CNRS Nantes University UFIP UFIP
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***  4fdo v/s 4p8l  ***

elNémo ID: 20122614375822011

Job options:

ID        	=	 20122614375822011
JOBID     	=	 4fdo v/s 4p8l
USERID    	=	 tweety.dec6
PRIVAT    	=	 0

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

DOPROJMODS	=	 on
DORMSD    	=	 on

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 4fdo v/s 4p8l

HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 29-MAY-12   4FDO              
TITLE     MYCOBACTERIUM TUBERCULOSIS DPRE1 IN COMPLEX WITH CT319                
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: OXIDOREDUCTASE DPRE1;                                      
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 1.-.-.-;                                                         
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 1773;                                                
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: DPRE1, MT3898, RV3790;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28A                                    
KEYWDS    ALPHA+BETA, OXIDOREDUCTASE, DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE,       
KEYWDS   2 OXIDOREDUCTASE-OXIDOREDUCTASE INHIBITOR COMPLEX                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    S.M.BATT,G.S.BESRA,K.FUTTERER                                         
REVDAT   2   31-OCT-12 4FDO    1       JRNL                                     
REVDAT   1   04-JUL-12 4FDO    0                                                
JRNL        AUTH   S.M.BATT,T.JABEEN,V.BHOWRUTH,L.QUILL,P.A.LUND,L.EGGELING,    
JRNL        AUTH 2 L.J.ALDERWICK,K.FUTTERER,G.S.BESRA                           
JRNL        TITL   STRUCTURAL BASIS OF INHIBITION OF MYCOBACTERIUM TUBERCULOSIS 
JRNL        TITL 2 DPRE1 BY BENZOTHIAZINONE INHIBITORS.                         
JRNL        REF    PROC.NATL.ACAD.SCI.USA        V. 109 11354 2012              
JRNL        REFN                   ISSN 0027-8424                               
JRNL        PMID   22733761                                                     
JRNL        DOI    10.1073/PNAS.1205735109                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.40 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : PHENIX (PHENIX.REFINE: 1.7.3_928)                    
REMARK   3   AUTHORS     : PAUL ADAMS,PAVEL AFONINE,VICENT CHEN,IAN             
REMARK   3               : DAVIS,KRESHNA GOPAL,RALF GROSSE-                     
REMARK   3               : KUNSTLEVE,LI-WEI HUNG,ROBERT IMMORMINO,              
REMARK   3               : TOM IOERGER,AIRLIE MCCOY,ERIK MCKEE,NIGEL            
REMARK   3               : MORIARTY,REETAL PAI,RANDY READ,JANE                  
REMARK   3               : RICHARDSON,DAVID RICHARDSON,TOD ROMO,JIM             
REMARK   3               : SACCHETTINI,NICHOLAS SAUTER,JACOB SMITH,             
REMARK   3               : LAURENT STORONI,TOM TERWILLIGER,PETER                
REMARK   3               : ZWART                                                
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : ML                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.40                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 41.86                          
REMARK   3   MIN(FOBS/SIGMA_FOBS)              : 1.410                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 23489                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.205                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.130                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1206                            
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT (IN BINS).                           
REMARK   3   BIN  RESOLUTION RANGE  COMPL.    NWORK NFREE   RWORK  RFREE        
REMARK   3     1 41.8662 -  4.9957    1.00     2552   134  0.1743 0.1961        
REMARK   3     2  4.9957 -  3.9662    1.00     2494   135  0.1353 0.1632        
REMARK   3     3  3.9662 -  3.4651    1.00     2508   113  0.1727 0.1982        
REMARK   3     4  3.4651 -  3.1484    1.00     2492   122  0.1717 0.2060        
REMARK   3     5  3.1484 -  2.9228    1.00     2439   129  0.1646 0.2059        
REMARK   3     6  2.9228 -  2.7505    1.00     2444   159  0.1747 0.2485        
REMARK   3     7  2.7505 -  2.6128    1.00     2472   136  0.1697 0.2202        
REMARK   3     8  2.6128 -  2.4991    1.00     2446   149  0.1921 0.2349        
REMARK   3     9  2.4991 -  2.4030    0.99     2436   129  0.1937 0.2477        
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED        : FLAT BULK SOLVENT MODEL                       
REMARK   3   SOLVENT RADIUS     : 1.20                                          
REMARK   3   SHRINKAGE RADIUS   : 0.98                                          
REMARK   3   K_SOL              : 0.34                                          
REMARK   3   B_SOL              : 26.35                                         
REMARK   3                                                                      
REMARK   3  ERROR ESTIMATES.                                                    
REMARK   3   COORDINATE ERROR (MAXIMUM-LIKELIHOOD BASED)     : 0.290            
REMARK   3   PHASE ERROR (DEGREES, MAXIMUM-LIKELIHOOD BASED) : 17.530           
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : NULL                           
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -0.40550                                             
REMARK   3    B22 (A**2) : -0.40550                                             
REMARK   3    B33 (A**2) : 0.81110                                              
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  TWINNING INFORMATION.                                               
REMARK   3   FRACTION: NULL                                                     
REMARK   3   OPERATOR: NULL                                                     
REMARK   3                                                                      
REMARK   3  DEVIATIONS FROM IDEAL VALUES.                                       
REMARK   3                 RMSD          COUNT                                  
REMARK   3   BOND      :  0.008           3380                                  
REMARK   3   ANGLE     :  1.138           4609                                  
REMARK   3   CHIRALITY :  0.077            512                                  
REMARK   3   PLANARITY :  0.005            590                                  
REMARK   3   DIHEDRAL  : 14.067           1193                                  
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    SELECTION: all                                                    
REMARK   3    ORIGIN FOR THE GROUP (A):  39.4006   8.9742   4.3822              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0684 T22:   0.0552                                     
REMARK   3      T33:   0.0539 T12:   0.0013                                     
REMARK   3      T13:  -0.0006 T23:  -0.0153                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.7880 L22:   0.6757                                     
REMARK   3      L33:   0.6115 L12:  -0.2259                                     
REMARK   3      L13:  -0.0025 L23:  -0.0339                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0054 S12:  -0.0555 S13:   0.0767                       
REMARK   3      S21:   0.0114 S22:  -0.0020 S23:  -0.0365                       
REMARK   3      S31:  -0.0774 S32:  -0.0289 S33:  -0.0001                       
REMARK   3                                                                      
REMARK   3  NCS DETAILS                                                         
REMARK   3   NUMBER OF NCS GROUPS : NULL                                        
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 4FDO COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 30-MAY-12.                  
REMARK 100 THE RCSB ID CODE IS RCSB072770.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 21-MAY-12                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 5.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU MICROMAX-007 HF             
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : VARIMAX                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU SATURN 944                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23613                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.400                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 45.250                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 7.300                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : 0.08800                            
REMARK 200   FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.40                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.53                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 98.1                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.33800                            
REMARK 200  R SYM FOR SHELL            (I) : 0.33800                            
REMARK 200   FOR SHELL         : 4.800                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: DPRE1 - MONOCLINIC CRYSTAL FORM                      
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 57.46                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.89                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1 M SODIUM CACODYLATE, 36% ETHYLENE    
REMARK 280  GLYCOL, PH 5.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 288K     
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
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       21.39233            
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       42.78467            
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        0.00000            
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       21.39233            
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       42.78467            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 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   -19                                                      
REMARK 465     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     GLY A     5                                                      
REMARK 465     ALA A     6                                                      
REMARK 465     ALA A   269                                                      
REMARK 465     PRO A   270                                                      
REMARK 465     GLN A   271                                                      
REMARK 465     LEU A   272                                                      
REMARK 465     LEU A   273                                                      
REMARK 465     THR A   274                                                      
REMARK 465     LEU A   275                                                      
REMARK 465     PRO A   276                                                      
REMARK 465     ASP A   277                                                      
REMARK 465     VAL A   278                                                      
REMARK 465     PHE A   279                                                      
REMARK 465     PRO A   280                                                      
REMARK 465     ASN A   281                                                      
REMARK 465     GLY A   282                                                      
REMARK 465     LEU A   283                                                      
REMARK 465     ALA A   284                                                      
REMARK 465     ASN A   285                                                      
REMARK 465     LYS A   286                                                      
REMARK 465     TYR A   287                                                      
REMARK 465     THR A   288                                                      
REMARK 465     PHE A   289                                                      
REMARK 465     GLY A   290                                                      
REMARK 465     PRO A   291                                                      
REMARK 465     ILE A   292                                                      
REMARK 465     GLY A   293                                                      
REMARK 465     GLU A   294                                                      
REMARK 465     LEU A   295                                                      
REMARK 465     TRP A   296                                                      
REMARK 465     TYR A   297                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     THR A   7    OG1  CG2                                            
REMARK 470     LYS A  37    CE   NZ                                             
REMARK 470     ARG A  41    NE   CZ   NH1  NH2                                  
REMARK 470     GLU A  44    CD   OE1  OE2                                       
REMARK 470     GLU A 157    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 166    CG   CD   OE1  OE2                                  
REMARK 470     GLU A 254    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 259    CG   CD   CE   NZ                                   
REMARK 470     LYS A 266    NZ                                                  
REMARK 470     ASP A 268    CG   OD1  OD2                                       
REMARK 470     ARG A 298    CG   CD   NE   CZ   NH1  NH2                        
REMARK 470     LYS A 299    CG   CD   CE   NZ                                   
REMARK 470     GLU A 342    CG   CD   OE1  OE2                                  
REMARK 470     LYS A 349    CE   NZ                                             
REMARK 470     ARG A 405    NE   CZ   NH1  NH2                                  
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A  1018     O    HOH A  1019              1.92            
REMARK 500   O    HOH A  1045     O    HOH A  1090              1.94            
REMARK 500   O    HOH A  1075     O    HOH A  1147              1.95            
REMARK 500   O    HOH A  1077     O    HOH A  1149              2.00            
REMARK 500   ND2  ASN A    25     O    HOH A  1158              2.10            
REMARK 500   O    HOH A  1111     O    HOH A  1176              2.12            
REMARK 500   OE1  GLN A   334     O    HOH A  1122              2.14            
REMARK 500   OE2  GLU A   221     O    HOH A  1029              2.14            
REMARK 500   O    HOH A  1074     O    HOH A  1113              2.17            
REMARK 500   OD2  ASP A   167     O    HOH A  1187              2.18            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  66       87.48   -153.13                                   
REMARK 500    ALA A 343       41.22    -99.42                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE FAD A 900                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 0T5 A 901                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4FDN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4FDP   RELATED DB: PDB                                   
DBREF  4FDO A    1   461  UNP    P72056   DPRE1_MYCTU      1    461             
SEQADV 4FDO MET A  -19  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO GLY A  -18  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO SER A  -17  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO SER A  -16  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A  -15  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A  -14  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A  -13  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A  -12  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A  -11  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A  -10  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO SER A   -9  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO SER A   -8  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO GLY A   -7  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO LEU A   -6  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO VAL A   -5  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO PRO A   -4  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO ARG A   -3  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO GLY A   -2  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO SER A   -1  UNP  P72056              EXPRESSION TAG                 
