PHE A  44     -20.490  46.878  -5.187  1.00185.13           C  
ANISOU  129  CE2 PHE A  44    17884  31356  21101  -3987    881   1765       C  
ATOM    130  CZ  PHE A  44     -20.937  45.605  -5.466  1.00181.07           C  
ANISOU  130  CZ  PHE A  44    17448  30821  20529  -3455    973   1701       C  
ATOM    131  N   LEU A  45     -21.498  50.903  -8.006  1.00176.64           N  
ANISOU  131  N   LEU A  45    17628  29470  20018  -5399   1212   2220       N  
ATOM    132  CA  LEU A  45     -22.248  51.760  -7.078  1.00174.36           C  
ANISOU  132  CA  LEU A  45    17713  28698  19837  -5610    975   2134       C  
ATOM    133  C   LEU A  45     -23.585  52.223  -7.673  1.00173.08           C  
ANISOU  133  C   LEU A  45    18104  28001  19659  -5567   1008   2171       C  
ATOM    134  O   LEU A  45     -24.591  52.257  -6.960  1.00168.50           O  
ANISOU  134  O   LEU A  45    17870  27024  19129  -5420    842   2041       O  
ATOM    135  CB  LEU A  45     -21.399  52.971  -6.646  1.00178.59           C  
ANISOU  135  CB  LEU A  45    18088  29303  20463  -6199    878   2194       C  
ATOM    136  CG  LEU A  45     -20.239  52.687  -5.689  1.00185.61           C  
ANISOU  136  CG  LEU A  45    18480  30650  21393  -6281    748   2115       C  
ATOM    137  CD1 LEU A  45     -19.104  53.686  -5.885  1.00191.03           C  
ANISOU  137  CD1 LEU A  45    18859  31602  22123  -6867    782   2245       C  
ATOM    138  CD2 LEU A  45     -20.712  52.667  -4.242  1.00184.23           C  
ANISOU  138  CD2 LEU A  45    18472  30241  21288  -6199    456   1914       C  
ATOM    139  N   ARG A  46     -23.590  52.562  -8.982  1.00170.29           N  
ANISOU  139  N   ARG A  46    17819  27661  19222  -5683   1224   2353       N  
ATOM    140  CA  ARG A  46     -24.772  53.004  -9.730  1.00167.47           C  
ANISOU  140  CA  ARG A  46    17948  26858  18824  -5639   1275   2425       C  
ATOM    141  C   ARG A  46     -25.787  51.868  -9.871  1.00165.79           C  
ANISOU  141  C   ARG A  46    17923  26531  18538  -5092   1288   2303       C  
ATOM    142  O   ARG A  46     -26.954  52.058  -9.528  1.00162.43           O  
ANISOU  142  O   ARG A  46    17895  25668  18150  -4970   1166   2227       O  
ATOM    143  CB  ARG A  46     -24.374  53.559 -11.111  1.00169.69           C  
ANISOU  143  CB  ARG A  46    18198  27274  19004  -5883   1515   2667       C  
ATOM    144  CG  ARG A  46     -23.871  55.006 -11.076  1.00181.94           C  
ANISOU  144  CG  ARG A  46    19799  28689  20640  -6475   1490   2821       C  
ATOM    145  CD  ARG A  46     -23.498  55.534 -12.451  1.00190.21           C  
ANISOU  145  CD  ARG A  46    20828  29875  21569  -6701   1742   3084       C  
ATOM    146  NE  ARG A  46     -23.480  57.001 -12.494  1.00197.69           N  
ANISOU  146  NE  ARG A  46    22019  30496  22600  -7223   1708   3248       N  
ATOM    147  CZ  ARG A  46     -24.546  57.761 -12.736  1.00208.43           C  
ANISOU  147  CZ  ARG A  46    23892  31328  23974  -7254   1661   3322       C  
ATOM    148  NH1 ARG A  46     -25.733  57.205 -12.952  1.00191.85           N  
ANISOU  148  NH1 ARG A  46    22092  28993  21808  -6807   1637   3243       N  
ATOM    149  NH2 ARG A  46     -24.437  59.083 -12.753  1.00198.21           N  
ANISOU  149  NH2 ARG A  46    22813  29732  22765  -7732   1634   3475       N  
ATOM    150  N   ARG A  47     -25.331  50.683 -10.337  1.00161.04           N  
ANISOU  150  N   ARG A  47    17029  26324  17837  -4766   1434   2276       N  
ATOM    151  CA  ARG A  47     -26.155  49.486 -10.523  1.00156.93           C  
ANISOU  151  CA  ARG A  47    16645  25743  17241  -4258   1467   2156       C  
ATOM    152  C   ARG A  47     -26.683  48.888  -9.209  1.00156.05           C  
ANISOU  152  C   ARG A  47    16617  25452  17223  -3999   1251   1955       C  
ATOM    153  O   ARG A  47     -27.895  48.688  -9.084  1.00152.28           O  
ANISOU  153  O   ARG A  47    16495  24619  16747  -3784   1181   1874       O  
ATOM    154  CB  ARG A  47     -25.396  48.423 -11.341  1.00159.48           C  
ANISOU  154  CB  ARG A  47    16617  26544  17436  -4005   1687   2174       C  
ATOM    155  CG  ARG A  47     -25.689  48.463 -12.839  1.00169.60           C  
ANISOU  155  CG  ARG A  47    18126  27737  18576  -3644   1823   2145       C  
ATOM    156  CD  ARG A  47     -24.960  47.357 -13.619  1.00184.27           C  
ANISOU  156  CD  ARG A  47    19672  30061  20280  -3482   2082   2193       C  
ATOM    157  NE  ARG A  47     -25.510  46.004 -13.419  1.00192.91           N  
ANISOU  157  NE  ARG A  47    20695  31268  21334  -2984   2111   2018       N  
ATOM    158  CZ  ARG A  47     -25.686  45.101 -14.386  1.00206.61           C  
ANISOU  158  CZ  ARG A  47    22466  33126  22910  -2692   2296   1986       C  
ATOM    159  NH1 ARG A  47     -25.384  45.397 -15.646  1.00195.10           N  
ANISOU  159  NH1 ARG A  47    21108  31721  21298  -2835   2470   2121       N  
ATOM    160  NH2 ARG A  47     -26.173  43.900 -14.102  1.00190.59           N  
ANISOU  160  NH2 ARG A  47    20391  31157  20867  -2255   2307   1815       N  
ATOM    161  N   ASN A  48     -25.777  48.609  -8.241  1.00151.82           N  
ANISOU  161  N   ASN A  48    15748  25178  16758  -4026   1146   1883       N  
ATOM    162  CA  ASN A  48     -26.093  47.990  -6.943  1.00148.14           C  
ANISOU  162  CA  ASN A  48    15310  24614  16361  -3786    946   1711       C  
ATOM    163  C   ASN A  48     -26.509  48.983  -5.838  1.00148.62           C  
ANISOU  163  C   ASN A  48    15596  24341  16531  -4060    715   1649       C  
ATOM    164  O   ASN A  48     -26.234  48.727  -4.662  1.00147.98           O  
ANISOU  164  O   ASN A  48    15390  24332  16502  -4018    544   1540       O  
ATOM    165  CB  ASN A  48     -24.919  47.115  -6.461  1.00150.72           C  
ANISOU  165  CB  ASN A  48    15163  25416  16687  -3624    945   1671       C  
ATOM    166  CG  ASN A  48     -24.431  46.089  -7.456  1.00172.98           C  
ANISOU  166  CG  ASN A  48    17746  28575  19401  -3316   1172   1705       C  
ATOM    167  OD1 ASN A  48     -24.070  46.402  -8.598  1.00168.02           O  
ANISOU  167  OD1 ASN A  48    17031  28113  18695  -3455   1371   1829       O  
ATOM    168  ND2 ASN A  48     -24.348  44.844  -7.021  1.00163.81           N  
ANISOU  168  ND2 ASN A  48    16468  27539  18232  -2894   1149   1597       N  
ATOM    169  N   ALA A  49     -27.205  50.081  -6.206  1.00143.04           N  
ANISOU  169  N   ALA A  49    15234  23266  15848  -4316    709   1715       N  
ATOM    170  CA  ALA A  49     -27.669  51.121  -5.280  1.00141.57           C  
ANISOU  170  CA  ALA A  49    15314  22716  15761  -4577    512   1652       C  
ATOM    171  C   ALA A  49     -28.457  50.540  -4.108  1.00140.23           C  
ANISOU  171  C   ALA A  49    15306  22354  15621  -4289    335   1467       C  
ATOM    172  O   ALA A  49     -28.057  50.718  -2.956  1.00141.01           O  
ANISOU  172  O   ALA A  49    15302  22504  15772  -4406    163   1369       O  
ATOM    173  CB  ALA A  49     -28.506  52.153  -6.020  1.00142.02           C  
ANISOU  173  CB  ALA A  49    15766  22370  15824  -4757    561   1753       C  
ATOM    174  N   LEU A  50     -29.534  49.798  -4.411  1.00131.25           N  
ANISOU  174  N   LEU A  50    14398  21033  14439  -3918    381   1420       N  
ATOM    175  CA  LEU A  50     -30.399  49.158  -3.427  1.00126.88           C  
ANISOU  175  CA  LEU A  50    14014  20293  13902  -3627    245   1263       C  
ATOM    176  C   LEU A  50     -29.662  48.065  -2.635  1.00129.20           C  
ANISOU  176  C   LEU A  50    13983  20924  14183  -3413    186   1187       C  
ATOM    177  O   LEU A  50     -29.745  48.062  -1.407  1.00128.40           O  
ANISOU  177  O   LEU A  50    13906  20766  14113  -3408      9   1079       O  
ATOM    178  CB  LEU A  50     -31.673  48.626  -4.119  1.00123.52           C  
ANISOU  178  CB  LEU A  50    13881  19623  13429  -3317    329   1252       C  
ATOM    179  CG  LEU A  50     -32.822  48.087  -3.267  1.00124.48           C  
ANISOU  179  CG  LEU A  50    14241  19490  13566  -3043    213   1110       C  
ATOM    180  CD1 LEU A  50     -33.243  49.070  -2.185  1.00124.48           C  
ANISOU  180  CD1 LEU A  50    14449  19212  13636  -3244     36   1029       C  
ATOM    181  CD2 LEU A  50     -34.002  47.746  -4.137  1.00124.09           C  
ANISOU  181  CD2 LEU A  50    14451  19227  13470  -2818    305   1121       C  
ATOM    182  N   LEU A  51     -28.909  47.178  -3.324  1.00125.18           N  
ANISOU  182  N   LEU A  51    13172  20771  13618  -3234    332   1246       N  
ATOM    183  CA  LEU A  51     -28.141  46.100  -2.688  1.00124.83           C  
ANISOU  183  CA  LEU A  51    12804  21065  13562  -2993    292   1195       C  
ATOM    184  C   LEU A  51     -27.183  46.641  -1.622  1.00129.44           C  
ANISOU  184  C   LEU A  51    13135  21855  14190  -3261    122   1174       C  
ATOM    185  O   LEU A  51     -27.185  46.128  -0.506  1.00128.46           O  
ANISOU  185  O   LEU A  51    12969  21768  14070  -3106    -33   1083       O  
ATOM    186  CB  LEU A  51     -27.375  45.275  -3.735  1.00126.39           C  
ANISOU  186  CB  LEU A  51    12708  21619  13695  -2803    498   1271       C  
ATOM    187  CG  LEU A  51     -26.552  44.103  -3.197  1.00132.09           C  
ANISOU  187  CG  LEU A  51    13089  22695  14405  -2502    477   1232       C  
ATOM    188  CD1 LEU A  51     -27.056  42.799  -3.738  1.00130.53           C  
ANISOU  188  CD1 LEU A  51    12982  22455  14157  -2048    600   1189       C  
ATOM    189  CD2 LEU A  51     -25.089  44.278  -3.521  1.00138.36           C  
ANISOU  189  CD2 LEU A  51    13417  23967  15187  -2665    557   1324       C  
ATOM    190  N   LEU A  52     -26.395  47.683  -1.961  1.00127.67           N  
ANISOU  190  N   LEU A  52    12755  21761  13991  -3676    146   1261       N  
ATOM    191  CA  LEU A  52     -25.430  48.305  -1.049  1.00129.63           C  
ANISOU  191  CA  LEU A  52    12750  22224  14281  -3997    -16   1239       C  
ATOM    192  C   LEU A  52     -26.108  49.100   0.063  1.00131.18           C  
ANISOU  192  C   LEU A  52    13257  22064  14522  -4183   -232   1120       C  
ATOM    193  O   LEU A  52     -25.554  49.184   1.160  1.00132.39           O  
ANISOU  193  O   LEU A  52    13243  22377  14681  -4291   -416   1041       O  
ATOM    194  CB  LEU A  52     -24.396  49.167  -1.804  1.00133.39           C  
ANISOU  194  CB  LEU A  52    12962  22947  14772  -4411     89   1372       C  
ATOM    195  CG  LEU A  52     -23.471  48.431  -2.793  1.00139.85           C  
ANISOU  195  CG  LEU A  52    13383  24222  15533  -4258    303   1485       C  
ATOM    196  CD1 LEU A  52     -22.755  49.409  -3.717  1.00143.45           C  
ANISOU  196  CD1 LEU A  52    13683  24828  15993  -4689    444   1637       C  
ATOM    197  CD2 LEU A  52     -22.478  47.524  -2.073  1.00143.69           C  
ANISOU  197  CD2 LEU A  52    13423  25168  16005  -4049    225   1443       C  
ATOM    198  N   LEU A  53     -27.313  49.656  -0.205  1.00124.06           N  
ANISOU  198  N   LEU A  53    12801  20695  13640  -4200   -213   1099       N  
ATOM    199  CA  LEU A  53     -28.089  50.410   0.784  1.00122.32           C  
ANISOU  199  CA  LEU A  53    12916  20104  13457  -4330   -394    974       C  
ATOM    200  C   LEU A  53     -28.541  49.533   1.959  1.00124.06           C  
ANISOU  200  C   LEU A  53    13177  20321  13638  -4008   -536    837       C  
ATOM    201  O   LEU A  53     -28.461  49.970   3.109  1.00124.65           O  
ANISOU  201  O   LEU A  53    13292  20355  13715  -4155   -725    724       O  
ATOM    202  CB  LEU A  53     -29.298  51.088   0.137  1.00120.16           C  
ANISOU  202  CB  LEU A  53    13085  19362  13210  -4351   -321    996       C  
ATOM    203  CG  LEU A  53     -29.117  52.541  -0.254  1.00127.01           C  
ANISOU  203  CG  LEU A  53    14096  20022  14139  -4802   -317   1064       C  
ATOM    204  CD1 LEU A  53     -30.141  52.943  -1.291  1.00125.63           C  
ANISOU  204  CD1 LEU A  53    14271  19493  13968  -4738   -188   1151       C  
ATOM    205  CD2 LEU A  53     -29.216  53.453   0.957  1.00130.05           C  
ANISOU  205  CD2 LEU A  53    14652  20186  14575  -5059   -527    919       C  
ATOM    206  N   THR A  54     -29.000  48.294   1.667  1.00117.65           N  
ANISOU  206  N   THR A  54    12364  19555  12784  -3580   -443    848       N  
ATOM    207  CA  THR A  54     -29.440  47.315   2.668  1.00115.07           C  
ANISOU  207  CA  THR A  54    12077  19229  12415  -3246   -548    752       C  
ATOM    208  C   THR A  54     -28.241  46.793   3.465  1.00120.04           C  
ANISOU  208  C   THR A  54    12313  20285  13012  -3224   -662    746       C  
ATOM    209  O   THR A  54     -28.412  46.427   4.626  1.00119.62           O  
ANISOU  209  O   THR A  54    12293  20239  12919  -3100   -819    660       O  
ATOM    210  CB  THR A  54     -30.240  46.169   2.033  1.00121.41           C  
ANISOU  210  CB  THR A  54    13001  19939  13191  -2832   -407    774       C  
ATOM    211  OG1 THR A  54     -29.402  45.460   1.123  1.00124.04           O  
ANISOU  211  OG1 THR A  54    13031  20591  13507  -2706   -256    871       O  
ATOM    212  CG2 THR A  54     -31.512  46.641   1.331  1.00117.34           C  
ANISOU  212  CG2 THR A  54    12869  19019  12695  -2831   -321    772       C  
ATOM    213  N   VAL A  55     -27.037  46.750   2.843  1.00117.97           N  
ANISOU  213  N   VAL A  55    11668  20398  12758  -3335   -582    844       N  
ATOM    214  CA  VAL A  55     -25.793  46.339   3.508  1.00120.25           C  
ANISOU  214  CA  VAL A  55    11527  21144  13019  -3333   -691    854       C  
ATOM    215  C   VAL A  55     -25.429  47.455   4.505  1.00126.14           C  
ANISOU  215  C   VAL A  55    12266  21886  13774  -3747   -906    770       C  
ATOM    216  O   VAL A  55     -25.120  47.166   5.664  1.00126.41           O  
ANISOU  216  O   VAL A  55    12187  22084  13757  -3689  -1095    698       O  
ATOM    217  CB  VAL A  55     -24.642  46.016   2.508  1.00126.47           C  
ANISOU  217  CB  VAL A  55    11892  22350  13812  -3334   -527    980       C  
ATOM    218  CG1 VAL A  55     -23.318  45.767   3.234  1.00129.73           C  
ANISOU  218  CG1 VAL A  55    11830  23259  14202  -3377   -659    991       C  
ATOM    219  CG2 VAL A  55     -24.997  44.816   1.637  1.00124.21           C  
ANISOU  219  CG2 VAL A  55    11629  22067  13500  -2890   -330   1028       C  
ATOM    220  N   LEU A  56     -25.551  48.727   4.056  1.00123.52           N  
ANISOU  220  N   LEU A  56    12099  21333  13500  -4155   -878    776       N  
ATOM    221  CA  LEU A  56     -25.322  49.943   4.843  1.00125.44           C  
ANISOU  221  CA  LEU A  56    12416  21479  13766  -4595  -1061    683       C  
ATOM    222  C   LEU A  56     -26.351  50.033   5.979  1.00127.43           C  
ANISOU  222  C   LEU A  56    13038  21401  13981  -4484  -1222    523       C  
ATOM    223  O   LEU A  56     -26.023  50.545   7.050  1.00129.01           O  
ANISOU  223  O   LEU A  56    13216  21653  14150  -4702  -1427    406       O  
ATOM    224  CB  LEU A  56     -25.408  51.182   3.924  1.00126.54           C  
ANISOU  224  CB  LEU A  56    12725  21370  13986  -4993   -953    748       C  
ATOM    225  CG  LEU A  56     -25.385  52.571   4.570  1.00133.14           C  
ANISOU  225  CG  LEU A  56    13754  21966  14866  -5465  -1114    645       C  
ATOM    226  CD1 LEU A  56     -23.998  52.931   5.070  1.00137.64           C  
ANISOU  226  CD1 LEU A  56    13912  22949  15437  -5826  -1248    634       C  
ATOM    227  CD2 LEU A  56     -25.896  53.622   3.613  1.00135.36           C  
ANISOU  227  CD2 LEU A  56    14344  21860  15226  -5721   -983    722       C  
ATOM    228  N   ALA A  57     -27.586  49.524   5.739  1.00120.15           N  
ANISOU  228  N   ALA A  57    12441  20161  13050  -4151  -1128    512       N  
ATOM    229  CA  ALA A  57     -28.685  49.473   6.712  1.00117.43           C  
ANISOU  229  CA  ALA A  57    12443  19513  12660  -3989  -1239    375       C  
ATOM    230  C   ALA A  57     -28.323  48.549   7.882  1.00120.50           C  
ANISOU  230  C   ALA A  57    12644  20189  12953  -3760  -1392    322       C  
ATOM    231  O   ALA A  57     -28.677  48.848   9.022  1.00120.19           O  
ANISOU  231  O   ALA A  57    12770  20046  12852  -3806  -1558    189       O  
ATOM    232  CB  ALA A  57     -29.959  48.993   6.041  1.00114.45           C  
ANISOU  232  CB  ALA A  57    12369  18818  12298  -3678  -1082    405       C  
ATOM    233  N   VAL A  58     -27.593  47.447   7.596  1.00116.40           N  
ANISOU  233  N   VAL A  58    11782  20035  12412  -3510  -1334    428       N  
ATOM    234  CA  VAL A  58     -27.105  46.490   8.593  1.00116.26           C  
ANISOU  234  CA  VAL A  58    11543  20327  12302  -3265  -1471    419       C  
ATOM    235  C   VAL A  58     -25.972  47.162   9.398  1.00123.39           C  
ANISOU  235  C   VAL A  58    12163  21550  13168  -3606  -1678    365       C  
ATOM    236  O   VAL A  58     -25.998  47.114  10.628  1.00123.05           O  
ANISOU  236  O   VAL A  58    12156  21569  13029  -3589  -1875    270       O  
ATOM    237  CB  VAL A  58     -26.683  45.140   7.943  1.00119.31           C  
ANISOU  237  CB  VAL A  58    11670  20972  12691  -2874  -1333    551       C  
ATOM    238  CG1 VAL A  58     -26.035  44.202   8.957  1.00120.47           C  
ANISOU  238  CG1 VAL A  58    11561  21463  12748  -2626  -1484    566       C  
ATOM    239  CG2 VAL A  58     -27.874  44.456   7.278  1.00115.28           C  
ANISOU  239  CG2 VAL A  58    11469  20128  12204  -2556  -1157    574       C  
ATOM    240  N   ILE A  59     -25.023  47.835   8.699  1.00122.90           N  
ANISOU  240  N   ILE A  59    11836  21686  13175  -3938  -1634    424       N  
ATOM    241  CA  ILE A  59     -23.886  48.559   9.295  1.00126.88           C  
ANISOU  241  CA  ILE A  59    12039  22509  13660  -4329  -1817    378       C  
ATOM    242  C   ILE A  59     -24.376  49.693  10.216  1.00131.29           C  
ANISOU  242  C   ILE A  59    12921  22770  14192  -4662  -1998    198       C  
ATOM    243  O   ILE A  59     -23.903  49.800  11.348  1.00133.25           O  
ANISOU  243  O   ILE A  59    13049  23230  14348  -4767  -2225     98       O  
ATOM    244  CB  ILE A  59     -22.870  49.072   8.226  1.00132.87           C  
ANISOU  244  CB  ILE A  59    12468  23509  14507  -4640  -1695    492       C  
ATOM    245  CG1 ILE A  59     -22.486  47.989   7.165  1.00132.72           C  
ANISOU  245  CG1 ILE A  59    12172  23747  14509  -4290  -1474    656       C  
ATOM    246  CG2 ILE A  59     -21.621  49.690   8.874  1.00138.25           C  
ANISOU  246  CG2 ILE A  59    12775  24586  15168  -5037  -1894    450       C  
ATOM    247  CD1 ILE A  59     -21.975  46.579   7.667  1.00140.48           C  
ANISOU  247  CD1 ILE A  59    12841  25118  15415  -3829  -1527    703       C  
ATOM    248  N   LEU A  60     -25.328  50.520   9.732  1.00125.59           N  
ANISOU  248  N   LEU A  60    12612  21563  13543  -4806  -1899    155       N  
ATOM    249  CA  LEU A  60     -25.918  51.622  10.495  1.00125.49           C  
ANISOU  249  CA  LEU A  60    12961  21200  13517  -5083  -2038    -25       C  
ATOM    250  C   LEU A  60     -26.829  51.124  11.617  1.00126.89           C  
ANISOU  250  C   LEU A  60    13398  21236  13577  -4780  -2147   -150       C  
ATOM    251  O   LEU A  60     -26.885  51.751  12.674  1.00127.91           O  
ANISOU  251  O   LEU A  60    13666  21303  13631  -4971  -2336   -321       O  
ATOM    252  CB  LEU A  60     -26.678  52.586   9.579  1.00124.21           C  
ANISOU  252  CB  LEU A  60    13160  20564  13472  -5268  -1887    -11       C  
ATOM    253  CG  LEU A  60     -25.896  53.796   9.091  1.00132.29           C  
ANISOU  253  CG  LEU A  60    14103  21572  14589  -5798  -1892      9       C  
ATOM    254  CD1 LEU A  60     -26.432  54.283   7.770  1.00131.04           C  
ANISOU  254  CD1 LEU A  60    14165  21084  14542  -5852  -1671    135       C  
ATOM    255  CD2 LEU A  60     -25.922  54.927  10.116  1.00137.06           C  
ANISOU  255  CD2 LEU A  60    14932  21969  15175  -6166  -2103   -199       C  
ATOM    256  N   GLY A  61     -27.513  50.004  11.377  1.00119.91           N  
ANISOU  256  N   GLY A  61    12578  20312  12670  -4323  -2024    -67       N  
ATOM    257  CA  GLY A  61     -28.411  49.374  12.340  1.00117.39           C  
ANISOU  257  CA  GLY A  61    12487  19875  12238  -4004  -2090   -148       C  
ATOM    258  C   GLY A  61     -27.697  48.839  13.567  1.00122.98           C  
ANISOU  258  C   GLY A  61    12956  20971  12801  -3934  -2303   -188       C  
ATOM    259  O   GLY A  61     -28.172  49.034  14.688  1.00122.96           O  
ANISOU  259  O   GLY A  61    13160  20879  12679  -3929  -2447   -328       O  
ATOM    260  N   VAL A  62     -26.546  48.161  13.358  1.00120.74           N  
ANISOU  260  N   VAL A  62    12227  21135  12513  -3866  -2324    -62       N  
ATOM    261  CA  VAL A  62     -25.697  47.604  14.420  1.00122.74           C  
ANISOU  261  CA  VAL A  62    12181  21825  12629  -3785  -2534    -66       C  
ATOM    262  C   VAL A  62     -25.090  48.762  15.248  1.00129.79           C  
ANISOU  262  C   VAL A  62    13026  22828  13460  -4248  -2767   -231       C  
ATOM    263  O   VAL A  62     -25.091  48.705  16.478  1.00129.88           O  
ANISOU  263  O   VAL A  62    13078  22958  13312  -4226  -2970   -337       O  
ATOM    264  CB  VAL A  62     -24.626  46.625  13.846  1.00127.86           C  
ANISOU  264  CB  VAL A  62    12355  22917  13309  -3576  -2476    118       C  
ATOM    265  CG1 VAL A  62     -23.512  46.335  14.850  1.00131.49           C  
ANISOU  265  CG1 VAL A  62    12434  23886  13642  -3592  -2719    117       C  
ATOM    266  CG2 VAL A  62     -25.262  45.322  13.374  1.00124.23           C  
ANISOU  266  CG2 VAL A  62    11983  22353  12867  -3069  -2298    245       C  
ATOM    267  N   VAL A  63     -24.624  49.823  14.563  1.00128.76           N  
ANISOU  267  N   VAL A  63    12836  22636  13449  -4675  -2732   -255       N  
ATOM    268  CA  VAL A  63     -24.043  51.021  15.173  1.00132.59           C  
ANISOU  268  CA  VAL A  63    13297  23172  13908  -5176  -2932   -417       C  
ATOM    269  C   VAL A  63     -25.086  51.756  16.025  1.00136.92           C  
ANISOU  269  C   VAL A  63    14339  23303  14382  -5262  -3023   -633       C  
ATOM    270  O   VAL A  63     -24.815  52.033  17.192  1.00138.61           O  
ANISOU  270  O   VAL A  63    14548  23668  14449  -5398  -3255   -789       O  
ATOM    271  CB  VAL A  63     -23.370  51.928  14.106  1.00138.41           C  
ANISOU  271  CB  VAL A  63    13885  23895  14810  -5605  -2834   -360       C  
ATOM    272  CG1 VAL A  63     -23.147  53.351  14.618  1.00141.41           C  
ANISOU  272  CG1 VAL A  63    14416  24118  15197  -6153  -3001   -553       C  
ATOM    273  CG2 VAL A  63     -22.057  51.318  13.628  1.00140.69           C  
ANISOU  273  CG2 VAL A  63    13595  24737  15124  -5595  -2817   -193       C  
ATOM    274  N   LEU A  64     -26.279  52.031  15.450  1.00131.64           N  
ANISOU  274  N   LEU A  64    14083  22135  13800  -5158  -2839   -644       N  
ATOM    275  CA  LEU A  64     -27.394  52.723  16.113  1.00130.94           C  
ANISOU  275  CA  LEU A  64    14478  21615  13659  -5188  -2879   -840       C  
ATOM    276  C   LEU A  64     -27.921  51.961  17.338  1.00135.41           C  
ANISOU  276  C   LEU A  64    15147  22279  14026  -4857  -2991   -916       C  
ATOM    277  O   LEU A  64     -28.130  52.568  18.393  1.00136.91           O  
ANISOU  277  O   LEU A  64    15537  22395  14088  -5004  -3157  -1123       O  
ATOM    278  CB  LEU A  64     -28.530  53.002  15.105  1.00127.59           C  
ANISOU  278  CB  LEU A  64    14405  20697  13375  -5078  -2642   -790       C  
ATOM    279  CG  LEU A  64     -29.824  53.616  15.646  1.00130.81           C  
ANISOU  279  CG  LEU A  64    15312  20645  13747  -5024  -2639   -970       C  
ATOM    280  CD1 LEU A  64     -29.692  55.125  15.838  1.00134.11           C  
ANISOU  280  CD1 LEU A  64    15951  20791  14214  -5484  -2737  -1154       C  
ATOM    281  CD2 LEU A  64     -30.984  53.296  14.738  1.00129.21           C  
ANISOU  281  CD2 LEU A  64    15348  20105  13640  -4725  -2405   -865       C  
ATOM    282  N   GLY A  65     -28.135  50.654  17.174  1.00130.24           N  
ANISOU  282  N   GLY A  65    14369  21775  13341  -4423  -2893   -750       N  
ATOM    283  CA  GLY A  65     -28.633  49.777  18.226  1.00129.20           C  
ANISOU  283  CA  GLY A  65    14321  21743  13027  -4079  -2968   -768       C  
ATOM    284  C   GLY A  65     -27.729  49.717  19.440  1.00137.57           C  
ANISOU  284  C   GLY A  65    15154  23222  13896  -4183  -3238   -845       C  
ATOM    285  O   GLY A  65     -28.221  49.785  20.565  1.00137.61           O  
ANISOU  285  O   GLY A  65    15372  23193  13720  -4127  -3360   -983       O  
ATOM    286  N   PHE A  66     -26.397  49.623  19.221  1.00137.88           N  
ANISOU  286  N   PHE A  66    14750  23677  13963  -4342  -3336   -761       N  
ATOM    287  CA  PHE A  66     -25.395  49.607  20.296  1.00141.93           C  
ANISOU  287  CA  PHE A  66    14981  24648  14298  -4473  -3615   -825       C  
ATOM    288  C   PHE A  66     -25.223  50.992  20.923  1.00150.38           C  
ANISOU  288  C   PHE A  66    16206  25618  15314  -4961  -3798  -1084       C  
ATOM    289  O   PHE A  66     -24.887  51.089  22.103  1.00152.34           O  
ANISOU  289  O   PHE A  66    16415  26113  15356  -5039  -4038  -1214       O  
ATOM    290  CB  PHE A  66     -24.041  49.064  19.807  1.00145.91           C  
ANISOU  290  CB  PHE A  66    14934  25647  14860  -4477  -3653   -649       C  
ATOM    291  CG  PHE A  66     -23.920  47.558  19.770  1.00145.91           C  
ANISOU  291  CG  PHE A  66    14722  25901  14816  -3963  -3593   -431       C  
ATOM    292  CD1 PHE A  66     -24.064  46.801  20.928  1.00149.22           C  
ANISOU  292  CD1 PHE A  66    15170  26506  15020  -3675  -3744   -420       C  
ATOM    293  CD2 PHE A  66     -23.593  46.900  18.592  1.00146.90           C  
ANISOU  293  CD2 PHE A  66    14614  26096  15104  -3774  -3392   -235       C  
ATOM    294  CE1 PHE A  66     -23.940  45.410  20.894  1.00149.17           C  
ANISOU  294  CE1 PHE A  66    14992  26703  14983  -3200  -3690   -207       C  
ATOM    295  CE2 PHE A  66     -23.471  45.509  18.559  1.00148.77           C  
ANISOU  295  CE2 PHE A  66    14680  26537  15308  -3292  -3337    -47       C  
ATOM    296  CZ  PHE A  66     -23.639  44.774  19.712  1.00147.15           C  
ANISOU  296  CZ  PHE A  66    14525  26478  14907  -3009  -3488    -29       C  
ATOM    297  N   LEU A  67     -25.449  52.058  20.125  1.00148.52           N  
ANISOU  297  N   LEU A  67    16156  25017  15257  -5287  -3686  -1158       N  
ATOM    298  CA  LEU A  67     -25.381  53.457  20.549  1.00152.07           C  
ANISOU  298  CA  LEU A  67    16819  25263  15697  -5766  -3824  -1407       C  
ATOM    299  C   LEU A  67     -26.567  53.748  21.479  1.00156.89           C  
ANISOU  299  C   LEU A  67    17915  25535  16162  -5638  -3855  -1614       C  
ATOM    300  O   LEU A  67     -26.390  54.382  22.519  1.00159.85           O  
ANISOU  300  O   LEU A  67    18392  25967  16377  -5870  -4070  -1842       O  
ATOM    301  CB  LEU A  67     -25.427  54.376  19.313  1.00151.91           C  
ANISOU  301  CB  LEU A  67    16904  24890  15925  -6071  -3651  -1377       C  
ATOM    302  CG  LEU A  67     -25.141  55.855  19.531  1.00160.28           C  
ANISOU  302  CG  LEU A  67    18136  25739  17026  -6627  -3780  -1599       C  
ATOM    303  CD1 LEU A  67     -23.717  56.197  19.129  1.00164.45           C  
ANISOU  303  CD1 LEU A  67    18217  26627  17640  -7046  -3868  -1529       C  
ATOM    304  CD2 LEU A  67     -26.125  56.710  18.760  1.00160.77           C  
ANISOU  304  CD2 LEU A  67    18650  25179  17255  -6705  -3587  -1639       C  
ATOM    305  N   LEU A  68     -27.763  53.257  21.108  1.00150.58           N  
ANISOU  305  N   LEU A  68    17396  24411  15408  -5265  -3640  -1537       N  
ATOM    306  CA  LEU A  68     -28.994  53.434  21.873  1.00149.57           C  
ANISOU  306  CA  LEU A  68    17709  23965  15154  -5090  -3620  -1704       C  
ATOM    307  C   LEU A  68     -29.242  52.329  22.910  1.00155.19           C  
ANISOU  307  C   LEU A  68    18381  24958  15627  -4711  -3695  -1663       C  
ATOM    308  O   LEU A  68     -30.215  52.429  23.661  1.00153.91           O  
ANISOU  308  O   LEU A  68    18556  24597  15327  -4568  -3687  -1802       O  
ATOM    309  CB  LEU A  68     -30.191  53.550  20.918  1.00145.65           C  
ANISOU  309  CB  LEU A  68    17529  22977  14834  -4913  -3350  -1643       C  
ATOM    310  CG  LEU A  68     -30.872  54.909  20.886  1.00151.15           C  
ANISOU  310  CG  LEU A  68    18641  23187  15603  -5167  -3325  -1862       C  
ATOM    311  CD1 LEU A  68     -30.323  55.773  19.761  1.00152.83           C  
ANISOU  311  CD1 LEU A  68    18792  23230  16046  -5527  -3264  -1808       C  
ATOM    312  CD2 LEU A  68     -32.366  54.757  20.735  1.00149.86           C  
ANISOU  312  CD2 LEU A  68    18843  22633  15463  -4836  -3130  -1868       C  
ATOM    313  N   ARG A  69     -28.359  51.297  22.976  1.00154.38           N  
ANISOU  313  N   ARG A  69    17868  25320  15469  -4548  -3769  -1471       N  
ATOM    314  CA  ARG A  69     -28.497  50.154  23.891  1.00154.56           C  
ANISOU  314  CA  ARG A  69    17826  25625  15273  -4172  -3839  -1381       C  
ATOM    315  C   ARG A  69     -28.765  50.539  25.361  1.00163.79           C  
ANISOU  315  C   ARG A  69    19211  26863  16157  -4232  -4038  -1606       C  
ATOM    316  O   ARG A  69     -29.708  49.940  25.877  1.00161.16           O  
ANISOU  316  O   ARG A  69    19104  26432  15695  -3908  -3959  -1580       O  
ATOM    317  CB  ARG A  69     -27.344  49.148  23.796  1.00155.13           C  
ANISOU  317  CB  ARG A  69    17412  26203  15327  -4029  -3927  -1160       C  
ATOM    318  CG  ARG A  69     -27.839  47.728  24.049  1.00159.66           C  
ANISOU  318  CG  ARG A  69    17989  26867  15807  -3520  -3844   -959       C  
ATOM    319  CD  ARG A  69     -26.722  46.739  24.299  1.00169.59           C  
ANISOU  319  CD  ARG A  69    18807  28647  16984  -3341  -3984   -770       C  
ATOM    320  NE  ARG A  69     -27.086  45.771  25.336  1.00177.47           N  
ANISOU  320  NE  ARG A  69    19883  29800  17746  -2985  -4058   -687       N  
ATOM    321  CZ  ARG A  69     -27.732  44.628  25.120  1.00189.00           C  
ANISOU  321  CZ  ARG A  69    21436  31145  19230  -2565  -3888   -490       C  
ATOM    322  NH1 ARG A  69     -28.098  44.288  23.887  1.00172.98           N  
ANISOU  322  NH1 ARG A  69    19430  28852  17444  -2439  -3639   -375       N  
ATOM    323  NH2 ARG A  69     -28.014  43.814  26.126  1.00176.95           N  
ANISOU  323  NH2 ARG A  69    19987  29768  17478  -2280  -3968   -407       N  
ATOM    324  N   PRO A  70     -28.053  51.499  26.051  1.00167.25           N  
ANISOU  324  N   PRO A  70    19608  27459  16482  -4628  -4281  -1830       N  
ATOM    325  CA  PRO A  70     -28.448  51.850  27.439  1.00169.93           C  
ANISOU  325  CA  PRO A  70    20199  27840  16525  -4654  -4451  -2063       C  
ATOM    326  C   PRO A  70     -29.919  52.269  27.417  1.00174.66           C  
ANISOU  326  C   PRO A  70    21292  27924  17147  -4527  -4252  -2193       C  
ATOM    327  O   PRO A  70     -30.265  53.304  26.839  1.00174.25           O  
ANISOU  327  O   PRO A  70    21468  27472  17269  -4763  -4163  -2336       O  
ATOM    328  CB  PRO A  70     -27.497  52.996  27.815  1.00176.15           C  
ANISOU  328  CB  PRO A  70    20895  28765  17270  -5168  -4699  -2301       C  
ATOM    329  CG  PRO A  70     -26.961  53.505  26.521  1.00180.51           C  
ANISOU  329  CG  PRO A  70    21284  29165  18136  -5441  -4596  -2226       C  
ATOM    330  CD  PRO A  70     -26.908  52.325  25.609  1.00172.65           C  
ANISOU  330  CD  PRO A  70    20031  28278  17290  -5084  -4406  -1893       C  
ATOM    331  N   TYR A  71     -30.787  51.375  27.942  1.00171.53           N  
ANISOU  331  N   TYR A  71    21039  27542  16594  -4125  -4163  -2104       N  
ATOM    332  CA  TYR A  71     -32.247  51.421  27.851  1.00169.23           C  
ANISOU  332  CA  TYR A  71    21142  26832  16328  -3906  -3939  -2154       C  
ATOM    333  C   TYR A  71     -33.032  51.988  29.076  1.00175.91           C  
ANISOU  333  C   TYR A  71    22347  27588  16901  -3906  -4003  -2427       C  
ATOM    334  O   TYR A  71     -33.730  51.213  29.744  1.00174.75           O  
ANISOU  334  O   TYR A  71    22307  27524  16567  -3587  -3941  -2356       O  
ATOM    335  CB  TYR A  71     -32.815  50.012  27.484  1.00166.97           C  
ANISOU  335  CB  TYR A  71    20788  26566  16085  -3459  -3743  -1856       C  
ATOM    336  CG  TYR A  71     -32.122  48.816  28.120  1.00170.33           C  
ANISOU  336  CG  TYR A  71    20926  27460  16332  -3230  -3867  -1649       C  
ATOM    337  CD1 TYR A  71     -31.640  47.769  27.342  1.00170.42           C  
ANISOU  337  CD1 TYR A  71    20651  27605  16496  -3018  -3782  -1360       C  
ATOM    338  CD2 TYR A  71     -31.976  48.719  29.504  1.00174.50           C  
ANISOU  338  CD2 TYR A  71    21490  28285  16528  -3200  -4063  -1739       C  
ATOM    339  CE1 TYR A  71     -31.003  46.670  27.918  1.00172.86           C  
ANISOU  339  CE1 TYR A  71    20715  28315  16649  -2774  -3893  -1159       C  
ATOM    340  CE2 TYR A  71     -31.333  47.630  30.091  1.00177.01           C  
ANISOU  340  CE2 TYR A  71    21557  29024  16674  -2969  -4182  -1527       C  
ATOM    341  CZ  TYR A  71     -30.852  46.605  29.294  1.00184.75           C  
ANISOU  341  CZ  TYR A  71    22258  30111  17828  -2748  -4095  -1232       C  
ATOM    342  OH  TYR A  71     -30.229  45.526  29.877  1.00186.42           O  
ANISOU  342  OH  TYR A  71    22242  30714  17877  -2491  -4213  -1016       O  
ATOM    343  N   PRO A  72     -33.118  53.329  29.295  1.00174.63           N  
ANISOU  343  N   PRO A  72    22432  27184  16734  -4228  -4077  -2738       N  
ATOM    344  CA  PRO A  72     -34.046  53.826  30.327  1.00175.16           C  
ANISOU  344  CA  PRO A  72    22882  27107  16566  -4163  -4076  -2999       C  
ATOM    345  C   PRO A  72     -35.466  53.860  29.711  1.00174.44           C  
ANISOU  345  C   PRO A  72    23086  26558  16636  -3912  -3776  -2970       C  
ATOM    346  O   PRO A  72     -36.381  54.520  30.217  1.00174.86           O  
ANISOU  346  O   PRO A  72    23490  26355  16592  -3875  -3711  -3203       O  
ATOM    347  CB  PRO A  72     -33.499  55.225  30.661  1.00181.04           C  
ANISOU  347  CB  PRO A  72    23762  27744  17281  -4609  -4266  -3336       C  
ATOM    348  CG  PRO A  72     -32.410  55.510  29.639  1.00186.27           C  
ANISOU  348  CG  PRO A  72    24123  28442  18209  -4922  -4331  -3226       C  
ATOM    349  CD  PRO A  72     -32.480  54.453  28.585  1.00177.92           C  
ANISOU  349  CD  PRO A  72    22828  27409  17365  -4649  -4137  -2867       C  
ATOM    350  N   LEU A  73     -35.625  53.109  28.594  1.00166.00           N  
ANISOU  350  N   LEU A  73    21852  25411  15811  -3731  -3596  -2682       N  
ATOM    351  CA  LEU A  73     -36.821  52.948  27.784  1.00161.49           C  
ANISOU  351  CA  LEU A  73    21463  24469  15426  -3493  -3322  -2589       C  
ATOM    352  C   LEU A  73     -37.423  51.534  27.922  1.00160.35           C  
ANISOU  352  C   LEU A  73    21241  24480  15206  -3091  -3184  -2341       C  
ATOM    353  O   LEU A  73     -36.743  50.523  27.709  1.00158.23           O  
ANISOU  353  O   LEU A  73    20675  24492  14955  -2988  -3218  -2096       O  
ATOM    354  CB  LEU A  73     -36.505  53.241  26.306  1.00160.21           C  
ANISOU  354  CB  LEU A  73    21198  24068  15607  -3638  -3223  -2470       C  
ATOM    355  CG  LEU A  73     -36.301  54.680  25.787  1.00167.11           C  
ANISOU  355  CG  LEU A  73    22265  24587  16641  -3984  -3250  -2683       C  
ATOM    356  CD1 LEU A  73     -36.462  54.730  24.283  1.00164.73           C  
ANISOU  356  CD1 LEU A  73    21915  24018  16656  -4000  -3078  -2505       C  
ATOM    357  CD2 LEU A  73     -37.163  55.735  26.468  1.00171.14           C  
ANISOU  357  CD2 LEU A  73    23201  24771  17053  -3970  -3214  -2977       C  
ATOM    358  N   SER A  74     -38.719  51.492  28.274  1.00155.15           N  
ANISOU  358  N   SER A  74    20859  23629  14463  -2872  -3027  -2412       N  
ATOM    359  CA  SER A  74     -39.548  50.303  28.508  1.00152.23           C  
ANISOU  359  CA  SER A  74    20503  23337  14002  -2515  -2871  -2226       C  
ATOM    360  C   SER A  74     -39.754  49.452  27.244  1.00150.77           C  
ANISOU  360  C   SER A  74    20157  23048  14082  -2347  -2696  -1939       C  
ATOM    361  O   SER A  74     -39.549  49.989  26.157  1.00149.57           O  
ANISOU  361  O   SER A  74    19969  22674  14186  -2485  -2647  -1931       O  
ATOM    362  CB  SER A  74     -40.886  50.729  29.118  1.00156.30           C  
ANISOU  362  CB  SER A  74    21356  23618  14414  -2386  -2728  -2413       C  
ATOM    363  OG  SER A  74     -42.001  50.677  28.250  1.00163.29           O  
ANISOU  363  OG  SER A  74    22365  24114  15563  -2332  -2530  -2408       O  
ATOM    364  N   PRO A  75     -40.202  48.162  27.328  1.00144.09           N  
ANISOU  364  N   PRO A  75    19239  22328  13182  -2056  -2588  -1709       N  
ATOM    365  CA  PRO A  75     -40.433  47.383  26.093  1.00140.12           C  
ANISOU  365  CA  PRO A  75    18614  21694  12932  -1906  -2419  -1470       C  
ATOM    366  C   PRO A  75     -41.439  48.032  25.142  1.00139.67           C  
ANISOU  366  C   PRO A  75    18742  21234  13094  -1905  -2230  -1542       C  
ATOM    367  O   PRO A  75     -41.354  47.815  23.934  1.00136.67           O  
ANISOU  367  O   PRO A  75    18255  20721  12951  -1893  -2135  -1405       O  
ATOM    368  CB  PRO A  75     -40.937  46.030  26.608  1.00140.88           C  
ANISOU  368  CB  PRO A  75    18687  21951  12889  -1613  -2339  -1266       C  
ATOM    369  CG  PRO A  75     -40.433  45.941  27.995  1.00148.48           C  
ANISOU  369  CG  PRO A  75    19644  23235  13536  -1632  -2522  -1329       C  
ATOM    370  CD  PRO A  75     -40.510  47.345  28.519  1.00146.32           C  
ANISOU  370  CD  PRO A  75    19560  22864  13170  -1860  -2611  -1651       C  
ATOM    371  N   ARG A  76     -42.362  48.855  25.697  1.00135.53           N  
ANISOU  371  N   ARG A  76    18491  20527  12475  -1911  -2183  -1765       N  
ATOM    372  CA  ARG A  76     -43.365  49.649  24.984  1.00133.04           C  
ANISOU  372  CA  ARG A  76    18382  19835  12331  -1899  -2029  -1872       C  
ATOM    373  C   ARG A  76     -42.624  50.650  24.086  1.00136.62           C  
ANISOU  373  C   ARG A  76    18806  20105  13000  -2164  -2098  -1934       C  
ATOM    374  O   ARG A  76     -42.983  50.803  22.914  1.00134.56           O  
ANISOU  374  O   ARG A  76    18552  19605  12968  -2142  -1972  -1849       O  
ATOM    375  CB  ARG A  76     -44.259  50.388  26.000  1.00133.10           C  
ANISOU  375  CB  ARG A  76    18672  19755  12146  -1862  -2011  -2132       C  
ATOM    376  CG  ARG A  76     -45.332  51.286  25.385  1.00140.66           C  
ANISOU  376  CG  ARG A  76    19859  20327  13259  -1823  -1865  -2269       C  
ATOM    377  CD  ARG A  76     -45.824  52.414  26.272  1.00151.72           C  
ANISOU  377  CD  ARG A  76    21545  21587  14516  -1877  -1900  -2592       C  
ATOM    378  NE  ARG A  76     -44.997  52.642  27.454  1.00169.43           N  
ANISOU  378  NE  ARG A  76    23804  24039  16532  -2071  -2110  -2765       N  
ATOM    379  CZ  ARG A  76     -44.877  53.808  28.072  1.00189.71           C  
ANISOU  379  CZ  ARG A  76    26612  26471  18997  -2205  -2192  -3074       C  
ATOM    380  NH1 ARG A  76     -44.112  53.920  29.149  1.00177.52           N  
ANISOU  380  NH1 ARG A  76    25064  25156  17230  -2387  -2395  -3225       N  
ATOM    381  NH2 ARG A  76     -45.521  54.879  27.620  1.00180.33           N  
ANISOU  381  NH2 ARG A  76    25673  24917  17928  -2153  -2077  -3236       N  
ATOM    382  N   GLU A  77     -41.574  51.303  24.639  1.00134.79           N  
ANISOU  382  N   GLU A  77    18530  20004  12681  -2425  -2301  -2070       N  
ATOM    383  CA  GLU A  77     -40.724  52.270  23.936  1.00135.17           C  
ANISOU  383  CA  GLU A  77    18535  19920  12906  -2733  -2390  -2130       C  
ATOM    384  C   GLU A  77     -39.816  51.577  22.899  1.00135.84           C  
ANISOU  384  C   GLU A  77    18301  20150  13163  -2766  -2382  -1873       C  
ATOM    385  O   GLU A  77     -39.468  52.181  21.880  1.00134.65           O  
ANISOU  385  O   GLU A  77    18121  19820  13222  -2941  -2353  -1843       O  
ATOM    386  CB  GLU A  77     -39.928  53.126  24.941  1.00140.41           C  
ANISOU  386  CB  GLU A  77    19233  20716  13400  -3013  -2618  -2360       C  
ATOM    387  CG  GLU A  77     -40.783  54.159  25.655  1.00150.68           C  
ANISOU  387  CG  GLU A  77    20893  21742  14615  -3071  -2618  -2666       C  
ATOM    388  CD  GLU A  77     -40.620  54.197  27.153  1.00172.16           C  
ANISOU  388  CD  GLU A  77    23743  24660  17009  -3038  -2731  -2875       C  
ATOM    389  OE1 GLU A  77     -39.642  54.819  27.621  1.00171.19           O  
ANISOU  389  OE1 GLU A  77    23447  24895  16702  -3152  -2922  -2880       O  
ATOM    390  OE2 GLU A  77     -41.495  53.648  27.866  1.00164.43           O  
ANISOU  390  OE2 GLU A  77    23056  23464  15955  -2911  -2633  -3059       O  
ATOM    391  N   VAL A  78     -39.462  50.298  23.160  1.00131.06           N  
ANISOU  391  N   VAL A  78    17469  19866  12461  -2586  -2400  -1684       N  
ATOM    392  CA  VAL A  78     -38.656  49.447  22.277  1.00129.58           C  
ANISOU  392  CA  VAL A  78    16974  19849  12410  -2548  -2379  -1439       C  
ATOM    393  C   VAL A  78     -39.490  49.151  21.025  1.00129.49           C  
ANISOU  393  C   VAL A  78    17021  19568  12613  -2389  -2156  -1306       C  
ATOM    394  O   VAL A  78     -38.967  49.228  19.913  1.00128.23           O  
ANISOU  394  O   VAL A  78    16719  19361  12640  -2484  -2113  -1201       O  
ATOM    395  CB  VAL A  78     -38.170  48.154  22.990  1.00133.95           C  
ANISOU  395  CB  VAL A  78    17319  20781  12793  -2352  -2454  -1282       C  
ATOM    396  CG1 VAL A  78     -37.497  47.187  22.017  1.00132.43           C  
ANISOU  396  CG1 VAL A  78    16840  20725  12753  -2243  -2396  -1030       C  
ATOM    397  CG2 VAL A  78     -37.229  48.483  24.141  1.00137.47           C  
ANISOU  397  CG2 VAL A  78    17674  21533  13023  -2528  -2699  -1404       C  
ATOM    398  N   LYS A  79     -40.797  48.858  21.217  1.00123.99           N  
ANISOU  398  N   LYS A  79    16529  18707  11876  -2161  -2017  -1320       N  
ATOM    399  CA  LYS A  79     -41.772  48.609  20.151  1.00120.66           C  
ANISOU  399  CA  LYS A  79    16186  18033  11626  -2001  -1815  -1222       C  
ATOM    400  C   LYS A  79     -41.936  49.875  19.296  1.00124.14           C  
ANISOU  400  C   LYS A  79    16766  18160  12242  -2185  -1779  -1321       C  
ATOM    401  O   LYS A  79     -42.025  49.776  18.069  1.00122.10           O  
ANISOU  401  O   LYS A  79    16453  17773  12165  -2166  -1671  -1194       O  
ATOM    402  CB  LYS A  79     -43.131  48.176  20.738  1.00122.06           C  
ANISOU  402  CB  LYS A  79    16548  18136  11694  -1758  -1698  -1250       C  
ATOM    403  CG  LYS A  79     -43.149  46.761  21.317  1.00139.67           C  
ANISOU  403  CG  LYS A  79    18660  20618  13791  -1547  -1684  -1089       C  
ATOM    404  CD  LYS A  79     -44.182  46.623  22.443  1.00153.44           C  
ANISOU  404  CD  LYS A  79    20589  22380  15332  -1406  -1639  -1178       C  
ATOM    405  CE  LYS A  79     -43.874  45.480  23.386  1.00165.31           C  
ANISOU  405  CE  LYS A  79    21992  24181  16637  -1274  -1695  -1048       C  
ATOM    406  NZ  LYS A  79     -44.790  45.457  24.558  1.00172.97           N  
ANISOU  406  NZ  LYS A  79    23143  25197  17380  -1167  -1653  -1138       N  
ATOM    407  N   TYR A  80     -41.940  51.061  19.950  1.00122.49           N  
ANISOU  407  N   TYR A  80    16747  17826  11967  -2364  -1874  -1547       N  
ATOM    408  CA  TYR A  80     -42.046  52.374  19.307  1.00122.85           C  
ANISOU  408  CA  TYR A  80    16969  17544  12165  -2555  -1860  -1657       C  
ATOM    409  C   TYR A  80     -40.827  52.622  18.430  1.00126.69           C  
ANISOU  409  C   TYR A  80    17255  18085  12796  -2812  -1920  -1553       C  
ATOM    410  O   TYR A  80     -40.963  53.087  17.296  1.00125.14           O  
ANISOU  410  O   TYR A  80    17106  17661  12783  -2875  -1829  -1482       O  
ATOM    411  CB  TYR A  80     -42.172  53.500  20.363  1.00126.91           C  
ANISOU  411  CB  TYR A  80    17730  17936  12554  -2700  -1970  -1939       C  
ATOM    412  CG  TYR A  80     -43.447  53.497  21.183  1.00128.26           C  
ANISOU  412  CG  TYR A  80    18131  18018  12584  -2461  -1892  -2077       C  
ATOM    413  CD1 TYR A  80     -44.597  52.863  20.721  1.00127.35           C  
ANISOU  413  CD1 TYR A  80    18046  17825  12518  -2172  -1710  -1962       C  
ATOM    414  CD2 TYR A  80     -43.520  54.172  22.398  1.00131.96           C  
ANISOU  414  CD2 TYR A  80    18790  18481  12867  -2537  -1995  -2335       C  
ATOM    415  CE1 TYR A  80     -45.773  52.865  21.466  1.00128.06           C  
ANISOU  415  CE1 TYR A  80    18319  17859  12477  -1961  -1626  -2084       C  
ATOM    416  CE2 TYR A  80     -44.694  54.190  23.148  1.00132.93           C  
ANISOU  416  CE2 TYR A  80    19117  18541  12849  -2310  -1905  -2468       C  
ATOM    417  CZ  TYR A  80     -45.824  53.549  22.668  1.00137.62           C  
ANISOU  417  CZ  TYR A  80    19715  19073  13502  -2023  -1715  -2336       C  
ATOM    418  OH  TYR A  80     -46.985  53.561  23.401  1.00139.03           O  
ANISOU  418  OH  TYR A  80    20066  19219  13540  -1804  -1615  -2461       O  
ATOM    419  N   PHE A  81     -39.635  52.290  18.958  1.00124.84           N  
ANISOU  419  N   PHE A  81    16788  18178  12469  -2956  -2073  -1537       N  
ATOM    420  CA  PHE A  81     -38.368  52.453  18.257  1.00125.76           C  
ANISOU  420  CA  PHE A  81    16659  18426  12697  -3209  -2138  -1439       C  
ATOM    421  C   PHE A  81     -38.309  51.575  17.002  1.00125.05           C  
ANISOU  421  C   PHE A  81    16375  18386  12753  -3056  -1988  -1191       C  
ATOM    422  O   PHE A  81     -38.039  52.086  15.917  1.00124.46           O  
ANISOU  422  O   PHE A  81    16277  18171  12842  -3208  -1925  -1119       O  
ATOM    423  CB  PHE A  81     -37.174  52.179  19.205  1.00130.49           C  
ANISOU  423  CB  PHE A  81    17021  19418  13142  -3351  -2342  -1475       C  
ATOM    424  CG  PHE A  81     -35.845  52.098  18.491  1.00133.69           C  
ANISOU  424  CG  PHE A  81    17096  20046  13653  -3563  -2394  -1341       C  
ATOM    425  CD1 PHE A  81     -35.165  53.253  18.120  1.00139.68           C  
ANISOU  425  CD1 PHE A  81    17862  20694  14515  -3944  -2463  -1421       C  
ATOM    426  CD2 PHE A  81     -35.300  50.869  18.141  1.00134.92           C  
ANISOU  426  CD2 PHE A  81    16939  20512  13814  -3377  -2361  -1130       C  
ATOM    427  CE1 PHE A  81     -33.963  53.178  17.413  1.00142.08           C  
ANISOU  427  CE1 PHE A  81    17840  21226  14918  -4147  -2490  -1286       C  
ATOM    428  CE2 PHE A  81     -34.100  50.795  17.433  1.00139.27           C  
ANISOU  428  CE2 PHE A  81    17169  21286  14463  -3549  -2388  -1007       C  
ATOM    429  CZ  PHE A  81     -33.436  51.950  17.081  1.00140.00           C  
ANISOU  429  CZ  PHE A  81    17247  21298  14649  -3939  -2451  -1083       C  
ATOM    430  N   ALA A  82     -38.578  50.267  17.157  1.00118.53           N  
ANISOU  430  N   ALA A  82    15429  17749  11859  -2761  -1930  -1062       N  
ATOM    431  CA  ALA A  82     -38.536  49.270  16.087  1.00115.61           C  
ANISOU  431  CA  ALA A  82    14882  17445  11600  -2581  -1794   -846       C  
ATOM    432  C   ALA A  82     -39.692  49.350  15.075  1.00116.13           C  
ANISOU  432  C   ALA A  82    15134  17195  11795  -2445  -1609   -798       C  
ATOM    433  O   ALA A  82     -39.694  48.575  14.112  1.00114.16           O  
ANISOU  433  O   ALA A  82    14760  16984  11634  -2311  -1494   -637       O  
ATOM    434  CB  ALA A  82     -38.448  47.872  16.684  1.00115.45           C  
ANISOU  434  CB  ALA A  82    14709  17698  11460  -2319  -1805   -738       C  
ATOM    435  N   PHE A  83     -40.639  50.304  15.258  1.00111.57           N  
ANISOU  435  N   PHE A  83    14849  16315  11227  -2477  -1585   -943       N  
ATOM    436  CA  PHE A  83     -41.796  50.491  14.377  1.00108.57           C  
ANISOU  436  CA  PHE A  83    14650  15643  10958  -2341  -1430   -909       C  
ATOM    437  C   PHE A  83     -41.461  50.585  12.864  1.00111.50           C  
ANISOU  437  C   PHE A  83    14927  15942  11495  -2415  -1337   -755       C  
ATOM    438  O   PHE A  83     -42.184  49.935  12.106  1.00109.54           O  
ANISOU  438  O   PHE A  83    14684  15636  11299  -2212  -1207   -650       O  
ATOM    439  CB  PHE A  83     -42.675  51.672  14.804  1.00110.91           C  
ANISOU  439  CB  PHE A  83    15259  15635  11247  -2382  -1437  -1095       C  
ATOM    440  CG  PHE A  83     -43.970  51.737  14.030  1.00109.96           C  
ANISOU  440  CG  PHE A  83    15301  15261  11218  -2187  -1286  -1054       C  
ATOM    441  CD1 PHE A  83     -44.955  50.772  14.209  1.00110.70           C  
ANISOU  441  CD1 PHE A  83    15394  15411  11257  -1907  -1191  -1011       C  
ATOM    442  CD2 PHE A  83     -44.189  52.738  13.093  1.00112.07           C  
ANISOU  442  CD2 PHE A  83    15711  15245  11624  -2288  -1243  -1044       C  
ATOM    443  CE1 PHE A  83     -46.141  50.818  13.477  1.00109.76           C  
ANISOU  443  CE1 PHE A  83    15393  15092  11220  -1737  -1063   -973       C  
ATOM    444  CE2 PHE A  83     -45.381  52.787  12.368  1.00113.01           C  
ANISOU  444  CE2 PHE A  83    15962  15158  11817  -2093  -1118   -998       C  
ATOM    445  CZ  PHE A  83     -46.347  51.827  12.566  1.00108.95           C  
ANISOU  445  CZ  PHE A  83    15423  14728  11247  -1820  -1033   -969       C  
ATOM    446  N   PRO A  84     -40.419  51.315  12.363  1.00108.82           N  
ANISOU  446  N   PRO A  84    14497  15617  11232  -2699  -1390   -731       N  
ATOM    447  CA  PRO A  84     -40.169  51.305  10.909  1.00107.59           C  
ANISOU  447  CA  PRO A  84    14251  15420  11209  -2743  -1279   -567       C  
ATOM    448  C   PRO A  84     -39.862  49.903  10.377  1.00108.64           C  
ANISOU  448  C   PRO A  84    14131  15814  11335  -2543  -1199   -408       C  
ATOM    449  O   PRO A  84     -40.239  49.575   9.255  1.00106.26           O  
ANISOU  449  O   PRO A  84    13825  15443  11106  -2437  -1070   -293       O  
ATOM    450  CB  PRO A  84     -38.989  52.262  10.744  1.00112.31           C  
ANISOU  450  CB  PRO A  84    14767  16046  11858  -3108  -1365   -577       C  
ATOM    451  CG  PRO A  84     -39.018  53.119  11.966  1.00118.81           C  
ANISOU  451  CG  PRO A  84    15760  16773  12608  -3259  -1509   -785       C  
ATOM    452  CD  PRO A  84     -39.437  52.180  13.045  1.00113.20           C  
ANISOU  452  CD  PRO A  84    15024  16236  11752  -3008  -1548   -848       C  
ATOM    453  N   GLY A  85     -39.240  49.079  11.218  1.00105.25           N  
ANISOU  453  N   GLY A  85    13514  15670  10808  -2476  -1281   -409       N  
ATOM    454  CA  GLY A  85     -38.942  47.687  10.914  1.00103.48           C  
ANISOU  454  CA  GLY A  85    13072  15679  10567  -2254  -1219   -274       C  
ATOM    455  C   GLY A  85     -40.176  46.811  10.999  1.00103.48           C  
ANISOU  455  C   GLY A  85    13210  15570  10538  -1956  -1125   -259       C  
ATOM    456  O   GLY A  85     -40.232  45.750  10.377  1.00101.54           O  
ANISOU  456  O   GLY A  85    12861  15402  10317  -1767  -1030   -146       O  
ATOM    457  N   GLU A  86     -41.186  47.259  11.767  1.00 98.87           N  
ANISOU  457  N   GLU A  86    12863  14804   9900  -1916  -1146   -382       N  
ATOM    458  CA  GLU A  86     -42.455  46.554  11.926  1.00 96.47           C  
ANISOU  458  CA  GLU A  86    12693  14395   9564  -1666  -1056   -379       C  
ATOM    459  C   GLU A  86     -43.320  46.739  10.691  1.00 98.26           C  
ANISOU  459  C   GLU A  86    13028  14402   9904  -1608   -924   -332       C  
ATOM    460  O   GLU A  86     -44.016  45.802  10.303  1.00 96.25           O  
ANISOU  460  O   GLU A  86    12773  14138   9661  -1411   -828   -265       O  
ATOM    461  CB  GLU A  86     -43.207  47.041  13.165  1.00 98.54           C  
ANISOU  461  CB  GLU A  86    13151  14572   9719  -1649  -1114   -531       C  
ATOM    462  CG  GLU A  86     -44.306  46.088  13.592  1.00109.20           C  
ANISOU  462  CG  GLU A  86    14574  15915  11003  -1400  -1033   -510       C  
ATOM    463  CD  GLU A  86     -45.371  46.677  14.492  1.00131.95           C  
ANISOU  463  CD  GLU A  86    17673  18664  13799  -1356  -1033   -657       C  
ATOM    464  OE1 GLU A  86     -46.564  46.401  14.235  1.00126.47           O  
ANISOU  464  OE1 GLU A  86    17076  17848  13128  -1201   -921   -647       O  
ATOM    465  OE2 GLU A  86     -45.019  47.378  15.470  1.00125.32           O  
ANISOU  465  OE2 GLU A  86    16896  17861  12859  -1473  -1144   -789       O  
ATOM    466  N   LEU A  87     -43.285  47.939  10.074  1.00 94.97           N  
ANISOU  466  N   LEU A  87    12710  13808   9568  -1784   -925   -362       N  
ATOM    467  CA  LEU A  87     -44.048  48.208   8.858  1.00 93.30           C  
ANISOU  467  CA  LEU A  87    12600  13399   9450  -1733   -815   -302       C  
ATOM    468  C   LEU A  87     -43.557  47.350   7.694  1.00 96.60           C  
ANISOU  468  C   LEU A  87    12836  13952   9916  -1679   -728   -152       C  
ATOM    469  O   LEU A  87     -44.373  46.930   6.871  1.00 94.90           O  
ANISOU  469  O   LEU A  87    12671  13653   9734  -1536   -629    -99       O  
ATOM    470  CB  LEU A  87     -44.023  49.692   8.486  1.00 94.75           C  
ANISOU  470  CB  LEU A  87    12942  13355   9703  -1935   -842   -347       C  
ATOM    471  CG  LEU A  87     -44.889  50.618   9.329  1.00100.14           C  
ANISOU  471  CG  LEU A  87    13875  13813  10361  -1926   -888   -505       C  
ATOM    472  CD1 LEU A  87     -44.768  52.047   8.837  1.00102.26           C  
ANISOU  472  CD1 LEU A  87    14312  13827  10716  -2125   -911   -529       C  
ATOM    473  CD2 LEU A  87     -46.353  50.181   9.318  1.00100.51           C  
ANISOU  473  CD2 LEU A  87    14036  13761  10394  -1661   -801   -521       C  
ATOM    474  N   LEU A  88     -42.236  47.053   7.650  1.00 94.08           N  
ANISOU  474  N   LEU A  88    12296  13860   9591  -1783   -765    -94       N  
ATOM    475  CA  LEU A  88     -41.648  46.193   6.621  1.00 93.15           C  
ANISOU  475  CA  LEU A  88    11987  13902   9503  -1714   -677     34       C  
ATOM    476  C   LEU A  88     -42.166  44.767   6.778  1.00 94.27           C  
ANISOU  476  C   LEU A  88    12096  14115   9607  -1444   -621     62       C  
ATOM    477  O   LEU A  88     -42.461  44.115   5.778  1.00 93.16           O  
ANISOU  477  O   LEU A  88    11937  13962   9499  -1324   -515    129       O  
ATOM    478  CB  LEU A  88     -40.108  46.225   6.648  1.00 95.28           C  
ANISOU  478  CB  LEU A  88    12004  14427   9771  -1873   -730     82       C  
ATOM    479  CG  LEU A  88     -39.396  45.400   5.565  1.00 99.76           C  
ANISOU  479  CG  LEU A  88    12357  15185  10364  -1794   -626    206       C  
ATOM    480  CD1 LEU A  88     -39.631  45.973   4.163  1.00 99.55           C  
ANISOU  480  CD1 LEU A  88    12399  15031  10396  -1878   -516    274       C  
ATOM    481  CD2 LEU A  88     -37.926  45.267   5.868  1.00104.34           C  
ANISOU  481  CD2 LEU A  88    12652  16066  10926  -1901   -691    242       C  
ATOM    482  N   MET A  89     -42.319  44.310   8.027  1.00 89.52           N  
ANISOU  482  N   MET A  89    11509  13573   8931  -1358   -693      7       N  
ATOM    483  CA  MET A  89     -42.861  42.997   8.336  1.00 87.72           C  
ANISOU  483  CA  MET A  89    11282  13382   8664  -1123   -647     39       C  
ATOM    484  C   MET A  89     -44.310  42.868   7.867  1.00 89.51           C  
ANISOU  484  C   MET A  89    11690  13400   8920  -1013   -553     19       C  
ATOM    485  O   MET A  89     -44.623  41.886   7.193  1.00 88.42           O  
ANISOU  485  O   MET A  89    11528  13262   8807   -871   -465     79       O  
ATOM    486  CB  MET A  89     -42.736  42.709   9.827  1.00 90.89           C  
ANISOU  486  CB  MET A  89    11682  13889   8961  -1082   -748     -4       C  
ATOM    487  CG  MET A  89     -41.344  42.354  10.233  1.00 96.53           C  
ANISOU  487  CG  MET A  89    12174  14866   9638  -1109   -835     48       C  
ATOM    488  SD  MET A  89     -40.932  40.703   9.655  1.00100.50           S  
ANISOU  488  SD  MET A  89    12523  15497  10164   -859   -747    184       S  
ATOM    489  CE  MET A  89     -40.231  40.044  11.119  1.00 98.99           C  
ANISOU  489  CE  MET A  89    12224  15535   9853   -770   -880    215       C  
ATOM    490  N   ARG A  90     -45.178  43.877   8.172  1.00 84.93           N  
ANISOU  490  N   ARG A  90    11286  12643   8338  -1078   -574    -70       N  
ATOM    491  CA  ARG A  90     -46.590  43.886   7.744  1.00 82.61           C  
ANISOU  491  CA  ARG A  90    11142  12173   8071   -974   -495    -92       C  
ATOM    492  C   ARG A  90     -46.673  43.876   6.204  1.00 86.64           C  
ANISOU  492  C   ARG A  90    11632  12630   8658   -973   -413    -18       C  
ATOM    493  O   ARG A  90     -47.488  43.146   5.642  1.00 85.65           O  
ANISOU  493  O   ARG A  90    11533  12467   8545   -845   -338      6       O  
ATOM    494  CB  ARG A  90     -47.386  45.102   8.288  1.00 80.38           C  
ANISOU  494  CB  ARG A  90    11041  11721   7780  -1029   -532   -202       C  
ATOM    495  CG  ARG A  90     -47.096  45.602   9.706  1.00 84.56           C  
ANISOU  495  CG  ARG A  90    11616  12289   8223  -1096   -631   -306       C  
ATOM    496  CD  ARG A  90     -48.212  45.381  10.721  1.00 88.96           C  
ANISOU  496  CD  ARG A  90    12283  12818   8700   -964   -612   -384       C  
ATOM    497  NE  ARG A  90     -49.535  45.808  10.261  1.00 95.22           N  
ANISOU  497  NE  ARG A  90    13206  13435   9537   -876   -538   -421       N  
ATOM    498  CZ  ARG A  90     -50.677  45.309  10.730  1.00115.77           C  
ANISOU  498  CZ  ARG A  90    15856  16037  12094   -733   -477   -449       C  
ATOM    499  NH1 ARG A  90     -50.664  44.366  11.663  1.00106.71           N  
ANISOU  499  NH1 ARG A  90    14661  15033  10852   -670   -474   -434       N  
ATOM    500  NH2 ARG A  90     -51.839  45.735  10.253  1.00106.25           N  
ANISOU  500  NH2 ARG A  90    14737  14699  10934   -651   -416   -479       N  
ATOM    501  N   MET A  91     -45.816  44.670   5.532  1.00 84.13           N  
ANISOU  501  N   MET A  91    11267  12321   8379  -1129   -428     18       N  
ATOM    502  CA  MET A  91     -45.759  44.775   4.073  1.00 84.09           C  
ANISOU  502  CA  MET A  91    11241  12288   8419  -1149   -352     99       C  
ATOM    503  C   MET A  91     -45.410  43.439   3.409  1.00 89.53           C  
ANISOU  503  C   MET A  91    11793  13126   9099  -1023   -275    164       C  
ATOM    504  O   MET A  91     -46.093  43.037   2.465  1.00 88.43           O  
ANISOU  504  O   MET A  91    11698  12933   8968   -933   -201    187       O  
ATOM    505  CB  MET A  91     -44.758  45.860   3.656  1.00 87.86           C  
ANISOU  505  CB  MET A  91    11680  12773   8928  -1369   -381    139       C  
ATOM    506  CG  MET A  91     -45.361  47.242   3.589  1.00 91.60           C  
ANISOU  506  CG  MET A  91    12352  13015   9438  -1474   -412    105       C  
ATOM    507  SD  MET A  91     -44.145  48.553   3.853  1.00 97.82           S  
ANISOU  507  SD  MET A  91    13129  13782  10258  -1780   -493    102       S  
ATOM    508  CE  MET A  91     -43.403  48.642   2.261  1.00 95.17           C  
ANISOU  508  CE  MET A  91    12682  13528   9950  -1886   -399    261       C  
ATOM    509  N   LEU A  92     -44.363  42.747   3.917  1.00 88.03           N  
ANISOU  509  N   LEU A  92    11440  13121   8888  -1006   -298    186       N  
ATOM    510  CA  LEU A  92     -43.905  41.450   3.407  1.00 88.08           C  
ANISOU  510  CA  LEU A  92    11319  13262   8888   -861   -228    239       C  
ATOM    511  C   LEU A  92     -44.923  40.345   3.675  1.00 92.81           C  
ANISOU  511  C   LEU A  92    12008  13781   9473   -677   -192    214       C  
ATOM    512  O   LEU A  92     -45.231  39.577   2.762  1.00 92.67           O  
ANISOU  512  O   LEU A  92    11997  13745   9467   -577   -108    231       O  
ATOM    513  CB  LEU A  92     -42.539  41.065   3.988  1.00 89.39           C  
ANISOU  513  CB  LEU A  92    11283  13647   9034   -868   -276    273       C  