SEQADV 4FDO HIS A    0  UNP  P72056              EXPRESSION TAG                 
SEQRES   1 A  481  MET GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY          
SEQRES   2 A  481  LEU VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA          
SEQRES   3 A  481  THR THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR          
SEQRES   4 A  481  ALA PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA          
SEQRES   5 A  481  GLU MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER          
SEQRES   6 A  481  GLY GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG          
SEQRES   7 A  481  SER TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL          
SEQRES   8 A  481  ILE ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP          
SEQRES   9 A  481  ALA ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN          
SEQRES  10 A  481  LEU ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU          
SEQRES  11 A  481  TRP VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL          
SEQRES  12 A  481  GLY GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS          
SEQRES  13 A  481  HIS SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET          
SEQRES  14 A  481  ASP LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR          
SEQRES  15 A  481  PRO THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL          
SEQRES  16 A  481  GLY GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR          
SEQRES  17 A  481  ILE GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA          
SEQRES  18 A  481  ASP GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA          
SEQRES  19 A  481  LEU HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER          
SEQRES  20 A  481  SER ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU          
SEQRES  21 A  481  GLY ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL          
SEQRES  22 A  481  GLU GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS          
SEQRES  23 A  481  PHE ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE          
SEQRES  24 A  481  PRO ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE          
SEQRES  25 A  481  GLY GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY          
SEQRES  26 A  481  LYS VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP          
SEQRES  27 A  481  MET PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY          
SEQRES  28 A  481  PHE LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL          
SEQRES  29 A  481  ASP GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER          
SEQRES  30 A  481  GLY HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY          
SEQRES  31 A  481  PRO ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY          
SEQRES  32 A  481  TRP ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU          
SEQRES  33 A  481  GLY LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU          
SEQRES  34 A  481  PHE GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR          
SEQRES  35 A  481  THR ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP          
SEQRES  36 A  481  GLU TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG          
SEQRES  37 A  481  VAL PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU          
HET    FAD  A 900      53                                                       
HET    0T5  A 901      24                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     0T5 3-NITRO-N-[(1R)-1-PHENYLETHYL]-5-(TRIFLUOROMETHYL)               
HETNAM   2 0T5  BENZAMIDE                                                       
FORMUL   2  FAD    C27 H33 N9 O15 P2                                            
FORMUL   3  0T5    C16 H13 F3 N2 O3                                             
FORMUL   4  HOH   *194(H2 O)                                                    
HELIX    1   1 ASP A   31  SER A   45  1                                  15    
HELIX    2   2 ASN A   97  LEU A  106  1                                  10    
HELIX    3   3 THR A  122  CYS A  129  1                                   8    
HELIX    4   4 ASN A  135  GLY A  140  1                                   6    
HELIX    5   5 SER A  141  ASN A  144  5                                   4    
HELIX    6   6 ASP A  167  VAL A  175  1                                   9    
HELIX    7   7 SER A  208  HIS A  216  1                                   9    
HELIX    8   8 GLY A  219  TYR A  224  5                                   6    
HELIX    9   9 THR A  252  LEU A  256  5                                   5    
HELIX   10  10 PRO A  257  SER A  262  5                                   6    
HELIX   11  11 LEU A  310  HIS A  315  1                                   6    
HELIX   12  12 GLU A  322  GLY A  328  1                                   7    
HELIX   13  13 ALA A  343  SER A  357  1                                  15    
HELIX   14  14 GLY A  395  PHE A  410  1                                  16    
HELIX   15  15 THR A  416  ASP A  419  5                                   4    
HELIX   16  16 THR A  423  TYR A  431  1                                   9    
HELIX   17  17 ARG A  433  ASP A  445  1                                  13    
HELIX   18  18 SER A  452  LEU A  458  1                                   7    
SHEET    1   A 4 THR A   8  LEU A  13  0                                        
SHEET    2   A 4 SER A  22  LEU A  27 -1  O  SER A  22   N  LEU A  13           
SHEET    3   A 4 LEU A  70  ASP A  73  1  O  VAL A  71   N  ASN A  25           
SHEET    4   A 4 ALA A  51  ARG A  54  1  N  ILE A  52   O  ILE A  72           
SHEET    1   B 5 ILE A  80  ILE A  83  0                                        
SHEET    2   B 5 LEU A  89  ASP A  93 -1  O  ASP A  91   N  SER A  82           
SHEET    3   B 5 ILE A 183  GLU A 190 -1  O  ALA A 187   N  ILE A  92           
SHEET    4   B 5 VAL A 146  LEU A 152 -1  N  LEU A 152   O  ILE A 183           
SHEET    5   B 5 ILE A 158  LEU A 161 -1  O  LEU A 161   N  MET A 149           
SHEET    1   C 2 LEU A 110  TRP A 111  0                                        
SHEET    2   C 2 THR A 192  PRO A 193 -1  O  THR A 192   N  TRP A 111           
SHEET    1   D 8 TYR A 303  ASN A 309  0                                        
SHEET    2   D 8 TYR A 198  VAL A 205 -1  N  PHE A 199   O  GLN A 308           
SHEET    3   D 8 ALA A 243  LEU A 250 -1  O  ARG A 247   N  ASP A 202           
SHEET    4   D 8 TYR A 226  PHE A 231 -1  N  TRP A 230   O  ALA A 244           
SHEET    5   D 8 VAL A 365  PHE A 369 -1  O  PHE A 366   N  ALA A 229           
SHEET    6   D 8 GLY A 383  PRO A 391 -1  O  ASN A 385   N  LYS A 367           
SHEET    7   D 8 PHE A 332  PRO A 340 -1  N  LEU A 333   O  PHE A 390           
SHEET    8   D 8 ARG A 413  LEU A 414 -1  O  ARG A 413   N  VAL A 338           
CISPEP   1 PRO A  237    PRO A  238          0         6.05                     
CISPEP   2 HIS A  315    PRO A  316          0         7.82                     
CISPEP   3 GLY A  328    PRO A  329          0         3.55                     
SITE     1 AC1 33 TRP A  16  ILE A  52  ALA A  53  ARG A  54                    
SITE     2 AC1 33 GLY A  55  LEU A  56  GLY A  57  ARG A  58                    
SITE     3 AC1 33 SER A  59  TYR A  60  ASN A  63  ALA A  64                    
SITE     4 AC1 33 MET A  74  ALA A  94  PRO A 116  GLY A 117                    
SITE     5 AC1 33 THR A 118  VAL A 121  THR A 122  GLY A 124                    
SITE     6 AC1 33 GLY A 125  ALA A 128  CYS A 129  ILE A 131                    
SITE     7 AC1 33 HIS A 132  ASN A 178  GLY A 179  GLY A 182                    
SITE     8 AC1 33 ILE A 184  TYR A 415  ALA A 417  0T5 A 901                    
SITE     9 AC1 33 HOH A1009                                                     
SITE     1 AC2 11 TYR A  60  GLY A 117  HIS A 132  GLY A 133                    
SITE     2 AC2 11 LYS A 134  LEU A 317  PHE A 320  GLN A 336                    
SITE     3 AC2 11 ASN A 385  CYS A 387  FAD A 900                               
CRYST1  127.884  127.884   64.177  90.00  90.00 120.00 P 64          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      0.007820  0.004515  0.000000        0.00000                         
SCALE2      0.000000  0.009029  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.015582        0.00000                         
ATOM      1  N   THR A   7      38.491 -22.938   2.928  1.00 50.91           N  
ANISOU    1  N   THR A   7     6700   5539   7105   -183    -69     61       N  
ATOM      2  CA  THR A   7      39.075 -21.689   2.433  1.00 55.97           C  
ANISOU    2  CA  THR A   7     7331   6237   7696   -151    -76     26       C  
ATOM      3  C   THR A   7      38.417 -20.425   3.042  1.00 57.47           C  
ANISOU    3  C   THR A   7     7484   6519   7834   -174    -67     54       C  
ATOM      4  O   THR A   7      39.117 -19.547   3.570  1.00 63.98           O  
ANISOU    4  O   THR A   7     8299   7407   8603   -141    -55     78       O  
ATOM      5  CB  THR A   7      39.067 -21.629   0.880  1.00 26.46           C  
ANISOU    5  CB  THR A   7     3611   2497   3948   -143    -99    -67       C  
ATOM      6  N   THR A   8      37.083 -20.341   2.988  1.00 46.32           N  
ANISOU    6  N   THR A   8     6049   5111   6441   -228    -73     50       N  
ATOM      7  CA  THR A   8      36.357 -19.175   3.525  1.00 38.46           C  
ANISOU    7  CA  THR A   8     5016   4198   5399   -247    -62     72       C  
ATOM      8  C   THR A   8      35.607 -19.403   4.858  1.00 30.82           C  
ANISOU    8  C   THR A   8     4026   3234   4450   -280    -37    151       C  
ATOM      9  O   THR A   8      35.239 -20.523   5.198  1.00 26.89           O  
ANISOU    9  O   THR A   8     3534   2668   4015   -309    -31    184       O  
ATOM     10  CB  THR A   8      35.383 -18.554   2.479  1.00 35.56           C  
ANISOU   10  CB  THR A   8     4629   3860   5021   -274    -86     10       C  
ATOM     11  OG1 THR A   8      34.243 -19.397   2.302  1.00 39.95           O  
ANISOU   11  OG1 THR A   8     5172   4365   5644   -329    -98      3       O  
ATOM     12  CG2 THR A   8      36.074 -18.364   1.133  1.00 35.65           C  
ANISOU   12  CG2 THR A   8     4667   3870   5009   -240   -108    -64       C  
ATOM     13  N   THR A   9      35.382 -18.314   5.592  1.00 25.05           N  
ANISOU   13  N   THR A   9     3270   2584   3664   -275    -21    180       N  
ATOM     14  CA  THR A   9      34.652 -18.330   6.861  1.00 23.65           C  
ANISOU   14  CA  THR A   9     3069   2429   3487   -300      9    251       C  
ATOM     15  C   THR A   9      33.463 -17.355   6.835  1.00 29.96           C  
ANISOU   15  C   THR A   9     3827   3292   4264   -328     13    238       C  
ATOM     16  O   THR A   9      33.650 -16.142   6.650  1.00 21.98           O  
ANISOU   16  O   THR A   9     2810   2348   3195   -303      8    209       O  
ATOM     17  CB  THR A   9      35.569 -17.922   8.030  1.00 22.12           C  
ANISOU   17  CB  THR A   9     2887   2280   3239   -257     28    305       C  
ATOM     18  OG1 THR A   9      36.652 -18.849   8.131  1.00 33.91           O  
ANISOU   18  OG1 THR A   9     4413   3715   4754   -226     24    325       O  
ATOM     19  CG2 THR A   9      34.800 -17.910   9.332  1.00 26.07           C  
ANISOU   19  CG2 THR A   9     3366   2810   3728   -277     62    379       C  
ATOM     20  N   ALA A  10      32.252 -17.884   7.022  1.00 23.35           N  
ANISOU   20  N   ALA A  10     2960   2434   3478   -380     23    260       N  
ATOM     21  CA  ALA A  10      31.056 -17.051   7.102  1.00 19.15           C  
ANISOU   21  CA  ALA A  10     2381   1962   2931   -406     32    256       C  
ATOM     22  C   ALA A  10      31.194 -16.180   8.331  1.00 20.17           C  
ANISOU   22  C   ALA A  10     2503   2165   2995   -378     65    306       C  
ATOM     23  O   ALA A  10      31.540 -16.660   9.402  1.00 21.53           O  
ANISOU   23  O   ALA A  10     2689   2331   3162   -370     92    371       O  
ATOM     24  CB  ALA A  10      29.766 -17.904   7.170  1.00 11.64           C  
ANISOU   24  CB  ALA A  10     1394    972   2056   -470     40    278       C  
ATOM     25  N   THR A  11      30.936 -14.891   8.165  1.00 19.09           N  
ANISOU   25  N   THR A  11     2347   2098   2806   -361     62    274       N  
ATOM     26  CA  THR A  11      31.259 -13.923   9.193  1.00 14.25           C  
ANISOU   26  CA  THR A  11     1736   1554   2123   -326     86    303       C  
ATOM     27  C   THR A  11      30.313 -12.746   9.104  1.00 17.29           C  
ANISOU   27  C   THR A  11     2084   2006   2480   -327     91    279       C  
ATOM     28  O   THR A  11      30.083 -12.198   8.014  1.00 16.01           O  
ANISOU   28  O   THR A  11     1913   1849   2320   -327     63    221       O  
ATOM     29  CB  THR A  11      32.710 -13.398   9.019  1.00 23.92           C  
ANISOU   29  CB  THR A  11     2999   2788   3300   -276     67    277       C  
ATOM     30  OG1 THR A  11      33.602 -14.502   8.826  1.00 23.69           O  
ANISOU   30  OG1 THR A  11     3002   2694   3305   -270     56    287       O  
ATOM     31  CG2 THR A  11      33.157 -12.589  10.238  1.00 16.86           C  
ANISOU   31  CG2 THR A  11     2111   1957   2339   -242     88    310       C  
ATOM     32  N   ARG A  12      29.761 -12.379  10.259  1.00 16.04           N  
ANISOU   32  N   ARG A  12     1905   1897   2293   -325    128    326       N  
ATOM     33  CA  ARG A  12      28.977 -11.161  10.425  1.00 17.51           C  
ANISOU   33  CA  ARG A  12     2059   2152   2443   -314    140    309       C  
ATOM     34  C   ARG A  12      29.923  -9.959  10.330  1.00 18.11           C  
ANISOU   34  C   ARG A  12     2163   2263   2453   -266    124    270       C  
ATOM     35  O   ARG A  12      30.876  -9.860  11.103  1.00 14.83           O  
ANISOU   35  O   ARG A  12     1778   1859   1997   -237    130    291       O  
ATOM     36  CB  ARG A  12      28.272 -11.181  11.791  1.00 10.02           C  
ANISOU   36  CB  ARG A  12     1086   1246   1474   -319    190    372       C  
ATOM     37  CG  ARG A  12      27.363  -9.988  12.055  1.00 19.77           C  
ANISOU   37  CG  ARG A  12     2285   2552   2675   -304    209    357       C  
ATOM     38  CD  ARG A  12      26.739 -10.062  13.452  1.00 19.21           C  
ANISOU   38  CD  ARG A  12     2193   2527   2578   -303    265    421       C  
ATOM     39  NE  ARG A  12      25.752  -9.004  13.696  1.00 20.65           N  
ANISOU   39  NE  ARG A  12     2335   2776   2735   -289    288    406       N  
ATOM     40  CZ  ARG A  12      26.053  -7.808  14.204  1.00 24.00           C  
ANISOU   40  CZ  ARG A  12     2776   3255   3088   -241    295    384       C  
ATOM     41  NH1 ARG A  12      27.312  -7.515  14.510  1.00 14.85           N  
ANISOU   41  NH1 ARG A  12     1670   2094   1879   -207    277    373       N  
ATOM     42  NH2 ARG A  12      25.103  -6.896  14.402  1.00 18.38           N  
ANISOU   42  NH2 ARG A  12     2027   2598   2359   -225    317    370       N  
ATOM     43  N   LEU A  13      29.676  -9.064   9.373  1.00 17.16           N  
ANISOU   43  N   LEU A  13     2034   2159   2327   -257    100    215       N  
ATOM     44  CA  LEU A  13      30.485  -7.855   9.226  1.00 12.90           C  
ANISOU   44  CA  LEU A  13     1518   1649   1735   -216     87    180       C  
ATOM     45  C   LEU A  13      29.681  -6.575   9.474  1.00 20.85           C  
ANISOU   45  C   LEU A  13     2500   2713   2710   -199    100    164       C  
ATOM     46  O   LEU A  13      28.486  -6.493   9.158  1.00 19.20           O  
ANISOU   46  O   LEU A  13     2251   2518   2526   -217    104    160       O  
ATOM     47  CB  LEU A  13      31.140  -7.795   7.840  1.00 16.41           C  
ANISOU   47  CB  LEU A  13     1983   2059   2193   -211     49    130       C  
ATOM     48  CG  LEU A  13      32.078  -8.952   7.451  1.00 18.86           C  
ANISOU   48  CG  LEU A  13     2323   2311   2533   -218     35    133       C  
ATOM     49  CD1 LEU A  13      32.554  -8.842   5.982  1.00 14.12           C  
ANISOU   49  CD1 LEU A  13     1740   1684   1941   -211      2     80       C  
ATOM     50  CD2 LEU A  13      33.279  -9.036   8.416  1.00 17.18           C  
ANISOU   50  CD2 LEU A  13     2138   2101   2288   -192     45    163       C  
ATOM     51  N   THR A  14      30.354  -5.576  10.041  1.00 13.34           N  
ANISOU   51  N   THR A  14     1570   1794   1705   -163    104    155       N  
ATOM     52  CA  THR A  14      29.815  -4.231  10.153  1.00 18.07           C  
ANISOU   52  CA  THR A  14     2156   2438   2273   -138    111    129       C  
ATOM     53  C   THR A  14      30.913  -3.223   9.813  1.00 20.50           C  
ANISOU   53  C   THR A  14     2498   2744   2550   -108     89     92       C  
ATOM     54  O   THR A  14      32.097  -3.566   9.775  1.00 17.95           O  
ANISOU   54  O   THR A  14     2203   2396   2221   -105     74     92       O  
ATOM     55  CB  THR A  14      29.338  -3.914  11.587  1.00 15.35           C  
ANISOU   55  CB  THR A  14     1800   2143   1890   -123    149    160       C  
ATOM     56  OG1 THR A  14      30.454  -3.980  12.484  1.00 20.14           O  
ANISOU   56  OG1 THR A  14     2443   2755   2456   -105    151    175       O  
ATOM     57  CG2 THR A  14      28.271  -4.896  12.057  1.00 15.93           C  
ANISOU   57  CG2 THR A  14     1837   2222   1995   -154    181    207       C  
ATOM     58  N   GLY A  15      30.515  -1.976   9.576  1.00 23.75           N  
ANISOU   58  N   GLY A  15     2902   3178   2943    -87     87     61       N  
ATOM     59  CA  GLY A  15      31.455  -0.874   9.556  1.00 22.44           C  
ANISOU   59  CA  GLY A  15     2766   3015   2747    -59     74     32       C  
ATOM     60  C   GLY A  15      32.044  -0.634  10.940  1.00 19.19           C  
ANISOU   60  C   GLY A  15     2371   2628   2291    -41     88     44       C  
ATOM     61  O   GLY A  15      31.701  -1.310  11.906  1.00 18.33           O  
ANISOU   61  O   GLY A  15     2254   2540   2171    -47    111     79       O  
ATOM     62  N   TRP A  16      32.918   0.355  11.035  1.00 20.53           N  
ANISOU   62  N   TRP A  16     2565   2799   2437    -21     74     14       N  
ATOM     63  CA  TRP A  16      33.634   0.651  12.267  1.00 17.68           C  
ANISOU   63  CA  TRP A  16     2223   2461   2032     -3     77     15       C  
ATOM     64  C   TRP A  16      32.735   0.861  13.481  1.00 23.09           C  
ANISOU   64  C   TRP A  16     2898   3194   2680     13    107     29       C  
ATOM     65  O   TRP A  16      33.027   0.350  14.565  1.00 29.70           O  
ANISOU   65  O   TRP A  16     3745   4056   3484     18    118     55       O  
ATOM     66  CB  TRP A  16      34.504   1.884  12.072  1.00 18.18           C  
ANISOU   66  CB  TRP A  16     2307   2516   2085     13     56    -27       C  
ATOM     67  CG  TRP A  16      35.385   2.199  13.262  1.00 22.98           C  
ANISOU   67  CG  TRP A  16     2935   3146   2651     29     47    -35       C  
ATOM     68  CD1 TRP A  16      35.308   3.298  14.078  1.00 15.96           C  
ANISOU   68  CD1 TRP A  16     2057   2282   1724     53     49    -66       C  
ATOM     69  CD2 TRP A  16      36.468   1.403  13.761  1.00 20.08           C  
ANISOU   69  CD2 TRP A  16     2579   2778   2274     25     32    -14       C  
ATOM     70  NE1 TRP A  16      36.286   3.235  15.041  1.00 27.44           N  
ANISOU   70  NE1 TRP A  16     3529   3754   3144     61     32    -69       N  
ATOM     71  CE2 TRP A  16      37.008   2.082  14.871  1.00 23.97           C  
ANISOU   71  CE2 TRP A  16     3087   3301   2720     45     21    -35       C  
ATOM     72  CE3 TRP A  16      37.034   0.180  13.376  1.00 22.65           C  
ANISOU   72  CE3 TRP A  16     2902   3079   2625      8     25     17       C  
ATOM     73  CZ2 TRP A  16      38.085   1.581  15.598  1.00 30.02           C  
ANISOU   73  CZ2 TRP A  16     3864   4078   3464     49      1    -22       C  
ATOM     74  CZ3 TRP A  16      38.098  -0.325  14.107  1.00 25.76           C  
ANISOU   74  CZ3 TRP A  16     3306   3480   2999     15      8     33       C  
ATOM     75  CH2 TRP A  16      38.613   0.377  15.205  1.00 30.30           C  
ANISOU   75  CH2 TRP A  16     3895   4091   3527     36     -5     15       C  
ATOM     76  N   GLY A  17      31.660   1.623  13.299  1.00 14.30           N  
ANISOU   76  N   GLY A  17     1766   2098   1570     25    123     11       N  
ATOM     77  CA  GLY A  17      30.750   1.918  14.385  1.00 25.26           C  
ANISOU   77  CA  GLY A  17     3141   3534   2921     46    157     20       C  
ATOM     78  C   GLY A  17      29.691   0.844  14.573  1.00 31.39           C  
ANISOU   78  C   GLY A  17     3882   4327   3716     25    189     68       C  
ATOM     79  O   GLY A  17      28.648   1.100  15.189  1.00 26.92           O  
ANISOU   79  O   GLY A  17     3292   3803   3134     39    224     77       O  
ATOM     80  N   ARG A  18      29.954  -0.338  14.010  1.00 25.48           N  
ANISOU   80  N   ARG A  18     3129   3545   3007     -9    178     97       N  
ATOM     81  CA  ARG A  18      29.187  -1.556  14.288  1.00 27.15           C  
ANISOU   81  CA  ARG A  18     3313   3761   3243    -37    205    149       C  
ATOM     82  C   ARG A  18      27.740  -1.527  13.785  1.00 29.91           C  
ANISOU   82  C   ARG A  18     3613   4123   3630    -50    223    151       C  
ATOM     83  O   ARG A  18      26.867  -2.200  14.330  1.00 28.93           O  
ANISOU   83  O   ARG A  18     3456   4019   3517    -66    258    193       O  
ATOM     84  CB  ARG A  18      29.207  -1.888  15.785  1.00 27.55           C  
ANISOU   84  CB  ARG A  18     3373   3854   3243    -23    239    189       C  
ATOM     85  CG  ARG A  18      30.600  -2.065  16.403  1.00 28.88           C  
ANISOU   85  CG  ARG A  18     3585   4017   3371     -9    218    194       C  
ATOM     86  CD  ARG A  18      30.425  -2.520  17.848  1.00 34.82           C  
ANISOU   86  CD  ARG A  18     4343   4815   4070      5    254    243       C  
ATOM     87  NE  ARG A  18      31.651  -2.477  18.643  1.00 41.48           N  
ANISOU   87  NE  ARG A  18     5228   5671   4862     28    233    242       N  
ATOM     88  CZ  ARG A  18      32.600  -3.407  18.615  1.00 41.54           C  
ANISOU   88  CZ  ARG A  18     5254   5648   4882     18    211    272       C  
ATOM     89  NH1 ARG A  18      32.493  -4.452  17.802  1.00 39.49           N  
ANISOU   89  NH1 ARG A  18     4981   5338   4687    -17    208    300       N  
ATOM     90  NH2 ARG A  18      33.669  -3.281  19.389  1.00 43.11           N  
ANISOU   90  NH2 ARG A  18     5484   5866   5029     43    189    270       N  
ATOM     91  N   THR A  19      27.487  -0.751  12.742  1.00 26.70           N  
ANISOU   91  N   THR A  19     3197   3703   3245    -43    199    110       N  
ATOM     92  CA  THR A  19      26.137  -0.654  12.218  1.00 31.29           C  
ANISOU   92  CA  THR A  19     3727   4299   3861    -51    209    108       C  
ATOM     93  C   THR A  19      25.936  -1.468  10.919  1.00 24.86           C  
ANISOU   93  C   THR A  19     2896   3444   3107    -89    178    106       C  
ATOM     94  O   THR A  19      26.902  -1.927  10.293  1.00 26.27           O  
ANISOU   94  O   THR A  19     3107   3580   3296   -103    148     97       O  
ATOM     95  CB  THR A  19      25.750   0.825  12.007  1.00 38.97           C  
ANISOU   95  CB  THR A  19     4698   5295   4816    -10    206     66       C  
ATOM     96  OG1 THR A  19      24.391   0.899  11.564  1.00 55.58           O  
ANISOU   96  OG1 THR A  19     6745   7419   6954    -13    216     68       O  
ATOM     97  CG2 THR A  19      26.648   1.463  10.973  1.00 25.69           C  
ANISOU   97  CG2 THR A  19     3051   3573   3137     -1    164     27       C  
ATOM     98  N   ALA A  20      24.676  -1.649  10.538  1.00 21.19           N  
ANISOU   98  N   ALA A  20     2377   2993   2680   -105    184    112       N  
ATOM     99  CA  ALA A  20      24.310  -2.343   9.300  1.00 25.54           C  
ANISOU   99  CA  ALA A  20     2906   3511   3286   -140    150    101       C  
ATOM    100  C   ALA A  20      25.054  -3.674   9.050  1.00 23.50           C  
ANISOU  100  C   ALA A  20     2672   3201   3055   -179    134    118       C  
ATOM    101  O   ALA A  20      25.796  -3.809   8.080  1.00 18.41           O  
ANISOU  101  O   ALA A  20     2058   2518   2417   -182     97     90       O  
ATOM    102  CB  ALA A  20      24.455  -1.404   8.108  1.00 20.92           C  
ANISOU  102  CB  ALA A  20     2335   2918   2697   -116    110     54       C  
ATOM    103  N   PRO A  21      24.835  -4.667   9.919  1.00 20.18           N  
ANISOU  103  N   PRO A  21     2238   2779   2651   -207    166    166       N  
ATOM    104  CA  PRO A  21      25.496  -5.968   9.767  1.00 15.04           C  
ANISOU  104  CA  PRO A  21     1610   2074   2031   -241    154    186       C  
ATOM    105  C   PRO A  21      24.986  -6.774   8.560  1.00 20.14           C  
ANISOU  105  C   PRO A  21     2232   2678   2742   -282    120    166       C  
ATOM    106  O   PRO A  21      23.810  -6.731   8.232  1.00 21.33           O  
ANISOU  106  O   PRO A  21     2330   2848   2927   -300    118    161       O  
ATOM    107  CB  PRO A  21      25.111  -6.698  11.056  1.00 14.22           C  
ANISOU  107  CB  PRO A  21     1489   1985   1930   -258    203    249       C  
ATOM    108  CG  PRO A  21      23.780  -6.108  11.447  1.00 14.23           C  
ANISOU  108  CG  PRO A  21     1433   2042   1932   -254    235    257       C  
ATOM    109  CD  PRO A  21      23.840  -4.660  11.012  1.00 21.62           C  
ANISOU  109  CD  PRO A  21     2377   3008   2829   -208    216    205       C  
ATOM    110  N   SER A  22      25.878  -7.493   7.894  1.00 20.92           N  
ANISOU  110  N   SER A  22     2370   2723   2858   -293     90    151       N  
ATOM    111  CA  SER A  22      25.460  -8.535   6.964  1.00 19.23           C  
ANISOU  111  CA  SER A  22     2139   2462   2707   -337     61    137       C  
ATOM    112  C   SER A  22      26.517  -9.638   6.992  1.00 19.58           C  
ANISOU  112  C   SER A  22     2228   2444   2767   -349     55    150       C  
ATOM    113  O   SER A  22      27.620  -9.424   7.486  1.00 20.17           O  
ANISOU  113  O   SER A  22     2345   2518   2799   -318     64    161       O  
ATOM    114  CB  SER A  22      25.220  -7.988   5.548  1.00 12.15           C  
ANISOU  114  CB  SER A  22     1237   1566   1812   -328     14     77       C  
ATOM    115  OG  SER A  22      26.443  -7.589   4.958  1.00 19.85           O  
ANISOU  115  OG  SER A  22     2268   2526   2749   -295     -7     47       O  
ATOM    116  N   VAL A  23      26.169 -10.823   6.495  1.00 18.56           N  
ANISOU  116  N   VAL A  23     2088   2262   2702   -393     39    149       N  
ATOM    117  CA  VAL A  23      27.052 -11.980   6.573  1.00 15.72           C  
ANISOU  117  CA  VAL A  23     1768   1837   2368   -405     36    166       C  
ATOM    118  C   VAL A  23      27.684 -12.286   5.223  1.00 19.70           C  
ANISOU  118  C   VAL A  23     2306   2296   2884   -400    -10    106       C  
ATOM    119  O   VAL A  23      26.991 -12.383   4.207  1.00 20.90           O  
ANISOU  119  O   VAL A  23     2436   2439   3065   -421    -44     63       O  
ATOM    120  CB  VAL A  23      26.288 -13.252   7.061  1.00 20.09           C  
ANISOU  120  CB  VAL A  23     2293   2348   2993   -460     56    212       C  
ATOM    121  CG1 VAL A  23      27.212 -14.465   7.058  1.00 14.85           C  
ANISOU  121  CG1 VAL A  23     1674   1606   2361   -468     50    227       C  
ATOM    122  CG2 VAL A  23      25.685 -13.027   8.441  1.00 13.84           C  
ANISOU  122  CG2 VAL A  23     1470   1604   2186   -463    110    279       C  
ATOM    123  N   ALA A  24      29.003 -12.442   5.211  1.00 16.21           N  
ANISOU  123  N   ALA A  24     1914   1828   2416   -369    -13    104       N  
ATOM    124  CA  ALA A  24      29.704 -12.778   3.981  1.00 14.11           C  
ANISOU  124  CA  ALA A  24     1682   1521   2157   -359    -50     50       C  
ATOM    125  C   ALA A  24      30.613 -13.968   4.218  1.00 19.57           C  
ANISOU  125  C   ALA A  24     2411   2146   2878   -360    -45     70       C  
ATOM    126  O   ALA A  24      31.014 -14.234   5.351  1.00 18.50           O  
ANISOU  126  O   ALA A  24     2282   2008   2737   -353    -15    126       O  
ATOM    127  CB  ALA A  24      30.528 -11.581   3.485  1.00 11.44           C  
ANISOU  127  CB  ALA A  24     1369   1223   1754   -310    -59     17       C  
ATOM    128  N   ASN A  25      30.934 -14.686   3.146  1.00 16.42           N  
ANISOU  128  N   ASN A  25     2036   1693   2508   -364    -76     23       N  
ATOM    129  CA  ASN A  25      32.057 -15.617   3.186  1.00 25.37           C  
ANISOU  129  CA  ASN A  25     3212   2767   3659   -347    -74     31       C  
ATOM    130  C   ASN A  25      33.353 -14.821   3.107  1.00 17.62           C  
ANISOU  130  C   ASN A  25     2260   1819   2616   -292    -70     21       C  
ATOM    131  O   ASN A  25      33.585 -14.121   2.136  1.00 22.93           O  
ANISOU  131  O   ASN A  25     2941   2517   3256   -271    -88    -29       O  
ATOM    132  CB  ASN A  25      31.983 -16.612   2.028  1.00 22.54           C  
ANISOU  132  CB  ASN A  25     2872   2341   3350   -365   -107    -24       C  
ATOM    133  CG  ASN A  25      30.678 -17.370   2.011  1.00 35.28           C  
ANISOU  133  CG  ASN A  25     4452   3920   5033   -426   -118    -22       C  
ATOM    134  OD1 ASN A  25      29.906 -17.270   1.054  1.00 42.75           O  
ANISOU  134  OD1 ASN A  25     5379   4871   5991   -448   -152    -76       O  
ATOM    135  ND2 ASN A  25      30.405 -18.108   3.084  1.00 30.62           N  
ANISOU  135  ND2 ASN A  25     3849   3297   4487   -455    -89     43       N  
ATOM    136  N   VAL A  26      34.182 -14.914   4.136  1.00 19.68           N  
ANISOU  136  N   VAL A  26     2534   2081   2862   -269    -46     70       N  
ATOM    137  CA  VAL A  26      35.430 -14.162   4.169  1.00 18.14           C  
ANISOU  137  CA  VAL A  26     2359   1919   2615   -221    -43     63       C  
ATOM    138  C   VAL A  26      36.607 -15.049   3.780  1.00 25.36           C  
ANISOU  138  C   VAL A  26     3307   2779   3550   -195    -49     53       C  
ATOM    139  O   VAL A  26      36.842 -16.099   4.387  1.00 24.08           O  
ANISOU  139  O   VAL A  26     3157   2568   3425   -199    -41     91       O  
ATOM    140  CB  VAL A  26      35.688 -13.536   5.558  1.00 19.12           C  
ANISOU  140  CB  VAL A  26     2473   2091   2699   -206    -18    118       C  
ATOM    141  CG1 VAL A  26      37.092 -12.904   5.623  1.00 17.40           C  
ANISOU  141  CG1 VAL A  26     2273   1898   2440   -161    -20    110       C  
ATOM    142  CG2 VAL A  26      34.608 -12.506   5.887  1.00 18.89           C  
ANISOU  142  CG2 VAL A  26     2412   2121   2644   -222     -9    120       C  
ATOM    143  N   LEU A  27      37.322 -14.642   2.738  1.00 24.86           N  
ANISOU  143  N   LEU A  27     3261   2723   3464   -166    -62      3       N  
ATOM    144  CA  LEU A  27      38.577 -15.287   2.402  1.00 21.62           C  
ANISOU  144  CA  LEU A  27     2878   2274   3063   -131    -63     -8       C  
ATOM    145  C   LEU A  27      39.686 -14.505   3.074  1.00 26.03           C  
ANISOU  145  C   LEU A  27     3433   2879   3580    -94    -50     19       C  
ATOM    146  O   LEU A  27      39.753 -13.272   2.975  1.00 21.78           O  