ATOM    514  CG  LEU A  92     -41.334  41.847   3.492  1.00 95.54           C  
ANISOU  514  CG  LEU A  92    11905  14568   9830  -1047   -284    318       C  
ATOM    515  CD1 LEU A  92     -40.119  41.536   4.335  1.00 97.18           C  
ANISOU  515  CD1 LEU A  92    11904  15008  10011  -1056   -363    337       C  
ATOM    516  CD2 LEU A  92     -41.044  41.559   2.033  1.00 98.47           C  
ANISOU  516  CD2 LEU A  92    12204  14995  10214  -1014   -160    380       C  
ATOM    517  N   LYS A  93     -45.462  40.282   4.916  1.00 89.86           N  
ANISOU  517  N   LYS A  93    11710  13362   9069   -647   -252    170       N  
ATOM    518  CA  LYS A  93     -46.490  39.321   5.336  1.00 89.00           C  
ANISOU  518  CA  LYS A  93    11693  13176   8945   -508   -217    154       C  
ATOM    519  C   LYS A  93     -47.739  39.464   4.442  1.00 93.53           C  
ANISOU  519  C   LYS A  93    12381  13606   9550   -493   -153    126       C  
ATOM    520  O   LYS A  93     -48.325  38.456   4.047  1.00 92.69           O  
ANISOU  520  O   LYS A  93    12301  13463   9452   -392    -91    132       O  
ATOM    521  CB  LYS A  93     -46.867  39.543   6.818  1.00 91.12           C  
ANISOU  521  CB  LYS A  93    12029  13436   9156   -515   -288    112       C  
ATOM    522  CG  LYS A  93     -45.940  38.862   7.820  1.00100.70           C  
ANISOU  522  CG  LYS A  93    13147  14801  10313   -461   -348    155       C  
ATOM    523  CD  LYS A  93     -46.072  39.464   9.231  1.00110.66           C  
ANISOU  523  CD  LYS A  93    14466  16091  11490   -518   -439    100       C  
ATOM    524  CE  LYS A  93     -47.193  38.868  10.074  1.00120.87           C  
ANISOU  524  CE  LYS A  93    15879  17319  12726   -423   -407     90       C  
ATOM    525  NZ  LYS A  93     -47.488  39.670  11.304  1.00127.70           N  
ANISOU  525  NZ  LYS A  93    16824  18200  13496   -486   -477      9       N  
ATOM    526  N   MET A  94     -48.119  40.717   4.101  1.00 91.24           N  
ANISOU  526  N   MET A  94    12160  13232   9276   -594   -174     97       N  
ATOM    527  CA  MET A  94     -49.272  41.046   3.256  1.00 90.99           C  
ANISOU  527  CA  MET A  94    12225  13083   9266   -576   -134     79       C  
ATOM    528  C   MET A  94     -49.313  40.209   1.975  1.00 93.92           C  
ANISOU  528  C   MET A  94    12558  13483   9645   -516    -59    114       C  
ATOM    529  O   MET A  94     -50.338  39.594   1.678  1.00 93.26           O  
ANISOU  529  O   MET A  94    12524  13349   9562   -443    -24     90       O  
ATOM    530  CB  MET A  94     -49.258  42.539   2.901  1.00 94.37           C  
ANISOU  530  CB  MET A  94    12717  13427   9713   -690   -170     76       C  
ATOM    531  CG  MET A  94     -50.425  42.977   2.052  1.00 98.26           C  
ANISOU  531  CG  MET A  94    13306  13807  10220   -650   -145     73       C  
ATOM    532  SD  MET A  94     -50.389  44.758   1.800  1.00104.51           S  
ANISOU  532  SD  MET A  94    14212  14457  11041   -764   -194     83       S  
ATOM    533  CE  MET A  94     -49.188  44.881   0.455  1.00102.12           C  
ANISOU  533  CE  MET A  94    13828  14234  10739   -875   -156    193       C  
ATOM    534  N   LEU A  95     -48.191  40.204   1.233  1.00 89.78           N  
ANISOU  534  N   LEU A  95    11939  13053   9119   -555    -36    164       N  
ATOM    535  CA  LEU A  95     -48.002  39.514  -0.038  1.00 88.86           C  
ANISOU  535  CA  LEU A  95    11782  12989   8990   -504     41    188       C  
ATOM    536  C   LEU A  95     -47.818  38.001   0.048  1.00 91.93           C  
ANISOU  536  C   LEU A  95    12131  13423   9377   -370     90    174       C  
ATOM    537  O   LEU A  95     -48.073  37.337  -0.955  1.00 91.06           O  
ANISOU  537  O   LEU A  95    12038  13309   9252   -312    153    157       O  
ATOM    538  CB  LEU A  95     -46.830  40.128  -0.800  1.00 89.91           C  
ANISOU  538  CB  LEU A  95    11819  13228   9114   -601     60    250       C  
ATOM    539  CG  LEU A  95     -46.938  41.605  -1.129  1.00 94.91           C  
ANISOU  539  CG  LEU A  95    12532  13778   9750   -729     34    281       C  
ATOM    540  CD1 LEU A  95     -45.585  42.143  -1.386  1.00 96.04           C  
ANISOU  540  CD1 LEU A  95    12639  13936   9917   -879    -23    306       C  
ATOM    541  CD2 LEU A  95     -47.891  41.867  -2.334  1.00 98.81           C  
ANISOU  541  CD2 LEU A  95    13017  14322  10205   -741    104    332       C  
ATOM    542  N   ILE A  96     -47.421  37.440   1.218  1.00 88.79           N  
ANISOU  542  N   ILE A  96    11696  13053   8986   -317     58    179       N  
ATOM    543  CA  ILE A  96     -47.187  35.992   1.347  1.00 88.76           C  
ANISOU  543  CA  ILE A  96    11676  13063   8988   -176    101    182       C  
ATOM    544  C   ILE A  96     -48.382  35.169   0.812  1.00 91.53           C  
ANISOU  544  C   ILE A  96    12143  13289   9347   -123    152    132       C  
ATOM    545  O   ILE A  96     -48.188  34.362  -0.103  1.00 91.97           O  
ANISOU  545  O   ILE A  96    12198  13346   9400    -51    217    111       O  
ATOM    546  CB  ILE A  96     -46.699  35.511   2.739  1.00 92.44           C  
ANISOU  546  CB  ILE A  96    12107  13568   9448   -118     48    215       C  
ATOM    547  CG1 ILE A  96     -47.759  35.688   3.850  1.00 93.36           C  
ANISOU  547  CG1 ILE A  96    12333  13591   9550   -149      4    194       C  
ATOM    548  CG2 ILE A  96     -45.354  36.157   3.106  1.00 93.34           C  
ANISOU  548  CG2 ILE A  96    12073  13845   9548   -172     -8    257       C  
ATOM    549  CD1 ILE A  96     -47.302  35.444   5.390  1.00107.86           C  
ANISOU  549  CD1 ILE A  96    14148  15487  11345   -108    -61    235       C  
ATOM    550  N   LEU A  97     -49.605  35.439   1.305  1.00 86.10           N  
ANISOU  550  N   LEU A  97    11545  12506   8663   -167    125    103       N  
ATOM    551  CA  LEU A  97     -50.818  34.732   0.886  1.00 84.46           C  
ANISOU  551  CA  LEU A  97    11426  12201   8465   -150    161     55       C  
ATOM    552  C   LEU A  97     -51.079  34.762  -0.643  1.00 85.52           C  
ANISOU  552  C   LEU A  97    11573  12341   8581   -163    198     16       C  
ATOM    553  O   LEU A  97     -51.197  33.667  -1.191  1.00 84.87           O  
ANISOU  553  O   LEU A  97    11526  12220   8499   -109    246    -24       O  
ATOM    554  CB  LEU A  97     -52.060  35.191   1.670  1.00 83.81           C  
ANISOU  554  CB  LEU A  97    11399  12060   8383   -200    128     35       C  
ATOM    555  CG  LEU A  97     -53.385  34.685   1.119  1.00 88.08           C  
ANISOU  555  CG  LEU A  97    11996  12537   8934   -215    155    -16       C  
ATOM    556  CD1 LEU A  97     -53.770  33.366   1.726  1.00 88.71           C  
ANISOU  556  CD1 LEU A  97    12123  12549   9033   -188    192    -15       C  
ATOM    557  CD2 LEU A  97     -54.449  35.704   1.282  1.00 90.07           C  
ANISOU  557  CD2 LEU A  97    12256  12786   9179   -262    120    -38       C  
ATOM    558  N   PRO A  98     -51.188  35.922  -1.362  1.00 80.93           N  
ANISOU  558  N   PRO A  98    10979  11797   7974   -231    176     25       N  
ATOM    559  CA  PRO A  98     -51.450  35.843  -2.806  1.00 80.81           C  
ANISOU  559  CA  PRO A  98    10983  11806   7916   -233    209     -3       C  
ATOM    560  C   PRO A  98     -50.275  35.249  -3.561  1.00 86.05           C  
ANISOU  560  C   PRO A  98    11593  12551   8549   -178    275      0       C  
ATOM    561  O   PRO A  98     -50.480  34.685  -4.619  1.00 85.57           O  
ANISOU  561  O   PRO A  98    11566  12504   8443   -149    319    -51       O  
ATOM    562  CB  PRO A  98     -51.706  37.297  -3.218  1.00 82.36           C  
ANISOU  562  CB  PRO A  98    11186  12017   8090   -308    166     39       C  
ATOM    563  CG  PRO A  98     -51.875  38.059  -1.974  1.00 86.43           C  
ANISOU  563  CG  PRO A  98    11709  12481   8648   -341    111     57       C  
ATOM    564  CD  PRO A  98     -51.095  37.332  -0.935  1.00 82.23           C  
ANISOU  564  CD  PRO A  98    11133  11970   8142   -306    120     62       C  
ATOM    565  N   LEU A  99     -49.061  35.331  -2.992  1.00 84.05           N  
ANISOU  565  N   LEU A  99    11252  12368   8315   -157    283     51       N  
ATOM    566  CA  LEU A  99     -47.849  34.789  -3.594  1.00 84.93           C  
ANISOU  566  CA  LEU A  99    11279  12588   8402    -84    353     60       C  
ATOM    567  C   LEU A  99     -47.812  33.259  -3.609  1.00 89.11           C  
ANISOU  567  C   LEU A  99    11850  13060   8946     56    406     -1       C  
ATOM    568  O   LEU A  99     -47.518  32.696  -4.657  1.00 89.48           O  
ANISOU  568  O   LEU A  99    11903  13146   8948    121    479    -51       O  
ATOM    569  CB  LEU A  99     -46.601  35.350  -2.909  1.00 85.58           C  
ANISOU  569  CB  LEU A  99    11227  12786   8503   -110    332    135       C  
ATOM    570  CG  LEU A  99     -45.301  35.145  -3.645  1.00 91.82           C  
ANISOU  570  CG  LEU A  99    11885  13741   9260    -58    409    159       C  
ATOM    571  CD1 LEU A  99     -45.094  36.224  -4.697  1.00 92.06           C  
ANISOU  571  CD1 LEU A  99    11884  13861   9233   -180    439    201       C  
ATOM    572  CD2 LEU A  99     -44.158  35.092  -2.669  1.00 96.28           C  
ANISOU  572  CD2 LEU A  99    12306  14417   9860    -23    380    213       C  
ATOM    573  N   ILE A 100     -48.080  32.589  -2.462  1.00 84.83           N  
ANISOU  573  N   ILE A 100    11352  12421   8461    105    376      4       N  
ATOM    574  CA  ILE A 100     -48.059  31.118  -2.365  1.00 84.80           C  
ANISOU  574  CA  ILE A 100    11419  12317   8484    235    422    -37       C  
ATOM    575  C   ILE A 100     -49.178  30.467  -3.203  1.00 86.79           C  
ANISOU  575  C   ILE A 100    11805  12449   8724    209    451   -138       C  
ATOM    576  O   ILE A 100     -48.901  29.576  -4.016  1.00 86.59           O  
ANISOU  576  O   ILE A 100    11827  12394   8680    298    517   -210       O  
ATOM    577  CB  ILE A 100     -48.060  30.662  -0.878  1.00 87.85           C  
ANISOU  577  CB  ILE A 100    11826  12633   8922    278    378     24       C  
ATOM    578  CG1 ILE A 100     -46.666  30.867  -0.270  1.00 89.33           C  
ANISOU  578  CG1 ILE A 100    11870  12963   9108    357    360    104       C  
ATOM    579  CG2 ILE A 100     -48.507  29.200  -0.719  1.00 89.31           C  
ANISOU  579  CG2 ILE A 100    12146  12644   9145    368    418     -9       C  
ATOM    580  CD1 ILE A 100     -46.643  31.039   1.204  1.00 99.60           C  
ANISOU  580  CD1 ILE A 100    13157  14266  10420    346    283    178       C  
ATOM    581  N   VAL A 101     -50.428  30.934  -2.995  1.00 81.78           N  
ANISOU  581  N   VAL A 101    11223  11755   8093     88    398   -151       N  
ATOM    582  CA  VAL A 101     -51.651  30.460  -3.644  1.00 81.31           C  
ANISOU  582  CA  VAL A 101    11263  11608   8022     25    399   -241       C  
ATOM    583  C   VAL A 101     -51.571  30.592  -5.175  1.00 87.07           C  
ANISOU  583  C   VAL A 101    11997  12418   8669     22    429   -313       C  
ATOM    584  O   VAL A 101     -51.911  29.641  -5.879  1.00 88.48           O  
ANISOU  584  O   VAL A 101    12264  12528   8827     40    462   -416       O  
ATOM    585  CB  VAL A 101     -52.908  31.143  -3.034  1.00 83.62           C  
ANISOU  585  CB  VAL A 101    11560  11879   8332    -90    334   -222       C  
ATOM    586  CG1 VAL A 101     -54.188  30.707  -3.731  1.00 83.41           C  
ANISOU  586  CG1 VAL A 101    11599  11804   8291   -168    323   -313       C  
ATOM    587  CG2 VAL A 101     -53.010  30.859  -1.541  1.00 83.36           C  
ANISOU  587  CG2 VAL A 101    11539  11779   8356    -83    320   -160       C  
ATOM    588  N   SER A 102     -51.101  31.741  -5.690  1.00 82.60           N  
ANISOU  588  N   SER A 102    11348  11990   8047     -6    421   -260       N  
ATOM    589  CA  SER A 102     -51.008  31.928  -7.136  1.00 82.61           C  
ANISOU  589  CA  SER A 102    11355  12088   7945    -11    454   -308       C  
ATOM    590  C   SER A 102     -49.850  31.159  -7.751  1.00 86.92           C  
ANISOU  590  C   SER A 102    11885  12690   8452    110    551   -351       C  
ATOM    591  O   SER A 102     -49.989  30.666  -8.868  1.00 87.44           O  
ANISOU  591  O   SER A 102    12010  12781   8432    134    593   -448       O  
ATOM    592  CB  SER A 102     -50.931  33.405  -7.494  1.00 86.06           C  
ANISOU  592  CB  SER A 102    11729  12638   8333    -89    419   -217       C  
ATOM    593  OG  SER A 102     -49.705  33.975  -7.068  1.00 97.06           O  
ANISOU  593  OG  SER A 102    13020  14109   9747    -77    445   -126       O  
ATOM    594  N   SER A 103     -48.722  31.040  -7.021  1.00 83.70           N  
ANISOU  594  N   SER A 103    11390  12315   8098    195    583   -286       N  
ATOM    595  CA  SER A 103     -47.523  30.335  -7.488  1.00 85.24           C  
ANISOU  595  CA  SER A 103    11536  12586   8265    344    681   -316       C  
ATOM    596  C   SER A 103     -47.741  28.840  -7.686  1.00 90.35           C  
ANISOU  596  C   SER A 103    12317  13082   8931    463    729   -441       C  
ATOM    597  O   SER A 103     -47.438  28.314  -8.754  1.00 91.31           O  
ANISOU  597  O   SER A 103    12475  13244   8973    542    807   -541       O  
ATOM    598  CB  SER A 103     -46.340  30.583  -6.555  1.00 89.50           C  
ANISOU  598  CB  SER A 103    11930  13214   8864    407    683   -210       C  
ATOM    599  OG  SER A 103     -45.900  31.928  -6.646  1.00100.06           O  
ANISOU  599  OG  SER A 103    13144  14707  10169    290    661   -114       O  
ATOM    600  N   LEU A 104     -48.285  28.159  -6.676  1.00 87.20           N  
ANISOU  600  N   LEU A 104    12003  12499   8629    469    686   -437       N  
ATOM    601  CA  LEU A 104     -48.518  26.717  -6.754  1.00 88.40           C  
ANISOU  601  CA  LEU A 104    12310  12459   8818    565    727   -544       C  
ATOM    602  C   LEU A 104     -49.678  26.333  -7.687  1.00 92.77           C  
ANISOU  602  C   LEU A 104    13005  12926   9319    457    717   -686       C  
ATOM    603  O   LEU A 104     -49.557  25.324  -8.381  1.00 93.84           O  
ANISOU  603  O   LEU A 104    13256  12970   9430    543    778   -817       O  
ATOM    604  CB  LEU A 104     -48.679  26.090  -5.364  1.00 88.21           C  
ANISOU  604  CB  LEU A 104    12342  12267   8908    597    692   -471       C  
ATOM    605  CG  LEU A 104     -47.436  26.158  -4.470  1.00 93.19           C  
ANISOU  605  CG  LEU A 104    12849  12980   9579    742    699   -348       C  
ATOM    606  CD1 LEU A 104     -47.814  26.174  -3.032  1.00 92.99           C  
ANISOU  606  CD1 LEU A 104    12839  12869   9623    697    627   -239       C  
ATOM    607  CD2 LEU A 104     -46.465  25.028  -4.757  1.00 96.55           C  
ANISOU  607  CD2 LEU A 104    13308  13354  10021    979    785   -394       C  
ATOM    608  N   ILE A 105     -50.774  27.132  -7.737  1.00 88.37           N  
ANISOU  608  N   ILE A 105    12434  12404   8738    280    637   -670       N  
ATOM    609  CA  ILE A 105     -51.908  26.846  -8.632  1.00 88.69           C  
ANISOU  609  CA  ILE A 105    12576  12404   8718    167    606   -800       C  
ATOM    610  C   ILE A 105     -51.457  26.948 -10.093  1.00 95.61           C  
ANISOU  610  C   ILE A 105    13455  13423   9449    215    659   -894       C  
ATOM    611  O   ILE A 105     -51.696  26.005 -10.845  1.00 97.33           O  
ANISOU  611  O   ILE A 105    13800  13561   9619    234    689  -1052       O  
ATOM    612  CB  ILE A 105     -53.206  27.662  -8.320  1.00 89.89           C  
ANISOU  612  CB  ILE A 105    12692  12584   8880     -7    505   -755       C  
ATOM    613  CG1 ILE A 105     -53.800  27.269  -6.950  1.00 89.33           C  
ANISOU  613  CG1 ILE A 105    12646  12360   8933    -59    474   -697       C  
ATOM    614  CG2 ILE A 105     -54.261  27.493  -9.424  1.00 90.99           C  
ANISOU  614  CG2 ILE A 105    12893  12750   8927   -116    461   -886       C  
ATOM    615  CD1 ILE A 105     -54.881  28.207  -6.426  1.00 91.67           C  
ANISOU  615  CD1 ILE A 105    12869  12716   9246   -189    393   -631       C  
ATOM    616  N   THR A 106     -50.769  28.051 -10.485  1.00 92.21           N  
ANISOU  616  N   THR A 106    12895  13198   8942    232    677   -801       N  
ATOM    617  CA  THR A 106     -50.293  28.210 -11.867  1.00 93.39           C  
ANISOU  617  CA  THR A 106    13039  13513   8933    275    742   -867       C  
ATOM    618  C   THR A 106     -49.178  27.235 -12.185  1.00100.17           C  
ANISOU  618  C   THR A 106    13921  14364   9774    463    865   -952       C  
ATOM    619  O   THR A 106     -49.329  26.467 -13.130  1.00101.23           O  
ANISOU  619  O   THR A 106    14167  14487   9810    508    913  -1114       O  
ATOM    620  CB  THR A 106     -49.923  29.655 -12.221  1.00 99.07           C  
ANISOU  620  CB  THR A 106    13627  14440   9573    216    732   -726       C  
ATOM    621  OG1 THR A 106     -48.837  30.103 -11.415  1.00 96.08           O  
ANISOU  621  OG1 THR A 106    13118  14113   9274    271    768   -596       O  
ATOM    622  CG2 THR A 106     -51.074  30.585 -12.091  1.00 97.39           C  
ANISOU  622  CG2 THR A 106    13414  14227   9364     66    615   -660       C  
ATOM    623  N   GLY A 107     -48.118  27.242 -11.362  1.00 97.91           N  
ANISOU  623  N   GLY A 107    13532  14088   9581    577    909   -850       N  
ATOM    624  CA  GLY A 107     -46.926  26.396 -11.474  1.00100.03           C  
ANISOU  624  CA  GLY A 107    13783  14369   9856    794   1024   -899       C  
ATOM    625  C   GLY A 107     -47.192  24.924 -11.732  1.00106.33           C  
ANISOU  625  C   GLY A 107    14779  14947  10675    903   1065  -1079       C  
ATOM    626  O   GLY A 107     -46.597  24.352 -12.651  1.00108.37           O  
ANISOU  626  O   GLY A 107    15077  15254  10844   1051   1171  -1204       O  
ATOM    627  N   LEU A 108     -48.106  24.311 -10.944  1.00102.18           N  
ANISOU  627  N   LEU A 108    14386  14175  10262    825    989  -1098       N  
ATOM    628  CA  LEU A 108     -48.482  22.898 -11.079  1.00103.86           C  
ANISOU  628  CA  LEU A 108    14818  14127  10516    888   1017  -1261       C  
ATOM    629  C   LEU A 108     -49.461  22.630 -12.220  1.00108.55           C  
ANISOU  629  C   LEU A 108    15553  14695  10996    757    994  -1450       C  
ATOM    630  O   LEU A 108     -49.501  21.504 -12.730  1.00110.30           O  
ANISOU  630  O   LEU A 108    15957  14747  11203    832   1044  -1631       O  
ATOM    631  CB  LEU A 108     -49.009  22.325  -9.756  1.00103.49           C  
ANISOU  631  CB  LEU A 108    14857  13828  10636    846    956  -1185       C  
ATOM    632  CG  LEU A 108     -47.985  21.809  -8.721  1.00109.30           C  
ANISOU  632  CG  LEU A 108    15563  14482  11484   1059    999  -1073       C  
ATOM    633  CD1 LEU A 108     -47.389  20.456  -9.059  1.00112.40           C  
ANISOU  633  CD1 LEU A 108    16086  14739  11881   1302   1104  -1202       C  
ATOM    634  CD2 LEU A 108     -47.065  22.874  -8.138  1.00111.24           C  
ANISOU  634  CD2 LEU A 108    15565  14967  11736   1093    979   -884       C  
ATOM    635  N   ALA A 109     -50.225  23.667 -12.644  1.00103.61           N  
ANISOU  635  N   ALA A 109    14849  14235  10282    568    913  -1411       N  
ATOM    636  CA  ALA A 109     -51.145  23.596 -13.782  1.00104.13           C  
ANISOU  636  CA  ALA A 109    15012  14343  10211    436    869  -1571       C  
ATOM    637  C   ALA A 109     -50.352  23.716 -15.083  1.00110.84           C  
ANISOU  637  C   ALA A 109    15849  15394  10870    552    965  -1666       C  
ATOM    638  O   ALA A 109     -50.771  23.149 -16.085  1.00112.59           O  
ANISOU  638  O   ALA A 109    16209  15602  10967    526    970  -1863       O  
ATOM    639  CB  ALA A 109     -52.182  24.705 -13.700  1.00102.75           C  
ANISOU  639  CB  ALA A 109    14738  14290  10011    233    746  -1468       C  
ATOM    640  N   SER A 110     -49.197  24.436 -15.053  1.00107.71           N  
ANISOU  640  N   SER A 110    15285  15196  10443    671   1044  -1530       N  
ATOM    641  CA  SER A 110     -48.268  24.677 -16.169  1.00109.52           C  
ANISOU  641  CA  SER A 110    15464  15660  10488    785   1159  -1583       C  
ATOM    642  C   SER A 110     -47.621  23.371 -16.665  1.00116.80           C  
ANISOU  642  C   SER A 110    16504  16493  11381   1007   1290  -1772       C  
ATOM    643  O   SER A 110     -47.277  23.258 -17.838  1.00118.37           O  
ANISOU  643  O   SER A 110    16732  16853  11391   1082   1381  -1897       O  
ATOM    644  CB  SER A 110     -47.142  25.622 -15.725  1.00112.73           C  
ANISOU  644  CB  SER A 110    15643  16303  10888    814   1206  -1370       C  
ATOM    645  OG  SER A 110     -47.547  26.826 -15.108  1.00121.87           O  
ANISOU  645  OG  SER A 110    16689  17385  12230    855   1187  -1217       O  
ATOM    646  N   LEU A 111     -47.368  22.434 -15.729  1.00114.42           N  
ANISOU  646  N   LEU A 111    16279  15936  11259   1124   1303  -1790       N  
ATOM    647  CA  LEU A 111     -46.676  21.166 -15.939  1.00117.27           C  
ANISOU  647  CA  LEU A 111    16771  16150  11635   1369   1422  -1954       C  
ATOM    648  C   LEU A 111     -47.632  20.000 -16.091  1.00123.42           C  
ANISOU  648  C   LEU A 111    17836  16607  12451   1304   1376  -2169       C  
ATOM    649  O   LEU A 111     -48.737  20.026 -15.540  1.00121.40           O  
ANISOU  649  O   LEU A 111    17645  16197  12285   1088   1249  -2135       O  
ATOM    650  CB  LEU A 111     -45.729  20.890 -14.743  1.00117.12           C  
ANISOU  650  CB  LEU A 111    16659  16043  11800   1559   1460  -1808       C  
ATOM    651  CG  LEU A 111     -44.399  21.666 -14.668  1.00121.57           C  
ANISOU  651  CG  LEU A 111    16943  16904  12343   1695   1539  -1639       C  
ATOM    652  CD1 LEU A 111     -44.095  22.057 -13.264  1.00119.89           C  
ANISOU  652  CD1 LEU A 111    16613  16629  12312   1701   1468  -1431       C  
ATOM    653  CD2 LEU A 111     -43.248  20.883 -15.261  1.00127.81           C  
ANISOU  653  CD2 LEU A 111    17715  17781  13065   2002   1708  -1756       C  
ATOM    654  N   ASP A 112     -47.174  18.958 -16.816  1.00124.17           N  
ANISOU  654  N   ASP A 112    18101  16597  12481   1496   1486  -2392       N  
ATOM    655  CA  ASP A 112     -47.874  17.689 -17.014  1.00126.65           C  
ANISOU  655  CA  ASP A 112    18719  16568  12836   1465   1465  -2626       C  
ATOM    656  C   ASP A 112     -47.735  16.943 -15.695  1.00130.21           C  
ANISOU  656  C   ASP A 112    19248  16693  13533   1557   1454  -2523       C  
ATOM    657  O   ASP A 112     -46.672  17.003 -15.075  1.00129.46           O  
ANISOU  657  O   ASP A 112    19020  16651  13518   1787   1526  -2379       O  
ATOM    658  CB  ASP A 112     -47.216  16.871 -18.145  1.00132.67           C  
ANISOU  658  CB  ASP A 112    19632  17330  13447   1691   1607  -2892       C  
ATOM    659  CG  ASP A 112     -47.990  15.625 -18.541  1.00150.93           C  
ANISOU  659  CG  ASP A 112    22285  19290  15772   1631   1581  -3174       C  
ATOM    660  OD1 ASP A 112     -47.820  14.579 -17.869  1.00153.59           O  
ANISOU  660  OD1 ASP A 112    22799  19275  16284   1774   1617  -3213       O  
ATOM    661  OD2 ASP A 112     -48.785  15.703 -19.502  1.00160.07           O  
ANISOU  661  OD2 ASP A 112    23538  20520  16763   1435   1519  -3351       O  
ATOM    662  N   ALA A 113     -48.799  16.257 -15.260  1.00127.39           N  
ANISOU  662  N   ALA A 113    19096  16016  13290   1371   1362  -2585       N  
ATOM    663  CA  ALA A 113     -48.839  15.518 -13.991  1.00127.49           C  
ANISOU  663  CA  ALA A 113    19217  15695  13528   1416   1343  -2472       C  
ATOM    664  C   ALA A 113     -47.624  14.621 -13.737  1.00132.39           C  
ANISOU  664  C   ALA A 113    19923  16152  14228   1789   1471  -2489       C  
ATOM    665  O   ALA A 113     -47.134  14.548 -12.608  1.00131.84           O  
ANISOU  665  O   ALA A 113    19785  16001  14305   1915   1469  -2284       O  
ATOM    666  CB  ALA A 113     -50.122  14.707 -13.891  1.00129.43           C  
ANISOU  666  CB  ALA A 113    19716  15610  13850   1161   1257  -2599       C  
ATOM    667  N   LYS A 114     -47.135  13.951 -14.783  1.00130.30           N  
ANISOU  667  N   LYS A 114    19801  15853  13855   1978   1580  -2733       N  
ATOM    668  CA  LYS A 114     -45.972  13.094 -14.643  1.00132.33           C  
ANISOU  668  CA  LYS A 114    20134  15969  14177   2369   1710  -2767       C  
ATOM    669  C   LYS A 114     -44.689  13.901 -14.503  1.00134.36           C  
ANISOU  669  C   LYS A 114    20058  16604  14387   2610   1790  -2592       C  
ATOM    670  O   LYS A 114     -43.805  13.480 -13.759  1.00134.90           O  
ANISOU  670  O   LYS A 114    20085  16594  14577   2891   1842  -2474       O  
ATOM    671  CB  LYS A 114     -45.885  12.040 -15.758  1.00138.71           C  
ANISOU  671  CB  LYS A 114    21232  16578  14895   2514   1809  -3106       C  
ATOM    672  CG  LYS A 114     -45.949  10.599 -15.229  1.00154.28           C  
ANISOU  672  CG  LYS A 114    23550  18018  17050   2654   1831  -3192       C  
ATOM    673  CD  LYS A 114     -44.628  10.116 -14.571  1.00162.92           C  
ANISOU  673  CD  LYS A 114    24561  19020  18320   2978   1877  -2952       C  
ATOM    674  CE  LYS A 114     -44.790   8.763 -13.920  1.00174.31           C  
ANISOU  674  CE  LYS A 114    26275  20106  19847   3357   1994  -3095       C  
ATOM    675  NZ  LYS A 114     -43.603   8.410 -13.100  1.00180.93           N  
ANISOU  675  NZ  LYS A 114    26979  20936  20831   3681   2022  -2834       N  
ATOM    676  N   ALA A 115     -44.598  15.068 -15.179  1.00128.73           N  
ANISOU  676  N   ALA A 115    19105  16303  13503   2491   1793  -2559       N  
ATOM    677  CA  ALA A 115     -43.433  15.951 -15.099  1.00127.62           C  
ANISOU  677  CA  ALA A 115    18629  16550  13311   2655   1865  -2387       C  
ATOM    678  C   ALA A 115     -43.372  16.590 -13.722  1.00128.54           C  
ANISOU  678  C   ALA A 115    18557  16699  13585   2576   1762  -2089       C  
ATOM    679  O   ALA A 115     -42.278  16.809 -13.205  1.00128.41           O  
ANISOU  679  O   ALA A 115    18328  16850  13614   2790   1813  -1940       O  
ATOM    680  CB  ALA A 115     -43.505  17.026 -16.171  1.00127.38           C  
ANISOU  680  CB  ALA A 115    18435  16905  13061   2496   1884  -2416       C  
ATOM    681  N   SER A 116     -44.555  16.851 -13.117  1.00122.59           N  
ANISOU  681  N   SER A 116    17879  15792  12906   2272   1619  -2013       N  
ATOM    682  CA  SER A 116     -44.687  17.427 -11.781  1.00119.67           C  
ANISOU  682  CA  SER A 116    17369  15428  12670   2168   1514  -1753       C  
ATOM    683  C   SER A 116     -44.205  16.461 -10.700  1.00124.30           C  
ANISOU  683  C   SER A 116    18052  15747  13429   2395   1524  -1663       C  
ATOM    684  O   SER A 116     -43.660  16.901  -9.686  1.00122.68           O  
ANISOU  684  O   SER A 116    17663  15653  13299   2459   1485  -1445       O  
ATOM    685  CB  SER A 116     -46.102  17.932 -11.521  1.00120.90           C  
ANISOU  685  CB  SER A 116    17580  15513  12843   1805   1378  -1718       C  
ATOM    686  OG  SER A 116     -47.112  16.947 -11.569  1.00131.86           O  
ANISOU  686  OG  SER A 116    19257  16559  14286   1685   1342  -1866       O  
ATOM    687  N   GLY A 117     -44.359  15.162 -10.955  1.00123.31           N  
ANISOU  687  N   GLY A 117    18222  15276  13354   2524   1575  -1833       N  
ATOM    688  CA  GLY A 117     -43.865  14.104 -10.082  1.00125.22           C  
ANISOU  688  CA  GLY A 117    18604  15222  13750   2782   1599  -1761       C  
ATOM    689  C   GLY A 117     -42.356  13.989 -10.174  1.00131.42           C  
ANISOU  689  C   GLY A 117    19214  16202  14517   3182   1710  -1728       C  
ATOM    690  O   GLY A 117     -41.692  13.747  -9.165  1.00131.19           O  
ANISOU  690  O   GLY A 117    19112  16137  14597   3387   1693  -1544       O  
ATOM    691  N   ARG A 118     -41.806  14.182 -11.397  1.00130.10           N  
ANISOU  691  N   ARG A 118    18963  16272  14199   3296   1824  -1901       N  
ATOM    692  CA  ARG A 118     -40.369  14.153 -11.689  1.00132.30           C  
ANISOU  692  CA  ARG A 118    19031  16805  14430   3666   1954  -1895       C  
ATOM    693  C   ARG A 118     -39.698  15.327 -10.986  1.00134.40           C  
ANISOU  693  C   ARG A 118    18907  17462  14697   3626   1902  -1633       C  
ATOM    694  O   ARG A 118     -38.768  15.115 -10.209  1.00135.25           O  
ANISOU  694  O   ARG A 118    18870  17627  14891   3887   1910  -1485       O  
ATOM    695  CB  ARG A 118     -40.106  14.185 -13.207  1.00134.69           C  
ANISOU  695  CB  ARG A 118    19337  17298  14540   3733   2091  -2144       C  
ATOM    696  CG  ARG A 118     -40.401  12.860 -13.900  1.00151.98           C  
ANISOU  696  CG  ARG A 118    21905  19113  16726   3885   2170  -2432       C  
ATOM    697  CD  ARG A 118     -39.911  12.826 -15.342  1.00169.52           C  
ANISOU  697  CD  ARG A 118    24111  21561  18740   4031   2329  -2680       C  
ATOM    698  NE  ARG A 118     -40.780  13.581 -16.247  1.00180.57           N  
ANISOU  698  NE  ARG A 118    25513  23135  19962   3676   2285  -2780       N  
ATOM    699  CZ  ARG A 118     -40.661  13.600 -17.569  1.00198.86           C  
ANISOU  699  CZ  ARG A 118    27865  25632  22061   3713   2396  -3009       C  
ATOM    700  NH1 ARG A 118     -39.700  12.900 -18.169  1.00190.77           N  
ANISOU  700  NH1 ARG A 118    26876  24639  20970   4092   2573  -3179       N  
ATOM    701  NH2 ARG A 118     -41.499  14.316 -18.311  1.00184.69           N  
ANISOU  701  NH2 ARG A 118    26070  23999  20103   3386   2333  -3067       N  
ATOM    702  N   LEU A 119     -40.224  16.553 -11.205  1.00128.12           N  
ANISOU  702  N   LEU A 119    17956  16912  13813   3290   1835  -1573       N  
ATOM    703  CA  LEU A 119     -39.780  17.807 -10.587  1.00125.53           C  
ANISOU  703  CA  LEU A 119    17290  16925  13480   3168   1770  -1343       C  
ATOM    704  C   LEU A 119     -39.862  17.690  -9.055  1.00128.37           C  
ANISOU  704  C   LEU A 119    17643  17132  14000   3165   1645  -1132       C  
ATOM    705  O   LEU A 119     -38.931  18.090  -8.350  1.00127.93           O  
ANISOU  705  O   LEU A 119    17331  17299  13978   3288   1625   -960       O  
ATOM    706  CB  LEU A 119     -40.686  18.954 -11.083  1.00122.70           C  
ANISOU  706  CB  LEU A 119    16889  16715  13018   2785   1704  -1344       C  
ATOM    707  CG  LEU A 119     -40.148  19.840 -12.203  1.00127.65           C  
ANISOU  707  CG  LEU A 119    17311  17723  13467   2747   1799  -1386       C  
ATOM    708  CD1 LEU A 119     -40.270  19.197 -13.571  1.00130.12           C  
ANISOU  708  CD1 LEU A 119    17804  17996  13640   2841   1921  -1644       C  
ATOM    709  CD2 LEU A 119     -40.766  21.206 -12.152  1.00127.24           C  
ANISOU  709  CD2 LEU A 119    17138  17843  13364   2402   1699  -1265       C  
ATOM    710  N   GLY A 120     -40.959  17.097  -8.578  1.00124.51           N  
ANISOU  710  N   GLY A 120    17436  16275  13598   3027   1566  -1153       N  
ATOM    711  CA  GLY A 120     -41.229  16.859  -7.165  1.00123.71           C  
ANISOU  711  CA  GLY A 120    17390  15985  13631   3003   1456   -965       C  
ATOM    712  C   GLY A 120     -40.212  15.946  -6.514  1.00130.83           C  
ANISOU  712  C   GLY A 120    18295  16793  14623   3386   1492   -880       C  
ATOM    713  O   GLY A 120     -39.712  16.263  -5.434  1.00129.83           O  
ANISOU  713  O   GLY A 120    17996  16787  14545   3444   1415   -670       O  
ATOM    714  N   MET A 121     -39.872  14.821  -7.190  1.00130.99           N  
ANISOU  714  N   MET A 121    18507  16607  14656   3664   1606  -1049       N  
ATOM    715  CA  MET A 121     -38.883  13.833  -6.727  1.00134.14           C  
ANISOU  715  CA  MET A 121    18937  16888  15141   4091   1657   -992       C  
ATOM    716  C   MET A 121     -37.490  14.447  -6.638  1.00135.73           C  
ANISOU  716  C   MET A 121    18738  17538  15295   4321   1691   -879       C  
ATOM    717  O   MET A 121     -36.738  14.098  -5.737  1.00136.48           O  
ANISOU  717  O   MET A 121    18739  17652  15466   4580   1654   -713       O  
ATOM    718  CB  MET A 121     -38.861  12.591  -7.637  1.00140.53           C  
ANISOU  718  CB  MET A 121    20049  17386  15960   4332   1786  -1238       C  
ATOM    719  CG  MET A 121     -39.983  11.606  -7.363  1.00145.50           C  
ANISOU  719  CG  MET A 121    21106  17492  16685   4184   1745  -1314       C  
ATOM    720  SD  MET A 121     -39.695  10.567  -5.910  1.00152.15           S  
ANISOU  720  SD  MET A 121    22139  17962  17710   4378   1669  -1072       S  
ATOM    721  CE  MET A 121     -38.842   9.186  -6.666  1.00154.21           C  
ANISOU  721  CE  MET A 121    22654  17909  18028   4884   1816  -1249       C  
ATOM    722  N   ARG A 122     -37.163  15.374  -7.560  1.00129.53           N  
ANISOU  722  N   ARG A 122    17712  17125  14379   4214   1756   -959       N  
ATOM    723  CA  ARG A 122     -35.891  16.098  -7.589  1.00129.05           C  
ANISOU  723  CA  ARG A 122    17238  17534  14261   4359   1796   -858       C  
ATOM    724  C   ARG A 122     -35.811  17.006  -6.366  1.00128.92           C  
ANISOU  724  C   ARG A 122    16997  17702  14286   4174   1639   -608       C  
ATOM    725  O   ARG A 122     -34.788  17.021  -5.682  1.00129.46           O  
ANISOU  725  O   ARG A 122    16822  17978  14388   4394   1612   -460       O  
ATOM    726  CB  ARG A 122     -35.757  16.921  -8.885  1.00127.96           C  
ANISOU  726  CB  ARG A 122    16939  17715  13964   4213   1903   -992       C  
ATOM    727  CG  ARG A 122     -35.560  16.076 -10.133  1.00138.54           C  
ANISOU  727  CG  ARG A 122    18442  18971  15227   4450   2078  -1247       C  
ATOM    728  CD  ARG A 122     -35.268  16.917 -11.349  1.00146.08           C  
ANISOU  728  CD  ARG A 122    19201  20301  16002   4336   2192  -1345       C  
ATOM    729  NE  ARG A 122     -34.745  16.090 -12.435  1.00156.78           N  
ANISOU  729  NE  ARG A 122    20644  21658  17269   4650   2379  -1573       N  
ATOM    730  CZ  ARG A 122     -35.445  15.701 -13.496  1.00169.03           C  
ANISOU  730  CZ  ARG A 122    22470  23040  18714   4579   2449  -1816       C  
ATOM    731  NH1 ARG A 122     -36.710  16.076 -13.640  1.00152.86           N  
ANISOU  731  NH1 ARG A 122    20614  20826  16638   4200   2342  -1852       N  
ATOM    732  NH2 ARG A 122     -34.883  14.943 -14.427  1.00157.34           N  
ANISOU  732  NH2 ARG A 122    21064  21571  17145   4893   2625  -2032       N  
ATOM    733  N   ALA A 123     -36.915  17.720  -6.070  1.00121.69           N  
ANISOU  733  N   ALA A 123    16170  16703  13364   3780   1531   -569       N  
ATOM    734  CA  ALA A 123     -37.041  18.619  -4.926  1.00118.97           C  
ANISOU  734  CA  ALA A 123    15666  16491  13046   3565   1380   -364       C  
ATOM    735  C   ALA A 123     -36.904  17.845  -3.607  1.00123.67           C  
ANISOU  735  C   ALA A 123    16353  16888  13749   3751   1289   -205       C  
ATOM    736  O   ALA A 123     -35.961  18.106  -2.865  1.00124.17           O  
ANISOU  736  O   ALA A 123    16161  17197  13820   3891   1231    -49       O  
ATOM    737  CB  ALA A 123     -38.369  19.360  -4.984  1.00116.35           C  
ANISOU  737  CB  ALA A 123    15464  16056  12687   3152   1306   -391       C  
ATOM    738  N   VAL A 124     -37.794  16.850  -3.363  1.00120.14           N  
ANISOU  738  N   VAL A 124    16266  16004  13375   3762   1280   -244       N  
ATOM    739  CA  VAL A 124     -37.830  15.983  -2.172  1.00120.86           C  
ANISOU  739  CA  VAL A 124    16520  15838  13564   3925   1205    -88       C  
ATOM    740  C   VAL A 124     -36.466  15.316  -1.903  1.00127.46           C  
ANISOU  740  C   VAL A 124    17215  16780  14433   4382   1238     -5       C  
ATOM    741  O   VAL A 124     -36.011  15.331  -0.760  1.00127.19           O  
ANISOU  741  O   VAL A 124    17069  16832  14423   4488   1133    201       O  
ATOM    742  CB  VAL A 124     -38.999  14.955  -2.233  1.00125.23           C  
ANISOU  742  CB  VAL A 124    17506  15887  14190   3848   1225   -176       C  
ATOM    743  CG1 VAL A 124     -38.956  13.968  -1.069  1.00127.01           C  
ANISOU  743  CG1 VAL A 124    17924  15820  14513   4046   1170     -1       C  
ATOM    744  CG2 VAL A 124     -40.351  15.658  -2.275  1.00121.76           C  
ANISOU  744  CG2 VAL A 124    17155  15388  13721   3400   1167   -215       C  
ATOM    745  N   VAL A 125     -35.813  14.764  -2.951  1.00126.59           N  
ANISOU  745  N   VAL A 125    17098  16690  14310   4661   1383   -168       N  
ATOM    746  CA  VAL A 125     -34.495  14.120  -2.843  1.00130.03           C  
ANISOU  746  CA  VAL A 125    17379  17252  14775   5134   1435   -115       C  
ATOM    747  C   VAL A 125     -33.431  15.144  -2.428  1.00134.41           C  
ANISOU  747  C   VAL A 125    17458  18341  15271   5147   1373     34       C  
ATOM    748  O   VAL A 125     -32.641  14.859  -1.531  1.00135.80           O  
ANISOU  748  O   VAL A 125    17490  18625  15484   5408   1299    209       O  
ATOM    749  CB  VAL A 125     -34.122  13.304  -4.115  1.00136.63           C  
ANISOU  749  CB  VAL A 125    18331  17983  15599   5424   1621   -352       C  
ATOM    750  CG1 VAL A 125     -32.614  13.103  -4.262  1.00139.76           C  
ANISOU  750  CG1 VAL A 125    18413  18706  15983   5869   1699   -319       C  
ATOM    751  CG2 VAL A 125     -34.848  11.963  -4.131  1.00138.27           C  
ANISOU  751  CG2 VAL A 125    19020  17613  15904   5546   1654   -444       C  
ATOM    752  N   TYR A 126     -33.450  16.343  -3.041  1.00129.88           N  
ANISOU  752  N   TYR A 126    16651  18093  14604   4849   1393    -27       N  
ATOM    753  CA  TYR A 126     -32.528  17.431  -2.713  1.00130.06           C  
ANISOU  753  CA  TYR A 126    16232  18614  14571   4779   1333     99       C  
ATOM    754  C   TYR A 126     -32.735  17.894  -1.263  1.00132.97           C  
ANISOU  754  C   TYR A 126    16548  19009  14964   4614   1136    312       C  
ATOM    755  O   TYR A 126     -31.756  18.080  -0.540  1.00134.17           O  
ANISOU  755  O   TYR A 126    16411  19456  15113   4769   1056    462       O  
ATOM    756  CB  TYR A 126     -32.705  18.611  -3.692  1.00129.76           C  
ANISOU  756  CB  TYR A 126    16035  18835  14433   4443   1396     -7       C  
ATOM    757  CG  TYR A 126     -32.038  19.890  -3.236  1.00131.88           C  
ANISOU  757  CG  TYR A 126    15907  19546  14655   4243   1308    131       C  
ATOM    758  CD1 TYR A 126     -30.702  20.147  -3.545  1.00136.62           C  
ANISOU  758  CD1 TYR A 126    16117  20575  15216   4424   1375    161       C  
ATOM    759  CD2 TYR A 126     -32.725  20.833  -2.481  1.00129.98           C  
ANISOU  759  CD2 TYR A 126    15678  19298  14409   3871   1159    226       C  
ATOM    760  CE1 TYR A 126     -30.073  21.311  -3.106  1.00137.36           C  
ANISOU  760  CE1 TYR A 126    15848  21069  15274   4211   1286    284       C  
ATOM    761  CE2 TYR A 126     -32.101  21.985  -2.013  1.00130.56           C  
ANISOU  761  CE2 TYR A 126    15414  19748  14445   3681   1068    340       C  
ATOM    762  CZ  TYR A 126     -30.777  22.229  -2.345  1.00141.79           C  
ANISOU  762  CZ  TYR A 126    16456  21584  15835   3834   1129    368       C  
ATOM    763  OH  TYR A 126     -30.169  23.388  -1.928  1.00143.79           O  
ANISOU  763  OH  TYR A 126    16378  22204  16053   3606   1039    471       O  
ATOM    764  N   TYR A 127     -34.011  18.106  -0.863  1.00126.83           N  
ANISOU  764  N   TYR A 127    16037  17954  14200   4295   1059    318       N  
ATOM    765  CA  TYR A 127     -34.414  18.570   0.464  1.00124.85           C  
ANISOU  765  CA  TYR A 127    15786  17699  13952   4101    887    494       C  
ATOM    766  C   TYR A 127     -33.919  17.642   1.567  1.00131.71           C  
ANISOU  766  C   TYR A 127    16701  18472  14870   4426    807    668       C  
ATOM    767  O   TYR A 127     -33.191  18.096   2.447  1.00132.08           O  
ANISOU  767  O   TYR A 127    16488  18813  14884   4466    686    824       O  
ATOM    768  CB  TYR A 127     -35.945  18.717   0.564  1.00122.96           C  
ANISOU  768  CB  TYR A 127    15863  17135  13723   3760    857    445       C  
ATOM    769  CG  TYR A 127     -36.600  19.778  -0.299  1.00121.76           C  
ANISOU  769  CG  TYR A 127    15673  17077  13513   3403    893    314       C  
ATOM    770  CD1 TYR A 127     -35.917  20.941  -0.652  1.00122.86           C  
ANISOU  770  CD1 TYR A 127    15486  17610  13586   3277    890    315       C  
ATOM    771  CD2 TYR A 127     -37.921  19.650  -0.710  1.00120.89           C  
ANISOU  771  CD2 TYR A 127    15853  16666  13414   3178    919    205       C  
ATOM    772  CE1 TYR A 127     -36.536  21.944  -1.399  1.00121.24           C  
ANISOU  772  CE1 TYR A 127    15267  17473  13326   2955    915    221       C  
ATOM    773  CE2 TYR A 127     -38.549  20.643  -1.460  1.00119.50           C  
ANISOU  773  CE2 TYR A 127    15642  16585  13179   2869    937    104       C  
ATOM    774  CZ  TYR A 127     -37.851  21.788  -1.806  1.00126.72           C  
ANISOU  774  CZ  TYR A 127    16252  17868  14026   2768    936    118       C  
ATOM    775  OH  TYR A 127     -38.468  22.756  -2.563  1.00126.32           O  
ANISOU  775  OH  TYR A 127    16188  17891  13916   2478    953     36       O  
ATOM    776  N   MET A 128     -34.303  16.345   1.511  1.00130.33           N  
ANISOU  776  N   MET A 128    16865  17883  14771   4652    867    643       N  
ATOM    777  CA  MET A 128     -33.942  15.330   2.509  1.00133.14           C  
ANISOU  777  CA  MET A 128    17338  18068  15180   4979    801    821       C  
ATOM    778  C   MET A 128     -32.443  15.102   2.622  1.00138.23           C  
ANISOU  778  C   MET A 128    17666  19036  15821   5392    795    906       C  
ATOM    779  O   MET A 128     -31.952  14.934   3.735  1.00139.02           O  
ANISOU  779  O   MET A 128    17673  19236  15911   5554    665   1113       O  
ATOM    780  CB  MET A 128     -34.661  13.983   2.269  1.00137.65           C  
ANISOU  780  CB  MET A 128    18363  18092  15844   5123    886    759       C  
ATOM    781  CG  MET A 128     -36.174  14.002   2.445  1.00139.47           C  
ANISOU  781  CG  MET A 128    18919  17982  16091   4737    869    723       C  
ATOM    782  SD  MET A 128     -36.932  14.407   4.036  1.00142.55           S  
ANISOU  782  SD  MET A 128    19382  18333  16448   4472    700    963       S  
ATOM    783  CE  MET A 128     -38.664  14.598   3.498  1.00135.83           C  
ANISOU  783  CE  MET A 128    18774  17235  15601   3980    747    794       C  
ATOM    784  N   SER A 129     -31.721  15.097   1.486  1.00135.02           N  
ANISOU  784  N   SER A 129    17080  18814  15408   5566    934    751       N  
ATOM    785  CA  SER A 129     -30.274  14.895   1.477  1.00137.89           C  
ANISOU  785  CA  SER A 129    17100  19527  15766   5970    951    814       C  
ATOM    786  C   SER A 129     -29.552  16.047   2.166  1.00140.48           C  
ANISOU  786  C   SER A 129    16985  20373  16018   5812    809    953       C  
ATOM    787  O   SER A 129     -28.835  15.796   3.130  1.00142.14           O  
ANISOU  787  O   SER A 129    17038  20742  16226   6050    686   1140       O  
ATOM    788  CB  SER A 129     -29.750  14.671   0.061  1.00143.07           C  
ANISOU  788  CB  SER A 129    17670  20275  16417   6163   1153    601       C  
ATOM    789  OG  SER A 129     -30.153  15.703  -0.823  1.00149.49           O  
ANISOU  789  OG  SER A 129    18386  21256  17157   5774   1220    452       O  
ATOM    790  N   THR A 130     -29.802  17.307   1.728  1.00134.05           N  
ANISOU  790  N   THR A 130    15996  19798  15138   5395    812    871       N  
ATOM    791  CA  THR A 130     -29.200  18.523   2.297  1.00132.97           C  
ANISOU  791  CA  THR A 130    15463  20127  14931   5168    681    974       C  
ATOM    792  C   THR A 130     -29.500  18.674   3.802  1.00136.43           C  
ANISOU  792  C   THR A 130    15960  20530  15349   5063    470   1165       C  
ATOM    793  O   THR A 130     -28.625  19.108   4.553  1.00137.52           O  
ANISOU  793  O   THR A 130    15770  21041  15439   5109    336   1297       O  
ATOM    794  CB  THR A 130     -29.549  19.787   1.495  1.00136.73           C  
ANISOU  794  CB  THR A 130    15825  20774  15353   4733    736    847       C  
ATOM    795  OG1 THR A 130     -30.965  19.888   1.336  1.00132.89           O  
ANISOU  795  OG1 THR A 130    15712  19903  14876   4438    748    764       O  
ATOM    796  CG2 THR A 130     -28.847  19.847   0.140  1.00136.35           C  
ANISOU  796  CG2 THR A 130    15571  20950  15284   4851    926    705       C  
ATOM    797  N   THR A 131     -30.720  18.294   4.242  1.00131.32           N  
ANISOU  797  N   THR A 131    15719  19452  14725   4923    440   1180       N  
ATOM    798  CA  THR A 131     -31.130  18.340   5.654  1.00130.57           C  
ANISOU  798  CA  THR A 131    15730  19287  14593   4828    263   1358       C  
ATOM    799  C   THR A 131     -30.403  17.227   6.440  1.00138.39           C  
ANISOU  799  C   THR A 131    16732  20245  15605   5288    196   1541       C  
ATOM    800  O   THR A 131     -29.973  17.472   7.569  1.00138.91           O  
ANISOU  800  O   THR A 131    16640  20538  15601   5313     24   1715       O  
ATOM    801  CB  THR A 131     -32.676  18.349   5.788  1.00135.00           C  
ANISOU  801  CB  THR A 131    16689  19438  15167   4512    276   1311       C  
ATOM    802  OG1 THR A 131     -33.192  19.513   5.138  1.00131.16           O  
ANISOU  802  OG1 THR A 131    16128  19058  14649   4116    311   1166       O  
ATOM    803  CG2 THR A 131     -33.153  18.360   7.236  1.00133.33           C  
ANISOU  803  CG2 THR A 131    16603  19155  14901   4416    115   1494       C  
ATOM    804  N   ILE A 132     -30.240  16.027   5.829  1.00137.25           N  
ANISOU  804  N   ILE A 132    16774  19828  15548   5660    327   1497       N  
ATOM    805  CA  ILE A 132     -29.522  14.897   6.431  1.00140.89           C  
ANISOU  805  CA  ILE A 132    17269  20218  16044   6151    283   1666       C  
ATOM    806  C   ILE A 132     -28.022  15.230   6.549  1.00147.38           C  
ANISOU  806  C   ILE A 132    17585  21589  16822   6412    217   1739       C  
ATOM    807  O   ILE A 132     -27.397  14.884   7.555  1.00149.11           O  
ANISOU  807  O   ILE A 132    17695  21952  17009   6669     71   1947       O  
ATOM    808  CB  ILE A 132     -29.846  13.558   5.693  1.00145.89           C  
ANISOU  808  CB  ILE A 132    18281  20358  16792   6455    450   1573       C  
ATOM    809  CG1 ILE A 132     -30.959  12.795   6.433  1.00145.76           C  
ANISOU  809  CG1 ILE A 132    18744  19825  16813   6382    410   1683       C  
ATOM    810  CG2 ILE A 132     -28.619  12.662   5.454  1.00151.39           C  
ANISOU  810  CG2 ILE A 132    18832  21152  17539   7036    504   1612       C  
ATOM    811  CD1 ILE A 132     -31.865  11.954   5.552  1.00153.12           C  
ANISOU  811  CD1 ILE A 132    20108  20225  17846   6363    576   1510       C  
ATOM    812  N   ILE A 133     -27.474  15.955   5.552  1.00143.79           N  
ANISOU  812  N   ILE A 133    16812  21464  16356   6317    317   1580       N  
ATOM    813  CA  ILE A 133     -26.066  16.351   5.534  1.00146.35           C  
ANISOU  813  CA  ILE A 133    16618  22347  16642   6512    276   1630       C  
ATOM    814  C   ILE A 133     -25.783  17.452   6.574  1.00150.02           C  
ANISOU  814  C   ILE A 133    16784  23212  17006   6213     58   1759       C  
ATOM    815  O   ILE A 133     -24.748  17.385   7.236  1.00152.61           O  
ANISOU  815  O   ILE A 133    16787  23903  17295   6457    -70   1906       O  
ATOM    816  CB  ILE A 133     -25.485  16.665   4.137  1.00149.83           C  
ANISOU  816  CB  ILE A 133    16806  23028  17096   6541    471   1437       C  
ATOM    817  CG1 ILE A 133     -26.198  17.786   3.440  1.00146.48           C  
ANISOU  817  CG1 ILE A 133    16392  22630  16633   6017    533   1281       C  
ATOM    818  CG2 ILE A 133     -25.446  15.392   3.272  1.00152.53           C  
ANISOU  818  CG2 ILE A 133    17395  23038  17522   6972    667   1325       C  
ATOM    819  CD1 ILE A 133     -25.398  18.579   2.591  1.00156.02           C  
ANISOU  819  CD1 ILE A 133    17207  24268  17805   5937    638   1182       C  
ATOM    820  N   ALA A 134     -26.719  18.407   6.763  1.00143.30           N  
ANISOU  820  N   ALA A 134    16056  22283  16109   5708      8   1705       N  
ATOM    821  CA  ALA A 134     -26.603  19.484   7.753  1.00142.26           C  
ANISOU  821  CA  ALA A 134    15708  22467  15876   5387   -195   1795       C  
ATOM    822  C   ALA A 134     -26.651  18.956   9.206  1.00148.60           C  
ANISOU  822  C   ALA A 134    16632  23210  16621   5548   -390   2012       C  
ATOM    823  O   ALA A 134     -25.843  19.390  10.030  1.00150.09           O  
ANISOU  823  O   ALA A 134    16498  23807  16723   5567   -569   2131       O  
ATOM    824  CB  ALA A 134     -27.694  20.521   7.530  1.00138.45           C  
ANISOU  824  CB  ALA A 134    15392  21841  15370   4857   -176   1669       C  
ATOM    825  N   VAL A 135     -27.578  18.013   9.507  1.00145.02           N  
ANISOU  825  N   VAL A 135    16636  22260  16205   5659   -355   2069       N  
ATOM    826  CA  VAL A 135     -27.748  17.409  10.838  1.00146.30           C  
ANISOU  826  CA  VAL A 135    16977  22305  16303   5812   -514   2292       C  
ATOM    827  C   VAL A 135     -26.531  16.518  11.213  1.00154.73           C  
ANISOU  827  C   VAL A 135    17844  23571  17374   6359   -585   2467       C  
ATOM    828  O   VAL A 135     -26.162  16.469  12.388  1.00156.12           O  
ANISOU  828  O   VAL A 135    17930  23941  17446   6460   -782   2666       O  
ATOM    829  CB  VAL A 135     -29.128  16.693  11.010  1.00148.59           C  
ANISOU  829  CB  VAL A 135    17813  22008  16636   5729   -440   2309       C  
ATOM    830  CG1 VAL A 135     -29.238  15.422  10.173  1.00150.34           C  
ANISOU  830  CG1 VAL A 135    18308  21819  16996   6072   -260   2261       C  
ATOM    831  CG2 VAL A 135     -29.432  16.397  12.470  1.00149.23           C  
ANISOU  831  CG2 VAL A 135    18062  22027  16612   5754   -611   2542       C  
ATOM    832  N   VAL A 136     -25.897  15.856  10.214  1.00153.33           N  
ANISOU  832  N   VAL A 136    17583  23372  17304   6715   -429   2388       N  
ATOM    833  CA  VAL A 136     -24.707  15.016  10.409  1.00158.00           C  
ANISOU  833  CA  VAL A 136    17959  24160  17914   7275   -471   2530       C  
ATOM    834  C   VAL A 136     -23.499  15.922  10.706  1.00162.95           C  
ANISOU  834  C   VAL A 136    17989  25472  18450   7245   -616   2570       C  
ATOM    835  O   VAL A 136     -22.747  15.643  11.645  1.00165.65           O  
ANISOU  835  O   VAL A 136    18138  26080  18722   7519   -798   2773       O  
ATOM    836  CB  VAL A 136     -24.490  14.028   9.225  1.00164.04           C  
ANISOU  836  CB  VAL A 136    18854  24655  18818   7665   -241   2407       C  
ATOM    837  CG1 VAL A 136     -23.044  13.539   9.130  1.00168.83           C  
ANISOU  837  CG1 VAL A 136    19075  25630  19442   8206   -253   2488       C  
ATOM    838  CG2 VAL A 136     -25.447  12.845   9.328  1.00164.05           C  
ANISOU  838  CG2 VAL A 136    19441  23990  18900   7816   -166   2452       C  
ATOM    839  N   LEU A 137     -23.359  17.032   9.941  1.00156.91           N  
ANISOU  839  N   LEU A 137    16948  24991  17681   6884   -546   2385       N  
ATOM    840  CA  LEU A 137     -22.309  18.041  10.117  1.00157.66           C  
ANISOU  840  CA  LEU A 137    16482  25723  17698   6744   -669   2394       C  
ATOM    841  C   LEU A 137     -22.476  18.720  11.480  1.00160.21           C  
ANISOU  841  C   LEU A 137    16766  26224  17883   6462   -932   2525       C  
ATOM    842  O   LEU A 137     -21.484  18.939  12.174  1.00162.45           O  
ANISOU  842  O   LEU A 137    16661  26979  18083   6578  -1117   2647       O  
ATOM    843  CB  LEU A 137     -22.363  19.085   8.988  1.00155.08           C  
ANISOU  843  CB  LEU A 137    15974  25551  17398   6347   -521   2174       C  
ATOM    844  CG  LEU A 137     -21.170  20.030   8.894  1.00161.90           C  
ANISOU  844  CG  LEU A 137    16237  27066  18211   6221   -593   2164       C  
ATOM    845  CD1 LEU A 137     -20.224  19.606   7.789  1.00165.28           C  
ANISOU  845  CD1 LEU A 137    16374  27714  18711   6549   -397   2088       C  
ATOM    846  CD2 LEU A 137     -21.621  21.447   8.663  1.00161.12           C  
ANISOU  846  CD2 LEU A 137    16079  27067  18070   5602   -607   2037       C  
ATOM    847  N   GLY A 138     -23.727  19.003  11.848  1.00152.24           N  
ANISOU  847  N   GLY A 138    16157  24844  16844   6114   -944   2494       N  
ATOM    848  CA  GLY A 138     -24.095  19.616  13.119  1.00150.60           C  
ANISOU  848  CA  GLY A 138    15998  24729  16493   5830  -1165   2591       C  
ATOM    849  C   GLY A 138     -23.728  18.769  14.322  1.00157.69           C  
ANISOU  849  C   GLY A 138    16938  25676  17302   6200  -1348   2845       C  
ATOM    850  O   GLY A 138     -23.220  19.301  15.312  1.00158.09           O  
ANISOU  850  O   GLY A 138    16744  26115  17209   6111  -1576   2945       O  
ATOM    851  N   ILE A 139     -23.972  17.441  14.235  1.00156.22           N  
ANISOU  851  N   ILE A 139    17069  25092  17195   6617  -1253   2952       N  
ATOM    852  CA  ILE A 139     -23.661  16.452  15.274  1.00159.29           C  
ANISOU  852  CA  ILE A 139    17560  25448  17515   7032  -1400   3220       C  
ATOM    853  C   ILE A 139     -22.131  16.292  15.431  1.00167.37           C  
ANISOU  853  C   ILE A 139    18075  27009  18509   7432  -1527   3332       C  
ATOM    854  O   ILE A 139     -21.639  16.260  16.558  1.00169.27           O  
ANISOU  854  O   ILE A 139    18167  27544  18605   7556  -1762   3529       O  
ATOM    855  CB  ILE A 139     -24.432  15.115  15.011  1.00162.45           C  
ANISOU  855  CB  ILE A 139    18487  25205  18033   7322  -1239   3284       C  
ATOM    856  CG1 ILE A 139     -25.881  15.212  15.541  1.00158.73           C  
ANISOU  856  CG1 ILE A 139    18486  24311  17514   6947  -1226   3293       C  
ATOM    857  CG2 ILE A 139     -23.719  13.882  15.590  1.00168.78           C  
ANISOU  857  CG2 ILE A 139    19320  25978  18830   7925  -1324   3545       C  
ATOM    858  CD1 ILE A 139     -26.871  14.142  15.043  1.00165.88           C  
ANISOU  858  CD1 ILE A 139    19918  24554  18556   7052  -1029   3279       C  
ATOM    859  N   ILE A 140     -21.391  16.234  14.306  1.00164.93           N  
ANISOU  859  N   ILE A 140    17486  26859  18322   7620  -1373   3201       N  
ATOM    860  CA  ILE A 140     -19.930  16.105  14.286  1.00169.01           C  
ANISOU  860  CA  ILE A 140    17473  27914  18827   7999  -1457   3279       C  
ATOM    861  C   ILE A 140     -19.254  17.319  14.963  1.00172.99           C  
ANISOU  861  C   ILE A 140    17493  29052  19183   7663  -1690   3289       C  
ATOM    862  O   ILE A 140     -18.381  17.124  15.813  1.00176.20           O  
ANISOU  862  O   ILE A 140    17605  29856  19488   7931  -1905   3474       O  
ATOM    863  CB  ILE A 140     -19.431  15.807  12.842  1.00172.79           C  
ANISOU  863  CB  ILE A 140    17795  28394  19465   8230  -1199   3108       C  
ATOM    864  CG1 ILE A 140     -19.482  14.288  12.579  1.00175.87           C  
ANISOU  864  CG1 ILE A 140    18521  28333  19968   8822  -1070   3194       C  
ATOM    865  CG2 ILE A 140     -18.026  16.367  12.554  1.00176.21           C  
ANISOU  865  CG2 ILE A 140    17549  29526  19876   8319  -1249   3082       C  
ATOM    866  CD1 ILE A 140     -19.821  13.891  11.158  1.00184.25           C  
ANISOU  866  CD1 ILE A 140    19783  29041  21182   8894   -766   2970       C  
ATOM    867  N   LEU A 141     -19.707  18.551  14.633  1.00165.83           N  
ANISOU  867  N   LEU A 141    16532  28218  18259   7077  -1658   3094       N  
ATOM    868  CA  LEU A 141     -19.183  19.805  15.191  1.00165.50           C  
ANISOU  868  CA  LEU A 141    16087  28709  18087   6677  -1864   3064       C  
ATOM    869  C   LEU A 141     -19.361  19.936  16.714  1.00169.85           C  
ANISOU  869  C   LEU A 141    16721  29367  18447   6600  -2149   3232       C  
ATOM    870  O   LEU A 141     -18.509  20.539  17.369  1.00171.48           O  
ANISOU  870  O   LEU A 141    16508  30116  18531   6507  -2372   3278       O  
ATOM    871  CB  LEU A 141     -19.772  21.025  14.464  1.00160.93           C  
ANISOU  871  CB  LEU A 141    15537  28068  17542   6078  -1752   2827       C  
ATOM    872  CG  LEU A 141     -19.009  21.502  13.233  1.00165.39           C  
ANISOU  872  CG  LEU A 141    15719  28910  18213   6013  -1580   2672       C  
ATOM    873  CD1 LEU A 141     -19.957  21.871  12.118  1.00160.95           C  
ANISOU  873  CD1 LEU A 141    15460  27943  17749   5686  -1338   2470       C  
ATOM    874  CD2 LEU A 141     -18.092  22.664  13.567  1.00167.99           C  
ANISOU  874  CD2 LEU A 141    15506  29865  18456   5693  -1754   2645       C  
ATOM    875  N   VAL A 142     -20.450  19.373  17.276  1.00165.05           N  
ANISOU  875  N   VAL A 142    16642  28265  17803   6620  -2141   3320       N  
ATOM    876  CA  VAL A 142     -20.693  19.420  18.724  1.00165.99           C  
ANISOU  876  CA  VAL A 142    16883  28468  17719   6560  -2392   3489       C  
ATOM    877  C   VAL A 142     -19.965  18.257  19.437  1.00176.70           C  
ANISOU  877  C   VAL A 142    18169  29955  19013   7158  -2534   3772       C  
ATOM    878  O   VAL A 142     -19.419  18.469  20.518  1.00178.82           O  
ANISOU  878  O   VAL A 142    18214  30637  19095   7185  -2802   3912       O  
ATOM    879  CB  VAL A 142     -22.189  19.561  19.123  1.00165.37           C  
ANISOU  879  CB  VAL A 142    17352  27893  17590   6231  -2340   3457       C  
ATOM    880  CG1 VAL A 142     -23.044  18.383  18.669  1.00164.07           C  
ANISOU  880  CG1 VAL A 142    17680  27099  17560   6491  -2125   3514       C  
ATOM    881  CG2 VAL A 142     -22.372  19.885  20.602  1.00165.99           C  
ANISOU  881  CG2 VAL A 142    17489  28157  17422   6092  -2601   3594       C  
ATOM    882  N   LEU A 143     -19.901  17.058  18.821  1.00175.75           N  
ANISOU  882  N   LEU A 143    18228  29504  19044   7642  -2364   3852       N  
ATOM    883  CA  LEU A 143     -19.195  15.919  19.421  1.00180.72           C  
ANISOU  883  CA  LEU A 143    18812  30217  19636   8254  -2484   4128       C  
ATOM    884  C   LEU A 143     -17.663  16.115  19.458  1.00189.04           C  
ANISOU  884  C   LEU A 143    19272  31777  20779   8366  -2667   4115       C  
ATOM    885  O   LEU A 143     -16.955  15.329  20.092  1.00191.44           O  
ANISOU  885  O   LEU A 143    19593  31853  21293   8518  -2887   4221       O  
ATOM    886  CB  LEU A 143     -19.577  14.585  18.749  1.00181.25           C  
ANISOU  886  CB  LEU A 143    19283  29698  19886   8698  -2254   4183       C  
ATOM    887  CG  LEU A 143     -21.028  14.096  18.896  1.00182.07           C  
ANISOU  887  CG  LEU A 143    20052  29107  20020   8535  -2126   4204       C  
ATOM    888  CD1 LEU A 143     -21.233  12.822  18.113  1.00183.42           C  
ANISOU  888  CD1 LEU A 143    20559  28746  20388   8964  -1901   4223       C  
ATOM    889  CD2 LEU A 143     -21.422  13.879  20.359  1.00185.28           C  
ANISOU  889  CD2 LEU A 143    20701  29477  20220   8528  -2341   4464       C  
ATOM    890  N   ILE A 144     -17.169  17.189  18.809  1.00185.51           N  
ANISOU  890  N   ILE A 144    18337  31896  20253   8159  -2606   3951       N  
ATOM    891  CA  ILE A 144     -15.759  17.579  18.767  1.00187.54           C  
ANISOU  891  CA  ILE A 144    18089  32415  20753   7982  -2789   3831       C  
ATOM    892  C   ILE A 144     -15.516  18.799  19.697  1.00192.08           C  
ANISOU  892  C   ILE A 144    18476  33237  21269   7363  -3086   3735       C  
ATOM    893  O   ILE A 144     -14.573  18.766  20.486  1.00193.15           O  
ANISOU  893  O   ILE A 144    18449  33348  21589   7239  -3395   3739       O  
ATOM    894  CB  ILE A 144     -15.269  17.767  17.292  1.00189.61           C  
ANISOU  894  CB  ILE A 144    18126  32629  21288   7918  -2536   3592       C  
ATOM    895  CG1 ILE A 144     -15.142  16.402  16.538  1.00190.91           C  
ANISOU  895  CG1 ILE A 144    18546  32209  21782   8342  -2358   3580       C  
ATOM    896  CG2 ILE A 144     -13.984  18.607  17.176  1.00190.78           C  
ANISOU  896  CG2 ILE A 144    17755  33059  21675   7525  -2690   3413       C  
ATOM    897  CD1 ILE A 144     -13.971  15.373  16.940  1.00197.88           C  
ANISOU  897  CD1 ILE A 144    19530  32214  23440   8123  -2653   3462       C  
ATOM    898  N   ILE A 145     -16.361  19.852  19.601  1.00188.83           N  
ANISOU  898  N   ILE A 145    17999  33279  20468   7129  -2974   3705       N  