ANISOU  146  O   LEU A  27     2881   2397   2997    -87    -48      7       O  
ATOM    147  CB  LEU A  27      38.801 -15.323   0.898  1.00 19.25           C  
ANISOU  147  CB  LEU A  27     2597   1960   2759   -117    -79    -76       C  
ATOM    148  CG  LEU A  27      40.150 -15.893   0.433  1.00 25.00           C  
ANISOU  148  CG  LEU A  27     3351   2656   3493    -73    -75    -93       C  
ATOM    149  CD1 LEU A  27      40.293 -17.369   0.796  1.00 15.78           C  
ANISOU  149  CD1 LEU A  27     2202   1410   2385    -75    -76    -74       C  
ATOM    150  CD2 LEU A  27      40.316 -15.687  -1.068  1.00 23.94           C  
ANISOU  150  CD2 LEU A  27     3234   2525   3337    -55    -86   -160       C  
ATOM    151  N   ARG A  28      40.544 -15.228   3.779  1.00 25.62           N  
ANISOU  151  N   ARG A  28     3391   2799   3544    -72    -43     55       N  
ATOM    152  CA  ARG A  28      41.665 -14.619   4.466  1.00 22.02           C  
ANISOU  152  CA  ARG A  28     2929   2385   3055    -37    -36     79       C  
ATOM    153  C   ARG A  28      42.929 -15.439   4.205  1.00 26.56           C  
ANISOU  153  C   ARG A  28     3519   2919   3652      3    -38     77       C  
ATOM    154  O   ARG A  28      43.229 -16.382   4.935  1.00 32.91           O  
ANISOU  154  O   ARG A  28     4333   3688   4485     13    -36    119       O  
ATOM    155  CB  ARG A  28      41.379 -14.538   5.966  1.00 21.27           C  
ANISOU  155  CB  ARG A  28     2822   2314   2945    -46    -28    141       C  
ATOM    156  CG  ARG A  28      42.474 -13.826   6.723  1.00 29.27           C  
ANISOU  156  CG  ARG A  28     3826   3376   3918    -13    -29    161       C  
ATOM    157  CD  ARG A  28      42.244 -13.751   8.228  1.00 29.31           C  
ANISOU  157  CD  ARG A  28     3825   3412   3899    -15    -23    219       C  
ATOM    158  NE  ARG A  28      43.517 -13.478   8.890  1.00 44.37           N  
ANISOU  158  NE  ARG A  28     5729   5351   5781     23    -32    236       N  
ATOM    159  CZ  ARG A  28      44.083 -12.276   8.957  1.00 52.83           C  
ANISOU  159  CZ  ARG A  28     6784   6476   6814     35    -40    212       C  
ATOM    160  NH1 ARG A  28      43.476 -11.223   8.420  1.00 49.26           N  
ANISOU  160  NH1 ARG A  28     6324   6051   6343     14    -37    174       N  
ATOM    161  NH2 ARG A  28      45.255 -12.124   9.564  1.00 54.13           N  
ANISOU  161  NH2 ARG A  28     6941   6665   6962     67    -54    227       N  
ATOM    162  N   THR A  29      43.665 -15.094   3.157  1.00 24.57           N  
ANISOU  162  N   THR A  29     3270   2675   3389     28    -38     31       N  
ATOM    163  CA  THR A  29      44.898 -15.814   2.844  1.00 29.22           C  
ANISOU  163  CA  THR A  29     3870   3232   3999     72    -35     25       C  
ATOM    164  C   THR A  29      46.022 -14.867   2.458  1.00 28.12           C  
ANISOU  164  C   THR A  29     3713   3142   3827    103    -28      7       C  
ATOM    165  O   THR A  29      45.781 -13.856   1.809  1.00 29.18           O  
ANISOU  165  O   THR A  29     3841   3316   3931     92    -25    -23       O  
ATOM    166  CB  THR A  29      44.702 -16.856   1.702  1.00 20.12           C  
ANISOU  166  CB  THR A  29     2747   2014   2885     75    -38    -21       C  
ATOM    167  OG1 THR A  29      45.976 -17.383   1.333  1.00 26.99           O  
ANISOU  167  OG1 THR A  29     3624   2863   3770    126    -31    -32       O  
ATOM    168  CG2 THR A  29      44.084 -16.210   0.469  1.00 20.63           C  
ANISOU  168  CG2 THR A  29     2815   2099   2923     59    -42    -79       C  
ATOM    169  N   PRO A  30      47.262 -15.198   2.846  1.00 29.05           N  
ANISOU  169  N   PRO A  30     3822   3259   3957    143    -25     27       N  
ATOM    170  CA  PRO A  30      48.408 -14.393   2.406  1.00 28.05           C  
ANISOU  170  CA  PRO A  30     3673   3176   3810    172    -16      9       C  
ATOM    171  C   PRO A  30      48.827 -14.773   0.990  1.00 24.07           C  
ANISOU  171  C   PRO A  30     3184   2647   3316    198     -2    -40       C  
ATOM    172  O   PRO A  30      49.727 -14.149   0.437  1.00 24.42           O  
ANISOU  172  O   PRO A  30     3209   2724   3345    221     13    -57       O  
ATOM    173  CB  PRO A  30      49.502 -14.792   3.394  1.00 21.41           C  
ANISOU  173  CB  PRO A  30     2814   2339   2983    207    -23     51       C  
ATOM    174  CG  PRO A  30      49.186 -16.226   3.695  1.00 22.72           C  
ANISOU  174  CG  PRO A  30     3006   2437   3189    215    -27     73       C  
ATOM    175  CD  PRO A  30      47.670 -16.287   3.753  1.00 23.54           C  
ANISOU  175  CD  PRO A  30     3131   2522   3292    164    -31     72       C  
ATOM    176  N   ASP A  31      48.164 -15.774   0.413  1.00 24.62           N  
ANISOU  176  N   ASP A  31     3285   2658   3410    192     -5    -64       N  
ATOM    177  CA  ASP A  31      48.528 -16.300  -0.905  1.00 27.00           C  
ANISOU  177  CA  ASP A  31     3609   2931   3719    222      7   -117       C  
ATOM    178  C   ASP A  31      47.806 -15.564  -2.032  1.00 27.49           C  
ANISOU  178  C   ASP A  31     3682   3019   3744    201      9   -163       C  
ATOM    179  O   ASP A  31      46.641 -15.837  -2.314  1.00 25.25           O  
ANISOU  179  O   ASP A  31     3419   2711   3464    168     -7   -183       O  
ATOM    180  CB  ASP A  31      48.232 -17.811  -0.966  1.00 30.81           C  
ANISOU  180  CB  ASP A  31     4124   3331   4252    230     -2   -125       C  
ATOM    181  CG  ASP A  31      48.658 -18.463  -2.291  1.00 39.31           C  
ANISOU  181  CG  ASP A  31     5227   4373   5335    267      9   -186       C  
ATOM    182  OD1 ASP A  31      49.293 -17.804  -3.135  1.00 42.70           O  
ANISOU  182  OD1 ASP A  31     5649   4846   5730    292     29   -215       O  
ATOM    183  OD2 ASP A  31      48.369 -19.662  -2.483  1.00 46.50           O  
ANISOU  183  OD2 ASP A  31     6170   5211   6288    272      0   -205       O  
ATOM    184  N   ALA A  32      48.512 -14.651  -2.690  1.00 27.27           N  
ANISOU  184  N   ALA A  32     3639   3040   3681    221     29   -178       N  
ATOM    185  CA  ALA A  32      47.924 -13.873  -3.778  1.00 22.16           C  
ANISOU  185  CA  ALA A  32     3005   2424   2993    207     33   -215       C  
ATOM    186  C   ALA A  32      47.239 -14.729  -4.855  1.00 30.59           C  
ANISOU  186  C   ALA A  32     4113   3449   4062    210     23   -270       C  
ATOM    187  O   ALA A  32      46.198 -14.337  -5.402  1.00 32.60           O  
ANISOU  187  O   ALA A  32     4380   3715   4291    182      8   -294       O  
ATOM    188  CB  ALA A  32      48.953 -12.958  -4.390  1.00 20.83           C  
ANISOU  188  CB  ALA A  32     2817   2304   2794    235     63   -218       C  
ATOM    189  N   GLU A  33      47.794 -15.904  -5.134  1.00 33.89           N  
ANISOU  189  N   GLU A  33     4550   3817   4511    244     28   -291       N  
ATOM    190  CA  GLU A  33      47.209 -16.799  -6.142  1.00 39.26           C  
ANISOU  190  CA  GLU A  33     5272   4451   5196    249     14   -351       C  
ATOM    191  C   GLU A  33      45.841 -17.351  -5.721  1.00 28.05           C  
ANISOU  191  C   GLU A  33     3865   2987   3808    197    -21   -352       C  
ATOM    192  O   GLU A  33      44.979 -17.592  -6.566  1.00 27.34           O  
ANISOU  192  O   GLU A  33     3799   2882   3708    180    -42   -402       O  
ATOM    193  CB  GLU A  33      48.162 -17.953  -6.487  1.00 44.91           C  
ANISOU  193  CB  GLU A  33     6006   5116   5942    301     29   -376       C  
ATOM    194  CG  GLU A  33      49.348 -17.560  -7.366  1.00 61.97           C  
ANISOU  194  CG  GLU A  33     8161   7317   8066    356     67   -397       C  
ATOM    195  CD  GLU A  33      48.972 -17.341  -8.831  1.00 77.99           C  
ANISOU  195  CD  GLU A  33    10219   9372  10042    362     73   -455       C  
ATOM    196  OE1 GLU A  33      47.956 -17.913  -9.287  1.00 80.63           O  
ANISOU  196  OE1 GLU A  33    10579   9680  10377    330     47   -487       O  
ATOM    197  OE2 GLU A  33      49.698 -16.598  -9.528  1.00 83.05           O  
ANISOU  197  OE2 GLU A  33    10849  10069  10639    392    107   -459       O  
ATOM    198  N   MET A  34      45.652 -17.572  -4.424  1.00 22.93           N  
ANISOU  198  N   MET A  34     3197   2320   3196    172    -28   -297       N  
ATOM    199  CA  MET A  34      44.343 -17.983  -3.922  1.00 28.96           C  
ANISOU  199  CA  MET A  34     3963   3049   3990    119    -55   -287       C  
ATOM    200  C   MET A  34      43.326 -16.854  -4.120  1.00 32.30           C  
ANISOU  200  C   MET A  34     4370   3529   4372     81    -66   -292       C  
ATOM    201  O   MET A  34      42.149 -17.092  -4.414  1.00 27.19           O  
ANISOU  201  O   MET A  34     3730   2865   3737     43    -91   -316       O  
ATOM    202  CB  MET A  34      44.421 -18.365  -2.447  1.00 28.83           C  
ANISOU  202  CB  MET A  34     3931   3012   4013    106    -52   -219       C  
ATOM    203  CG  MET A  34      45.048 -19.729  -2.195  1.00 46.18           C  
ANISOU  203  CG  MET A  34     6149   5133   6266    134    -50   -211       C  
ATOM    204  SD  MET A  34      44.220 -21.048  -3.121  1.00 85.17           S  
ANISOU  204  SD  MET A  34    11129   9984  11250    115    -71   -273       S  
ATOM    205  CE  MET A  34      45.441 -21.416  -4.384  1.00 52.87           C  
ANISOU  205  CE  MET A  34     7061   5896   7130    182    -49   -330       C  
ATOM    206  N   ILE A  35      43.799 -15.622  -3.964  1.00 26.84           N  
ANISOU  206  N   ILE A  35     3657   2905   3637     92    -49   -269       N  
ATOM    207  CA  ILE A  35      42.954 -14.456  -4.150  1.00 24.39           C  
ANISOU  207  CA  ILE A  35     3332   2649   3287     65    -57   -270       C  
ATOM    208  C   ILE A  35      42.568 -14.340  -5.622  1.00 28.33           C  
ANISOU  208  C   ILE A  35     3855   3158   3753     73    -68   -330       C  
ATOM    209  O   ILE A  35      41.395 -14.160  -5.952  1.00 24.98           O  
ANISOU  209  O   ILE A  35     3430   2740   3320     42    -93   -350       O  
ATOM    210  CB  ILE A  35      43.651 -13.194  -3.641  1.00 23.03           C  
ANISOU  210  CB  ILE A  35     3133   2535   3082     76    -36   -233       C  
ATOM    211  CG1 ILE A  35      43.838 -13.290  -2.119  1.00 19.43           C  
ANISOU  211  CG1 ILE A  35     2655   2075   2651     64    -34   -176       C  
ATOM    212  CG2 ILE A  35      42.872 -11.955  -4.036  1.00 20.03           C  
ANISOU  212  CG2 ILE A  35     2744   2205   2659     57    -42   -239       C  
ATOM    213  CD1 ILE A  35      44.649 -12.165  -1.511  1.00 23.49           C  
ANISOU  213  CD1 ILE A  35     3143   2641   3140     76    -18   -145       C  
ATOM    214  N   VAL A  36      43.553 -14.483  -6.504  1.00 30.15           N  
ANISOU  214  N   VAL A  36     4105   3390   3962    118    -49   -360       N  
ATOM    215  CA  VAL A  36      43.288 -14.503  -7.937  1.00 26.17           C  
ANISOU  215  CA  VAL A  36     3630   2895   3418    135    -58   -421       C  
ATOM    216  C   VAL A  36      42.307 -15.626  -8.278  1.00 31.15           C  
ANISOU  216  C   VAL A  36     4284   3470   4083    111    -95   -467       C  
ATOM    217  O   VAL A  36      41.332 -15.407  -8.997  1.00 33.76           O  
ANISOU  217  O   VAL A  36     4620   3820   4386     90   -121   -498       O  
ATOM    218  CB  VAL A  36      44.585 -14.670  -8.751  1.00 29.42           C  
ANISOU  218  CB  VAL A  36     4059   3313   3806    192    -25   -444       C  
ATOM    219  CG1 VAL A  36      44.276 -14.922 -10.228  1.00 25.11           C  
ANISOU  219  CG1 VAL A  36     3547   2775   3217    210    -33   -506       C  
ATOM    220  CG2 VAL A  36      45.484 -13.452  -8.580  1.00 23.47           C  
ANISOU  220  CG2 VAL A  36     3279   2619   3021    210     10   -402       C  
ATOM    221  N   LYS A  37      42.541 -16.817  -7.733  1.00 30.13           N  
ANISOU  221  N   LYS A  37     4162   3274   4011    109    -97   -463       N  
ATOM    222  CA  LYS A  37      41.664 -17.958  -8.025  1.00 34.66           C  
ANISOU  222  CA  LYS A  37     4750   3802   4619     76   -121   -489       C  
ATOM    223  C   LYS A  37      40.249 -17.681  -7.559  1.00 27.54           C  
ANISOU  223  C   LYS A  37     3825   2905   3735     18   -152   -476       C  
ATOM    224  O   LYS A  37      39.288 -18.018  -8.253  1.00 31.59           O  
ANISOU  224  O   LYS A  37     4342   3418   4243     -9   -178   -511       O  
ATOM    225  CB  LYS A  37      42.166 -19.273  -7.394  1.00 39.30           C  
ANISOU  225  CB  LYS A  37     5347   4317   5268     82   -111   -473       C  
ATOM    226  CG  LYS A  37      43.413 -19.881  -8.041  1.00 55.32           C  
ANISOU  226  CG  LYS A  37     7400   6331   7288    138    -82   -497       C  
ATOM    227  CD  LYS A  37      43.203 -20.186  -9.517  1.00 63.65           C  
ANISOU  227  CD  LYS A  37     8482   7400   8303    148    -87   -561       C  
ATOM    228  N   ALA A  38      40.116 -17.070  -6.384  1.00 23.05           N  
ANISOU  228  N   ALA A  38     3228   2344   3184     -1   -149   -424       N  
ATOM    229  CA  ALA A  38      38.785 -16.836  -5.812  1.00 28.38           C  
ANISOU  229  CA  ALA A  38     3874   3029   3880    -57   -170   -402       C  
ATOM    230  C   ALA A  38      37.950 -15.887  -6.671  1.00 23.69           C  
ANISOU  230  C   ALA A  38     3272   2493   3236    -65   -192   -435       C  
ATOM    231  O   ALA A  38      36.764 -16.118  -6.898  1.00 23.60           O  
ANISOU  231  O   ALA A  38     3247   2477   3241   -104   -222   -453       O  
ATOM    232  CB  ALA A  38      38.883 -16.330  -4.371  1.00 21.86           C  
ANISOU  232  CB  ALA A  38     3016   2225   3064    -70   -146   -325       C  
ATOM    233  N   VAL A  39      38.587 -14.829  -7.158  1.00 23.57           N  
ANISOU  233  N   VAL A  39     3261   2536   3158    -29   -173   -434       N  
ATOM    234  CA  VAL A  39      37.930 -13.874  -8.045  1.00 25.65           C  
ANISOU  234  CA  VAL A  39     3522   2855   3368    -27   -191   -459       C  
ATOM    235  C   VAL A  39      37.508 -14.554  -9.344  1.00 30.94           C  
ANISOU  235  C   VAL A  39     4216   3518   4021    -23   -217   -519       C  
ATOM    236  O   VAL A  39      36.393 -14.342  -9.838  1.00 28.50           O  
ANISOU  236  O   VAL A  39     3896   3235   3700    -47   -248   -537       O  
ATOM    237  CB  VAL A  39      38.861 -12.685  -8.358  1.00 23.22           C  
ANISOU  237  CB  VAL A  39     3218   2604   3000     15   -159   -440       C  
ATOM    238  CG1 VAL A  39      38.301 -11.825  -9.477  1.00 16.16           C  
ANISOU  238  CG1 VAL A  39     2333   1762   2045     27   -176   -468       C  
ATOM    239  CG2 VAL A  39      39.091 -11.865  -7.098  1.00 17.52           C  
ANISOU  239  CG2 VAL A  39     2463   1906   2286      3   -133   -374       C  
ATOM    240  N   ALA A  40      38.402 -15.384  -9.879  1.00 28.98           N  
ANISOU  240  N   ALA A  40     3997   3241   3771      7   -199   -543       N  
ATOM    241  CA  ALA A  40      38.131 -16.144 -11.095  1.00 31.26           C  
ANISOU  241  CA  ALA A  40     4310   3524   4042     12   -215   -594       C  
ATOM    242  C   ALA A  40      36.924 -17.071 -10.928  1.00 35.02           C  
ANISOU  242  C   ALA A  40     4775   3960   4570    -40   -252   -610       C  
ATOM    243  O   ALA A  40      36.068 -17.171 -11.805  1.00 37.82           O  
ANISOU  243  O   ALA A  40     5132   4334   4905    -54   -283   -647       O  
ATOM    244  CB  ALA A  40      39.367 -16.946 -11.490  1.00 40.13           C  
ANISOU  244  CB  ALA A  40     5465   4617   5167     53   -185   -613       C  
ATOM    245  N   ARG A  41      36.864 -17.742  -9.786  1.00 34.59           N  
ANISOU  245  N   ARG A  41     4708   3852   4585    -69   -246   -578       N  
ATOM    246  CA  ARG A  41      35.770 -18.643  -9.468  1.00 30.64           C  
ANISOU  246  CA  ARG A  41     4192   3308   4142   -122   -273   -582       C  
ATOM    247  C   ARG A  41      34.437 -17.894  -9.357  1.00 35.92           C  
ANISOU  247  C   ARG A  41     4821   4020   4807   -162   -302   -574       C  
ATOM    248  O   ARG A  41      33.397 -18.412  -9.756  1.00 38.77           O  
ANISOU  248  O   ARG A  41     5170   4372   5187   -197   -334   -600       O  
ATOM    249  CB  ARG A  41      36.102 -19.397  -8.173  1.00 37.59           C  
ANISOU  249  CB  ARG A  41     5066   4125   5091   -140   -252   -534       C  
ATOM    250  CG  ARG A  41      35.021 -20.336  -7.653  1.00 48.40           C  
ANISOU  250  CG  ARG A  41     6416   5447   6526   -198   -270   -523       C  
ATOM    251  CD  ARG A  41      35.362 -20.823  -6.240  1.00 50.54           C  
ANISOU  251  CD  ARG A  41     6678   5668   6855   -211   -244   -459       C  
ATOM    252  N   VAL A  42      34.465 -16.675  -8.819  1.00 34.02           N  
ANISOU  252  N   VAL A  42     4557   3825   4542   -155   -293   -539       N  
ATOM    253  CA  VAL A  42      33.256 -15.856  -8.739  1.00 27.79           C  
ANISOU  253  CA  VAL A  42     3730   3083   3746   -184   -318   -531       C  
ATOM    254  C   VAL A  42      32.827 -15.462 -10.148  1.00 28.00           C  
ANISOU  254  C   VAL A  42     3767   3158   3712   -165   -346   -578       C  
ATOM    255  O   VAL A  42      31.648 -15.502 -10.482  1.00 26.40           O  
ANISOU  255  O   VAL A  42     3540   2972   3518   -195   -380   -594       O  
ATOM    256  CB  VAL A  42      33.471 -14.597  -7.859  1.00 30.71           C  
ANISOU  256  CB  VAL A  42     4078   3490   4101   -175   -299   -486       C  
ATOM    257  CG1 VAL A  42      32.336 -13.583  -8.045  1.00 24.36           C  
ANISOU  257  CG1 VAL A  42     3238   2745   3273   -189   -325   -486       C  
ATOM    258  CG2 VAL A  42      33.610 -14.989  -6.386  1.00 25.53           C  
ANISOU  258  CG2 VAL A  42     3402   2790   3508   -203   -278   -434       C  
ATOM    259  N   ALA A  43      33.804 -15.105 -10.978  1.00 30.38           N  
ANISOU  259  N   ALA A  43     4106   3483   3954   -114   -330   -596       N  
ATOM    260  CA  ALA A  43      33.550 -14.739 -12.372  1.00 32.11           C  
ANISOU  260  CA  ALA A  43     4343   3750   4109    -89   -351   -635       C  
ATOM    261  C   ALA A  43      32.978 -15.902 -13.182  1.00 41.80           C  
ANISOU  261  C   ALA A  43     5582   4947   5352   -108   -383   -686       C  
ATOM    262  O   ALA A  43      32.105 -15.709 -14.030  1.00 42.66           O  
ANISOU  262  O   ALA A  43     5685   5091   5433   -114   -419   -714       O  
ATOM    263  CB  ALA A  43      34.825 -14.213 -13.029  1.00 22.63           C  
ANISOU  263  CB  ALA A  43     3177   2575   2845    -31   -317   -637       C  
ATOM    264  N   GLU A  44      33.479 -17.106 -12.916  1.00 45.33           N  
ANISOU  264  N   GLU A  44     6049   5330   5846   -116   -370   -698       N  
ATOM    265  CA  GLU A  44      33.034 -18.299 -13.626  1.00 50.52           C  
ANISOU  265  CA  GLU A  44     6722   5949   6524   -135   -398   -749       C  
ATOM    266  C   GLU A  44      31.671 -18.795 -13.146  1.00 53.96           C  
ANISOU  266  C   GLU A  44     7119   6361   7021   -198   -433   -747       C  
ATOM    267  O   GLU A  44      31.050 -19.614 -13.800  1.00 52.38           O  
ANISOU  267  O   GLU A  44     6926   6140   6837   -220   -465   -791       O  
ATOM    268  CB  GLU A  44      34.086 -19.410 -13.546  1.00 49.97           C  
ANISOU  268  CB  GLU A  44     6690   5815   6482   -117   -370   -762       C  
ATOM    269  CG  GLU A  44      35.204 -19.272 -14.578  1.00 52.82           C  
ANISOU  269  CG  GLU A  44     7093   6200   6778    -56   -346   -792       C  
ATOM    270  N   SER A  45      31.212 -18.296 -12.003  1.00 57.90           N  
ANISOU  270  N   SER A  45     7576   6865   7556   -227   -425   -695       N  
ATOM    271  CA  SER A  45      29.852 -18.568 -11.550  1.00 56.37           C  
ANISOU  271  CA  SER A  45     7337   6665   7418   -286   -454   -686       C  
ATOM    272  C   SER A  45      28.934 -17.504 -12.152  1.00 60.29           C  
ANISOU  272  C   SER A  45     7804   7235   7867   -283   -486   -696       C  
ATOM    273  O   SER A  45      27.736 -17.449 -11.860  1.00 56.77           O  
ANISOU  273  O   SER A  45     7311   6802   7456   -325   -511   -687       O  
ATOM    274  CB  SER A  45      29.759 -18.588 -10.015  1.00 51.86           C  
ANISOU  274  CB  SER A  45     6732   6065   6908   -318   -425   -623       C  
ATOM    275  OG  SER A  45      29.815 -17.280  -9.462  1.00 52.27           O  
ANISOU  275  OG  SER A  45     6760   6170   6931   -303   -411   -584       O  
ATOM    276  N   GLY A  46      29.525 -16.658 -12.997  1.00 64.35           N  
ANISOU  276  N   GLY A  46     8346   7799   8304   -230   -483   -710       N  
ATOM    277  CA  GLY A  46      28.797 -15.657 -13.759  1.00 62.25           C  
ANISOU  277  CA  GLY A  46     8063   7604   7983   -216   -514   -720       C  
ATOM    278  C   GLY A  46      28.391 -14.405 -13.001  1.00 60.70           C  
ANISOU  278  C   GLY A  46     7827   7454   7783   -216   -506   -671       C  
ATOM    279  O   GLY A  46      27.450 -13.721 -13.409  1.00 62.36           O  
ANISOU  279  O   GLY A  46     8009   7714   7971   -217   -538   -674       O  
ATOM    280  N   GLY A  47      29.096 -14.100 -11.910  1.00 58.05           N  
ANISOU  280  N   GLY A  47     7488   7101   7467   -213   -466   -628       N  
ATOM    281  CA  GLY A  47      28.744 -12.978 -11.051  1.00 53.54           C  
ANISOU  281  CA  GLY A  47     6879   6566   6898   -216   -456   -583       C  
ATOM    282  C   GLY A  47      28.220 -13.383  -9.676  1.00 56.72           C  
ANISOU  282  C   GLY A  47     7238   6936   7379   -267   -444   -546       C  
ATOM    283  O   GLY A  47      28.922 -13.225  -8.677  1.00 50.04           O  
ANISOU  283  O   GLY A  47     6393   6068   6551   -264   -409   -510       O  
ATOM    284  N   GLY A  48      26.991 -13.907  -9.621  1.00 62.51           N  
ANISOU  284  N   GLY A  48     7929   7665   8158   -312   -471   -553       N  
ATOM    285  CA  GLY A  48      26.362 -14.282  -8.360  1.00 56.83           C  
ANISOU  285  CA  GLY A  48     7161   6919   7511   -363   -456   -512       C  
ATOM    286  C   GLY A  48      26.181 -13.074  -7.450  1.00 50.02           C  
ANISOU  286  C   GLY A  48     6262   6101   6644   -356   -436   -466       C  
ATOM    287  O   GLY A  48      25.688 -12.033  -7.884  1.00 47.63           O  
ANISOU  287  O   GLY A  48     5940   5857   6301   -334   -455   -472       O  
ATOM    288  N   ARG A  49      26.586 -13.185  -6.190  1.00 36.64           N  
ANISOU  288  N   ARG A  49     4556   4377   4988   -372   -397   -420       N  
ATOM    289  CA  ARG A  49      26.532 -12.016  -5.324  1.00 31.38           C  
ANISOU  289  CA  ARG A  49     3861   3755   4309   -360   -373   -377       C  
ATOM    290  C   ARG A  49      27.866 -11.307  -5.185  1.00 24.38           C  
ANISOU  290  C   ARG A  49     3021   2880   3361   -307   -335   -356       C  
ATOM    291  O   ARG A  49      28.019 -10.392  -4.384  1.00 32.04           O  
ANISOU  291  O   ARG A  49     3981   3886   4309   -289   -299   -310       O  
ATOM    292  CB  ARG A  49      25.886 -12.320  -3.974  1.00 39.83           C  
ANISOU  292  CB  ARG A  49     4881   4815   5437   -402   -340   -320       C  
ATOM    293  CG  ARG A  49      24.409 -12.004  -4.021  1.00 44.41           C  
ANISOU  293  CG  ARG A  49     5392   5437   6045   -431   -365   -323       C  
ATOM    294  CD  ARG A  49      23.723 -12.250  -2.725  1.00 48.08           C  
ANISOU  294  CD  ARG A  49     5804   5900   6564   -471   -326   -265       C  
ATOM    295  NE  ARG A  49      23.667 -11.069  -1.865  1.00 46.05           N  
ANISOU  295  NE  ARG A  49     5528   5701   6266   -439   -284   -217       N  
ATOM    296  CZ  ARG A  49      22.833 -10.047  -2.025  1.00 37.22           C  
ANISOU  296  CZ  ARG A  49     4369   4647   5127   -422   -294   -219       C  
ATOM    297  NH1 ARG A  49      21.999 -10.018  -3.053  1.00 36.62           N  
ANISOU  297  NH1 ARG A  49     4265   4590   5061   -430   -348   -265       N  
ATOM    298  NH2 ARG A  49      22.845  -9.041  -1.154  1.00 35.28           N  
ANISOU  298  NH2 ARG A  49     4112   4445   4848   -392   -251   -177       N  
ATOM    299  N   GLY A  50      28.823 -11.738  -5.991  1.00 20.52           N  
ANISOU  299  N   GLY A  50     2586   2363   2849   -282   -344   -392       N  
ATOM    300  CA  GLY A  50      30.049 -11.001  -6.179  1.00 22.76           C  
ANISOU  300  CA  GLY A  50     2911   2665   3072   -231   -315   -383       C  
ATOM    301  C   GLY A  50      31.058 -11.051  -5.054  1.00 20.82           C  
ANISOU  301  C   GLY A  50     2677   2399   2834   -223   -266   -333       C  
ATOM    302  O   GLY A  50      31.020 -11.916  -4.174  1.00 22.74           O  
ANISOU  302  O   GLY A  50     2909   2601   3129   -253   -252   -307       O  
ATOM    303  N   ALA A  51      31.973 -10.096  -5.104  1.00 16.25           N  
ANISOU  303  N   ALA A  51     2120   1851   2204   -181   -241   -318       N  
ATOM    304  CA  ALA A  51      33.117 -10.058  -4.216  1.00 15.63           C  
ANISOU  304  CA  ALA A  51     2056   1759   2124   -166   -201   -279       C  
ATOM    305  C   ALA A  51      33.485  -8.611  -3.960  1.00 20.28           C  
ANISOU  305  C   ALA A  51     2642   2398   2666   -137   -179   -253       C  
ATOM    306  O   ALA A  51      33.292  -7.752  -4.824  1.00 19.28           O  
ANISOU  306  O   ALA A  51     2521   2306   2500   -116   -191   -272       O  
ATOM    307  CB  ALA A  51      34.308 -10.813  -4.843  1.00  9.37           C  
ANISOU  307  CB  ALA A  51     1306    928   1327   -142   -197   -305       C  
ATOM    308  N   ILE A  52      33.998  -8.340  -2.765  1.00 17.47           N  
ANISOU  308  N   ILE A  52     2277   2045   2315   -136   -148   -210       N  
ATOM    309  CA  ILE A  52      34.577  -7.042  -2.467  1.00 13.79           C  
ANISOU  309  CA  ILE A  52     1813   1615   1810   -110   -127   -189       C  
ATOM    310  C   ILE A  52      35.786  -7.236  -1.559  1.00 17.00           C  
ANISOU  310  C   ILE A  52     2230   2007   2223   -100   -100   -161       C  
ATOM    311  O   ILE A  52      35.849  -8.198  -0.798  1.00 18.28           O  
ANISOU  311  O   ILE A  52     2388   2140   2417   -117    -95   -142       O  
ATOM    312  CB  ILE A  52      33.546  -6.080  -1.799  1.00 15.49           C  
ANISOU  312  CB  ILE A  52     1996   1870   2021   -118   -124   -168       C  
ATOM    313  CG1 ILE A  52      33.946  -4.624  -2.035  1.00 10.50           C  
ANISOU  313  CG1 ILE A  52     1372   1270   1346    -88   -113   -165       C  
ATOM    314  CG2 ILE A  52      33.360  -6.394  -0.307  1.00 11.29           C  
ANISOU  314  CG2 ILE A  52     1442   1334   1512   -138   -103   -129       C  
ATOM    315  CD1 ILE A  52      33.842  -4.188  -3.504  1.00  9.63           C  
ANISOU  315  CD1 ILE A  52     1280   1172   1206    -67   -133   -195       C  
ATOM    316  N   ALA A  53      36.744  -6.322  -1.642  1.00 16.83           N  
ANISOU  316  N   ALA A  53     2219   2004   2170    -74    -85   -155       N  
ATOM    317  CA  ALA A  53      37.897  -6.349  -0.750  1.00 14.41           C  
ANISOU  317  CA  ALA A  53     1916   1693   1868    -64    -64   -130       C  
ATOM    318  C   ALA A  53      37.571  -5.730   0.601  1.00 16.51           C  
ANISOU  318  C   ALA A  53     2160   1982   2130    -73    -54    -98       C  
ATOM    319  O   ALA A  53      36.682  -4.892   0.727  1.00 13.51           O  
ANISOU  319  O   ALA A  53     1766   1629   1737    -78    -56    -97       O  
ATOM    320  CB  ALA A  53      39.078  -5.626  -1.381  1.00 11.68           C  
ANISOU  320  CB  ALA A  53     1584   1358   1497    -36    -52   -138       C  
ATOM    321  N   ARG A  54      38.311  -6.142   1.616  1.00 12.54           N  
ANISOU  321  N   ARG A  54     1657   1471   1636    -71    -44    -72       N  
ATOM    322  CA  ARG A  54      38.196  -5.509   2.908  1.00  9.99           C  
ANISOU  322  CA  ARG A  54     1320   1176   1300    -73    -35    -45       C  
ATOM    323  C   ARG A  54      39.586  -5.279   3.466  1.00 15.30           C  
ANISOU  323  C   ARG A  54     1997   1852   1962    -55    -29    -34       C  
ATOM    324  O   ARG A  54      40.441  -6.151   3.377  1.00 14.26           O  
ANISOU  324  O   ARG A  54     1874   1697   1848    -46    -30    -29       O  
ATOM    325  CB  ARG A  54      37.370  -6.372   3.861  1.00  5.87           C  
ANISOU  325  CB  ARG A  54      786    648    797    -95    -31    -17       C  
ATOM    326  CG  ARG A  54      37.211  -5.795   5.254  1.00  7.76           C  
ANISOU  326  CG  ARG A  54     1014    921   1014    -93    -19     11       C  
ATOM    327  CD  ARG A  54      36.198  -6.612   6.030  1.00 16.95           C  
ANISOU  327  CD  ARG A  54     2163   2082   2195   -115     -9     43       C  
ATOM    328  NE  ARG A  54      35.991  -6.140   7.392  1.00 21.05           N  
ANISOU  328  NE  ARG A  54     2674   2639   2686   -110      7     71       N  
ATOM    329  CZ  ARG A  54      34.950  -5.424   7.799  1.00 20.24           C  
ANISOU  329  CZ  ARG A  54     2553   2571   2567   -114     19     72       C  
ATOM    330  NH1 ARG A  54      33.990  -5.083   6.951  1.00 24.05           N  
ANISOU  330  NH1 ARG A  54     3019   3055   3063   -124     14     49       N  
ATOM    331  NH2 ARG A  54      34.873  -5.054   9.066  1.00 16.65           N  
ANISOU  331  NH2 ARG A  54     2095   2151   2081   -103     35     95       N  
ATOM    332  N   GLY A  55      39.802  -4.102   4.043  1.00 17.38           N  
ANISOU  332  N   GLY A  55     2254   2146   2203    -48    -26    -32       N  
ATOM    333  CA  GLY A  55      41.062  -3.808   4.702  1.00 20.85           C  
ANISOU  333  CA  GLY A  55     2693   2595   2636    -35    -26    -24       C  
ATOM    334  C   GLY A  55      40.932  -3.976   6.199  1.00 18.07           C  
ANISOU  334  C   GLY A  55     2334   2261   2270    -36    -27      3       C  
ATOM    335  O   GLY A  55      40.555  -5.042   6.685  1.00 16.60           O  
ANISOU  335  O   GLY A  55     2149   2064   2095    -43    -24     28       O  
ATOM    336  N   LEU A  56      41.216  -2.911   6.936  1.00 12.53           N  
ANISOU  336  N   LEU A  56     1628   1588   1544    -31    -29     -2       N  
ATOM    337  CA  LEU A  56      41.154  -2.984   8.389  1.00 14.83           C  
ANISOU  337  CA  LEU A  56     1916   1905   1812    -27    -32     20       C  
ATOM    338  C   LEU A  56      39.777  -2.637   8.963  1.00 17.90           C  
ANISOU  338  C   LEU A  56     2303   2318   2182    -34    -19     25       C  
ATOM    339  O   LEU A  56      39.590  -2.593  10.180  1.00 18.61           O  
ANISOU  339  O   LEU A  56     2392   2435   2243    -28    -16     42       O  
ATOM    340  CB  LEU A  56      42.247  -2.116   8.999  1.00 17.35           C  
ANISOU  340  CB  LEU A  56     2232   2245   2114    -15    -46      7       C  
ATOM    341  CG  LEU A  56      43.602  -2.820   9.091  1.00 18.42           C  
ANISOU  341  CG  LEU A  56     2363   2371   2264     -4    -59     19       C  
ATOM    342  CD1 LEU A  56      44.698  -1.815   9.393  1.00 14.19           C  
ANISOU  342  CD1 LEU A  56     1815   1853   1722      2    -76     -2       C  
ATOM    343  CD2 LEU A  56      43.528  -3.909  10.178  1.00  9.36           C  
ANISOU  343  CD2 LEU A  56     1219   1232   1104      5    -62     58       C  
ATOM    344  N   GLY A  57      38.815  -2.408   8.077  1.00 15.69           N  
ANISOU  344  N   GLY A  57     2018   2028   1914    -44    -12     10       N  
ATOM    345  CA  GLY A  57      37.446  -2.131   8.471  1.00 15.32           C  
ANISOU  345  CA  GLY A  57     1962   2004   1857    -50      1     15       C  
ATOM    346  C   GLY A  57      37.250  -0.796   9.180  1.00 22.79           C  
ANISOU  346  C   GLY A  57     2907   2982   2770    -36      5     -2       C  
ATOM    347  O   GLY A  57      36.359  -0.676  10.022  1.00 15.73           O  