ATOM    899  CA  ILE A 145     -16.286  21.067  20.430  1.00189.02           C  
ANISOU  899  CA  ILE A 145    17819  33702  20298   6628  -3210   3639       C  
ATOM    900  C   ILE A 145     -17.287  20.869  21.556  1.00192.97           C  
ANISOU  900  C   ILE A 145    18867  33751  20701   6481  -3331   3715       C  
ATOM    901  O   ILE A 145     -18.461  20.678  21.260  1.00189.67           O  
ANISOU  901  O   ILE A 145    18863  32948  20254   6409  -3126   3684       O  
ATOM    902  CB  ILE A 145     -16.695  22.350  19.634  1.00188.43           C  
ANISOU  902  CB  ILE A 145    17676  33652  20267   6041  -3066   3369       C  
ATOM    903  CG1 ILE A 145     -15.941  22.520  18.270  1.00189.87           C  
ANISOU  903  CG1 ILE A 145    17474  34030  20638   6085  -2857   3241       C  
ATOM    904  CG2 ILE A 145     -16.585  23.618  20.494  1.00189.27           C  
ANISOU  904  CG2 ILE A 145    17590  34135  20190   5516  -3323   3284       C  
ATOM    905  CD1 ILE A 145     -14.372  22.640  18.289  1.00198.27           C  
ANISOU  905  CD1 ILE A 145    18361  34656  22317   5748  -3080   3031       C  
ATOM    906  N   HIS A 146     -16.883  20.934  22.806  1.00192.97           N  
ANISOU  906  N   HIS A 146    18836  33892  20593   6473  -3642   3834       N  
ATOM    907  CA  HIS A 146     -17.861  20.764  23.866  1.00192.89           C  
ANISOU  907  CA  HIS A 146    19225  33748  20317   6473  -3732   3986       C  
ATOM    908  C   HIS A 146     -18.222  22.155  24.426  1.00194.81           C  
ANISOU  908  C   HIS A 146    19417  34234  20366   5875  -3880   3813       C  
ATOM    909  O   HIS A 146     -17.514  22.639  25.310  1.00196.36           O  
ANISOU  909  O   HIS A 146    19449  34586  20572   5629  -4193   3760       O  
ATOM    910  CB  HIS A 146     -17.301  19.797  24.922  1.00195.95           C  
ANISOU  910  CB  HIS A 146    19835  33689  20930   6628  -4018   4123       C  
ATOM    911  CG  HIS A 146     -18.169  19.580  26.123  1.00198.68           C  
ANISOU  911  CG  HIS A 146    20652  33709  21128   6479  -4185   4233       C  
ATOM    912  ND1 HIS A 146     -18.901  18.417  26.284  1.00199.66           N  
ANISOU  912  ND1 HIS A 146    21278  33342  21241   6704  -4031   4399       N  
ATOM    913  CD2 HIS A 146     -18.357  20.366  27.209  1.00200.76           C  
ANISOU  913  CD2 HIS A 146    20934  34122  21224   6155  -4483   4209       C  
ATOM    914  CE1 HIS A 146     -19.511  18.536  27.453  1.00199.78           C  
ANISOU  914  CE1 HIS A 146    21501  33447  20958   6629  -4207   4542       C  
ATOM    915  NE2 HIS A 146     -19.221  19.696  28.041  1.00200.59           N  
ANISOU  915  NE2 HIS A 146    21345  33900  20969   6279  -4486   4414       N  
ATOM    916  N   PRO A 147     -19.272  22.863  23.933  1.00186.91           N  
ANISOU  916  N   PRO A 147    18650  33034  19334   5507  -3688   3644       N  
ATOM    917  CA  PRO A 147     -19.569  24.190  24.493  1.00189.75           C  
ANISOU  917  CA  PRO A 147    18976  33584  19536   4938  -3835   3459       C  
ATOM    918  C   PRO A 147     -20.110  24.146  25.920  1.00217.33           C  
ANISOU  918  C   PRO A 147    23661  35096  23816   4069  -4178   3091       C  
ATOM    919  O   PRO A 147     -19.946  25.093  26.677  1.00191.21           O  
ANISOU  919  O   PRO A 147    19362  34030  19260   4492  -4220   3445       O  
ATOM    920  CB  PRO A 147     -20.606  24.764  23.526  1.00185.39           C  
ANISOU  920  CB  PRO A 147    18732  32551  19156   4559  -3562   3227       C  
ATOM    921  CG  PRO A 147     -20.651  23.852  22.369  1.00187.18           C  
ANISOU  921  CG  PRO A 147    19062  32431  19627   4896  -3290   3267       C  
ATOM    922  CD  PRO A 147     -20.226  22.528  22.859  1.00185.33           C  
ANISOU  922  CD  PRO A 147    18846  32221  19351   5481  -3360   3548       C  
ATOM    923  N   GLU A 171     -48.921  18.149  24.335  1.00122.72           N  
ANISOU  923  N   GLU A 171    18277  16656  11697   1451      7   3411       N  
ATOM    924  CA  GLU A 171     -48.010  17.004  24.364  1.00125.56           C  
ANISOU  924  CA  GLU A 171    18763  16835  12109   1738    -53   3637       C  
ATOM    925  C   GLU A 171     -47.314  16.857  23.000  1.00128.17           C  
ANISOU  925  C   GLU A 171    19000  17003  12695   1880    -74   3473       C  
ATOM    926  O   GLU A 171     -47.728  17.507  22.040  1.00124.87           O  
ANISOU  926  O   GLU A 171    18465  16567  12413   1716    -19   3213       O  
ATOM    927  CB  GLU A 171     -48.780  15.725  24.747  1.00129.77           C  
ANISOU  927  CB  GLU A 171    19613  17033  12660   1688     83   3898       C  
ATOM    928  CG  GLU A 171     -47.983  14.712  25.551  1.00147.18           C  
ANISOU  928  CG  GLU A 171    21987  19176  14760   1973      2   4234       C  
ATOM    929  CD  GLU A 171     -47.686  15.126  26.978  1.00179.03           C  
ANISOU  929  CD  GLU A 171    25980  23583  18461   2020   -106   4403       C  
ATOM    930  OE1 GLU A 171     -48.626  15.128  27.807  1.00179.39           O  
ANISOU  930  OE1 GLU A 171    26143  23676  18339   1815     -6   4511       O  
ATOM    931  OE2 GLU A 171     -46.511  15.451  27.266  1.00178.16           O  
ANISOU  931  OE2 GLU A 171    25709  23735  18247   2260   -289   4423       O  
ATOM    932  N   VAL A 172     -46.258  16.025  22.910  1.00127.12           N  
ANISOU  932  N   VAL A 172    18914  16767  12619   2195   -151   3624       N  
ATOM    933  CA  VAL A 172     -45.493  15.835  21.669  1.00126.37           C  
ANISOU  933  CA  VAL A 172    18722  16549  12744   2371   -166   3476       C  
ATOM    934  C   VAL A 172     -46.315  15.084  20.587  1.00129.36           C  
ANISOU  934  C   VAL A 172    19297  16492  13362   2255      2   3384       C  
ATOM    935  O   VAL A 172     -46.166  15.407  19.409  1.00126.93           O  
ANISOU  935  O   VAL A 172    18868  16145  13214   2239     28   3148       O  
ATOM    936  CB  VAL A 172     -44.095  15.214  21.931  1.00133.38           C  
ANISOU  936  CB  VAL A 172    19572  17497  13609   2772   -299   3656       C  
ATOM    937  CG1 VAL A 172     -43.288  15.061  20.642  1.00132.67           C  
ANISOU  937  CG1 VAL A 172    19360  17315  13735   2965   -298   3491       C  
ATOM    938  CG2 VAL A 172     -43.322  16.067  22.929  1.00133.65           C  
ANISOU  938  CG2 VAL A 172    19377  18002  13401   2840   -481   3707       C  
ATOM    939  N   LEU A 173     -47.209  14.145  20.974  1.00127.34           N  
ANISOU  939  N   LEU A 173    19333  15928  13120   2146    116   3558       N  
ATOM    940  CA  LEU A 173     -48.074  13.457  20.002  1.00126.60           C  
ANISOU  940  CA  LEU A 173    19427  15431  13243   1985    267   3456       C  
ATOM    941  C   LEU A 173     -49.036  14.478  19.387  1.00126.23           C  
ANISOU  941  C   LEU A 173    19222  15509  13230   1652    333   3180       C  
ATOM    942  O   LEU A 173     -49.242  14.472  18.173  1.00124.20           O  
ANISOU  942  O   LEU A 173    18942  15097  13151   1587    388   2965       O  
ATOM    943  CB  LEU A 173     -48.851  12.290  20.646  1.00129.73           C  
ANISOU  943  CB  LEU A 173    20165  15489  13637   1895    372   3716       C  
ATOM    944  CG  LEU A 173     -50.049  11.717  19.861  1.00134.21           C  
ANISOU  944  CG  LEU A 173    20919  15686  14387   1607    534   3610       C  
ATOM    945  CD1 LEU A 173     -49.609  10.945  18.617  1.00135.00           C  
ANISOU  945  CD1 LEU A 173    21133  15435  14728   1765    560   3480       C  
ATOM    946  CD2 LEU A 173     -50.904  10.847  20.740  1.00139.78           C  
ANISOU  946  CD2 LEU A 173    21908  16165  15037   1441    634   3881       C  
ATOM    947  N   ASP A 174     -49.566  15.389  20.231  1.00121.58           N  
ANISOU  947  N   ASP A 174    18517  15222  12454   1469    319   3184       N  
ATOM    948  CA  ASP A 174     -50.455  16.485  19.854  1.00118.33           C  
ANISOU  948  CA  ASP A 174    17940  14980  12039   1187    366   2947       C  
ATOM    949  C   ASP A 174     -49.833  17.361  18.779  1.00119.50           C  
ANISOU  949  C   ASP A 174    17853  15268  12284   1245    299   2682       C  
ATOM    950  O   ASP A 174     -50.568  17.897  17.959  1.00117.45           O  
ANISOU  950  O   ASP A 174    17517  14994  12115   1047    361   2471       O  
ATOM    951  CB  ASP A 174     -50.827  17.331  21.077  1.00120.09           C  
ANISOU  951  CB  ASP A 174    18078  15535  12017   1072    340   3009       C  
ATOM    952  CG  ASP A 174     -51.931  16.750  21.938  1.00134.31           C  
ANISOU  952  CG  ASP A 174    20071  17235  13725    883    464   3199       C  
ATOM    953  OD1 ASP A 174     -52.925  16.248  21.369  1.00135.70           O  
ANISOU  953  OD1 ASP A 174    20352  17164  14042    678    595   3155       O  
ATOM    954  OD2 ASP A 174     -51.846  16.879  23.178  1.00141.33           O  
ANISOU  954  OD2 ASP A 174    20990  18323  14387    918    430   3380       O  
ATOM    955  N   CYS A 175     -48.488  17.481  18.761  1.00115.88           N  
ANISOU  955  N   CYS A 175    17275  14949  11806   1517    175   2703       N  
ATOM    956  CA  CYS A 175     -47.747  18.237  17.751  1.00113.41           C  
ANISOU  956  CA  CYS A 175    16735  14775  11580   1587    115   2482       C  
ATOM    957  C   CYS A 175     -47.885  17.582  16.375  1.00115.86           C  
ANISOU  957  C   CYS A 175    17130  14781  12112   1603    206   2351       C  
ATOM    958  O   CYS A 175     -48.118  18.291  15.393  1.00113.62           O  
ANISOU  958  O   CYS A 175    16716  14550  11906   1480    230   2124       O  
ATOM    959  CB  CYS A 175     -46.281  18.400  18.146  1.00115.11           C  
ANISOU  959  CB  CYS A 175    16796  15227  11715   1867    -33   2563       C  
ATOM    960  SG  CYS A 175     -46.001  19.553  19.512  1.00118.97           S  
ANISOU  960  SG  CYS A 175    17115  16152  11934   1812   -173   2616       S  
ATOM    961  N   PHE A 176     -47.768  16.236  16.306  1.00113.27           N  
ANISOU  961  N   PHE A 176    17037  14127  11875   1752    257   2491       N  
ATOM    962  CA  PHE A 176     -47.896  15.483  15.056  1.00112.51           C  
ANISOU  962  CA  PHE A 176    17064  13708  11977   1778    345   2363       C  
ATOM    963  C   PHE A 176     -49.307  15.569  14.490  1.00111.96           C  
ANISOU  963  C   PHE A 176    17075  13485  11981   1439    455   2218       C  
ATOM    964  O   PHE A 176     -49.456  15.782  13.288  1.00109.94           O  
ANISOU  964  O   PHE A 176    16762  13175  11836   1375    491   1997       O  
ATOM    965  CB  PHE A 176     -47.466  14.023  15.235  1.00118.26           C  
ANISOU  965  CB  PHE A 176    18055  14097  12779   2022    371   2555       C  
ATOM    966  CG  PHE A 176     -45.990  13.849  15.505  1.00122.20           C  
ANISOU  966  CG  PHE A 176    18452  14736  13241   2408    263   2667       C  
ATOM    967  CD1 PHE A 176     -45.080  13.757  14.458  1.00125.70           C  
ANISOU  967  CD1 PHE A 176    18785  15179  13795   2633    256   2519       C  
ATOM    968  CD2 PHE A 176     -45.511  13.757  16.808  1.00126.92           C  
ANISOU  968  CD2 PHE A 176    19054  15489  13681   2553    169   2925       C  
ATOM    969  CE1 PHE A 176     -43.714  13.591  14.709  1.00128.81           C  
ANISOU  969  CE1 PHE A 176    19052  15735  14156   2998    160   2626       C  
ATOM    970  CE2 PHE A 176     -44.145  13.594  17.061  1.00131.92           C  
ANISOU  970  CE2 PHE A 176    19566  16282  14276   2917     56   3033       C  
ATOM    971  CZ  PHE A 176     -43.256  13.509  16.009  1.00130.12           C  
ANISOU  971  CZ  PHE A 176    19208  16059  14173   3140     54   2883       C  
ATOM    972  N   LEU A 177     -50.334  15.447  15.359  1.00106.98           N  
ANISOU  972  N   LEU A 177    16557  12818  11274   1222    507   2344       N  
ATOM    973  CA  LEU A 177     -51.753  15.536  14.986  1.00104.86           C  
ANISOU  973  CA  LEU A 177    16335  12450  11057    884    609   2232       C  
ATOM    974  C   LEU A 177     -52.129  16.941  14.512  1.00104.25           C  
ANISOU  974  C   LEU A 177    15996  12672  10943    727    584   2009       C  
ATOM    975  O   LEU A 177     -52.888  17.062  13.551  1.00103.09           O  
ANISOU  975  O   LEU A 177    15832  12442  10896    547    639   1827       O  
ATOM    976  CB  LEU A 177     -52.671  15.115  16.138  1.00106.43           C  
ANISOU  976  CB  LEU A 177    16683  12593  11160    706    675   2444       C  
ATOM    977  CG  LEU A 177     -52.391  13.773  16.788  1.00114.55           C  
ANISOU  977  CG  LEU A 177    17997  13326  12201    839    702   2713       C  
ATOM    978  CD1 LEU A 177     -52.749  13.815  18.237  1.00116.09           C  
ANISOU  978  CD1 LEU A 177    18239  13665  12205    768    713   2958       C  
ATOM    979  CD2 LEU A 177     -53.134  12.661  16.095  1.00118.20           C  
ANISOU  979  CD2 LEU A 177    18707  13362  12840    683    812   2689       C  
ATOM    980  N   ASP A 178     -51.594  17.996  15.175  1.00 98.11           N  
ANISOU  980  N   ASP A 178    15023  12233  10021    797    493   2020       N  
ATOM    981  CA  ASP A 178     -51.818  19.397  14.807  1.00 94.65           C  
ANISOU  981  CA  ASP A 178    14353  12067   9544    677    458   1823       C  
ATOM    982  C   ASP A 178     -51.252  19.685  13.422  1.00 96.70           C  
ANISOU  982  C   ASP A 178    14506  12309   9928    752    436   1624       C  
ATOM    983  O   ASP A 178     -51.876  20.416  12.651  1.00 94.18           O  
ANISOU  983  O   ASP A 178    14085  12051   9648    591    458   1443       O  
ATOM    984  CB  ASP A 178     -51.204  20.350  15.842  1.00 96.09           C  
ANISOU  984  CB  ASP A 178    14385  12578   9548    753    356   1880       C  
ATOM    985  CG  ASP A 178     -52.035  20.542  17.097  1.00108.23           C  
ANISOU  985  CG  ASP A 178    15970  14227  10925    613    389   1998       C  
ATOM    986  OD1 ASP A 178     -53.165  20.008  17.150  1.00109.60           O  
ANISOU  986  OD1 ASP A 178    16267  14245  11132    434    502   2036       O  
ATOM    987  OD2 ASP A 178     -51.553  21.227  18.031  1.00114.55           O  
ANISOU  987  OD2 ASP A 178    16680  15286  11559    675    304   2048       O  
ATOM    988  N   LEU A 179     -50.083  19.085  13.104  1.00 94.17           N  
ANISOU  988  N   LEU A 179    14209  11911   9661   1006    398   1666       N  
ATOM    989  CA  LEU A 179     -49.425  19.196  11.805  1.00 93.14           C  
ANISOU  989  CA  LEU A 179    13989  11763   9635   1110    393   1497       C  
ATOM    990  C   LEU A 179     -50.318  18.559  10.727  1.00 97.05           C  
ANISOU  990  C   LEU A 179    14630  11982  10262    968    492   1365       C  
ATOM    991  O   LEU A 179     -50.601  19.213   9.724  1.00 95.22           O  
ANISOU  991  O   LEU A 179    14289  11822  10068    862    503   1174       O  
ATOM    992  CB  LEU A 179     -48.038  18.526  11.846  1.00 95.16           C  
ANISOU  992  CB  LEU A 179    14251  11994   9912   1436    347   1595       C  
ATOM    993  CG  LEU A 179     -47.328  18.348  10.501  1.00 99.43           C  
ANISOU  993  CG  LEU A 179    14736  12479  10563   1581    372   1438       C  
ATOM    994  CD1 LEU A 179     -46.345  19.475  10.244  1.00 97.98           C  
ANISOU  994  CD1 LEU A 179    14264  12638  10327   1654    294   1358       C  
ATOM    995  CD2 LEU A 179     -46.644  16.998  10.430  1.00104.73           C  
ANISOU  995  CD2 LEU A 179    15582  12898  11311   1859    400   1538       C  
ATOM    996  N   ALA A 180     -50.790  17.304  10.964  1.00 95.00           N  
ANISOU  996  N   ALA A 180    14622  11410  10064    952    559   1471       N  
ATOM    997  CA  ALA A 180     -51.674  16.551  10.064  1.00 94.67           C  
ANISOU  997  CA  ALA A 180    14749  11076  10145    792    647   1355       C  
ATOM    998  C   ALA A 180     -52.966  17.317   9.846  1.00 95.24           C  
ANISOU  998  C   ALA A 180    14726  11265  10197    477    673   1237       C  
ATOM    999  O   ALA A 180     -53.408  17.445   8.705  1.00 93.20           O  
ANISOU  999  O   ALA A 180    14442  10963  10007    366    696   1043       O  
ATOM   1000  CB  ALA A 180     -51.962  15.173  10.635  1.00 98.41           C  
ANISOU 1000  CB  ALA A 180    15513  11207  10672    800    705   1528       C  
ATOM   1001  N   ARG A 181     -53.522  17.895  10.936  1.00 91.46           N  
ANISOU 1001  N   ARG A 181    14176  10965   9609    354    665   1348       N  
ATOM   1002  CA  ARG A 181     -54.727  18.723  10.911  1.00 89.77           C  
ANISOU 1002  CA  ARG A 181    13842  10907   9358     91    690   1254       C  
ATOM   1003  C   ARG A 181     -54.532  19.944  10.030  1.00 92.57           C  
ANISOU 1003  C   ARG A 181    13981  11484   9706     97    636   1059       C  
ATOM   1004  O   ARG A 181     -55.440  20.287   9.281  1.00 92.05           O  
ANISOU 1004  O   ARG A 181    13860  11436   9680    -82    660    915       O  
ATOM   1005  CB  ARG A 181     -55.130  19.158  12.320  1.00 88.90           C  
ANISOU 1005  CB  ARG A 181    13692  10977   9110     24    693   1410       C  
ATOM   1006  CG  ARG A 181     -56.053  18.172  12.985  1.00 98.58           C  
ANISOU 1006  CG  ARG A 181    15099  12015  10342   -142    785   1561       C  
ATOM   1007  CD  ARG A 181     -56.605  18.741  14.258  1.00105.23           C  
ANISOU 1007  CD  ARG A 181    15872  13083  11027   -234    806   1682       C  
ATOM   1008  NE  ARG A 181     -55.743  18.438  15.395  1.00114.41           N  
ANISOU 1008  NE  ARG A 181    17117  14278  12074    -48    767   1897       N  
ATOM   1009  CZ  ARG A 181     -56.041  17.560  16.343  1.00132.44           C  
ANISOU 1009  CZ  ARG A 181    19578  16439  14302    -90    828   2123       C  
ATOM   1010  NH1 ARG A 181     -55.203  17.347  17.349  1.00123.99           N  
ANISOU 1010  NH1 ARG A 181    18573  15428  13109    101    775   2321       N  
ATOM   1011  NH2 ARG A 181     -57.186  16.890  16.302  1.00119.27           N  
ANISOU 1011  NH2 ARG A 181    18021  14603  12695   -335    941   2161       N  
ATOM   1012  N   ASN A 182     -53.340  20.572  10.080  1.00 87.99           N  
ANISOU 1012  N   ASN A 182    13282  11073   9079    297    560   1059       N  
ATOM   1013  CA  ASN A 182     -53.030  21.747   9.269  1.00 85.18           C  
ANISOU 1013  CA  ASN A 182    12733  10918   8714    302    510    898       C  
ATOM   1014  C   ASN A 182     -52.765  21.414   7.787  1.00 87.77           C  
ANISOU 1014  C   ASN A 182    13079  11127   9141    343    531    743       C  
ATOM   1015  O   ASN A 182     -53.061  22.255   6.939  1.00 86.00           O  
ANISOU 1015  O   ASN A 182    12737  11019   8918    257    518    599       O  
ATOM   1016  CB  ASN A 182     -51.906  22.562   9.890  1.00 85.34           C  
ANISOU 1016  CB  ASN A 182    12610  11170   8644    455    424    955       C  
ATOM   1017  CG  ASN A 182     -52.379  23.361  11.082  1.00111.12           C  
ANISOU 1017  CG  ASN A 182    15813  14619  11788    360    395   1020       C  
ATOM   1018  OD1 ASN A 182     -53.439  23.999  11.058  1.00104.21           O  
ANISOU 1018  OD1 ASN A 182    14895  13806  10895    184    423    943       O  
ATOM   1019  ND2 ASN A 182     -51.603  23.345  12.153  1.00105.82           N  
ANISOU 1019  ND2 ASN A 182    15133  14053  11021    485    336   1157       N  
ATOM   1020  N   ILE A 183     -52.273  20.187   7.468  1.00 84.78           N  
ANISOU 1020  N   ILE A 183    12864  10512   8838    476    568    771       N  
ATOM   1021  CA  ILE A 183     -52.054  19.733   6.083  1.00 84.25           C  
ANISOU 1021  CA  ILE A 183    12847  10313   8851    524    601    611       C  
ATOM   1022  C   ILE A 183     -53.418  19.680   5.381  1.00 87.40           C  
ANISOU 1022  C   ILE A 183    13295  10626   9288    263    639    477       C  
ATOM   1023  O   ILE A 183     -53.498  19.962   4.186  1.00 86.74           O  
ANISOU 1023  O   ILE A 183    13163  10575   9220    229    639    308       O  
ATOM   1024  CB  ILE A 183     -51.301  18.369   6.024  1.00 89.61           C  
ANISOU 1024  CB  ILE A 183    13719  10726   9601    737    638    669       C  
ATOM   1025  CG1 ILE A 183     -49.873  18.517   6.537  1.00 90.78           C  
ANISOU 1025  CG1 ILE A 183    13765  11018   9709   1021    589    781       C  
ATOM   1026  CG2 ILE A 183     -51.278  17.775   4.614  1.00 90.31           C  
ANISOU 1026  CG2 ILE A 183    13906  10642   9766    762    689    478       C  
ATOM   1027  CD1 ILE A 183     -49.332  17.331   7.278  1.00105.49           C  
ANISOU 1027  CD1 ILE A 183    15808  12668  11604   1224    600    953       C  
ATOM   1028  N   PHE A 184     -54.492  19.392   6.151  1.00 83.44           N  
ANISOU 1028  N   PHE A 184    12867  10051   8786     73    666    561       N  
ATOM   1029  CA  PHE A 184     -55.869  19.296   5.669  1.00 82.77           C  
ANISOU 1029  CA  PHE A 184    12802   9911   8734   -194    698    459       C  
ATOM   1030  C   PHE A 184     -56.776  20.338   6.352  1.00 86.39           C  
ANISOU 1030  C   PHE A 184    13097  10609   9120   -355    684    494       C  
ATOM   1031  O   PHE A 184     -57.532  19.973   7.248  1.00 87.15           O  
ANISOU 1031  O   PHE A 184    13246  10662   9203   -487    726    606       O  
ATOM   1032  CB  PHE A 184     -56.390  17.862   5.867  1.00 86.82           C  
ANISOU 1032  CB  PHE A 184    13559  10097   9330   -296    763    515       C  
ATOM   1033  CG  PHE A 184     -55.539  16.804   5.201  1.00 89.94           C  
ANISOU 1033  CG  PHE A 184    14146  10224   9804   -120    783    464       C  
ATOM   1034  CD1 PHE A 184     -55.732  16.471   3.868  1.00 92.98           C  
ANISOU 1034  CD1 PHE A 184    14589  10497  10241   -176    792    254       C  
ATOM   1035  CD2 PHE A 184     -54.539  16.146   5.906  1.00 93.54           C  
ANISOU 1035  CD2 PHE A 184    14724  10545  10271    119    791    622       C  
ATOM   1036  CE1 PHE A 184     -54.937  15.503   3.251  1.00 95.71           C  
ANISOU 1036  CE1 PHE A 184    15122  10592  10651      6    822    187       C  
ATOM   1037  CE2 PHE A 184     -53.747  15.175   5.288  1.00 98.01           C  
ANISOU 1037  CE2 PHE A 184    15468  10859  10914    316    816    568       C  
ATOM   1038  CZ  PHE A 184     -53.953  14.858   3.966  1.00 96.36           C  
ANISOU 1038  CZ  PHE A 184    15323  10531  10757    259    838    343       C  
ATOM   1039  N   PRO A 185     -56.719  21.640   5.971  1.00 82.33           N  
ANISOU 1039  N   PRO A 185    12387  10343   8551   -341    632    405       N  
ATOM   1040  CA  PRO A 185     -57.564  22.648   6.651  1.00 81.57           C  
ANISOU 1040  CA  PRO A 185    12147  10459   8385   -461    622    429       C  
ATOM   1041  C   PRO A 185     -59.064  22.440   6.450  1.00 86.72           C  
ANISOU 1041  C   PRO A 185    12787  11096   9067   -703    664    374       C  
ATOM   1042  O   PRO A 185     -59.490  22.146   5.334  1.00 87.41           O  
ANISOU 1042  O   PRO A 185    12888  11112   9210   -791    659    242       O  
ATOM   1043  CB  PRO A 185     -57.110  23.972   6.024  1.00 81.34           C  
ANISOU 1043  CB  PRO A 185    11954  10636   8317   -383    557    328       C  
ATOM   1044  CG  PRO A 185     -56.546  23.585   4.691  1.00 85.61           C  
ANISOU 1044  CG  PRO A 185    12538  11080   8912   -317    549    213       C  
ATOM   1045  CD  PRO A 185     -55.874  22.268   4.933  1.00 82.84           C  
ANISOU 1045  CD  PRO A 185    12362  10504   8610   -212    587    287       C  
ATOM   1046  N   SER A 186     -59.861  22.606   7.517  1.00 82.88           N  
ANISOU 1046  N   SER A 186    12259  10699   8532   -811    705    471       N  
ATOM   1047  CA  SER A 186     -61.314  22.440   7.446  1.00 83.10           C  
ANISOU 1047  CA  SER A 186    12234  10758   8582  -1047    752    434       C  
ATOM   1048  C   SER A 186     -62.013  23.633   6.787  1.00 85.67           C  
ANISOU 1048  C   SER A 186    12357  11308   8885  -1090    708    297       C  
ATOM   1049  O   SER A 186     -63.167  23.501   6.385  1.00 86.15           O  
ANISOU 1049  O   SER A 186    12347  11411   8977  -1271    726    231       O  
ATOM   1050  CB  SER A 186     -61.894  22.186   8.831  1.00 87.16           C  
ANISOU 1050  CB  SER A 186    12765  11313   9040  -1137    828    594       C  
ATOM   1051  OG  SER A 186     -61.615  23.270   9.701  1.00 93.07           O  
ANISOU 1051  OG  SER A 186    13404  12282   9677  -1020    810    639       O  
ATOM   1052  N   ASN A 187     -61.329  24.799   6.701  1.00 80.53           N  
ANISOU 1052  N   ASN A 187    11613  10805   8181   -928    646    262       N  
ATOM   1053  CA  ASN A 187     -61.853  26.037   6.110  1.00 79.07           C  
ANISOU 1053  CA  ASN A 187    11259  10812   7971   -927    597    152       C  
ATOM   1054  C   ASN A 187     -60.720  26.823   5.476  1.00 82.39           C  
ANISOU 1054  C   ASN A 187    11664  11265   8377   -760    526    102       C  
ATOM   1055  O   ASN A 187     -59.777  27.200   6.173  1.00 81.02           O  
ANISOU 1055  O   ASN A 187    11507  11117   8159   -635    510    171       O  
ATOM   1056  CB  ASN A 187     -62.563  26.892   7.156  1.00 77.74           C  
ANISOU 1056  CB  ASN A 187    10975  10832   7731   -942    626    196       C  
ATOM   1057  CG  ASN A 187     -63.413  27.976   6.558  1.00 90.24           C  
ANISOU 1057  CG  ASN A 187    12393  12588   9304   -957    590     90       C  
ATOM   1058  OD1 ASN A 187     -62.934  29.065   6.225  1.00 79.48           O  
ANISOU 1058  OD1 ASN A 187    10982  11301   7917   -834    528     41       O  
ATOM   1059  ND2 ASN A 187     -64.697  27.691   6.409  1.00 82.48           N  
ANISOU 1059  ND2 ASN A 187    11319  11673   8344  -1110    626     61       N  
ATOM   1060  N   LEU A 188     -60.821  27.068   4.152  1.00 79.42           N  
ANISOU 1060  N   LEU A 188    11250  10901   8027   -771    481    -14       N  
ATOM   1061  CA  LEU A 188     -59.814  27.762   3.346  1.00 78.18           C  
ANISOU 1061  CA  LEU A 188    11074  10778   7853   -641    425    -62       C  
ATOM   1062  C   LEU A 188     -59.677  29.241   3.653  1.00 81.66           C  
ANISOU 1062  C   LEU A 188    11408  11378   8242   -570    382    -55       C  
ATOM   1063  O   LEU A 188     -58.560  29.760   3.601  1.00 80.94           O  
ANISOU 1063  O   LEU A 188    11319  11303   8131   -462    351    -36       O  
ATOM   1064  CB  LEU A 188     -60.067  27.542   1.858  1.00 78.44           C  
ANISOU 1064  CB  LEU A 188    11109  10790   7905   -688    398   -181       C  
ATOM   1065  CG  LEU A 188     -59.938  26.109   1.373  1.00 84.79           C  
ANISOU 1065  CG  LEU A 188    12052  11405   8759   -738    433   -222       C  
ATOM   1066  CD1 LEU A 188     -60.679  25.914   0.063  1.00 85.54           C  
ANISOU 1066  CD1 LEU A 188    12132  11517   8853   -844    400   -360       C  
ATOM   1067  CD2 LEU A 188     -58.474  25.703   1.257  1.00 87.65           C  
ANISOU 1067  CD2 LEU A 188    12509  11665   9128   -575    447   -196       C  
ATOM   1068  N   VAL A 189     -60.803  29.921   3.968  1.00 78.38           N  
ANISOU 1068  N   VAL A 189    10897  11077   7806   -629    381    -72       N  
ATOM   1069  CA  VAL A 189     -60.830  31.343   4.332  1.00 77.45           C  
ANISOU 1069  CA  VAL A 189    10701  11083   7645   -557    346    -77       C  
ATOM   1070  C   VAL A 189     -60.118  31.507   5.680  1.00 83.69           C  
ANISOU 1070  C   VAL A 189    11532  11878   8390   -494    362      2       C  
ATOM   1071  O   VAL A 189     -59.266  32.389   5.806  1.00 83.39           O  
ANISOU 1071  O   VAL A 189    11490  11870   8324   -413    316      2       O  
ATOM   1072  CB  VAL A 189     -62.263  31.948   4.315  1.00 80.90           C  
ANISOU 1072  CB  VAL A 189    11024  11641   8074   -607    349   -121       C  
ATOM   1073  CG1 VAL A 189     -62.271  33.411   4.752  1.00 79.93           C  
ANISOU 1073  CG1 VAL A 189    10850  11610   7910   -508    319   -133       C  
ATOM   1074  CG2 VAL A 189     -62.874  31.824   2.933  1.00 80.78           C  
ANISOU 1074  CG2 VAL A 189    10959  11647   8086   -662    310   -196       C  
ATOM   1075  N   SER A 190     -60.416  30.629   6.662  1.00 81.79           N  
ANISOU 1075  N   SER A 190    11335  11606   8134   -542    423     72       N  
ATOM   1076  CA  SER A 190     -59.748  30.699   7.961  1.00 82.07           C  
ANISOU 1076  CA  SER A 190    11416  11665   8103   -481    431    155       C  
ATOM   1077  C   SER A 190     -58.270  30.301   7.854  1.00 86.38           C  
ANISOU 1077  C   SER A 190    12030  12133   8658   -391    392    203       C  
ATOM   1078  O   SER A 190     -57.440  30.943   8.493  1.00 86.52           O  
ANISOU 1078  O   SER A 190    12040  12216   8619   -316    347    227       O  
ATOM   1079  CB  SER A 190     -60.502  29.918   9.039  1.00 86.72           C  
ANISOU 1079  CB  SER A 190    12035  12260   8654   -557    513    237       C  
ATOM   1080  OG  SER A 190     -60.151  28.547   9.116  1.00 96.31           O  
ANISOU 1080  OG  SER A 190    13360  13328   9904   -587    548    324       O  
ATOM   1081  N   ALA A 191     -57.933  29.320   6.975  1.00 82.53           N  
ANISOU 1081  N   ALA A 191    11599  11520   8239   -393    402    199       N  
ATOM   1082  CA  ALA A 191     -56.558  28.847   6.734  1.00 82.06           C  
ANISOU 1082  CA  ALA A 191    11588  11393   8196   -282    377    237       C  
ATOM   1083  C   ALA A 191     -55.635  29.974   6.294  1.00 83.59           C  
ANISOU 1083  C   ALA A 191    11701  11688   8371   -212    312    194       C  
ATOM   1084  O   ALA A 191     -54.431  29.914   6.528  1.00 83.12           O  
ANISOU 1084  O   ALA A 191    11635  11648   8297   -117    281    242       O  
ATOM   1085  CB  ALA A 191     -56.555  27.747   5.684  1.00 83.51           C  
ANISOU 1085  CB  ALA A 191    11846  11428   8455   -294    409    198       C  
ATOM   1086  N   ALA A 192     -56.207  31.006   5.678  1.00 78.95           N  
ANISOU 1086  N   ALA A 192    11047  11167   7783   -260    289    114       N  
ATOM   1087  CA  ALA A 192     -55.480  32.171   5.195  1.00 77.79           C  
ANISOU 1087  CA  ALA A 192    10838  11097   7624   -226    233     80       C  
ATOM   1088  C   ALA A 192     -54.928  33.086   6.313  1.00 80.01           C  
ANISOU 1088  C   ALA A 192    11092  11462   7845   -202    186    110       C  
ATOM   1089  O   ALA A 192     -54.062  33.912   6.028  1.00 79.27           O  
ANISOU 1089  O   ALA A 192    10955  11418   7746   -187    136     98       O  
ATOM   1090  CB  ALA A 192     -56.362  32.962   4.242  1.00 77.97           C  
ANISOU 1090  CB  ALA A 192    10820  11144   7660   -279    221      3       C  
ATOM   1091  N   PHE A 193     -55.406  32.943   7.566  1.00 75.75           N  
ANISOU 1091  N   PHE A 193    10580  10947   7253   -211    202    146       N  
ATOM   1092  CA  PHE A 193     -54.956  33.790   8.676  1.00 75.45           C  
ANISOU 1092  CA  PHE A 193    10533  10999   7137   -194    153    154       C  
ATOM   1093  C   PHE A 193     -54.885  33.071  10.045  1.00 81.31           C  
ANISOU 1093  C   PHE A 193    11322  11772   7799   -168    169    240       C  
ATOM   1094  O   PHE A 193     -54.600  33.724  11.051  1.00 81.51           O  
ANISOU 1094  O   PHE A 193    11347  11888   7735   -158    127    237       O  
ATOM   1095  CB  PHE A 193     -55.829  35.065   8.761  1.00 76.53           C  
ANISOU 1095  CB  PHE A 193    10652  11173   7253   -229    144     68       C  
ATOM   1096  CG  PHE A 193     -57.222  34.838   9.302  1.00 78.07           C  
ANISOU 1096  CG  PHE A 193    10855  11386   7421   -254    212     57       C  
ATOM   1097  CD1 PHE A 193     -58.241  34.379   8.476  1.00 80.73           C  
ANISOU 1097  CD1 PHE A 193    11165  11686   7820   -295    261     37       C  
ATOM   1098  CD2 PHE A 193     -57.513  35.077  10.641  1.00 80.52           C  
ANISOU 1098  CD2 PHE A 193    11188  11772   7633   -244    229     63       C  
ATOM   1099  CE1 PHE A 193     -59.520  34.152   8.986  1.00 82.29           C  
ANISOU 1099  CE1 PHE A 193    11340  11931   7995   -333    329     32       C  
ATOM   1100  CE2 PHE A 193     -58.793  34.850  11.149  1.00 83.71           C  
ANISOU 1100  CE2 PHE A 193    11579  12222   8004   -270    310     60       C  
ATOM   1101  CZ  PHE A 193     -59.778  34.369  10.325  1.00 81.86           C  
ANISOU 1101  CZ  PHE A 193    11300  11957   7846   -319    361     50       C  
ATOM   1102  N   ARG A 194     -55.149  31.749  10.088  1.00 78.90           N  
ANISOU 1102  N   ARG A 194    11072  11388   7520   -162    228    317       N  
ATOM   1103  CA  ARG A 194     -55.147  30.945  11.317  1.00 79.94           C  
ANISOU 1103  CA  ARG A 194    11270  11530   7574   -140    254    429       C  
ATOM   1104  C   ARG A 194     -54.575  29.553  11.095  1.00 85.74           C  
ANISOU 1104  C   ARG A 194    12073  12143   8360    -79    275    529       C  
ATOM   1105  O   ARG A 194     -54.752  28.982  10.021  1.00 85.57           O  
ANISOU 1105  O   ARG A 194    12071  12004   8439    -95    309    495       O  
ATOM   1106  CB  ARG A 194     -56.577  30.758  11.816  1.00 80.67           C  
ANISOU 1106  CB  ARG A 194    11387  11628   7637   -226    339    432       C  
ATOM   1107  CG  ARG A 194     -57.182  31.914  12.562  1.00 93.76           C  
ANISOU 1107  CG  ARG A 194    13003  13419   9201   -247    338    364       C  
ATOM   1108  CD  ARG A 194     -58.522  31.436  13.058  1.00107.58           C  
ANISOU 1108  CD  ARG A 194    14763  15190  10923   -324    443    394       C  
ATOM   1109  NE  ARG A 194     -59.360  32.510  13.575  1.00122.39           N  
ANISOU 1109  NE  ARG A 194    16583  17193  12726   -331    469    305       N  
ATOM   1110  CZ  ARG A 194     -60.687  32.485  13.557  1.00140.90           C  
ANISOU 1110  CZ  ARG A 194    18872  19585  15079   -394    556    278       C  
ATOM   1111  NH1 ARG A 194     -61.332  31.449  13.026  1.00124.89           N  
ANISOU 1111  NH1 ARG A 194    16837  17484  13132   -487    617    330       N  
ATOM   1112  NH2 ARG A 194     -61.384  33.496  14.058  1.00133.30           N  
ANISOU 1112  NH2 ARG A 194    17856  18746  14046   -365    583    191       N  
ATOM   1113  N   SER A 195     -53.955  28.982  12.138  1.00 84.47           N  
ANISOU 1113  N   SER A 195    11964  12008   8124     -4    255    653       N  
ATOM   1114  CA  SER A 195     -53.409  27.618  12.156  1.00 86.22           C  
ANISOU 1114  CA  SER A 195    12277  12101   8384     85    275    775       C  
ATOM   1115  C   SER A 195     -54.013  26.869  13.350  1.00 92.80           C  
ANISOU 1115  C   SER A 195    13219  12906   9134     57    328    914       C  
ATOM   1116  O   SER A 195     -54.467  27.512  14.298  1.00 92.62           O  
ANISOU 1116  O   SER A 195    13175  13023   8993      6    328    919       O  
ATOM   1117  CB  SER A 195     -51.887  27.645  12.264  1.00 90.41           C  
ANISOU 1117  CB  SER A 195    12752  12707   8893    237    185    822       C  
ATOM   1118  OG  SER A 195     -51.294  28.247  11.125  1.00 97.50           O  
ANISOU 1118  OG  SER A 195    13547  13633   9865    253    154    712       O  
ATOM   1119  N   TYR A 196     -54.045  25.526  13.308  1.00 91.66           N  
ANISOU 1119  N   TYR A 196    13203  12578   9045     87    381   1026       N  
ATOM   1120  CA  TYR A 196     -54.615  24.736  14.404  1.00 93.76           C  
ANISOU 1120  CA  TYR A 196    13592  12798   9235     45    442   1186       C  
ATOM   1121  C   TYR A 196     -53.595  24.503  15.505  1.00102.25           C  
ANISOU 1121  C   TYR A 196    14703  13960  10187    199    372   1343       C  
ATOM   1122  O   TYR A 196     -52.433  24.202  15.220  1.00102.81           O  
ANISOU 1122  O   TYR A 196    14763  14006  10295    363    303   1376       O  
ATOM   1123  CB  TYR A 196     -55.145  23.384  13.898  1.00 95.55           C  
ANISOU 1123  CB  TYR A 196    13968  12757   9579    -13    530   1246       C  
ATOM   1124  CG  TYR A 196     -56.109  22.702  14.845  1.00 98.12           C  
ANISOU 1124  CG  TYR A 196    14408  13031   9844   -139    623   1390       C  
ATOM   1125  CD1 TYR A 196     -57.484  22.797  14.654  1.00 99.70           C  
ANISOU 1125  CD1 TYR A 196    14578  13232  10071   -350    713   1326       C  
ATOM   1126  CD2 TYR A 196     -55.653  21.916  15.894  1.00100.98           C  
ANISOU 1126  CD2 TYR A 196    14903  13346  10120    -49    625   1603       C  
ATOM   1127  CE1 TYR A 196     -58.379  22.156  15.510  1.00102.05           C  
ANISOU 1127  CE1 TYR A 196    14964  13500  10311   -488    813   1466       C  
ATOM   1128  CE2 TYR A 196     -56.536  21.297  16.774  1.00103.80           C  
ANISOU 1128  CE2 TYR A 196    15371  13662  10408   -180    722   1755       C  
ATOM   1129  CZ  TYR A 196     -57.901  21.401  16.565  1.00111.24           C  
ANISOU 1129  CZ  TYR A 196    16273  14611  11382   -409    823   1685       C  
ATOM   1130  OH  TYR A 196     -58.775  20.759  17.404  1.00115.93           O  
ANISOU 1130  OH  TYR A 196    16962  15175  11910   -558    933   1843       O  
ATOM   1131  N   SER A 197     -54.038  24.606  16.765  1.00101.64           N  
ANISOU 1131  N   SER A 197    14663  14001   9953    155    392   1444       N  
ATOM   1132  CA  SER A 197     -53.193  24.331  17.925  1.00104.19           C  
ANISOU 1132  CA  SER A 197    15033  14426  10127    291    322   1613       C  
ATOM   1133  C   SER A 197     -54.011  23.798  19.105  1.00110.43           C  
ANISOU 1133  C   SER A 197    15948  15231  10779    212    406   1779       C  
ATOM   1134  O   SER A 197     -54.760  24.549  19.735  1.00109.98           O  
ANISOU 1134  O   SER A 197    15844  15346  10599    104    444   1725       O  
ATOM   1135  CB  SER A 197     -52.360  25.547  18.317  1.00108.53           C  
ANISOU 1135  CB  SER A 197    15439  15235  10564    354    196   1522       C  
ATOM   1136  OG  SER A 197     -51.370  25.156  19.254  1.00123.48           O  
ANISOU 1136  OG  SER A 197    17361  17228  12327    507    104   1684       O  
ATOM   1137  N   THR A 198     -53.869  22.489  19.391  1.00108.78           N  
ANISOU 1137  N   THR A 198    15907  14836  10589    272    444   1986       N  
ATOM   1138  CA  THR A 198     -54.600  21.815  20.465  1.00127.36           C  
ANISOU 1138  CA  THR A 198    18403  17173  12816    189    537   2184       C  
ATOM   1139  C   THR A 198     -53.914  22.027  21.820  1.00143.45           C  
ANISOU 1139  C   THR A 198    20453  19440  14611    314    451   2329       C  
ATOM   1140  O   THR A 198     -53.309  23.072  22.054  1.00102.23           O  
ANISOU 1140  O   THR A 198    15094  14456   9293    377    342   2211       O  
ATOM   1141  CB  THR A 198     -54.850  20.343  20.097  1.00135.10           C  
ANISOU 1141  CB  THR A 198    19582  17816  13936    168    622   2338       C  
ATOM   1142  OG1 THR A 198     -56.007  19.870  20.777  1.00135.74           O  
ANISOU 1142  OG1 THR A 198    19766  17863  13946    -23    756   2466       O  
ATOM   1143  CG2 THR A 198     -53.659  19.443  20.369  1.00134.80           C  
ANISOU 1143  CG2 THR A 198    19668  17654  13894    409    541   2528       C  
ATOM   1144  N   GLN A 216     -58.946  26.533  19.993  1.00116.54           N  
ANISOU 1144  N   GLN A 216    16452  16492  11336   -383    775   1385       N  
ATOM   1145  CA  GLN A 216     -58.246  25.434  19.331  1.00116.48           C  
ANISOU 1145  CA  GLN A 216    16541  16243  11471   -341    739   1488       C  
ATOM   1146  C   GLN A 216     -57.533  25.834  18.033  1.00117.15           C  
ANISOU 1146  C   GLN A 216    16553  16236  11723   -270    642   1335       C  
ATOM   1147  O   GLN A 216     -56.684  25.076  17.557  1.00116.64           O  
ANISOU 1147  O   GLN A 216    16558  16011  11749   -180    593   1402       O  
ATOM   1148  CB  GLN A 216     -59.187  24.257  19.088  1.00119.45           C  
ANISOU 1148  CB  GLN A 216    17005  16438  11944   -496    869   1596       C  
ATOM   1149  CG  GLN A 216     -59.503  23.471  20.339  1.00145.61           C  
ANISOU 1149  CG  GLN A 216    20446  19774  15105   -542    956   1828       C  
ATOM   1150  CD  GLN A 216     -60.828  22.784  20.189  1.00177.70           C  
ANISOU 1150  CD  GLN A 216    24519  23779  19222   -768   1113   1875       C  
ATOM   1151  OE1 GLN A 216     -61.875  23.416  19.974  1.00174.59           O  
ANISOU 1151  OE1 GLN A 216    23975  23491  18871   -885   1171   1721       O  
ATOM   1152  NE2 GLN A 216     -60.824  21.471  20.351  1.00175.82           N  
ANISOU 1152  NE2 GLN A 216    24450  23387  18966   -838   1188   2102       N  
ATOM   1153  N   GLU A 217     -57.886  27.006  17.456  1.00111.54           N  
ANISOU 1153  N   GLU A 217    15709  15624  11048   -301    621   1138       N  
ATOM   1154  CA  GLU A 217     -57.266  27.550  16.243  1.00109.25           C  
ANISOU 1154  CA  GLU A 217    15342  15276  10890   -248    536    995       C  
ATOM   1155  C   GLU A 217     -56.582  28.895  16.534  1.00111.41           C  
ANISOU 1155  C   GLU A 217    15531  15723  11078   -173    434    885       C  
ATOM   1156  O   GLU A 217     -57.242  29.940  16.583  1.00110.72           O  
ANISOU 1156  O   GLU A 217    15372  15739  10956   -218    448    757       O  
ATOM   1157  CB  GLU A 217     -58.262  27.645  15.072  1.00109.53           C  
ANISOU 1157  CB  GLU A 217    15315  15233  11069   -361    593    873       C  
ATOM   1158  CG  GLU A 217     -58.113  26.510  14.072  1.00121.66           C  
ANISOU 1158  CG  GLU A 217    16923  16544  12756   -382    609    904       C  
ATOM   1159  CD  GLU A 217     -59.044  26.503  12.870  1.00147.83           C  
ANISOU 1159  CD  GLU A 217    20182  19789  16199   -501    647    781       C  
ATOM   1160  OE1 GLU A 217     -59.671  27.550  12.584  1.00150.94           O  
ANISOU 1160  OE1 GLU A 217    20454  20312  16584   -537    641    658       O  
ATOM   1161  OE2 GLU A 217     -59.117  25.455  12.185  1.00139.54           O  
ANISOU 1161  OE2 GLU A 217    19215  18550  15254   -549    675    801       O  
ATOM   1162  N   VAL A 218     -55.252  28.844  16.755  1.00106.80           N  
ANISOU 1162  N   VAL A 218    14956  15165  10459    -56    328    937       N  
ATOM   1163  CA  VAL A 218     -54.386  29.987  17.052  1.00105.47           C  
ANISOU 1163  CA  VAL A 218    14712  15150  10212     -3    213    846       C  
ATOM   1164  C   VAL A 218     -54.266  30.935  15.842  1.00106.41           C  
ANISOU 1164  C   VAL A 218    14736  15236  10458    -32    175    680       C  
ATOM   1165  O   VAL A 218     -54.512  30.508  14.713  1.00105.55           O  
ANISOU 1165  O   VAL A 218    14618  14991  10493    -53    217    658       O  
ATOM   1166  CB  VAL A 218     -53.017  29.487  17.588  1.00110.66           C  
ANISOU 1166  CB  VAL A 218    15383  15859  10803    121    110    970       C  
ATOM   1167  CG1 VAL A 218     -52.052  29.111  16.461  1.00109.80           C  
ANISOU 1167  CG1 VAL A 218    15224  15649  10848    200     62    968       C  
ATOM   1168  CG2 VAL A 218     -52.392  30.496  18.542  1.00111.22           C  
ANISOU 1168  CG2 VAL A 218    15407  16143  10708    139      1    917       C  
ATOM   1169  N   GLU A 219     -53.917  32.216  16.070  1.00101.63           N  
ANISOU 1169  N   GLU A 219    14075  14748   9793    -41     99    563       N  
ATOM   1170  CA  GLU A 219     -53.774  33.179  14.970  1.00 99.73           C  
ANISOU 1170  CA  GLU A 219    13761  14467   9663    -74     63    426       C  
ATOM   1171  C   GLU A 219     -52.471  32.959  14.217  1.00102.88           C  
ANISOU 1171  C   GLU A 219    14102  14844  10145    -22    -12    455       C  
ATOM   1172  O   GLU A 219     -51.547  32.339  14.741  1.00103.46           O  
ANISOU 1172  O   GLU A 219    14172  14971  10167     54    -64    558       O  
ATOM   1173  CB  GLU A 219     -53.913  34.639  15.442  1.00101.15           C  
ANISOU 1173  CB  GLU A 219    13927  14740   9765   -113     15    289       C  
ATOM   1174  CG  GLU A 219     -55.304  35.019  15.943  1.00113.36           C  
ANISOU 1174  CG  GLU A 219    15508  16311  11250   -142    106    226       C  
ATOM   1175  CD  GLU A 219     -56.452  34.943  14.950  1.00131.59           C  
ANISOU 1175  CD  GLU A 219    17789  18525  13684   -176    196    186       C  
ATOM   1176  OE1 GLU A 219     -56.266  35.365  13.785  1.00120.61           O  
ANISOU 1176  OE1 GLU A 219    16357  17054  12415   -187    165    129       O  
ATOM   1177  OE2 GLU A 219     -57.551  34.494  15.352  1.00125.04           O  
ANISOU 1177  OE2 GLU A 219    16969  17722  12819   -198    297    215       O  
ATOM   1178  N   GLY A 220     -52.426  33.431  12.983  1.00 98.73           N  
ANISOU 1178  N   GLY A 220    13525  14251   9738    -53    -10    374       N  
ATOM   1179  CA  GLY A 220     -51.268  33.261  12.114  1.00 98.76           C  
ANISOU 1179  CA  GLY A 220    13457  14247   9820    -10    -56    392       C  
ATOM   1180  C   GLY A 220     -51.537  32.266  11.002  1.00101.87           C  
ANISOU 1180  C   GLY A 220    13873  14505  10330     21     20    418       C  
ATOM   1181  O   GLY A 220     -51.877  31.111  11.270  1.00102.32           O  
ANISOU 1181  O   GLY A 220    14004  14481  10390     62     75    501       O  
ATOM   1182  N   MET A 221     -51.383  32.725   9.749  1.00 96.62           N  
ANISOU 1182  N   MET A 221    13156  13807   9750     -7     24    345       N  
ATOM   1183  CA  MET A 221     -51.613  31.991   8.503  1.00 95.99           C  
ANISOU 1183  CA  MET A 221    13092  13614   9765     10     88    330       C  
ATOM   1184  C   MET A 221     -51.090  30.552   8.492  1.00 99.20           C  
ANISOU 1184  C   MET A 221    13546  13945  10201    119    121    417       C  
ATOM   1185  O   MET A 221     -49.967  30.305   8.921  1.00100.15           O  
ANISOU 1185  O   MET A 221    13621  14137  10295    217     74    485       O  
ATOM   1186  CB  MET A 221     -51.012  32.793   7.344  1.00 98.09           C  
ANISOU 1186  CB  MET A 221    13276  13917  10076    -12     65    265       C  
ATOM   1187  CG  MET A 221     -51.197  32.179   5.990  1.00102.04           C  
ANISOU 1187  CG  MET A 221    13792  14330  10647      4    125    231       C  
ATOM   1188  SD  MET A 221     -50.452  33.289   4.795  1.00106.52           S  
ANISOU 1188  SD  MET A 221    14263  14978  11232    -34    100    180       S  
ATOM   1189  CE  MET A 221     -50.159  32.169   3.443  1.00103.71           C  
ANISOU 1189  CE  MET A 221    13921  14562  10923     46    174    160       C  
ATOM   1190  N   ASN A 222     -51.918  29.614   8.000  1.00 94.01           N  
ANISOU 1190  N   ASN A 222    12979  13141   9601    101    195    411       N  
ATOM   1191  CA  ASN A 222     -51.594  28.194   7.842  1.00 93.89           C  
ANISOU 1191  CA  ASN A 222    13049  12991   9632    198    239    475       C  
ATOM   1192  C   ASN A 222     -50.957  28.029   6.446  1.00 95.62           C  
ANISOU 1192  C   ASN A 222    13232  13181   9917    257    258    402       C  
ATOM   1193  O   ASN A 222     -51.640  27.661   5.487  1.00 95.30           O  
ANISOU 1193  O   ASN A 222    13246  13035   9928    203    308    323       O  
ATOM   1194  CB  ASN A 222     -52.878  27.350   8.018  1.00 92.44           C  
ANISOU 1194  CB  ASN A 222    12992  12657   9474    108    311    491       C  
ATOM   1195  CG  ASN A 222     -52.798  25.865   7.753  1.00102.94           C  
ANISOU 1195  CG  ASN A 222    14455  13787  10870    170    366    539       C  
ATOM   1196  OD1 ASN A 222     -51.737  25.282   7.502  1.00 94.91           O  
ANISOU 1196  OD1 ASN A 222    13454  12727   9880    324    359    572       O  
ATOM   1197  ND2 ASN A 222     -53.950  25.218   7.804  1.00 93.02           N  
ANISOU 1197  ND2 ASN A 222    13299  12400   9644     48    427    540       N  
ATOM   1198  N   ILE A 223     -49.650  28.354   6.331  1.00 90.61           N  
ANISOU 1198  N   ILE A 223    12491  12668   9270    361    215    422       N  
ATOM   1199  CA  ILE A 223     -48.903  28.290   5.063  1.00 89.64           C  
ANISOU 1199  CA  ILE A 223    12305  12566   9187    429    242    360       C  
ATOM   1200  C   ILE A 223     -48.924  26.864   4.471  1.00 92.44           C  
ANISOU 1200  C   ILE A 223    12782  12740   9602    536    316    347       C  
ATOM   1201  O   ILE A 223     -49.261  26.717   3.304  1.00 91.93           O  
ANISOU 1201  O   ILE A 223    12749  12614   9566    503    365    245       O  
ATOM   1202  CB  ILE A 223     -47.471  28.895   5.188  1.00 93.11           C  
ANISOU 1202  CB  ILE A 223    12579  13201   9598    509    187    398       C  
ATOM   1203  CG1 ILE A 223     -47.534  30.411   5.468  1.00 92.35           C  
ANISOU 1203  CG1 ILE A 223    12387  13245   9456    361    121    371       C  
ATOM   1204  CG2 ILE A 223     -46.618  28.626   3.942  1.00 94.20           C  
ANISOU 1204  CG2 ILE A 223    12645  13377   9769    607    240    351       C  
ATOM   1205  CD1 ILE A 223     -46.810  30.837   6.681  1.00101.12           C  
ANISOU 1205  CD1 ILE A 223    13417  14496  10506    374     32    441       C  
ATOM   1206  N   LEU A 224     -48.650  25.836   5.291  1.00 88.58           N  
ANISOU 1206  N   LEU A 224    12379  12152   9124    655    321    448       N  
ATOM   1207  CA  LEU A 224     -48.642  24.424   4.904  1.00 89.20           C  
ANISOU 1207  CA  LEU A 224    12610  12014   9267    770    388    448       C  
ATOM   1208  C   LEU A 224     -49.964  23.951   4.295  1.00 92.09           C  
ANISOU 1208  C   LEU A 224    13123  12189   9676    617    445    355       C  
ATOM   1209  O   LEU A 224     -49.937  23.305   3.246  1.00 92.82           O  
ANISOU 1209  O   LEU A 224    13291  12163   9815    658    498    256       O  
ATOM   1210  CB  LEU A 224     -48.272  23.563   6.115  1.00 90.82           C  
ANISOU 1210  CB  LEU A 224    12900  12143   9466    904    369    606       C  
ATOM   1211  CG  LEU A 224     -48.035  22.089   5.870  1.00 97.56           C  
ANISOU 1211  CG  LEU A 224    13926  12751  10392   1067    431    632       C  
ATOM   1212  CD1 LEU A 224     -46.728  21.861   5.126  1.00 99.11           C  
ANISOU 1212  CD1 LEU A 224    14029  13017  10610   1297    446    594       C  
ATOM   1213  CD2 LEU A 224     -48.011  21.358   7.175  1.00100.89           C  
ANISOU 1213  CD2 LEU A 224    14462  13075  10796   1147    409    813       C  
ATOM   1214  N   GLY A 225     -51.087  24.280   4.942  1.00 86.58           N  
ANISOU 1214  N   GLY A 225    12455  11482   8958    443    433    379       N  
ATOM   1215  CA  GLY A 225     -52.427  23.938   4.467  1.00 85.56           C  
ANISOU 1215  CA  GLY A 225    12424  11220   8865    268    476    298       C  
ATOM   1216  C   GLY A 225     -52.735  24.511   3.096  1.00 86.74           C  
ANISOU 1216  C   GLY A 225    12510  11431   9017    194    478    143       C  
ATOM   1217  O   GLY A 225     -53.289  23.817   2.239  1.00 86.57           O  
ANISOU 1217  O   GLY A 225    12587  11272   9033    135    515     44       O  
ATOM   1218  N   LEU A 226     -52.341  25.780   2.880  1.00 81.24           N  
ANISOU 1218  N   LEU A 226    11659  10939   8271    193    433    124       N  
ATOM   1219  CA  LEU A 226     -52.501  26.496   1.621  1.00 80.24           C  
ANISOU 1219  CA  LEU A 226    11463  10901   8125    138    427      8       C  
ATOM   1220  C   LEU A 226     -51.538  25.958   0.557  1.00 86.45           C  
ANISOU 1220  C   LEU A 226    12264  11666   8918    271    468    -56       C  
ATOM   1221  O   LEU A 226     -51.928  25.851  -0.606  1.00 86.22           O  
ANISOU 1221  O   LEU A 226    12267  11616   8878    224    491   -172       O  
ATOM   1222  CB  LEU A 226     -52.316  28.006   1.821  1.00 78.73           C  
ANISOU 1222  CB  LEU A 226    11126  10903   7883     97    371     30       C  
ATOM   1223  CG  LEU A 226     -53.365  28.686   2.691  1.00 82.78           C  
ANISOU 1223  CG  LEU A 226    11623  11452   8379    -22    339     58       C  
ATOM   1224  CD1 LEU A 226     -52.888  30.015   3.163  1.00 82.04           C  
ANISOU 1224  CD1 LEU A 226    11423  11507   8242    -24    283     90       C  
ATOM   1225  CD2 LEU A 226     -54.692  28.834   1.964  1.00 85.73           C  
ANISOU 1225  CD2 LEU A 226    12010  11804   8759   -150    345    -29       C  
ATOM   1226  N   VAL A 227     -50.295  25.596   0.957  1.00 84.31           N  
ANISOU 1226  N   VAL A 227    11964  11416   8655    447    478     15       N  
ATOM   1227  CA  VAL A 227     -49.280  25.000   0.077  1.00 85.11           C  
ANISOU 1227  CA  VAL A 227    12065  11510   8762    616    532    -39       C  
ATOM   1228  C   VAL A 227     -49.873  23.698  -0.502  1.00 88.93           C  
ANISOU 1228  C   VAL A 227    12748  11751   9291    625    590   -135       C  
ATOM   1229  O   VAL A 227     -49.974  23.575  -1.722  1.00 89.15           O  
ANISOU 1229  O   VAL A 227    12805  11773   9294    614    628   -268       O  
ATOM   1230  CB  VAL A 227     -47.910  24.783   0.801  1.00 90.53           C  
ANISOU 1230  CB  VAL A 227    12667  12275   9455    820    523     73       C  
ATOM   1231  CG1 VAL A 227     -46.993  23.829   0.027  1.00 92.48           C  
ANISOU 1231  CG1 VAL A 227    12948  12468   9723   1035    598     17       C  
ATOM   1232  CG2 VAL A 227     -47.199  26.109   1.067  1.00 89.27           C  
ANISOU 1232  CG2 VAL A 227    12298  12375   9245    788    466    129       C  
ATOM   1233  N   VAL A 228     -50.342  22.782   0.378  1.00 84.92           N  
ANISOU 1233  N   VAL A 228    12384  11042   8839    617    595    -68       N  
ATOM   1234  CA  VAL A 228     -50.962  21.506   0.010  1.00 85.84           C  
ANISOU 1234  CA  VAL A 228    12716  10885   9013    590    644   -146       C  
ATOM   1235  C   VAL A 228     -52.210  21.704  -0.885  1.00 89.91           C  
ANISOU 1235  C   VAL A 228    13265  11385   9513    366    638   -289       C  
ATOM   1236  O   VAL A 228     -52.227  21.168  -1.992  1.00 90.74           O  
ANISOU 1236  O   VAL A 228    13459  11408   9612    381    674   -437       O  
ATOM   1237  CB  VAL A 228     -51.242  20.621   1.247  1.00 90.33           C  
ANISOU 1237  CB  VAL A 228    13427  11252   9641    596    648    -10       C  
ATOM   1238  CG1 VAL A 228     -51.945  19.326   0.854  1.00 91.91           C  
ANISOU 1238  CG1 VAL A 228    13868  11140   9912    526    700    -91       C  
ATOM   1239  CG2 VAL A 228     -49.950  20.315   2.001  1.00 91.14           C  
ANISOU 1239  CG2 VAL A 228    13505  11374   9751    853    645    128       C  
ATOM   1240  N   PHE A 229     -53.214  22.495  -0.437  1.00 85.67           N  
ANISOU 1240  N   PHE A 229    12648  10948   8956    173    591   -253       N  
ATOM   1241  CA  PHE A 229     -54.429  22.759  -1.224  1.00 85.51           C  
ANISOU 1241  CA  PHE A 229    12623  10954   8915    -29    570   -374       C  
ATOM   1242  C   PHE A 229     -54.143  23.385  -2.592  1.00 89.37           C  
ANISOU 1242  C   PHE A 229    13035  11592   9330     -3    560   -498       C  
ATOM   1243  O   PHE A 229     -54.716  22.937  -3.585  1.00 90.08           O  
ANISOU 1243  O   PHE A 229    13203  11623   9401    -87    565   -640       O  
ATOM   1244  CB  PHE A 229     -55.467  23.591  -0.454  1.00 86.26           C  
ANISOU 1244  CB  PHE A 229    12616  11163   8998   -194    525   -304       C  
ATOM   1245  CG  PHE A 229     -56.662  23.987  -1.302  1.00 87.93           C  
ANISOU 1245  CG  PHE A 229    12779  11449   9180   -373    490   -419       C  
ATOM   1246  CD1 PHE A 229     -57.740  23.121  -1.464  1.00 92.65           C  
ANISOU 1246  CD1 PHE A 229    13471  11912   9819   -543    499   -488       C  
ATOM   1247  CD2 PHE A 229     -56.693  25.212  -1.964  1.00 89.16           C  
ANISOU 1247  CD2 PHE A 229    12797  11813   9268   -373    444   -453       C  
ATOM   1248  CE1 PHE A 229     -58.833  23.478  -2.264  1.00 93.76           C  
ANISOU 1248  CE1 PHE A 229    13543  12156   9925   -704    453   -596       C  
ATOM   1249  CE2 PHE A 229     -57.783  25.565  -2.766  1.00 92.21           C  
ANISOU 1249  CE2 PHE A 229    13135  12284   9618   -513    400   -548       C  
ATOM   1250  CZ  PHE A 229     -58.846  24.696  -2.910  1.00 91.64           C  
ANISOU 1250  CZ  PHE A 229    13132  12106   9579   -674    400   -622       C  
ATOM   1251  N   SER A 230     -53.282  24.421  -2.649  1.00 84.77           N  
ANISOU 1251  N   SER A 230    12304  11208   8696     94    546   -442       N  
ATOM   1252  CA  SER A 230     -52.924  25.051  -3.921  1.00 84.26           C  
ANISOU 1252  CA  SER A 230    12168  11296   8549    118    549   -530       C  
ATOM   1253  C   SER A 230     -52.340  24.021  -4.897  1.00 90.52           C  
ANISOU 1253  C   SER A 230    13077  11991   9327    236    617   -656       C  
ATOM   1254  O   SER A 230     -52.712  24.054  -6.064  1.00 91.05           O  
ANISOU 1254  O   SER A 230    13171  12103   9322    179    618   -785       O  
ATOM   1255  CB  SER A 230     -51.956  26.212  -3.721  1.00 85.95           C  
ANISOU 1255  CB  SER A 230    12219  11713   8727    195    535   -432       C  
ATOM   1256  OG  SER A 230     -52.505  27.219  -2.889  1.00 90.70           O  
ANISOU 1256  OG  SER A 230    12735  12393   9333     91    472   -343       O  
ATOM   1257  N   MET A 231     -51.485  23.076  -4.412  1.00 88.58           N  
ANISOU 1257  N   MET A 231    12910  11606   9142    407    670   -623       N  
ATOM   1258  CA  MET A 231     -50.872  22.017  -5.225  1.00 90.84           C  
ANISOU 1258  CA  MET A 231    13323  11768   9423    560    747   -747       C  
ATOM   1259  C   MET A 231     -51.938  21.099  -5.842  1.00 95.52           C  
ANISOU 1259  C   MET A 231    14113  12154  10028    424    748   -907       C  
ATOM   1260  O   MET A 231     -51.930  20.921  -7.064  1.00 96.15           O  
ANISOU 1260  O   MET A 231    14243  12263  10029    431    776  -1070       O  
ATOM   1261  CB  MET A 231     -49.879  21.191  -4.407  1.00 94.79           C  
ANISOU 1261  CB  MET A 231    13875  12140  10000    783    791   -657       C  
ATOM   1262  CG  MET A 231     -48.496  21.226  -4.876  1.00100.10           C  
ANISOU 1262  CG  MET A 231    14453  12946  10635   1022    854   -667       C  
ATOM   1263  SD  MET A 231     -47.711  20.011  -3.816  1.00107.07           S  
ANISOU 1263  SD  MET A 231    15441  13616  11626   1274    885   -559       S  
ATOM   1264  CE  MET A 231     -47.923  20.821  -2.181  1.00102.00           C  
ANISOU 1264  CE  MET A 231    14671  13072  11013   1162    785   -329       C  
ATOM   1265  N   VAL A 232     -52.869  20.553  -5.009  1.00 91.31           N  
ANISOU 1265  N   VAL A 232    13685  11430   9581    281    718   -862       N  
ATOM   1266  CA  VAL A 232     -53.978  19.673  -5.431  1.00 91.88           C  
ANISOU 1266  CA  VAL A 232    13934  11297   9681     98    710  -1000       C  
ATOM   1267  C   VAL A 232     -54.910  20.420  -6.399  1.00 94.64           C  
ANISOU 1267  C   VAL A 232    14192  11833   9934    -93    648  -1114       C  
ATOM   1268  O   VAL A 232     -55.403  19.813  -7.350  1.00 96.11           O  
ANISOU 1268  O   VAL A 232    14498  11937  10083   -182    644  -1296       O  
ATOM   1269  CB  VAL A 232     -54.782  19.047  -4.253  1.00 95.72           C  
ANISOU 1269  CB  VAL A 232    14518  11574  10275    -42    698   -895       C  
ATOM   1270  CG1 VAL A 232     -55.601  17.851  -4.726  1.00 97.61           C  
ANISOU 1270  CG1 VAL A 232    14982  11541  10564   -197    711  -1046       C  
ATOM   1271  CG2 VAL A 232     -53.878  18.639  -3.094  1.00 96.01           C  
ANISOU 1271  CG2 VAL A 232    14595  11500  10383    151    736   -719       C  
ATOM   1272  N   PHE A 233     -55.130  21.731  -6.163  1.00 88.58           N  
ANISOU 1272  N   PHE A 233    13222  11313   9120   -146    594  -1011       N  
ATOM   1273  CA  PHE A 233     -55.963  22.577  -7.015  1.00 87.94           C  
ANISOU 1273  CA  PHE A 233    13039  11430   8944   -290    526  -1083       C  
ATOM   1274  C   PHE A 233     -55.274  22.825  -8.374  1.00 93.70           C  
ANISOU 1274  C   PHE A 233    13761  12294   9546   -184    551  -1197       C  
ATOM   1275  O   PHE A 233     -55.932  22.812  -9.421  1.00 94.29           O  
ANISOU 1275  O   PHE A 233    13864  12435   9530   -289    511  -1336       O  
ATOM   1276  CB  PHE A 233     -56.288  23.895  -6.300  1.00 87.56           C  
ANISOU 1276  CB  PHE A 233    12803  11572   8892   -337    472   -930       C  
ATOM   1277  CG  PHE A 233     -57.434  24.661  -6.914  1.00 88.79           C  
ANISOU 1277  CG  PHE A 233    12864  11892   8980   -495    391   -977       C  
ATOM   1278  CD1 PHE A 233     -58.750  24.359  -6.584  1.00 92.57           C  
ANISOU 1278  CD1 PHE A 233    13341  12328   9502   -685    345  -1003       C  
ATOM   1279  CD2 PHE A 233     -57.200  25.689  -7.817  1.00 90.36           C  
ANISOU 1279  CD2 PHE A 233    12966  12298   9067   -453    360   -984       C  
ATOM   1280  CE1 PHE A 233     -59.813  25.065  -7.161  1.00 93.23           C  
ANISOU 1280  CE1 PHE A 233    13312  12590   9520   -808    262  -1043       C  
ATOM   1281  CE2 PHE A 233     -58.262  26.396  -8.388  1.00 92.92           C  
ANISOU 1281  CE2 PHE A 233    13206  12776   9323   -572    275  -1013       C  
ATOM   1282  CZ  PHE A 233     -59.562  26.077  -8.060  1.00 91.40           C  
ANISOU 1282  CZ  PHE A 233    12997  12554   9176   -739    222  -1046       C  
ATOM   1283  N   GLY A 234     -53.952  23.016  -8.331  1.00 90.35           N  
ANISOU 1283  N   GLY A 234    13292  11927   9108     21    616  -1135       N  