ANISOU  347  O   GLY A  57     2004   2115   1856    -33     20      9       O  
ATOM    348  N   ARG A  58      38.069   0.209   8.864  1.00 14.21           N  
ANISOU  348  N   ARG A  58     1829   1890   1679    -26     -7    -29       N  
ATOM    349  CA  ARG A  58      37.930   1.489   9.561  1.00 17.55           C  
ANISOU  349  CA  ARG A  58     2256   2337   2076    -13     -6    -51       C  
ATOM    350  C   ARG A  58      36.850   2.376   8.953  1.00 14.64           C  
ANISOU  350  C   ARG A  58     1882   1968   1712     -7      3    -69       C  
ATOM    351  O   ARG A  58      36.443   3.372   9.545  1.00 14.16           O  
ANISOU  351  O   ARG A  58     1824   1925   1631      7      8    -86       O  
ATOM    352  CB  ARG A  58      39.268   2.237   9.696  1.00 13.15           C  
ANISOU  352  CB  ARG A  58     1707   1772   1516     -8    -23    -72       C  
ATOM    353  CG  ARG A  58      39.928   2.047  11.067  1.00 11.54           C  
ANISOU  353  CG  ARG A  58     1507   1595   1282      0    -35    -67       C  
ATOM    354  CD  ARG A  58      40.296   0.581  11.343  1.00 10.58           C  
ANISOU  354  CD  ARG A  58     1382   1473   1164     -4    -36    -29       C  
ATOM    355  NE  ARG A  58      41.034   0.448  12.595  1.00 17.55           N  
ANISOU  355  NE  ARG A  58     2269   2383   2015      9    -52    -21       N  
ATOM    356  CZ  ARG A  58      41.319  -0.707  13.194  1.00 23.70           C  
ANISOU  356  CZ  ARG A  58     3049   3171   2786     14    -54     16       C  
ATOM    357  NH1 ARG A  58      40.924  -1.866  12.669  1.00 24.32           N  
ANISOU  357  NH1 ARG A  58     3124   3224   2891      4    -40     48       N  
ATOM    358  NH2 ARG A  58      42.005  -0.704  14.333  1.00 25.75           N  
ANISOU  358  NH2 ARG A  58     3313   3461   3010     29    -73     21       N  
ATOM    359  N   SER A  59      36.381   2.009   7.772  1.00 18.39           N  
ANISOU  359  N   SER A  59     2352   2425   2211    -16      3    -66       N  
ATOM    360  CA  SER A  59      35.261   2.720   7.173  1.00 15.98           C  
ANISOU  360  CA  SER A  59     2038   2124   1910     -8      8    -77       C  
ATOM    361  C   SER A  59      34.016   2.520   8.056  1.00 19.67           C  
ANISOU  361  C   SER A  59     2485   2623   2365     -5     25    -65       C  
ATOM    362  O   SER A  59      33.758   1.412   8.549  1.00 11.48           O  
ANISOU  362  O   SER A  59     1437   1594   1331    -19     33    -39       O  
ATOM    363  CB  SER A  59      35.046   2.247   5.731  1.00 10.41           C  
ANISOU  363  CB  SER A  59     1330   1397   1228    -17     -1    -77       C  
ATOM    364  OG  SER A  59      33.824   2.719   5.210  1.00 22.58           O  
ANISOU  364  OG  SER A  59     2857   2949   2772     -8      0    -84       O  
ATOM    365  N   TYR A  60      33.282   3.603   8.302  1.00 15.37           N  
ANISOU  365  N   TYR A  60     1936   2095   1809     15     34    -81       N  
ATOM    366  CA  TYR A  60      32.063   3.528   9.104  1.00 17.87           C  
ANISOU  366  CA  TYR A  60     2229   2447   2114     23     55    -71       C  
ATOM    367  C   TYR A  60      30.904   2.951   8.311  1.00 24.23           C  
ANISOU  367  C   TYR A  60     3003   3256   2947     11     57    -58       C  
ATOM    368  O   TYR A  60      29.886   2.576   8.880  1.00 28.65           O  
ANISOU  368  O   TYR A  60     3534   3844   3508      8     76    -42       O  
ATOM    369  CB  TYR A  60      31.671   4.906   9.636  1.00 14.75           C  
ANISOU  369  CB  TYR A  60     1838   2068   1697     55     65    -97       C  
ATOM    370  CG  TYR A  60      32.556   5.415  10.760  1.00 26.78           C  
ANISOU  370  CG  TYR A  60     3388   3600   3189     66     65   -113       C  
ATOM    371  CD1 TYR A  60      32.080   5.472  12.067  1.00 25.42           C  
ANISOU  371  CD1 TYR A  60     3211   3467   2979     83     86   -111       C  
ATOM    372  CD2 TYR A  60      33.874   5.838  10.515  1.00 24.79           C  
ANISOU  372  CD2 TYR A  60     3161   3318   2941     61     42   -131       C  
ATOM    373  CE1 TYR A  60      32.873   5.946  13.100  1.00 36.24           C  
ANISOU  373  CE1 TYR A  60     4607   4849   4314     96     80   -132       C  
ATOM    374  CE2 TYR A  60      34.677   6.312  11.544  1.00 27.27           C  
ANISOU  374  CE2 TYR A  60     3494   3641   3227     69     35   -151       C  
ATOM    375  CZ  TYR A  60      34.169   6.363  12.839  1.00 36.05           C  
ANISOU  375  CZ  TYR A  60     4606   4793   4297     88     52   -153       C  
ATOM    376  OH  TYR A  60      34.941   6.825  13.883  1.00 31.24           O  
ANISOU  376  OH  TYR A  60     4018   4197   3654     99     39   -178       O  
ATOM    377  N   GLY A  61      31.066   2.878   6.996  1.00 21.18           N  
ANISOU  377  N   GLY A  61     2621   2842   2583      4     35    -67       N  
ATOM    378  CA  GLY A  61      29.988   2.455   6.134  1.00 20.27           C  
ANISOU  378  CA  GLY A  61     2478   2732   2493     -6     27    -64       C  
ATOM    379  C   GLY A  61      29.882   0.964   5.866  1.00 19.60           C  
ANISOU  379  C   GLY A  61     2379   2634   2433    -40     21    -46       C  
ATOM    380  O   GLY A  61      30.452   0.125   6.569  1.00 14.73           O  
ANISOU  380  O   GLY A  61     1771   2009   1815    -56     30    -27       O  
ATOM    381  N   ASP A  62      29.140   0.651   4.816  1.00 12.71           N  
ANISOU  381  N   ASP A  62     1487   1757   1584    -50      2    -54       N  
ATOM    382  CA  ASP A  62      28.889  -0.718   4.413  1.00 17.09           C  
ANISOU  382  CA  ASP A  62     2028   2295   2170    -84     -9    -45       C  
ATOM    383  C   ASP A  62      29.598  -1.025   3.080  1.00 13.97           C  
ANISOU  383  C   ASP A  62     1661   1868   1779    -86    -38    -67       C  
ATOM    384  O   ASP A  62      29.195  -1.923   2.330  1.00 15.18           O  
ANISOU  384  O   ASP A  62     1804   2007   1957   -108    -58    -76       O  
ATOM    385  CB  ASP A  62      27.369  -0.960   4.308  1.00 18.88           C  
ANISOU  385  CB  ASP A  62     2205   2546   2424    -97    -11    -41       C  
ATOM    386  CG  ASP A  62      26.678   0.006   3.330  1.00 18.46           C  
ANISOU  386  CG  ASP A  62     2138   2510   2366    -72    -33    -65       C  
ATOM    387  OD1 ASP A  62      27.302   1.014   2.937  1.00 14.32           O  
ANISOU  387  OD1 ASP A  62     1645   1980   1815    -42    -38    -79       O  
ATOM    388  OD2 ASP A  62      25.513  -0.250   2.952  1.00 17.68           O  
ANISOU  388  OD2 ASP A  62     1996   2429   2294    -84    -46    -68       O  
ATOM    389  N   ASN A  63      30.674  -0.297   2.802  1.00 11.17           N  
ANISOU  389  N   ASN A  63     1341   1502   1399    -65    -39    -77       N  
ATOM    390  CA  ASN A  63      31.424  -0.504   1.558  1.00 13.64           C  
ANISOU  390  CA  ASN A  63     1682   1791   1710    -61    -59    -95       C  
ATOM    391  C   ASN A  63      32.428  -1.664   1.598  1.00 11.48           C  
ANISOU  391  C   ASN A  63     1428   1486   1448    -78    -58    -91       C  
ATOM    392  O   ASN A  63      32.860  -2.150   0.557  1.00 17.84           O  
ANISOU  392  O   ASN A  63     2250   2271   2256    -78    -73   -108       O  
ATOM    393  CB  ASN A  63      32.095   0.798   1.090  1.00  7.56           C  
ANISOU  393  CB  ASN A  63      937   1021    914    -32    -57   -104       C  
ATOM    394  CG  ASN A  63      32.871   1.489   2.207  1.00 20.18           C  
ANISOU  394  CG  ASN A  63     2546   2621   2500    -23    -36    -95       C  
ATOM    395  OD1 ASN A  63      32.698   1.176   3.394  1.00 19.22           O  
ANISOU  395  OD1 ASN A  63     2411   2510   2380    -32    -22    -81       O  
ATOM    396  ND2 ASN A  63      33.722   2.433   1.835  1.00 17.06           N  
ANISOU  396  ND2 ASN A  63     2174   2216   2092     -6    -33   -101       N  
ATOM    397  N   ALA A  64      32.785  -2.114   2.796  1.00 12.87           N  
ANISOU  397  N   ALA A  64     1601   1660   1629    -88    -40    -68       N  
ATOM    398  CA  ALA A  64      33.720  -3.235   2.940  1.00 14.99           C  
ANISOU  398  CA  ALA A  64     1886   1897   1911    -99    -39    -59       C  
ATOM    399  C   ALA A  64      33.026  -4.507   3.408  1.00 21.28           C  
ANISOU  399  C   ALA A  64     2665   2681   2741   -128    -37    -40       C  
ATOM    400  O   ALA A  64      33.601  -5.298   4.157  1.00 20.60           O  
ANISOU  400  O   ALA A  64     2587   2577   2664   -135    -27    -16       O  
ATOM    401  CB  ALA A  64      34.833  -2.876   3.897  1.00 14.59           C  
ANISOU  401  CB  ALA A  64     1850   1852   1843    -86    -25    -44       C  
ATOM    402  N   GLN A  65      31.781  -4.689   2.987  1.00 20.64           N  
ANISOU  402  N   GLN A  65     2558   2607   2680   -145    -47    -48       N  
ATOM    403  CA  GLN A  65      31.069  -5.918   3.275  1.00 18.53           C  
ANISOU  403  CA  GLN A  65     2269   2319   2453   -180    -47    -32       C  
ATOM    404  C   GLN A  65      30.186  -6.239   2.087  1.00 15.59           C  
ANISOU  404  C   GLN A  65     1881   1938   2105   -196    -77    -63       C  
ATOM    405  O   GLN A  65      29.953  -5.391   1.239  1.00 19.38           O  
ANISOU  405  O   GLN A  65     2361   2440   2564   -177    -94    -90       O  
ATOM    406  CB  GLN A  65      30.255  -5.805   4.558  1.00 14.17           C  
ANISOU  406  CB  GLN A  65     1686   1797   1903   -190    -19      5       C  
ATOM    407  CG  GLN A  65      29.332  -4.624   4.592  1.00 17.86           C  
ANISOU  407  CG  GLN A  65     2125   2309   2351   -175    -15     -4       C  
ATOM    408  CD  GLN A  65      28.822  -4.340   5.981  1.00 21.74           C  
ANISOU  408  CD  GLN A  65     2594   2836   2830   -172     21     30       C  
ATOM    409  OE1 GLN A  65      29.348  -3.479   6.681  1.00 28.45           O  
ANISOU  409  OE1 GLN A  65     3461   3708   3640   -144     36     33       O  
ATOM    410  NE2 GLN A  65      27.790  -5.064   6.391  1.00 27.72           N  
ANISOU  410  NE2 GLN A  65     3313   3599   3621   -202     35     55       N  
ATOM    411  N   ASN A  66      29.726  -7.476   2.012  1.00 10.93           N  
ANISOU  411  N   ASN A  66     1277   1314   1560   -232    -85    -61       N  
ATOM    412  CA  ASN A  66      28.971  -7.925   0.856  1.00 14.50           C  
ANISOU  412  CA  ASN A  66     1717   1754   2039   -251   -121    -98       C  
ATOM    413  C   ASN A  66      28.043  -9.052   1.280  1.00 17.92           C  
ANISOU  413  C   ASN A  66     2114   2162   2531   -300   -121    -81       C  
ATOM    414  O   ASN A  66      28.418 -10.233   1.198  1.00 14.04           O  
ANISOU  414  O   ASN A  66     1641   1617   2076   -322   -126    -82       O  
ATOM    415  CB  ASN A  66      29.923  -8.420  -0.234  1.00 12.98           C  
ANISOU  415  CB  ASN A  66     1568   1524   1838   -239   -144   -135       C  
ATOM    416  CG  ASN A  66      29.200  -8.763  -1.520  1.00 16.08           C  
ANISOU  416  CG  ASN A  66     1954   1911   2246   -251   -188   -183       C  
ATOM    417  OD1 ASN A  66      28.101  -8.272  -1.771  1.00 14.85           O  
ANISOU  417  OD1 ASN A  66     1761   1789   2092   -259   -205   -192       O  
ATOM    418  ND2 ASN A  66      29.811  -9.613  -2.340  1.00 16.38           N  
ANISOU  418  ND2 ASN A  66     2026   1907   2291   -251   -207   -217       N  
ATOM    419  N   GLY A  67      26.847  -8.687   1.742  1.00 18.44           N  
ANISOU  419  N   GLY A  67     2129   2265   2612   -315   -112    -64       N  
ATOM    420  CA  GLY A  67      25.930  -9.648   2.336  1.00 16.75           C  
ANISOU  420  CA  GLY A  67     1873   2034   2458   -364   -101    -36       C  
ATOM    421  C   GLY A  67      25.641 -10.772   1.366  1.00 17.79           C  
ANISOU  421  C   GLY A  67     2003   2114   2642   -402   -141    -72       C  
ATOM    422  O   GLY A  67      25.287 -10.507   0.234  1.00 17.92           O  
ANISOU  422  O   GLY A  67     2015   2141   2651   -397   -183   -121       O  
ATOM    423  N   GLY A  68      25.854 -12.016   1.788  1.00 16.77           N  
ANISOU  423  N   GLY A  68     1884   1927   2562   -436   -131    -50       N  
ATOM    424  CA  GLY A  68      25.546 -13.169   0.955  1.00 14.71           C  
ANISOU  424  CA  GLY A  68     1622   1608   2360   -476   -168    -87       C  
ATOM    425  C   GLY A  68      26.568 -13.482  -0.126  1.00 23.59           C  
ANISOU  425  C   GLY A  68     2805   2693   3464   -451   -201   -140       C  
ATOM    426  O   GLY A  68      26.375 -14.398  -0.942  1.00 20.44           O  
ANISOU  426  O   GLY A  68     2414   2246   3108   -478   -238   -183       O  
ATOM    427  N   GLY A  69      27.659 -12.724  -0.140  1.00 19.84           N  
ANISOU  427  N   GLY A  69     2372   2241   2925   -399   -187   -139       N  
ATOM    428  CA  GLY A  69      28.677 -12.904  -1.154  1.00 12.88           C  
ANISOU  428  CA  GLY A  69     1543   1333   2017   -369   -209   -186       C  
ATOM    429  C   GLY A  69      30.056 -13.099  -0.561  1.00 11.79           C  
ANISOU  429  C   GLY A  69     1448   1171   1861   -339   -178   -157       C  
ATOM    430  O   GLY A  69      30.188 -13.469   0.599  1.00 12.97           O  
ANISOU  430  O   GLY A  69     1591   1306   2032   -351   -146   -103       O  
ATOM    431  N   LEU A  70      31.078 -12.829  -1.365  1.00 14.06           N  
ANISOU  431  N   LEU A  70     1777   1458   2108   -299   -186   -191       N  
ATOM    432  CA  LEU A  70      32.459 -12.991  -0.946  1.00 12.64           C  
ANISOU  432  CA  LEU A  70     1632   1258   1911   -267   -161   -170       C  
ATOM    433  C   LEU A  70      33.081 -11.661  -0.499  1.00 18.39           C  
ANISOU  433  C   LEU A  70     2363   2045   2582   -230   -137   -146       C  
ATOM    434  O   LEU A  70      32.903 -10.633  -1.146  1.00 21.06           O  
ANISOU  434  O   LEU A  70     2698   2426   2880   -212   -147   -169       O  
ATOM    435  CB  LEU A  70      33.290 -13.596  -2.082  1.00 11.65           C  
ANISOU  435  CB  LEU A  70     1549   1094   1782   -244   -179   -221       C  
ATOM    436  CG  LEU A  70      34.789 -13.799  -1.790  1.00 24.92           C  
ANISOU  436  CG  LEU A  70     3264   2755   3449   -205   -155   -204       C  
ATOM    437  CD1 LEU A  70      35.000 -14.865  -0.726  1.00 21.00           C  
ANISOU  437  CD1 LEU A  70     2768   2207   3004   -222   -138   -159       C  
ATOM    438  CD2 LEU A  70      35.569 -14.156  -3.052  1.00 27.14           C  
ANISOU  438  CD2 LEU A  70     3583   3014   3715   -174   -168   -260       C  
ATOM    439  N   VAL A  71      33.794 -11.692   0.623  1.00 16.97           N  
ANISOU  439  N   VAL A  71     2187   1863   2399   -220   -108   -100       N  
ATOM    440  CA  VAL A  71      34.620 -10.575   1.061  1.00 19.89           C  
ANISOU  440  CA  VAL A  71     2562   2275   2719   -186    -89    -83       C  
ATOM    441  C   VAL A  71      36.046 -11.091   1.207  1.00 22.79           C  
ANISOU  441  C   VAL A  71     2959   2614   3086   -159    -79    -75       C  
ATOM    442  O   VAL A  71      36.272 -12.132   1.819  1.00 17.97           O  
ANISOU  442  O   VAL A  71     2354   1962   2510   -168    -73    -48       O  
ATOM    443  CB  VAL A  71      34.162  -9.993   2.413  1.00 15.87           C  
ANISOU  443  CB  VAL A  71     2027   1804   2199   -193    -67    -36       C  
ATOM    444  CG1 VAL A  71      35.300  -9.185   3.063  1.00  7.89           C  
ANISOU  444  CG1 VAL A  71     1029    820   1147   -160    -50    -19       C  
ATOM    445  CG2 VAL A  71      32.891  -9.139   2.244  1.00 12.13           C  
ANISOU  445  CG2 VAL A  71     1522   1372   1715   -206    -72    -46       C  
ATOM    446  N   ILE A  72      37.009 -10.379   0.632  1.00 21.58           N  
ANISOU  446  N   ILE A  72     2821   2481   2898   -126    -77    -95       N  
ATOM    447  CA  ILE A  72      38.394 -10.809   0.728  1.00 19.17           C  
ANISOU  447  CA  ILE A  72     2536   2153   2594    -97    -67    -88       C  