ATOM   1284  CA  GLY A 234     -53.098  23.214  -9.499  1.00 90.68           C  
ANISOU 1284  CA  GLY A 234    13313  12112   9028    147    669  -1219       C  
ATOM   1285  C   GLY A 234     -53.114  22.006 -10.416  1.00 96.84           C  
ANISOU 1285  C   GLY A 234    14285  12740   9769    184    719  -1430       C  
ATOM   1286  O   GLY A 234     -53.241  22.153 -11.631  1.00 96.82           O  
ANISOU 1286  O   GLY A 234    14299  12862   9626    160    718  -1562       O  
ATOM   1287  N   PHE A 235     -53.032  20.799  -9.827  1.00 95.29           N  
ANISOU 1287  N   PHE A 235    14254  12263   9689    237    757  -1464       N  
ATOM   1288  CA  PHE A 235     -53.095  19.522 -10.534  1.00 97.91           C  
ANISOU 1288  CA  PHE A 235    14813  12375  10012    267    804  -1674       C  
ATOM   1289  C   PHE A 235     -54.483  19.353 -11.183  1.00101.23           C  
ANISOU 1289  C   PHE A 235    15308  12774  10380      0    718  -1824       C  
ATOM   1290  O   PHE A 235     -54.562  18.962 -12.352  1.00102.87           O  
ANISOU 1290  O   PHE A 235    15621  12995  10472     -8    728  -2030       O  
ATOM   1291  CB  PHE A 235     -52.760  18.370  -9.563  1.00101.50           C  
ANISOU 1291  CB  PHE A 235    15435  12505  10626    372    853  -1631       C  
ATOM   1292  CG  PHE A 235     -53.053  16.964 -10.020  1.00106.56           C  
ANISOU 1292  CG  PHE A 235    16357  12831  11299    350    886  -1837       C  
ATOM   1293  CD1 PHE A 235     -52.182  16.298 -10.876  1.00112.26           C  
ANISOU 1293  CD1 PHE A 235    17209  13473  11970    579    980  -1996       C  
ATOM   1294  CD2 PHE A 235     -54.159  16.277  -9.534  1.00110.14           C  
ANISOU 1294  CD2 PHE A 235    16949  13060  11839    100    829  -1872       C  
ATOM   1295  CE1 PHE A 235     -52.441  14.984 -11.275  1.00116.62           C  
ANISOU 1295  CE1 PHE A 235    18051  13703  12556    561   1010  -2206       C  
ATOM   1296  CE2 PHE A 235     -54.419  14.963  -9.936  1.00116.46           C  
ANISOU 1296  CE2 PHE A 235    18029  13542  12677     53    854  -2071       C  
ATOM   1297  CZ  PHE A 235     -53.552  14.321 -10.796  1.00116.91           C  
ANISOU 1297  CZ  PHE A 235    18240  13497  12685    287    942  -2242       C  
ATOM   1298  N   ALA A 236     -55.562  19.705 -10.441  1.00 95.27           N  
ANISOU 1298  N   ALA A 236    14482  12019   9696   -215    632  -1725       N  
ATOM   1299  CA  ALA A 236     -56.946  19.635 -10.915  1.00 95.31           C  
ANISOU 1299  CA  ALA A 236    14506  12045   9662   -482    537  -1842       C  
ATOM   1300  C   ALA A 236     -57.155  20.490 -12.164  1.00 99.27           C  
ANISOU 1300  C   ALA A 236    14902  12841   9976   -513    481  -1929       C  
ATOM   1301  O   ALA A 236     -57.650  19.963 -13.155  1.00101.08           O  
ANISOU 1301  O   ALA A 236    15236  13060  10111   -617    445  -2133       O  
ATOM   1302  CB  ALA A 236     -57.914  20.043  -9.817  1.00 94.40           C  
ANISOU 1302  CB  ALA A 236    14276  11944   9649   -661    473  -1687       C  
ATOM   1303  N   LEU A 237     -56.709  21.773 -12.141  1.00 93.86           N  
ANISOU 1303  N   LEU A 237    14024  12408   9229   -420    476  -1776       N  
ATOM   1304  CA  LEU A 237     -56.820  22.714 -13.268  1.00 93.42           C  
ANISOU 1304  CA  LEU A 237    13869  12637   8991   -430    428  -1809       C  
ATOM   1305  C   LEU A 237     -56.043  22.268 -14.500  1.00100.38           C  
ANISOU 1305  C   LEU A 237    14860  13558   9720   -303    500  -1978       C  
ATOM   1306  O   LEU A 237     -56.494  22.501 -15.624  1.00100.77           O  
ANISOU 1306  O   LEU A 237    14916  13775   9598   -374    446  -2094       O  
ATOM   1307  CB  LEU A 237     -56.421  24.141 -12.879  1.00 90.83           C  
ANISOU 1307  CB  LEU A 237    13342  12517   8650   -361    419  -1593       C  
ATOM   1308  CG  LEU A 237     -57.344  24.920 -11.939  1.00 93.09           C  
ANISOU 1308  CG  LEU A 237    13496  12847   9028   -484    333  -1444       C  
ATOM   1309  CD1 LEU A 237     -56.825  26.306 -11.754  1.00 91.16           C  
ANISOU 1309  CD1 LEU A 237    13099  12785   8753   -402    329  -1267       C  
ATOM   1310  CD2 LEU A 237     -58.769  25.000 -12.470  1.00 95.89           C  
ANISOU 1310  CD2 LEU A 237    13821  13290   9323   -676    216  -1529       C  
ATOM   1311  N   GLY A 238     -54.888  21.639 -14.265  1.00 98.79           N  
ANISOU 1311  N   GLY A 238    14741  13222   9574   -104    621  -1990       N  
ATOM   1312  CA  GLY A 238     -54.022  21.076 -15.293  1.00101.24           C  
ANISOU 1312  CA  GLY A 238    15162  13547   9757     59    719  -2158       C  
ATOM   1313  C   GLY A 238     -54.725  19.950 -16.024  1.00109.41           C  
ANISOU 1313  C   GLY A 238    16419  14411  10743    -50    692  -2425       C  
ATOM   1314  O   GLY A 238     -54.550  19.794 -17.234  1.00111.40           O  
ANISOU 1314  O   GLY A 238    16745  14773  10809    -10    717  -2605       O  
ATOM   1315  N   LYS A 239     -55.563  19.183 -15.291  1.00107.14           N  
ANISOU 1315  N   LYS A 239    16238  13858  10612   -207    637  -2453       N  
ATOM   1316  CA  LYS A 239     -56.367  18.075 -15.814  1.00110.07           C  
ANISOU 1316  CA  LYS A 239    16826  14018  10978   -373    594  -2697       C  
ATOM   1317  C   LYS A 239     -57.698  18.554 -16.443  1.00115.58           C  
ANISOU 1317  C   LYS A 239    17444  14921  11551   -639    445  -2774       C  
ATOM   1318  O   LYS A 239     -58.443  17.736 -16.985  1.00117.85           O  
ANISOU 1318  O   LYS A 239    17890  15095  11791   -801    391  -3003       O  
ATOM   1319  CB  LYS A 239     -56.647  17.052 -14.701  1.00112.69           C  
ANISOU 1319  CB  LYS A 239    17285  13991  11540   -457    601  -2649       C  
ATOM   1320  CG  LYS A 239     -55.535  16.039 -14.486  1.00129.57           C  
ANISOU 1320  CG  LYS A 239    19721  15760  13750   -362    687  -2830       C  
ATOM   1321  CD  LYS A 239     -55.857  15.037 -13.353  1.00140.44           C  
ANISOU 1321  CD  LYS A 239    21201  16798  15362   -391    712  -2692       C  
ATOM   1322  CE  LYS A 239     -57.233  14.389 -13.349  1.00149.31           C  
ANISOU 1322  CE  LYS A 239    22411  17739  16580   -738    621  -2738       C  
ATOM   1323  NZ  LYS A 239     -57.626  13.946 -11.980  1.00155.29           N  
ANISOU 1323  NZ  LYS A 239    23247  18209  17547   -755    660  -2553       N  
ATOM   1324  N   MET A 240     -57.995  19.866 -16.375  1.00110.80           N  
ANISOU 1324  N   MET A 240    16598  14607  10892   -685    370  -2592       N  
ATOM   1325  CA  MET A 240     -59.243  20.434 -16.901  1.00111.47           C  
ANISOU 1325  CA  MET A 240    16594  14897  10862   -909    220  -2652       C  
ATOM   1326  C   MET A 240     -59.123  20.978 -18.327  1.00116.49           C  
ANISOU 1326  C   MET A 240    17184  15842  11234   -853    187  -2723       C  
ATOM   1327  O   MET A 240     -60.146  21.319 -18.926  1.00116.48           O  
ANISOU 1327  O   MET A 240    17111  16033  11114  -1020     50  -2776       O  
ATOM   1328  CB  MET A 240     -59.769  21.572 -16.012  1.00111.95           C  
ANISOU 1328  CB  MET A 240    16444  15066  11025  -1049    123  -2450       C  
ATOM   1329  CG  MET A 240     -59.554  21.430 -14.552  1.00113.46           C  
ANISOU 1329  CG  MET A 240    16513  15240  11357   -919    186  -2195       C  
ATOM   1330  SD  MET A 240     -60.889  22.145 -13.615  1.00116.49           S  
ANISOU 1330  SD  MET A 240    16735  15620  11906  -1108    102  -2032       S  
ATOM   1331  CE  MET A 240     -61.902  20.774 -13.585  1.00115.54           C  
ANISOU 1331  CE  MET A 240    16808  15170  11921  -1288    119  -2178       C  
ATOM   1332  N   GLY A 241     -57.894  21.130 -18.821  1.00114.06           N  
ANISOU 1332  N   GLY A 241    16913  15595  10827   -626    310  -2724       N  
ATOM   1333  CA  GLY A 241     -57.630  21.676 -20.147  1.00115.38           C  
ANISOU 1333  CA  GLY A 241    17054  16058  10726   -561    306  -2779       C  
ATOM   1334  C   GLY A 241     -58.027  23.135 -20.279  1.00118.97           C  
ANISOU 1334  C   GLY A 241    17296  16810  11096   -603    211  -2567       C  
ATOM   1335  O   GLY A 241     -57.644  23.960 -19.444  1.00116.70           O  
ANISOU 1335  O   GLY A 241    16869  16539  10932   -534    242  -2330       O  
ATOM   1336  N   GLU A 242     -58.831  23.442 -21.320  1.00117.27           N  
ANISOU 1336  N   GLU A 242    17065  16824  10667   -715     88  -2656       N  
ATOM   1337  CA  GLU A 242     -59.332  24.773 -21.683  1.00116.26           C  
ANISOU 1337  CA  GLU A 242    16764  16989  10422   -745    -20  -2471       C  
ATOM   1338  C   GLU A 242     -60.205  25.393 -20.584  1.00118.54           C  
ANISOU 1338  C   GLU A 242    16889  17241  10908   -845   -118  -2288       C  
ATOM   1339  O   GLU A 242     -59.974  26.551 -20.209  1.00116.54           O  
ANISOU 1339  O   GLU A 242    16501  17090  10687   -766   -114  -2053       O  
ATOM   1340  CB  GLU A 242     -60.081  24.747 -23.018  1.00120.24           C  
ANISOU 1340  CB  GLU A 242    17303  17731  10651   -844   -147  -2628       C  
ATOM   1341  CG  GLU A 242     -59.254  24.237 -24.196  1.00137.33           C  
ANISOU 1341  CG  GLU A 242    19622  19985  12572   -733    -47  -2804       C  
ATOM   1342  CD  GLU A 242     -59.208  22.731 -24.420  1.00168.24           C  
ANISOU 1342  CD  GLU A 242    23755  23703  16466   -788    -17  -3135       C  
ATOM   1343  OE1 GLU A 242     -60.138  22.019 -23.968  1.00167.30           O  
ANISOU 1343  OE1 GLU A 242    23680  23374  16511   -959    -97  -3247       O  
ATOM   1344  OE2 GLU A 242     -58.244  22.272 -25.074  1.00166.24           O  
ANISOU 1344  OE2 GLU A 242    23633  23522  16007   -673     80  -3293       O  
ATOM   1345  N   GLN A 243     -61.192  24.626 -20.056  1.00115.15           N  
ANISOU 1345  N   GLN A 243    16478  16662  10613  -1022   -196  -2398       N  
ATOM   1346  CA  GLN A 243     -62.075  25.080 -18.974  1.00112.76           C  
ANISOU 1346  CA  GLN A 243    16017  16330  10496  -1121   -272  -2246       C  
ATOM   1347  C   GLN A 243     -61.211  25.560 -17.799  1.00111.93           C  
ANISOU 1347  C   GLN A 243    15864  16089  10575   -978   -152  -2036       C  
ATOM   1348  O   GLN A 243     -61.488  26.602 -17.207  1.00109.87           O  
ANISOU 1348  O   GLN A 243    15450  15918  10377   -953   -191  -1839       O  
ATOM   1349  CB  GLN A 243     -63.055  23.957 -18.543  1.00115.70           C  
ANISOU 1349  CB  GLN A 243    16438  16534  10989  -1343   -334  -2409       C  
ATOM   1350  CG  GLN A 243     -63.968  24.271 -17.342  1.00131.95           C  
ANISOU 1350  CG  GLN A 243    18331  18563  13242  -1455   -387  -2263       C  
ATOM   1351  CD  GLN A 243     -65.056  25.287 -17.618  1.00151.56           C  
ANISOU 1351  CD  GLN A 243    20601  21344  15642  -1512   -541  -2172       C  
ATOM   1352  OE1 GLN A 243     -64.851  26.505 -17.525  1.00144.44           O  
ANISOU 1352  OE1 GLN A 243    19582  20586  14713  -1367   -547  -1977       O  
ATOM   1353  NE2 GLN A 243     -66.259  24.802 -17.901  1.00146.05           N  
ANISOU 1353  NE2 GLN A 243    19845  20735  14914  -1726   -671  -2308       N  
ATOM   1354  N   GLY A 244     -60.133  24.827 -17.538  1.00106.70           N  
ANISOU 1354  N   GLY A 244    15335  15229   9977   -869    -12  -2088       N  
ATOM   1355  CA  GLY A 244     -59.171  25.140 -16.493  1.00103.59           C  
ANISOU 1355  CA  GLY A 244    14903  14722   9735   -724    100  -1912       C  
ATOM   1356  C   GLY A 244     -58.335  26.369 -16.769  1.00103.61           C  
ANISOU 1356  C   GLY A 244    14804  14917   9646   -580    140  -1738       C  
ATOM   1357  O   GLY A 244     -58.080  27.139 -15.840  1.00101.29           O  
ANISOU 1357  O   GLY A 244    14404  14611   9470   -534    156  -1547       O  
ATOM   1358  N   GLN A 245     -57.932  26.582 -18.047  1.00 99.24           N  
ANISOU 1358  N   GLN A 245    14288  14547   8873   -523    156  -1803       N  
ATOM   1359  CA  GLN A 245     -57.074  27.693 -18.485  1.00 97.55           C  
ANISOU 1359  CA  GLN A 245    13996  14522   8546   -405    210  -1642       C  
ATOM   1360  C   GLN A 245     -57.465  29.064 -17.941  1.00 97.69           C  
ANISOU 1360  C   GLN A 245    13866  14631   8621   -427    135  -1408       C  
ATOM   1361  O   GLN A 245     -56.571  29.783 -17.492  1.00 96.49           O  
ANISOU 1361  O   GLN A 245    13652  14487   8523   -341    210  -1245       O  
ATOM   1362  CB  GLN A 245     -56.938  27.751 -20.015  1.00100.97           C  
ANISOU 1362  CB  GLN A 245    14491  15173   8701   -383    211  -1744       C  
ATOM   1363  CG  GLN A 245     -55.811  28.665 -20.532  1.00116.39           C  
ANISOU 1363  CG  GLN A 245    16392  17305  10528   -259    315  -1591       C  
ATOM   1364  CD  GLN A 245     -54.418  28.330 -20.031  1.00139.14           C  
ANISOU 1364  CD  GLN A 245    19269  20091  13507   -119    486  -1565       C  
ATOM   1365  OE1 GLN A 245     -54.065  27.170 -19.770  1.00136.75           O  
ANISOU 1365  OE1 GLN A 245    19060  19617  13283    -60    558  -1724       O  
ATOM   1366  NE2 GLN A 245     -53.577  29.346 -19.926  1.00131.48           N  
ANISOU 1366  NE2 GLN A 245    18192  19236  12529    -60    552  -1363       N  
ATOM   1367  N   LEU A 246     -58.773  29.423 -17.964  1.00 92.05           N  
ANISOU 1367  N   LEU A 246    13092  13985   7898   -539    -11  -1397       N  
ATOM   1368  CA  LEU A 246     -59.270  30.710 -17.451  1.00 89.23           C  
ANISOU 1368  CA  LEU A 246    12606  13699   7598   -539    -88  -1192       C  
ATOM   1369  C   LEU A 246     -58.763  30.988 -16.036  1.00 91.34           C  
ANISOU 1369  C   LEU A 246    12822  13800   8082   -496    -21  -1063       C  
ATOM   1370  O   LEU A 246     -58.220  32.068 -15.784  1.00 89.82           O  
ANISOU 1370  O   LEU A 246    12576  13647   7907   -432      3   -889       O  
ATOM   1371  CB  LEU A 246     -60.808  30.778 -17.499  1.00 89.10           C  
ANISOU 1371  CB  LEU A 246    12519  13761   7576   -652   -247  -1231       C  
ATOM   1372  CG  LEU A 246     -61.483  31.894 -16.692  1.00 91.31           C  
ANISOU 1372  CG  LEU A 246    12665  14063   7965   -639   -320  -1051       C  
ATOM   1373  CD1 LEU A 246     -61.172  33.267 -17.248  1.00 91.13           C  
ANISOU 1373  CD1 LEU A 246    12615  14179   7831   -541   -343   -867       C  
ATOM   1374  CD2 LEU A 246     -62.949  31.695 -16.645  1.00 93.84           C  
ANISOU 1374  CD2 LEU A 246    12894  14461   8298   -747   -455  -1120       C  
ATOM   1375  N   LEU A 247     -58.930  30.005 -15.131  1.00 87.63           N  
ANISOU 1375  N   LEU A 247    12383  13144   7769   -541      8  -1148       N  
ATOM   1376  CA  LEU A 247     -58.497  30.086 -13.743  1.00 85.82           C  
ANISOU 1376  CA  LEU A 247    12117  12761   7729   -505     66  -1043       C  
ATOM   1377  C   LEU A 247     -56.989  30.123 -13.606  1.00 91.86           C  
ANISOU 1377  C   LEU A 247    12905  13491   8505   -382    188   -985       C  
ATOM   1378  O   LEU A 247     -56.488  30.808 -12.717  1.00 90.62           O  
ANISOU 1378  O   LEU A 247    12683  13303   8446   -340    213   -844       O  
ATOM   1379  CB  LEU A 247     -59.080  28.946 -12.924  1.00 85.67           C  
ANISOU 1379  CB  LEU A 247    12141  12563   7847   -590     67  -1140       C  
ATOM   1380  CG  LEU A 247     -60.274  29.302 -12.082  1.00 89.39           C  
ANISOU 1380  CG  LEU A 247    12512  13035   8416   -685    -14  -1081       C  
ATOM   1381  CD1 LEU A 247     -60.795  28.088 -11.374  1.00 90.25           C  
ANISOU 1381  CD1 LEU A 247    12676  12973   8643   -793      3  -1172       C  
ATOM   1382  CD2 LEU A 247     -59.908  30.327 -11.050  1.00 90.86           C  
ANISOU 1382  CD2 LEU A 247    12616  13213   8693   -609      7   -904       C  
ATOM   1383  N   VAL A 248     -56.264  29.413 -14.497  1.00 91.09           N  
ANISOU 1383  N   VAL A 248    12893  13415   8302   -324    264  -1101       N  
ATOM   1384  CA  VAL A 248     -54.794  29.391 -14.523  1.00 91.69           C  
ANISOU 1384  CA  VAL A 248    12967  13503   8369   -193    391  -1059       C  
ATOM   1385  C   VAL A 248     -54.301  30.784 -14.940  1.00 96.34           C  
ANISOU 1385  C   VAL A 248    13464  14275   8868   -174    394   -892       C  
ATOM   1386  O   VAL A 248     -53.359  31.307 -14.342  1.00 95.25           O  
ANISOU 1386  O   VAL A 248    13253  14138   8800   -122    454   -767       O  
ATOM   1387  CB  VAL A 248     -54.234  28.261 -15.432  1.00 97.88           C  
ANISOU 1387  CB  VAL A 248    13865  14275   9049   -118    479  -1244       C  
ATOM   1388  CG1 VAL A 248     -52.705  28.213 -15.389  1.00 98.14           C  
ANISOU 1388  CG1 VAL A 248    13862  14344   9083     38    618  -1195       C  
ATOM   1389  CG2 VAL A 248     -54.809  26.908 -15.031  1.00 98.47           C  
ANISOU 1389  CG2 VAL A 248    14063  14128   9225   -160    466  -1406       C  
ATOM   1390  N   ASP A 249     -54.981  31.398 -15.928  1.00 94.11           N  
ANISOU 1390  N   ASP A 249    13185  14142   8430   -228    320   -883       N  
ATOM   1391  CA  ASP A 249     -54.683  32.744 -16.406  1.00 93.96           C  
ANISOU 1391  CA  ASP A 249    13109  14277   8316   -226    311   -711       C  
ATOM   1392  C   ASP A 249     -55.020  33.786 -15.339  1.00 94.54           C  
ANISOU 1392  C   ASP A 249    13107  14275   8537   -259    245   -547       C  
ATOM   1393  O   ASP A 249     -54.267  34.749 -15.180  1.00 93.33           O  
ANISOU 1393  O   ASP A 249    12909  14157   8396   -247    283   -395       O  
ATOM   1394  CB  ASP A 249     -55.410  33.025 -17.725  1.00 97.90           C  
ANISOU 1394  CB  ASP A 249    13649  14947   8601   -261    236   -743       C  
ATOM   1395  CG  ASP A 249     -54.875  32.234 -18.907  1.00114.73           C  
ANISOU 1395  CG  ASP A 249    15860  17192  10539   -219    318   -891       C  
ATOM   1396  OD1 ASP A 249     -53.649  31.966 -18.941  1.00115.99           O  
ANISOU 1396  OD1 ASP A 249    16014  17363  10694   -139    458   -893       O  
ATOM   1397  OD2 ASP A 249     -55.670  31.934 -19.828  1.00124.24           O  
ANISOU 1397  OD2 ASP A 249    17124  18497  11585   -261    240  -1004       O  
ATOM   1398  N   PHE A 250     -56.127  33.568 -14.586  1.00 89.53           N  
ANISOU 1398  N   PHE A 250    12462  13539   8015   -308    155   -587       N  
ATOM   1399  CA  PHE A 250     -56.562  34.425 -13.475  1.00 87.48           C  
ANISOU 1399  CA  PHE A 250    12139  13202   7896   -324     99   -467       C  
ATOM   1400  C   PHE A 250     -55.480  34.460 -12.397  1.00 91.10           C  
ANISOU 1400  C   PHE A 250    12569  13558   8487   -290    181   -403       C  
ATOM   1401  O   PHE A 250     -55.143  35.540 -11.909  1.00 90.69           O  
ANISOU 1401  O   PHE A 250    12478  13497   8482   -291    173   -269       O  
ATOM   1402  CB  PHE A 250     -57.896  33.937 -12.867  1.00 88.37           C  
ANISOU 1402  CB  PHE A 250    12233  13250   8094   -381     15   -546       C  
ATOM   1403  CG  PHE A 250     -58.316  34.676 -11.616  1.00 88.06           C  
ANISOU 1403  CG  PHE A 250    12131  13132   8197   -380    -21   -447       C  
ATOM   1404  CD1 PHE A 250     -57.874  34.267 -10.363  1.00 90.54           C  
ANISOU 1404  CD1 PHE A 250    12438  13312   8650   -375     36   -443       C  
ATOM   1405  CD2 PHE A 250     -59.150  35.781 -11.691  1.00 89.88           C  
ANISOU 1405  CD2 PHE A 250    12316  13424   8409   -368   -110   -358       C  
ATOM   1406  CE1 PHE A 250     -58.242  34.966  -9.208  1.00 90.51           C  
ANISOU 1406  CE1 PHE A 250    12387  13252   8753   -371      8   -364       C  
ATOM   1407  CE2 PHE A 250     -59.543  36.460 -10.534  1.00 91.93           C  
ANISOU 1407  CE2 PHE A 250    12529  13609   8791   -350   -132   -287       C  
ATOM   1408  CZ  PHE A 250     -59.072  36.061  -9.302  1.00 89.23           C  
ANISOU 1408  CZ  PHE A 250    12185  13147   8573   -358    -70   -296       C  
ATOM   1409  N   PHE A 251     -54.952  33.279 -12.018  1.00 87.17           N  
ANISOU 1409  N   PHE A 251    12098  12977   8046   -259    253   -501       N  
ATOM   1410  CA  PHE A 251     -53.918  33.171 -10.998  1.00 86.07           C  
ANISOU 1410  CA  PHE A 251    11921  12760   8020   -211    320   -445       C  
ATOM   1411  C   PHE A 251     -52.541  33.604 -11.497  1.00 91.22           C  
ANISOU 1411  C   PHE A 251    12529  13523   8609   -162    405   -374       C  
ATOM   1412  O   PHE A 251     -51.675  33.913 -10.685  1.00 89.76           O  
ANISOU 1412  O   PHE A 251    12278  13322   8506   -142    437   -292       O  
ATOM   1413  CB  PHE A 251     -53.895  31.768 -10.371  1.00 87.88           C  
ANISOU 1413  CB  PHE A 251    12201  12851   8338   -177    358   -553       C  
ATOM   1414  CG  PHE A 251     -54.982  31.571  -9.341  1.00 88.25           C  
ANISOU 1414  CG  PHE A 251    12255  12783   8495   -243    292   -557       C  
ATOM   1415  CD1 PHE A 251     -54.879  32.144  -8.079  1.00 89.47           C  
ANISOU 1415  CD1 PHE A 251    12355  12890   8751   -243    276   -453       C  
ATOM   1416  CD2 PHE A 251     -56.115  30.824  -9.636  1.00 90.60           C  
ANISOU 1416  CD2 PHE A 251    12605  13036   8782   -315    249   -670       C  
ATOM   1417  CE1 PHE A 251     -55.897  31.992  -7.146  1.00 89.64           C  
ANISOU 1417  CE1 PHE A 251    12375  12833   8852   -300    230   -455       C  
ATOM   1418  CE2 PHE A 251     -57.130  30.666  -8.696  1.00 92.41           C  
ANISOU 1418  CE2 PHE A 251    12819  13188   9107   -389    201   -664       C  
ATOM   1419  CZ  PHE A 251     -57.014  31.250  -7.460  1.00 89.30           C  
ANISOU 1419  CZ  PHE A 251    12369  12757   8803   -373    200   -553       C  
ATOM   1420  N   ASN A 252     -52.338  33.652 -12.821  1.00 90.66           N  
ANISOU 1420  N   ASN A 252    12482  13585   8380   -152    441   -402       N  
ATOM   1421  CA  ASN A 252     -51.062  34.088 -13.382  1.00 91.86           C  
ANISOU 1421  CA  ASN A 252    12576  13875   8453   -121    538   -325       C  
ATOM   1422  C   ASN A 252     -50.947  35.605 -13.322  1.00 95.93           C  
ANISOU 1422  C   ASN A 252    13045  14439   8965   -200    499   -147       C  
ATOM   1423  O   ASN A 252     -49.868  36.128 -13.039  1.00 96.09           O  
ANISOU 1423  O   ASN A 252    12984  14510   9016   -214    558    -47       O  
ATOM   1424  CB  ASN A 252     -50.880  33.581 -14.801  1.00 95.44           C  
ANISOU 1424  CB  ASN A 252    13079  14464   8719    -79    604   -419       C  
ATOM   1425  CG  ASN A 252     -49.455  33.202 -15.074  1.00128.04           C  
ANISOU 1425  CG  ASN A 252    17143  18696  12810     11    747   -425       C  
ATOM   1426  OD1 ASN A 252     -48.560  34.053 -15.125  1.00126.87           O  
ANISOU 1426  OD1 ASN A 252    16897  18664  12642    -16    801   -286       O  
ATOM   1427  ND2 ASN A 252     -49.202  31.909 -15.204  1.00121.77           N  
ANISOU 1427  ND2 ASN A 252    16397  17856  12012    120    814   -587       N  
ATOM   1428  N   SER A 253     -52.070  36.304 -13.577  1.00 91.89           N  
ANISOU 1428  N   SER A 253    12584  13911   8420   -253    397   -107       N  
ATOM   1429  CA  SER A 253     -52.160  37.756 -13.527  1.00 91.38           C  
ANISOU 1429  CA  SER A 253    12514  13846   8359   -315    346     58       C  
ATOM   1430  C   SER A 253     -52.033  38.200 -12.082  1.00 94.30           C  
ANISOU 1430  C   SER A 253    12845  14079   8908   -340    313    106       C  
ATOM   1431  O   SER A 253     -51.362  39.191 -11.822  1.00 94.66           O  
ANISOU 1431  O   SER A 253    12864  14117   8985   -396    324    229       O  
ATOM   1432  CB  SER A 253     -53.481  38.231 -14.114  1.00 94.95           C  
ANISOU 1432  CB  SER A 253    13029  14310   8738   -323    237     73       C  
ATOM   1433  OG  SER A 253     -53.669  37.708 -15.418  1.00106.76           O  
ANISOU 1433  OG  SER A 253    14566  15947  10052   -303    252      5       O  
ATOM   1434  N   LEU A 254     -52.627  37.442 -11.138  1.00 89.43           N  
ANISOU 1434  N   LEU A 254    12226  13354   8397   -310    278      8       N  
ATOM   1435  CA  LEU A 254     -52.554  37.735  -9.705  1.00 88.20           C  
ANISOU 1435  CA  LEU A 254    12040  13084   8388   -324    249     38       C  
ATOM   1436  C   LEU A 254     -51.127  37.514  -9.150  1.00 92.87           C  
ANISOU 1436  C   LEU A 254    12556  13701   9028   -318    323     64       C  
ATOM   1437  O   LEU A 254     -50.757  38.166  -8.174  1.00 92.03           O  
ANISOU 1437  O   LEU A 254    12416  13544   9006   -358    297    125       O  
ATOM   1438  CB  LEU A 254     -53.602  36.907  -8.930  1.00 87.29           C  
ANISOU 1438  CB  LEU A 254    11944  12874   8348   -299    204    -63       C  
ATOM   1439  CG  LEU A 254     -53.660  37.081  -7.406  1.00 90.11           C  
ANISOU 1439  CG  LEU A 254    12278  13127   8831   -305    178    -45       C  
ATOM   1440  CD1 LEU A 254     -54.777  37.997  -7.005  1.00 90.05           C  
ANISOU 1440  CD1 LEU A 254    12290  13070   8854   -322     98    -15       C  
ATOM   1441  CD2 LEU A 254     -53.797  35.752  -6.717  1.00 89.88           C  
ANISOU 1441  CD2 LEU A 254    12255  13036   8861   -272    205   -132       C  
ATOM   1442  N   ASN A 255     -50.330  36.615  -9.770  1.00 90.32           N  
ANISOU 1442  N   ASN A 255    12202  13467   8647   -261    413     12       N  
ATOM   1443  CA  ASN A 255     -48.962  36.360  -9.320  1.00 90.55           C  
ANISOU 1443  CA  ASN A 255    12131  13557   8716   -230    484     40       C  
ATOM   1444  C   ASN A 255     -48.048  37.504  -9.729  1.00 96.43           C  
ANISOU 1444  C   ASN A 255    12805  14417   9418   -319    516    167       C  
ATOM   1445  O   ASN A 255     -47.358  38.058  -8.875  1.00 96.07           O  
ANISOU 1445  O   ASN A 255    12683  14369   9450   -374    500    234       O  
ATOM   1446  CB  ASN A 255     -48.440  35.031  -9.851  1.00 91.21           C  
ANISOU 1446  CB  ASN A 255    12206  13696   8754   -113    576    -63       C  
ATOM   1447  CG  ASN A 255     -47.091  34.657  -9.297  1.00110.21           C  
ANISOU 1447  CG  ASN A 255    14491  16172  11212    -43    642    -38       C  
ATOM   1448  OD1 ASN A 255     -46.044  34.987  -9.864  1.00109.97           O  
ANISOU 1448  OD1 ASN A 255    14358  16305  11122    -45    719     17       O  
ATOM   1449  ND2 ASN A 255     -47.086  33.956  -8.180  1.00 97.09           N  
ANISOU 1449  ND2 ASN A 255    12829  14407   9654     24    613    -67       N  
ATOM   1450  N   GLU A 256     -48.068  37.871 -11.028  1.00 94.64           N  
ANISOU 1450  N   GLU A 256    12608  14292   9060   -346    557    202       N  
ATOM   1451  CA  GLU A 256     -47.266  38.951 -11.593  1.00 95.77           C  
ANISOU 1451  CA  GLU A 256    12701  14545   9143   -450    601    341       C  
ATOM   1452  C   GLU A 256     -47.607  40.311 -10.966  1.00 98.15           C  
ANISOU 1452  C   GLU A 256    13047  14721   9523   -572    509    452       C  
ATOM   1453  O   GLU A 256     -46.692  41.102 -10.730  1.00 98.06           O  
ANISOU 1453  O   GLU A 256    12967  14748   9544   -682    531    553       O  
ATOM   1454  CB  GLU A 256     -47.379  38.954 -13.129  1.00 98.91           C  
ANISOU 1454  CB  GLU A 256    13149  15075   9359   -443    662    358       C  
ATOM   1455  CG  GLU A 256     -46.410  39.872 -13.867  1.00117.89           C  
ANISOU 1455  CG  GLU A 256    15497  17621  11676   -554    740    513       C  
ATOM   1456  CD  GLU A 256     -45.002  40.031 -13.324  1.00154.99           C  
ANISOU 1456  CD  GLU A 256    20025  22426  16437   -606    821    567       C  
ATOM   1457  OE1 GLU A 256     -44.307  39.001 -13.173  1.00163.39           O  
ANISOU 1457  OE1 GLU A 256    20986  23587  17507   -492    897    470       O  
ATOM   1458  OE2 GLU A 256     -44.581  41.187 -13.086  1.00153.59           O  
ANISOU 1458  OE2 GLU A 256    19818  22236  16304   -761    806    706       O  
ATOM   1459  N   ALA A 257     -48.910  40.556 -10.654  1.00 93.45           N  
ANISOU 1459  N   ALA A 257    12562  13981   8966   -552    407    423       N  
ATOM   1460  CA  ALA A 257     -49.397  41.785 -10.017  1.00 92.89           C  
ANISOU 1460  CA  ALA A 257    12558  13764   8973   -626    318    501       C  
ATOM   1461  C   ALA A 257     -48.888  41.905  -8.595  1.00 97.28           C  
ANISOU 1461  C   ALA A 257    13057  14247   9660   -664    290    481       C  
ATOM   1462  O   ALA A 257     -48.531  43.010  -8.193  1.00 97.90           O  
ANISOU 1462  O   ALA A 257    13153  14258   9786   -774    258    562       O  
ATOM   1463  CB  ALA A 257     -50.913  41.848 -10.037  1.00 92.78           C  
ANISOU 1463  CB  ALA A 257    12643  13651   8959   -558    228    457       C  
ATOM   1464  N   THR A 258     -48.822  40.782  -7.834  1.00 93.55           N  
ANISOU 1464  N   THR A 258    12526  13783   9237   -581    298    376       N  
ATOM   1465  CA  THR A 258     -48.281  40.823  -6.467  1.00 93.30           C  
ANISOU 1465  CA  THR A 258    12433  13712   9305   -608    266    363       C  
ATOM   1466  C   THR A 258     -46.755  40.864  -6.537  1.00 99.08           C  
ANISOU 1466  C   THR A 258    13026  14590  10029   -669    329    418       C  
ATOM   1467  O   THR A 258     -46.122  41.446  -5.655  1.00 99.77           O  
ANISOU 1467  O   THR A 258    13058  14671  10178   -758    289    449       O  
ATOM   1468  CB  THR A 258     -48.861  39.758  -5.520  1.00 99.69           C  
ANISOU 1468  CB  THR A 258    13250  14461  10167   -503    240    261       C  
ATOM   1469  OG1 THR A 258     -48.379  38.453  -5.839  1.00 98.10           O  
ANISOU 1469  OG1 THR A 258    12991  14342   9940   -405    311    207       O  
ATOM   1470  CG2 THR A 258     -50.378  39.792  -5.464  1.00 98.50           C  
ANISOU 1470  CG2 THR A 258    13205  14197  10024   -466    185    213       C  
ATOM   1471  N   MET A 259     -46.169  40.321  -7.624  1.00 95.92           N  
ANISOU 1471  N   MET A 259    12563  14339   9543   -629    427    428       N  
ATOM   1472  CA  MET A 259     -44.730  40.389  -7.853  1.00 96.93           C  
ANISOU 1472  CA  MET A 259    12530  14646   9651   -683    504    489       C  
ATOM   1473  C   MET A 259     -44.350  41.837  -8.186  1.00100.23           C  
ANISOU 1473  C   MET A 259    12955  15067  10059   -879    496    618       C  
ATOM   1474  O   MET A 259     -43.264  42.280  -7.836  1.00101.22           O  
ANISOU 1474  O   MET A 259    12951  15291  10219   -994    511    677       O  
ATOM   1475  CB  MET A 259     -44.289  39.422  -8.965  1.00100.41           C  
ANISOU 1475  CB  MET A 259    12910  15249   9990   -570    625    453       C  
ATOM   1476  CG  MET A 259     -44.029  38.000  -8.472  1.00104.19           C  
ANISOU 1476  CG  MET A 259    13333  15751  10505   -391    653    345       C  
ATOM   1477  SD  MET A 259     -42.836  37.852  -7.110  1.00109.27           S  
ANISOU 1477  SD  MET A 259    13793  16472  11253   -380    623    370       S  
ATOM   1478  CE  MET A 259     -41.325  38.227  -7.959  1.00108.36           C  
ANISOU 1478  CE  MET A 259    13463  16638  11071   -445    742    458       C  
ATOM   1479  N   LYS A 260     -45.274  42.586  -8.812  1.00 94.88           N  
ANISOU 1479  N   LYS A 260    12433  14275   9341   -920    464    667       N  
ATOM   1480  CA  LYS A 260     -45.086  44.000  -9.132  1.00 94.80           C  
ANISOU 1480  CA  LYS A 260    12483  14208   9328  -1098    449    802       C  
ATOM   1481  C   LYS A 260     -45.114  44.870  -7.866  1.00 95.70           C  
ANISOU 1481  C   LYS A 260    12639  14155   9566  -1205    346    800       C  
ATOM   1482  O   LYS A 260     -44.488  45.927  -7.856  1.00 96.86           O  
ANISOU 1482  O   LYS A 260    12789  14275   9740  -1389    341    897       O  
ATOM   1483  CB  LYS A 260     -46.115  44.480 -10.165  1.00 97.36           C  
ANISOU 1483  CB  LYS A 260    12972  14454   9565  -1072    436    861       C  
ATOM   1484  CG  LYS A 260     -45.724  44.154 -11.597  1.00113.40           C  
ANISOU 1484  CG  LYS A 260    14967  16679  11441  -1061    549    921       C  
ATOM   1485  CD  LYS A 260     -46.157  45.259 -12.553  1.00125.54           C  
ANISOU 1485  CD  LYS A 260    16624  18174  12901  -1178    553   1092       C  
ATOM   1486  CE  LYS A 260     -45.953  44.986 -14.026  1.00136.70           C  
ANISOU 1486  CE  LYS A 260    18049  19767  14123  -1136    645   1146       C  
ATOM   1487  NZ  LYS A 260     -44.626  44.383 -14.338  1.00149.61           N  
ANISOU 1487  NZ  LYS A 260    19503  21656  15686  -1150    790   1134       N  
ATOM   1488  N   LEU A 261     -45.803  44.415  -6.799  1.00 88.38           N  
ANISOU 1488  N   LEU A 261    11751  13122   8709  -1101    269    686       N  
ATOM   1489  CA  LEU A 261     -45.877  45.135  -5.528  1.00 87.29           C  
ANISOU 1489  CA  LEU A 261    11660  12839   8667  -1180    173    656       C  
ATOM   1490  C   LEU A 261     -44.607  44.965  -4.689  1.00 92.56           C  
ANISOU 1490  C   LEU A 261    12159  13632   9376  -1267    168    640       C  
ATOM   1491  O   LEU A 261     -44.196  45.925  -4.043  1.00 93.15           O  
ANISOU 1491  O   LEU A 261    12253  13635   9506  -1427    107    658       O  
ATOM   1492  CB  LEU A 261     -47.108  44.700  -4.735  1.00 85.23           C  
ANISOU 1492  CB  LEU A 261    11493  12450   8442  -1035    107    547       C  
ATOM   1493  CG  LEU A 261     -48.338  45.591  -4.782  1.00 89.10           C  
ANISOU 1493  CG  LEU A 261    12163  12742   8951  -1015     44    554       C  
ATOM   1494  CD1 LEU A 261     -49.069  45.530  -6.099  1.00 89.39           C  
ANISOU 1494  CD1 LEU A 261    12266  12786   8910   -947     75    613       C  
ATOM   1495  CD2 LEU A 261     -49.290  45.208  -3.710  1.00 89.54           C  
ANISOU 1495  CD2 LEU A 261    12258  12715   9047   -899    -10    441       C  
ATOM   1496  N   VAL A 262     -43.967  43.766  -4.728  1.00 89.23           N  
ANISOU 1496  N   VAL A 262    11576  13399   8928  -1161    227    606       N  
ATOM   1497  CA  VAL A 262     -42.717  43.477  -4.006  1.00 89.86           C  
ANISOU 1497  CA  VAL A 262    11461  13644   9037  -1207    221    601       C  
ATOM   1498  C   VAL A 262     -41.566  44.397  -4.500  1.00 97.63           C  
ANISOU 1498  C   VAL A 262    12331  14750  10016  -1429    258    708       C  
ATOM   1499  O   VAL A 262     -40.614  44.628  -3.758  1.00 97.83           O  
ANISOU 1499  O   VAL A 262    12213  14878  10079  -1544    213    711       O  
ATOM   1500  CB  VAL A 262     -42.345  41.964  -3.985  1.00 92.80           C  
ANISOU 1500  CB  VAL A 262    11703  14171   9386  -1005    279    549       C  
ATOM   1501  CG1 VAL A 262     -41.817  41.472  -5.321  1.00 93.41           C  
ANISOU 1501  CG1 VAL A 262    11688  14416   9387   -953    411    590       C  
ATOM   1502  CG2 VAL A 262     -41.351  41.651  -2.879  1.00 93.41           C  
ANISOU 1502  CG2 VAL A 262    11609  14380   9503  -1008    227    534       C  
ATOM   1503  N   ALA A 263     -41.697  44.965  -5.722  1.00 97.26           N  
ANISOU 1503  N   ALA A 263    12351  14689   9915  -1504    330    801       N  
ATOM   1504  CA  ALA A 263     -40.738  45.913  -6.302  1.00100.22           C  
ANISOU 1504  CA  ALA A 263    12648  15154  10277  -1740    379    927       C  
ATOM   1505  C   ALA A 263     -40.766  47.219  -5.502  1.00107.39           C  
ANISOU 1505  C   ALA A 263    13669  15865  11270  -1957    269    943       C  
ATOM   1506  O   ALA A 263     -39.715  47.819  -5.265  1.00109.34           O  
ANISOU 1506  O   ALA A 263    13791  16204  11549  -2178    262    994       O  
ATOM   1507  CB  ALA A 263     -41.088  46.189  -7.752  1.00101.44           C  
ANISOU 1507  CB  ALA A 263    12897  15309  10336  -1746    476   1029       C  
ATOM   1508  N   ILE A 264     -41.976  47.626  -5.063  1.00103.82           N  
ANISOU 1508  N   ILE A 264    13445  15147  10854  -1890    184    886       N  
ATOM   1509  CA  ILE A 264     -42.234  48.815  -4.250  1.00104.77           C  
ANISOU 1509  CA  ILE A 264    13723  15031  11052  -2043     77    866       C  
ATOM   1510  C   ILE A 264     -41.720  48.590  -2.813  1.00110.72           C  
ANISOU 1510  C   ILE A 264    14371  15840  11856  -2076    -16    751       C  
ATOM   1511  O   ILE A 264     -40.968  49.430  -2.310  1.00112.53           O  
ANISOU 1511  O   ILE A 264    14573  16054  12130  -2308    -72    759       O  
ATOM   1512  CB  ILE A 264     -43.739  49.225  -4.309  1.00106.39           C  
ANISOU 1512  CB  ILE A 264    14189  14967  11267  -1910     31    838       C  
ATOM   1513  CG1 ILE A 264     -44.206  49.465  -5.760  1.00106.72           C  
ANISOU 1513  CG1 ILE A 264    14327  14983  11240  -1878    107    967       C  
ATOM   1514  CG2 ILE A 264     -44.034  50.445  -3.427  1.00108.26           C  
ANISOU 1514  CG2 ILE A 264    14608  14942  11584  -2034    -73    796       C  
ATOM   1515  CD1 ILE A 264     -45.632  49.033  -6.052  1.00109.15           C  
ANISOU 1515  CD1 ILE A 264    14762  15197  11513  -1642     91    922       C  
ATOM   1516  N   ILE A 265     -42.101  47.449  -2.175  1.00106.65           N  
ANISOU 1516  N   ILE A 265    13799  15397  11325  -1857    -34    650       N  
ATOM   1517  CA  ILE A 265     -41.717  47.022  -0.808  1.00106.77           C  
ANISOU 1517  CA  ILE A 265    13718  15492  11360  -1836   -122    550       C  
ATOM   1518  C   ILE A 265     -40.188  47.011  -0.633  1.00113.67           C  
ANISOU 1518  C   ILE A 265    14340  16615  12237  -2001   -127    591       C  
ATOM   1519  O   ILE A 265     -39.691  47.315   0.454  1.00114.26           O  
ANISOU 1519  O   ILE A 265    14360  16721  12331  -2111   -231    531       O  
ATOM   1520  CB  ILE A 265     -42.363  45.644  -0.466  1.00107.98           C  
ANISOU 1520  CB  ILE A 265    13844  15700  11483  -1563   -107    481       C  
ATOM   1521  CG1 ILE A 265     -43.879  45.690  -0.820  1.00107.16           C  
ANISOU 1521  CG1 ILE A 265    13945  15398  11373  -1416    -88    452       C  
ATOM   1522  CG2 ILE A 265     -42.099  45.220   1.009  1.00108.36           C  
ANISOU 1522  CG2 ILE A 265    13832  15806  11534  -1526   -204    394       C  
ATOM   1523  CD1 ILE A 265     -44.490  44.668  -0.938  1.00116.18           C  
ANISOU 1523  CD1 ILE A 265    15052  16607  12483  -1235    -28    439       C  
ATOM   1524  N   MET A 266     -39.458  46.693  -1.727  1.00111.67           N  
ANISOU 1524  N   MET A 266    13924  16553  11951  -2015    -13    690       N  
ATOM   1525  CA  MET A 266     -38.001  46.629  -1.804  1.00113.76           C  
ANISOU 1525  CA  MET A 266    13908  17102  12211  -2154     15    748       C  
ATOM   1526  C   MET A 266     -37.301  47.958  -1.538  1.00118.98           C  
ANISOU 1526  C   MET A 266    14554  17733  12918  -2498    -49    787       C  
ATOM   1527  O   MET A 266     -36.177  47.955  -1.037  1.00120.12           O  
ANISOU 1527  O   MET A 266    14463  18103  13073  -2629    -91    788       O  
ATOM   1528  CB  MET A 266     -37.567  46.056  -3.152  1.00116.94           C  
ANISOU 1528  CB  MET A 266    14178  17697  12556  -2077    175    841       C  
ATOM   1529  CG  MET A 266     -37.251  44.597  -3.085  1.00120.56           C  
ANISOU 1529  CG  MET A 266    14463  18362  12981  -1807    223    797       C  
ATOM   1530  SD  MET A 266     -36.697  43.951  -4.672  1.00126.46           S  
ANISOU 1530  SD  MET A 266    15061  19343  13644  -1708    422    878       S  
ATOM   1531  CE  MET A 266     -35.857  42.476  -4.114  1.00123.60           C  
ANISOU 1531  CE  MET A 266    14436  19249  13279  -1447    438    819       C  
ATOM   1532  N   TRP A 267     -37.946  49.084  -1.877  1.00115.51           N  
ANISOU 1532  N   TRP A 267    14364  17017  12509  -2644    -60    820       N  
ATOM   1533  CA  TRP A 267     -37.367  50.401  -1.640  1.00117.82           C  
ANISOU 1533  CA  TRP A 267    14695  17216  12857  -2988   -121    853       C  
ATOM   1534  C   TRP A 267     -37.474  50.817  -0.184  1.00120.17           C  
ANISOU 1534  C   TRP A 267    15072  17393  13195  -3063   -284    708       C  
ATOM   1535  O   TRP A 267     -36.680  51.637   0.277  1.00122.39           O  
ANISOU 1535  O   TRP A 267    15299  17691  13514  -3355   -359    698       O  
ATOM   1536  CB  TRP A 267     -37.942  51.455  -2.595  1.00117.85           C  
ANISOU 1536  CB  TRP A 267    14948  16953  12875  -3108    -67    960       C  
ATOM   1537  CG  TRP A 267     -37.446  51.274  -3.995  1.00119.98           C  
ANISOU 1537  CG  TRP A 267    15096  17405  13086  -3142     90   1123       C  
ATOM   1538  CD1 TRP A 267     -38.163  50.831  -5.067  1.00121.97           C  
ANISOU 1538  CD1 TRP A 267    15436  17638  13268  -2942    193   1189       C  
ATOM   1539  CD2 TRP A 267     -36.091  51.405  -4.448  1.00122.94           C  
ANISOU 1539  CD2 TRP A 267    15204  18059  13448  -3375    165   1229       C  
ATOM   1540  NE1 TRP A 267     -37.348  50.714  -6.167  1.00123.18           N  
ANISOU 1540  NE1 TRP A 267    15419  18030  13355  -3032    333   1327       N  
ATOM   1541  CE2 TRP A 267     -36.069  51.067  -5.816  1.00127.07           C  
ANISOU 1541  CE2 TRP A 267    15685  18712  13885  -3296    327   1360       C  
ATOM   1542  CE3 TRP A 267     -34.891  51.806  -3.830  1.00126.70           C  
ANISOU 1542  CE3 TRP A 267    15464  18707  13971  -3655    111   1225       C  
ATOM   1543  CZ2 TRP A 267     -34.899  51.120  -6.584  1.00129.01           C  
ANISOU 1543  CZ2 TRP A 267    15680  19252  14086  -3479    452   1491       C  
ATOM   1544  CZ3 TRP A 267     -33.731  51.842  -4.586  1.00130.81           C  
ANISOU 1544  CZ3 TRP A 267    15715  19525  14460  -3842    226   1357       C  
ATOM   1545  CH2 TRP A 267     -33.742  51.508  -5.947  1.00131.55           C  
ANISOU 1545  CH2 TRP A 267    15774  19743  14466  -3751    404   1491       C  
ATOM   1546  N   TYR A 268     -38.426  50.231   0.546  1.00113.00           N  
ANISOU 1546  N   TYR A 268    14285  16382  12269  -2811   -338    593       N  
ATOM   1547  CA  TYR A 268     -38.614  50.509   1.960  1.00112.36           C  
ANISOU 1547  CA  TYR A 268    14286  16209  12196  -2840   -483    445       C  
ATOM   1548  C   TYR A 268     -37.662  49.665   2.793  1.00115.76           C  
ANISOU 1548  C   TYR A 268    14436  16961  12586  -2810   -546    402       C  
ATOM   1549  O   TYR A 268     -37.266  50.101   3.874  1.00116.63           O  
ANISOU 1549  O   TYR A 268    14532  17091  12691  -2955   -678    306       O  
ATOM   1550  CB  TYR A 268     -40.065  50.242   2.368  1.00111.15           C  
ANISOU 1550  CB  TYR A 268    14369  15834  12028  -2582   -496    355       C  
ATOM   1551  CG  TYR A 268     -40.367  50.615   3.801  1.00113.28           C  
ANISOU 1551  CG  TYR A 268    14757  15998  12287  -2605   -629    197       C  
ATOM   1552  CD1 TYR A 268     -40.607  51.938   4.162  1.00116.79           C  
ANISOU 1552  CD1 TYR A 268    15427  16175  12775  -2792   -700    127       C  
ATOM   1553  CD2 TYR A 268     -40.408  49.648   4.799  1.00113.26           C  
ANISOU 1553  CD2 TYR A 268    14655  16156  12222  -2434   -682    118       C  
ATOM   1554  CE1 TYR A 268     -40.869  52.291   5.485  1.00118.35           C  
ANISOU 1554  CE1 TYR A 268    15742  16284  12944  -2807   -817    -39       C  
ATOM   1555  CE2 TYR A 268     -40.660  49.989   6.127  1.00114.80           C  
ANISOU 1555  CE2 TYR A 268    14958  16281  12379  -2456   -800    -28       C  
ATOM   1556  CZ  TYR A 268     -40.892  51.313   6.466  1.00123.36           C  
ANISOU 1556  CZ  TYR A 268    16261  17113  13497  -2641   -866   -116       C  
ATOM   1557  OH  TYR A 268     -41.166  51.656   7.767  1.00123.42           O  
ANISOU 1557  OH  TYR A 268    16389  17056  13450  -2654   -976   -279       O  
ATOM   1558  N   ALA A 269     -37.299  48.462   2.286  1.00111.09           N  
ANISOU 1558  N   ALA A 269    13630  16619  11960  -2612   -457    470       N  
ATOM   1559  CA  ALA A 269     -36.420  47.481   2.936  1.00111.25           C  
ANISOU 1559  CA  ALA A 269    13373  16956  11940  -2511   -501    456       C  
ATOM   1560  C   ALA A 269     -35.171  48.079   3.632  1.00118.45           C  
ANISOU 1560  C   ALA A 269    14078  18072  12857  -2789   -618    438       C  
ATOM   1561  O   ALA A 269     -35.035  47.790   4.819  1.00118.61           O  
ANISOU 1561  O   ALA A 269    14054  18176  12836  -2741   -746    350       O  
ATOM   1562  CB  ALA A 269     -36.025  46.377   1.969  1.00111.42           C  
ANISOU 1562  CB  ALA A 269    13198  17195  11941  -2312   -362    550       C  
ATOM   1563  N   PRO A 270     -34.298  48.943   3.024  1.00117.31           N  
ANISOU 1563  N   PRO A 270    13815  18005  12753  -3097   -592    512       N  
ATOM   1564  CA  PRO A 270     -33.159  49.488   3.803  1.00119.90           C  
ANISOU 1564  CA  PRO A 270    13937  18536  13084  -3382   -725    476       C  
ATOM   1565  C   PRO A 270     -33.555  50.229   5.088  1.00123.16           C  
ANISOU 1565  C   PRO A 270    14557  18752  13487  -3513   -902    319       C  
ATOM   1566  O   PRO A 270     -32.880  50.067   6.100  1.00124.07           O  
ANISOU 1566  O   PRO A 270    14501  19084  13556  -3569  -1041    249       O  
ATOM   1567  CB  PRO A 270     -32.439  50.413   2.812  1.00124.22           C  
ANISOU 1567  CB  PRO A 270    14399  19113  13685  -3714   -644    589       C  
ATOM   1568  CG  PRO A 270     -32.886  49.986   1.480  1.00127.22           C  
ANISOU 1568  CG  PRO A 270    14828  19450  14062  -3537   -455    707       C  
ATOM   1569  CD  PRO A 270     -34.272  49.441   1.632  1.00119.46           C  
ANISOU 1569  CD  PRO A 270    14123  18210  13058  -3215   -445    639       C  
ATOM   1570  N   LEU A 271     -34.659  51.010   5.061  1.00117.90           N  
ANISOU 1570  N   LEU A 271    14256  17689  12853  -3537   -898    260       N  
ATOM   1571  CA  LEU A 271     -35.165  51.748   6.225  1.00117.78           C  
ANISOU 1571  CA  LEU A 271    14476  17456  12821  -3630  -1046     92       C  
ATOM   1572  C   LEU A 271     -35.676  50.768   7.291  1.00119.34           C  
ANISOU 1572  C   LEU A 271    14679  17738  12926  -3329  -1113     -3       C  
ATOM   1573  O   LEU A 271     -35.414  50.966   8.479  1.00120.70           O  
ANISOU 1573  O   LEU A 271    14845  17979  13035  -3411  -1264   -127       O  
ATOM   1574  CB  LEU A 271     -36.273  52.735   5.814  1.00117.26           C  
ANISOU 1574  CB  LEU A 271    14791  16947  12815  -3680  -1005     63       C  
ATOM   1575  CG  LEU A 271     -36.508  53.910   6.757  1.00123.62           C  
ANISOU 1575  CG  LEU A 271    15848  17502  13622  -3865  -1148   -116       C  
ATOM   1576  CD1 LEU A 271     -36.646  55.195   5.987  1.00127.12           C  
ANISOU 1576  CD1 LEU A 271    16372  17776  14151  -4278  -1176    -98       C  
ATOM   1577  CD2 LEU A 271     -37.728  53.684   7.632  1.00124.20           C  
ANISOU 1577  CD2 LEU A 271    16253  17248  13688  -3625  -1122   -202       C  
ATOM   1578  N   GLY A 272     -36.371  49.722   6.845  1.00112.18           N  
ANISOU 1578  N   GLY A 272    13785  16836  12004  -3001  -1001     60       N  
ATOM   1579  CA  GLY A 272     -36.930  48.677   7.695  1.00109.79           C  
ANISOU 1579  CA  GLY A 272    13497  16597  11621  -2703  -1032      8       C  
ATOM   1580  C   GLY A 272     -35.883  47.805   8.360  1.00113.48           C  
ANISOU 1580  C   GLY A 272    13662  17436  12021  -2643  -1114     31       C  
ATOM   1581  O   GLY A 272     -35.936  47.634   9.577  1.00112.92           O  
ANISOU 1581  O   GLY A 272    13613  17430  11862  -2597  -1239    -60       O  
ATOM   1582  N   ILE A 273     -34.913  47.260   7.570  1.00110.18           N  
ANISOU 1582  N   ILE A 273    12954  17278  11632  -2631  -1044    155       N  
ATOM   1583  CA  ILE A 273     -33.812  46.395   8.045  1.00110.92           C  
ANISOU 1583  CA  ILE A 273    12715  17756  11672  -2544  -1110    202       C  
ATOM   1584  C   ILE A 273     -32.991  47.103   9.121  1.00116.19           C  
ANISOU 1584  C   ILE A 273    13271  18589  12289  -2806  -1305    115       C  
ATOM   1585  O   ILE A 273     -32.659  46.478  10.126  1.00116.34           O  
ANISOU 1585  O   ILE A 273    13170  18817  12215  -2682  -1424     91       O  
ATOM   1586  CB  ILE A 273     -32.919  45.828   6.890  1.00114.86           C  
ANISOU 1586  CB  ILE A 273    12922  18502  12218  -2491   -980    341       C  
ATOM   1587  CG1 ILE A 273     -33.746  45.095   5.786  1.00112.86           C  
ANISOU 1587  CG1 ILE A 273    12796  18088  11997  -2232   -792    407       C  
ATOM   1588  CG2 ILE A 273     -31.769  44.939   7.415  1.00117.21           C  
ANISOU 1588  CG2 ILE A 273    12862  19208  12463  -2366  -1054    389       C  
ATOM   1589  CD1 ILE A 273     -34.525  43.817   6.182  1.00118.60           C  
ANISOU 1589  CD1 ILE A 273    13624  18756  12681  -1863   -769    398       C  
ATOM   1590  N   LEU A 274     -32.710  48.410   8.927  1.00113.69           N  
ANISOU 1590  N   LEU A 274    13011  18160  12025  -3171  -1343     67       N  
ATOM   1591  CA  LEU A 274     -31.973  49.251   9.874  1.00116.09           C  
ANISOU 1591  CA  LEU A 274    13242  18577  12288  -3484  -1533    -41       C  
ATOM   1592  C   LEU A 274     -32.646  49.199  11.253  1.00119.14           C  
ANISOU 1592  C   LEU A 274    13835  18872  12562  -3380  -1672   -191       C  
ATOM   1593  O   LEU A 274     -31.994  48.817  12.221  1.00120.29           O  
ANISOU 1593  O   LEU A 274    13796  19304  12603  -3365  -1822   -226       O  
ATOM   1594  CB  LEU A 274     -31.893  50.706   9.357  1.00117.70           C  
ANISOU 1594  CB  LEU A 274    13591  18544  12585  -3880  -1524    -76       C  
ATOM   1595  CG  LEU A 274     -30.912  51.661  10.053  1.00126.03           C  
ANISOU 1595  CG  LEU A 274    14528  19730  13626  -4289  -1703   -173       C  
ATOM   1596  CD1 LEU A 274     -30.321  52.628   9.063  1.00128.28           C  
ANISOU 1596  CD1 LEU A 274    14763  19950  14027  -4656  -1632    -95       C  
ATOM   1597  CD2 LEU A 274     -31.591  52.450  11.160  1.00128.69           C  
ANISOU 1597  CD2 LEU A 274    15195  19797  13906  -4391  -1846   -380       C  
ATOM   1598  N   PHE A 275     -33.953  49.533  11.321  1.00113.42           N  
ANISOU 1598  N   PHE A 275    13477  17773  11844  -3285  -1617   -269       N  
ATOM   1599  CA  PHE A 275     -34.737  49.561  12.557  1.00112.63           C  
ANISOU 1599  CA  PHE A 275    13604  17561  11630  -3181  -1716   -417       C  
ATOM   1600  C   PHE A 275     -35.109  48.183  13.105  1.00115.34           C  
ANISOU 1600  C   PHE A 275    13893  18057  11873  -2811  -1701   -362       C  
ATOM   1601  O   PHE A 275     -35.261  48.040  14.319  1.00115.71           O  
ANISOU 1601  O   PHE A 275    14001  18179  11784  -2756  -1823   -456       O  
ATOM   1602  CB  PHE A 275     -35.988  50.432  12.388  1.00112.97           C  
ANISOU 1602  CB  PHE A 275    14035  17168  11722  -3202  -1648   -516       C  
ATOM   1603  CG  PHE A 275     -35.686  51.910  12.414  1.00116.96           C  
ANISOU 1603  CG  PHE A 275    14674  17483  12281  -3577  -1726   -628       C  
ATOM   1604  CD1 PHE A 275     -35.375  52.593  11.247  1.00120.59           C  
ANISOU 1604  CD1 PHE A 275    15126  17814  12878  -3785  -1638   -536       C  
ATOM   1605  CD2 PHE A 275     -35.712  52.619  13.606  1.00121.22           C  
ANISOU 1605  CD2 PHE A 275    15363  17967  12728  -3730  -1884   -828       C  
ATOM   1606  CE1 PHE A 275     -35.090  53.958  11.272  1.00124.25           C  
ANISOU 1606  CE1 PHE A 275    15736  18071  13402  -4148  -1708   -628       C  
ATOM   1607  CE2 PHE A 275     -35.429  53.986  13.631  1.00126.76           C  
ANISOU 1607  CE2 PHE A 275    16216  18459  13489  -4088  -1957   -945       C  
ATOM   1608  CZ  PHE A 275     -35.118  54.646  12.464  1.00125.44           C  
ANISOU 1608  CZ  PHE A 275    16046  18140  13474  -4300  -1869   -838       C  
ATOM   1609  N   LEU A 276     -35.261  47.177  12.223  1.00110.43           N  
ANISOU 1609  N   LEU A 276    13174  17474  11310  -2566  -1553   -212       N  
ATOM   1610  CA  LEU A 276     -35.617  45.799  12.597  1.00108.91           C  
ANISOU 1610  CA  LEU A 276    12946  17388  11046  -2215  -1519   -138       C  
ATOM   1611  C   LEU A 276     -34.461  45.135  13.350  1.00115.07           C  
ANISOU 1611  C   LEU A 276    13430  18559  11733  -2168  -1655    -88       C  
ATOM   1612  O   LEU A 276     -34.710  44.401  14.308  1.00114.31           O  
ANISOU 1612  O   LEU A 276    13367  18549  11518  -1969  -1720    -85       O  
ATOM   1613  CB  LEU A 276     -35.949  44.959  11.345  1.00106.92           C  
ANISOU 1613  CB  LEU A 276    12662  17070  10893  -2002  -1329     -4       C  
ATOM   1614  CG  LEU A 276     -37.349  44.376  11.110  1.00108.93           C  
ANISOU 1614  CG  LEU A 276    13165  17064  11161  -1764  -1202      2       C  
ATOM   1615  CD1 LEU A 276     -37.573  44.195   9.634  1.00107.98           C  
ANISOU 1615  CD1 LEU A 276    13041  16833  11155  -1721  -1037     85       C  
ATOM   1616  CD2 LEU A 276     -37.568  43.051  11.801  1.00110.73           C  
ANISOU 1616  CD2 LEU A 276    13367  17396  11308  -1471  -1204     61       C  
ATOM   1617  N   ILE A 277     -33.205  45.395  12.927  1.00114.17           N  
ANISOU 1617  N   ILE A 277    13019  18697  11665  -2349  -1700    -39       N  
ATOM   1618  CA  ILE A 277     -32.027  44.805  13.566  1.00116.57           C  
ANISOU 1618  CA  ILE A 277    12996  19412  11886  -2301  -1837     17       C  
ATOM   1619  C   ILE A 277     -31.560  45.649  14.761  1.00123.90           C  
ANISOU 1619  C   ILE A 277    13908  20471  12698  -2565  -2061   -122       C  
ATOM   1620  O   ILE A 277     -31.096  45.073  15.746  1.00125.46           O  
ANISOU 1620  O   ILE A 277    13968  20940  12760  -2449  -2206   -109       O  
ATOM   1621  CB  ILE A 277     -30.871  44.458  12.579  1.00121.11           C  
ANISOU 1621  CB  ILE A 277    13204  20263  12551  -2309  -1770    148       C  
ATOM   1622  CG1 ILE A 277     -30.144  45.699  12.047  1.00123.82           C  
ANISOU 1622  CG1 ILE A 277    13426  20648  12972  -2723  -1792    108       C  
ATOM   1623  CG2 ILE A 277     -31.339  43.560  11.434  1.00119.55           C  
ANISOU 1623  CG2 ILE A 277    13039  19941  12443  -2028  -1551    264       C  
ATOM   1624  CD1 ILE A 277     -28.716  45.644  12.285  1.00135.94           C  
ANISOU 1624  CD1 ILE A 277    14550  22623  14479  -2845  -1913    151       C  
ATOM   1625  N   ALA A 278     -31.699  46.998  14.685  1.00121.30           N  
ANISOU 1625  N   ALA A 278    13735  19940  12413  -2913  -2095   -256       N  
ATOM   1626  CA  ALA A 278     -31.304  47.923  15.758  1.00123.88           C  
ANISOU 1626  CA  ALA A 278    14091  20343  12635  -3204  -2306   -424       C  
ATOM   1627  C   ALA A 278     -32.125  47.699  17.026  1.00127.04           C  
ANISOU 1627  C   ALA A 278    14736  20670  12864  -3040  -2393   -533       C  
ATOM   1628  O   ALA A 278     -31.568  47.760  18.121  1.00129.66           O  
ANISOU 1628  O   ALA A 278    14974  21251  13041  -3117  -2590   -610       O  
ATOM   1629  CB  ALA A 278     -31.427  49.368  15.300  1.00125.55           C  
ANISOU 1629  CB  ALA A 278    14482  20270  12951  -3581  -2292   -541       C  
ATOM   1630  N   GLY A 279     -33.419  47.416  16.859  1.00119.78           N  
ANISOU 1630  N   GLY A 279    14109  19439  11962  -2815  -2246   -532       N  
ATOM   1631  CA  GLY A 279     -34.344  47.142  17.952  1.00118.55           C  
ANISOU 1631  CA  GLY A 279    14195  19200  11648  -2636  -2282   -616       C  
ATOM   1632  C   GLY A 279     -34.027  45.853  18.681  1.00122.48           C  
ANISOU 1632  C   GLY A 279    14527  20004  12005  -2355  -2346   -495       C  
ATOM   1633  O   GLY A 279     -34.058  45.820  19.915  1.00123.97           O  
ANISOU 1633  O   GLY A 279    14777  20325  12001  -2335  -2488   -574       O  
ATOM   1634  N   LYS A 280     -33.688  44.787  17.923  1.00117.18           N  
ANISOU 1634  N   LYS A 280    13652  19449  11421  -2131  -2245   -300       N  
ATOM   1635  CA  LYS A 280     -33.352  43.481  18.491  1.00116.98           C  
ANISOU 1635  CA  LYS A 280    13475  19685  11287  -1832  -2292   -156       C  
ATOM   1636  C   LYS A 280     -32.027  43.459  19.238  1.00124.11           C  
ANISOU 1636  C   LYS A 280    14071  21014  12070  -1920  -2514   -143       C  
ATOM   1637  O   LYS A 280     -31.864  42.615  20.121  1.00125.21           O  
ANISOU 1637  O   LYS A 280    14156  21364  12056  -1702  -2609    -63       O  
ATOM   1638  CB  LYS A 280     -33.415  42.369  17.448  1.00117.30           C  
ANISOU 1638  CB  LYS A 280    13419  19687  11461  -1556  -2114     28       C  
ATOM   1639  CG  LYS A 280     -34.812  41.785  17.339  1.00130.04           C  
ANISOU 1639  CG  LYS A 280    15332  20989  13089  -1333  -1952     54       C  
ATOM   1640  CD  LYS A 280     -35.053  40.632  18.299  1.00142.29           C  
ANISOU 1640  CD  LYS A 280    16925  22645  14492  -1047  -1992    156       C  
ATOM   1641  CE  LYS A 280     -36.456  40.099  18.155  1.00153.51           C  
ANISOU 1641  CE  LYS A 280    18632  23758  15937   -873  -1824    179       C  
ATOM   1642  NZ  LYS A 280     -36.767  39.077  19.187  1.00164.82           N  
ANISOU 1642  NZ  LYS A 280    20142  25270  17212   -637  -1860    280       N  
ATOM   1643  N   ILE A 281     -31.100  44.398  18.936  1.00121.81           N  
ANISOU 1643  N   ILE A 281    13586  20857  11839  -2247  -2605   -218       N  
ATOM   1644  CA  ILE A 281     -29.829  44.470  19.663  1.00124.72           C  
ANISOU 1644  CA  ILE A 281    13637  21660  12091  -2372  -2836   -224       C  
ATOM   1645  C   ILE A 281     -29.980  45.400  20.890  1.00129.18           C  
ANISOU 1645  C   ILE A 281    14377  22231  12475  -2618  -3031   -437       C  
ATOM   1646  O   ILE A 281     -29.004  45.633  21.603  1.00132.47           O  
ANISOU 1646  O   ILE A 281    14566  22997  12769  -2777  -3252   -483       O  
ATOM   1647  CB  ILE A 281     -28.578  44.764  18.782  1.00129.75           C  
ANISOU 1647  CB  ILE A 281    13892  22541  12867  -2572  -2846   -165       C  
ATOM   1648  CG1 ILE A 281     -28.505  46.217  18.313  1.00130.96           C  
ANISOU 1648  CG1 ILE A 281    14124  22508  13125  -3019  -2844   -318       C  
ATOM   1649  CG2 ILE A 281     -28.482  43.792  17.603  1.00128.52           C  
ANISOU 1649  CG2 ILE A 281    13586  22382  12863  -2292  -2640     29       C  
ATOM   1650  CD1 ILE A 281     -27.160  46.572  17.788  1.00141.73           C  
ANISOU 1650  CD1 ILE A 281    15086  24194  14572  -3275  -2906   -273       C  
ATOM   1651  N   VAL A 282     -31.222  45.884  21.144  1.00122.50           N  
ANISOU 1651  N   VAL A 282    13930  21013  11602  -2630  -2950   -569       N  
ATOM   1652  CA  VAL A 282     -31.626  46.690  22.304  1.00136.95           C  
ANISOU 1652  CA  VAL A 282    16003  22784  13249  -2798  -3091   -789       C  
ATOM   1653  C   VAL A 282     -32.577  45.808  23.130  1.00148.86           C  
ANISOU 1653  C   VAL A 282    17720  24253  14587  -2458  -3046   -738       C  
ATOM   1654  O   VAL A 282     -32.172  44.819  23.737  1.00111.27           O  
ANISOU 1654  O   VAL A 282    12805  19793   9678  -2244  -3140   -608       O  
ATOM   1655  CB  VAL A 282     -32.299  48.044  21.922  1.00140.06           C  
ANISOU 1655  CB  VAL A 282    16696  22770  13752  -3080  -3018   -992       C  
ATOM   1656  CG1 VAL A 282     -32.844  48.767  23.155  1.00141.35           C  
ANISOU 1656  CG1 VAL A 282    17148  22846  13712  -3187  -3138  -1232       C  
ATOM   1657  CG2 VAL A 282     -31.335  48.953  21.170  1.00141.84           C  
ANISOU 1657  CG2 VAL A 282    16731  23029  14134  -3452  -3068  -1030       C  
ATOM   1658  N   GLY A 291     -24.432  30.088  31.709  1.00186.47           N  
ANISOU 1658  N   GLY A 291    20174  33318  17357   2277  -4773   2570       N  
ATOM   1659  CA  GLY A 291     -23.497  31.203  31.743  1.00188.83           C  
ANISOU 1659  CA  GLY A 291    20076  34042  17629   1947  -4983   2359       C  
ATOM   1660  C   GLY A 291     -22.634  31.284  30.502  1.00192.93           C  
ANISOU 1660  C   GLY A 291    20225  34611  18467   1955  -4886   2324       C  
ATOM   1661  O   GLY A 291     -23.160  31.396  29.390  1.00188.05           O  
ANISOU 1661  O   GLY A 291    19748  33583  18119   1876  -4611   2237       O  
ATOM   1662  N   GLY A 292     -21.314  31.205  30.701  1.00195.02           N  
ANISOU 1662  N   GLY A 292    20008  35404  18688   2061  -5112   2402       N  
ATOM   1663  CA  GLY A 292     -20.305  31.255  29.642  1.00195.56           C  
ANISOU 1663  CA  GLY A 292    19643  35639  19020   2093  -5049   2391       C  
ATOM   1664  C   GLY A 292     -20.368  30.101  28.658  1.00196.48           C  
ANISOU 1664  C   GLY A 292    19807  35468  19379   2551  -4799   2594       C  
ATOM   1665  O   GLY A 292     -19.842  30.208  27.545  1.00195.26           O  
ANISOU 1665  O   GLY A 292    19357  35370  19465   2582  -4679   2567       O  
ATOM   1666  N   GLN A 293     -21.009  28.982  29.078  1.00192.79           N  
ANISOU 1666  N   GLN A 293    19721  34690  18841   2902  -4716   2799       N  
ATOM   1667  CA  GLN A 293     -21.216  27.775  28.277  1.00191.25           C  
ANISOU 1667  CA  GLN A 293    19670  34141  18853   3343  -4478   2993       C  
ATOM   1668  C   GLN A 293     -22.140  28.076  27.106  1.00189.38           C  
ANISOU 1668  C   GLN A 293    19690  33384  18880   3131  -4154   2817       C  
ATOM   1669  O   GLN A 293     -21.841  27.659  25.984  1.00188.25           O  