ATOM    448  C   ILE A  72      39.191  -9.922   1.664  1.00 12.58           C  
ANISOU  448  C   ILE A  72     1692   1356   1731    -79    -51    -57       C  
ATOM    449  O   ILE A  72      39.458  -8.770   1.356  1.00 19.21           O  
ANISOU  449  O   ILE A  72     2528   2232   2538    -66    -48    -69       O  
ATOM    450  CB  ILE A  72      39.049 -10.896  -0.655  1.00 16.74           C  
ANISOU  450  CB  ILE A  72     2251   1833   2275    -73    -74   -135       C  
ATOM    451  CG1 ILE A  72      38.228 -11.842  -1.527  1.00 13.94           C  
ANISOU  451  CG1 ILE A  72     1908   1440   1949    -92    -96   -172       C  
ATOM    452  CG2 ILE A  72      40.491 -11.393  -0.533  1.00 18.06           C  
ANISOU  452  CG2 ILE A  72     2433   1980   2451    -40    -60   -126       C  
ATOM    453  CD1 ILE A  72      38.778 -12.081  -2.889  1.00 17.80           C  
ANISOU  453  CD1 ILE A  72     2424   1916   2422    -65   -103   -222       C  
ATOM    454  N   ASP A  73      39.515 -10.465   2.834  1.00 12.96           N  
ANISOU  454  N   ASP A  73     1737   1395   1793    -79    -43    -16       N  
ATOM    455  CA  ASP A  73      40.340  -9.779   3.813  1.00 16.54           C  
ANISOU  455  CA  ASP A  73     2182   1882   2220    -61    -35     11       C  
ATOM    456  C   ASP A  73      41.733  -9.649   3.231  1.00 15.88           C  
ANISOU  456  C   ASP A  73     2106   1795   2131    -29    -34     -6       C  
ATOM    457  O   ASP A  73      42.428 -10.642   3.097  1.00 14.31           O  
ANISOU  457  O   ASP A  73     1919   1561   1957    -13    -34     -3       O  
ATOM    458  CB  ASP A  73      40.422 -10.610   5.090  1.00 26.30           C  
ANISOU  458  CB  ASP A  73     3418   3105   3470    -63    -29     60       C  
ATOM    459  CG  ASP A  73      41.291  -9.965   6.184  1.00 32.53           C  
ANISOU  459  CG  ASP A  73     4200   3934   4227    -42    -27     86       C  
ATOM    460  OD1 ASP A  73      42.010  -8.972   5.927  1.00 19.81           O  
ANISOU  460  OD1 ASP A  73     2582   2351   2592    -26    -30     64       O  
ATOM    461  OD2 ASP A  73      41.254 -10.481   7.326  1.00 39.21           O  
ANISOU  461  OD2 ASP A  73     5046   4781   5072    -41    -23    130       O  
ATOM    462  N   MET A  74      42.134  -8.420   2.917  1.00 19.35           N  
ANISOU  462  N   MET A  74     2539   2271   2541    -20    -31    -23       N  
ATOM    463  CA  MET A  74      43.433  -8.130   2.311  1.00 15.81           C  
ANISOU  463  CA  MET A  74     2091   1827   2089      7    -25    -38       C  
ATOM    464  C   MET A  74      44.565  -7.893   3.324  1.00 16.35           C  
ANISOU  464  C   MET A  74     2144   1915   2155     23    -25    -12       C  
ATOM    465  O   MET A  74      45.726  -7.742   2.931  1.00 16.88           O  
ANISOU  465  O   MET A  74     2202   1984   2225     44    -20    -20       O  
ATOM    466  CB  MET A  74      43.313  -6.916   1.382  1.00 10.09           C  
ANISOU  466  CB  MET A  74     1366   1127   1339      7    -19    -64       C  
ATOM    467  CG  MET A  74      42.376  -7.143   0.206  1.00  8.03           C  
ANISOU  467  CG  MET A  74     1121    853   1076     -1    -24    -93       C  
ATOM    468  SD  MET A  74      42.981  -8.486  -0.836  1.00 20.32           S  
ANISOU  468  SD  MET A  74     2699   2367   2654     20    -22   -119       S  
ATOM    469  CE  MET A  74      44.489  -7.770  -1.470  1.00 16.19           C  
ANISOU  469  CE  MET A  74     2171   1866   2114     52      0   -125       C  
ATOM    470  N   THR A  75      44.243  -7.847   4.616  1.00 15.34           N  
ANISOU  470  N   THR A  75     2008   1802   2017     14    -32     17       N  
ATOM    471  CA  THR A  75      45.276  -7.653   5.643  1.00 16.68           C  
ANISOU  471  CA  THR A  75     2164   1995   2179     30    -40     39       C  
ATOM    472  C   THR A  75      46.435  -8.673   5.669  1.00 18.98           C  
ANISOU  472  C   THR A  75     2453   2263   2497     59    -43     53       C  
ATOM    473  O   THR A  75      47.501  -8.351   6.168  1.00 22.57           O  
ANISOU  473  O   THR A  75     2889   2740   2947     76    -52     61       O  
ATOM    474  CB  THR A  75      44.697  -7.484   7.086  1.00 19.47           C  
ANISOU  474  CB  THR A  75     2515   2374   2508     21    -47     70       C  
ATOM    475  OG1 THR A  75      44.109  -8.707   7.527  1.00 14.60           O  
ANISOU  475  OG1 THR A  75     1910   1729   1907     17    -44    101       O  
ATOM    476  CG2 THR A  75      43.671  -6.358   7.143  1.00 14.99           C  
ANISOU  476  CG2 THR A  75     1946   1834   1915      1    -42     54       C  
ATOM    477  N   PRO A  76      46.239  -9.900   5.143  1.00 22.60           N  
ANISOU  477  N   PRO A  76     2929   2675   2984     65    -38     55       N  
ATOM    478  CA  PRO A  76      47.446 -10.736   5.131  1.00 14.72           C  
ANISOU  478  CA  PRO A  76     1925   1655   2010     99    -40     65       C  
ATOM    479  C   PRO A  76      48.442 -10.417   4.012  1.00 23.93           C  
ANISOU  479  C   PRO A  76     3081   2825   3185    120    -28     33       C  
ATOM    480  O   PRO A  76      49.592 -10.854   4.116  1.00 26.14           O  
ANISOU  480  O   PRO A  76     3347   3103   3483    152    -29     42       O  
ATOM    481  CB  PRO A  76      46.896 -12.159   4.953  1.00 17.52           C  
ANISOU  481  CB  PRO A  76     2306   1952   2399     99    -38     75       C  
ATOM    482  CG  PRO A  76      45.480 -12.088   5.394  1.00 20.86           C  
ANISOU  482  CG  PRO A  76     2738   2375   2812     62    -38     88       C  
ATOM    483  CD  PRO A  76      45.026 -10.716   4.957  1.00 19.17           C  
ANISOU  483  CD  PRO A  76     2514   2204   2566     43    -35     58       C  
ATOM    484  N   LEU A  77      48.034  -9.708   2.964  1.00 19.09           N  
ANISOU  484  N   LEU A  77     2474   2221   2559    107    -16     -1       N  
ATOM    485  CA  LEU A  77      49.003  -9.247   1.969  1.00 19.96           C  
ANISOU  485  CA  LEU A  77     2571   2342   2669    126      0    -25       C  
ATOM    486  C   LEU A  77      49.647  -7.962   2.485  1.00 25.52           C  
ANISOU  486  C   LEU A  77     3245   3092   3359    119     -2    -17       C  
ATOM    487  O   LEU A  77      49.199  -6.853   2.156  1.00 17.91           O  
ANISOU  487  O   LEU A  77     2281   2149   2375     98      3    -31       O  
ATOM    488  CB  LEU A  77      48.327  -8.954   0.633  1.00 25.72           C  
ANISOU  488  CB  LEU A  77     3323   3066   3384    117     14    -60       C  
ATOM    489  CG  LEU A  77      48.022 -10.061  -0.354  1.00 33.17           C  
ANISOU  489  CG  LEU A  77     4295   3968   4341    131     20    -87       C  
ATOM    490  CD1 LEU A  77      47.696  -9.402  -1.676  1.00 34.01           C  
ANISOU  490  CD1 LEU A  77     4415   4089   4419    130     33   -120       C  
ATOM    491  CD2 LEU A  77      49.212 -10.976  -0.486  1.00 36.04           C  
ANISOU  491  CD2 LEU A  77     4653   4310   4731    171     30    -86       C  
ATOM    492  N   ASN A  78      50.689  -8.099   3.295  1.00 19.72           N  
ANISOU  492  N   ASN A  78     2483   2371   2638    137    -13      3       N  
ATOM    493  CA  ASN A  78      51.251  -6.945   3.985  1.00 16.60           C  
ANISOU  493  CA  ASN A  78     2058   2017   2233    125    -25      8       C  
ATOM    494  C   ASN A  78      52.774  -6.830   3.805  1.00 21.76           C  
ANISOU  494  C   ASN A  78     2671   2687   2911    148    -20      8       C  
ATOM    495  O   ASN A  78      53.494  -6.393   4.707  1.00 15.89           O  
ANISOU  495  O   ASN A  78     1896   1972   2171    148    -41     19       O  
ATOM    496  CB  ASN A  78      50.881  -7.015   5.463  1.00 14.51           C  
ANISOU  496  CB  ASN A  78     1794   1767   1952    117    -53     33       C  
ATOM    497  CG  ASN A  78      51.511  -8.209   6.170  1.00 18.85           C  
ANISOU  497  CG  ASN A  78     2338   2305   2518    148    -67     62       C  
ATOM    498  OD1 ASN A  78      51.973  -9.153   5.536  1.00 22.58           O  
ANISOU  498  OD1 ASN A  78     2814   2749   3019    174    -56     63       O  
ATOM    499  ND2 ASN A  78      51.552  -8.153   7.491  1.00 19.19           N  
ANISOU  499  ND2 ASN A  78     2375   2373   2543    149    -94     87       N  
ATOM    500  N   THR A  79      53.263  -7.242   2.642  1.00 21.16           N  
ANISOU  500  N   THR A  79     2594   2595   2852    169      8     -5       N  
ATOM    501  CA  THR A  79      54.680  -7.106   2.352  1.00 21.79           C  
ANISOU  501  CA  THR A  79     2630   2693   2957    192     21     -5       C  
ATOM    502  C   THR A  79      55.019  -5.747   1.758  1.00 21.06           C  
ANISOU  502  C   THR A  79     2514   2625   2862    168     40    -16       C  
ATOM    503  O   THR A  79      54.390  -5.272   0.803  1.00 18.56           O  
ANISOU  503  O   THR A  79     2223   2302   2527    155     64    -31       O  
ATOM    504  CB  THR A  79      55.180  -8.192   1.393  1.00 21.23           C  
ANISOU  504  CB  THR A  79     2564   2596   2906    232     47    -13       C  
ATOM    505  OG1 THR A  79      54.912  -9.458   1.973  1.00 18.16           O  
ANISOU  505  OG1 THR A  79     2198   2176   2527    254     29      0       O  
ATOM    506  CG2 THR A  79      56.710  -8.063   1.159  1.00 17.98           C  
ANISOU  506  CG2 THR A  79     2098   2210   2525    259     64     -9       C  
ATOM    507  N   ILE A  80      56.016  -5.118   2.353  1.00 17.78           N  
ANISOU  507  N   ILE A  80     2050   2238   2467    162     28     -8       N  
ATOM    508  CA  ILE A  80      56.645  -3.952   1.762  1.00 18.21           C  
ANISOU  508  CA  ILE A  80     2072   2311   2535    143     51    -14       C  
ATOM    509  C   ILE A  80      57.783  -4.430   0.859  1.00 17.72           C  
ANISOU  509  C   ILE A  80     1977   2254   2501    175     87    -12       C  
ATOM    510  O   ILE A  80      58.786  -4.934   1.342  1.00 24.44           O  
ANISOU  510  O   ILE A  80     2785   3119   3381    199     75     -2       O  
ATOM    511  CB  ILE A  80      57.194  -3.054   2.859  1.00 21.08           C  
ANISOU  511  CB  ILE A  80     2396   2701   2913    117     16    -11       C  
ATOM    512  CG1 ILE A  80      56.032  -2.515   3.692  1.00 17.16           C  
ANISOU  512  CG1 ILE A  80     1936   2202   2383     89    -13    -17       C  
ATOM    513  CG2 ILE A  80      58.062  -1.938   2.267  1.00 23.25           C  
ANISOU  513  CG2 ILE A  80     2627   2991   3217     95     41    -14       C  
ATOM    514  CD1 ILE A  80      56.461  -1.690   4.898  1.00 13.14           C  
ANISOU  514  CD1 ILE A  80     1395   1718   1878     66    -54    -22       C  
ATOM    515  N   HIS A  81      57.622  -4.286  -0.451  1.00 16.92           N  
ANISOU  515  N   HIS A  81     1895   2146   2389    181    132    -21       N  
ATOM    516  CA  HIS A  81      58.573  -4.873  -1.399  1.00 12.99           C  
ANISOU  516  CA  HIS A  81     1374   1653   1909    220    174    -22       C  
ATOM    517  C   HIS A  81      59.838  -4.029  -1.580  1.00 20.13           C  
ANISOU  517  C   HIS A  81     2210   2588   2848    211    198     -9       C  
ATOM    518  O   HIS A  81      60.942  -4.561  -1.641  1.00 20.28           O  
ANISOU  518  O   HIS A  81     2183   2622   2900    242    211     -3       O  
ATOM    519  CB  HIS A  81      57.899  -5.124  -2.758  1.00 15.34           C  
ANISOU  519  CB  HIS A  81     1723   1936   2172    235    212    -39       C  
ATOM    520  CG  HIS A  81      56.716  -6.042  -2.688  1.00 29.76           C  
ANISOU  520  CG  HIS A  81     3608   3729   3971    243    189    -55       C  
ATOM    521  ND1 HIS A  81      56.828  -7.413  -2.810  1.00 32.72           N  
ANISOU  521  ND1 HIS A  81     4000   4079   4355    284    189    -65       N  
ATOM    522  CD2 HIS A  81      55.396  -5.790  -2.512  1.00 26.47           C  
ANISOU  522  CD2 HIS A  81     3235   3297   3525    215    167    -62       C  
ATOM    523  CE1 HIS A  81      55.632  -7.963  -2.707  1.00 31.63           C  
ANISOU  523  CE1 HIS A  81     3912   3910   4196    275    166    -78       C  
ATOM    524  NE2 HIS A  81      54.746  -7.000  -2.523  1.00 33.84           N  
ANISOU  524  NE2 HIS A  81     4207   4199   4452    234    153    -75       N  
ATOM    525  N   SER A  82      59.678  -2.713  -1.685  1.00 13.84           N  
ANISOU  525  N   SER A  82     1408   1800   2052    167    204     -5       N  
ATOM    526  CA  SER A  82      60.827  -1.852  -1.859  1.00 17.88           C  
ANISOU  526  CA  SER A  82     1855   2336   2605    149    228      9       C  
ATOM    527  C   SER A  82      60.595  -0.434  -1.333  1.00 22.29           C  
ANISOU  527  C   SER A  82     2403   2892   3172     93    208     12       C  
ATOM    528  O   SER A  82      59.477   0.064  -1.313  1.00 23.02           O  
ANISOU  528  O   SER A  82     2548   2967   3233     71    196      5       O  
ATOM    529  CB  SER A  82      61.296  -1.841  -3.326  1.00 20.56           C  
ANISOU  529  CB  SER A  82     2188   2683   2939    172    298     17       C  
ATOM    530  OG  SER A  82      60.446  -1.082  -4.170  1.00 18.78           O  
ANISOU  530  OG  SER A  82     2011   2447   2677    152    325     19       O  
ATOM    531  N   ILE A  83      61.675   0.193  -0.888  1.00 21.77           N  
ANISOU  531  N   ILE A  83     2269   2846   3158     70    201     20       N  
ATOM    532  CA  ILE A  83      61.662   1.588  -0.483  1.00 22.39           C  
ANISOU  532  CA  ILE A  83     2331   2918   3258     15    185     19       C  
ATOM    533  C   ILE A  83      62.857   2.237  -1.144  1.00 24.76           C  
ANISOU  533  C   ILE A  83     2564   3232   3610     -2    230     39       C  
ATOM    534  O   ILE A  83      63.966   1.698  -1.101  1.00 21.88           O  
ANISOU  534  O   ILE A  83     2137   2894   3283     19    238     46       O  
ATOM    535  CB  ILE A  83      61.745   1.761   1.057  1.00 24.30           C  
ANISOU  535  CB  ILE A  83     2551   3167   3512     -6    113      3       C  
ATOM    536  CG1 ILE A  83      60.547   1.073   1.733  1.00 22.62           C  
ANISOU  536  CG1 ILE A  83     2404   2944   3246     13     75    -10       C  
ATOM    537  CG2 ILE A  83      61.827   3.241   1.432  1.00 10.13           C  
ANISOU  537  CG2 ILE A  83      738   1362   1747    -63     98     -5       C  
ATOM    538  CD1 ILE A  83      60.347   1.435   3.186  1.00 13.43           C  
ANISOU  538  CD1 ILE A  83     1237   1788   2077     -9     11    -27       C  
ATOM    539  N   ASP A  84      62.618   3.383  -1.769  1.00 20.42           N  
ANISOU  539  N   ASP A  84     2027   2666   3067    -38    263     51       N  
ATOM    540  CA  ASP A  84      63.633   4.078  -2.540  1.00 20.90           C  
ANISOU  540  CA  ASP A  84     2031   2735   3176    -59    317     77       C  
ATOM    541  C   ASP A  84      63.628   5.539  -2.103  1.00 25.71           C  
ANISOU  541  C   ASP A  84     2624   3319   3824   -123    299     77       C  
ATOM    542  O   ASP A  84      62.657   6.248  -2.342  1.00 26.20           O  
ANISOU  542  O   ASP A  84     2746   3351   3858   -141    302     78       O  
ATOM    543  CB  ASP A  84      63.296   3.958  -4.029  1.00 15.42           C  
ANISOU  543  CB  ASP A  84     1378   2039   2442    -32    390    100       C  
ATOM    544  CG  ASP A  84      64.397   4.490  -4.936  1.00 21.29           C  
ANISOU  544  CG  ASP A  84     2062   2798   3229    -43    459    135       C  
ATOM    545  OD1 ASP A  84      64.956   5.570  -4.632  1.00 20.48           O  
ANISOU  545  OD1 ASP A  84     1910   2686   3185    -96    458    148       O  
ATOM    546  OD2 ASP A  84      64.682   3.832  -5.970  1.00 18.27           O  
ANISOU  546  OD2 ASP A  84     1682   2437   2821      2    518    149       O  
ATOM    547  N   ALA A  85      64.706   5.993  -1.468  1.00 20.11           N  
ANISOU  547  N   ALA A  85     1837   2621   3183   -157    277     75       N  
ATOM    548  CA  ALA A  85      64.747   7.361  -0.959  1.00 17.97           C  