ANISOU 1669  O   GLN A 293    19409  33131  18985   3301  -3973   2833       O  
ATOM   1670  CB  GLN A 293     -21.754  26.620  29.131  1.00193.59           C  
ANISOU 1670  CB  GLN A 293    20319  34258  18977   3721  -4504   3262       C  
ATOM   1671  CG  GLN A 293     -20.673  25.945  29.971  1.00209.83           C  
ANISOU 1671  CG  GLN A 293    22631  35691  21404   3694  -4857   3246       C  
ATOM   1672  CD  GLN A 293     -21.062  24.556  30.408  1.00225.04           C  
ANISOU 1672  CD  GLN A 293    25537  35919  24047   3583  -4922   3206       C  
ATOM   1673  OE1 GLN A 293     -21.256  23.648  29.590  1.00221.93           O  
ANISOU 1673  OE1 GLN A 293    25044  35587  23693   3981  -4710   3401       O  
ATOM   1674  NE2 GLN A 293     -21.137  24.348  31.713  1.00220.61           N  
ANISOU 1674  NE2 GLN A 293    24996  35790  23034   3735  -5125   3410       N  
ATOM   1675  N   LEU A 294     -23.231  28.858  27.354  1.00182.67           N  
ANISOU 1675  N   LEU A 294    19191  32247  17967   2751  -4088   2635       N  
ATOM   1676  CA  LEU A 294     -24.172  29.321  26.321  1.00177.57           C  
ANISOU 1676  CA  LEU A 294    18784  31140  17544   2495  -3811   2446       C  
ATOM   1677  C   LEU A 294     -23.457  30.251  25.334  1.00180.15           C  
ANISOU 1677  C   LEU A 294    18732  31668  18047   2230  -3791   2266       C  
ATOM   1678  O   LEU A 294     -23.968  30.499  24.241  1.00176.53           O  
ANISOU 1678  O   LEU A 294    18350  30903  17819   2133  -3553   2165       O  
ATOM   1679  CB  LEU A 294     -25.385  30.032  26.941  1.00175.10           C  
ANISOU 1679  CB  LEU A 294    18844  30590  17094   2139  -3796   2280       C  
ATOM   1680  CG  LEU A 294     -26.418  29.123  27.592  1.00179.24           C  
ANISOU 1680  CG  LEU A 294    19798  30831  17475   2337  -3739   2435       C  
ATOM   1681  CD1 LEU A 294     -27.021  29.778  28.816  1.00179.50           C  
ANISOU 1681  CD1 LEU A 294    20035  30923  17243   2033  -3862   2301       C  
ATOM   1682  CD2 LEU A 294     -27.478  28.684  26.590  1.00178.54           C  
ANISOU 1682  CD2 LEU A 294    20032  30189  17615   2435  -3423   2456       C  
ATOM   1683  N   GLY A 295     -22.285  30.738  25.746  1.00178.88           N  
ANISOU 1683  N   GLY A 295    18166  32039  17763   2110  -4050   2237       N  
ATOM   1684  CA  GLY A 295     -21.395  31.568  24.953  1.00179.03           C  
ANISOU 1684  CA  GLY A 295    17751  32363  17910   1857  -4081   2102       C  
ATOM   1685  C   GLY A 295     -20.711  30.774  23.867  1.00181.31           C  
ANISOU 1685  C   GLY A 295    17773  32691  18424   2188  -3918   2221       C  
ATOM   1686  O   GLY A 295     -20.785  31.173  22.708  1.00177.71           O  
ANISOU 1686  O   GLY A 295    17289  32054  18180   2014  -3710   2100       O  
ATOM   1687  N   MET A 296     -20.067  29.637  24.217  1.00180.44           N  
ANISOU 1687  N   MET A 296    17490  32805  18266   2682  -4002   2460       N  
ATOM   1688  CA  MET A 296     -19.355  28.779  23.264  1.00181.21           C  
ANISOU 1688  CA  MET A 296    17327  32966  18559   3073  -3857   2583       C  
ATOM   1689  C   MET A 296     -20.306  28.127  22.263  1.00179.28           C  
ANISOU 1689  C   MET A 296    17467  32131  18520   3239  -3525   2584       C  
ATOM   1690  O   MET A 296     -19.921  27.903  21.114  1.00178.54           O  
ANISOU 1690  O   MET A 296    17197  32012  18629   3357  -3337   2562       O  
ATOM   1691  CB  MET A 296     -18.516  27.725  24.002  1.00188.40           C  
ANISOU 1691  CB  MET A 296    18024  34214  19345   3589  -4043   2845       C  
ATOM   1692  CG  MET A 296     -17.505  26.999  23.119  1.00194.86           C  
ANISOU 1692  CG  MET A 296    18463  35222  20353   3979  -3950   2946       C  
ATOM   1693  SD  MET A 296     -16.159  28.056  22.536  1.00198.68           S  
ANISOU 1693  SD  MET A 296    18627  35577  21285   3467  -4058   2648       S  
ATOM   1694  CE  MET A 296     -15.051  27.963  23.927  1.00198.49           C  
ANISOU 1694  CE  MET A 296    18488  35670  21259   3419  -4505   2670       C  
ATOM   1695  N   TYR A 297     -21.555  27.853  22.706  1.00172.16           N  
ANISOU 1695  N   TYR A 297    17082  30775  17556   3232  -3456   2602       N  
ATOM   1696  CA  TYR A 297     -22.644  27.244  21.928  1.00167.56           C  
ANISOU 1696  CA  TYR A 297    16922  29605  17139   3346  -3166   2599       C  
ATOM   1697  C   TYR A 297     -23.032  28.073  20.708  1.00167.28           C  
ANISOU 1697  C   TYR A 297    16907  29358  17296   2999  -2952   2376       C  
ATOM   1698  O   TYR A 297     -23.170  27.527  19.612  1.00165.76           O  
ANISOU 1698  O   TYR A 297    16770  28917  17293   3178  -2721   2375       O  
ATOM   1699  CB  TYR A 297     -23.853  26.956  22.841  1.00166.36           C  
ANISOU 1699  CB  TYR A 297    17264  29105  16842   3329  -3177   2658       C  
ATOM   1700  CG  TYR A 297     -25.223  26.933  22.186  1.00162.90           C  
ANISOU 1700  CG  TYR A 297    17267  28090  16536   3190  -2914   2557       C  
ATOM   1701  CD1 TYR A 297     -25.654  25.827  21.451  1.00163.69           C  
ANISOU 1701  CD1 TYR A 297    17587  27806  16801   3510  -2696   2653       C  
ATOM   1702  CD2 TYR A 297     -26.129  27.969  22.390  1.00160.69           C  
ANISOU 1702  CD2 TYR A 297    17203  27648  16203   2755  -2895   2370       C  
ATOM   1703  CE1 TYR A 297     -26.927  25.789  20.875  1.00160.39           C  
ANISOU 1703  CE1 TYR A 297    17561  26886  16495   3369  -2472   2560       C  
ATOM   1704  CE2 TYR A 297     -27.405  27.941  21.824  1.00157.75           C  
ANISOU 1704  CE2 TYR A 297    17212  26781  15946   2639  -2666   2285       C  
ATOM   1705  CZ  TYR A 297     -27.802  26.847  21.069  1.00164.99           C  
ANISOU 1705  CZ  TYR A 297    18315  27348  17025   2937  -2459   2381       C  
ATOM   1706  OH  TYR A 297     -29.058  26.823  20.503  1.00164.08           O  
ANISOU 1706  OH  TYR A 297    18556  26771  17018   2808  -2247   2293       O  
ATOM   1707  N   MET A 298     -23.195  29.392  20.911  1.00161.77           N  
ANISOU 1707  N   MET A 298    16173  28755  16537   2509  -3034   2187       N  
ATOM   1708  CA  MET A 298     -23.533  30.383  19.884  1.00158.24           C  
ANISOU 1708  CA  MET A 298    15741  28138  16244   2127  -2868   1980       C  
ATOM   1709  C   MET A 298     -22.449  30.372  18.784  1.00162.49           C  
ANISOU 1709  C   MET A 298    15853  28943  16942   2201  -2778   1977       C  
ATOM   1710  O   MET A 298     -22.781  30.457  17.606  1.00160.05           O  
ANISOU 1710  O   MET A 298    15621  28386  16804   2142  -2544   1897       O  
ATOM   1711  CB  MET A 298     -23.585  31.780  20.521  1.00160.48           C  
ANISOU 1711  CB  MET A 298    16000  28570  16407   1625  -3035   1804       C  
ATOM   1712  CG  MET A 298     -24.938  32.391  20.672  1.00160.51           C  
ANISOU 1712  CG  MET A 298    16458  28144  16385   1360  -2951   1671       C  
ATOM   1713  SD  MET A 298     -24.694  34.119  21.137  1.00165.37           S  
ANISOU 1713  SD  MET A 298    16980  28946  16908    772  -3124   1434       S  
ATOM   1714  CE  MET A 298     -24.783  34.870  19.537  1.00159.83           C  
ANISOU 1714  CE  MET A 298    16200  28063  16464    516  -2889   1304       C  
ATOM   1715  N   VAL A 299     -21.160  30.240  19.181  1.00161.93           N  
ANISOU 1715  N   VAL A 299    15325  29398  16803   2343  -2963   2070       N  
ATOM   1716  CA  VAL A 299     -19.990  30.189  18.294  1.00163.59           C  
ANISOU 1716  CA  VAL A 299    15060  29960  17137   2447  -2899   2088       C  
ATOM   1717  C   VAL A 299     -19.974  28.869  17.515  1.00166.58           C  
ANISOU 1717  C   VAL A 299    15503  30142  17648   2968  -2689   2212       C  
ATOM   1718  O   VAL A 299     -19.502  28.857  16.382  1.00166.45           O  
ANISOU 1718  O   VAL A 299    15270  30195  17779   3013  -2509   2171       O  
ATOM   1719  CB  VAL A 299     -18.652  30.442  19.045  1.00172.24           C  
ANISOU 1719  CB  VAL A 299    15630  31706  18106   2443  -3179   2151       C  
ATOM   1720  CG1 VAL A 299     -17.496  30.670  18.078  1.00174.43           C  
ANISOU 1720  CG1 VAL A 299    15386  32374  18515   2433  -3096   2134       C  
ATOM   1721  CG2 VAL A 299     -18.766  31.628  19.994  1.00172.25           C  
ANISOU 1721  CG2 VAL A 299    15641  31860  17947   1950  -3413   2020       C  
ATOM   1722  N   THR A 300     -20.510  27.776  18.103  1.00162.17           N  
ANISOU 1722  N   THR A 300    15261  29323  17035   3347  -2703   2360       N  
ATOM   1723  CA  THR A 300     -20.573  26.449  17.477  1.00161.86           C  
ANISOU 1723  CA  THR A 300    15351  29032  17116   3854  -2516   2477       C  
ATOM   1724  C   THR A 300     -21.482  26.455  16.244  1.00160.12           C  
ANISOU 1724  C   THR A 300    15438  28332  17067   3743  -2216   2341       C  
ATOM   1725  O   THR A 300     -21.018  26.110  15.154  1.00160.16           O  
ANISOU 1725  O   THR A 300    15275  28369  17210   3921  -2035   2314       O  
ATOM   1726  CB  THR A 300     -20.957  25.361  18.498  1.00172.79           C  
ANISOU 1726  CB  THR A 300    17027  30236  18388   4230  -2621   2678       C  
ATOM   1727  OG1 THR A 300     -20.240  25.582  19.715  1.00177.05           O  
ANISOU 1727  OG1 THR A 300    17307  31234  18730   4238  -2925   2782       O  
ATOM   1728  CG2 THR A 300     -20.684  23.947  17.982  1.00173.61           C  
ANISOU 1728  CG2 THR A 300    17179  30178  18608   4809  -2481   2826       C  
ATOM   1729  N   VAL A 301     -22.761  26.865  16.416  1.00151.70           N  
ANISOU 1729  N   VAL A 301    14806  26853  15980   3449  -2167   2251       N  
ATOM   1730  CA  VAL A 301     -23.741  26.932  15.323  1.00147.13           C  
ANISOU 1730  CA  VAL A 301    14536  25822  15544   3314  -1908   2120       C  
ATOM   1731  C   VAL A 301     -23.312  27.909  14.240  1.00149.58           C  
ANISOU 1731  C   VAL A 301    14582  26302  15951   3006  -1798   1964       C  
ATOM   1732  O   VAL A 301     -23.387  27.552  13.071  1.00148.41           O  
ANISOU 1732  O   VAL A 301    14466  25989  15934   3121  -1575   1915       O  
ATOM   1733  CB  VAL A 301     -25.221  27.175  15.726  1.00147.03           C  
ANISOU 1733  CB  VAL A 301    15016  25358  15491   3075  -1877   2059       C  
ATOM   1734  CG1 VAL A 301     -26.137  26.189  15.015  1.00144.69           C  
ANISOU 1734  CG1 VAL A 301    15095  24565  15315   3300  -1650   2070       C  
ATOM   1735  CG2 VAL A 301     -25.435  27.126  17.231  1.00147.87           C  
ANISOU 1735  CG2 VAL A 301    15241  25536  15407   3076  -2100   2163       C  
ATOM   1736  N   ILE A 302     -22.845  29.122  14.620  1.00146.20           N  
ANISOU 1736  N   ILE A 302    13897  26201  15450   2613  -1953   1889       N  
ATOM   1737  CA  ILE A 302     -22.386  30.158  13.684  1.00145.54           C  
ANISOU 1737  CA  ILE A 302    13553  26298  15447   2268  -1867   1761       C  
ATOM   1738  C   ILE A 302     -21.297  29.595  12.754  1.00151.11           C  
ANISOU 1738  C   ILE A 302    13875  27294  16247   2560  -1740   1813       C  
ATOM   1739  O   ILE A 302     -21.385  29.792  11.541  1.00149.27           O  
ANISOU 1739  O   ILE A 302    13637  26957  16123   2477  -1523   1730       O  
ATOM   1740  CB  ILE A 302     -21.993  31.475  14.419  1.00149.74           C  
ANISOU 1740  CB  ILE A 302    13883  27135  15878   1807  -2085   1684       C  
ATOM   1741  CG1 ILE A 302     -23.273  32.281  14.767  1.00146.41           C  
ANISOU 1741  CG1 ILE A 302    13894  26318  15418   1443  -2093   1559       C  
ATOM   1742  CG2 ILE A 302     -21.003  32.338  13.602  1.00152.45           C  
ANISOU 1742  CG2 ILE A 302    13794  27839  16293   1533  -2041   1618       C  
ATOM   1743  CD1 ILE A 302     -23.139  33.325  15.884  1.00154.09           C  
ANISOU 1743  CD1 ILE A 302    14814  27488  16245   1075  -2345   1487       C  
ATOM   1744  N   VAL A 303     -20.335  28.833  13.315  1.00150.75           N  
ANISOU 1744  N   VAL A 303    13533  27595  16150   2936  -1868   1956       N  
ATOM   1745  CA  VAL A 303     -19.273  28.158  12.562  1.00153.41           C  
ANISOU 1745  CA  VAL A 303    13492  28232  16565   3300  -1757   2019       C  
ATOM   1746  C   VAL A 303     -19.888  27.040  11.685  1.00155.20           C  
ANISOU 1746  C   VAL A 303    14044  28022  16902   3679  -1502   2022       C  
ATOM   1747  O   VAL A 303     -19.591  26.974  10.490  1.00154.89           O  
ANISOU 1747  O   VAL A 303    13874  28017  16960   3727  -1287   1953       O  
ATOM   1748  CB  VAL A 303     -18.122  27.683  13.495  1.00161.86           C  
ANISOU 1748  CB  VAL A 303    14161  29796  17541   3609  -1987   2176       C  
ATOM   1749  CG1 VAL A 303     -17.293  26.558  12.879  1.00164.82           C  
ANISOU 1749  CG1 VAL A 303    14290  30337  17996   4168  -1859   2273       C  
ATOM   1750  CG2 VAL A 303     -17.228  28.855  13.885  1.00163.97           C  
ANISOU 1750  CG2 VAL A 303    13965  30599  17736   3204  -2178   2133       C  
ATOM   1751  N   GLY A 304     -20.782  26.241  12.274  1.00149.66           N  
ANISOU 1751  N   GLY A 304    13780  26907  16177   3890  -1524   2087       N  
ATOM   1752  CA  GLY A 304     -21.496  25.158  11.600  1.00147.73           C  
ANISOU 1752  CA  GLY A 304    13909  26191  16031   4214  -1311   2085       C  
ATOM   1753  C   GLY A 304     -22.319  25.595  10.401  1.00147.51           C  
ANISOU 1753  C   GLY A 304    14111  25840  16097   3949  -1076   1915       C  
ATOM   1754  O   GLY A 304     -22.397  24.864   9.410  1.00147.16           O  
ANISOU 1754  O   GLY A 304    14156  25613  16146   4208   -863   1873       O  
ATOM   1755  N   LEU A 305     -22.929  26.798  10.479  1.00140.76           N  
ANISOU 1755  N   LEU A 305    13356  24917  15209   3441  -1116   1811       N  
ATOM   1756  CA  LEU A 305     -23.741  27.386   9.407  1.00136.93           C  
ANISOU 1756  CA  LEU A 305    13084  24150  14795   3143   -924   1659       C  
ATOM   1757  C   LEU A 305     -22.870  27.961   8.291  1.00142.23           C  
ANISOU 1757  C   LEU A 305    13376  25149  15515   3026   -794   1593       C  
ATOM   1758  O   LEU A 305     -23.319  28.023   7.149  1.00140.30           O  
ANISOU 1758  O   LEU A 305    13271  24702  15335   2960   -585   1495       O  
ATOM   1759  CB  LEU A 305     -24.718  28.459   9.930  1.00133.57           C  
ANISOU 1759  CB  LEU A 305    12906  23527  14316   2672  -1020   1583       C  
ATOM   1760  CG  LEU A 305     -25.779  28.035  10.957  1.00136.28           C  
ANISOU 1760  CG  LEU A 305    13656  23524  14598   2715  -1117   1631       C  
ATOM   1761  CD1 LEU A 305     -26.585  29.220  11.415  1.00133.68           C  
ANISOU 1761  CD1 LEU A 305    13501  23080  14212   2255  -1202   1537       C  
ATOM   1762  CD2 LEU A 305     -26.708  26.968  10.417  1.00136.92           C  
ANISOU 1762  CD2 LEU A 305    14122  23145  14758   2967   -940   1628       C  
ATOM   1763  N   VAL A 306     -21.633  28.383   8.618  1.00141.81           N  
ANISOU 1763  N   VAL A 306    12839  25618  15422   2989   -917   1648       N  
ATOM   1764  CA  VAL A 306     -20.685  28.910   7.636  1.00143.40           C  
ANISOU 1764  CA  VAL A 306    12630  26193  15662   2870   -795   1606       C  
ATOM   1765  C   VAL A 306     -20.136  27.733   6.802  1.00150.32           C  
ANISOU 1765  C   VAL A 306    13383  27134  16597   3380   -601   1634       C  
ATOM   1766  O   VAL A 306     -20.004  27.871   5.585  1.00149.80           O  
ANISOU 1766  O   VAL A 306    13249  27091  16578   3341   -380   1554       O  
ATOM   1767  CB  VAL A 306     -19.584  29.804   8.281  1.00150.05           C  
ANISOU 1767  CB  VAL A 306    12991  27578  16443   2605   -996   1648       C  
ATOM   1768  CG1 VAL A 306     -18.433  30.079   7.313  1.00152.94           C  
ANISOU 1768  CG1 VAL A 306    12866  28396  16848   2579   -859   1642       C  
ATOM   1769  CG2 VAL A 306     -20.172  31.121   8.779  1.00147.30           C  
ANISOU 1769  CG2 VAL A 306    12803  27111  16052   2044  -1125   1570       C  
ATOM   1770  N   ILE A 307     -19.879  26.563   7.450  1.00149.69           N  
ANISOU 1770  N   ILE A 307    13317  27049  16510   3868   -678   1743       N  
ATOM   1771  CA  ILE A 307     -19.407  25.334   6.789  1.00152.35           C  
ANISOU 1771  CA  ILE A 307    13591  27389  16907   4413   -507   1767       C  
ATOM   1772  C   ILE A 307     -20.493  24.816   5.834  1.00154.34           C  
ANISOU 1772  C   ILE A 307    14312  27107  17223   4480   -276   1652       C  
ATOM   1773  O   ILE A 307     -20.188  24.531   4.677  1.00155.20           O  
ANISOU 1773  O   ILE A 307    14327  27267  17374   4629    -53   1572       O  
ATOM   1774  CB  ILE A 307     -18.904  24.242   7.784  1.00158.77           C  
ANISOU 1774  CB  ILE A 307    14324  28297  17702   4951   -644   1925       C  
ATOM   1775  CG1 ILE A 307     -17.746  24.769   8.654  1.00159.16           C  
ANISOU 1775  CG1 ILE A 307    14392  28429  17655   4820   -948   2043       C  
ATOM   1776  CG2 ILE A 307     -18.455  22.972   7.035  1.00164.33           C  
ANISOU 1776  CG2 ILE A 307    14482  29530  18425   5313   -584   1974       C  
ATOM   1777  CD1 ILE A 307     -17.680  24.086  10.042  1.00171.29           C  
ANISOU 1777  CD1 ILE A 307    15482  30475  19127   5129  -1156   2205       C  
ATOM   1778  N   HIS A 308     -21.755  24.729   6.306  1.00147.92           N  
ANISOU 1778  N   HIS A 308    13990  25805  16408   4352   -329   1638       N  
ATOM   1779  CA  HIS A 308     -22.863  24.260   5.475  1.00145.07           C  
ANISOU 1779  CA  HIS A 308    14085  24932  16104   4374   -136   1525       C  
ATOM   1780  C   HIS A 308     -23.237  25.268   4.387  1.00145.76           C  
ANISOU 1780  C   HIS A 308    14184  25002  16196   3959     11   1383       C  
ATOM   1781  O   HIS A 308     -23.253  24.920   3.206  1.00145.37           O  
ANISOU 1781  O   HIS A 308    14179  24876  16180   4082    230   1286       O  
ATOM   1782  CB  HIS A 308     -24.084  23.849   6.318  1.00143.51           C  
ANISOU 1782  CB  HIS A 308    14372  24255  15900   4352   -234   1563       C  
ATOM   1783  CG  HIS A 308     -25.167  23.205   5.510  1.00144.85           C  
ANISOU 1783  CG  HIS A 308    14987  23916  16133   4412    -49   1455       C  
ATOM   1784  ND1 HIS A 308     -25.095  21.872   5.134  1.00148.70           N  
ANISOU 1784  ND1 HIS A 308    15637  24181  16682   4872     71   1457       N  
ATOM   1785  CD2 HIS A 308     -26.300  23.743   5.002  1.00143.04           C  
ANISOU 1785  CD2 HIS A 308    15056  23382  15913   4065     26   1338       C  
ATOM   1786  CE1 HIS A 308     -26.187  21.641   4.426  1.00145.59           C  
ANISOU 1786  CE1 HIS A 308    15631  23358  16327   4765    210   1332       C  
ATOM   1787  NE2 HIS A 308     -26.945  22.736   4.323  1.00142.44           N  
ANISOU 1787  NE2 HIS A 308    15315  22910  15897   4290    185   1263       N  
ATOM   1788  N   GLY A 309     -23.491  26.504   4.802  1.00140.06           N  
ANISOU 1788  N   GLY A 309    13425  24360  15433   3487   -112   1375       N  
ATOM   1789  CA  GLY A 309     -23.900  27.597   3.932  1.00137.45           C  
ANISOU 1789  CA  GLY A 309    13130  23992  15101   3058     -7   1268       C  
ATOM   1790  C   GLY A 309     -22.899  28.055   2.895  1.00143.19           C  
ANISOU 1790  C   GLY A 309    13463  25117  15828   2992    140   1239       C  
ATOM   1791  O   GLY A 309     -23.256  28.184   1.723  1.00141.70           O  
ANISOU 1791  O   GLY A 309    13390  24803  15648   2912    338   1146       O  
ATOM   1792  N   LEU A 310     -21.651  28.319   3.304  1.00142.80           N  
ANISOU 1792  N   LEU A 310    12937  25565  15756   3010     45   1320       N  
ATOM   1793  CA  LEU A 310     -20.651  28.836   2.373  1.00144.94           C  
ANISOU 1793  CA  LEU A 310    12790  26261  16020   2903    186   1306       C  
ATOM   1794  C   LEU A 310     -19.659  27.800   1.816  1.00152.66           C  
ANISOU 1794  C   LEU A 310    13471  27522  17011   3400    336   1326       C  
ATOM   1795  O   LEU A 310     -18.859  28.165   0.952  1.00154.63           O  
ANISOU 1795  O   LEU A 310    13375  28132  17247   3330    486   1310       O  
ATOM   1796  CB  LEU A 310     -19.905  30.013   3.003  1.00146.48           C  
ANISOU 1796  CB  LEU A 310    12608  26865  16184   2500     10   1364       C  
ATOM   1797  CG  LEU A 310     -20.611  31.346   2.867  1.00148.38           C  
ANISOU 1797  CG  LEU A 310    13043  26920  16415   1928    -35   1310       C  
ATOM   1798  CD1 LEU A 310     -21.067  31.899   4.206  1.00146.16           C  
ANISOU 1798  CD1 LEU A 310    13061  26361  16113   1776   -269   1314       C  
ATOM   1799  CD2 LEU A 310     -19.762  32.316   2.059  1.00153.99           C  
ANISOU 1799  CD2 LEU A 310    13314  28085  17112   1546    -49   1337       C  
ATOM   1800  N   ILE A 311     -19.714  26.521   2.257  1.00149.98           N  
ANISOU 1800  N   ILE A 311    13271  27017  16697   3902    310   1362       N  
ATOM   1801  CA  ILE A 311     -18.790  25.499   1.733  1.00153.38           C  
ANISOU 1801  CA  ILE A 311    13445  27687  17147   4421    458   1371       C  
ATOM   1802  C   ILE A 311     -19.554  24.265   1.202  1.00155.69           C  
ANISOU 1802  C   ILE A 311    14185  27489  17480   4822    615   1289       C  
ATOM   1803  O   ILE A 311     -19.347  23.898   0.044  1.00156.22           O  
ANISOU 1803  O   ILE A 311    14224  27584  17547   5003    855   1189       O  
ATOM   1804  CB  ILE A 311     -17.639  25.128   2.739  1.00160.53           C  
ANISOU 1804  CB  ILE A 311    13914  29037  18044   4716    277   1514       C  
ATOM   1805  CG1 ILE A 311     -16.717  26.344   3.085  1.00162.56           C  
ANISOU 1805  CG1 ILE A 311    13656  29854  18258   4305    143   1574       C  
ATOM   1806  CG2 ILE A 311     -16.812  23.913   2.279  1.00165.33           C  
ANISOU 1806  CG2 ILE A 311    14318  29818  18680   5339    430   1524       C  
ATOM   1807  CD1 ILE A 311     -15.884  27.032   1.900  1.00171.56           C  
ANISOU 1807  CD1 ILE A 311    14372  31429  19385   4104    356   1524       C  
ATOM   1808  N   VAL A 312     -20.434  23.649   2.027  1.00150.02           N  
ANISOU 1808  N   VAL A 312    13883  26328  16789   4937    486   1325       N  
ATOM   1809  CA  VAL A 312     -21.209  22.450   1.668  1.00148.94           C  
ANISOU 1809  CA  VAL A 312    14201  25688  16702   5286    608   1255       C  
ATOM   1810  C   VAL A 312     -22.165  22.724   0.492  1.00149.50           C  
ANISOU 1810  C   VAL A 312    14595  25441  16769   5039    802   1085       C  
ATOM   1811  O   VAL A 312     -21.973  22.146  -0.581  1.00150.45           O  
ANISOU 1811  O   VAL A 312    14735  25536  16892   5287   1020    974       O  
ATOM   1812  CB  VAL A 312     -21.927  21.788   2.882  1.00151.59           C  
ANISOU 1812  CB  VAL A 312    14896  25639  17062   5420    421   1356       C  
ATOM   1813  CG1 VAL A 312     -22.787  20.615   2.444  1.00150.54           C  
ANISOU 1813  CG1 VAL A 312    15255  24955  16990   5708    556   1275       C  
ATOM   1814  CG2 VAL A 312     -20.933  21.340   3.949  1.00155.21           C  
ANISOU 1814  CG2 VAL A 312    15050  26413  17510   5757    242   1532       C  
ATOM   1815  N   LEU A 313     -23.164  23.609   0.688  1.00141.94           N  
ANISOU 1815  N   LEU A 313    13879  24259  15793   4565    721   1061       N  
ATOM   1816  CA  LEU A 313     -24.160  23.963  -0.330  1.00138.59           C  
ANISOU 1816  CA  LEU A 313    13763  23541  15356   4299    868    918       C  
ATOM   1817  C   LEU A 313     -23.548  24.494  -1.660  1.00144.04           C  
ANISOU 1817  C   LEU A 313    14184  24550  15995   4201   1078    833       C  
ATOM   1818  O   LEU A 313     -23.986  24.012  -2.709  1.00143.38           O  
ANISOU 1818  O   LEU A 313    14325  24256  15896   4313   1266    701       O  
ATOM   1819  CB  LEU A 313     -25.236  24.931   0.213  1.00134.40           C  
ANISOU 1819  CB  LEU A 313    13475  22779  14814   3819    726    928       C  
ATOM   1820  CG  LEU A 313     -26.185  24.416   1.313  1.00137.09           C  
ANISOU 1820  CG  LEU A 313    14182  22720  15186   3861    570    981       C  
ATOM   1821  CD1 LEU A 313     -27.053  25.533   1.839  1.00133.66           C  
ANISOU 1821  CD1 LEU A 313    13891  22166  14726   3387    439    987       C  
ATOM   1822  CD2 LEU A 313     -27.076  23.284   0.818  1.00138.76           C  
ANISOU 1822  CD2 LEU A 313    14822  22459  15441   4097    692    889       C  
ATOM   1823  N   PRO A 314     -22.528  25.407  -1.688  1.00142.13           N  
ANISOU 1823  N   PRO A 314    13474  24814  15717   4007   1061    901       N  
ATOM   1824  CA  PRO A 314     -21.986  25.850  -2.982  1.00143.11           C  
ANISOU 1824  CA  PRO A 314    13363  25232  15782   3918   1283    834       C  
ATOM   1825  C   PRO A 314     -21.343  24.738  -3.812  1.00150.45           C  
ANISOU 1825  C   PRO A 314    14194  26270  16699   4423   1498    756       C  
ATOM   1826  O   PRO A 314     -21.589  24.696  -5.016  1.00149.93           O  
ANISOU 1826  O   PRO A 314    14244  26146  16575   4414   1710    635       O  
ATOM   1827  CB  PRO A 314     -20.976  26.939  -2.593  1.00146.58           C  
ANISOU 1827  CB  PRO A 314    13307  26184  16201   3625   1188    948       C  
ATOM   1828  CG  PRO A 314     -21.386  27.381  -1.254  1.00149.23           C  
ANISOU 1828  CG  PRO A 314    13744  26386  16570   3403    916   1033       C  
ATOM   1829  CD  PRO A 314     -21.858  26.129  -0.589  1.00144.65           C  
ANISOU 1829  CD  PRO A 314    13462  25464  16037   3818    844   1037       C  
ATOM   1830  N   LEU A 315     -20.563  23.821  -3.184  1.00150.23           N  
ANISOU 1830  N   LEU A 315    13977  26386  16717   4879   1445    821       N  
ATOM   1831  CA  LEU A 315     -19.918  22.722  -3.912  1.00153.48           C  
ANISOU 1831  CA  LEU A 315    14306  26883  17125   5411   1649    740       C  
ATOM   1832  C   LEU A 315     -20.966  21.724  -4.439  1.00155.59           C  
ANISOU 1832  C   LEU A 315    15126  26579  17410   5622   1758    587       C  
ATOM   1833  O   LEU A 315     -20.724  21.100  -5.474  1.00157.25           O  
ANISOU 1833  O   LEU A 315    15360  26804  17582   5907   1985    453       O  
ATOM   1834  CB  LEU A 315     -18.786  22.069  -3.085  1.00157.54           C  
ANISOU 1834  CB  LEU A 315    14470  27699  17687   5861   1555    859       C  
ATOM   1835  CG  LEU A 315     -18.879  20.595  -2.736  1.00164.55           C  
ANISOU 1835  CG  LEU A 315    15562  28332  18626   6488   1642    803       C  
ATOM   1836  CD1 LEU A 315     -17.892  19.820  -3.554  1.00169.59           C  
ANISOU 1836  CD1 LEU A 315    15760  29437  19239   6901   1826    777       C  
ATOM   1837  CD2 LEU A 315     -18.621  20.359  -1.247  1.00166.74           C  
ANISOU 1837  CD2 LEU A 315    16015  28360  18980   6704   1404    939       C  
ATOM   1838  N   ILE A 316     -22.144  21.630  -3.762  1.00148.65           N  
ANISOU 1838  N   ILE A 316    14686  25213  16582   5461   1602    601       N  
ATOM   1839  CA  ILE A 316     -23.274  20.797  -4.193  1.00146.71           C  
ANISOU 1839  CA  ILE A 316    14979  24405  16358   5569   1677    461       C  
ATOM   1840  C   ILE A 316     -23.832  21.397  -5.494  1.00148.82           C  
ANISOU 1840  C   ILE A 316    15372  24637  16537   5267   1851    309       C  
ATOM   1841  O   ILE A 316     -24.012  20.664  -6.469  1.00149.69           O  
ANISOU 1841  O   ILE A 316    15679  24582  16613   5498   2037    145       O  
ATOM   1842  CB  ILE A 316     -24.345  20.614  -3.071  1.00146.69           C  
ANISOU 1842  CB  ILE A 316    15359  23950  16426   5439   1466    535       C  
ATOM   1843  CG1 ILE A 316     -23.815  19.679  -1.961  1.00149.66           C  
ANISOU 1843  CG1 ILE A 316    15694  24296  16875   5858   1336    671       C  
ATOM   1844  CG2 ILE A 316     -25.688  20.093  -3.628  1.00144.77           C  
ANISOU 1844  CG2 ILE A 316    15657  23156  16195   5367   1539    384       C  
ATOM   1845  CD1 ILE A 316     -24.683  19.612  -0.694  1.00154.43           C  
ANISOU 1845  CD1 ILE A 316    16593  24560  17524   5711   1116    789       C  
ATOM   1846  N   TYR A 317     -24.029  22.735  -5.523  1.00142.91           N  
ANISOU 1846  N   TYR A 317    14497  24063  15741   4766   1790    365       N  
ATOM   1847  CA  TYR A 317     -24.509  23.472  -6.698  1.00141.16           C  
ANISOU 1847  CA  TYR A 317    14360  23853  15421   4446   1933    263       C  
ATOM   1848  C   TYR A 317     -23.529  23.353  -7.869  1.00148.98           C  
ANISOU 1848  C   TYR A 317    15055  25234  16318   4644   2181    188       C  
ATOM   1849  O   TYR A 317     -23.966  23.130  -8.999  1.00148.06           O  
ANISOU 1849  O   TYR A 317    15147  24994  16115   4665   2357     36       O  
ATOM   1850  CB  TYR A 317     -24.799  24.947  -6.343  1.00139.38           C  
ANISOU 1850  CB  TYR A 317    14037  23743  15180   3899   1800    370       C  
ATOM   1851  CG  TYR A 317     -25.287  25.800  -7.497  1.00139.02           C  
ANISOU 1851  CG  TYR A 317    14074  23716  15032   3556   1929    303       C  
ATOM   1852  CD1 TYR A 317     -26.579  25.671  -7.994  1.00138.12           C  
ANISOU 1852  CD1 TYR A 317    14404  23187  14890   3459   1958    183       C  
ATOM   1853  CD2 TYR A 317     -24.471  26.776  -8.056  1.00141.08           C  
ANISOU 1853  CD2 TYR A 317    13975  24409  15222   3307   2010    372       C  
ATOM   1854  CE1 TYR A 317     -27.034  26.466  -9.047  1.00137.82           C  
ANISOU 1854  CE1 TYR A 317    14444  23177  14743   3157   2061    137       C  
ATOM   1855  CE2 TYR A 317     -24.916  27.583  -9.102  1.00140.72           C  
ANISOU 1855  CE2 TYR A 317    14022  24375  15073   2993   2125    336       C  
ATOM   1856  CZ  TYR A 317     -26.192  27.414  -9.606  1.00144.87           C  
ANISOU 1856  CZ  TYR A 317    14989  24493  15560   2936   2149    219       C  
ATOM   1857  OH  TYR A 317     -26.621  28.199 -10.649  1.00144.19           O  
ANISOU 1857  OH  TYR A 317    14993  24433  15357   2648   2252    197       O  
ATOM   1858  N   PHE A 318     -22.211  23.467  -7.585  1.00149.83           N  
ANISOU 1858  N   PHE A 318    14671  25827  16432   4799   2195    291       N  
ATOM   1859  CA  PHE A 318     -21.129  23.357  -8.567  1.00153.97           C  
ANISOU 1859  CA  PHE A 318    14834  26800  16868   5012   2434    241       C  
ATOM   1860  C   PHE A 318     -21.063  21.943  -9.145  1.00160.78           C  
ANISOU 1860  C   PHE A 318    15888  27476  17723   5565   2604     76       C  
ATOM   1861  O   PHE A 318     -20.930  21.797 -10.354  1.00161.78           O  
ANISOU 1861  O   PHE A 318    16021  27711  17737   5656   2839    -63       O  
ATOM   1862  CB  PHE A 318     -19.780  23.745  -7.934  1.00158.92           C  
ANISOU 1862  CB  PHE A 318    14878  27982  17524   5058   2372    401       C  
ATOM   1863  CG  PHE A 318     -18.662  24.023  -8.913  1.00163.98           C  
ANISOU 1863  CG  PHE A 318    15065  29179  18063   5127   2611    387       C  
ATOM   1864  CD1 PHE A 318     -18.454  25.305  -9.412  1.00166.43           C  
ANISOU 1864  CD1 PHE A 318    15140  29804  18290   4643   2670    454       C  
ATOM   1865  CD2 PHE A 318     -17.794  23.015  -9.306  1.00169.93           C  
ANISOU 1865  CD2 PHE A 318    15619  30146  18802   5679   2783    316       C  
ATOM   1866  CE1 PHE A 318     -17.416  25.565 -10.312  1.00171.47           C  
ANISOU 1866  CE1 PHE A 318    15349  30975  18825   4688   2905    455       C  
ATOM   1867  CE2 PHE A 318     -16.757  23.275 -10.208  1.00176.59           C  
ANISOU 1867  CE2 PHE A 318    16022  31533  19540   5747   3020    302       C  
ATOM   1868  CZ  PHE A 318     -16.576  24.549 -10.704  1.00174.59           C  
ANISOU 1868  CZ  PHE A 318    15534  31605  19199   5239   3083    376       C  
ATOM   1869  N   LEU A 319     -21.178  20.908  -8.288  1.00158.65           N  
ANISOU 1869  N   LEU A 319    15799  26913  17569   5930   2485     90       N  
ATOM   1870  CA  LEU A 319     -21.146  19.496  -8.686  1.00161.56           C  
ANISOU 1870  CA  LEU A 319    16399  27028  17959   6477   2619    -60       C  
ATOM   1871  C   LEU A 319     -22.306  19.121  -9.621  1.00164.83           C  
ANISOU 1871  C   LEU A 319    17334  26978  18316   6401   2732   -272       C  
ATOM   1872  O   LEU A 319     -22.141  18.240 -10.467  1.00167.23           O  
ANISOU 1872  O   LEU A 319    17764  27204  18573   6767   2928   -453       O  
ATOM   1873  CB  LEU A 319     -21.182  18.606  -7.438  1.00162.15           C  
ANISOU 1873  CB  LEU A 319    16606  26828  18177   6795   2428     42       C  
ATOM   1874  CG  LEU A 319     -20.602  17.208  -7.579  1.00170.98           C  
ANISOU 1874  CG  LEU A 319    17773  27848  19341   7453   2544    -40       C  
ATOM   1875  CD1 LEU A 319     -19.646  16.910  -6.455  1.00173.99           C  
ANISOU 1875  CD1 LEU A 319    17799  28504  19807   7771   2402    156       C  
ATOM   1876  CD2 LEU A 319     -21.699  16.163  -7.615  1.00171.97           C  
ANISOU 1876  CD2 LEU A 319    18516  27290  19534   7601   2528   -162       C  
ATOM   1877  N   ILE A 320     -23.469  19.784  -9.461  1.00157.89           N  
ANISOU 1877  N   ILE A 320    16749  25806  17437   5933   2604   -257       N  
ATOM   1878  CA  ILE A 320     -24.687  19.534 -10.238  1.00155.93           C  
ANISOU 1878  CA  ILE A 320    16982  25128  17135   5794   2666   -440       C  
ATOM   1879  C   ILE A 320     -24.756  20.390 -11.517  1.00160.75           C  
ANISOU 1879  C   ILE A 320    17511  25991  17573   5498   2832   -525       C  
ATOM   1880  O   ILE A 320     -24.956  19.838 -12.602  1.00161.89           O  
ANISOU 1880  O   ILE A 320    17854  26042  17615   5657   3015   -727       O  
ATOM   1881  CB  ILE A 320     -25.948  19.688  -9.327  1.00154.66           C  
ANISOU 1881  CB  ILE A 320    17185  24509  17071   5494   2434   -373       C  
ATOM   1882  CG1 ILE A 320     -26.028  18.518  -8.312  1.00156.10           C  
ANISOU 1882  CG1 ILE A 320    17570  24343  17396   5856   2324   -334       C  
ATOM   1883  CG2 ILE A 320     -27.253  19.805 -10.142  1.00152.50           C  
ANISOU 1883  CG2 ILE A 320    17326  23890  16726   5213   2471   -531       C  
ATOM   1884  CD1 ILE A 320     -26.820  18.784  -7.029  1.00160.19           C  
ANISOU 1884  CD1 ILE A 320    18262  24589  18015   5609   2076   -180       C  
ATOM   1885  N   THR A 321     -24.600  21.720 -11.388  1.00156.36           N  
ANISOU 1885  N   THR A 321    16688  25742  16981   5071   2767   -373       N  
ATOM   1886  CA  THR A 321     -24.717  22.666 -12.505  1.00156.03           C  
ANISOU 1886  CA  THR A 321    16582  25924  16776   4742   2903   -407       C  
ATOM   1887  C   THR A 321     -23.414  22.943 -13.257  1.00164.67           C  
ANISOU 1887  C   THR A 321    17218  27593  17757   4859   3119   -389       C  
ATOM   1888  O   THR A 321     -23.462  23.195 -14.463  1.00164.63           O  
ANISOU 1888  O   THR A 321    17240  27728  17584   4769   3308   -485       O  
ATOM   1889  CB  THR A 321     -25.350  23.988 -12.037  1.00161.67           C  
ANISOU 1889  CB  THR A 321    17310  26606  17510   4194   2726   -257       C  
ATOM   1890  OG1 THR A 321     -24.432  24.687 -11.194  1.00162.76           O  
ANISOU 1890  OG1 THR A 321    17026  27099  17715   4078   2627    -64       O  
ATOM   1891  CG2 THR A 321     -26.692  23.791 -11.324  1.00156.44           C  
ANISOU 1891  CG2 THR A 321    17082  25410  16946   4055   2526   -274       C  
ATOM   1892  N   ARG A 322     -22.266  22.930 -12.542  1.00164.65           N  
ANISOU 1892  N   ARG A 322    16782  27945  17830   5039   3089   -258       N  
ATOM   1893  CA  ARG A 322     -20.910  23.244 -13.042  1.00168.60           C  
ANISOU 1893  CA  ARG A 322    16760  29056  18244   5139   3277   -208       C  
ATOM   1894  C   ARG A 322     -20.755  24.772 -13.242  1.00170.76           C  
ANISOU 1894  C   ARG A 322    16775  29654  18450   4579   3260    -49       C  
ATOM   1895  O   ARG A 322     -19.798  25.245 -13.865  1.00173.37           O  
ANISOU 1895  O   ARG A 322    16699  30492  18682   4534   3434      3       O  
ATOM   1896  CB  ARG A 322     -20.534  22.416 -14.291  1.00172.37           C  
ANISOU 1896  CB  ARG A 322    17276  29639  18578   5528   3574   -415       C  
ATOM   1897  CG  ARG A 322     -19.033  22.238 -14.504  1.00191.85           C  
ANISOU 1897  CG  ARG A 322    19194  32755  20946   5694   3800   -379       C  
ATOM   1898  CD  ARG A 322     -18.765  21.137 -15.498  1.00208.01           C  
ANISOU 1898  CD  ARG A 322    21482  34326  23227   5871   4041   -663       C  
ATOM   1899  NE  ARG A 322     -18.578  19.857 -14.819  1.00217.91           N  
ANISOU 1899  NE  ARG A 322    23197  34307  25292   5645   3915   -864       N  
ATOM   1900  CZ  ARG A 322     -17.387  19.322 -14.548  1.00230.91           C  
ANISOU 1900  CZ  ARG A 322    24993  34671  28073   4852   3803   -989       C  
ATOM   1901  NH1 ARG A 322     -16.276  19.955 -14.900  1.00222.50           N  
ANISOU 1901  NH1 ARG A 322    23332  34446  26762   5059   3871   -802       N  
ATOM   1902  NH2 ARG A 322     -17.312  18.158 -13.919  1.00224.54           N  
ANISOU 1902  NH2 ARG A 322    24102  34142  27071   5615   3754   -985       N  
ATOM   1903  N   LYS A 323     -21.695  25.541 -12.652  1.00162.44           N  
ANISOU 1903  N   LYS A 323    15958  28303  17460   4158   3046     35       N  
ATOM   1904  CA  LYS A 323     -21.749  27.004 -12.680  1.00160.22           C  
ANISOU 1904  CA  LYS A 323    15533  28199  17146   3607   2986    186       C  
ATOM   1905  C   LYS A 323     -21.210  27.535 -11.356  1.00164.06           C  
ANISOU 1905  C   LYS A 323    15723  28843  17771   3453   2764    360       C  
ATOM   1906  O   LYS A 323     -21.341  26.856 -10.333  1.00162.94           O  
ANISOU 1906  O   LYS A 323    15671  28489  17751   3683   2596    363       O  
ATOM   1907  CB  LYS A 323     -23.194  27.481 -12.896  1.00157.89           C  
ANISOU 1907  CB  LYS A 323    15716  27449  16826   3273   2892    148       C  
ATOM   1908  CG  LYS A 323     -23.817  27.010 -14.206  1.00168.54           C  
ANISOU 1908  CG  LYS A 323    17376  28643  18020   3382   3083    -29       C  
ATOM   1909  CD  LYS A 323     -25.325  27.173 -14.190  1.00173.16           C  
ANISOU 1909  CD  LYS A 323    18453  28724  18615   3156   2946    -85       C  
ATOM   1910  CE  LYS A 323     -25.973  26.589 -15.416  1.00183.40           C  
ANISOU 1910  CE  LYS A 323    20067  29860  19758   3286   3107   -280       C  
ATOM   1911  NZ  LYS A 323     -27.451  26.725 -15.366  1.00188.53           N  
ANISOU 1911  NZ  LYS A 323    21165  30045  20423   3069   2959   -333       N  
ATOM   1912  N   ASN A 324     -20.591  28.734 -11.375  1.00161.90           N  
ANISOU 1912  N   ASN A 324    15104  28941  17470   3058   2761    506       N  
ATOM   1913  CA  ASN A 324     -20.006  29.348 -10.184  1.00162.23           C  
ANISOU 1913  CA  ASN A 324    14836  29180  17623   2860   2550    660       C  
ATOM   1914  C   ASN A 324     -21.100  29.696  -9.167  1.00161.91           C  
ANISOU 1914  C   ASN A 324    15158  28677  17683   2620   2280    686       C  
ATOM   1915  O   ASN A 324     -21.982  30.504  -9.470  1.00158.72           O  
ANISOU 1915  O   ASN A 324    15030  28028  17248   2250   2251    692       O  
ATOM   1916  CB  ASN A 324     -19.117  30.544 -10.540  1.00165.66           C  
ANISOU 1916  CB  ASN A 324    14837  30103  18002   2465   2625    794       C  
ATOM   1917  CG  ASN A 324     -18.091  30.857  -9.479  1.00191.13           C  
ANISOU 1917  CG  ASN A 324    17611  33686  21324   2396   2459    921       C  
ATOM   1918  OD1 ASN A 324     -18.410  31.393  -8.411  1.00182.10           O  
ANISOU 1918  OD1 ASN A 324    16545  32375  20270   2125   2209    989       O  
ATOM   1919  ND2 ASN A 324     -16.826  30.543  -9.753  1.00188.00           N  
ANISOU 1919  ND2 ASN A 324    16719  33811  20900   2640   2594    950       N  
ATOM   1920  N   PRO A 325     -21.104  29.015  -7.997  1.00158.02           N  
ANISOU 1920  N   PRO A 325    14695  28044  17300   2867   2092    698       N  
ATOM   1921  CA  PRO A 325     -22.181  29.231  -7.018  1.00153.82           C  
ANISOU 1921  CA  PRO A 325    14525  27071  16849   2681   1854    713       C  
ATOM   1922  C   PRO A 325     -22.144  30.533  -6.240  1.00156.03           C  
ANISOU 1922  C   PRO A 325    14680  27438  17165   2198   1662    832       C  
ATOM   1923  O   PRO A 325     -23.182  30.939  -5.725  1.00151.98           O  
ANISOU 1923  O   PRO A 325    14507  26552  16689   1974   1513    826       O  
ATOM   1924  CB  PRO A 325     -22.047  28.035  -6.080  1.00156.48           C  
ANISOU 1924  CB  PRO A 325    14898  27287  17268   3127   1742    704       C  
ATOM   1925  CG  PRO A 325     -20.626  27.674  -6.146  1.00165.54           C  
ANISOU 1925  CG  PRO A 325    15551  28940  18407   3411   1828    751       C  
ATOM   1926  CD  PRO A 325     -20.153  27.987  -7.527  1.00163.02           C  
ANISOU 1926  CD  PRO A 325    15047  28913  17979   3350   2095    705       C  
ATOM   1927  N   PHE A 326     -20.969  31.165  -6.118  1.00155.63           N  
ANISOU 1927  N   PHE A 326    14151  27874  17108   2042   1661    932       N  
ATOM   1928  CA  PHE A 326     -20.846  32.403  -5.353  1.00154.94           C  
ANISOU 1928  CA  PHE A 326    13935  27878  17058   1570   1472   1031       C  
ATOM   1929  C   PHE A 326     -21.350  33.636  -6.127  1.00157.25           C  
ANISOU 1929  C   PHE A 326    14375  28072  17302   1085   1545   1052       C  
ATOM   1930  O   PHE A 326     -21.559  34.688  -5.517  1.00155.83           O  
ANISOU 1930  O   PHE A 326    14230  27818  17159    678   1382   1109       O  
ATOM   1931  CB  PHE A 326     -19.425  32.579  -4.804  1.00160.80           C  
ANISOU 1931  CB  PHE A 326    14109  29169  17819   1571   1410   1128       C  
ATOM   1932  CG  PHE A 326     -19.082  31.526  -3.769  1.00163.53           C  
ANISOU 1932  CG  PHE A 326    14361  29554  18219   2004   1264   1135       C  
ATOM   1933  CD1 PHE A 326     -19.561  31.622  -2.464  1.00164.58           C  
ANISOU 1933  CD1 PHE A 326    14668  29459  18404   1930    996   1162       C  
ATOM   1934  CD2 PHE A 326     -18.304  30.424  -4.107  1.00168.84           C  
ANISOU 1934  CD2 PHE A 326    14794  30478  18880   2507   1401   1118       C  
ATOM   1935  CE1 PHE A 326     -19.260  30.638  -1.517  1.00166.70           C  
ANISOU 1935  CE1 PHE A 326    14872  29758  18707   2337    861   1190       C  
ATOM   1936  CE2 PHE A 326     -17.999  29.445  -3.156  1.00172.92           C  
ANISOU 1936  CE2 PHE A 326    15247  31008  19447   2929   1262   1143       C  
ATOM   1937  CZ  PHE A 326     -18.474  29.561  -1.868  1.00169.02           C  
ANISOU 1937  CZ  PHE A 326    14929  30293  18999   2835    990   1189       C  
ATOM   1938  N   VAL A 327     -21.606  33.484  -7.446  1.00153.41           N  
ANISOU 1938  N   VAL A 327    14010  27553  16726   1144   1782   1000       N  
ATOM   1939  CA  VAL A 327     -22.176  34.522  -8.322  1.00151.47           C  
ANISOU 1939  CA  VAL A 327    13954  27184  16413    747   1870   1027       C  
ATOM   1940  C   VAL A 327     -23.710  34.412  -8.204  1.00149.85           C  
ANISOU 1940  C   VAL A 327    14298  26412  16226    738   1777    945       C  
ATOM   1941  O   VAL A 327     -24.422  35.411  -8.335  1.00147.42           O  
ANISOU 1941  O   VAL A 327    14211  25889  15912    373   1724    981       O  
ATOM   1942  CB  VAL A 327     -21.692  34.394  -9.795  1.00157.87           C  
ANISOU 1942  CB  VAL A 327    14619  28276  17091    821   2168   1020       C  
ATOM   1943  CG1 VAL A 327     -22.050  35.636 -10.608  1.00157.00           C  
ANISOU 1943  CG1 VAL A 327    14618  28128  16906    355   2243   1103       C  
ATOM   1944  CG2 VAL A 327     -20.190  34.137  -9.863  1.00162.34           C  
ANISOU 1944  CG2 VAL A 327    14627  29414  17642    976   2279   1073       C  
ATOM   1945  N   PHE A 328     -24.201  33.184  -7.935  1.00144.17           N  
ANISOU 1945  N   PHE A 328    13789  25454  15533   1144   1756    839       N  
ATOM   1946  CA  PHE A 328     -25.612  32.869  -7.719  1.00139.56           C  
ANISOU 1946  CA  PHE A 328    13689  24360  14977   1183   1664    755       C  
ATOM   1947  C   PHE A 328     -26.031  33.478  -6.382  1.00139.16           C  
ANISOU 1947  C   PHE A 328    13727  24126  15023    954   1407    809       C  
ATOM   1948  O   PHE A 328     -27.062  34.147  -6.322  1.00135.61           O  
ANISOU 1948  O   PHE A 328    13579  23365  14580    700   1330    801       O  
ATOM   1949  CB  PHE A 328     -25.822  31.344  -7.714  1.00141.61           C  
ANISOU 1949  CB  PHE A 328    14098  24457  15250   1673   1713    640       C  
ATOM   1950  CG  PHE A 328     -27.259  30.880  -7.736  1.00139.84           C  
ANISOU 1950  CG  PHE A 328    14360  23734  15038   1726   1665    539       C  
ATOM   1951  CD1 PHE A 328     -27.908  30.630  -8.940  1.00142.40           C  
ANISOU 1951  CD1 PHE A 328    14926  23912  15269   1765   1821    436       C  
ATOM   1952  CD2 PHE A 328     -27.947  30.642  -6.555  1.00139.53           C  
ANISOU 1952  CD2 PHE A 328    14525  23396  15094   1744   1466    545       C  
ATOM   1953  CE1 PHE A 328     -29.229  30.177  -8.961  1.00140.33           C  
ANISOU 1953  CE1 PHE A 328    15085  23215  15020   1803   1769    337       C  
ATOM   1954  CE2 PHE A 328     -29.271  30.199  -6.578  1.00139.46           C  
ANISOU 1954  CE2 PHE A 328    14938  22952  15098   1778   1430    456       C  
ATOM   1955  CZ  PHE A 328     -29.897  29.954  -7.781  1.00136.95           C  
ANISOU 1955  CZ  PHE A 328    14838  22497  14698   1807   1578    350       C  
ATOM   1956  N   ILE A 329     -25.197  33.290  -5.326  1.00136.11           N  
ANISOU 1956  N   ILE A 329    13058  23959  14697   1044   1277    864       N  
ATOM   1957  CA  ILE A 329     -25.399  33.829  -3.973  1.00134.04           C  
ANISOU 1957  CA  ILE A 329    12828  23597  14504    846   1028    911       C  
ATOM   1958  C   ILE A 329     -25.419  35.375  -4.010  1.00137.15           C  
ANISOU 1958  C   ILE A 329    13186  24030  14895    330    971    972       C  
ATOM   1959  O   ILE A 329     -26.130  35.992  -3.214  1.00134.36           O  
ANISOU 1959  O   ILE A 329    13047  23424  14580    110    801    968       O  
ATOM   1960  CB  ILE A 329     -24.386  33.225  -2.942  1.00139.34           C  
ANISOU 1960  CB  ILE A 329    13173  24557  15215   1085    908    961       C  
ATOM   1961  CG1 ILE A 329     -24.554  31.692  -2.831  1.00139.81           C  
ANISOU 1961  CG1 ILE A 329    13361  24470  15289   1603    948    907       C  
ATOM   1962  CG2 ILE A 329     -24.510  33.870  -1.551  1.00138.88           C  
ANISOU 1962  CG2 ILE A 329    13124  24448  15197    848    646   1005       C  
ATOM   1963  CD1 ILE A 329     -23.338  30.934  -2.288  1.00150.92           C  
ANISOU 1963  CD1 ILE A 329    14388  26240  16714   1941    914    964       C  
ATOM   1964  N   ALA A 330     -24.690  35.987  -4.969  1.00135.83           N  
ANISOU 1964  N   ALA A 330    12774  24159  14678    143   1127   1027       N  
ATOM   1965  CA  ALA A 330     -24.655  37.441  -5.157  1.00135.71           C  
ANISOU 1965  CA  ALA A 330    12736  24167  14659   -351   1101   1099       C  
ATOM   1966  C   ALA A 330     -26.015  37.978  -5.645  1.00136.11           C  
ANISOU 1966  C   ALA A 330    13244  23779  14692   -521   1114   1067       C  
ATOM   1967  O   ALA A 330     -26.408  39.082  -5.264  1.00134.87           O  
ANISOU 1967  O   ALA A 330    13219  23456  14570   -876    997   1100       O  
ATOM   1968  CB  ALA A 330     -23.555  37.816  -6.138  1.00139.90           C  
ANISOU 1968  CB  ALA A 330    12899  25127  15131   -479   1292   1179       C  
ATOM   1969  N   GLY A 331     -26.713  37.189  -6.468  1.00130.65           N  
ANISOU 1969  N   GLY A 331    12787  22907  13946   -258   1248    995       N  
ATOM   1970  CA  GLY A 331     -28.028  37.527  -7.002  1.00127.12           C  
ANISOU 1970  CA  GLY A 331    12755  22075  13471   -358   1262    958       C  
ATOM   1971  C   GLY A 331     -29.123  37.508  -5.953  1.00126.88           C  
ANISOU 1971  C   GLY A 331    13035  21660  13515   -358   1065    901       C  
ATOM   1972  O   GLY A 331     -29.992  38.384  -5.948  1.00124.44           O  
ANISOU 1972  O   GLY A 331    12977  21090  13216   -604    999    912       O  
ATOM   1973  N   ILE A 332     -29.075  36.512  -5.043  1.00122.50           N  
ANISOU 1973  N   ILE A 332    12461  21076  13008    -72    974    850       N  
ATOM   1974  CA  ILE A 332     -30.037  36.335  -3.945  1.00119.23           C  
ANISOU 1974  CA  ILE A 332    12312  20336  12652    -36    798    803       C  
ATOM   1975  C   ILE A 332     -29.565  37.005  -2.649  1.00123.24           C  
ANISOU 1975  C   ILE A 332    12673  20943  13212   -232    602    849       C  
ATOM   1976  O   ILE A 332     -30.045  36.655  -1.570  1.00121.40           O  
ANISOU 1976  O   ILE A 332    12572  20543  13011   -139    457    818       O  
ATOM   1977  CB  ILE A 332     -30.428  34.843  -3.725  1.00121.30           C  
ANISOU 1977  CB  ILE A 332    12709  20452  12927    375    815    728       C  
ATOM   1978  CG1 ILE A 332     -29.212  33.930  -3.509  1.00124.17           C  
ANISOU 1978  CG1 ILE A 332    12753  21129  13295    672    852    750       C  
ATOM   1979  CG2 ILE A 332     -31.307  34.342  -4.837  1.00120.89           C  
ANISOU 1979  CG2 ILE A 332    12921  20184  12826    493    957    649       C  
ATOM   1980  CD1 ILE A 332     -29.179  33.314  -2.187  1.00129.78           C  
ANISOU 1980  CD1 ILE A 332    13468  21786  14058    847    689    763       C  
ATOM   1981  N   LEU A 333     -28.637  37.975  -2.760  1.00121.85           N  
ANISOU 1981  N   LEU A 333    12226  21039  13033   -518    599    920       N  
ATOM   1982  CA  LEU A 333     -28.051  38.689  -1.622  1.00122.76           C  
ANISOU 1982  CA  LEU A 333    12167  21292  13186   -748    413    952       C  
ATOM   1983  C   LEU A 333     -29.060  39.517  -0.845  1.00124.13           C  
ANISOU 1983  C   LEU A 333    12653  21125  13388   -979    255    911       C  
ATOM   1984  O   LEU A 333     -29.018  39.495   0.385  1.00123.65           O  
ANISOU 1984  O   LEU A 333    12580  21061  13342   -978     79    887       O  
ATOM   1985  CB  LEU A 333     -26.879  39.572  -2.063  1.00125.87           C  
ANISOU 1985  CB  LEU A 333    12212  22040  13572  -1045    464   1035       C  
ATOM   1986  CG  LEU A 333     -25.460  39.208  -1.637  1.00133.86           C  
ANISOU 1986  CG  LEU A 333    12756  23521  14585   -960    434   1081       C  
ATOM   1987  CD1 LEU A 333     -24.506  40.320  -1.971  1.00137.05           C  
ANISOU 1987  CD1 LEU A 333    12861  24223  14990  -1356    464   1161       C  
ATOM   1988  CD2 LEU A 333     -25.359  38.892  -0.158  1.00135.97           C  
ANISOU 1988  CD2 LEU A 333    12977  23809  14875   -873    203   1055       C  
ATOM   1989  N   GLN A 334     -29.978  40.224  -1.553  1.00118.81           N  
ANISOU 1989  N   GLN A 334    12260  20173  12711  -1153    318    902       N  
ATOM   1990  CA  GLN A 334     -31.045  41.041  -0.946  1.00116.45           C  
ANISOU 1990  CA  GLN A 334    12280  19527  12439  -1344    193    857       C  
ATOM   1991  C   GLN A 334     -31.999  40.149  -0.137  1.00117.02           C  
ANISOU 1991  C   GLN A 334    12578  19368  12515  -1074    113    781       C  
ATOM   1992  O   GLN A 334     -32.486  40.571   0.911  1.00115.67           O  
ANISOU 1992  O   GLN A 334    12548  19044  12359  -1170    -38    737       O  
ATOM   1993  CB  GLN A 334     -31.832  41.823  -2.014  1.00116.87           C  
ANISOU 1993  CB  GLN A 334    12574  19350  12482  -1512    295    878       C  
ATOM   1994  CG  GLN A 334     -31.004  42.842  -2.788  1.00142.73           C  
ANISOU 1994  CG  GLN A 334    15678  22803  15750  -1828    373    975       C  
ATOM   1995  CD  GLN A 334     -31.648  43.200  -4.104  1.00169.11           C  
ANISOU 1995  CD  GLN A 334    19217  25988  19047  -1877    520   1022       C  
ATOM   1996  OE1 GLN A 334     -31.611  42.433  -5.076  1.00166.33           O  
ANISOU 1996  OE1 GLN A 334    18826  25741  18632  -1670    677   1032       O  
ATOM   1997  NE2 GLN A 334     -32.233  44.387  -4.174  1.00162.84           N  
ANISOU 1997  NE2 GLN A 334    18647  24947  18278  -2147    472   1052       N  
ATOM   1998  N   ALA A 335     -32.239  38.909  -0.622  1.00111.95           N  
ANISOU 1998  N   ALA A 335    11973  18709  11856   -742    220    763       N  
ATOM   1999  CA  ALA A 335     -33.080  37.903   0.025  1.00109.35           C  
ANISOU 1999  CA  ALA A 335    11846  18170  11532   -476    172    707       C  
ATOM   2000  C   ALA A 335     -32.438  37.385   1.314  1.00114.10           C  
ANISOU 2000  C   ALA A 335    12286  18930  12135   -351     33    723       C  
ATOM   2001  O   ALA A 335     -33.155  37.134   2.281  1.00113.02           O  
ANISOU 2001  O   ALA A 335    12334  18611  11997   -288    -74    692       O  
ATOM   2002  CB  ALA A 335     -33.352  36.754  -0.927  1.00109.51           C  
ANISOU 2002  CB  ALA A 335    11935  18140  11535   -186    329    682       C  
ATOM   2003  N   LEU A 336     -31.097  37.247   1.338  1.00112.19           N  
ANISOU 2003  N   LEU A 336    11693  19048  11888   -317     34    778       N  
ATOM   2004  CA  LEU A 336     -30.363  36.780   2.517  1.00112.99           C  
ANISOU 2004  CA  LEU A 336    11599  19355  11978   -190   -110    809       C  
ATOM   2005  C   LEU A 336     -30.268  37.876   3.569  1.00116.09           C  
ANISOU 2005  C   LEU A 336    11973  19778  12357   -500   -299    796       C  
ATOM   2006  O   LEU A 336     -30.464  37.591   4.747  1.00115.45           O  
ANISOU 2006  O   LEU A 336    11956  19663  12247   -421   -445    785       O  
ATOM   2007  CB  LEU A 336     -28.959  36.262   2.158  1.00116.22           C  
ANISOU 2007  CB  LEU A 336    11609  20168  12382    -30    -48    871       C  
ATOM   2008  CG  LEU A 336     -28.843  35.128   1.131  1.00121.35           C  
ANISOU 2008  CG  LEU A 336    12239  20835  13034    310    145    869       C  
ATOM   2009  CD1 LEU A 336     -27.402  34.894   0.769  1.00124.93           C  
ANISOU 2009  CD1 LEU A 336    12262  21727  13479    416    209    927       C  
ATOM   2010  CD2 LEU A 336     -29.483  33.830   1.626  1.00122.98           C  
ANISOU 2010  CD2 LEU A 336    12667  20811  13250    671    127    849       C  
ATOM   2011  N   ILE A 337     -29.979  39.129   3.148  1.00112.89           N  
ANISOU 2011  N   ILE A 337    11498  19428  11967   -859   -294    795       N  
ATOM   2012  CA  ILE A 337     -29.877  40.291   4.039  1.00113.22           C  
ANISOU 2012  CA  ILE A 337    11546  19470  12002  -1195   -466    761       C  
ATOM   2013  C   ILE A 337     -31.261  40.578   4.669  1.00115.16           C  
ANISOU 2013  C   ILE A 337    12190  19325  12239  -1225   -537    681       C  
ATOM   2014  O   ILE A 337     -31.315  40.923   5.853  1.00115.53           O  
ANISOU 2014  O   ILE A 337    12278  19368  12249  -1318   -706    635       O  
ATOM   2015  CB  ILE A 337     -29.189  41.512   3.342  1.00117.80           C  
ANISOU 2015  CB  ILE A 337    11965  20183  12612  -1575   -426    791       C  
ATOM   2016  CG1 ILE A 337     -27.686  41.231   3.154  1.00121.28           C  
ANISOU 2016  CG1 ILE A 337    11943  21093  13046  -1560   -406    865       C  
ATOM   2017  CG2 ILE A 337     -29.372  42.831   4.112  1.00118.72           C  
ANISOU 2017  CG2 ILE A 337    12204  20171  12735  -1953   -585    730       C  
ATOM   2018  CD1 ILE A 337     -27.106  41.726   1.882  1.00128.73           C  
ANISOU 2018  CD1 ILE A 337    12716  22185  14010  -1738   -235    932       C  
ATOM   2019  N   THR A 338     -32.370  40.350   3.917  1.00109.13           N  
ANISOU 2019  N   THR A 338    11703  18265  11497  -1124   -410    662       N  
ATOM   2020  CA  THR A 338     -33.723  40.511   4.466  1.00106.53           C  
ANISOU 2020  CA  THR A 338    11721  17594  11160  -1115   -460    591       C  
ATOM   2021  C   THR A 338     -34.061  39.355   5.407  1.00109.88           C  
ANISOU 2021  C   THR A 338    12207  17996  11545   -824   -520    586       C  
ATOM   2022  O   THR A 338     -34.839  39.556   6.336  1.00108.95           O  
ANISOU 2022  O   THR A 338    12289  17711  11396   -850   -614    533       O  
ATOM   2023  CB  THR A 338     -34.804  40.756   3.400  1.00114.12           C  
ANISOU 2023  CB  THR A 338    12936  18272  12153  -1131   -327    574       C  
ATOM   2024  OG1 THR A 338     -34.700  39.782   2.367  1.00116.11           O  
ANISOU 2024  OG1 THR A 338    13127  18581  12409   -906   -174    614       O  
ATOM   2025  CG2 THR A 338     -34.756  42.159   2.815  1.00113.61           C  
ANISOU 2025  CG2 THR A 338    12910  18139  12116  -1459   -314    580       C  
ATOM   2026  N   ALA A 339     -33.479  38.151   5.184  1.00106.79           N  
ANISOU 2026  N   ALA A 339    11653  17769  11153   -541   -460    646       N  
ATOM   2027  CA  ALA A 339     -33.696  36.988   6.058  1.00106.05           C  
ANISOU 2027  CA  ALA A 339    11618  17652  11025   -254   -513    670       C  
ATOM   2028  C   ALA A 339     -32.999  37.221   7.399  1.00110.71           C  
ANISOU 2028  C   ALA A 339    12056  18460  11550   -311   -705    686       C  
ATOM   2029  O   ALA A 339     -33.560  36.924   8.452  1.00109.38           O  
ANISOU 2029  O   ALA A 339    12044  18193  11324   -235   -800    677       O  
ATOM   2030  CB  ALA A 339     -33.177  35.719   5.399  1.00107.70           C  
ANISOU 2030  CB  ALA A 339    11700  17964  11258     64   -396    727       C  
ATOM   2031  N   LEU A 340     -31.805  37.831   7.343  1.00109.46           N  
ANISOU 2031  N   LEU A 340    11593  18607  11390   -476   -763    706       N  
ATOM   2032  CA  LEU A 340     -30.956  38.210   8.472  1.00111.59           C  
ANISOU 2032  CA  LEU A 340    11659  19148  11593   -588   -958    712       C  
ATOM   2033  C   LEU A 340     -31.655  39.251   9.359  1.00114.85           C  
ANISOU 2033  C   LEU A 340    12294  19388  11957   -855  -1088    613       C  
ATOM   2034  O   LEU A 340     -31.396  39.300  10.559  1.00115.81           O  
ANISOU 2034  O   LEU A 340    12374  19641  11987   -873  -1259    598       O  
ATOM   2035  CB  LEU A 340     -29.629  38.767   7.902  1.00114.22           C  
ANISOU 2035  CB  LEU A 340    11619  19823  11956   -767   -954    744       C  
ATOM   2036  CG  LEU A 340     -28.498  39.246   8.831  1.00121.78           C  
ANISOU 2036  CG  LEU A 340    12272  21144  12856   -934  -1152    750       C  
ATOM   2037  CD1 LEU A 340     -28.122  38.207   9.887  1.00123.22           C  
ANISOU 2037  CD1 LEU A 340    12345  21519  12955   -625  -1283    812       C  
ATOM   2038  CD2 LEU A 340     -27.277  39.615   8.020  1.00126.45           C  
ANISOU 2038  CD2 LEU A 340    12483  22068  13495  -1082  -1095    797       C  
ATOM   2039  N   GLY A 341     -32.531  40.053   8.757  1.00109.51           N  
ANISOU 2039  N   GLY A 341    11853  18424  11331  -1041  -1005    546       N  
ATOM   2040  CA  GLY A 341     -33.273  41.105   9.439  1.00108.72           C  
ANISOU 2040  CA  GLY A 341    11990  18119  11198  -1277  -1099    439       C  
ATOM   2041  C   GLY A 341     -34.603  40.682  10.031  1.00110.24           C  
ANISOU 2041  C   GLY A 341    12501  18037  11349  -1117  -1089    397       C  
ATOM   2042  O   GLY A 341     -34.901  41.027  11.179  1.00110.26           O  
ANISOU 2042  O   GLY A 341    12613  18016  11263  -1182  -1217    329       O  
ATOM   2043  N   THR A 342     -35.415  39.942   9.247  1.00104.21           N  
ANISOU 2043  N   THR A 342    11881  17075  10637   -918   -933    432       N  
ATOM   2044  CA  THR A 342     -36.750  39.486   9.647  1.00101.66           C  
ANISOU 2044  CA  THR A 342    11845  16492  10289   -776   -897    402       C  
ATOM   2045  C   THR A 342     -36.738  38.195  10.470  1.00105.70           C  
ANISOU 2045  C   THR A 342    12348  17080  10734   -500   -932    474       C  
ATOM   2046  O   THR A 342     -37.522  38.073  11.414  1.00104.33           O  
ANISOU 2046  O   THR A 342    12356  16798  10485   -460   -980    447       O  
ATOM   2047  CB  THR A 342     -37.667  39.312   8.424  1.00107.05           C  
ANISOU 2047  CB  THR A 342    12687  16933  11056   -719   -728    401       C  
ATOM   2048  OG1 THR A 342     -37.226  38.201   7.639  1.00106.97           O  
ANISOU 2048  OG1 THR A 342    12554  17006  11085   -503   -624    481       O  
ATOM   2049  CG2 THR A 342     -37.784  40.574   7.575  1.00105.16           C  
ANISOU 2049  CG2 THR A 342    12491  16590  10874   -971   -688    354       C  
ATOM   2050  N   SER A 343     -35.866  37.229  10.097  1.00103.74           N  
ANISOU 2050  N   SER A 343    11896  17012  10509   -300   -897    571       N  
ATOM   2051  CA  SER A 343     -35.738  35.888  10.693  1.00104.35           C  
ANISOU 2051  CA  SER A 343    11961  17146  10542      1   -914    667       C  
ATOM   2052  C   SER A 343     -36.977  35.042  10.376  1.00105.76           C  
ANISOU 2052  C   SER A 343    12408  17019  10756    165   -784    676       C  
ATOM   2053  O   SER A 343     -37.428  34.240  11.200  1.00105.58           O  
ANISOU 2053  O   SER A 343    12512  16928  10677    323   -811    730       O  
ATOM   2054  CB  SER A 343     -35.465  35.952  12.196  1.00109.88           C  
ANISOU 2054  CB  SER A 343    12636  18003  11110     -4  -1094    685       C  
ATOM   2055  OG  SER A 343     -35.185  34.665  12.715  1.00119.19           O  
ANISOU 2055  OG  SER A 343    13783  19257  12246    297  -1115    808       O  
ATOM   2056  N   SER A 344     -37.509  35.219   9.159  1.00100.16           N  
ANISOU 2056  N   SER A 344    11780  16139  10137    113   -646    628       N  
ATOM   2057  CA  SER A 344     -38.687  34.519   8.669  1.00 97.87           C  
ANISOU 2057  CA  SER A 344    11724  15574   9890    223   -523    616       C  
ATOM   2058  C   SER A 344     -38.450  34.100   7.220  1.00102.16           C  
ANISOU 2058  C   SER A 344    12208  16091  10516    305   -382    614       C  
ATOM   2059  O   SER A 344     -38.139  34.955   6.386  1.00102.14           O  
ANISOU 2059  O   SER A 344    12116  16149  10544    144   -347    576       O  
ATOM   2060  CB  SER A 344     -39.910  35.425   8.789  1.00 98.89           C  
ANISOU 2060  CB  SER A 344    12060  15501  10010     30   -520    527       C  
ATOM   2061  OG  SER A 344     -41.095  34.811   8.314  1.00104.39           O  
ANISOU 2061  OG  SER A 344    12959  15957  10748    110   -410    510       O  
ATOM   2062  N   SER A 345     -38.542  32.782   6.928  1.00 98.86           N  
ANISOU 2062  N   SER A 345    11847  15587  10127    554   -301    657       N  
ATOM   2063  CA  SER A 345     -38.371  32.246   5.568  1.00 98.51           C  
ANISOU 2063  CA  SER A 345    11776  15507  10145    663   -159    635       C  
ATOM   2064  C   SER A 345     -39.590  32.616   4.726  1.00100.44           C  
ANISOU 2064  C   SER A 345    12222  15523  10418    531    -73    551       C  
ATOM   2065  O   SER A 345     -39.457  32.845   3.522  1.00100.18           O  
ANISOU 2065  O   SER A 345    12146  15507  10409    494     20    512       O  
ATOM   2066  CB  SER A 345     -38.191  30.731   5.590  1.00102.60           C  
ANISOU 2066  CB  SER A 345    12339  15959  10686    969   -106    689       C  
ATOM   2067  OG  SER A 345     -36.861  30.358   5.906  1.00113.08           O  
ANISOU 2067  OG  SER A 345    13426  17540  12001   1139   -152    766       O  
ATOM   2068  N   SER A 346     -40.773  32.698   5.374  1.00 95.44           N  
ANISOU 2068  N   SER A 346    11794  14698   9771    463   -106    529       N  
ATOM   2069  CA  SER A 346     -42.030  33.067   4.739  1.00 93.58           C  
ANISOU 2069  CA  SER A 346    11738  14263   9557    345    -46    455       C  
ATOM   2070  C   SER A 346     -42.068  34.553   4.396  1.00 97.84           C  
ANISOU 2070  C   SER A 346    12235  14849  10089    113    -76    412       C  
ATOM   2071  O   SER A 346     -42.440  34.886   3.275  1.00 97.71           O  
ANISOU 2071  O   SER A 346    12259  14772  10095     51     -2    372       O  
ATOM   2072  CB  SER A 346     -43.224  32.672   5.602  1.00 96.16           C  
ANISOU 2072  CB  SER A 346    12262  14407   9869    353    -66    453       C  
ATOM   2073  OG  SER A 346     -43.233  33.358   6.842  1.00106.81           O  
ANISOU 2073  OG  SER A 346    13602  15822  11157    260   -175    468       O  
ATOM   2074  N   ALA A 347     -41.653  35.442   5.322  1.00 94.77           N  
ANISOU 2074  N   ALA A 347    11777  14568   9666    -14   -187    420       N  
ATOM   2075  CA  ALA A 347     -41.645  36.889   5.066  1.00 94.64           C  
ANISOU 2075  CA  ALA A 347    11746  14563   9651   -244   -221    380       C  
ATOM   2076  C   ALA A 347     -40.687  37.316   3.959  1.00 99.97           C  
ANISOU 2076  C   ALA A 347    12255  15378  10352   -316   -167    403       C  
ATOM   2077  O   ALA A 347     -40.987  38.270   3.242  1.00 99.61           O  
ANISOU 2077  O   ALA A 347    12260  15266  10322   -474   -140    382       O  
ATOM   2078  CB  ALA A 347     -41.344  37.666   6.335  1.00 96.15           C  
ANISOU 2078  CB  ALA A 347    11907  14831   9793   -365   -355    365       C  
ATOM   2079  N   THR A 348     -39.550  36.617   3.808  1.00 97.68           N  
ANISOU 2079  N   THR A 348    11767  15285  10060   -193   -146    455       N  
ATOM   2080  CA  THR A 348     -38.561  36.976   2.789  1.00 98.56           C  
ANISOU 2080  CA  THR A 348    11688  15575  10184   -258    -80    484       C  
ATOM   2081  C   THR A 348     -38.811  36.272   1.458  1.00102.14           C  
ANISOU 2081  C   THR A 348    12186  15975  10649   -126     70    473       C  
ATOM   2082  O   THR A 348     -38.163  36.618   0.467  1.00103.08           O  
ANISOU 2082  O   THR A 348    12177  16229  10760   -187    150    494       O  
ATOM   2083  CB  THR A 348     -37.137  36.801   3.307  1.00106.43           C  
ANISOU 2083  CB  THR A 348    12409  16863  11168   -220   -138    540       C  
ATOM   2084  OG1 THR A 348     -36.934  35.455   3.733  1.00105.87           O  
ANISOU 2084  OG1 THR A 348    12311  16825  11092     62   -132    570       O  
ATOM   2085  CG2 THR A 348     -36.842  37.744   4.435  1.00105.45           C  
ANISOU 2085  CG2 THR A 348    12235  16813  11019   -417   -292    533       C  
ATOM   2086  N   LEU A 349     -39.796  35.344   1.416  1.00 96.96           N  
ANISOU 2086  N   LEU A 349    11720  15122  10000     30    110    435       N  
ATOM   2087  CA  LEU A 349     -40.194  34.611   0.210  1.00 96.01           C  
ANISOU 2087  CA  LEU A 349    11681  14920   9880    150    238    396       C  
ATOM   2088  C   LEU A 349     -40.512  35.542  -0.983  1.00 97.83           C  
ANISOU 2088  C   LEU A 349    11948  15136  10087    -17    300    380       C  
ATOM   2089  O   LEU A 349     -39.959  35.281  -2.048  1.00 98.06           O  
ANISOU 2089  O   LEU A 349    11891  15280  10088     41    407    380       O  
ATOM   2090  CB  LEU A 349     -41.348  33.627   0.499  1.00 94.87           C  
ANISOU 2090  CB  LEU A 349    11755  14540   9751    277    246    351       C  
ATOM   2091  CG  LEU A 349     -41.844  32.747  -0.652  1.00 99.45           C  
ANISOU 2091  CG  LEU A 349    12446  15013  10329    394    362    287       C  
ATOM   2092  CD1 LEU A 349     -40.810  31.701  -1.038  1.00101.50           C  
ANISOU 2092  CD1 LEU A 349    12592  15385  10590    619    441    291       C  
ATOM   2093  CD2 LEU A 349     -43.146  32.081  -0.288  1.00100.36           C  
ANISOU 2093  CD2 LEU A 349    12781  14887  10466    426    348    243       C  
ATOM   2094  N   PRO A 350     -41.297  36.652  -0.853  1.00 92.84           N  
ANISOU 2094  N   PRO A 350    11432  14384   9457   -210    242    374       N  
ATOM   2095  CA  PRO A 350     -41.522  37.519  -2.022  1.00 92.71           C  
ANISOU 2095  CA  PRO A 350    11454  14359   9414   -348    299    385       C  
ATOM   2096  C   PRO A 350     -40.242  38.135  -2.589  1.00100.16           C  
ANISOU 2096  C   PRO A 350    12192  15528  10336   -457    345    453       C  
ATOM   2097  O   PRO A 350     -40.142  38.328  -3.808  1.00100.51           O  
ANISOU 2097  O   PRO A 350    12226  15628  10333   -488    444    473       O  
ATOM   2098  CB  PRO A 350     -42.502  38.570  -1.495  1.00 93.02           C  
ANISOU 2098  CB  PRO A 350    11649  14222   9472   -501    208    373       C  
ATOM   2099  CG  PRO A 350     -42.305  38.580  -0.039  1.00 97.33           C  
ANISOU 2099  CG  PRO A 350    12165  14772  10045   -507    104    366       C  
ATOM   2100  CD  PRO A 350     -42.049  37.158   0.314  1.00 93.12           C  
ANISOU 2100  CD  PRO A 350    11583  14286   9512   -293    129    357       C  
ATOM   2101  N   ILE A 351     -39.241  38.390  -1.713  1.00 98.60           N  
ANISOU 2101  N   ILE A 351    11818  15484  10163   -515    277    490       N  
ATOM   2102  CA  ILE A 351     -37.948  38.950  -2.119  1.00100.44           C  
ANISOU 2102  CA  ILE A 351    11814  15965  10383   -641    315    559       C  
ATOM   2103  C   ILE A 351     -37.039  37.834  -2.695  1.00105.58           C  
ANISOU 2103  C   ILE A 351    12274  16835  11007   -425    428    566       C  
ATOM   2104  O   ILE A 351     -36.300  38.116  -3.639  1.00107.09           O  
ANISOU 2104  O   ILE A 351    12317  17212  11161   -487    532    612       O  
ATOM   2105  CB  ILE A 351     -37.311  39.818  -0.999  1.00104.38           C  
ANISOU 2105  CB  ILE A 351    12201  16544  10915   -833    182    584       C  
ATOM   2106  CG1 ILE A 351     -38.050  41.178  -0.945  1.00104.31           C  
ANISOU 2106  CG1 ILE A 351    12382  16328  10924  -1079    121    581       C  
ATOM   2107  CG2 ILE A 351     -35.801  40.027  -1.200  1.00107.26           C  
ANISOU 2107  CG2 ILE A 351    12251  17229  11272   -922    211    651       C  
ATOM   2108  CD1 ILE A 351     -37.732  42.091   0.229  1.00116.39           C  
ANISOU 2108  CD1 ILE A 351    13888  17853  12482  -1278    -24    566       C  
ATOM   2109  N   THR A 352     -37.155  36.568  -2.209  1.00100.99           N  
ANISOU 2109  N   THR A 352    11716  16216  10440   -165    423    522       N  
ATOM   2110  CA  THR A 352     -36.395  35.433  -2.763  1.00101.90           C  
ANISOU 2110  CA  THR A 352    11691  16492  10535     86    536    513       C  
ATOM   2111  C   THR A 352     -36.884  35.172  -4.196  1.00105.39           C  
ANISOU 2111  C   THR A 352    12251  16871  10919    136    680    465       C  
ATOM   2112  O   THR A 352     -36.084  34.817  -5.067  1.00107.02           O  
ANISOU 2112  O   THR A 352    12306  17277  11079    235    808    467       O  
ATOM   2113  CB  THR A 352     -36.494  34.189  -1.866  1.00108.12           C  
ANISOU 2113  CB  THR A 352    12525  17199  11358    347    487    488       C  
ATOM   2114  OG1 THR A 352     -36.178  34.553  -0.525  1.00109.80           O  
ANISOU 2114  OG1 THR A 352    12656  17467  11597    275    338    535       O  
ATOM   2115  CG2 THR A 352     -35.554  33.079  -2.300  1.00107.34           C  
ANISOU 2115  CG2 THR A 352    12264  17271  11250    627    591    484       C  
ATOM   2116  N   PHE A 353     -38.190  35.408  -4.436  1.00 99.47           N  
ANISOU 2116  N   PHE A 353    11760  15871  10163     60    657    420       N  
ATOM   2117  CA  PHE A 353     -38.826  35.281  -5.737  1.00 98.93           C  
ANISOU 2117  CA  PHE A 353    11829  15735  10025     76    761    372       C  
ATOM   2118  C   PHE A 353     -38.267  36.325  -6.700  1.00105.44           C  
ANISOU 2118  C   PHE A 353    12543  16737  10782   -110    835    446       C  
ATOM   2119  O   PHE A 353     -37.798  35.946  -7.773  1.00106.55           O  
ANISOU 2119  O   PHE A 353    12613  17028  10841    -24    972    432       O  
ATOM   2120  CB  PHE A 353     -40.345  35.416  -5.617  1.00 98.22           C  
ANISOU 2120  CB  PHE A 353    12005  15368   9948     17    690    323       C  
ATOM   2121  CG  PHE A 353     -41.089  34.105  -5.609  1.00 98.81           C  
ANISOU 2121  CG  PHE A 353    12235  15276  10033    215    708    223       C  
ATOM   2122  CD1 PHE A 353     -41.431  33.490  -4.414  1.00100.87           C  
ANISOU 2122  CD1 PHE A 353    12545  15415  10368    312    632    210       C  
ATOM   2123  CD2 PHE A 353     -41.487  33.504  -6.796  1.00101.36           C  
ANISOU 2123  CD2 PHE A 353    12673  15554  10285    284    797    142       C  
ATOM   2124  CE1 PHE A 353     -42.139  32.287  -4.406  1.00101.46           C  
ANISOU 2124  CE1 PHE A 353    12780  15310  10460    466    652    129       C  
ATOM   2125  CE2 PHE A 353     -42.183  32.295  -6.787  1.00103.94           C  
ANISOU 2125  CE2 PHE A 353    13158  15707  10629    436    808     39       C  
ATOM   2126  CZ  PHE A 353     -42.490  31.685  -5.592  1.00101.34           C  
ANISOU 2126  CZ  PHE A 353    12872  15243  10388    524    741     38       C  
ATOM   2127  N   LYS A 354     -38.268  37.623  -6.301  1.00102.70           N  
ANISOU 2127  N   LYS A 354    12185  16374  10465   -363    752    526       N  
ATOM   2128  CA  LYS A 354     -37.746  38.733  -7.115  1.00104.41           C  
ANISOU 2128  CA  LYS A 354    12316  16726  10628   -582    813    623       C  
ATOM   2129  C   LYS A 354     -36.265  38.530  -7.502  1.00112.12           C  
ANISOU 2129  C   LYS A 354    12991  18038  11570   -557    925    673       C  
ATOM   2130  O   LYS A 354     -35.894  38.781  -8.651  1.00113.41           O  
ANISOU 2130  O   LYS A 354    13095  18353  11642   -610   1057    721       O  
ATOM   2131  CB  LYS A 354     -37.975  40.089  -6.413  1.00106.18           C  
ANISOU 2131  CB  LYS A 354    12601  16830  10915   -849    689    687       C  
ATOM   2132  CG  LYS A 354     -37.612  41.308  -7.268  1.00119.23           C  
ANISOU 2132  CG  LYS A 354    14228  18552  12521  -1100    746    802       C  
ATOM   2133  CD  LYS A 354     -38.759  42.293  -7.427  1.00126.37           C  
ANISOU 2133  CD  LYS A 354    15396  19188  13431  -1236    678    830       C  
ATOM   2134  CE  LYS A 354     -39.688  41.928  -8.560  1.00134.01           C  
ANISOU 2134  CE  LYS A 354    16533  20081  14304  -1116    749    810       C  
ATOM   2135  NZ  LYS A 354     -40.722  42.966  -8.787  1.00140.88           N  
ANISOU 2135  NZ  LYS A 354    17632  20724  15174  -1238    683    861       N  
ATOM   2136  N   CYS A 355     -35.446  38.037  -6.558  1.00109.61           N  
ANISOU 2136  N   CYS A 355    12479  17853  11315   -462    876    665       N  
ATOM   2137  CA  CYS A 355     -34.028  37.776  -6.773  1.00112.06           C  
ANISOU 2137  CA  CYS A 355    12464  18509  11604   -409    968    710       C  
ATOM   2138  C   CYS A 355     -33.766  36.623  -7.732  1.00117.11           C  
ANISOU 2138  C   CYS A 355    13060  19270  12168   -124   1134    646       C  
ATOM   2139  O   CYS A 355     -32.988  36.792  -8.660  1.00118.87           O  
ANISOU 2139  O   CYS A 355    13107  19746  12312   -154   1278    690       O  
ATOM   2140  CB  CYS A 355     -33.302  37.581  -5.448  1.00112.99           C  
ANISOU 2140  CB  CYS A 355    12390  18739  11803   -372    845    722       C  
ATOM   2141  SG  CYS A 355     -33.257  39.060  -4.406  1.00116.65           S  
ANISOU 2141  SG  CYS A 355    12844  19146  12332   -745    666    785       S  
ATOM   2142  N   LEU A 356     -34.413  35.467  -7.530  1.00112.48           N  
ANISOU 2142  N   LEU A 356    12642  18498  11599    141   1122    540       N  
ATOM   2143  CA  LEU A 356     -34.214  34.299  -8.389  1.00113.50           C  
ANISOU 2143  CA  LEU A 356    12769  18695  11662    430   1273    451       C  
ATOM   2144  C   LEU A 356     -34.775  34.489  -9.801  1.00117.18           C  
ANISOU 2144  C   LEU A 356    13387  19133  12002    376   1396    415       C  
ATOM   2145  O   LEU A 356     -34.077  34.184 -10.768  1.00118.47           O  
ANISOU 2145  O   LEU A 356    13421  19527  12067    478   1560    398       O  
ATOM   2146  CB  LEU A 356     -34.832  33.055  -7.728  1.00112.44           C  
ANISOU 2146  CB  LEU A 356    12812  18319  11593    692   1211    352       C  
ATOM   2147  CG  LEU A 356     -33.969  31.895  -7.255  1.00118.97           C  
ANISOU 2147  CG  LEU A 356    13493  19252  12458   1019   1249    320       C  
ATOM   2148  CD1 LEU A 356     -32.612  32.303  -6.831  1.00121.33           C  
ANISOU 2148  CD1 LEU A 356    13432  19890  12780   1007   1243    419       C  
ATOM   2149  CD2 LEU A 356     -34.635  31.164  -6.171  1.00119.96           C  
ANISOU 2149  CD2 LEU A 356    13802  19104  12671   1154   1129    286       C  
ATOM   2150  N   GLU A 357     -36.021  34.996  -9.921  1.00112.30           N  
ANISOU 2150  N   GLU A 357    13034  18258  11376    225   1317    404       N  
ATOM   2151  CA  GLU A 357     -36.679  35.226 -11.207  1.00112.45           C  
ANISOU 2151  CA  GLU A 357    13217  18245  11265    168   1402    379       C  
ATOM   2152  C   GLU A 357     -35.896  36.216 -12.059  1.00119.32           C  
ANISOU 2152  C   GLU A 357    13923  19378  12037    -23   1510    502       C  
ATOM   2153  O   GLU A 357     -35.739  35.990 -13.265  1.00120.99           O  
ANISOU 2153  O   GLU A 357    14136  19733  12101     39   1658    476       O  
ATOM   2154  CB  GLU A 357     -38.122  35.717 -11.017  1.00111.36           C  
ANISOU 2154  CB  GLU A 357    13353  17807  11151     35   1272    369       C  
ATOM   2155  CG  GLU A 357     -39.126  34.614 -10.714  1.00121.71           C  
ANISOU 2155  CG  GLU A 357    14873  18873  12500    217   1218    229       C  
ATOM   2156  CD  GLU A 357     -40.568  35.063 -10.560  1.00144.88           C  
ANISOU 2156  CD  GLU A 357    18042  21552  15453     95   1098    216       C  
ATOM   2157  OE1 GLU A 357     -40.827  36.285 -10.652  1.00142.65           O  
ANISOU 2157  OE1 GLU A 357    17781  21258  15160   -113   1048    318       O  
ATOM   2158  OE2 GLU A 357     -41.445  34.189 -10.373  1.00138.06           O  
ANISOU 2158  OE2 GLU A 357    17340  20499  14616    210   1058    105       O  
ATOM   2159  N   GLU A 358     -35.373  37.289 -11.427  1.00116.05           N  
ANISOU 2159  N   GLU A 358    13367  19033  11695   -261   1441    633       N  
ATOM   2160  CA  GLU A 358     -34.624  38.336 -12.120  1.00117.95           C  
ANISOU 2160  CA  GLU A 358    13454  19500  11860   -497   1534    774       C  
ATOM   2161  C   GLU A 358     -33.109  38.143 -12.090  1.00124.04           C  
ANISOU 2161  C   GLU A 358    13862  20638  12629   -462   1643    820       C  
ATOM   2162  O   GLU A 358     -32.541  37.632 -13.057  1.00125.44           O  
ANISOU 2162  O   GLU A 358    13921  21053  12685   -327   1822    798       O  
ATOM   2163  CB  GLU A 358     -35.007  39.731 -11.600  1.00118.54           C  
ANISOU 2163  CB  GLU A 358    13621  19411  12009   -817   1401    891       C  
ATOM   2164  CG  GLU A 358     -36.429  40.142 -11.925  1.00129.34           C  
ANISOU 2164  CG  GLU A 358    15316  20478  13347   -868   1326    880       C  
ATOM   2165  CD  GLU A 358     -36.875  41.476 -11.362  1.00156.23           C  
ANISOU 2165  CD  GLU A 358    18841  23684  16837  -1138   1193    979       C  
ATOM   2166  OE1 GLU A 358     -36.025  42.236 -10.842  1.00153.43           O  
ANISOU 2166  OE1 GLU A 358    18324  23425  16549  -1343   1167   1067       O  
ATOM   2167  OE2 GLU A 358     -38.089  41.767 -11.457  1.00154.42           O  
ANISOU 2167  OE2 GLU A 358    18868  23202  16604  -1142   1114    962       O  
ATOM   2168  N   ASN A 359     -32.468  38.566 -10.983  1.00120.82           N  
ANISOU 2168  N   ASN A 359    13269  20292  12346   -585   1534    877       N  
ATOM   2169  CA  ASN A 359     -31.024  38.573 -10.723  1.00123.36           C  
ANISOU 2169  CA  ASN A 359    13207  20975  12690   -606   1591    939       C  
ATOM   2170  C   ASN A 359     -30.297  37.269 -11.115  1.00128.05           C  
ANISOU 2170  C   ASN A 359    13610  21814  13230   -246   1737    852       C  
ATOM   2171  O   ASN A 359     -29.211  37.340 -11.695  1.00130.98           O  
ANISOU 2171  O   ASN A 359    13687  22545  13533   -258   1889    911       O  
ATOM   2172  CB  ASN A 359     -30.744  38.947  -9.254  1.00125.63           C  
ANISOU 2172  CB  ASN A 359    13392  21219  13122   -724   1397    962       C  
ATOM   2173  CG  ASN A 359     -31.614  40.057  -8.677  1.00156.96           C  
ANISOU 2173  CG  ASN A 359    17601  24880  17156  -1010   1234   1000       C  
ATOM   2174  OD1 ASN A 359     -32.256  40.839  -9.393  1.00153.75           O  
ANISOU 2174  OD1 ASN A 359    17395  24325  16700  -1189   1265   1054       O  
ATOM   2175  ND2 ASN A 359     -31.638  40.164  -7.354  1.00149.60           N  
ANISOU 2175  ND2 ASN A 359    16657  23852  16330  -1049   1057    975       N  
ATOM   2176  N   ASN A 360     -30.896  36.094 -10.822  1.00121.75           N  
ANISOU 2176  N   ASN A 360    12982  20817  12461     70   1701    716       N  
ATOM   2177  CA  ASN A 360     -30.318  34.789 -11.167  1.00122.62           C  
ANISOU 2177  CA  ASN A 360    12972  21087  12531    447   1833    615       C  
ATOM   2178  C   ASN A 360     -30.909  34.195 -12.450  1.00125.62           C  
ANISOU 2178  C   ASN A 360    13565  21396  12769    603   1987    506       C  
ATOM   2179  O   ASN A 360     -30.353  33.235 -12.987  1.00127.43           O  
ANISOU 2179  O   ASN A 360    13694  21789  12934    896   2136    417       O  
ATOM   2180  CB  ASN A 360     -30.426  33.801  -9.999  1.00121.51           C  
ANISOU 2180  CB  ASN A 360    12866  20789  12513    708   1704    543       C  
ATOM   2181  CG  ASN A 360     -29.427  34.003  -8.881  1.00143.93           C  
ANISOU 2181  CG  ASN A 360    15393  23842  15450    680   1599    630       C  
ATOM   2182  OD1 ASN A 360     -28.448  34.753  -8.984  1.00141.29           O  
ANISOU 2182  OD1 ASN A 360    14752  23833  15101    492   1639    732       O  
ATOM   2183  ND2 ASN A 360     -29.643  33.311  -7.783  1.00133.84           N  
ANISOU 2183  ND2 ASN A 360    14182  22402  14269    862   1460    595       N  
ATOM   2184  N   GLY A 361     -32.013  34.781 -12.924  1.00119.33           N  
ANISOU 2184  N   GLY A 361    13055  20367  11919    415   1946    510       N  
ATOM   2185  CA  GLY A 361     -32.711  34.382 -14.143  1.00118.81           C  
ANISOU 2185  CA  GLY A 361    13215  20227  11700    506   2058    412       C  
ATOM   2186  C   GLY A 361     -33.219  32.957 -14.144  1.00121.82           C  
ANISOU 2186  C   GLY A 361    13780  20415  12089    841   2066    221       C  
ATOM   2187  O   GLY A 361     -33.082  32.248 -15.144  1.00123.33           O  
ANISOU 2187  O   GLY A 361    14005  20707  12148   1035   2224    108       O  
ATOM   2188  N   VAL A 362     -33.794  32.530 -13.014  1.00116.04           N  
ANISOU 2188  N   VAL A 362    13176  19406  11510    904   1901    183       N  
ATOM   2189  CA  VAL A 362     -34.354  31.190 -12.820  1.00115.31           C  
ANISOU 2189  CA  VAL A 362    13284  19071  11457   1189   1885     19       C  
ATOM   2190  C   VAL A 362     -35.759  31.160 -13.471  1.00117.37           C  
ANISOU 2190  C   VAL A 362    13882  19069  11644   1106   1848    -75       C  
ATOM   2191  O   VAL A 362     -36.356  32.223 -13.658  1.00115.89           O  
ANISOU 2191  O   VAL A 362    13767  18844  11423    839   1784     13       O  
ATOM   2192  CB  VAL A 362     -34.341  30.795 -11.312  1.00118.04           C  
ANISOU 2192  CB  VAL A 362    13611  19256  11984   1271   1728     48       C  
ATOM   2193  CG1 VAL A 362     -34.642  29.319 -11.115  1.00118.21           C  
ANISOU 2193  CG1 VAL A 362    13803  19059  12051   1591   1740    -98       C  
ATOM   2194  CG2 VAL A 362     -32.995  31.120 -10.676  1.00119.67           C  
ANISOU 2194  CG2 VAL A 362    13455  19767  12246   1283   1731    166       C  
ATOM   2195  N   ASP A 363     -36.251  29.972 -13.881  1.00113.84           N  
ANISOU 2195  N   ASP A 363    13637  18455  11164   1330   1893   -253       N  
ATOM   2196  CA  ASP A 363     -37.564  29.874 -14.519  1.00112.17           C  
ANISOU 2196  CA  ASP A 363    13722  18025  10874   1245   1851   -355       C  
ATOM   2197  C   ASP A 363     -38.674  30.055 -13.510  1.00112.81           C  
ANISOU 2197  C   ASP A 363    13971  17799  11090   1112   1659   -328       C  
ATOM   2198  O   ASP A 363     -38.623  29.465 -12.428  1.00112.02           O  
ANISOU 2198  O   ASP A 363    13875  17552  11137   1219   1586   -330       O  
ATOM   2199  CB  ASP A 363     -37.752  28.548 -15.280  1.00115.79           C  
ANISOU 2199  CB  ASP A 363    14348  18399  11246   1497   1956   -572       C  
ATOM   2200  CG  ASP A 363     -38.750  28.620 -16.428  1.00126.82           C  
ANISOU 2200  CG  ASP A 363    15987  19715  12486   1397   1957   -686       C  
ATOM   2201  OD1 ASP A 363     -39.877  29.126 -16.215  1.00126.73           O  
ANISOU 2201  OD1 ASP A 363    15975  19786  12390   1158   1915   -577       O  
ATOM   2202  OD2 ASP A 363     -38.417  28.152 -17.533  1.00133.97           O  
ANISOU 2202  OD2 ASP A 363    17090  20459  13354   1553   1986   -881       O  
ATOM   2203  N   LYS A 364     -39.696  30.852 -13.884  1.00107.54           N  
ANISOU 2203  N   LYS A 364    13443  17050  10367    889   1582   -296       N  
ATOM   2204  CA  LYS A 364     -40.872  31.104 -13.051  1.00104.78           C  
ANISOU 2204  CA  LYS A 364    13251  16435  10127    755   1411   -276       C  
ATOM   2205  C   LYS A 364     -41.586  29.789 -12.784  1.00108.35           C  
ANISOU 2205  C   LYS A 364    13899  16630  10638    909   1379   -435       C  
ATOM   2206  O   LYS A 364     -41.998  29.555 -11.651  1.00107.32           O  
ANISOU 2206  O   LYS A 364    13816  16312  10649    903   1274   -410       O  
ATOM   2207  CB  LYS A 364     -41.831  32.107 -13.707  1.00106.40           C  
ANISOU 2207  CB  LYS A 364    13567  16623  10237    538   1354   -228       C  
ATOM   2208  CG  LYS A 364     -41.351  33.551 -13.669  1.00126.12           C  
ANISOU 2208  CG  LYS A 364    15922  19272  12725    335   1340    -40       C  
ATOM   2209  CD  LYS A 364     -42.386  34.490 -14.266  1.00138.75           C  
ANISOU 2209  CD  LYS A 364    17665  20808  14246    153   1266     16       C  
ATOM   2210  CE  LYS A 364     -42.941  35.458 -13.250  1.00150.15           C  
ANISOU 2210  CE  LYS A 364    19132  22097  15820    -10   1120    125       C  
ATOM   2211  NZ  LYS A 364     -42.076  36.659 -13.106  1.00159.74           N  
ANISOU 2211  NZ  LYS A 364    20200  23447  17049   -174   1137    295       N  
ATOM   2212  N   ARG A 365     -41.658  28.902 -13.806  1.00105.48           N  
ANISOU 2212  N   ARG A 365    13650  16265  10163   1047   1479   -599       N  
ATOM   2213  CA  ARG A 365     -42.278  27.577 -13.723  1.00105.43           C  
ANISOU 2213  CA  ARG A 365    13854  16002  10204   1183   1465   -771       C  
ATOM   2214  C   ARG A 365     -41.732  26.744 -12.582  1.00108.80           C  
ANISOU 2214  C   ARG A 365    14246  16300  10793   1367   1456   -755       C  
ATOM   2215  O   ARG A 365     -42.503  26.024 -11.949  1.00108.03           O  
ANISOU 2215  O   ARG A 365    14321  15929  10797   1381   1379   -810       O  
ATOM   2216  CB  ARG A 365     -42.102  26.805 -15.030  1.00109.26           C  
ANISOU 2216  CB  ARG A 365    14439  16546  10528   1325   1596   -958       C  
ATOM   2217  CG  ARG A 365     -43.101  27.182 -16.116  1.00122.09           C  
ANISOU 2217  CG  ARG A 365    16207  18194  11989   1161   1565  -1033       C  
ATOM   2218  CD  ARG A 365     -42.901  26.371 -17.380  1.00134.97           C  
ANISOU 2218  CD  ARG A 365    17943  19900  13439   1308   1696  -1238       C  
ATOM   2219  NE  ARG A 365     -41.580  26.609 -17.966  1.00148.61           N  
ANISOU 2219  NE  ARG A 365    19477  21931  15058   1442   1867  -1198       N  
ATOM   2220  CZ  ARG A 365     -41.349  26.756 -19.264  1.00169.46           C  
ANISOU 2220  CZ  ARG A 365    22117  24802  17467   1458   1985  -1267       C  
ATOM   2221  NH1 ARG A 365     -42.348  26.689 -20.136  1.00159.94           N  
ANISOU 2221  NH1 ARG A 365    21106  23557  16107   1356   1938  -1388       N  
ATOM   2222  NH2 ARG A 365     -40.116  26.963 -19.706  1.00159.63           N  
ANISOU 2222  NH2 ARG A 365    20670  23848  16133   1577   2152  -1218       N  
ATOM   2223  N   ILE A 366     -40.414  26.858 -12.297  1.00105.68           N  
ANISOU 2223  N   ILE A 366    13620  16113  10420   1501   1530   -668       N  
ATOM   2224  CA  ILE A 366     -39.799  26.079 -11.225  1.00105.67           C  
ANISOU 2224  CA  ILE A 366    13565  16024  10559   1704   1515   -635       C  
ATOM   2225  C   ILE A 366     -39.672  26.875  -9.893  1.00106.62           C  
ANISOU 2225  C   ILE A 366    13544  16170  10797   1571   1383   -449       C  
ATOM   2226  O   ILE A 366     -39.660  26.223  -8.850  1.00106.09           O  
ANISOU 2226  O   ILE A 366    13518  15946  10846   1685   1320   -419       O  
ATOM   2227  CB  ILE A 366     -38.467  25.385 -11.634  1.00111.79           C  
ANISOU 2227  CB  ILE A 366    14192  16983  11300   2004   1669   -684       C  
ATOM   2228  CG1 ILE A 366     -37.288  26.362 -11.719  1.00113.18           C  
ANISOU 2228  CG1 ILE A 366    14032  17540  11431   1963   1726   -544       C  
ATOM   2229  CG2 ILE A 366     -38.613  24.568 -12.915  1.00114.25           C  
ANISOU 2229  CG2 ILE A 366    14668  17256  11484   2146   1803   -893       C  
ATOM   2230  CD1 ILE A 366     -36.510  26.410 -10.445  1.00121.33           C  
ANISOU 2230  CD1 ILE A 366    14866  18638  12595   2039   1651   -404       C  
ATOM   2231  N   THR A 367     -39.555  28.238  -9.905  1.00101.46           N  
ANISOU 2231  N   THR A 367    12741  15702  10107   1340   1343   -327       N  
ATOM   2232  CA  THR A 367     -39.489  29.024  -8.645  1.00 99.64           C  
ANISOU 2232  CA  THR A 367    12402  15480   9976   1200   1211   -179       C  
ATOM   2233  C   THR A 367     -40.832  28.930  -7.912  1.00101.04           C  
ANISOU 2233  C   THR A 367    12801  15364  10226   1091   1084   -193       C  
ATOM   2234  O   THR A 367     -40.871  28.840  -6.684  1.00 99.40           O  
ANISOU 2234  O   THR A 367    12584  15069  10114   1099    989   -124       O  
ATOM   2235  CB  THR A 367     -39.067  30.499  -8.839  1.00105.45           C  
ANISOU 2235  CB  THR A 367    12958  16443  10665    967   1199    -57       C  
ATOM   2236  OG1 THR A 367     -40.003  31.194  -9.663  1.00103.09           O  
ANISOU 2236  OG1 THR A 367    12798  16089  10283    780   1193    -78       O  
ATOM   2237  CG2 THR A 367     -37.650  30.657  -9.355  1.00105.90           C  
ANISOU 2237  CG2 THR A 367    12747  16825  10665   1045   1320    -13       C  
ATOM   2238  N   ARG A 368     -41.927  28.892  -8.692  1.00 97.04           N  
ANISOU 2238  N   ARG A 368    12484  14726   9660    998   1086   -287       N  
ATOM   2239  CA  ARG A 368     -43.301  28.730  -8.221  1.00 95.13           C  
ANISOU 2239  CA  ARG A 368    12443  14231   9470    892    986   -322       C  
ATOM   2240  C   ARG A 368     -43.509  27.324  -7.647  1.00100.62           C  
ANISOU 2240  C   ARG A 368    13282  14700  10250   1064    988   -392       C  
ATOM   2241  O   ARG A 368     -44.380  27.138  -6.799  1.00 99.24           O  
ANISOU 2241  O   ARG A 368    13222  14335  10150    991    902   -373       O  
ATOM   2242  CB  ARG A 368     -44.281  28.982  -9.375  1.00 93.68           C  
ANISOU 2242  CB  ARG A 368    12391  14019   9183    770    995   -412       C  
ATOM   2243  CG  ARG A 368     -44.386  30.454  -9.755  1.00 96.60           C  
ANISOU 2243  CG  ARG A 368    12674  14543   9488    575    962   -313       C  
ATOM   2244  CD  ARG A 368     -45.202  30.649 -11.008  1.00 96.18           C  
ANISOU 2244  CD  ARG A 368    12735  14503   9305    495    976   -389       C  
ATOM   2245  NE  ARG A 368     -45.260  32.060 -11.384  1.00 94.28           N  
ANISOU 2245  NE  ARG A 368    12428  14392   9002    326    946   -271       N  
ATOM   2246  CZ  ARG A 368     -46.028  32.541 -12.347  1.00102.17           C  
ANISOU 2246  CZ  ARG A 368    13513  15419   9887    232    928   -286       C  
ATOM   2247  NH1 ARG A 368     -46.822  31.736 -13.047  1.00 87.17           N  
ANISOU 2247  NH1 ARG A 368    11756  13448   7917    273    928   -430       N  
ATOM   2248  NH2 ARG A 368     -46.021  33.841 -12.626  1.00 85.70           N  
ANISOU 2248  NH2 ARG A 368    11379  13427   7754     92    901   -156       N  
ATOM   2249  N   PHE A 369     -42.697  26.348  -8.103  1.00 99.73           N  
ANISOU 2249  N   PHE A 369    13164  14607  10123   1296   1094   -467       N  
ATOM   2250  CA  PHE A 369     -42.727  24.949  -7.678  1.00100.97           C  
ANISOU 2250  CA  PHE A 369    13473  14532  10358   1494   1114   -532       C  
ATOM   2251  C   PHE A 369     -41.854  24.694  -6.436  1.00105.04           C  
ANISOU 2251  C   PHE A 369    13868  15073  10970   1648   1078   -399       C  
ATOM   2252  O   PHE A 369     -42.308  24.027  -5.506  1.00104.74           O  
ANISOU 2252  O   PHE A 369    13964  14813  11020   1684   1018   -365       O  
ATOM   2253  CB  PHE A 369     -42.269  24.044  -8.837  1.00105.54           C  
ANISOU 2253  CB  PHE A 369    14121  15112  10866   1695   1251   -693       C  
ATOM   2254  CG  PHE A 369     -42.529  22.569  -8.662  1.00109.12           C  
ANISOU 2254  CG  PHE A 369    14805  15262  11394   1877   1279   -800       C  
ATOM   2255  CD1 PHE A 369     -41.702  21.790  -7.857  1.00114.23           C  
ANISOU 2255  CD1 PHE A 369    15422  15845  12135   2130   1296   -734       C  
ATOM   2256  CD2 PHE A 369     -43.535  21.937  -9.377  1.00111.85           C  
ANISOU 2256  CD2 PHE A 369    15398  15392  11707   1805   1290   -972       C  
ATOM   2257  CE1 PHE A 369     -41.930  20.421  -7.714  1.00117.05           C  
ANISOU 2257  CE1 PHE A 369    16021  15886  12566   2304   1326   -822       C  
ATOM   2258  CE2 PHE A 369     -43.755  20.567  -9.238  1.00116.58           C  
ANISOU 2258  CE2 PHE A 369    16232  15680  12381   1954   1319  -1077       C  
ATOM   2259  CZ  PHE A 369     -42.980  19.829  -8.375  1.00116.14           C  
ANISOU 2259  CZ  PHE A 369    16171  15525  12434   2198   1336   -992       C  
ATOM   2260  N   VAL A 370     -40.599  25.189  -6.443  1.00101.92           N  
ANISOU 2260  N   VAL A 370    13216  14960  10549   1737   1115   -321       N  
ATOM   2261  CA  VAL A 370     -39.602  24.980  -5.386  1.00102.38           C  
ANISOU 2261  CA  VAL A 370    13113  15113  10676   1904   1078   -197       C  
ATOM   2262  C   VAL A 370     -39.792  25.908  -4.169  1.00104.09           C  
ANISOU 2262  C   VAL A 370    13240  15379  10931   1712    934    -53       C  
ATOM   2263  O   VAL A 370     -40.078  25.406  -3.083  1.00103.63           O  
ANISOU 2263  O   VAL A 370    13274  15161  10940   1763    856     11       O  
ATOM   2264  CB  VAL A 370     -38.148  25.051  -5.946  1.00108.26           C  
ANISOU 2264  CB  VAL A 370    13592  16171  11372   2088   1182   -186       C  
ATOM   2265  CG1 VAL A 370     -37.104  24.868  -4.841  1.00109.22           C  
ANISOU 2265  CG1 VAL A 370    13512  16428  11558   2262   1124    -52       C  
ATOM   2266  CG2 VAL A 370     -37.936  24.028  -7.061  1.00110.27           C  
ANISOU 2266  CG2 VAL A 370    13950  16366  11580   2320   1333   -345       C  
ATOM   2267  N   LEU A 371     -39.606  27.237  -4.350  1.00 99.31           N  
ANISOU 2267  N   LEU A 371    12468  14989  10277   1498    906     -1       N  
ATOM   2268  CA  LEU A 371     -39.624  28.272  -3.304  1.00 97.65           C  
ANISOU 2268  CA  LEU A 371    12154  14859  10089   1308    778    115       C  
ATOM   2269  C   LEU A 371     -40.792  28.235  -2.276  1.00100.43           C  
ANISOU 2269  C   LEU A 371    12699  14972  10489   1199    668    138       C  
ATOM   2270  O   LEU A 371     -40.452  28.329  -1.093  1.00100.28           O  
ANISOU 2270  O   LEU A 371    12608  14995  10498   1216    577    233       O  
ATOM   2271  CB  LEU A 371     -39.524  29.688  -3.886  1.00 96.69           C  
ANISOU 2271  CB  LEU A 371    11909  14919   9911   1064    778    139       C  
ATOM   2272  CG  LEU A 371     -38.238  30.062  -4.618  1.00102.85           C  
ANISOU 2272  CG  LEU A 371    12433  16006  10639   1099    868    166       C  
ATOM   2273  CD1 LEU A 371     -38.309  31.486  -5.122  1.00102.38           C  
ANISOU 2273  CD1 LEU A 371    12303  16067  10529    820    860    209       C  
ATOM   2274  CD2 LEU A 371     -37.019  29.890  -3.732  1.00105.75           C  
ANISOU 2274  CD2 LEU A 371    12563  16572  11046   1227    826    255       C  
ATOM   2275  N   PRO A 372     -42.119  28.144  -2.616  1.00 95.44           N  
ANISOU 2275  N   PRO A 372    12285  14122   9855   1083    669     62       N  
ATOM   2276  CA  PRO A 372     -43.141  28.132  -1.547  1.00 93.64           C  
ANISOU 2276  CA  PRO A 372    12198  13713   9669    984    576     98       C  
ATOM   2277  C   PRO A 372     -43.094  26.878  -0.669  1.00 99.17           C  
ANISOU 2277  C   PRO A 372    13001  14254  10424   1167    564    138       C  
ATOM   2278  O   PRO A 372     -43.464  26.938   0.506  1.00 98.50           O  
ANISOU 2278  O   PRO A 372    12956  14111  10357   1118    482    218       O  
ATOM   2279  CB  PRO A 372     -44.472  28.254  -2.304  1.00 93.94           C  
ANISOU 2279  CB  PRO A 372    12405  13601   9689    837    594      2       C  
ATOM   2280  CG  PRO A 372     -44.121  28.578  -3.710  1.00 99.10           C  
ANISOU 2280  CG  PRO A 372    12999  14379  10275    829    675    -68       C  
ATOM   2281  CD  PRO A 372     -42.759  28.014  -3.941  1.00 96.75           C  
ANISOU 2281  CD  PRO A 372    12567  14220   9973   1039    749    -57       C  
ATOM   2282  N   VAL A 373     -42.623  25.748  -1.238  1.00 97.44           N  
ANISOU 2282  N   VAL A 373    12836  13962  10224   1384    651     86       N  
ATOM   2283  CA  VAL A 373     -42.474  24.464  -0.544  1.00 98.46           C  
ANISOU 2283  CA  VAL A 373    13086  13911  10411   1595    655    130       C  
ATOM   2284  C   VAL A 373     -41.189  24.498   0.298  1.00104.32           C  
ANISOU 2284  C   VAL A 373    13627  14855  11156   1768    607    259       C  
ATOM   2285  O   VAL A 373     -41.228  24.159   1.479  1.00104.74           O  
ANISOU 2285  O   VAL A 373    13724  14842  11231   1821    531    369       O  
ATOM   2286  CB  VAL A 373     -42.556  23.254  -1.521  1.00103.51           C  
ANISOU 2286  CB  VAL A 373    13897  14357  11075   1761    767      4       C  
ATOM   2287  CG1 VAL A 373     -42.266  21.935  -0.817  1.00105.17           C  
ANISOU 2287  CG1 VAL A 373    14242  14362  11355   2004    774     63       C  
ATOM   2288  CG2 VAL A 373     -43.917  23.193  -2.205  1.00102.11           C  
ANISOU 2288  CG2 VAL A 373    13918  13989  10889   1561    786   -121       C  
ATOM   2289  N   GLY A 374     -40.091  24.959  -0.297  1.00101.99           N  
ANISOU 2289  N   GLY A 374    13098  14827  10827   1836    645    250       N  
ATOM   2290  CA  GLY A 374     -38.802  25.077   0.374  1.00103.82           C  
ANISOU 2290  CA  GLY A 374    13084  15309  11054   1986    596    362       C  
ATOM   2291  C   GLY A 374     -38.831  25.962   1.607  1.00107.84           C  
ANISOU 2291  C   GLY A 374    13499  15933  11542   1818    452    473       C  
ATOM   2292  O   GLY A 374     -38.145  25.680   2.592  1.00108.30           O  
ANISOU 2292  O   GLY A 374    13458  16092  11600   1958    373    584       O  
ATOM   2293  N   ALA A 375     -39.647  27.030   1.561  1.00103.85           N  
ANISOU 2293  N   ALA A 375    13034  15413  11011   1528    414    439       N  
ATOM   2294  CA  ALA A 375     -39.813  28.015   2.634  1.00103.42           C  
ANISOU 2294  CA  ALA A 375    12922  15448  10927   1337    286    507       C  
ATOM   2295  C   ALA A 375     -40.357  27.441   3.936  1.00108.24           C  
ANISOU 2295  C   ALA A 375    13679  15908  11537   1385    206    586       C  
ATOM   2296  O   ALA A 375     -40.136  28.035   4.986  1.00108.09           O  
ANISOU 2296  O   ALA A 375    13576  16018  11475   1307     94    656       O  
ATOM   2297  CB  ALA A 375     -40.707  29.152   2.164  1.00102.20           C  
ANISOU 2297  CB  ALA A 375    12823  15254  10753   1057    284    437       C  
ATOM   2298  N   THR A 376     -41.084  26.311   3.871  1.00105.51           N  
ANISOU 2298  N   THR A 376    13563  15295  11233   1493    265    574       N  
ATOM   2299  CA  THR A 376     -41.696  25.672   5.044  1.00105.59           C  
ANISOU 2299  CA  THR A 376    13741  15139  11239   1525    211    664       C  
ATOM   2300  C   THR A 376     -41.049  24.316   5.440  1.00111.39           C  
ANISOU 2300  C   THR A 376    14527  15792  12004   1830    222    762       C  
ATOM   2301  O   THR A 376     -40.958  24.033   6.638  1.00111.35           O  
ANISOU 2301  O   THR A 376    14553  15792  11964   1893    140    891       O  
ATOM   2302  CB  THR A 376     -43.232  25.549   4.879  1.00113.75           C  
ANISOU 2302  CB  THR A 376    15010  15915  12294   1352    255    597       C  
ATOM   2303  OG1 THR A 376     -43.762  24.730   5.926  1.00116.75           O  
ANISOU 2303  OG1 THR A 376    15549  16143  12668   1387    223    700       O  
ATOM   2304  CG2 THR A 376     -43.671  25.010   3.506  1.00112.44           C  
ANISOU 2304  CG2 THR A 376    14971  15567  12184   1384    371    474       C  
ATOM   2305  N   ILE A 377     -40.624  23.482   4.461  1.00108.73           N  
ANISOU 2305  N   ILE A 377    14217  15373  11723   2027    324    701       N  
ATOM   2306  CA  ILE A 377     -40.068  22.158   4.770  1.00110.63           C  
ANISOU 2306  CA  ILE A 377    14545  15483  12006   2341    345    783       C  
ATOM   2307  C   ILE A 377     -38.530  22.097   4.658  1.00118.16           C  
ANISOU 2307  C   ILE A 377    15232  16711  12951   2603    334    831       C  
ATOM   2308  O   ILE A 377     -37.916  21.394   5.465  1.00120.42           O  
ANISOU 2308  O   ILE A 377    15507  17008  13239   2844    279    967       O  
ATOM   2309  CB  ILE A 377     -40.764  21.016   3.972  1.00113.76           C  
ANISOU 2309  CB  ILE A 377    15220  15526  12477   2415    464    687       C  
ATOM   2310  CG1 ILE A 377     -40.507  21.103   2.459  1.00114.10           C  
ANISOU 2310  CG1 ILE A 377    15204  15616  12534   2447    577    512       C  
ATOM   2311  CG2 ILE A 377     -42.269  20.952   4.290  1.00112.65           C  
ANISOU 2311  CG2 ILE A 377    15325  15129  12348   2161    462    669       C  
ATOM   2312  CD1 ILE A 377     -40.421  19.790   1.787  1.00122.26           C  
ANISOU 2312  CD1 ILE A 377    16438  16383  13631   2682    681    438       C  
ATOM   2313  N   ASN A 378     -37.913  22.820   3.687  1.00115.19           N  
ANISOU 2313  N   ASN A 378    14636  16571  12560   2558    385    734       N  
ATOM   2314  CA  ASN A 378     -36.454  22.835   3.494  1.00117.76           C  
ANISOU 2314  CA  ASN A 378    14665  17205  12875   2780    389    770       C  
ATOM   2315  C   ASN A 378     -35.776  23.808   4.458  1.00122.18           C  
ANISOU 2315  C   ASN A 378    14955  18095  13372   2670    243    878       C  
ATOM   2316  O   ASN A 378     -35.514  24.967   4.112  1.00120.81           O  
ANISOU 2316  O   ASN A 378    14584  18154  13163   2447    228    831       O  
ATOM   2317  CB  ASN A 378     -36.074  23.132   2.038  1.00119.86           C  
ANISOU 2317  CB  ASN A 378    14811  17591  13139   2772    523    627       C  
ATOM   2318  CG  ASN A 378     -34.596  22.996   1.719  1.00147.54           C  
ANISOU 2318  CG  ASN A 378    18008  21412  16638   3027    563    654       C  
ATOM   2319  OD1 ASN A 378     -33.972  21.955   1.944  1.00143.61           O  
ANISOU 2319  OD1 ASN A 378    17511  20880  16175   3375    581    707       O  
ATOM   2320  ND2 ASN A 378     -34.020  24.027   1.119  1.00139.43           N  
ANISOU 2320  ND2 ASN A 378    16715  20695  15566   2868    589    617       N  
ATOM   2321  N   MET A 379     -35.507  23.323   5.680  1.00120.20           N  
ANISOU 2321  N   MET A 379    14715  17854  13102   2821    131   1025       N  
ATOM   2322  CA  MET A 379     -34.879  24.101   6.738  1.00120.62           C  
ANISOU 2322  CA  MET A 379    14538  18213  13078   2736    -30   1128       C  
ATOM   2323  C   MET A 379     -33.541  23.472   7.130  1.00128.35           C  
ANISOU 2323  C   MET A 379    15286  19431  14051   3080    -84   1246       C  
ATOM   2324  O   MET A 379     -33.448  22.760   8.134  1.00129.92           O  
ANISOU 2324  O   MET A 379    15566  19574  14225   3273   -173   1387       O  
ATOM   2325  CB  MET A 379     -35.831  24.248   7.939  1.00121.76           C  
ANISOU 2325  CB  MET A 379    14889  18208  13167   2574   -137   1201       C  
ATOM   2326  CG  MET A 379     -37.204  24.764   7.570  1.00122.67           C  
ANISOU 2326  CG  MET A 379    15226  18086  13295   2276    -78   1090       C  
ATOM   2327  SD  MET A 379     -37.697  26.217   8.511  1.00125.13           S  
ANISOU 2327  SD  MET A 379    15492  18540  13510   1922   -211   1082       S  
ATOM   2328  CE  MET A 379     -39.066  26.660   7.616  1.00118.88           C  
ANISOU 2328  CE  MET A 379    14904  17498  12765   1675   -101    938       C  
ATOM   2329  N   ASP A 380     -32.505  23.722   6.305  1.00126.31           N  
ANISOU 2329  N   ASP A 380    14733  19450  13810   3167    -24   1196       N  
ATOM   2330  CA  ASP A 380     -31.142  23.207   6.498  1.00129.46           C  
ANISOU 2330  CA  ASP A 380    14845  20138  14206   3504    -59   1291       C  
ATOM   2331  C   ASP A 380     -30.466  23.758   7.771  1.00133.08           C  
ANISOU 2331  C   ASP A 380    15062  20925  14577   3453   -269   1424       C  
ATOM   2332  O   ASP A 380     -29.903  22.983   8.545  1.00134.94           O  
ANISOU 2332  O   ASP A 380    15250  21228  14792   3757   -357   1566       O  
ATOM   2333  CB  ASP A 380     -30.272  23.480   5.251  1.00132.58           C  
ANISOU 2333  CB  ASP A 380    14958  20789  14629   3557     74   1192       C  
ATOM   2334  CG  ASP A 380     -30.733  22.790   3.979  1.00142.81           C  
ANISOU 2334  CG  ASP A 380    16467  21809  15987   3679    279   1057       C  
ATOM   2335  OD1 ASP A 380     -30.903  21.553   4.002  1.00144.79           O  
ANISOU 2335  OD1 ASP A 380    16939  21787  16288   3993    331   1076       O  
ATOM   2336  OD2 ASP A 380     -30.872  23.481   2.947  1.00147.87           O  
ANISOU 2336  OD2 ASP A 380    17051  22513  16620   3468    385    934       O  
ATOM   2337  N   GLY A 381     -30.544  25.079   7.961  1.00127.06           N  
ANISOU 2337  N   GLY A 381    14165  20352  13761   3074   -349   1375       N  
ATOM   2338  CA  GLY A 381     -29.968  25.797   9.095  1.00127.39           C  
ANISOU 2338  CA  GLY A 381    13983  20713  13707   2946   -554   1458       C  
ATOM   2339  C   GLY A 381     -30.630  25.509  10.427  1.00129.78           C  
ANISOU 2339  C   GLY A 381    14520  20858  13931   2950   -691   1561       C  
ATOM   2340  O   GLY A 381     -29.957  25.513  11.462  1.00131.33           O  
ANISOU 2340  O   GLY A 381    14548  21313  14037   3037   -863   1677       O  
ATOM   2341  N   THR A 382     -31.958  25.278  10.412  1.00123.11           N  
ANISOU 2341  N   THR A 382    14054  19615  13107   2845   -618   1521       N  
ATOM   2342  CA  THR A 382     -32.743  24.937  11.600  1.00122.13           C  
ANISOU 2342  CA  THR A 382    14191  19309  12906   2838   -710   1620       C  
ATOM   2343  C   THR A 382     -32.329  23.539  12.063  1.00128.63           C  
ANISOU 2343  C   THR A 382    15084  20055  13733   3257   -727   1790       C  
ATOM   2344  O   THR A 382     -32.065  23.365  13.246  1.00129.89           O  
ANISOU 2344  O   THR A 382    15222  20345  13785   3346   -881   1934       O  
ATOM   2345  CB  THR A 382     -34.249  25.114  11.323  1.00125.72           C  
ANISOU 2345  CB  THR A 382    14987  19391  13392   2599   -607   1523       C  
ATOM   2346  OG1 THR A 382     -34.511  26.507  11.169  1.00123.09           O  
ANISOU 2346  OG1 THR A 382    14567  19173  13029   2236   -636   1398       O  
ATOM   2347  CG2 THR A 382     -35.143  24.552  12.433  1.00123.39           C  
ANISOU 2347  CG2 THR A 382    14981  18875  13026   2619   -657   1634       C  
ATOM   2348  N   ALA A 383     -32.204  22.577  11.121  1.00126.07           N  
ANISOU 2348  N   ALA A 383    14836  19538  13527   3523   -575   1770       N  
ATOM   2349  CA  ALA A 383     -31.784  21.193  11.375  1.00129.05           C  
ANISOU 2349  CA  ALA A 383    15306  19789  13937   3957   -565   1917       C  
ATOM   2350  C   ALA A 383     -30.413  21.105  12.059  1.00136.68           C  
ANISOU 2350  C   ALA A 383    15931  21167  14834   4219   -721   2061       C  
ATOM   2351  O   ALA A 383     -30.252  20.321  12.997  1.00138.46           O  
ANISOU 2351  O   ALA A 383    16251  21354  15005   4471   -819   2247       O  
ATOM   2352  CB  ALA A 383     -31.763  20.409  10.073  1.00130.28           C  
ANISOU 2352  CB  ALA A 383    15556  19716  14230   4163   -368   1815       C  
ATOM   2353  N   LEU A 384     -29.438  21.916  11.592  1.00134.14           N  
ANISOU 2353  N   LEU A 384    15209  21250  14508   4148   -746   1985       N  
ATOM   2354  CA  LEU A 384     -28.078  21.997  12.136  1.00137.38           C  
ANISOU 2354  CA  LEU A 384    15219  22126  14853   4348   -899   2097       C  
ATOM   2355  C   LEU A 384     -28.138  22.539  13.567  1.00141.06           C  
ANISOU 2355  C   LEU A 384    15657  22780  15160   4179  -1128   2204       C  
ATOM   2356  O   LEU A 384     -27.456  22.019  14.445  1.00143.55           O  
ANISOU 2356  O   LEU A 384    15857  23291  15395   4451  -1277   2378       O  
ATOM   2357  CB  LEU A 384     -27.215  22.913  11.247  1.00137.77           C  
ANISOU 2357  CB  LEU A 384    14863  22548  14934   4197   -854   1967       C  
ATOM   2358  CG  LEU A 384     -25.700  22.736  11.334  1.00146.77           C  
ANISOU 2358  CG  LEU A 384    15546  24162  16057   4486   -936   2055       C  
ATOM   2359  CD1 LEU A 384     -25.075  22.717   9.947  1.00147.76           C  
ANISOU 2359  CD1 LEU A 384    15445  24413  16285   4588   -743   1939       C  
ATOM   2360  CD2 LEU A 384     -25.065  23.834  12.172  1.00150.33           C  
ANISOU 2360  CD2 LEU A 384    15662  25068  16389   4212  -1154   2081       C  
ATOM   2361  N   TYR A 385     -28.988  23.554  13.794  1.00134.73           N  
ANISOU 2361  N   TYR A 385    14978  21910  14305   3746  -1154   2098       N  
ATOM   2362  CA  TYR A 385     -29.216  24.197  15.085  1.00134.55           C  
ANISOU 2362  CA  TYR A 385    14973  22032  14118   3529  -1349   2151       C  
ATOM   2363  C   TYR A 385     -29.945  23.275  16.068  1.00139.28           C  
ANISOU 2363  C   TYR A 385    15920  22360  14640   3698  -1389   2316       C  
ATOM   2364  O   TYR A 385     -29.656  23.326  17.263  1.00140.68           O  
ANISOU 2364  O   TYR A 385    16043  22750  14657   3733  -1577   2443       O  
ATOM   2365  CB  TYR A 385     -29.941  25.542  14.877  1.00132.46           C  
ANISOU 2365  CB  TYR A 385    14757  21732  13839   3043  -1331   1965       C  
ATOM   2366  CG  TYR A 385     -30.873  25.960  15.992  1.00133.00           C  
ANISOU 2366  CG  TYR A 385    15072  21693  13771   2820  -1430   1976       C  
ATOM   2367  CD1 TYR A 385     -30.394  26.628  17.115  1.00136.81           C  
ANISOU 2367  CD1 TYR A 385    15391  22508  14083   2695  -1648   2009       C  
ATOM   2368  CD2 TYR A 385     -32.240  25.701  15.917  1.00131.17           C  
ANISOU 2368  CD2 TYR A 385    15225  21045  13569   2727  -1305   1945       C  
ATOM   2369  CE1 TYR A 385     -31.248  27.017  18.146  1.00137.27           C  
ANISOU 2369  CE1 TYR A 385    15680  22481  13996   2504  -1728   2007       C  
ATOM   2370  CE2 TYR A 385     -33.103  26.079  16.944  1.00131.18           C  
ANISOU 2370  CE2 TYR A 385    15437  20970  13435   2536  -1379   1955       C  
ATOM   2371  CZ  TYR A 385     -32.605  26.743  18.053  1.00142.20           C  
ANISOU 2371  CZ  TYR A 385    16680  22696  14654   2431  -1585   1982       C  
ATOM   2372  OH  TYR A 385     -33.450  27.128  19.064  1.00144.51           O  
ANISOU 2372  OH  TYR A 385    17185  22927  14796   2255  -1646   1979       O  
ATOM   2373  N   GLU A 386     -30.887  22.449  15.565  1.00134.83           N  
ANISOU 2373  N   GLU A 386    15712  21337  14181   3785  -1213   2315       N  
ATOM   2374  CA  GLU A 386     -31.670  21.490  16.353  1.00135.24           C  
ANISOU 2374  CA  GLU A 386    16127  21072  14184   3923  -1211   2476       C  
ATOM   2375  C   GLU A 386     -30.762  20.416  16.935  1.00143.17           C  
ANISOU 2375  C   GLU A 386    17065  22179  15152   4375  -1307   2705       C  
ATOM   2376  O   GLU A 386     -30.896  20.095  18.112  1.00144.65           O  
ANISOU 2376  O   GLU A 386    17374  22390  15196   4448  -1434   2885       O  
ATOM   2377  CB  GLU A 386     -32.782  20.837  15.510  1.00134.59           C  
ANISOU 2377  CB  GLU A 386    16404  20488  14247   3900   -995   2404       C  
ATOM   2378  CG  GLU A 386     -33.945  21.753  15.168  1.00141.37           C  
ANISOU 2378  CG  GLU A 386    17404  21193  15116   3474   -913   2223       C  
ATOM   2379  CD  GLU A 386     -35.014  21.975  16.218  1.00162.01           C  
ANISOU 2379  CD  GLU A 386    20263  23688  17605   3255   -961   2278       C  
ATOM   2380  OE1 GLU A 386     -36.010  22.655  15.885  1.00154.74           O  
ANISOU 2380  OE1 GLU A 386    19463  22625  16708   2944   -880   2130       O  
ATOM   2381  OE2 GLU A 386     -34.887  21.452  17.349  1.00160.95           O  
ANISOU 2381  OE2 GLU A 386    20207  23601  17346   3406  -1070   2473       O  
ATOM   2382  N   ALA A 387     -29.831  19.880  16.119  1.00141.22           N  
ANISOU 2382  N   ALA A 387    16623  22010  15024   4689  -1246   2701       N  
ATOM   2383  CA  ALA A 387     -28.871  18.864  16.542  1.00145.11           C  
ANISOU 2383  CA  ALA A 387    17020  22614  15503   5171  -1329   2911       C  
ATOM   2384  C   ALA A 387     -27.881  19.442  17.558  1.00151.00           C  
ANISOU 2384  C   ALA A 387    17403  23896  16073   5191  -1582   3019       C  
ATOM   2385  O   ALA A 387     -27.687  18.841  18.614  1.00153.35           O  
ANISOU 2385  O   ALA A 387    17773  24242  16249   5420  -1723   3242       O  
ATOM   2386  CB  ALA A 387     -28.128  18.313  15.340  1.00147.41           C  
ANISOU 2386  CB  ALA A 387    17156  22893  15960   5477  -1187   2838       C  
ATOM   2387  N   VAL A 388     -27.289  20.623  17.252  1.00146.46           N  
ANISOU 2387  N   VAL A 388    16451  23720  15478   4930  -1642   2862       N  
ATOM   2388  CA  VAL A 388     -26.319  21.340  18.092  1.00148.45           C  
ANISOU 2388  CA  VAL A 388    16316  24517  15571   4872  -1885   2915       C  
ATOM   2389  C   VAL A 388     -26.891  21.617  19.490  1.00151.68           C  
ANISOU 2389  C   VAL A 388    16911  24953  15768   4696  -2062   3015       C  
ATOM   2390  O   VAL A 388     -26.252  21.262  20.481  1.00154.67           O  
ANISOU 2390  O   VAL A 388    17172  25598  15997   4922  -2258   3205       O  
ATOM   2391  CB  VAL A 388     -25.765  22.621  17.386  1.00151.30           C  
ANISOU 2391  CB  VAL A 388    16297  25219  15971   4536  -1883   2703       C  
ATOM   2392  CG1 VAL A 388     -25.085  23.583  18.365  1.00152.73           C  
ANISOU 2392  CG1 VAL A 388    16159  25899  15971   4319  -2144   2712       C  
ATOM   2393  CG2 VAL A 388     -24.807  22.257  16.255  1.00152.93           C  
ANISOU 2393  CG2 VAL A 388    16204  25572  16330   4804  -1760   2665       C  
ATOM   2394  N   ALA A 389     -28.099  22.198  19.558  1.00144.23           N  
ANISOU 2394  N   ALA A 389    16260  23738  14804   4320  -1986   2893       N  
ATOM   2395  CA  ALA A 389     -28.767  22.532  20.814  1.00143.56           C  
ANISOU 2395  CA  ALA A 389    16373  23662  14511   4123  -2117   2954       C  
ATOM   2396  C   ALA A 389     -29.294  21.325  21.599  1.00148.87           C  
ANISOU 2396  C   ALA A 389    17396  24059  15109   4403  -2114   3200       C  
ATOM   2397  O   ALA A 389     -29.379  21.409  22.823  1.00149.75           O  
ANISOU 2397  O   ALA A 389    17568  24328  15001   4374  -2279   3325       O  
ATOM   2398  CB  ALA A 389     -29.877  23.537  20.570  1.00140.13           C  
ANISOU 2398  CB  ALA A 389    16120  23033  14090   3662  -2019   2738       C  
ATOM   2399  N   ALA A 390     -29.643  20.214  20.917  1.00145.67           N  
ANISOU 2399  N   ALA A 390    17231  23243  14874   4661  -1931   3270       N  
ATOM   2400  CA  ALA A 390     -30.118  18.993  21.583  1.00147.63           C  
ANISOU 2400  CA  ALA A 390    17833  23183  15076   4929  -1912   3520       C  
ATOM   2401  C   ALA A 390     -28.968  18.316  22.332  1.00157.69           C  
ANISOU 2401  C   ALA A 390    18923  24751  16242   5357  -2103   3772       C  
ATOM   2402  O   ALA A 390     -29.186  17.745  23.400  1.00159.50           O  
ANISOU 2402  O   ALA A 390    19357  24936  16309   5491  -2200   4006       O  
ATOM   2403  CB  ALA A 390     -30.717  18.029  20.574  1.00147.37           C  
ANISOU 2403  CB  ALA A 390    18094  22631  15270   5073  -1672   3500       C  
ATOM   2404  N   ILE A 391     -27.744  18.402  21.777  1.00157.00           N  
ANISOU 2404  N   ILE A 391    18435  24986  16231   5569  -2159   3732       N  
ATOM   2405  CA  ILE A 391     -26.532  17.842  22.372  1.00161.88           C  
ANISOU 2405  CA  ILE A 391    18797  25951  16759   5995  -2349   3953       C  
ATOM   2406  C   ILE A 391     -25.925  18.836  23.379  1.00167.44           C  
ANISOU 2406  C   ILE A 391    19176  27223  17219   5799  -2622   3957       C  
ATOM   2407  O   ILE A 391     -25.401  18.398  24.403  1.00170.68           O  
ANISOU 2407  O   ILE A 391    19534  27867  17451   6057  -2822   4192       O  
ATOM   2408  CB  ILE A 391     -25.538  17.341  21.277  1.00167.03           C  
ANISOU 2408  CB  ILE A 391    19179  26671  17615   6357  -2259   3916       C  
ATOM   2409  CG1 ILE A 391     -26.114  16.097  20.589  1.00167.42           C  
ANISOU 2409  CG1 ILE A 391    19626  26131  17856   6641  -2032   3972       C  
ATOM   2410  CG2 ILE A 391     -24.156  16.992  21.847  1.00173.13           C  
ANISOU 2410  CG2 ILE A 391    19570  27922  18291   6771  -2478   4111       C  
ATOM   2411  CD1 ILE A 391     -25.927  16.031  19.127  1.00172.70           C  
ANISOU 2411  CD1 ILE A 391    20202  26664  18754   6693  -1820   3763       C  
ATOM   2412  N   PHE A 392     -26.037  20.160  23.116  1.00161.57           N  
ANISOU 2412  N   PHE A 392    18245  26682  16460   5339  -2636   3700       N  
ATOM   2413  CA  PHE A 392     -25.514  21.191  24.019  1.00162.78           C  
ANISOU 2413  CA  PHE A 392    18113  27346  16390   5094  -2890   3658       C  
ATOM   2414  C   PHE A 392     -26.169  21.164  25.404  1.00168.08           C  
ANISOU 2414  C   PHE A 392    19065  28004  16795   5007  -3026   3797       C  
ATOM   2415  O   PHE A 392     -25.460  21.327  26.396  1.00170.93           O  
ANISOU 2415  O   PHE A 392    19217  28795  16932   5079  -3281   3911       O  
ATOM   2416  CB  PHE A 392     -25.575  22.608  23.407  1.00161.55           C  
ANISOU 2416  CB  PHE A 392    17755  27336  16292   4605  -2856   3348       C  
ATOM   2417  CG  PHE A 392     -25.175  23.701  24.371  1.00164.39           C  
ANISOU 2417  CG  PHE A 392    17884  28156  16419   4304  -3112   3278       C  
ATOM   2418  CD1 PHE A 392     -23.847  23.864  24.750  1.00171.71           C  
ANISOU 2418  CD1 PHE A 392    18356  29634  17251   4437  -3345   3342       C  
ATOM   2419  CD2 PHE A 392     -26.135  24.524  24.950  1.00164.13           C  
ANISOU 2419  CD2 PHE A 392    18096  28014  16252   3904  -3129   3148       C  
ATOM   2420  CE1 PHE A 392     -23.486  24.837  25.682  1.00174.12           C  
ANISOU 2420  CE1 PHE A 392    18466  30363  17328   4148  -3597   3269       C  
ATOM   2421  CE2 PHE A 392     -25.772  25.500  25.878  1.00168.45           C  
ANISOU 2421  CE2 PHE A 392    18463  28969  16572   3636  -3370   3068       C  
ATOM   2422  CZ  PHE A 392     -24.449  25.651  26.235  1.00170.61           C  
ANISOU 2422  CZ  PHE A 392    18296  29776  16750   3747  -3607   3125       C  
ATOM   2423  N   ILE A 393     -27.508  20.986  25.479  1.00162.65           N  
ANISOU 2423  N   ILE A 393    18827  26856  16117   4839  -2860   3783       N  
ATOM   2424  CA  ILE A 393     -28.225  20.938  26.764  1.00163.60           C  
ANISOU 2424  CA  ILE A 393    19236  26945  15978   4748  -2951   3917       C  
ATOM   2425  C   ILE A 393     -27.848  19.652  27.541  1.00173.75           C  
ANISOU 2425  C   ILE A 393    20639  28228  17151   5220  -3051   4278       C  
ATOM   2426  O   ILE A 393     -27.840  19.667  28.776  1.00175.24           O  
ANISOU 2426  O   ILE A 393    20887  28639  17057   5233  -3233   4435       O  
ATOM   2427  CB  ILE A 393     -29.768  21.164  26.591  1.00162.45           C  
ANISOU 2427  CB  ILE A 393    19506  26340  15879   4427  -2732   3799       C  
ATOM   2428  CG1 ILE A 393     -30.121  22.659  26.316  1.00159.42           C  
ANISOU 2428  CG1 ILE A 393    19014  26051  15507   3938  -2708   3468       C  
ATOM   2429  CG2 ILE A 393     -30.603  20.579  27.706  1.00164.09           C  
ANISOU 2429  CG2 ILE A 393    20074  26407  15867   4459  -2752   4012       C  
ATOM   2430  CD1 ILE A 393     -29.478  23.815  27.248  1.00169.88           C  
ANISOU 2430  CD1 ILE A 393    20091  27879  16578   3677  -2961   3353       C  
ATOM   2431  N   ALA A 394     -27.484  18.571  26.812  1.00173.53           N  
ANISOU 2431  N   ALA A 394    20641  27958  17334   5617  -2937   4405       N  
ATOM   2432  CA  ALA A 394     -27.060  17.290  27.388  1.00177.92           C  
ANISOU 2432  CA  ALA A 394    21316  28455  17829   6115  -3013   4752       C  
ATOM   2433  C   ALA A 394     -25.675  17.376  28.051  1.00184.57           C  
ANISOU 2433  C   ALA A 394    21735  29894  18499   6382  -3308   4888       C  
ATOM   2434  O   ALA A 394     -25.369  16.546  28.908  1.00187.73           O  
ANISOU 2434  O   ALA A 394    22232  30351  18747   6737  -3441   5198       O  
ATOM   2435  CB  ALA A 394     -27.071  16.204  26.323  1.00179.18           C  
ANISOU 2435  CB  ALA A 394    21628  28171  18283   6447  -2796   4799       C  
ATOM   2436  N   GLN A 395     -24.848  18.378  27.657  1.00181.67           N  
ANISOU 2436  N   GLN A 395    20900  29974  18154   6205  -3412   4667       N  
ATOM   2437  CA  GLN A 395     -23.505  18.626  28.204  1.00186.25           C  
ANISOU 2437  CA  GLN A 395    21005  31182  18578   6386  -3702   4749       C  
ATOM   2438  C   GLN A 395     -23.612  19.022  29.669  1.00193.53           C  
ANISOU 2438  C   GLN A 395    21978  32418  19137   6243  -3954   4860       C  
ATOM   2439  O   GLN A 395     -22.886  18.487  30.511  1.00195.10           O  
ANISOU 2439  O   GLN A 395    22176  32628  19326   6389  -4217   5021       O  
ATOM   2440  CB  GLN A 395     -22.789  19.752  27.437  1.00186.17           C  
ANISOU 2440  CB  GLN A 395    20519  31544  18673   6105  -3730   4454       C  
ATOM   2441  CG  GLN A 395     -22.634  19.492  25.944  1.00193.82           C  
ANISOU 2441  CG  GLN A 395    21402  32268  19975   6212  -3478   4319       C  
ATOM   2442  CD  GLN A 395     -21.618  20.358  25.262  1.00207.87           C  
ANISOU 2442  CD  GLN A 395    22729  34287  21966   5952  -3555   4061       C  
ATOM   2443  OE1 GLN A 395     -21.206  21.413  25.760  1.00203.06           O  
ANISOU 2443  OE1 GLN A 395    21746  34324  21085   5742  -3721   4000       O  
ATOM   2444  NE2 GLN A 395     -21.146  19.874  24.124  1.00198.88           N  
ANISOU 2444  NE2 GLN A 395    21335  33297  20934   6380  -3377   4114       N  
ATOM   2445  N   VAL A 396     -24.530  19.964  29.959  1.00188.24           N  
ANISOU 2445  N   VAL A 396    21491  31671  18362   5747  -3916   4657       N  
ATOM   2446  CA  VAL A 396     -24.820  20.483  31.297  1.00190.14           C  
ANISOU 2446  CA  VAL A 396    21828  32170  18247   5534  -4117   4697       C  
ATOM   2447  C   VAL A 396     -25.418  19.354  32.147  1.00197.98           C  
ANISOU 2447  C   VAL A 396    23245  32894  19084   5822  -4098   5038       C  
ATOM   2448  O   VAL A 396     -24.961  19.125  33.268  1.00199.55           O  
ANISOU 2448  O   VAL A 396    23531  33113  19178   5799  -4379   5151       O  
ATOM   2449  CB  VAL A 396     -25.755  21.725  31.247  1.00189.90           C  
ANISOU 2449  CB  VAL A 396    21926  32043  18186   4957  -4027   4372       C  
ATOM   2450  CG1 VAL A 396     -25.791  22.444  32.594  1.00191.27           C  
ANISOU 2450  CG1 VAL A 396    22100  32598  17978   4728  -4270   4353       C  
ATOM   2451  CG2 VAL A 396     -25.344  22.690  30.136  1.00187.49           C  
ANISOU 2451  CG2 VAL A 396    21288  31837  18110   4685  -3966   4056       C  
ATOM   2452  N   ASN A 397     -26.404  18.627  31.583  1.00193.44           N  
ANISOU 2452  N   ASN A 397    23073  31716  18709   5869  -3813   5089       N  
ATOM   2453  CA  ASN A 397     -27.096  17.505  32.219  1.00195.16           C  
ANISOU 2453  CA  ASN A 397    23741  31577  18836   6102  -3737   5408       C  
ATOM   2454  C   ASN A 397     -26.223  16.261  32.403  1.00202.51           C  
ANISOU 2454  C   ASN A 397    24811  32032  20102   6284  -3933   5561       C  
ATOM   2455  O   ASN A 397     -26.580  15.398  33.205  1.00203.85           O  
ANISOU 2455  O   ASN A 397    25342  31910  20203   6374  -3982   5818       O  
ATOM   2456  CB  ASN A 397     -28.370  17.152  31.439  1.00191.45           C  
ANISOU 2456  CB  ASN A 397    23672  30464  18606   5938  -3404   5324       C  
ATOM   2457  CG  ASN A 397     -29.444  18.218  31.456  1.00208.18           C  
ANISOU 2457  CG  ASN A 397    25922  32503  20673   5404  -3294   5047       C  
ATOM   2458  OD1 ASN A 397     -29.522  19.066  32.356  1.00201.33           O  
ANISOU 2458  OD1 ASN A 397    24993  31978  19526   5154  -3448   4973       O  
ATOM   2459  ND2 ASN A 397     -30.322  18.178  30.471  1.00197.84           N  
ANISOU 2459  ND2 ASN A 397    24811  30733  19625   5230  -3023   4886       N  
ATOM   2460  N   ASN A 398     -25.079  16.175  31.678  1.00201.83           N  
ANISOU 2460  N   ASN A 398    24355  32085  20248   6487  -4011   5487       N  
ATOM   2461  CA  ASN A 398     -24.121  15.054  31.705  1.00203.98           C  
ANISOU 2461  CA  ASN A 398    24683  31916  20903   6648  -4207   5583       C  
ATOM   2462  C   ASN A 398     -24.800  13.730  31.288  1.00207.74           C  
ANISOU 2462  C   ASN A 398    25648  31537  21745   6663  -4039   5673       C  
ATOM   2463  O   ASN A 398     -24.517  12.669  31.855  1.00209.35           O  
ANISOU 2463  O   ASN A 398    26102  31280  22163   6674  -4231   5836       O  
ATOM   2464  CB  ASN A 398     -23.382  14.945  33.062  1.00205.71           C  
ANISOU 2464  CB  ASN A 398    24981  32029  21152   6399  -4651   5625       C  
ATOM   2465  CG  ASN A 398     -22.822  16.251  33.571  1.00219.05           C  
ANISOU 2465  CG  ASN A 398    26773  33124  23333   5291  -5053   5012       C  
ATOM   2466  OD1 ASN A 398     -21.922  16.854  32.972  1.00215.16           O  
ANISOU 2466  OD1 ASN A 398    25773  33159  22819   5477  -5070   4921       O  
ATOM   2467  ND2 ASN A 398     -23.341  16.717  34.700  1.00212.78           N  
ANISOU 2467  ND2 ASN A 398    25974  33019  21853   5481  -5082   5251       N  
ATOM   2468  N   TYR A 399     -25.709  13.820  30.289  1.00204.60           N  
ANISOU 2468  N   TYR A 399    25275  31290  21174   6975  -3611   5710       N  
ATOM   2469  CA  TYR A 399     -26.484  12.708  29.738  1.00204.61           C  
ANISOU 2469  CA  TYR A 399    25684  30702  21357   7171  -3351   5842       C  
ATOM   2470  C   TYR A 399     -25.590  11.778  28.911  1.00208.88           C  
ANISOU 2470  C   TYR A 399    26186  30657  22520   7139  -3451   5693       C  
ATOM   2471  O   TYR A 399     -24.802  12.249  28.079  1.00208.52           O  
ANISOU 2471  O   TYR A 399    25752  30867  22610   7215  -3437   5494       O  
ATOM   2472  CB  TYR A 399     -27.649  13.246  28.894  1.00202.83           C  
ANISOU 2472  CB  TYR A 399    25568  30469  21031   7108  -2979   5710       C  
ATOM   2473  CG  TYR A 399     -28.807  12.281  28.731  1.00204.32           C  
ANISOU 2473  CG  TYR A 399    26296  30014  21324   7116  -2741   5843       C  
ATOM   2474  CD1 TYR A 399     -29.922  12.354  29.562  1.00205.46           C  
ANISOU 2474  CD1 TYR A 399    26771  30041  21254   6853  -2683   5947       C  
ATOM   2475  CD2 TYR A 399     -28.816  11.333  27.714  1.00205.47           C  
ANISOU 2475  CD2 TYR A 399    26615  29645  21808   7325  -2575   5829       C  
ATOM   2476  CE1 TYR A 399     -30.999  11.483  29.409  1.00206.40           C  
ANISOU 2476  CE1 TYR A 399    27366  29619  21438   6882  -2446   6096       C  
ATOM   2477  CE2 TYR A 399     -29.895  10.465  27.541  1.00206.35           C  
ANISOU 2477  CE2 TYR A 399    27222  29186  21996   7337  -2349   5954       C  
ATOM   2478  CZ  TYR A 399     -30.990  10.553  28.387  1.00211.66           C  
ANISOU 2478  CZ  TYR A 399    28207  29623  22593   6836  -2365   5981       C  
ATOM   2479  OH  TYR A 399     -32.057   9.701  28.242  1.00212.35           O  
ANISOU 2479  OH  TYR A 399    28757  29138  22787   6754  -2164   6089       O  
ATOM   2480  N   GLU A 400     -25.724  10.455  29.155  1.00207.85           N  
ANISOU 2480  N   GLU A 400    26393  30026  22553   7328  -3469   5928       N  
ATOM   2481  CA  GLU A 400     -24.950   9.392  28.508  1.00208.83           C  
ANISOU 2481  CA  GLU A 400    26487  29695  23165   7470  -3540   5892       C  
ATOM   2482  C   GLU A 400     -25.117   9.375  26.982  1.00210.24           C  
ANISOU 2482  C   GLU A 400    26607  29642  23634   7482  -3255   5625       C  
ATOM   2483  O   GLU A 400     -26.215   9.599  26.467  1.00208.51           O  
ANISOU 2483  O   GLU A 400    26602  29442  23182   7598  -2911   5637       O  
ATOM   2484  CB  GLU A 400     -25.230   8.003  29.142  1.00211.47           C  
ANISOU 2484  CB  GLU A 400    27236  29339  23774   7344  -3698   6098       C  
ATOM   2485  CG  GLU A 400     -26.649   7.449  29.013  1.00218.30           C  
ANISOU 2485  CG  GLU A 400    28581  29475  24888   6764  -3578   6015       C  
ATOM   2486  CD  GLU A 400     -27.609   7.559  30.188  1.00232.20           C  
ANISOU 2486  CD  GLU A 400    30650  30614  26963   5459  -3953   5783       C  
ATOM   2487  OE1 GLU A 400     -27.176   7.896  31.315  1.00226.11           O  
ANISOU 2487  OE1 GLU A 400    29790  30458  25665   5812  -4050   6010       O  
ATOM   2488  OE2 GLU A 400     -28.810   7.281  29.971  1.00227.85           O  
ANISOU 2488  OE2 GLU A 400    30436  29956  26183   5699  -3655   6024       O  
ATOM   2489  N   LEU A 401     -23.997   9.138  26.282  1.00208.82           N  
ANISOU 2489  N   LEU A 401    26103  29541  23700   7757  -3297   5536       N  
ATOM   2490  CA  LEU A 401     -23.872   9.087  24.825  1.00208.09           C  
ANISOU 2490  CA  LEU A 401    25878  29396  23792   7973  -3022   5335       C  
ATOM   2491  C   LEU A 401     -24.175   7.662  24.306  1.00211.77           C  
ANISOU 2491  C   LEU A 401    26699  29015  24750   7894  -2968   5309       C  
ATOM   2492  O   LEU A 401     -23.322   6.773  24.408  1.00213.23           O  
ANISOU 2492  O   LEU A 401    26812  28861  25346   7886  -3195   5321       O  
ATOM   2493  CB  LEU A 401     -22.437   9.535  24.450  1.00208.60           C  
ANISOU 2493  CB  LEU A 401    25411  29749  24097   7948  -3209   5136       C  
ATOM   2494  CG  LEU A 401     -22.106   9.791  22.979  1.00210.91           C  
ANISOU 2494  CG  LEU A 401    25461  29976  24697   7857  -3016   4795       C  
ATOM   2495  CD1 LEU A 401     -21.254  11.027  22.839  1.00210.39           C  
ANISOU 2495  CD1 LEU A 401    24884  30466  24590   7693  -3136   4614       C  
ATOM   2496  CD2 LEU A 401     -21.370   8.607  22.358  1.00214.10           C  
ANISOU 2496  CD2 LEU A 401    25876  29783  25689   7882  -3061   4687       C  
ATOM   2497  N   ASP A 402     -25.398   7.445  23.773  1.00207.99           N  
ANISOU 2497  N   ASP A 402    26608  28430  23990   8213  -2573   5415       N  
ATOM   2498  CA  ASP A 402     -25.803   6.138  23.243  1.00208.40           C  
ANISOU 2498  CA  ASP A 402    27028  27802  24352   8326  -2442   5449       C  
ATOM   2499  C   ASP A 402     -25.722   6.147  21.719  1.00209.86           C  
ANISOU 2499  C   ASP A 402    27106  27845  24786   8368  -2201   5129       C  
ATOM   2500  O   ASP A 402     -26.279   7.045  21.081  1.00207.61           O  
ANISOU 2500  O   ASP A 402    26806  27887  24190   8461  -1931   5019       O  
ATOM   2501  CB  ASP A 402     -27.210   5.723  23.725  1.00209.30           C  
ANISOU 2501  CB  ASP A 402    27669  27518  24339   8127  -2319   5614       C  
ATOM   2502  CG  ASP A 402     -27.664   6.379  25.023  1.00216.64           C  
ANISOU 2502  CG  ASP A 402    28590  28497  25226   7365  -2626   5612       C  
ATOM   2503  OD1 ASP A 402     -27.250   5.914  26.094  1.00218.74           O  
ANISOU 2503  OD1 ASP A 402    28858  28635  25619   7159  -2968   5762       O  
ATOM   2504  OD2 ASP A 402     -28.317   7.441  24.955  1.00218.77           O  
ANISOU 2504  OD2 ASP A 402    28833  28996  25292   7050  -2522   5461       O  
ATOM   2505  N   PHE A 403     -25.025   5.139  21.143  1.00208.41           N  
ANISOU 2505  N   PHE A 403    26887  27352  24948   8653  -2208   5098       N  
ATOM   2506  CA  PHE A 403     -24.803   4.959  19.696  1.00207.66           C  
ANISOU 2506  CA  PHE A 403    26705  27147  25050   8853  -1963   4832       C  
ATOM   2507  C   PHE A 403     -26.110   4.906  18.888  1.00207.85           C  
ANISOU 2507  C   PHE A 403    27141  26846  24988   8787  -1627   4716       C  
ATOM   2508  O   PHE A 403     -26.129   5.296  17.718  1.00206.77           O  
ANISOU 2508  O   PHE A 403    26933  26850  24779   8979  -1367   4498       O  
ATOM   2509  CB  PHE A 403     -23.947   3.703  19.377  1.00211.00           C  
ANISOU 2509  CB  PHE A 403    27017  27037  26118   8775  -2151   4728       C  
ATOM   2510  CG  PHE A 403     -22.702   3.384  20.186  1.00213.68           C  
ANISOU 2510  CG  PHE A 403    26984  27409  26797   8603  -2568   4774       C  
ATOM   2511  CD1 PHE A 403     -21.691   4.327  20.345  1.00215.41           C  
ANISOU 2511  CD1 PHE A 403    26716  28102  27026   8423  -2738   4634       C  
ATOM   2512  CD2 PHE A 403     -22.494   2.106  20.693  1.00217.17           C  
ANISOU 2512  CD2 PHE A 403    27527  27290  27696   8438  -2839   4884       C  
ATOM   2513  CE1 PHE A 403     -20.530   4.019  21.067  1.00217.86           C  
ANISOU 2513  CE1 PHE A 403    26725  28410  27640   8308  -3110   4676       C  
ATOM   2514  CE2 PHE A 403     -21.333   1.799  21.410  1.00220.65           C  
ANISOU 2514  CE2 PHE A 403    27623  27670  28546   8160  -3267   4880       C  
ATOM   2515  CZ  PHE A 403     -20.359   2.756  21.591  1.00219.34           C  
ANISOU 2515  CZ  PHE A 403    27058  28100  28181   8300  -3342   4835       C  
ATOM   2516  N   GLY A 404     -27.174   4.424  19.530  1.00204.82           N  
ANISOU 2516  N   GLY A 404    27271  26162  24389   8870  -1536   4977       N  
ATOM   2517  CA  GLY A 404     -28.507   4.298  18.953  1.00203.38           C  
ANISOU 2517  CA  GLY A 404    27584  25636  24056   8885  -1203   4938       C  
ATOM   2518  C   GLY A 404     -29.418   5.474  19.240  1.00203.20           C  
ANISOU 2518  C   GLY A 404    27614  25957  23636   8663  -1087   4942       C  
ATOM   2519  O   GLY A 404     -30.341   5.735  18.463  1.00200.64           O  
ANISOU 2519  O   GLY A 404    27537  25479  23218   8602   -816   4787       O  
ATOM   2520  N   GLN A 405     -29.172   6.190  20.359  1.00199.65           N  
ANISOU 2520  N   GLN A 405    26997  26055  22807   8776  -1223   5190       N  
ATOM   2521  CA  GLN A 405     -29.973   7.352  20.748  1.00194.67           C  
ANISOU 2521  CA  GLN A 405    26298  25702  21968   8281  -1229   5109       C  
ATOM   2522  C   GLN A 405     -29.524   8.638  20.039  1.00193.30           C  
ANISOU 2522  C   GLN A 405    25626  26027  21791   8045  -1246   4792       C  
ATOM   2523  O   GLN A 405     -30.322   9.570  19.918  1.00188.90           O  
ANISOU 2523  O   GLN A 405    25045  25535  21193   7539  -1202   4601       O  
ATOM   2524  CB  GLN A 405     -30.048   7.522  22.275  1.00197.47           C  
ANISOU 2524  CB  GLN A 405    26681  26296  22053   8224  -1429   5419       C  
ATOM   2525  CG  GLN A 405     -30.851   6.428  23.004  1.00213.56           C  
ANISOU 2525  CG  GLN A 405    29094  27548  24500   7554  -1616   5471       C  
ATOM   2526  CD  GLN A 405     -32.250   6.201  22.461  1.00227.98           C  
ANISOU 2526  CD  GLN A 405    31080  28677  26863   6476  -1630   5100       C  
ATOM   2527  OE1 GLN A 405     -33.071   7.120  22.349  1.00223.13           O  
ANISOU 2527  OE1 GLN A 405    30638  28381  25761   6718  -1324   5151       O  
ATOM   2528  NE2 GLN A 405     -32.546   4.960  22.108  1.00224.12           N  
ANISOU 2528  NE2 GLN A 405    30980  27700  26475   6829  -1462   5255       N  
ATOM   2529  N   ILE A 406     -28.264   8.681  19.552  1.00190.85           N  
ANISOU 2529  N   ILE A 406    24928  26051  21534   8412  -1295   4735       N  
ATOM   2530  CA  ILE A 406     -27.753   9.801  18.759  1.00187.60           C  
ANISOU 2530  CA  ILE A 406    24049  26086  21143   8215  -1286   4443       C  
ATOM   2531  C   ILE A 406     -28.397   9.689  17.365  1.00187.66           C  
ANISOU 2531  C   ILE A 406    24239  25700  21362   8047  -1030   4145       C  
ATOM   2532  O   ILE A 406     -28.667  10.707  16.725  1.00183.71           O  
ANISOU 2532  O   ILE A 406    23547  25382  20873   7656   -971   3886       O  
ATOM   2533  CB  ILE A 406     -26.197   9.862  18.743  1.00194.41           C  
ANISOU 2533  CB  ILE A 406    24415  27475  21979   8651  -1424   4503       C  
ATOM   2534  CG1 ILE A 406     -25.691  11.174  18.140  1.00192.28           C  
ANISOU 2534  CG1 ILE A 406    23629  27752  21676   8353  -1457   4249       C  
ATOM   2535  CG2 ILE A 406     -25.535   8.641  18.089  1.00198.15           C  
ANISOU 2535  CG2 ILE A 406    24954  27616  22718   9103  -1343   4494       C  
ATOM   2536  CD1 ILE A 406     -24.776  11.893  19.045  1.00202.30           C  
ANISOU 2536  CD1 ILE A 406    24447  29544  22875   8281  -1756   4324       C  
ATOM   2537  N   ILE A 407     -28.716   8.439  16.952  1.00184.47           N  
ANISOU 2537  N   ILE A 407    24246  24728  21117   8324   -884   4193       N  
ATOM   2538  CA  ILE A 407     -29.397   8.117  15.700  1.00181.67           C  
ANISOU 2538  CA  ILE A 407    24144  23931  20953   8189   -648   3929       C  
ATOM   2539  C   ILE A 407     -30.838   8.662  15.770  1.00180.52           C  
ANISOU 2539  C   ILE A 407    24254  23561  20776   7590   -584   3827       C  
ATOM   2540  O   ILE A 407     -31.339   9.157  14.758  1.00176.92           O  
ANISOU 2540  O   ILE A 407    23779  23041  20403   7293   -448   3542       O  
ATOM   2541  CB  ILE A 407     -29.275   6.593  15.361  1.00188.80           C  
ANISOU 2541  CB  ILE A 407    25415  24295  22027   8672   -526   4003       C  
ATOM   2542  CG1 ILE A 407     -27.823   6.256  14.896  1.00191.83           C  
ANISOU 2542  CG1 ILE A 407    25454  24929  22503   9106   -472   3856       C  
ATOM   2543  CG2 ILE A 407     -30.319   6.138  14.318  1.00187.18           C  
ANISOU 2543  CG2 ILE A 407    25711  23434  21974   8416   -318   3837       C  
ATOM   2544  CD1 ILE A 407     -27.433   4.748  14.745  1.00202.66           C  
ANISOU 2544  CD1 ILE A 407    26906  25824  24273   9318   -545   3864       C  
ATOM   2545  N   THR A 408     -31.472   8.641  16.975  1.00176.18           N  
ANISOU 2545  N   THR A 408    23899  22955  20086   7416   -689   4059       N  
ATOM   2546  CA  THR A 408     -32.820   9.197  17.174  1.00171.47           C  
ANISOU 2546  CA  THR A 408    23506  22206  19441   6866   -635   3981       C  
ATOM   2547  C   THR A 408     -32.794  10.732  17.096  1.00170.06           C  
ANISOU 2547  C   THR A 408    22933  22529  19153   6483   -704   3786       C  
ATOM   2548  O   THR A 408     -33.776  11.318  16.643  1.00165.87           O  
ANISOU 2548  O   THR A 408    22488  21884  18652   6059   -604   3590       O  
ATOM   2549  CB  THR A 408     -33.525   8.663  18.443  1.00180.88           C  
ANISOU 2549  CB  THR A 408    25042  23171  20514   6800   -696   4286       C  
ATOM   2550  OG1 THR A 408     -32.996   9.289  19.614  1.00180.89           O  
ANISOU 2550  OG1 THR A 408    24788  23658  20285   6816   -907   4471       O  
ATOM   2551  CG2 THR A 408     -33.475   7.141  18.560  1.00184.50           C  
ANISOU 2551  CG2 THR A 408    25906  23111  21082   7189   -636   4507       C  
ATOM   2552  N   ILE A 409     -31.670  11.373  17.520  1.00166.41           N  
ANISOU 2552  N   ILE A 409    22042  22615  18571   6633   -874   3836       N  
ATOM   2553  CA  ILE A 409     -31.477  12.833  17.467  1.00162.25           C  
ANISOU 2553  CA  ILE A 409    21125  22576  17945   6293   -954   3657       C  
ATOM   2554  C   ILE A 409     -31.396  13.293  16.007  1.00161.78           C  
ANISOU 2554  C   ILE A 409    20906  22523  18041   6178   -801   3346       C  
ATOM   2555  O   ILE A 409     -32.105  14.224  15.641  1.00157.66           O  
ANISOU 2555  O   ILE A 409    20358  22034  17511   5750   -749   3153       O  
ATOM   2556  CB  ILE A 409     -30.280  13.334  18.333  1.00167.71           C  
ANISOU 2556  CB  ILE A 409    21408  23849  18467   6469  -1189   3799       C  
ATOM   2557  CG1 ILE A 409     -30.570  13.137  19.830  1.00169.65           C  
ANISOU 2557  CG1 ILE A 409    21822  24131  18508   6462  -1348   4078       C  
ATOM   2558  CG2 ILE A 409     -29.943  14.815  18.034  1.00165.68           C  
ANISOU 2558  CG2 ILE A 409    20733  24067  18150   6129  -1251   3575       C  
ATOM   2559  CD1 ILE A 409     -29.346  13.175  20.752  1.00179.92           C  
ANISOU 2559  CD1 ILE A 409    22804  25914  19642   6773  -1589   4288       C  
ATOM   2560  N   SER A 410     -30.572  12.616  15.174  1.00160.10           N  
ANISOU 2560  N   SER A 410    20606  22264  17961   6570   -720   3302       N  
ATOM   2561  CA  SER A 410     -30.433  12.916  13.742  1.00157.91           C  
ANISOU 2561  CA  SER A 410    20194  21989  17817   6513   -558   3019       C  
ATOM   2562  C   SER A 410     -31.768  12.741  13.007  1.00157.82           C  
ANISOU 2562  C   SER A 410    20564  21491  17909   6209   -378   2846       C  
ATOM   2563  O   SER A 410     -32.055  13.486  12.070  1.00154.12           O  
ANISOU 2563  O   SER A 410    19987  21090  17480   5934   -283   2604       O  
ATOM   2564  CB  SER A 410     -29.359  12.040  13.105  1.00164.85           C  
ANISOU 2564  CB  SER A 410    20962  22868  18804   7043   -494   3027       C  
ATOM   2565  OG  SER A 410     -29.656  10.660  13.243  1.00175.59           O  
ANISOU 2565  OG  SER A 410    22742  23719  20254   7360   -428   3162       O  
ATOM   2566  N   ILE A 411     -32.588  11.773  13.466  1.00154.58           N  
ANISOU 2566  N   ILE A 411    20595  20605  17532   6246   -340   2984       N  
ATOM   2567  CA  ILE A 411     -33.911  11.470  12.926  1.00151.85           C  
ANISOU 2567  CA  ILE A 411    20634  19784  17280   5957   -187   2854       C  
ATOM   2568  C   ILE A 411     -34.937  12.536  13.354  1.00151.55           C  
ANISOU 2568  C   ILE A 411    20590  19853  17138   5431   -225   2800       C  
ATOM   2569  O   ILE A 411     -35.655  13.044  12.493  1.00147.93           O  
ANISOU 2569  O   ILE A 411    20160  19310  16736   5122   -118   2571       O  
ATOM   2570  CB  ILE A 411     -34.331  10.003  13.263  1.00158.01           C  
ANISOU 2570  CB  ILE A 411    21877  20016  18142   6193   -132   3033       C  
ATOM   2571  CG1 ILE A 411     -33.655   9.016  12.285  1.00161.60           C  
ANISOU 2571  CG1 ILE A 411    22412  20232  18756   6628    -15   2944       C  
ATOM   2572  CG2 ILE A 411     -35.861   9.806  13.270  1.00156.48           C  
ANISOU 2572  CG2 ILE A 411    22074  19394  17985   5793    -35   2992       C  
ATOM   2573  CD1 ILE A 411     -33.559   7.568  12.755  1.00173.55           C  
ANISOU 2573  CD1 ILE A 411    24304  21293  20343   7012     -3   3171       C  
ATOM   2574  N   THR A 412     -34.998  12.886  14.661  1.00147.89           N  
ANISOU 2574  N   THR A 412    20087  19590  16515   5343   -376   3004       N  
ATOM   2575  CA  THR A 412     -35.974  13.871  15.150  1.00144.02           C  
ANISOU 2575  CA  THR A 412    19604  19200  15915   4878   -407   2953       C  
ATOM   2576  C   THR A 412     -35.586  15.319  14.824  1.00144.90           C  
ANISOU 2576  C   THR A 412    19323  19767  15966   4647   -467   2766       C  
ATOM   2577  O   THR A 412     -36.487  16.152  14.726  1.00141.46           O  
ANISOU 2577  O   THR A 412    18913  19335  15501   4257   -434   2632       O  
ATOM   2578  CB  THR A 412     -36.330  13.690  16.630  1.00153.58           C  
ANISOU 2578  CB  THR A 412    20966  20423  16965   4842   -520   3219       C  
ATOM   2579  OG1 THR A 412     -35.150  13.532  17.415  1.00156.80           O  
ANISOU 2579  OG1 THR A 412    21172  21138  17265   5180   -685   3420       O  
ATOM   2580  CG2 THR A 412     -37.285  12.529  16.853  1.00153.56           C  
ANISOU 2580  CG2 THR A 412    21422  19897  17028   4845   -413   3356       C  
ATOM   2581  N   ALA A 413     -34.281  15.621  14.625  1.00142.52           N  
ANISOU 2581  N   ALA A 413    18662  19838  15650   4877   -547   2754       N  
ATOM   2582  CA  ALA A 413     -33.837  16.971  14.246  1.00139.77           C  
ANISOU 2582  CA  ALA A 413    17941  19908  15258   4647   -596   2581       C  
ATOM   2583  C   ALA A 413     -34.165  17.240  12.773  1.00140.05           C  
ANISOU 2583  C   ALA A 413    17974  19808  15431   4503   -424   2324       C  
ATOM   2584  O   ALA A 413     -34.403  18.388  12.400  1.00137.19           O  
ANISOU 2584  O   ALA A 413    17453  19629  15043   4178   -422   2165       O  
ATOM   2585  CB  ALA A 413     -32.351  17.152  14.507  1.00143.28           C  
ANISOU 2585  CB  ALA A 413    17993  20802  15646   4921   -732   2661       C  
ATOM   2586  N   THR A 414     -34.200  16.174  11.949  1.00136.39           N  
ANISOU 2586  N   THR A 414    17707  19011  15105   4745   -282   2284       N  
ATOM   2587  CA  THR A 414     -34.593  16.233  10.542  1.00133.64           C  
ANISOU 2587  CA  THR A 414    17417  18490  14872   4635   -111   2044       C  
ATOM   2588  C   THR A 414     -36.131  16.345  10.519  1.00133.23           C  
ANISOU 2588  C   THR A 414    17681  18107  14833   4266    -45   1973       C  
ATOM   2589  O   THR A 414     -36.681  17.093   9.708  1.00130.20           O  
ANISOU 2589  O   THR A 414    17259  17740  14470   3981     25   1779       O  
ATOM   2590  CB  THR A 414     -34.035  15.012   9.788  1.00142.75           C  
ANISOU 2590  CB  THR A 414    18676  19416  16147   5050      4   2024       C  
ATOM   2591  OG1 THR A 414     -32.612  15.042   9.873  1.00144.12           O  
ANISOU 2591  OG1 THR A 414    18499  19964  16295   5381    -65   2094       O  
ATOM   2592  CG2 THR A 414     -34.450  14.971   8.319  1.00139.72           C  
ANISOU 2592  CG2 THR A 414    18379  18845  15862   4954    182   1766       C  
ATOM   2593  N   ALA A 415     -36.808  15.638  11.447  1.00129.32           N  
ANISOU 2593  N   ALA A 415    17480  17341  14315   4270    -74   2144       N  
ATOM   2594  CA  ALA A 415     -38.261  15.653  11.594  1.00126.32           C  
ANISOU 2594  CA  ALA A 415    17385  16671  13939   3932    -16   2112       C  
ATOM   2595  C   ALA A 415     -38.760  17.046  11.988  1.00126.17           C  
ANISOU 2595  C   ALA A 415    17196  16934  13808   3556    -87   2047       C  
ATOM   2596  O   ALA A 415     -39.700  17.545  11.368  1.00122.95           O  
ANISOU 2596  O   ALA A 415    16854  16426  13435   3260     -9   1882       O  
ATOM   2597  CB  ALA A 415     -38.693  14.622  12.623  1.00129.19           C  
ANISOU 2597  CB  ALA A 415    18057  16747  14282   4035    -37   2348       C  
ATOM   2598  N   ALA A 416     -38.105  17.684  12.988  1.00122.88           N  
ANISOU 2598  N   ALA A 416    16558  16875  13257   3579   -239   2167       N  
ATOM   2599  CA  ALA A 416     -38.440  19.024  13.484  1.00120.11           C  
ANISOU 2599  CA  ALA A 416    16047  16801  12787   3254   -324   2106       C  
ATOM   2600  C   ALA A 416     -38.128  20.104  12.457  1.00122.02           C  
ANISOU 2600  C   ALA A 416    16035  17257  13069   3095   -297   1890       C  
ATOM   2601  O   ALA A 416     -38.844  21.101  12.404  1.00119.09           O  
ANISOU 2601  O   ALA A 416    15646  16940  12663   2776   -295   1775       O  
ATOM   2602  CB  ALA A 416     -37.712  19.312  14.787  1.00122.54           C  
ANISOU 2602  CB  ALA A 416    16197  17429  12933   3348   -502   2281       C  
ATOM   2603  N   SER A 417     -37.068  19.905  11.644  1.00120.00           N  
ANISOU 2603  N   SER A 417    15586  17124  12884   3325   -270   1841       N  
ATOM   2604  CA  SER A 417     -36.672  20.815  10.570  1.00118.37           C  
ANISOU 2604  CA  SER A 417    15140  17119  12717   3199   -223   1655       C  
ATOM   2605  C   SER A 417     -37.857  20.968   9.596  1.00119.83           C  
ANISOU 2605  C   SER A 417    15525  17029  12976   2955    -86   1482       C  
ATOM   2606  O   SER A 417     -38.309  22.092   9.371  1.00117.16           O  
ANISOU 2606  O   SER A 417    15108  16801  12607   2656    -95   1372       O  
ATOM   2607  CB  SER A 417     -35.431  20.282   9.857  1.00124.63           C  
ANISOU 2607  CB  SER A 417    15738  18041  13574   3533   -182   1649       C  
ATOM   2608  OG  SER A 417     -35.276  20.770   8.533  1.00133.32           O  
ANISOU 2608  OG  SER A 417    16711  19208  14735   3445    -69   1463       O  
ATOM   2609  N   ILE A 418     -38.402  19.830   9.099  1.00116.86           N  
ANISOU 2609  N   ILE A 418    15424  16285  12694   3078     30   1466       N  
ATOM   2610  CA  ILE A 418     -39.551  19.759   8.184  1.00114.58           C  
ANISOU 2610  CA  ILE A 418    15345  15717  12474   2873    153   1307       C  
ATOM   2611  C   ILE A 418     -40.800  20.405   8.814  1.00117.56           C  
ANISOU 2611  C   ILE A 418    15838  16034  12796   2535    119   1309       C  
ATOM   2612  O   ILE A 418     -41.490  21.193   8.157  1.00115.01           O  
ANISOU 2612  O   ILE A 418    15495  15723  12479   2282    159   1162       O  
ATOM   2613  CB  ILE A 418     -39.807  18.285   7.747  1.00119.18           C  
ANISOU 2613  CB  ILE A 418    16216  15906  13159   3085    259   1310       C  
ATOM   2614  CG1 ILE A 418     -38.622  17.734   6.931  1.00121.71           C  
ANISOU 2614  CG1 ILE A 418    16416  16291  13536   3427    318   1260       C  
ATOM   2615  CG2 ILE A 418     -41.127  18.145   6.971  1.00117.78           C  
ANISOU 2615  CG2 ILE A 418    16277  15433  13041   2836    362   1157       C  
ATOM   2616  CD1 ILE A 418     -38.535  16.219   6.876  1.00130.93           C  
ANISOU 2616  CD1 ILE A 418    17851  17103  14793   3736    386   1315       C  
ATOM   2617  N   GLY A 419     -41.045  20.067  10.081  1.00115.85           N  
ANISOU 2617  N   GLY A 419    15732  15771  12515   2554     47   1481       N  
ATOM   2618  CA  GLY A 419     -42.182  20.532  10.867  1.00114.39           C  
ANISOU 2618  CA  GLY A 419    15663  15542  12260   2282     22   1511       C  
ATOM   2619  C   GLY A 419     -42.241  22.027  11.096  1.00116.81           C  
ANISOU 2619  C   GLY A 419    15764  16140  12478   2045    -53   1431       C  
ATOM   2620  O   GLY A 419     -43.211  22.666  10.677  1.00114.16           O  
ANISOU 2620  O   GLY A 419    15473  15747  12156   1796     -5   1306       O  
ATOM   2621  N   ALA A 420     -41.196  22.585  11.759  1.00114.81           N  
ANISOU 2621  N   ALA A 420    15288  16200  12134   2127   -178   1500       N  
ATOM   2622  CA  ALA A 420     -41.047  24.006  12.109  1.00113.44           C  
ANISOU 2622  CA  ALA A 420    14918  16313  11869   1917   -272   1432       C  
ATOM   2623  C   ALA A 420     -41.390  24.961  10.962  1.00115.10           C  
ANISOU 2623  C   ALA A 420    15050  16539  12143   1707   -208   1239       C  
ATOM   2624  O   ALA A 420     -40.845  24.836   9.862  1.00114.95           O  
ANISOU 2624  O   ALA A 420    14937  16532  12207   1793   -145   1165       O  
ATOM   2625  CB  ALA A 420     -39.640  24.283  12.627  1.00116.12           C  
ANISOU 2625  CB  ALA A 420    14999  16984  12138   2067   -405   1509       C  
ATOM   2626  N   ALA A 421     -42.330  25.885  11.224  1.00109.19           N  
ANISOU 2626  N   ALA A 421    14353  15786  11349   1448   -217   1164       N  
ATOM   2627  CA  ALA A 421     -42.806  26.877  10.264  1.00106.46           C  
ANISOU 2627  CA  ALA A 421    13961  15440  11049   1239   -168   1002       C  
ATOM   2628  C   ALA A 421     -41.745  27.929   9.980  1.00109.86           C  
ANISOU 2628  C   ALA A 421    14137  16144  11461   1187   -239    950       C  
ATOM   2629  O   ALA A 421     -40.902  28.208  10.832  1.00110.77           O  
ANISOU 2629  O   ALA A 421    14113  16478  11498   1227   -354   1019       O  
ATOM   2630  CB  ALA A 421     -44.063  27.539  10.792  1.00105.57           C  
ANISOU 2630  CB  ALA A 421    13970  15257  10885   1018   -169    956       C  
ATOM   2631  N   GLY A 422     -41.805  28.513   8.790  1.00105.21           N  
ANISOU 2631  N   GLY A 422    13490  15549  10937   1083   -172    833       N  
ATOM   2632  CA  GLY A 422     -40.874  29.545   8.354  1.00105.34           C  
ANISOU 2632  CA  GLY A 422    13276  15802  10947    994   -216    785       C  
ATOM   2633  C   GLY A 422     -41.146  30.899   8.969  1.00108.63           C  
ANISOU 2633  C   GLY A 422    13662  16314  11299    753   -307    736       C  
ATOM   2634  O   GLY A 422     -41.262  31.895   8.254  1.00107.39           O  
ANISOU 2634  O   GLY A 422    13461  16175  11168    580   -286    649       O  
ATOM   2635  N   ILE A 423     -41.242  30.944  10.300  1.00105.96           N  
ANISOU 2635  N   ILE A 423    13362  16031  10868    747   -407    793       N  
ATOM   2636  CA  ILE A 423     -41.515  32.161  11.061  1.00105.58           C  
ANISOU 2636  CA  ILE A 423    13313  16063  10739    538   -500    733       C  
ATOM   2637  C   ILE A 423     -40.510  32.299  12.222  1.00112.50           C  
ANISOU 2637  C   ILE A 423    14047  17191  11506    573   -652    800       C  
ATOM   2638  O   ILE A 423     -39.967  31.278  12.652  1.00113.79           O  
ANISOU 2638  O   ILE A 423    14176  17416  11644    784   -678    919       O  
ATOM   2639  CB  ILE A 423     -43.005  32.232  11.529  1.00107.24           C  
ANISOU 2639  CB  ILE A 423    13753  16074  10917    454   -457    696       C  
ATOM   2640  CG1 ILE A 423     -43.380  31.080  12.486  1.00108.38           C  
ANISOU 2640  CG1 ILE A 423    14027  16153  11000    604   -454    814       C  
ATOM   2641  CG2 ILE A 423     -43.980  32.323  10.335  1.00106.61           C  
ANISOU 2641  CG2 ILE A 423    13776  15792  10939    386   -332    614       C  
ATOM   2642  CD1 ILE A 423     -44.303  31.481  13.611  1.00115.62           C  
ANISOU 2642  CD1 ILE A 423    15074  17054  11802    502   -484    801       C  
ATOM   2643  N   PRO A 424     -40.241  33.522  12.752  1.00110.01           N  
ANISOU 2643  N   PRO A 424    13656  17022  11122    377   -760    726       N  
ATOM   2644  CA  PRO A 424     -39.277  33.645  13.862  1.00112.37           C  
ANISOU 2644  CA  PRO A 424    13811  17583  11300    395   -922    777       C  
ATOM   2645  C   PRO A 424     -39.627  32.848  15.110  1.00118.37           C  
ANISOU 2645  C   PRO A 424    14697  18345  11934    536   -973    879       C  
ATOM   2646  O   PRO A 424     -40.804  32.629  15.400  1.00116.67           O  
ANISOU 2646  O   PRO A 424    14700  17934  11694    524   -901    871       O  
ATOM   2647  CB  PRO A 424     -39.255  35.148  14.154  1.00113.95           C  
ANISOU 2647  CB  PRO A 424    13984  17858  11454    119  -1010    644       C  
ATOM   2648  CG  PRO A 424     -40.517  35.666  13.588  1.00116.04           C  
ANISOU 2648  CG  PRO A 424    14448  17859  11782      4   -897    546       C  
ATOM   2649  CD  PRO A 424     -40.763  34.846  12.367  1.00110.35           C  
ANISOU 2649  CD  PRO A 424    13747  16992  11191    132   -750    591       C  
ATOM   2650  N   GLN A 425     -38.574  32.396  15.823  1.00118.46           N  
ANISOU 2650  N   GLN A 425    14554  18596  11859    673  -1098    986       N  
ATOM   2651  CA  GLN A 425     -38.572  31.614  17.066  1.00120.39           C  
ANISOU 2651  CA  GLN A 425    14875  18912  11958    833  -1178   1121       C  
ATOM   2652  C   GLN A 425     -39.279  30.242  16.951  1.00124.22           C  
ANISOU 2652  C   GLN A 425    15559  19149  12491   1047  -1051   1250       C  
ATOM   2653  O   GLN A 425     -39.558  29.618  17.976  1.00124.63           O  
ANISOU 2653  O   GLN A 425    15736  19200  12420   1149  -1088   1370       O  
ATOM   2654  CB  GLN A 425     -39.113  32.438  18.252  1.00122.13           C  
ANISOU 2654  CB  GLN A 425    15204  19198  12003    658  -1272   1047       C  
ATOM   2655  CG  GLN A 425     -38.038  33.264  18.956  1.00147.24           C  
ANISOU 2655  CG  GLN A 425    18179  22706  15059    549  -1471   1000       C  
ATOM   2656  CD  GLN A 425     -38.117  34.739  18.638  1.00172.04           C  
ANISOU 2656  CD  GLN A 425    21288  25848  18232    252  -1496    799       C  
ATOM   2657  OE1 GLN A 425     -39.040  35.445  19.064  1.00167.36           O  
ANISOU 2657  OE1 GLN A 425    20879  25136  17576    103  -1477    682       O  
ATOM   2658  NE2 GLN A 425     -37.128  35.246  17.913  1.00166.78           N  
ANISOU 2658  NE2 GLN A 425    20388  25320  17660    162  -1537    758       N  
ATOM   2659  N   ALA A 426     -39.494  29.740  15.718  1.00120.29           N  
ANISOU 2659  N   ALA A 426    15090  18452  12163   1114   -906   1233       N  
ATOM   2660  CA  ALA A 426     -40.125  28.436  15.489  1.00120.34           C  
ANISOU 2660  CA  ALA A 426    15292  18197  12234   1293   -785   1335       C  
ATOM   2661  C   ALA A 426     -39.168  27.261  15.741  1.00127.66           C  
ANISOU 2661  C   ALA A 426    16153  19194  13157   1600   -828   1509       C  
ATOM   2662  O   ALA A 426     -39.625  26.136  15.959  1.00128.00           O  
ANISOU 2662  O   ALA A 426    16389  19031  13213   1759   -764   1632       O  
ATOM   2663  CB  ALA A 426     -40.695  28.360  14.084  1.00119.07           C  
ANISOU 2663  CB  ALA A 426    15193  17809  12239   1243   -628   1231       C  
ATOM   2664  N   GLY A 427     -37.863  27.535  15.718  1.00126.39           N  
ANISOU 2664  N   GLY A 427    15721  19321  12980   1679   -937   1524       N  
ATOM   2665  CA  GLY A 427     -36.814  26.543  15.943  1.00129.10           C  
ANISOU 2665  CA  GLY A 427    15947  19787  13317   1996   -996   1684       C  
ATOM   2666  C   GLY A 427     -36.801  25.991  17.353  1.00134.71           C  
ANISOU 2666  C   GLY A 427    16750  20570  13863   2126  -1114   1862       C  
ATOM   2667  O   GLY A 427     -36.780  24.781  17.554  1.00135.53           O  
ANISOU 2667  O   GLY A 427    16983  20531  13982   2388  -1083   2026       O  
ATOM   2668  N   LEU A 428     -36.849  26.885  18.328  1.00131.65           N  
ANISOU 2668  N   LEU A 428    16318  20393  13310   1941  -1248   1829       N  
ATOM   2669  CA  LEU A 428     -36.862  26.652  19.767  1.00133.63           C  
ANISOU 2669  CA  LEU A 428    16641  20777  13354   2012  -1380   1975       C  
ATOM   2670  C   LEU A 428     -38.167  25.947  20.229  1.00137.33           C  
ANISOU 2670  C   LEU A 428    17459  20941  13781   2005  -1266   2061       C  
ATOM   2671  O   LEU A 428     -38.131  25.131  21.155  1.00139.03           O  
ANISOU 2671  O   LEU A 428    17787  21165  13872   2179  -1319   2259       O  
ATOM   2672  CB  LEU A 428     -36.753  28.083  20.325  1.00133.54           C  
ANISOU 2672  CB  LEU A 428    16480  21057  13201   1747  -1529   1835       C  
ATOM   2673  CG  LEU A 428     -36.754  28.354  21.784  1.00140.10           C  
ANISOU 2673  CG  LEU A 428    17358  22093  13781   1709  -1684   1897       C  
ATOM   2674  CD1 LEU A 428     -35.348  28.614  22.270  1.00143.01           C  
ANISOU 2674  CD1 LEU A 428    17414  22881  14041   1750  -1905   1916       C  
ATOM   2675  CD2 LEU A 428     -37.581  29.581  22.077  1.00140.99           C  
ANISOU 2675  CD2 LEU A 428    17603  22153  13815   1395  -1661   1711       C  
ATOM   2676  N   VAL A 429     -39.309  26.273  19.583  1.00131.32           N  
ANISOU 2676  N   VAL A 429    16855  19920  13123   1807  -1111   1924       N  
ATOM   2677  CA  VAL A 429     -40.621  25.694  19.909  1.00130.44           C  
ANISOU 2677  CA  VAL A 429    17041  19532  12990   1760   -986   1986       C  
ATOM   2678  C   VAL A 429     -40.686  24.214  19.475  1.00136.27           C  
ANISOU 2678  C   VAL A 429    17934  19991  13853   1999   -881   2146       C  
ATOM   2679  O   VAL A 429     -41.339  23.416  20.148  1.00136.78           O  
ANISOU 2679  O   VAL A 429    18223  19896  13850   2048   -834   2301       O  
ATOM   2680  CB  VAL A 429     -41.806  26.557  19.375  1.00131.17           C  
ANISOU 2680  CB  VAL A 429    17220  19474  13145   1477   -869   1786       C  
ATOM   2681  CG1 VAL A 429     -43.158  25.915  19.660  1.00130.38           C  
ANISOU 2681  CG1 VAL A 429    17390  19098  13049   1430   -725   1852       C  
ATOM   2682  CG2 VAL A 429     -41.763  27.970  19.943  1.00130.45           C  
ANISOU 2682  CG2 VAL A 429    17035  19619  12912   1263   -974   1644       C  
ATOM   2683  N   THR A 430     -39.977  23.848  18.386  1.00133.75           N  
ANISOU 2683  N   THR A 430    17501  19614  13704   2148   -841   2110       N  
ATOM   2684  CA  THR A 430     -39.929  22.471  17.868  1.00135.19           C  
ANISOU 2684  CA  THR A 430    17831  19517  14018   2394   -741   2229       C  
ATOM   2685  C   THR A 430     -38.833  21.628  18.543  1.00143.06           C  
ANISOU 2685  C   THR A 430    18769  20641  14947   2730   -856   2448       C  
ATOM   2686  O   THR A 430     -38.733  20.426  18.266  1.00144.32           O  
ANISOU 2686  O   THR A 430    19075  20557  15204   2973   -787   2570       O  
ATOM   2687  CB  THR A 430     -39.843  22.430  16.328  1.00142.61           C  
ANISOU 2687  CB  THR A 430    18714  20308  15163   2400   -620   2066       C  
ATOM   2688  OG1 THR A 430     -39.006  23.485  15.855  1.00141.57           O  
ANISOU 2688  OG1 THR A 430    18284  20469  15037   2328   -690   1930       O  
ATOM   2689  CG2 THR A 430     -41.210  22.503  15.665  1.00139.37           C  
ANISOU 2689  CG2 THR A 430    18503  19606  14844   2171   -467   1939       C  
ATOM   2690  N   MET A 431     -38.041  22.244  19.453  1.00141.33           N  
ANISOU 2690  N   MET A 431    18346  20796  14555   2747  -1038   2499       N  
ATOM   2691  CA  MET A 431     -37.002  21.553  20.226  1.00145.03           C  
ANISOU 2691  CA  MET A 431    18730  21450  14924   3062  -1180   2719       C  
ATOM   2692  C   MET A 431     -37.660  20.571  21.213  1.00151.88           C  
ANISOU 2692  C   MET A 431    19911  22112  15686   3164  -1162   2956       C  
ATOM   2693  O   MET A 431     -37.024  19.605  21.638  1.00154.61           O  
ANISOU 2693  O   MET A 431    20294  22450  16002   3482  -1223   3177       O  
ATOM   2694  CB  MET A 431     -36.108  22.555  20.970  1.00148.29           C  
ANISOU 2694  CB  MET A 431    18848  22333  15161   2995  -1390   2690       C  
ATOM   2695  CG  MET A 431     -34.866  22.945  20.213  1.00152.44           C  
ANISOU 2695  CG  MET A 431    19019  23121  15780   3080  -1452   2594       C  
ATOM   2696  SD  MET A 431     -33.464  23.285  21.293  1.00160.13           S  
ANISOU 2696  SD  MET A 431    19660  24632  16550   3221  -1731   2712       S  
ATOM   2697  CE  MET A 431     -32.964  21.630  21.677  1.00160.62           C  
ANISOU 2697  CE  MET A 431    19836  24578  16616   3718  -1748   3021       C  
ATOM   2698  N   VAL A 432     -38.956  20.813  21.539  1.00147.42           N  
ANISOU 2698  N   VAL A 432    19569  21376  15067   2897  -1068   2915       N  
ATOM   2699  CA  VAL A 432     -39.814  19.988  22.405  1.00148.72           C  
ANISOU 2699  CA  VAL A 432    20046  21328  15133   2909  -1011   3122       C  
ATOM   2700  C   VAL A 432     -39.845  18.546  21.865  1.00153.52           C  
ANISOU 2700  C   VAL A 432    20868  21547  15914   3155   -897   3271       C  
ATOM   2701  O   VAL A 432     -39.720  17.610  22.647  1.00156.24           O  
ANISOU 2701  O   VAL A 432    21384  21806  16174   3358   -930   3534       O  
ATOM   2702  CB  VAL A 432     -41.237  20.610  22.548  1.00150.38           C  
ANISOU 2702  CB  VAL A 432    20405  21430  15300   2553   -895   2996       C  
ATOM   2703  CG1 VAL A 432     -42.183  19.704  23.341  1.00151.79           C  
ANISOU 2703  CG1 VAL A 432    20902  21379  15394   2540   -804   3213       C  
ATOM   2704  CG2 VAL A 432     -41.171  21.999  23.181  1.00149.15           C  
ANISOU 2704  CG2 VAL A 432    20071  21638  14960   2344  -1013   2852       C  
ATOM   2705  N   ILE A 433     -39.941  18.385  20.530  1.00147.63           N  
ANISOU 2705  N   ILE A 433    20116  20575  15401   3147   -772   3104       N  
ATOM   2706  CA  ILE A 433     -39.935  17.096  19.831  1.00148.58           C  
ANISOU 2706  CA  ILE A 433    20436  20310  15707   3369   -657   3182       C  
ATOM   2707  C   ILE A 433     -38.586  16.372  19.999  1.00154.78           C  
ANISOU 2707  C   ILE A 433    21120  21193  16494   3797   -765   3355       C  
ATOM   2708  O   ILE A 433     -38.578  15.212  20.417  1.00157.41           O  
ANISOU 2708  O   ILE A 433    21692  21281  16835   4026   -748   3585       O  
ATOM   2709  CB  ILE A 433     -40.342  17.291  18.333  1.00149.13           C  
ANISOU 2709  CB  ILE A 433    20491  20179  15992   3230   -510   2917       C  
ATOM   2710  CG1 ILE A 433     -41.838  17.622  18.202  1.00147.32           C  
ANISOU 2710  CG1 ILE A 433    20442  19753  15780   2863   -385   2807       C  
ATOM   2711  CG2 ILE A 433     -39.979  16.094  17.447  1.00151.36           C  
ANISOU 2711  CG2 ILE A 433    20907  20138  16466   3511   -417   2940       C  
ATOM   2712  CD1 ILE A 433     -42.120  18.943  17.524  1.00154.71           C  
ANISOU 2712  CD1 ILE A 433    21174  20941  16668   2559   -403   2579       C  
ATOM   2713  N   VAL A 434     -37.461  17.055  19.681  1.00150.13           N  
ANISOU 2713  N   VAL A 434    20178  20964  15900   3901   -874   3252       N  
ATOM   2714  CA  VAL A 434     -36.114  16.478  19.728  1.00152.66           C  
ANISOU 2714  CA  VAL A 434    20330  21443  16232   4315   -978   3387       C  
ATOM   2715  C   VAL A 434     -35.633  16.198  21.191  1.00157.51           C  
ANISOU 2715  C   VAL A 434    20945  22279  16623   4499  -1160   3673       C  
ATOM   2716  O   VAL A 434     -34.926  15.211  21.398  1.00160.37           O  
ANISOU 2716  O   VAL A 434    21352  22579  17004   4888  -1206   3879       O  
ATOM   2717  CB  VAL A 434     -35.096  17.298  18.876  1.00155.89           C  
ANISOU 2717  CB  VAL A 434    20336  22188  16708   4341  -1022   3186       C  
ATOM   2718  CG1 VAL A 434     -34.670  18.603  19.551  1.00154.86           C  
ANISOU 2718  CG1 VAL A 434    19902  22539  16398   4131  -1195   3125       C  
ATOM   2719  CG2 VAL A 434     -33.885  16.458  18.478  1.00159.17           C  
ANISOU 2719  CG2 VAL A 434    20615  22646  17215   4796  -1045   3281       C  
ATOM   2720  N   LEU A 435     -36.049  17.018  22.186  1.00151.49           N  
ANISOU 2720  N   LEU A 435    20157  21758  15646   4239  -1258   3686       N  
ATOM   2721  CA  LEU A 435     -35.659  16.808  23.588  1.00153.48           C  
ANISOU 2721  CA  LEU A 435    20419  22244  15651   4386  -1434   3946       C  
ATOM   2722  C   LEU A 435     -36.381  15.635  24.229  1.00158.12           C  
ANISOU 2722  C   LEU A 435    21411  22468  16199   4494  -1358   4218       C  
ATOM   2723  O   LEU A 435     -35.790  14.928  25.044  1.00161.69           O  
ANISOU 2723  O   LEU A 435    21912  22993  16530   4797  -1477   4496       O  
ATOM   2724  CB  LEU A 435     -35.831  18.073  24.446  1.00151.97           C  
ANISOU 2724  CB  LEU A 435    20076  22441  15224   4078  -1564   3852       C  
ATOM   2725  CG  LEU A 435     -34.847  19.225  24.210  1.00155.76           C  
ANISOU 2725  CG  LEU A 435    20136  23371  15675   4002  -1711   3656       C  
ATOM   2726  CD1 LEU A 435     -35.015  20.289  25.265  1.00155.46           C  
ANISOU 2726  CD1 LEU A 435    20018  23676  15375   3739  -1856   3601       C  
ATOM   2727  CD2 LEU A 435     -33.394  18.747  24.189  1.00161.53           C  
ANISOU 2727  CD2 LEU A 435    20601  24354  16419   4394  -1857   3787       C  
ATOM   2728  N   THR A 436     -37.654  15.431  23.865  1.00151.40           N  
ANISOU 2728  N   THR A 436    20843  21235  15446   4241  -1166   4149       N  
ATOM   2729  CA  THR A 436     -38.483  14.344  24.377  1.00152.72           C  
ANISOU 2729  CA  THR A 436    21411  21019  15598   4270  -1063   4392       C  
ATOM   2730  C   THR A 436     -38.021  12.978  23.888  1.00160.40           C  
ANISOU 2730  C   THR A 436    22565  21624  16754   4646  -1007   4553       C  
ATOM   2731  O   THR A 436     -37.875  12.066  24.703  1.00163.93           O  
ANISOU 2731  O   THR A 436    23223  21954  17109   4877  -1053   4866       O  
ATOM   2732  CB  THR A 436     -39.957  14.576  24.081  1.00154.51           C  
ANISOU 2732  CB  THR A 436    21842  20982  15881   3870   -878   4254       C  
ATOM   2733  OG1 THR A 436     -40.119  14.976  22.728  1.00151.37           O  
ANISOU 2733  OG1 THR A 436    21335  20472  15706   3733   -771   3953       O  
ATOM   2734  CG2 THR A 436     -40.592  15.546  25.045  1.00150.75           C  
ANISOU 2734  CG2 THR A 436    21330  20793  15153   3572   -925   4238       C  
ATOM   2735  N   ALA A 437     -37.770  12.849  22.567  1.00156.19           N  
ANISOU 2735  N   ALA A 437    21962  20915  16470   4717   -909   4343       N  
ATOM   2736  CA  ALA A 437     -37.335  11.621  21.889  1.00159.07           C  
ANISOU 2736  CA  ALA A 437    22496  20906  17037   5072   -833   4423       C  
ATOM   2737  C   ALA A 437     -36.118  10.928  22.526  1.00168.68           C  
ANISOU 2737  C   ALA A 437    23652  22261  18180   5562   -987   4698       C  
ATOM   2738  O   ALA A 437     -36.151   9.706  22.724  1.00171.77           O  
ANISOU 2738  O   ALA A 437    24356  22274  18633   5823   -943   4930       O  
ATOM   2739  CB  ALA A 437     -37.072  11.903  20.423  1.00157.56           C  
ANISOU 2739  CB  ALA A 437    22136  20667  17064   5066   -735   4111       C  
ATOM   2740  N   VAL A 438     -35.065  11.705  22.855  1.00166.08           N  
ANISOU 2740  N   VAL A 438    22923  22463  17717   5680  -1173   4678       N  
ATOM   2741  CA  VAL A 438     -33.849  11.182  23.483  1.00170.51           C  
ANISOU 2741  CA  VAL A 438    23353  23245  18187   6145  -1348   4929       C  
ATOM   2742  C   VAL A 438     -34.065  10.820  24.953  1.00177.84           C  
ANISOU 2742  C   VAL A 438    24473  24237  18862   6193  -1471   5270       C  
ATOM   2743  O   VAL A 438     -33.624   9.758  25.405  1.00181.56           O  
ANISOU 2743  O   VAL A 438    25117  24548  19319   6585  -1521   5567       O  
ATOM   2744  CB  VAL A 438     -32.583  12.056  23.319  1.00174.45           C  
ANISOU 2744  CB  VAL A 438    23336  24305  18642   6271  -1509   4797       C  
ATOM   2745  CG1 VAL A 438     -31.455  11.242  22.719  1.00176.99           C  
ANISOU 2745  CG1 VAL A 438    23550  24541  19156   6733  -1478   4800       C  
ATOM   2746  CG2 VAL A 438     -32.836  13.349  22.565  1.00169.65           C  
ANISOU 2746  CG2 VAL A 438    22470  23946  18044   5836  -1479   4459       C  
ATOM   2747  N   GLY A 439     -34.743  11.708  25.676  1.00172.81           N  
ANISOU 2747  N   GLY A 439    23814  23824  18023   5807  -1511   5226       N  
ATOM   2748  CA  GLY A 439     -35.028  11.548  27.096  1.00175.22           C  
ANISOU 2748  CA  GLY A 439    24282  24249  18044   5789  -1618   5516       C  
ATOM   2749  C   GLY A 439     -34.465  12.671  27.945  1.00179.54           C  
ANISOU 2749  C   GLY A 439    24487  25416  18314   5686  -1841   5474       C  
ATOM   2750  O   GLY A 439     -34.162  12.464  29.124  1.00182.57           O  
ANISOU 2750  O   GLY A 439    24905  26025  18438   5830  -2002   5743       O  
ATOM   2751  N   LEU A 440     -34.319  13.865  27.345  1.00172.68           N  
ANISOU 2751  N   LEU A 440    23297  24820  17492   5429  -1855   5137       N  
ATOM   2752  CA  LEU A 440     -33.816  15.072  28.001  1.00172.14           C  
ANISOU 2752  CA  LEU A 440    22895  25320  17191   5265  -2057   5028       C  
ATOM   2753  C   LEU A 440     -34.991  15.955  28.460  1.00174.35           C  
ANISOU 2753  C   LEU A 440    23299  25621  17324   4794  -1989   4882       C  
ATOM   2754  O   LEU A 440     -36.079  15.832  27.891  1.00171.23           O  
ANISOU 2754  O   LEU A 440    23138  24841  17081   4571  -1773   4778       O  
ATOM   2755  CB  LEU A 440     -32.882  15.848  27.057  1.00170.61           C  
ANISOU 2755  CB  LEU A 440    22276  25405  17144   5270  -2113   4757       C  
ATOM   2756  CG  LEU A 440     -31.470  15.287  26.891  1.00178.90           C  
ANISOU 2756  CG  LEU A 440    23064  26665  18245   5735  -2252   4891       C  
ATOM   2757  CD1 LEU A 440     -30.814  15.842  25.658  1.00177.25           C  
ANISOU 2757  CD1 LEU A 440    22514  26582  18252   5717  -2208   4615       C  
ATOM   2758  CD2 LEU A 440     -30.605  15.603  28.100  1.00184.55           C  
ANISOU 2758  CD2 LEU A 440    23543  27915  18661   5859  -2539   5055       C  
ATOM   2759  N   PRO A 441     -34.831  16.826  29.491  1.00172.81           N  
ANISOU 2759  N   PRO A 441    22963  25865  16831   4642  -2166   4870       N  
ATOM   2760  CA  PRO A 441     -35.977  17.642  29.933  1.00170.48           C  
ANISOU 2760  CA  PRO A 441    22802  25577  16396   4224  -2084   4723       C  
ATOM   2761  C   PRO A 441     -36.242  18.854  29.047  1.00171.27           C  
ANISOU 2761  C   PRO A 441    22705  25729  16640   3891  -2016   4333       C  
ATOM   2762  O   PRO A 441     -35.329  19.638  28.777  1.00170.64           O  
ANISOU 2762  O   PRO A 441    22287  25978  16569   3883  -2158   4168       O  
ATOM   2763  CB  PRO A 441     -35.621  18.034  31.376  1.00174.97           C  
ANISOU 2763  CB  PRO A 441    23309  26592  16578   4231  -2305   4858       C  
ATOM   2764  CG  PRO A 441     -34.199  17.579  31.599  1.00183.07           C  
ANISOU 2764  CG  PRO A 441    24104  27898  17555   4628  -2530   5043       C  
ATOM   2765  CD  PRO A 441     -33.631  17.110  30.302  1.00177.79           C  
ANISOU 2765  CD  PRO A 441    23307  27013  17233   4839  -2448   4975       C  
ATOM   2766  N   THR A 442     -37.505  19.006  28.603  1.00165.39           N  
ANISOU 2766  N   THR A 442    22173  24664  16005   3612  -1800   4198       N  
ATOM   2767  CA  THR A 442     -37.954  20.093  27.726  1.00161.46           C  
ANISOU 2767  CA  THR A 442    21547  24150  15652   3295  -1709   3849       C  
ATOM   2768  C   THR A 442     -37.852  21.477  28.381  1.00165.48           C  
ANISOU 2768  C   THR A 442    21870  25065  15941   3045  -1851   3657       C  
ATOM   2769  O   THR A 442     -37.735  22.471  27.666  1.00162.72           O  
ANISOU 2769  O   THR A 442    21326  24795  15704   2852  -1848   3382       O  
ATOM   2770  CB  THR A 442     -39.360  19.823  27.170  1.00166.81           C  
ANISOU 2770  CB  THR A 442    22499  24398  16482   3087  -1456   3783       C  
ATOM   2771  OG1 THR A 442     -40.229  19.435  28.234  1.00167.77           O  
ANISOU 2771  OG1 THR A 442    22888  24460  16398   3015  -1405   3971       O  
ATOM   2772  CG2 THR A 442     -39.361  18.768  26.077  1.00165.00           C  
ANISOU 2772  CG2 THR A 442    22384  23763  16545   3266  -1313   3836       C  
ATOM   2773  N   ASP A 443     -37.849  21.545  29.727  1.00165.08           N  
ANISOU 2773  N   ASP A 443    21882  25269  15569   3053  -1980   3801       N  
ATOM   2774  CA  ASP A 443     -37.733  22.805  30.469  1.00165.13           C  
ANISOU 2774  CA  ASP A 443    21742  25664  15334   2829  -2130   3617       C  
ATOM   2775  C   ASP A 443     -36.336  23.457  30.347  1.00170.10           C  
ANISOU 2775  C   ASP A 443    21998  26682  15951   2892  -2363   3510       C  
ATOM   2776  O   ASP A 443     -36.166  24.613  30.742  1.00169.58           O  
ANISOU 2776  O   ASP A 443    21786  26912  15735   2670  -2489   3304       O  
ATOM   2777  CB  ASP A 443     -38.159  22.629  31.939  1.00169.80           C  
ANISOU 2777  CB  ASP A 443    22528  26423  15564   2825  -2191   3801       C  
ATOM   2778  CG  ASP A 443     -39.661  22.463  32.136  1.00179.27           C  
ANISOU 2778  CG  ASP A 443    24040  27338  16736   2637  -1958   3815       C  
ATOM   2779  OD1 ASP A 443     -40.414  23.418  31.825  1.00176.55           O  
ANISOU 2779  OD1 ASP A 443    23692  26954  16436   2352  -1857   3540       O  
ATOM   2780  OD2 ASP A 443     -40.080  21.398  32.641  1.00188.03           O  
ANISOU 2780  OD2 ASP A 443    25394  28278  17771   2775  -1880   4107       O  
ATOM   2781  N   ASP A 444     -35.360  22.738  29.758  1.00167.93           N  
ANISOU 2781  N   ASP A 444    21566  26398  15843   3185  -2412   3637       N  
ATOM   2782  CA  ASP A 444     -34.005  23.244  29.525  1.00169.06           C  
ANISOU 2782  CA  ASP A 444    21320  26909  16006   3262  -2612   3553       C  
ATOM   2783  C   ASP A 444     -33.938  24.258  28.363  1.00168.95           C  
ANISOU 2783  C   ASP A 444    21106  26863  16224   3009  -2538   3231       C  
ATOM   2784  O   ASP A 444     -32.943  24.977  28.257  1.00169.52           O  
ANISOU 2784  O   ASP A 444    20848  27276  16286   2961  -2701   3114       O  
ATOM   2785  CB  ASP A 444     -33.018  22.091  29.291  1.00174.00           C  
ANISOU 2785  CB  ASP A 444    21841  27545  16726   3693  -2673   3807       C  
ATOM   2786  CG  ASP A 444     -32.456  21.440  30.540  1.00188.81           C  
ANISOU 2786  CG  ASP A 444    23736  29685  18320   3965  -2876   4107       C  
ATOM   2787  OD1 ASP A 444     -32.122  22.174  31.491  1.00190.82           O  
ANISOU 2787  OD1 ASP A 444    23861  30345  18297   3837  -3081   4062       O  
ATOM   2788  OD2 ASP A 444     -32.260  20.204  30.529  1.00197.21           O  
ANISOU 2788  OD2 ASP A 444    24931  30558  19442   4319  -2842   4385       O  
ATOM   2789  N   ILE A 445     -35.003  24.332  27.514  1.00161.03           N  
ANISOU 2789  N   ILE A 445    20299  25468  15417   2835  -2299   3097       N  
ATOM   2790  CA  ILE A 445     -35.140  25.268  26.380  1.00157.18           C  
ANISOU 2790  CA  ILE A 445    19684  24895  15141   2584  -2202   2808       C  
ATOM   2791  C   ILE A 445     -34.967  26.731  26.861  1.00160.56           C  
ANISOU 2791  C   ILE A 445    19955  25639  15413   2273  -2348   2579       C  
ATOM   2792  O   ILE A 445     -34.419  27.553  26.128  1.00159.28           O  
ANISOU 2792  O   ILE A 445    19556  25583  15379   2127  -2377   2390       O  
ATOM   2793  CB  ILE A 445     -36.482  25.022  25.602  1.00156.75           C  
ANISOU 2793  CB  ILE A 445    19910  24376  15271   2462  -1935   2737       C  
ATOM   2794  CG1 ILE A 445     -36.426  23.713  24.783  1.00157.28           C  
ANISOU 2794  CG1 ILE A 445    20074  24128  15556   2742  -1797   2894       C  
ATOM   2795  CG2 ILE A 445     -36.884  26.200  24.699  1.00154.08           C  
ANISOU 2795  CG2 ILE A 445    19488  23975  15078   2153  -1851   2436       C  
ATOM   2796  CD1 ILE A 445     -37.790  23.179  24.278  1.00159.71           C  
ANISOU 2796  CD1 ILE A 445    20700  23981  16001   2653  -1557   2886       C  
ATOM   2797  N   THR A 446     -35.387  27.024  28.113  1.00158.13           N  
ANISOU 2797  N   THR A 446    19777  25487  14817   2181  -2446   2604       N  
ATOM   2798  CA  THR A 446     -35.299  28.334  28.785  1.00158.02           C  
ANISOU 2798  CA  THR A 446    19669  25763  14607   1900  -2598   2390       C  
ATOM   2799  C   THR A 446     -33.879  28.916  28.833  1.00163.57           C  
ANISOU 2799  C   THR A 446    19999  26873  15277   1888  -2835   2324       C  
ATOM   2800  O   THR A 446     -33.715  30.138  28.786  1.00162.76           O  
ANISOU 2800  O   THR A 446    19774  26916  15152   1599  -2915   2077       O  
ATOM   2801  CB  THR A 446     -35.890  28.259  30.200  1.00166.77           C  
ANISOU 2801  CB  THR A 446    20990  26996  15378   1888  -2665   2480       C  
ATOM   2802  OG1 THR A 446     -35.245  27.209  30.923  1.00169.23           O  
ANISOU 2802  OG1 THR A 446    21283  27476  15541   2202  -2791   2783       O  
ATOM   2803  CG2 THR A 446     -37.400  28.051  30.198  1.00162.64           C  
ANISOU 2803  CG2 THR A 446    20804  26129  14864   1794  -2430   2473       C  
ATOM   2804  N   LEU A 447     -32.868  28.041  28.936  1.00162.29           N  
ANISOU 2804  N   LEU A 447    19656  26890  15117   2200  -2946   2547       N  
ATOM   2805  CA  LEU A 447     -31.449  28.404  28.984  1.00164.49           C  
ANISOU 2805  CA  LEU A 447    19539  27590  15369   2235  -3173   2526       C  
ATOM   2806  C   LEU A 447     -30.951  29.005  27.661  1.00166.32           C  
ANISOU 2806  C   LEU A 447    19527  27780  15886   2092  -3095   2339       C  
ATOM   2807  O   LEU A 447     -30.169  29.952  27.691  1.00167.06           O  
ANISOU 2807  O   LEU A 447    19346  28183  15946   1882  -3251   2180       O  
ATOM   2808  CB  LEU A 447     -30.598  27.175  29.360  1.00168.05           C  
ANISOU 2808  CB  LEU A 447    19876  28214  15761   2662  -3286   2838       C  
ATOM   2809  CG  LEU A 447     -30.971  26.455  30.666  1.00175.31           C  
ANISOU 2809  CG  LEU A 447    21040  29186  16386   2838  -3369   3077       C  
ATOM   2810  CD1 LEU A 447     -30.477  25.036  30.666  1.00177.89           C  
ANISOU 2810  CD1 LEU A 447    21374  29466  16752   3295  -3377   3409       C  
ATOM   2811  CD2 LEU A 447     -30.441  27.190  31.883  1.00181.65           C  
ANISOU 2811  CD2 LEU A 447    21705  30467  16846   2698  -3653   3019       C  
ATOM   2812  N   ILE A 448     -31.435  28.459  26.513  1.00160.10           N  
ANISOU 2812  N   ILE A 448    18854  26609  15367   2183  -2851   2353       N  
ATOM   2813  CA  ILE A 448     -31.116  28.789  25.103  1.00157.79           C  
ANISOU 2813  CA  ILE A 448    18382  26217  15354   2092  -2726   2209       C  
ATOM   2814  C   ILE A 448     -31.943  29.977  24.544  1.00157.50           C  
ANISOU 2814  C   ILE A 448    18470  25971  15403   1701  -2607   1941       C  
ATOM   2815  O   ILE A 448     -31.692  30.369  23.402  1.00156.03           O  
ANISOU 2815  O   ILE A 448    18145  25712  15425   1597  -2508   1823       O  
ATOM   2816  CB  ILE A 448     -31.394  27.548  24.162  1.00159.97           C  
ANISOU 2816  CB  ILE A 448    18763  26159  15861   2396  -2513   2348       C  
ATOM   2817  CG1 ILE A 448     -30.964  26.181  24.748  1.00163.73           C  
ANISOU 2817  CG1 ILE A 448    19244  26697  16269   2828  -2581   2640       C  
ATOM   2818  CG2 ILE A 448     -30.803  27.737  22.772  1.00159.65           C  
ANISOU 2818  CG2 ILE A 448    18486  26105  16068   2359  -2409   2228       C  
ATOM   2819  CD1 ILE A 448     -31.734  24.963  24.164  1.00170.28           C  
ANISOU 2819  CD1 ILE A 448    20375  27065  17258   3061  -2358   2770       C  
ATOM   2820  N   ILE A 449     -32.973  30.478  25.274  1.00151.63           N  
ANISOU 2820  N   ILE A 449    17996  25112  14505   1511  -2596   1856       N  
ATOM   2821  CA  ILE A 449     -33.891  31.512  24.780  1.00147.70           C  
ANISOU 2821  CA  ILE A 449    17650  24378  14089   1191  -2470   1618       C  
ATOM   2822  C   ILE A 449     -33.200  32.880  24.542  1.00150.97           C  
ANISOU 2822  C   ILE A 449    17832  25007  14524    880  -2590   1395       C  
ATOM   2823  O   ILE A 449     -33.425  33.501  23.497  1.00148.14           O  
ANISOU 2823  O   ILE A 449    17460  24465  14361    705  -2465   1251       O  
ATOM   2824  CB  ILE A 449     -35.150  31.597  25.699  1.00149.96           C  
ANISOU 2824  CB  ILE A 449    18275  24511  14194   1115  -2420   1599       C  
ATOM   2825  CG1 ILE A 449     -36.423  31.836  24.882  1.00146.84           C  
ANISOU 2825  CG1 ILE A 449    18102  23729  13961    956  -2191   1457       C  
ATOM   2826  CG2 ILE A 449     -35.032  32.585  26.875  1.00153.04           C  
ANISOU 2826  CG2 ILE A 449    18655  25194  14299    934  -2622   1487       C  
ATOM   2827  CD1 ILE A 449     -37.683  31.230  25.517  1.00155.09           C  
ANISOU 2827  CD1 ILE A 449    19470  24554  14903   1014  -2061   1540       C  
ATOM   2828  N   ALA A 450     -32.339  33.308  25.486  1.00150.10           N  
ANISOU 2828  N   ALA A 450    17537  25284  14210    813  -2835   1377       N  
ATOM   2829  CA  ALA A 450     -31.640  34.594  25.484  1.00150.76           C  
ANISOU 2829  CA  ALA A 450    17409  25599  14276    491  -2984   1170       C  
ATOM   2830  C   ALA A 450     -30.802  34.875  24.232  1.00153.59           C  
ANISOU 2830  C   ALA A 450    17473  26005  14879    418  -2937   1130       C  
ATOM   2831  O   ALA A 450     -30.905  35.963  23.660  1.00151.96           O  
ANISOU 2831  O   ALA A 450    17257  25702  14777    109  -2897    936       O  
ATOM   2832  CB  ALA A 450     -30.785  34.719  26.737  1.00155.40           C  
ANISOU 2832  CB  ALA A 450    17826  26628  14590    489  -3270   1200       C  
ATOM   2833  N   VAL A 451     -29.996  33.892  23.800  1.00150.76           N  
ANISOU 2833  N   VAL A 451    16887  25785  14609    711  -2930   1319       N  
ATOM   2834  CA  VAL A 451     -29.086  34.032  22.658  1.00150.54           C  
ANISOU 2834  CA  VAL A 451    16541  25869  14789    687  -2882   1305       C  
ATOM   2835  C   VAL A 451     -29.737  33.688  21.302  1.00150.27           C  
ANISOU 2835  C   VAL A 451    16646  25446  15001    754  -2603   1301       C  
ATOM   2836  O   VAL A 451     -29.251  34.159  20.270  1.00149.42           O  
ANISOU 2836  O   VAL A 451    16345  25370  15058    623  -2530   1229       O  
ATOM   2837  CB  VAL A 451     -27.751  33.261  22.861  1.00158.10           C  
ANISOU 2837  CB  VAL A 451    17130  27232  15708    971  -3026   1488       C  
ATOM   2838  CG1 VAL A 451     -26.980  33.775  24.076  1.00161.65           C  
ANISOU 2838  CG1 VAL A 451    17386  28120  15913    859  -3327   1470       C  
ATOM   2839  CG2 VAL A 451     -27.945  31.746  22.924  1.00157.98           C  
ANISOU 2839  CG2 VAL A 451    17238  27075  15711   1432  -2934   1725       C  
ATOM   2840  N   ASP A 452     -30.819  32.875  21.320  1.00144.09           N  
ANISOU 2840  N   ASP A 452    16193  24320  14234    944  -2452   1382       N  
ATOM   2841  CA  ASP A 452     -31.576  32.367  20.168  1.00140.67           C  
ANISOU 2841  CA  ASP A 452    15937  23506  14005   1040  -2199   1390       C  
ATOM   2842  C   ASP A 452     -31.784  33.347  19.014  1.00140.73           C  
ANISOU 2842  C   ASP A 452    15918  23370  14182    762  -2074   1215       C  
ATOM   2843  O   ASP A 452     -31.532  32.970  17.871  1.00139.70           O  
ANISOU 2843  O   ASP A 452    15687  23172  14222    866  -1935   1241       O  
ATOM   2844  CB  ASP A 452     -32.943  31.825  20.620  1.00140.84           C  
ANISOU 2844  CB  ASP A 452    16353  23190  13969   1112  -2093   1430       C  
ATOM   2845  CG  ASP A 452     -33.686  31.025  19.564  1.00150.60           C  
ANISOU 2845  CG  ASP A 452    17767  24067  15388   1287  -1862   1488       C  
ATOM   2846  OD1 ASP A 452     -33.731  29.790  19.689  1.00153.10           O  
ANISOU 2846  OD1 ASP A 452    18052  24378  15743   1606  -1835   1657       O  
ATOM   2847  OD2 ASP A 452     -34.280  31.644  18.648  1.00153.19           O  
ANISOU 2847  OD2 ASP A 452    18319  24098  15788   1127  -1720   1377       O  
ATOM   2848  N   TRP A 453     -32.286  34.572  19.302  1.00134.89           N  
ANISOU 2848  N   TRP A 453    15290  22570  13390    426  -2116   1040       N  
ATOM   2849  CA  TRP A 453     -32.619  35.597  18.304  1.00132.00           C  
ANISOU 2849  CA  TRP A 453    14955  22029  13169    148  -2005    880       C  
ATOM   2850  C   TRP A 453     -31.537  35.801  17.228  1.00135.87           C  
ANISOU 2850  C   TRP A 453    15120  22701  13802     98  -1975    886       C  
ATOM   2851  O   TRP A 453     -31.881  35.919  16.056  1.00133.87           O  
ANISOU 2851  O   TRP A 453    14915  22244  13704     56  -1801    850       O  
ATOM   2852  CB  TRP A 453     -33.005  36.939  18.975  1.00130.69           C  
ANISOU 2852  CB  TRP A 453    14912  21843  12901   -192  -2108    696       C  
ATOM   2853  CG  TRP A 453     -31.835  37.753  19.439  1.00134.35           C  
ANISOU 2853  CG  TRP A 453    15102  22660  13285   -410  -2316    628       C  
ATOM   2854  CD1 TRP A 453     -31.208  37.671  20.647  1.00140.42           C  
ANISOU 2854  CD1 TRP A 453    15758  23742  13854   -387  -2534    654       C  
ATOM   2855  CD2 TRP A 453     -31.089  38.699  18.661  1.00135.15           C  
ANISOU 2855  CD2 TRP A 453    14987  22862  13501   -685  -2329    537       C  
ATOM   2856  NE1 TRP A 453     -30.120  38.512  20.673  1.00142.28           N  
ANISOU 2856  NE1 TRP A 453    15709  24271  14078   -641  -2690    571       N  
ATOM   2857  CE2 TRP A 453     -30.008  39.136  19.457  1.00142.35           C  
ANISOU 2857  CE2 TRP A 453    15646  24154  14285   -831  -2562    505       C  
ATOM   2858  CE3 TRP A 453     -31.196  39.179  17.344  1.00134.56           C  
ANISOU 2858  CE3 TRP A 453    14898  22610  13619   -822  -2166    495       C  
ATOM   2859  CZ2 TRP A 453     -29.083  40.079  19.006  1.00143.32           C  
ANISOU 2859  CZ2 TRP A 453    15517  24461  14477  -1143  -2632    420       C  
ATOM   2860  CZ3 TRP A 453     -30.269  40.102  16.893  1.00137.75           C  
ANISOU 2860  CZ3 TRP A 453    15055  23199  14085  -1111  -2227    430       C  
ATOM   2861  CH2 TRP A 453     -29.218  40.528  17.714  1.00141.72           C  
ANISOU 2861  CH2 TRP A 453    15310  24067  14471  -1274  -2454    395       C  
ATOM   2862  N   LEU A 454     -30.248  35.850  17.631  1.00134.62           N  
ANISOU 2862  N   LEU A 454    14625  22946  13579     97  -2144    931       N  
ATOM   2863  CA  LEU A 454     -29.094  36.074  16.748  1.00135.55           C  
ANISOU 2863  CA  LEU A 454    14376  23319  13807     36  -2132    944       C  
ATOM   2864  C   LEU A 454     -28.813  34.842  15.895  1.00137.39           C  
ANISOU 2864  C   LEU A 454    14516  23531  14155    405  -1976   1085       C  
ATOM   2865  O   LEU A 454     -28.496  34.979  14.711  1.00136.69           O  
ANISOU 2865  O   LEU A 454    14296  23434  14206    365  -1833   1066       O  
ATOM   2866  CB  LEU A 454     -27.856  36.441  17.586  1.00139.54           C  
ANISOU 2866  CB  LEU A 454    14542  24292  14186    -53  -2380    957       C  
ATOM   2867  CG  LEU A 454     -26.889  37.482  17.034  1.00146.22           C  
ANISOU 2867  CG  LEU A 454    15120  25371  15064   -451  -2469    839       C  
ATOM   2868  CD1 LEU A 454     -26.247  38.229  18.165  1.00149.49           C  
ANISOU 2868  CD1 LEU A 454    15397  26112  15291   -611  -2748    790       C  
ATOM   2869  CD2 LEU A 454     -25.800  36.862  16.220  1.00150.60           C  
ANISOU 2869  CD2 LEU A 454    15276  26200  15745   -380  -2396    922       C  
ATOM   2870  N   LEU A 455     -28.946  33.639  16.497  1.00132.77           N  
ANISOU 2870  N   LEU A 455    14019  22926  13503    763  -1998   1225       N  
ATOM   2871  CA  LEU A 455     -28.756  32.357  15.815  1.00131.88           C  
ANISOU 2871  CA  LEU A 455    13871  22746  13489   1150  -1858   1355       C  
ATOM   2872  C   LEU A 455     -29.895  32.103  14.821  1.00130.69           C  
ANISOU 2872  C   LEU A 455    14030  22155  13470   1164  -1621   1302       C  
ATOM   2873  O   LEU A 455     -29.665  31.527  13.757  1.00130.24           O  
ANISOU 2873  O   LEU A 455    13906  22043  13538   1339  -1464   1327       O  
ATOM   2874  CB  LEU A 455     -28.614  31.199  16.823  1.00133.60           C  
ANISOU 2874  CB  LEU A 455    14131  23036  13595   1511  -1963   1529       C  
ATOM   2875  CG  LEU A 455     -27.339  31.211  17.687  1.00141.92           C  
ANISOU 2875  CG  LEU A 455    14822  24579  14522   1589  -2199   1615       C  
ATOM   2876  CD1 LEU A 455     -27.453  30.249  18.846  1.00143.66           C  
ANISOU 2876  CD1 LEU A 455    15170  24822  14591   1889  -2321   1784       C  
ATOM   2877  CD2 LEU A 455     -26.097  30.888  16.874  1.00146.50           C  
ANISOU 2877  CD2 LEU A 455    15000  25456  15209   1769  -2161   1671       C  
ATOM   2878  N   ASP A 456     -31.104  32.595  15.151  1.00123.12           N  
ANISOU 2878  N   ASP A 456    13395  20908  12475    970  -1599   1216       N  
ATOM   2879  CA  ASP A 456     -32.305  32.525  14.323  1.00119.09           C  
ANISOU 2879  CA  ASP A 456    13181  19999  12070    929  -1403   1150       C  
ATOM   2880  C   ASP A 456     -32.084  33.334  13.036  1.00120.81           C  
ANISOU 2880  C   ASP A 456    13278  20213  12412    721  -1291   1045       C  
ATOM   2881  O   ASP A 456     -32.378  32.823  11.956  1.00119.71           O  
ANISOU 2881  O   ASP A 456    13206  19897  12384    838  -1116   1045       O  
ATOM   2882  CB  ASP A 456     -33.514  33.062  15.111  1.00118.99           C  
ANISOU 2882  CB  ASP A 456    13475  19767  11968    745  -1435   1075       C  
ATOM   2883  CG  ASP A 456     -34.888  32.589  14.669  1.00124.09           C  
ANISOU 2883  CG  ASP A 456    14452  20017  12681    798  -1264   1058       C  
ATOM   2884  OD1 ASP A 456     -35.005  32.058  13.542  1.00122.14           O  
ANISOU 2884  OD1 ASP A 456    14221  19622  12565    908  -1109   1065       O  
ATOM   2885  OD2 ASP A 456     -35.861  32.844  15.403  1.00130.02           O  
ANISOU 2885  OD2 ASP A 456    15433  20620  13349    702  -1284   1021       O  
ATOM   2886  N   ARG A 457     -31.502  34.560  13.146  1.00116.48           N  
ANISOU 2886  N   ARG A 457    12547  19874  11839    413  -1394    963       N  
ATOM   2887  CA  ARG A 457     -31.183  35.442  12.012  1.00115.01           C  
ANISOU 2887  CA  ARG A 457    12230  19714  11754    176  -1303    886       C  
ATOM   2888  C   ARG A 457     -30.252  34.752  11.026  1.00119.55           C  
ANISOU 2888  C   ARG A 457    12538  20473  12413    384  -1193    962       C  
ATOM   2889  O   ARG A 457     -30.395  34.945   9.821  1.00118.33           O  
ANISOU 2889  O   ARG A 457    12395  20213  12353    323  -1030    926       O  
ATOM   2890  CB  ARG A 457     -30.520  36.759  12.474  1.00115.66           C  
ANISOU 2890  CB  ARG A 457    12133  20027  11787   -181  -1460    808       C  
ATOM   2891  CG  ARG A 457     -31.279  37.609  13.494  1.00121.48           C  
ANISOU 2891  CG  ARG A 457    13108  20623  12426   -409  -1584    702       C  
ATOM   2892  CD  ARG A 457     -32.730  37.783  13.137  1.00124.70           C  
ANISOU 2892  CD  ARG A 457    13887  20615  12879   -443  -1450    633       C  
ATOM   2893  NE  ARG A 457     -33.251  39.100  13.475  1.00131.89           N  
ANISOU 2893  NE  ARG A 457    14958  21391  13762   -766  -1511    493       N  
ATOM   2894  CZ  ARG A 457     -34.280  39.309  14.280  1.00145.74           C  
ANISOU 2894  CZ  ARG A 457    16993  22947  15435   -786  -1544    422       C  
ATOM   2895  NH1 ARG A 457     -34.897  38.285  14.868  1.00132.20           N  
ANISOU 2895  NH1 ARG A 457    15420  21157  13652   -528  -1524    492       N  
ATOM   2896  NH2 ARG A 457     -34.718  40.539  14.507  1.00133.71           N  
ANISOU 2896  NH2 ARG A 457    15616  21291  13897  -1062  -1588    282       N  
ATOM   2897  N   PHE A 458     -29.299  33.952  11.535  1.00118.07           N  
ANISOU 2897  N   PHE A 458    12109  20570  12181    641  -1281   1069       N  
ATOM   2898  CA  PHE A 458     -28.364  33.226  10.685  1.00119.45           C  
ANISOU 2898  CA  PHE A 458    12013  20945  12426    889  -1177   1140       C  
ATOM   2899  C   PHE A 458     -28.977  31.954  10.118  1.00120.85           C  
ANISOU 2899  C   PHE A 458    12414  20838  12667   1241  -1009   1183       C  
ATOM   2900  O   PHE A 458     -28.856  31.725   8.917  1.00120.14           O  
ANISOU 2900  O   PHE A 458    12277  20708  12662   1313   -833   1157       O  
ATOM   2901  CB  PHE A 458     -27.029  32.965  11.392  1.00125.10           C  
ANISOU 2901  CB  PHE A 458    12343  22113  13076   1025  -1341   1234       C  
ATOM   2902  CG  PHE A 458     -26.246  34.222  11.690  1.00128.39           C  
ANISOU 2902  CG  PHE A 458    12479  22852  13451    647  -1488   1178       C  
ATOM   2903  CD1 PHE A 458     -25.859  35.083  10.666  1.00131.54           C  
ANISOU 2903  CD1 PHE A 458    12713  23338  13930    369  -1385   1115       C  
ATOM   2904  CD2 PHE A 458     -25.876  34.536  12.991  1.00132.17           C  
ANISOU 2904  CD2 PHE A 458    12864  23553  13802    559  -1730   1191       C  
ATOM   2905  CE1 PHE A 458     -25.143  36.248  10.944  1.00134.37           C  
ANISOU 2905  CE1 PHE A 458    12828  23968  14259    -12  -1519   1064       C  
ATOM   2906  CE2 PHE A 458     -25.156  35.697  13.265  1.00136.92           C  
ANISOU 2906  CE2 PHE A 458    13218  24440  14365    183  -1874   1121       C  
ATOM   2907  CZ  PHE A 458     -24.798  36.548  12.242  1.00135.19           C  
ANISOU 2907  CZ  PHE A 458    12846  24275  14245   -108  -1766   1058       C  
ATOM   2908  N   ARG A 459     -29.661  31.154  10.961  1.00115.85           N  
ANISOU 2908  N   ARG A 459    12035  20000  11984   1438  -1060   1243       N  
ATOM   2909  CA  ARG A 459     -30.386  29.919  10.613  1.00114.40           C  
ANISOU 2909  CA  ARG A 459    12123  19490  11855   1740   -922   1284       C  
ATOM   2910  C   ARG A 459     -31.342  30.150   9.453  1.00116.04           C  
ANISOU 2910  C   ARG A 459    12555  19384  12151   1602   -735   1170       C  
ATOM   2911  O   ARG A 459     -31.552  29.249   8.640  1.00115.96           O  
ANISOU 2911  O   ARG A 459    12649  19197  12212   1826   -583   1169       O  
ATOM   2912  CB  ARG A 459     -31.355  29.666  11.754  1.00112.65           C  
ANISOU 2912  CB  ARG A 459    12205  19046  11550   1740  -1012   1324       C  
ATOM   2913  CG  ARG A 459     -31.263  28.424  12.520  1.00121.87           C  
ANISOU 2913  CG  ARG A 459    13462  20166  12676   2089  -1058   1472       C  
ATOM   2914  CD  ARG A 459     -32.506  28.394  13.387  1.00125.77           C  
ANISOU 2914  CD  ARG A 459    14303  20389  13096   1984  -1092   1480       C  
ATOM   2915  NE  ARG A 459     -32.261  28.958  14.716  1.00129.62           N  
ANISOU 2915  NE  ARG A 459    14717  21107  13425   1867  -1297   1519       N  
ATOM   2916  CZ  ARG A 459     -33.211  29.274  15.586  1.00138.10           C  
ANISOU 2916  CZ  ARG A 459    16031  22044  14397   1711  -1349   1502       C  
ATOM   2917  NH1 ARG A 459     -34.490  29.101  15.277  1.00118.48           N  
ANISOU 2917  NH1 ARG A 459    13857  19198  11962   1645  -1212   1453       N  
ATOM   2918  NH2 ARG A 459     -32.893  29.770  16.771  1.00128.14           N  
ANISOU 2918  NH2 ARG A 459    14692  21023  12973   1620  -1539   1526       N  
ATOM   2919  N   THR A 460     -32.009  31.329   9.444  1.00110.09           N  
ANISOU 2919  N   THR A 460    11908  18539  11383   1242   -755   1073       N  
ATOM   2920  CA  THR A 460     -32.987  31.703   8.424  1.00106.97           C  
ANISOU 2920  CA  THR A 460    11727  17864  11055   1085   -605    971       C  
ATOM   2921  C   THR A 460     -32.295  31.874   7.079  1.00111.77           C  
ANISOU 2921  C   THR A 460    12131  18608  11728   1078   -471    939       C  
ATOM   2922  O   THR A 460     -32.802  31.358   6.084  1.00110.49           O  
ANISOU 2922  O   THR A 460    12112  18247  11620   1180   -312    899       O  
ATOM   2923  CB  THR A 460     -33.799  32.926   8.876  1.00111.68           C  
ANISOU 2923  CB  THR A 460    12475  18346  11613    743   -678    890       C  
ATOM   2924  OG1 THR A 460     -34.405  32.630  10.130  1.00110.80           O  
ANISOU 2924  OG1 THR A 460    12542  18135  11421    789   -784    924       O  
ATOM   2925  CG2 THR A 460     -34.884  33.310   7.890  1.00108.32           C  
ANISOU 2925  CG2 THR A 460    12274  17634  11248    602   -540    800       C  
ATOM   2926  N   MET A 461     -31.114  32.543   7.065  1.00110.18           N  
ANISOU 2926  N   MET A 461    11588  18764  11511    961   -533    958       N  
ATOM   2927  CA  MET A 461     -30.299  32.772   5.864  1.00111.09           C  
ANISOU 2927  CA  MET A 461    11456  19081  11671    936   -404    945       C  
ATOM   2928  C   MET A 461     -29.910  31.465   5.178  1.00114.44           C  
ANISOU 2928  C   MET A 461    11828  19522  12132   1328   -265    977       C  
ATOM   2929  O   MET A 461     -29.930  31.415   3.953  1.00113.81           O  
ANISOU 2929  O   MET A 461    11747  19408  12086   1342    -94    928       O  
ATOM   2930  CB  MET A 461     -29.042  33.588   6.181  1.00116.37           C  
ANISOU 2930  CB  MET A 461    11740  20164  12312    752   -514    979       C  
ATOM   2931  CG  MET A 461     -29.332  34.973   6.698  1.00119.78           C  
ANISOU 2931  CG  MET A 461    12225  20571  12715    337   -638    924       C  
ATOM   2932  SD  MET A 461     -27.830  35.813   7.242  1.00128.21           S  
ANISOU 2932  SD  MET A 461    12840  22127  13745    112   -799    958       S  
ATOM   2933  CE  MET A 461     -27.274  36.533   5.680  1.00125.60           C  
ANISOU 2933  CE  MET A 461    12311  21929  13481   -108   -608    948       C  
ATOM   2934  N   VAL A 462     -29.589  30.408   5.966  1.00110.95           N  
ANISOU 2934  N   VAL A 462    11365  19116  11676   1653   -336   1058       N  
ATOM   2935  CA  VAL A 462     -29.225  29.067   5.478  1.00111.61           C  
ANISOU 2935  CA  VAL A 462    11434  19174  11799   2073   -219   1091       C  
ATOM   2936  C   VAL A 462     -30.478  28.301   4.972  1.00113.03           C  
ANISOU 2936  C   VAL A 462    12025  18900  12021   2178    -92   1028       C  
ATOM   2937  O   VAL A 462     -30.382  27.535   4.009  1.00112.71           O  
ANISOU 2937  O   VAL A 462    12020  18783  12023   2402     67    985       O  
ATOM   2938  CB  VAL A 462     -28.403  28.260   6.521  1.00117.72           C  
ANISOU 2938  CB  VAL A 462    12039  20145  12542   2389   -352   1218       C  
ATOM   2939  CG1 VAL A 462     -27.797  27.006   5.900  1.00119.78           C  
ANISOU 2939  CG1 VAL A 462    12226  20432  12854   2834   -221   1246       C  
ATOM   2940  CG2 VAL A 462     -27.303  29.117   7.140  1.00119.59           C  
ANISOU 2940  CG2 VAL A 462    11881  20834  12724   2224   -513   1268       C  
ATOM   2941  N   ASN A 463     -31.649  28.534   5.611  1.00107.59           N  
ANISOU 2941  N   ASN A 463    11637  17927  11315   2005   -162   1013       N  
ATOM   2942  CA  ASN A 463     -32.940  27.939   5.237  1.00105.32           C  
ANISOU 2942  CA  ASN A 463    11727  17226  11065   2035    -64    954       C  
ATOM   2943  C   ASN A 463     -33.430  28.479   3.889  1.00108.48           C  
ANISOU 2943  C   ASN A 463    12194  17533  11491   1852     82    833       C  
ATOM   2944  O   ASN A 463     -34.047  27.737   3.124  1.00107.31           O  
ANISOU 2944  O   ASN A 463    12254  17140  11378   1973    208    768       O  
ATOM   2945  CB  ASN A 463     -33.990  28.209   6.316  1.00102.63           C  
ANISOU 2945  CB  ASN A 463    11627  16681  10686   1868   -179    975       C  
ATOM   2946  CG  ASN A 463     -33.792  27.457   7.609  1.00125.77           C  
ANISOU 2946  CG  ASN A 463    14591  19622  13574   2073   -302   1102       C  
ATOM   2947  OD1 ASN A 463     -32.871  26.652   7.778  1.00120.74           O  
ANISOU 2947  OD1 ASN A 463    13807  19127  12943   2373   -318   1189       O  
ATOM   2948  ND2 ASN A 463     -34.658  27.721   8.568  1.00118.92           N  
ANISOU 2948  ND2 ASN A 463    13916  18615  12653   1924   -392   1123       N  
ATOM   2949  N   VAL A 464     -33.159  29.780   3.621  1.00105.33           N  
ANISOU 2949  N   VAL A 464    11627  17325  11068   1552     57    806       N  
ATOM   2950  CA  VAL A 464     -33.506  30.515   2.396  1.00103.98           C  
ANISOU 2950  CA  VAL A 464    11489  17118  10903   1344    176    721       C  
ATOM   2951  C   VAL A 464     -32.516  30.136   1.290  1.00109.44           C  
ANISOU 2951  C   VAL A 464    11958  18028  11597   1513    322    708       C  
ATOM   2952  O   VAL A 464     -32.942  29.734   0.209  1.00108.13           O  
ANISOU 2952  O   VAL A 464    11928  17721  11434   1584    469    631       O  
ATOM   2953  CB  VAL A 464     -33.574  32.055   2.644  1.00107.13           C  
ANISOU 2953  CB  VAL A 464    11818  17610  11277    960     85    717       C  
ATOM   2954  CG1 VAL A 464     -33.695  32.837   1.335  1.00106.43           C  
ANISOU 2954  CG1 VAL A 464    11719  17532  11186    764    209    665       C  
ATOM   2955  CG2 VAL A 464     -34.722  32.414   3.587  1.00104.72           C  
ANISOU 2955  CG2 VAL A 464    11772  17057  10961    813    -27    701       C  
ATOM   2956  N   LEU A 465     -31.201  30.235   1.581  1.00109.00           N  
ANISOU 2956  N   LEU A 465    11552  18332  11530   1586    281    778       N  
ATOM   2957  CA  LEU A 465     -30.086  29.891   0.688  1.00111.88           C  
ANISOU 2957  CA  LEU A 465    11636  18983  11890   1769    417    779       C  
ATOM   2958  C   LEU A 465     -30.255  28.488   0.072  1.00117.22           C  
ANISOU 2958  C   LEU A 465    12469  19480  12589   2152    557    725       C  
ATOM   2959  O   LEU A 465     -29.868  28.278  -1.078  1.00117.73           O  
ANISOU 2959  O   LEU A 465    12448  19648  12635   2252    726    665       O  
ATOM   2960  CB  LEU A 465     -28.761  29.974   1.475  1.00114.90           C  
ANISOU 2960  CB  LEU A 465    11632  19760  12264   1846    306    878       C  
ATOM   2961  CG  LEU A 465     -27.448  29.820   0.712  1.00122.70           C  
ANISOU 2961  CG  LEU A 465    12235  21142  13243   1998    427    896       C  
ATOM   2962  CD1 LEU A 465     -26.975  31.150   0.153  1.00123.40           C  
ANISOU 2962  CD1 LEU A 465    12092  21491  13305   1616    459    901       C  
ATOM   2963  CD2 LEU A 465     -26.384  29.268   1.615  1.00127.15           C  
ANISOU 2963  CD2 LEU A 465    12505  21996  13810   2260    314    992       C  
ATOM   2964  N   GLY A 466     -30.829  27.564   0.850  1.00114.04           N  
ANISOU 2964  N   GLY A 466    12304  18808  12218   2351    488    744       N  
ATOM   2965  CA  GLY A 466     -31.112  26.191   0.446  1.00114.83           C  
ANISOU 2965  CA  GLY A 466    12616  18661  12353   2696    596    693       C  
ATOM   2966  C   GLY A 466     -32.184  26.112  -0.620  1.00117.24           C  
ANISOU 2966  C   GLY A 466    13216  18676  12654   2591    724    560       C  
ATOM   2967  O   GLY A 466     -32.060  25.318  -1.555  1.00118.60           O  
ANISOU 2967  O   GLY A 466    13450  18785  12827   2815    875    471       O  
ATOM   2968  N   ASP A 467     -33.245  26.946  -0.492  1.00110.56           N  
ANISOU 2968  N   ASP A 467    12550  17661  11796   2256    662    538       N  
ATOM   2969  CA  ASP A 467     -34.351  27.026  -1.457  1.00108.10           C  
ANISOU 2969  CA  ASP A 467    12500  17102  11470   2115    755    421       C  
ATOM   2970  C   ASP A 467     -33.873  27.691  -2.747  1.00110.50           C  
ANISOU 2970  C   ASP A 467    12640  17633  11714   2010    886    366       C  
ATOM   2971  O   ASP A 467     -34.302  27.297  -3.835  1.00109.22           O  
ANISOU 2971  O   ASP A 467    12627  17354  11519   2062   1014    256       O  
ATOM   2972  CB  ASP A 467     -35.537  27.838  -0.893  1.00107.35           C  
ANISOU 2972  CB  ASP A 467    12595  16816  11377   1802    644    429       C  
ATOM   2973  CG  ASP A 467     -36.000  27.499   0.509  1.00121.01           C  
ANISOU 2973  CG  ASP A 467    14451  18388  13140   1828    505    505       C  
ATOM   2974  OD1 ASP A 467     -35.675  26.390   0.995  1.00124.26           O  
ANISOU 2974  OD1 ASP A 467    14899  18730  13583   2109    500    548       O  
ATOM   2975  OD2 ASP A 467     -36.721  28.326   1.109  1.00126.05           O  
ANISOU 2975  OD2 ASP A 467    15167  18960  13767   1577    408    523       O  
ATOM   2976  N   ALA A 468     -33.009  28.721  -2.611  1.00107.18           N  
ANISOU 2976  N   ALA A 468    11918  17536  11268   1839    848    444       N  
ATOM   2977  CA  ALA A 468     -32.442  29.475  -3.720  1.00107.78           C  
ANISOU 2977  CA  ALA A 468    11803  17866  11281   1701    968    429       C  
ATOM   2978  C   ALA A 468     -31.552  28.571  -4.560  1.00115.84           C  
ANISOU 2978  C   ALA A 468    12677  19064  12272   2020   1136    380       C  
ATOM   2979  O   ALA A 468     -31.797  28.445  -5.760  1.00116.23           O  
ANISOU 2979  O   ALA A 468    12818  19086  12257   2035   1285    287       O  
ATOM   2980  CB  ALA A 468     -31.671  30.681  -3.210  1.00108.90           C  
ANISOU 2980  CB  ALA A 468    11657  18300  11420   1444    876    534       C  
ATOM   2981  N   LEU A 469     -30.572  27.890  -3.935  1.00115.12           N  
ANISOU 2981  N   LEU A 469    12375  19147  12220   2300   1112    434       N  
ATOM   2982  CA  LEU A 469     -29.679  26.964  -4.641  1.00118.19           C  
ANISOU 2982  CA  LEU A 469    12613  19708  12588   2660   1273    384       C  
ATOM   2983  C   LEU A 469     -30.439  25.736  -5.141  1.00122.65           C  
ANISOU 2983  C   LEU A 469    13527  19913  13163   2920   1364    251       C  
ATOM   2984  O   LEU A 469     -30.135  25.234  -6.225  1.00123.67           O  
ANISOU 2984  O   LEU A 469    13648  20106  13236   3105   1541    145       O  
ATOM   2985  CB  LEU A 469     -28.472  26.563  -3.781  1.00120.99           C  
ANISOU 2985  CB  LEU A 469    12646  20340  12985   2911   1206    487       C  
ATOM   2986  CG  LEU A 469     -27.448  27.669  -3.505  1.00126.92           C  
ANISOU 2986  CG  LEU A 469    12976  21533  13714   2684   1148    597       C  
ATOM   2987  CD1 LEU A 469     -26.700  27.403  -2.230  1.00128.94           C  
ANISOU 2987  CD1 LEU A 469    13011  21963  14018   2841    984    711       C  
ATOM   2988  CD2 LEU A 469     -26.472  27.841  -4.656  1.00132.05           C  
ANISOU 2988  CD2 LEU A 469    13319  22557  14298   2735   1346    572       C  
ATOM   2989  N   GLY A 470     -31.455  25.322  -4.375  1.00118.16           N  
ANISOU 2989  N   GLY A 470    13267  18973  12656   2900   1245    252       N  
ATOM   2990  CA  GLY A 470     -32.349  24.215  -4.700  1.00118.14           C  
ANISOU 2990  CA  GLY A 470    13633  18576  12677   3071   1301    132       C  
ATOM   2991  C   GLY A 470     -33.117  24.440  -5.983  1.00122.49           C  
ANISOU 2991  C   GLY A 470    14369  19020  13151   2910   1417    -11       C  
ATOM   2992  O   GLY A 470     -33.278  23.507  -6.774  1.00123.72           O  
ANISOU 2992  O   GLY A 470    14699  19024  13285   3122   1540   -151       O  
ATOM   2993  N   ALA A 471     -33.571  25.697  -6.206  1.00117.41           N  
ANISOU 2993  N   ALA A 471    13692  18460  12459   2540   1374     21       N  
ATOM   2994  CA  ALA A 471     -34.274  26.123  -7.421  1.00116.07           C  
ANISOU 2994  CA  ALA A 471    13665  18242  12194   2356   1465    -84       C  
ATOM   2995  C   ALA A 471     -33.309  26.027  -8.602  1.00121.39           C  
ANISOU 2995  C   ALA A 471    14144  19211  12766   2504   1656   -146       C  
ATOM   2996  O   ALA A 471     -33.632  25.376  -9.592  1.00121.13           O  
ANISOU 2996  O   ALA A 471    14287  19074  12663   2629   1778   -296       O  
ATOM   2997  CB  ALA A 471     -34.785  27.548  -7.269  1.00114.50           C  
ANISOU 2997  CB  ALA A 471    13437  18094  11975   1963   1370      1       C  
ATOM   2998  N   GLY A 472     -32.107  26.589  -8.436  1.00119.68           N  
ANISOU 2998  N   GLY A 472    13564  19369  12540   2504   1679    -36       N  
ATOM   2999  CA  GLY A 472     -31.036  26.542  -9.427  1.00122.69           C  
ANISOU 2999  CA  GLY A 472    13693  20100  12825   2649   1868    -69       C  
ATOM   3000  C   GLY A 472     -30.618  25.131  -9.806  1.00129.63           C  
ANISOU 3000  C   GLY A 472    14626  20925  13702   3091   1998   -199       C  
ATOM   3001  O   GLY A 472     -30.337  24.861 -10.981  1.00131.31           O  
ANISOU 3001  O   GLY A 472    14827  21266  13800   3213   2183   -315       O  
ATOM   3002  N   ILE A 473     -30.601  24.213  -8.814  1.00126.31           N  
ANISOU 3002  N   ILE A 473    14289  20301  13402   3341   1904   -182       N  
ATOM   3003  CA  ILE A 473     -30.249  22.804  -9.001  1.00128.82           C  
ANISOU 3003  CA  ILE A 473    14705  20494  13748   3788   2005   -294       C  
ATOM   3004  C   ILE A 473     -31.355  22.050  -9.769  1.00132.56           C  
ANISOU 3004  C   ILE A 473    15606  20575  14186   3820   2068   -490       C  
ATOM   3005  O   ILE A 473     -31.046  21.344 -10.731  1.00134.70           O  
ANISOU 3005  O   ILE A 473    15929  20867  14382   4070   2240   -648       O  
ATOM   3006  CB  ILE A 473     -29.859  22.151  -7.642  1.00132.68           C  
ANISOU 3006  CB  ILE A 473    15145  20894  14372   4028   1870   -177       C  
ATOM   3007  CG1 ILE A 473     -28.417  22.542  -7.266  1.00135.68           C  
ANISOU 3007  CG1 ILE A 473    15045  21752  14754   4146   1874    -42       C  
ATOM   3008  CG2 ILE A 473     -30.024  20.624  -7.648  1.00135.25           C  
ANISOU 3008  CG2 ILE A 473    15750  20878  14759   4433   1924   -289       C  
ATOM   3009  CD1 ILE A 473     -28.101  22.566  -5.777  1.00143.32           C  
ANISOU 3009  CD1 ILE A 473    15885  22747  15822   4180   1673    133       C  
ATOM   3010  N   VAL A 474     -32.629  22.221  -9.358  1.00126.39           N  
ANISOU 3010  N   VAL A 474    15116  19458  13449   3561   1933   -489       N  
ATOM   3011  CA  VAL A 474     -33.795  21.574  -9.976  1.00125.52           C  
ANISOU 3011  CA  VAL A 474    15403  18974  13313   3530   1958   -666       C  
ATOM   3012  C   VAL A 474     -34.005  22.067 -11.421  1.00130.39           C  
ANISOU 3012  C   VAL A 474    16038  19745  13760   3385   2090   -795       C  
ATOM   3013  O   VAL A 474     -34.186  21.235 -12.312  1.00132.04           O  
ANISOU 3013  O   VAL A 474    16444  19826  13900   3559   2209   -990       O  
ATOM   3014  CB  VAL A 474     -35.067  21.694  -9.086  1.00126.01           C  
ANISOU 3014  CB  VAL A 474    15717  18692  13468   3279   1777   -609       C  
ATOM   3015  CG1 VAL A 474     -36.338  21.343  -9.853  1.00124.63           C  
ANISOU 3015  CG1 VAL A 474    15892  18216  13245   3140   1793   -783       C  
ATOM   3016  CG2 VAL A 474     -34.943  20.825  -7.834  1.00126.50           C  
ANISOU 3016  CG2 VAL A 474    15856  18533  13674   3494   1684   -521       C  
ATOM   3017  N   GLU A 475     -33.937  23.402 -11.652  1.00125.83           N  
ANISOU 3017  N   GLU A 475    15262  19442  13107   3078   2070   -686       N  
ATOM   3018  CA  GLU A 475     -34.093  24.043 -12.971  1.00125.94           C  
ANISOU 3018  CA  GLU A 475    15268  19641  12943   2911   2184   -758       C  
ATOM   3019  C   GLU A 475     -33.144  23.413 -13.986  1.00134.49           C  
ANISOU 3019  C   GLU A 475    16243  20951  13908   3216   2403   -887       C  
ATOM   3020  O   GLU A 475     -33.567  23.049 -15.085  1.00134.58           O  
ANISOU 3020  O   GLU A 475    16447  20905  13782   3248   2507  -1065       O  
ATOM   3021  CB  GLU A 475     -33.809  25.553 -12.868  1.00125.78           C  
ANISOU 3021  CB  GLU A 475    14991  19911  12887   2588   2138   -572       C  
ATOM   3022  CG  GLU A 475     -34.202  26.363 -14.095  1.00134.56           C  
ANISOU 3022  CG  GLU A 475    16143  21163  13821   2357   2218   -600       C  
ATOM   3023  CD  GLU A 475     -33.437  27.659 -14.301  1.00153.95           C  
ANISOU 3023  CD  GLU A 475    18290  23991  16214   2134   2258   -427       C  
ATOM   3024  OE1 GLU A 475     -32.248  27.729 -13.912  1.00145.72           O  
ANISOU 3024  OE1 GLU A 475    16933  23221  15214   2240   2309   -337       O  
ATOM   3025  OE2 GLU A 475     -34.015  28.590 -14.905  1.00148.82           O  
ANISOU 3025  OE2 GLU A 475    17713  23368  15465   1854   2245   -380       O  
ATOM   3026  N   HIS A 476     -31.865  23.267 -13.588  1.00134.72           N  
ANISOU 3026  N   HIS A 476    15956  21248  13984   3448   2467   -805       N  
ATOM   3027  CA  HIS A 476     -30.796  22.695 -14.390  1.00139.16           C  
ANISOU 3027  CA  HIS A 476    16346  22079  14448   3778   2682   -906       C  
ATOM   3028  C   HIS A 476     -31.051  21.220 -14.711  1.00146.22           C  
ANISOU 3028  C   HIS A 476    17544  22657  15356   4140   2758  -1131       C  
ATOM   3029  O   HIS A 476     -30.852  20.811 -15.854  1.00148.54           O  
ANISOU 3029  O   HIS A 476    17894  23044  15498   4300   2939  -1310       O  
ATOM   3030  CB  HIS A 476     -29.444  22.900 -13.695  1.00142.03           C  
ANISOU 3030  CB  HIS A 476    16281  22797  14887   3932   2697   -744       C  
ATOM   3031  CG  HIS A 476     -28.273  22.528 -14.550  1.00149.74           C  
ANISOU 3031  CG  HIS A 476    16999  24148  15747   4231   2933   -820       C  
ATOM   3032  ND1 HIS A 476     -27.639  23.450 -15.362  1.00152.71           N  
ANISOU 3032  ND1 HIS A 476    17084  24965  15974   4051   3069   -755       N  
ATOM   3033  CD2 HIS A 476     -27.677  21.324 -14.707  1.00155.03           C  
ANISOU 3033  CD2 HIS A 476    17677  24799  16428   4699   3061   -956       C  
ATOM   3034  CE1 HIS A 476     -26.667  22.785 -15.966  1.00156.16           C  
ANISOU 3034  CE1 HIS A 476    17336  25667  16330   4412   3279   -854       C  
ATOM   3035  NE2 HIS A 476     -26.656  21.501 -15.612  1.00158.03           N  
ANISOU 3035  NE2 HIS A 476    17748  25637  16660   4823   3283   -985       N  
ATOM   3036  N   LEU A 477     -31.508  20.438 -13.711  1.00142.48           N  
ANISOU 3036  N   LEU A 477    17280  21801  15055   4257   2620  -1123       N  
ATOM   3037  CA  LEU A 477     -31.824  19.012 -13.835  1.00144.41           C  
ANISOU 3037  CA  LEU A 477    17856  21664  15348   4574   2664  -1318       C  
ATOM   3038  C   LEU A 477     -33.113  18.751 -14.629  1.00148.99           C  
ANISOU 3038  C   LEU A 477    18837  21929  15843   4385   2658  -1518       C  
ATOM   3039  O   LEU A 477     -33.281  17.649 -15.156  1.00151.18           O  
ANISOU 3039  O   LEU A 477    19382  21959  16101   4628   2747  -1736       O  
ATOM   3040  CB  LEU A 477     -31.950  18.379 -12.436  1.00143.60           C  
ANISOU 3040  CB  LEU A 477    17851  21255  15455   4702   2505  -1201       C  
ATOM   3041  CG  LEU A 477     -30.673  17.901 -11.760  1.00150.60           C  
ANISOU 3041  CG  LEU A 477    18467  22321  16432   5093   2535  -1093       C  
ATOM   3042  CD1 LEU A 477     -30.790  18.024 -10.271  1.00148.84           C  
ANISOU 3042  CD1 LEU A 477    18207  21977  16368   5023   2328   -874       C  
ATOM   3043  CD2 LEU A 477     -30.385  16.455 -12.105  1.00156.50           C  
ANISOU 3043  CD2 LEU A 477    19429  22825  17209   5561   2661  -1275       C  
ATOM   3044  N   SER A 478     -34.026  19.744 -14.695  1.00143.41           N  
ANISOU 3044  N   SER A 478    18177  21224  15091   3962   2547  -1449       N  
ATOM   3045  CA  SER A 478     -35.320  19.604 -15.365  1.00142.67           C  
ANISOU 3045  CA  SER A 478    18426  20865  14917   3747   2507  -1613       C  
ATOM   3046  C   SER A 478     -35.459  20.367 -16.698  1.00148.84           C  
ANISOU 3046  C   SER A 478    19160  21928  15462   3561   2606  -1689       C  
ATOM   3047  O   SER A 478     -36.584  20.608 -17.141  1.00147.15           O  
ANISOU 3047  O   SER A 478    19164  21568  15177   3302   2528  -1761       O  
ATOM   3048  CB  SER A 478     -36.446  20.000 -14.413  1.00142.33           C  
ANISOU 3048  CB  SER A 478    18520  20558  15002   3436   2293  -1491       C  
ATOM   3049  OG  SER A 478     -36.665  19.000 -13.434  1.00151.48           O  
ANISOU 3049  OG  SER A 478    19862  21353  16340   3597   2215  -1488       O  
ATOM   3050  N   ARG A 479     -34.332  20.703 -17.356  1.00148.79           N  
ANISOU 3050  N   ARG A 479    18874  22334  15327   3699   2779  -1672       N  
ATOM   3051  CA  ARG A 479     -34.305  21.450 -18.626  1.00149.65           C  
ANISOU 3051  CA  ARG A 479    18914  22754  15191   3533   2892  -1711       C  
ATOM   3052  C   ARG A 479     -35.055  20.757 -19.788  1.00156.42           C  
ANISOU 3052  C   ARG A 479    20106  23454  15873   3576   2963  -1995       C  
ATOM   3053  O   ARG A 479     -35.514  21.454 -20.692  1.00155.56           O  
ANISOU 3053  O   ARG A 479    20032  23504  15569   3346   2979  -2012       O  
ATOM   3054  CB  ARG A 479     -32.854  21.813 -19.033  1.00152.85           C  
ANISOU 3054  CB  ARG A 479    18928  23650  15496   3681   3082  -1624       C  
ATOM   3055  CG  ARG A 479     -32.032  20.710 -19.745  1.00168.48           C  
ANISOU 3055  CG  ARG A 479    20890  25753  17370   4106   3312  -1834       C  
ATOM   3056  CD  ARG A 479     -31.629  19.562 -18.829  1.00178.33           C  
ANISOU 3056  CD  ARG A 479    22138  26794  18824   4480   3297  -1861       C  
ATOM   3057  NE  ARG A 479     -31.016  18.455 -19.561  1.00187.84           N  
ANISOU 3057  NE  ARG A 479    23402  28026  19942   4913   3504  -2097       N  
ATOM   3058  CZ  ARG A 479     -30.675  17.290 -19.019  1.00199.39           C  
ANISOU 3058  CZ  ARG A 479    25009  29198  21552   5285   3510  -2202       C  
ATOM   3059  NH1 ARG A 479     -30.123  16.343 -19.764  1.00190.73           N  
ANISOU 3059  NH1 ARG A 479    23973  28132  20363   5688   3710  -2428       N  
ATOM   3060  NH2 ARG A 479     -30.888  17.060 -17.727  1.00178.66           N  
ANISOU 3060  NH2 ARG A 479    22485  26238  19159   5264   3318  -2081       N  
ATOM   3061  N   LYS A 480     -35.182  19.409 -19.765  1.00156.02           N  
ANISOU 3061  N   LYS A 480    20312  23083  15886   3857   2995  -2214       N  
ATOM   3062  CA  LYS A 480     -35.895  18.659 -20.806  1.00157.95           C  
ANISOU 3062  CA  LYS A 480    20898  23143  15972   3889   3046  -2512       C  
ATOM   3063  C   LYS A 480     -37.406  18.922 -20.721  1.00160.14           C  
ANISOU 3063  C   LYS A 480    21434  23145  16267   3522   2843  -2527       C  
ATOM   3064  O   LYS A 480     -38.027  19.213 -21.744  1.00159.95           O  
ANISOU 3064  O   LYS A 480    21531  23209  16032   3348   2850  -2645       O  
ATOM   3065  CB  LYS A 480     -35.574  17.149 -20.736  1.00163.58           C  
ANISOU 3065  CB  LYS A 480    21829  23556  16770   4288   3133  -2741       C  
ATOM   3066  CG  LYS A 480     -36.041  16.321 -21.949  1.00178.26           C  
ANISOU 3066  CG  LYS A 480    24015  25281  18432   4375   3230  -3091       C  
ATOM   3067  CD  LYS A 480     -35.087  16.375 -23.151  1.00190.31           C  
ANISOU 3067  CD  LYS A 480    25382  27240  19685   4569   3472  -3211       C  
ATOM   3068  CE  LYS A 480     -35.626  15.626 -24.350  1.00202.57           C  
ANISOU 3068  CE  LYS A 480    27274  28681  21012   4607   3547  -3564       C  
ATOM   3069  NZ  LYS A 480     -34.815  15.877 -25.571  1.00213.75           N  
ANISOU 3069  NZ  LYS A 480    28526  30564  22124   4747   3781  -3660       N  
ATOM   3070  N   GLU A 481     -37.977  18.842 -19.504  1.00155.23           N  
ANISOU 3070  N   GLU A 481    20877  22220  15883   3409   2665  -2398       N  
ATOM   3071  CA  GLU A 481     -39.403  19.078 -19.236  1.00152.74           C  
ANISOU 3071  CA  GLU A 481    20768  21650  15617   3072   2470  -2387       C  
ATOM   3072  C   GLU A 481     -39.803  20.527 -19.543  1.00154.88           C  
ANISOU 3072  C   GLU A 481    20873  22203  15770   2740   2398  -2216       C  
ATOM   3073  O   GLU A 481     -40.914  20.783 -20.014  1.00153.40           O  
ANISOU 3073  O   GLU A 481    20850  21941  15493   2494   2297  -2282       O  
ATOM   3074  CB  GLU A 481     -39.745  18.731 -17.776  1.00152.33           C  
ANISOU 3074  CB  GLU A 481    20771  21269  15840   3052   2324  -2254       C  
ATOM   3075  CG  GLU A 481     -39.686  17.242 -17.462  1.00166.19           C  
ANISOU 3075  CG  GLU A 481    22784  22639  17721   3324   2358  -2422       C  
ATOM   3076  CD  GLU A 481     -38.380  16.720 -16.891  1.00190.39           C  
ANISOU 3076  CD  GLU A 481    25694  25751  20896   3708   2463  -2352       C  
ATOM   3077  OE1 GLU A 481     -37.304  17.047 -17.443  1.00185.27           O  
ANISOU 3077  OE1 GLU A 481    24797  25467  20130   3892   2613  -2342       O  
ATOM   3078  OE2 GLU A 481     -38.438  15.949 -15.905  1.00185.97           O  
ANISOU 3078  OE2 GLU A 481    25261  24867  20534   3835   2399  -2304       O  
ATOM   3079  N   LEU A 482     -38.882  21.464 -19.276  1.00151.16           N  
ANISOU 3079  N   LEU A 482    20077  22056  15302   2736   2448  -1995       N  
ATOM   3080  CA  LEU A 482     -39.053  22.894 -19.505  1.00148.98           C  
ANISOU 3080  CA  LEU A 482    19628  22046  14931   2445   2398  -1803       C  
ATOM   3081  C   LEU A 482     -38.991  23.222 -20.994  1.00155.63           C  
ANISOU 3081  C   LEU A 482    20484  23166  15481   2408   2523  -1904       C  
ATOM   3082  O   LEU A 482     -39.704  24.118 -21.440  1.00153.63           O  
ANISOU 3082  O   LEU A 482    20258  23000  15115   2142   2442  -1827       O  
ATOM   3083  CB  LEU A 482     -37.986  23.675 -18.727  1.00148.23           C  
ANISOU 3083  CB  LEU A 482    19191  22190  14940   2457   2422  -1553       C  
ATOM   3084  CG  LEU A 482     -38.368  24.187 -17.332  1.00149.37           C  
ANISOU 3084  CG  LEU A 482    19279  22168  15306   2288   2235  -1354       C  
ATOM   3085  CD1 LEU A 482     -38.722  23.050 -16.372  1.00149.13           C  
ANISOU 3085  CD1 LEU A 482    19430  21763  15471   2441   2154  -1430       C  
ATOM   3086  CD2 LEU A 482     -37.238  24.990 -16.740  1.00151.62           C  
ANISOU 3086  CD2 LEU A 482    19219  22734  15654   2288   2266  -1138       C  
ATOM   3087  N   GLU A 483     -38.154  22.491 -21.763  1.00156.58           N  
ANISOU 3087  N   GLU A 483    20595  23430  15468   2689   2721  -2077       N  
ATOM   3088  CA  GLU A 483     -38.024  22.679 -23.213  1.00159.14           C  
ANISOU 3088  CA  GLU A 483    20945  24040  15484   2690   2864  -2196       C  
ATOM   3089  C   GLU A 483     -39.232  22.122 -23.974  1.00164.17           C  
ANISOU 3089  C   GLU A 483    21929  24464  15983   2600   2785  -2441       C  
ATOM   3090  O   GLU A 483     -39.542  22.617 -25.059  1.00164.44           O  
ANISOU 3090  O   GLU A 483    22005  24717  15757   2471   2816  -2478       O  
ATOM   3091  CB  GLU A 483     -36.710  22.091 -23.745  1.00164.45           C  
ANISOU 3091  CB  GLU A 483    21475  24958  16051   3035   3113  -2306       C  
ATOM   3092  CG  GLU A 483     -35.542  23.065 -23.678  1.00177.56           C  
ANISOU 3092  CG  GLU A 483    22739  27040  17684   3021   3233  -2059       C  
ATOM   3093  CD  GLU A 483     -35.346  24.009 -24.856  1.00205.51           C  
ANISOU 3093  CD  GLU A 483    26169  30980  20935   2847   3347  -1978       C  
ATOM   3094  OE1 GLU A 483     -36.200  24.028 -25.773  1.00204.29           O  
ANISOU 3094  OE1 GLU A 483    26246  30795  20579   2709   3308  -2092       O  
ATOM   3095  OE2 GLU A 483     -34.336  24.747 -24.849  1.00202.52           O  
ANISOU 3095  OE2 GLU A 483    25465  30956  20527   2835   3470  -1789       O  
ATOM   3096  N   LYS A 484     -39.922  21.117 -23.399  1.00161.17           N  
ANISOU 3096  N   LYS A 484    21795  23670  15773   2652   2677  -2596       N  
ATOM   3097  CA  LYS A 484     -41.121  20.507 -23.986  1.00161.82           C  
ANISOU 3097  CA  LYS A 484    22206  23516  15763   2538   2578  -2838       C  
ATOM   3098  C   LYS A 484     -42.311  21.468 -23.866  1.00163.67           C  
ANISOU 3098  C   LYS A 484    22456  23739  15991   2170   2373  -2690       C  
ATOM   3099  O   LYS A 484     -43.082  21.614 -24.814  1.00163.79           O  
ANISOU 3099  O   LYS A 484    22610  23829  15793   2023   2323  -2807       O  
ATOM   3100  CB  LYS A 484     -41.446  19.169 -23.301  1.00164.94           C  
ANISOU 3100  CB  LYS A 484    22844  23455  16372   2678   2527  -3015       C  
ATOM   3101  CG  LYS A 484     -40.596  17.994 -23.762  1.00182.34           C  
ANISOU 3101  CG  LYS A 484    25164  25593  18524   3048   2716  -3270       C  
ATOM   3102  CD  LYS A 484     -40.726  16.860 -22.770  1.00191.80           C  
ANISOU 3102  CD  LYS A 484    26559  26324  19993   3186   2656  -3345       C  
ATOM   3103  CE  LYS A 484     -39.851  15.678 -23.095  1.00204.59           C  
ANISOU 3103  CE  LYS A 484    28315  27820  21598   3586   2835  -3588       C  
ATOM   3104  NZ  LYS A 484     -39.946  14.641 -22.038  1.00212.83           N  
ANISOU 3104  NZ  LYS A 484    29558  28386  22923   3717   2769  -3615       N  
ATOM   3105  N   GLN A 485     -42.440  22.135 -22.700  1.00158.07           N  
ANISOU 3105  N   GLN A 485    21599  22952  15508   2038   2253  -2434       N  
ATOM   3106  CA  GLN A 485     -43.502  23.108 -22.414  1.00155.38           C  
ANISOU 3106  CA  GLN A 485    21246  22593  15197   1723   2064  -2270       C  
ATOM   3107  C   GLN A 485     -43.303  24.443 -23.171  1.00159.87           C  
ANISOU 3107  C   GLN A 485    21648  23535  15561   1579   2094  -2092       C  
ATOM   3108  O   GLN A 485     -44.233  25.253 -23.239  1.00157.43           O  
ANISOU 3108  O   GLN A 485    21360  23237  15217   1341   1948  -1986       O  
ATOM   3109  CB  GLN A 485     -43.619  23.367 -20.894  1.00153.86           C  
ANISOU 3109  CB  GLN A 485    20956  22202  15302   1656   1946  -2068       C  
ATOM   3110  CG  GLN A 485     -44.840  22.794 -20.159  1.00165.32           C  
ANISOU 3110  CG  GLN A 485    22604  23291  16919   1524   1774  -2134       C  
ATOM   3111  CD  GLN A 485     -46.202  23.129 -20.731  1.00182.78           C  
ANISOU 3111  CD  GLN A 485    24945  25489  19015   1272   1632  -2196       C  
ATOM   3112  OE1 GLN A 485     -46.459  24.243 -21.208  1.00177.67           O  
ANISOU 3112  OE1 GLN A 485    24199  25080  18226   1126   1593  -2072       O  
ATOM   3113  NE2 GLN A 485     -47.141  22.202 -20.588  1.00174.05           N  
ANISOU 3113  NE2 GLN A 485    24053  24090  17988   1205   1537  -2365       N  
ATOM   3114  N   ASP A 486     -42.096  24.667 -23.733  1.00159.41           N  
ANISOU 3114  N   ASP A 486    21420  23780  15367   1726   2287  -2051       N  
ATOM   3115  CA  ASP A 486     -41.762  25.866 -24.505  1.00160.06           C  
ANISOU 3115  CA  ASP A 486    21349  24224  15242   1598   2350  -1874       C  
ATOM   3116  C   ASP A 486     -42.081  25.692 -25.995  1.00167.06           C  
ANISOU 3116  C   ASP A 486    22389  25295  15790   1599   2416  -2052       C  
ATOM   3117  O   ASP A 486     -41.884  26.634 -26.771  1.00167.45           O  
ANISOU 3117  O   ASP A 486    22346  25650  15626   1493   2473  -1910       O  
ATOM   3118  CB  ASP A 486     -40.289  26.273 -24.294  1.00163.13           C  
ANISOU 3118  CB  ASP A 486    21446  24877  15660   1718   2525  -1711       C  
ATOM   3119  CG  ASP A 486     -40.005  27.004 -22.993  1.00172.87           C  
ANISOU 3119  CG  ASP A 486    22483  26042  17157   1613   2433  -1457       C  
ATOM   3120  OD1 ASP A 486     -40.877  27.786 -22.542  1.00170.95           O  
ANISOU 3120  OD1 ASP A 486    22282  25677  16995   1378   2258  -1318       O  
ATOM   3121  OD2 ASP A 486     -38.892  26.834 -22.448  1.00180.52           O  
ANISOU 3121  OD2 ASP A 486    23247  27106  18238   1769   2537  -1397       O  
ATOM   3122  N   ALA A 487     -42.589  24.496 -26.392  1.00165.17           N  
ANISOU 3122  N   ALA A 487    22397  24864  15494   1704   2401  -2360       N  
ATOM   3123  CA  ALA A 487     -42.970  24.198 -27.775  1.00167.51           C  
ANISOU 3123  CA  ALA A 487    22873  25312  15461   1704   2441  -2576       C  
ATOM   3124  C   ALA A 487     -44.005  25.217 -28.298  1.00169.68           C  
ANISOU 3124  C   ALA A 487    23176  25722  15573   1426   2284  -2432       C  
ATOM   3125  O   ALA A 487     -43.804  25.773 -29.382  1.00171.13           O  
ANISOU 3125  O   ALA A 487    23330  26234  15458   1400   2373  -2389       O  
ATOM   3126  CB  ALA A 487     -43.498  22.778 -27.894  1.00169.71           C  
ANISOU 3126  CB  ALA A 487    23433  25283  15766   1800   2395  -2922       C  
ATOM   3127  N   GLU A 488     -45.069  25.495 -27.496  1.00162.52           N  
ANISOU 3127  N   GLU A 488    22312  24577  14862   1233   2060  -2338       N  
ATOM   3128  CA  GLU A 488     -46.147  26.478 -27.718  1.00178.22           C  
ANISOU 3128  CA  GLU A 488    24310  26639  16767    988   1879  -2176       C  
ATOM   3129  C   GLU A 488     -47.206  26.403 -26.623  1.00187.12           C  
ANISOU 3129  C   GLU A 488    25477  27450  18170    845   1664  -2134       C  
ATOM   3130  O   GLU A 488     -46.866  26.452 -25.443  1.00142.84           O  
ANISOU 3130  O   GLU A 488    19769  21660  12843    874   1660  -2025       O  
ATOM   3131  CB  GLU A 488     -46.779  26.434 -29.131  1.00181.98           C  
ANISOU 3131  CB  GLU A 488    24943  27320  16880    931   1847  -2328       C  
ATOM   3132  CG  GLU A 488     -47.340  25.092 -29.573  1.00192.88           C  
ANISOU 3132  CG  GLU A 488    26565  28530  18191    979   1798  -2699       C  
ATOM   3133  CD  GLU A 488     -47.450  24.947 -31.078  1.00209.49           C  
ANISOU 3133  CD  GLU A 488    28804  30905  19887    983   1832  -2878       C  
ATOM   3134  OE1 GLU A 488     -48.308  25.629 -31.683  1.00200.34           O  
ANISOU 3134  OE1 GLU A 488    27675  29887  18556    809   1674  -2798       O  
ATOM   3135  OE2 GLU A 488     -46.672  24.153 -31.654  1.00202.20           O  
ANISOU 3135  OE2 GLU A 488    27956  30066  18807   1174   2016  -3100       O  
TER    3136      GLU A 488                                                      
HETATM 3137 NA    NA A 601     -37.164  27.683   4.190  1.00125.45          NA1+
ANISOU 3137 NA    NA A 601    15245  18739  13681   1669    131    721      NA1+
HETATM 3138 NA    NA A 602     -32.796  20.279   2.841  1.00139.92          NA1+
ANISOU 3138 NA    NA A 602    17012  20389  15763   3995    545    874      NA1+
HETATM 3139 NA    NA A 603     -39.641  23.635   8.408  1.00 90.13          NA1+
ANISOU 3139 NA    NA A 603    11712  13340   9192   2160    -25   1135      NA1+
HETATM 3140  N   ASP A 604     -37.134  31.513  11.825  1.00106.26           N  
ANISOU 3140  N   ASP A 604    12654  16977  10742    902   -777    965       N  
HETATM 3141  CA  ASP A 604     -36.634  30.462  10.938  1.00110.21           C  
ANISOU 3141  CA  ASP A 604    13089  17453  11334   1151   -672   1020       C  
HETATM 3142  C   ASP A 604     -37.027  30.699   9.483  1.00118.06           C  
ANISOU 3142  C   ASP A 604    14122  18301  12435   1068   -517    919       C  
HETATM 3143  O   ASP A 604     -36.256  30.301   8.586  1.00121.36           O  
ANISOU 3143  O   ASP A 604    14387  18811  12914   1203   -441    926       O  
HETATM 3144  CB  ASP A 604     -37.114  29.083  11.400  1.00112.75           C  
ANISOU 3144  CB  ASP A 604    13612  17578  11651   1406   -635   1127       C  
HETATM 3145  CG  ASP A 604     -36.724  28.766  12.825  1.00126.45           C  
ANISOU 3145  CG  ASP A 604    15322  19462  13262   1515   -785   1254       C  
HETATM 3146  OD1 ASP A 604     -35.885  27.865  13.022  1.00134.72           O  
ANISOU 3146  OD1 ASP A 604    16267  20613  14307   1789   -818   1375       O  
HETATM 3147  OD2 ASP A 604     -37.252  29.429  13.746  1.00126.64           O  
ANISOU 3147  OD2 ASP A 604    15430  19508  13181   1337   -871   1231       O  
HETATM 3148  OXT ASP A 604     -38.116  31.251   9.237  1.00134.67           O  
ANISOU 3148  OXT ASP A 604    16406  20209  14552    883   -470    836       O  
HETATM 3149  N1  6Z6 A 605     -40.917  21.448  -3.982  1.00108.68           N  
ANISOU 3149  N1  6Z6 A 605    14583  15014  11696   2308   1053   -268       N  
HETATM 3150  C2  6Z6 A 605     -43.043  18.320  -0.182  1.00114.75           C  
ANISOU 3150  C2  6Z6 A 605    16144  14692  12764   2392    863     59       C  
HETATM 3151  O2  6Z6 A 605     -45.027  19.885  -5.825  1.00106.67           O  
ANISOU 3151  O2  6Z6 A 605    15174  13914  11443   1792   1082   -734       O  
HETATM 3152  C4  6Z6 A 605     -43.516  18.666  -2.566  1.00111.71           C  
ANISOU 3152  C4  6Z6 A 605    15782  14364  12299   2244    990   -288       C  
HETATM 3153  C5  6Z6 A 605     -44.744  19.264  -2.197  1.00110.81           C  
ANISOU 3153  C5  6Z6 A 605    15715  14209  12178   1923    917   -265       C  
HETATM 3154  C6  6Z6 A 605     -45.130  19.427  -0.857  1.00111.12           C  
ANISOU 3154  C6  6Z6 A 605    15761  14208  12252   1830    831    -94       C  
HETATM 3155  O1  6Z6 A 605     -43.173  15.717  -4.419  1.00115.28           O  
ANISOU 3155  O1  6Z6 A 605    16776  14195  12829   2728   1230   -670       O  
HETATM 3156  C9  6Z6 A 605     -44.095  16.374  -4.901  1.00112.77           C  
ANISOU 3156  C9  6Z6 A 605    16455  13937  12454   2426   1200   -751       C  
HETATM 3157  C8  6Z6 A 605     -44.126  17.864  -4.837  1.00110.35           C  
ANISOU 3157  C8  6Z6 A 605    15866  13995  12067   2225   1138   -669       C  
HETATM 3158  C13 6Z6 A 605     -45.022  18.533  -5.608  1.00107.94           C  
ANISOU 3158  C13 6Z6 A 605    15561  13764  11687   1955   1121   -780       C  
HETATM 3159  C14 6Z6 A 605     -44.038  20.633  -5.253  1.00106.90           C  
ANISOU 3159  C14 6Z6 A 605    14952  14202  11464   1882   1062   -583       C  
HETATM 3160  N   6Z6 A 605     -44.153  21.923  -5.715  1.00105.35           N  
ANISOU 3160  N   6Z6 A 605    14581  14265  11182   1694   1037   -573       N  
HETATM 3161  C15 6Z6 A 605     -43.023  20.072  -4.498  1.00108.64           C  
ANISOU 3161  C15 6Z6 A 605    15115  14417  11745   2144   1073   -476       C  
HETATM 3162  C16 6Z6 A 605     -41.863  20.817  -4.205  1.00108.54           C  
ANISOU 3162  C16 6Z6 A 605    14813  14725  11704   2244   1064   -360       C  
HETATM 3163  C7  6Z6 A 605     -43.080  18.623  -4.028  1.00111.03           C  
ANISOU 3163  C7  6Z6 A 605    15664  14375  12146   2339   1096   -479       C  
HETATM 3164  C3  6Z6 A 605     -42.680  18.180  -1.548  1.00114.05           C  
ANISOU 3164  C3  6Z6 A 605    16040  14646  12647   2484    963   -126       C  
HETATM 3165  C1  6Z6 A 605     -44.266  18.973   0.160  1.00113.34           C  
ANISOU 3165  C1  6Z6 A 605    16009  14487  12568   2058    803     70       C  
HETATM 3166  O   6Z6 A 605     -44.478  19.228   1.518  1.00113.20           O  
ANISOU 3166  O   6Z6 A 605    15970  14491  12551   1988    714    250       O  
HETATM 3167  C   6Z6 A 605     -45.683  18.765   2.119  1.00113.01           C  
ANISOU 3167  C   6Z6 A 605    16166  14208  12564   1814    700    291       C  
HETATM 3168  C10 6Z6 A 605     -45.230  15.668  -5.689  1.00112.50           C  
ANISOU 3168  C10 6Z6 A 605    16713  13606  12426   2250   1224   -957       C  
HETATM 3169  C11 6Z6 A 605     -45.844  16.497  -6.831  1.00109.98           C  
ANISOU 3169  C11 6Z6 A 605    16320  13485  11983   2012   1221  -1114       C  
HETATM 3170  C12 6Z6 A 605     -46.128  17.951  -6.402  1.00107.13           C  
ANISOU 3170  C12 6Z6 A 605    15701  13431  11572   1791   1134   -969       C  
HETATM 3171  C17 6Z6 A 605     -47.105  15.899  -7.500  1.00109.50           C  
ANISOU 3171  C17 6Z6 A 605    16520  13168  11919   1783   1210  -1306       C  
HETATM 3172  C18 6Z6 A 605     -46.933  15.284  -8.742  1.00111.44           C  
ANISOU 3172  C18 6Z6 A 605    16902  13350  12091   1879   1293  -1550       C  
HETATM 3173  C19 6Z6 A 605     -48.028  14.763  -9.502  1.00111.69           C  
ANISOU 3173  C19 6Z6 A 605    17161  13183  12093   1661   1275  -1760       C  
HETATM 3174  C20 6Z6 A 605     -49.312  14.871  -9.035  1.00109.95           C  
ANISOU 3174  C20 6Z6 A 605    17005  12844  11928   1340   1176  -1716       C  
HETATM 3175  C21 6Z6 A 605     -49.582  15.504  -7.789  1.00107.25           C  
ANISOU 3175  C21 6Z6 A 605    16522  12567  11662   1235   1103  -1467       C  
HETATM 3176  C26 6Z6 A 605     -48.497  16.011  -6.975  1.00106.92           C  
ANISOU 3176  C26 6Z6 A 605    16281  12699  11643   1453   1116  -1261       C  
HETATM 3177  C22 6Z6 A 605     -50.956  15.675  -7.401  1.00106.28           C  
ANISOU 3177  C22 6Z6 A 605    16440  12366  11576    901   1016  -1437       C  
HETATM 3178  C23 6Z6 A 605     -51.261  16.329  -6.227  1.00105.70           C  
ANISOU 3178  C23 6Z6 A 605    16232  12374  11557    800    956  -1214       C  
HETATM 3179  C24 6Z6 A 605     -50.206  16.820  -5.378  1.00105.27           C  
ANISOU 3179  C24 6Z6 A 605    16010  12469  11519   1013    964  -1016       C  
HETATM 3180  C25 6Z6 A 605     -48.879  16.656  -5.736  1.00105.64           C  
ANISOU 3180  C25 6Z6 A 605    16001  12599  11537   1320   1035  -1037       C  
HETATM 3181 BA    BA A 606     -51.493  23.877 -21.314  0.35179.96          BA2+
ANISOU 3181 BA    BA A 606    24915  24900  18562    395    975  -2339      BA2+
CONECT  767 3138                                                                
CONECT  795 3138                                                                
CONECT  802 3138                                                                
CONECT 2067 3137                                                                
CONECT 2292 3137                                                                
CONECT 2296 3137                                                                
CONECT 2301 3139                                                                
CONECT 2316 3137                                                                
CONECT 2319 3138                                                                
CONECT 2335 3138                                                                
CONECT 2606 3139                                                                
CONECT 2612 3139                                                                
CONECT 2624 3139                                                                
CONECT 2975 3137                                                                
CONECT 3137 2067 2292 2296 2316                                                 
CONECT 3137 2975                                                                
CONECT 3138  767  795  802 2319                                                 
CONECT 3138 2335                                                                
CONECT 3139 2301 2606 2612 2624                                                 
CONECT 3149 3162                                                                
CONECT 3150 3164 3165                                                           
CONECT 3151 3158 3159                                                           
CONECT 3152 3153 3163 3164                                                      
CONECT 3153 3152 3154                                                           
CONECT 3154 3153 3165                                                           
CONECT 3155 3156                                                                
CONECT 3156 3155 3157 3168                                                      
CONECT 3157 3156 3158 3163                                                      
CONECT 3158 3151 3157 3170                                                      
CONECT 3159 3151 3160 3161                                                      
CONECT 3160 3159                                                                
CONECT 3161 3159 3162 3163                                                      
CONECT 3162 3149 3161                                                           
CONECT 3163 3152 3157 3161                                                      
CONECT 3164 3150 3152                                                           
CONECT 3165 3150 3154 3166                                                      
CONECT 3166 3165 3167                                                           
CONECT 3167 3166                                                                
CONECT 3168 3156 3169                                                           
CONECT 3169 3168 3170 3171                                                      
CONECT 3170 3158 3169                                                           
CONECT 3171 3169 3172 3176                                                      
CONECT 3172 3171 3173                                                           
CONECT 3173 3172 3174                                                           
CONECT 3174 3173 3175                                                           
CONECT 3175 3174 3176 3177                                                      
CONECT 3176 3171 3175 3180                                                      
CONECT 3177 3175 3178                                                           
CONECT 3178 3177 3179                                                           
CONECT 3179 3178 3180                                                           
CONECT 3180 3176 3179                                                           
MASTER      420    0    6   23    2    0    0    6 3180    1   51   41          
END                                                                             



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elNémo is maintained by Yves-Henri Sanejouand.
It was developed by Karsten Suhre.
Between 2003 and 2014, it was hosted by IGS (Marseille).
Last modification: October 18th, 2018.