ANISOU  548  CA  ALA A  85     1551   2321   2957   -221    252     67       C  
ATOM    549  C   ALA A  85      65.023   8.418  -2.036  1.00 24.34           C  
ANISOU  549  C   ALA A  85     2345   3103   3799   -256    321    105       C  
ATOM    550  O   ALA A  85      64.723   9.595  -1.833  1.00 27.19           O  
ANISOU  550  O   ALA A  85     2720   3425   4186   -304    309    102       O  
ATOM    551  CB  ALA A  85      65.733   7.481   0.189  1.00 16.01           C  
ANISOU  551  CB  ALA A  85     1224   2092   2769   -248    193     44       C  
ATOM    552  N   ASP A  86      65.579   8.012  -3.176  1.00 16.10           N  
ANISOU  552  N   ASP A  86     1280   2082   2756   -229    393    141       N  
ATOM    553  CA  ASP A  86      65.890   8.975  -4.239  1.00 18.54           C  
ANISOU  553  CA  ASP A  86     1598   2374   3071   -253    453    180       C  
ATOM    554  C   ASP A  86      64.622   9.349  -4.986  1.00 25.16           C  
ANISOU  554  C   ASP A  86     2517   3181   3861   -244    488    198       C  
ATOM    555  O   ASP A  86      64.317  10.525  -5.168  1.00 26.54           O  
ANISOU  555  O   ASP A  86     2719   3317   4049   -283    494    213       O  
ATOM    556  CB  ASP A  86      66.893   8.413  -5.253  1.00 19.61           C  
ANISOU  556  CB  ASP A  86     1700   2551   3201   -219    514    210       C  
ATOM    557  CG  ASP A  86      68.244   8.103  -4.641  1.00 25.68           C  
ANISOU  557  CG  ASP A  86     2384   3352   4020   -226    487    198       C  
ATOM    558  OD1 ASP A  86      68.547   8.648  -3.558  1.00 19.33           O  
ANISOU  558  OD1 ASP A  86     1546   2537   3261   -269    426    174       O  
ATOM    559  OD2 ASP A  86      68.998   7.314  -5.255  1.00 26.83           O  
ANISOU  559  OD2 ASP A  86     2500   3538   4158   -185    527    211       O  
ATOM    560  N   THR A  87      63.894   8.337  -5.434  1.00 18.78           N  
ANISOU  560  N   THR A  87     1762   2393   2982   -188    499    191       N  
ATOM    561  CA  THR A  87      62.635   8.571  -6.110  1.00 16.77           C  
ANISOU  561  CA  THR A  87     1597   2117   2660   -171    514    199       C  
ATOM    562  C   THR A  87      61.478   8.811  -5.128  1.00 26.32           C  
ANISOU  562  C   THR A  87     2859   3297   3845   -183    442    162       C  
ATOM    563  O   THR A  87      60.401   9.228  -5.550  1.00 34.21           O  
ANISOU  563  O   THR A  87     3925   4273   4800   -177    447    168       O  
ATOM    564  CB  THR A  87      62.286   7.412  -7.011  1.00 14.89           C  
ANISOU  564  CB  THR A  87     1398   1909   2349   -106    547    200       C  
ATOM    565  OG1 THR A  87      61.970   6.264  -6.204  1.00 18.23           O  
ANISOU  565  OG1 THR A  87     1832   2345   2749    -76    491    158       O  
ATOM    566  CG2 THR A  87      63.461   7.102  -7.948  1.00 15.57           C  
ANISOU  566  CG2 THR A  87     1430   2030   2455    -86    621    233       C  
ATOM    567  N   LYS A  88      61.713   8.563  -3.835  1.00 24.06           N  
ANISOU  567  N   LYS A  88     2541   3015   3586   -197    378    125       N  
ATOM    568  CA  LYS A  88      60.682   8.677  -2.783  1.00 25.98           C  
ANISOU  568  CA  LYS A  88     2831   3239   3803   -204    310     88       C  
ATOM    569  C   LYS A  88      59.568   7.630  -2.924  1.00 24.56           C  
ANISOU  569  C   LYS A  88     2716   3071   3546   -154    298     73       C  
ATOM    570  O   LYS A  88      58.538   7.719  -2.262  1.00 25.20           O  
ANISOU  570  O   LYS A  88     2842   3138   3596   -155    255     49       O  
ATOM    571  CB  LYS A  88      60.057  10.087  -2.723  1.00 25.04           C  
ANISOU  571  CB  LYS A  88     2743   3072   3698   -244    305     90       C  
ATOM    572  CG  LYS A  88      60.898  11.164  -2.029  1.00 32.36           C  
ANISOU  572  CG  LYS A  88     3615   3974   4706   -303    284     83       C  
ATOM    573  CD  LYS A  88      62.014  11.696  -2.897  1.00 40.48           C  
ANISOU  573  CD  LYS A  88     4587   4998   5794   -330    346    126       C  
ATOM    574  CE  LYS A  88      61.472  12.507  -4.056  1.00 52.37           C  
ANISOU  574  CE  LYS A  88     6141   6472   7286   -333    405    170       C  
ATOM    575  NZ  LYS A  88      62.575  12.978  -4.950  1.00 54.35           N  
ANISOU  575  NZ  LYS A  88     6345   6725   7580   -352    467    217       N  
ATOM    576  N   LEU A  89      59.771   6.650  -3.796  1.00 21.61           N  
ANISOU  576  N   LEU A  89     2345   2722   3142   -112    337     87       N  
ATOM    577  CA  LEU A  89      58.747   5.642  -4.060  1.00 25.77           C  
ANISOU  577  CA  LEU A  89     2933   3257   3604    -68    328     72       C  
ATOM    578  C   LEU A  89      58.790   4.466  -3.093  1.00 22.37           C  
ANISOU  578  C   LEU A  89     2492   2842   3167    -46    281     45       C  
ATOM    579  O   LEU A  89      59.851   3.901  -2.846  1.00 24.46           O  
ANISOU  579  O   LEU A  89     2702   3128   3465    -35    282     46       O  
ATOM    580  CB  LEU A  89      58.862   5.121  -5.497  1.00 17.82           C  
ANISOU  580  CB  LEU A  89     1943   2266   2562    -30    390     93       C  
ATOM    581  CG  LEU A  89      58.819   6.207  -6.567  1.00 21.83           C  
ANISOU  581  CG  LEU A  89     2466   2763   3066    -45    443    129       C  
ATOM    582  CD1 LEU A  89      59.057   5.613  -7.952  1.00 19.00           C  
ANISOU  582  CD1 LEU A  89     2122   2430   2666     -1    506    148       C  
ATOM    583  CD2 LEU A  89      57.496   6.965  -6.491  1.00 16.89           C  
ANISOU  583  CD2 LEU A  89     1901   2107   2408    -58    418    125       C  
ATOM    584  N   VAL A  90      57.630   4.099  -2.555  1.00 16.88           N  
ANISOU  584  N   VAL A  90     1846   2136   2430    -37    241     24       N  
ATOM    585  CA  VAL A  90      57.489   2.830  -1.840  1.00 17.46           C  
ANISOU  585  CA  VAL A  90     1923   2221   2488     -9    206      6       C  
ATOM    586  C   VAL A  90      56.544   1.904  -2.611  1.00 20.79           C  
ANISOU  586  C   VAL A  90     2402   2638   2859     26    219      0       C  
ATOM    587  O   VAL A  90      55.531   2.339  -3.145  1.00 20.89           O  
ANISOU  587  O   VAL A  90     2461   2638   2838     22    227      0       O  
ATOM    588  CB  VAL A  90      57.027   3.001  -0.361  1.00 21.91           C  
ANISOU  588  CB  VAL A  90     2491   2782   3053    -29    144    -13       C  
ATOM    589  CG1 VAL A  90      58.004   3.885   0.398  1.00 20.81           C  
ANISOU  589  CG1 VAL A  90     2295   2647   2964    -64    123    -16       C  
ATOM    590  CG2 VAL A  90      55.605   3.565  -0.277  1.00 16.57           C  
ANISOU  590  CG2 VAL A  90     1871   2085   2338    -41    131    -23       C  
ATOM    591  N   ASP A  91      56.919   0.628  -2.689  1.00 26.97           N  
ANISOU  591  N   ASP A  91     3179   3430   3640     63    222     -5       N  
ATOM    592  CA  ASP A  91      56.184  -0.386  -3.431  1.00 18.31           C  
ANISOU  592  CA  ASP A  91     2130   2325   2502     97    233    -17       C  
ATOM    593  C   ASP A  91      55.675  -1.409  -2.418  1.00 22.70           C  
ANISOU  593  C   ASP A  91     2701   2872   3054    107    187    -30       C  
ATOM    594  O   ASP A  91      56.438  -2.231  -1.904  1.00 22.17           O  
ANISOU  594  O   ASP A  91     2604   2809   3010    128    176    -28       O  
ATOM    595  CB  ASP A  91      57.119  -1.017  -4.469  1.00 20.75           C  
ANISOU  595  CB  ASP A  91     2420   2647   2815    134    281    -12       C  
ATOM    596  CG  ASP A  91      56.457  -2.115  -5.290  1.00 24.87           C  
ANISOU  596  CG  ASP A  91     2993   3159   3297    172    291    -33       C  
ATOM    597  OD1 ASP A  91      55.287  -2.452  -5.017  1.00 26.92           O  
ANISOU  597  OD1 ASP A  91     3297   3400   3530    167    258    -48       O  
ATOM    598  OD2 ASP A  91      57.123  -2.649  -6.211  1.00 21.64           O  
ANISOU  598  OD2 ASP A  91     2578   2761   2883    208    333    -35       O  
ATOM    599  N   ILE A  92      54.383  -1.339  -2.101  1.00 21.15           N  
ANISOU  599  N   ILE A  92     2547   2661   2827     93    161    -39       N  
ATOM    600  CA  ILE A  92      53.845  -2.144  -1.014  1.00 17.74           C  
ANISOU  600  CA  ILE A  92     2128   2221   2393     96    119    -44       C  
ATOM    601  C   ILE A  92      52.562  -2.877  -1.363  1.00 16.36           C  
ANISOU  601  C   ILE A  92     2003   2026   2187    103    112    -57       C  
ATOM    602  O   ILE A  92      51.793  -2.418  -2.203  1.00 22.66           O  
ANISOU  602  O   ILE A  92     2831   2821   2959     97    126    -64       O  
ATOM    603  CB  ILE A  92      53.618  -1.310   0.279  1.00 24.41           C  
ANISOU  603  CB  ILE A  92     2959   3073   3242     64     83    -41       C  
ATOM    604  CG1 ILE A  92      52.369  -0.427   0.171  1.00 26.11           C  
ANISOU  604  CG1 ILE A  92     3210   3281   3431     40     79    -48       C  
ATOM    605  CG2 ILE A  92      54.855  -0.499   0.621  1.00 19.57           C  
ANISOU  605  CG2 ILE A  92     2294   2477   2665     49     84    -34       C  
ATOM    606  CD1 ILE A  92      52.506   0.780  -0.752  1.00  6.37           C  
ANISOU  606  CD1 ILE A  92      708    780    932     26    109    -44       C  
ATOM    607  N   ASP A  93      52.346  -4.024  -0.716  1.00 17.01           N  
ANISOU  607  N   ASP A  93     2094   2094   2274    117     90    -57       N  
ATOM    608  CA  ASP A  93      51.069  -4.746  -0.815  1.00 24.20           C  
ANISOU  608  CA  ASP A  93     3047   2983   3165    115     77    -67       C  
ATOM    609  C   ASP A  93      49.906  -3.861  -0.341  1.00 21.85           C  
ANISOU  609  C   ASP A  93     2764   2692   2846     84     59    -67       C  
ATOM    610  O   ASP A  93      50.093  -2.972   0.484  1.00 12.99           O  
ANISOU  610  O   ASP A  93     1622   1586   1727     66     47    -58       O  
ATOM    611  CB  ASP A  93      51.088  -6.015   0.037  1.00 18.69           C  
ANISOU  611  CB  ASP A  93     2351   2267   2485    129     55    -58       C  
ATOM    612  CG  ASP A  93      51.872  -7.159  -0.595  1.00 17.46           C  
ANISOU  612  CG  ASP A  93     2195   2091   2348    167     72    -65       C  
ATOM    613  OD1 ASP A  93      52.147  -7.148  -1.812  1.00 16.40           O  
ANISOU  613  OD1 ASP A  93     2068   1957   2206    184    100    -84       O  
ATOM    614  OD2 ASP A  93      52.207  -8.096   0.144  1.00 17.44           O  
ANISOU  614  OD2 ASP A  93     2187   2073   2367    184     56    -52       O  
ATOM    615  N   ALA A  94      48.703  -4.123  -0.841  1.00 19.49           N  
ANISOU  615  N   ALA A  94     2497   2380   2527     78     56    -79       N  
ATOM    616  CA  ALA A  94      47.542  -3.303  -0.483  1.00 13.24           C  
ANISOU  616  CA  ALA A  94     1717   1596   1716     53     42    -79       C  
ATOM    617  C   ALA A  94      47.115  -3.472   0.972  1.00 13.26           C  
ANISOU  617  C   ALA A  94     1712   1602   1723     40     17    -65       C  
ATOM    618  O   ALA A  94      46.402  -2.631   1.524  1.00 18.57           O  
ANISOU  618  O   ALA A  94     2386   2288   2382     22      8    -64       O  
ATOM    619  CB  ALA A  94      46.384  -3.608  -1.395  1.00 13.59           C  
ANISOU  619  CB  ALA A  94     1791   1630   1742     53     41    -96       C  
ATOM    620  N   GLY A  95      47.532  -4.572   1.585  1.00 15.08           N  
ANISOU  620  N   GLY A  95     1938   1821   1970     51      8    -54       N  
ATOM    621  CA  GLY A  95      47.153  -4.848   2.952  1.00 14.99           C  
ANISOU  621  CA  GLY A  95     1923   1815   1956     42    -12    -35       C  
ATOM    622  C   GLY A  95      48.077  -4.199   3.961  1.00 17.04           C  
ANISOU  622  C   GLY A  95     2157   2101   2216     43    -24    -24       C  
ATOM    623  O   GLY A  95      47.813  -4.266   5.153  1.00 12.30           O  
ANISOU  623  O   GLY A  95     1555   1514   1605     39    -41     -9       O  
ATOM    624  N   VAL A  96      49.163  -3.567   3.516  1.00 22.22           N  
ANISOU  624  N   VAL A  96     2790   2766   2884     48    -15    -32       N  
ATOM    625  CA  VAL A  96      50.017  -2.925   4.505  1.00 17.22           C  
ANISOU  625  CA  VAL A  96     2128   2158   2255     45    -34    -27       C  
ATOM    626  C   VAL A  96      49.323  -1.689   5.033  1.00 14.21           C  
ANISOU  626  C   VAL A  96     1754   1792   1854     21    -43    -37       C  
ATOM    627  O   VAL A  96      48.645  -0.986   4.294  1.00 12.69           O  
ANISOU  627  O   VAL A  96     1576   1591   1653      9    -28    -49       O  
ATOM    628  CB  VAL A  96      51.510  -2.668   4.067  1.00 17.65           C  
ANISOU  628  CB  VAL A  96     2146   2220   2339     54    -25    -29       C  
ATOM    629  CG1 VAL A  96      51.892  -3.468   2.862  1.00 18.96           C  
ANISOU  629  CG1 VAL A  96     2315   2368   2520     76      3    -30       C  
ATOM    630  CG2 VAL A  96      51.821  -1.205   3.913  1.00 16.63           C  
ANISOU  630  CG2 VAL A  96     2000   2103   2215     31    -21    -42       C  
ATOM    631  N   ASN A  97      49.447  -1.466   6.335  1.00 11.77           N  
ANISOU  631  N   ASN A  97     1435   1504   1531     18    -69    -34       N  
ATOM    632  CA  ASN A  97      48.776  -0.344   6.957  1.00 14.00           C  
ANISOU  632  CA  ASN A  97     1727   1801   1792      1    -79    -49       C  
ATOM    633  C   ASN A  97      49.730   0.840   7.129  1.00 16.23           C  
ANISOU  633  C   ASN A  97     1984   2092   2091    -12    -90    -68       C  
ATOM    634  O   ASN A  97      50.945   0.690   7.015  1.00 16.00           O  
ANISOU  634  O   ASN A  97     1924   2067   2087     -8    -95    -65       O  
ATOM    635  CB  ASN A  97      48.091  -0.762   8.262  1.00 10.54           C  
ANISOU  635  CB  ASN A  97     1301   1381   1321      6    -97    -37       C  
ATOM    636  CG  ASN A  97      49.081  -1.083   9.368  1.00 20.97           C  
ANISOU  636  CG  ASN A  97     2603   2727   2637     19   -126    -27       C  
ATOM    637  OD1 ASN A  97      49.735  -0.186   9.900  1.00 22.36           O  
ANISOU  637  OD1 ASN A  97     2762   2922   2811     12   -148    -47       O  
ATOM    638  ND2 ASN A  97      49.178  -2.364   9.737  1.00 12.85           N  
ANISOU  638  ND2 ASN A  97     1579   1698   1607     38   -130      3       N  
ATOM    639  N   LEU A  98      49.173   2.017   7.376  1.00 15.49           N  
ANISOU  639  N   LEU A  98     1900   1998   1985    -28    -94    -88       N  
ATOM    640  CA  LEU A  98      49.947   3.255   7.324  1.00 11.94           C  
ANISOU  640  CA  LEU A  98     1432   1545   1560    -47   -100   -108       C  
ATOM    641  C   LEU A  98      50.894   3.397   8.504  1.00 16.14           C  
ANISOU  641  C   LEU A  98     1938   2102   2094    -49   -138   -120       C  
ATOM    642  O   LEU A  98      51.938   4.023   8.398  1.00 17.30           O  
ANISOU  642  O   LEU A  98     2052   2246   2274    -65   -147   -132       O  
ATOM    643  CB  LEU A  98      49.030   4.456   7.247  1.00 10.38           C  
ANISOU  643  CB  LEU A  98     1257   1334   1352    -60    -93   -128       C  
ATOM    644  CG  LEU A  98      48.153   4.525   6.003  1.00 17.65           C  
ANISOU  644  CG  LEU A  98     2201   2233   2273    -57    -61   -118       C  
ATOM    645  CD1 LEU A  98      47.494   5.912   5.905  1.00 14.02           C  
ANISOU  645  CD1 LEU A  98     1757   1756   1812    -67    -56   -136       C  
ATOM    646  CD2 LEU A  98      48.963   4.200   4.755  1.00  7.32           C  
ANISOU  646  CD2 LEU A  98      878    912    992    -56    -36   -102       C  
ATOM    647  N   ASP A  99      50.513   2.808   9.627  1.00 20.17           N  
ANISOU  647  N   ASP A  99     2460   2638   2567    -34   -161   -115       N  
ATOM    648  CA  ASP A  99      51.387   2.710  10.775  1.00 23.75           C  
ANISOU  648  CA  ASP A  99     2890   3122   3012    -29   -202   -122       C  
ATOM    649  C   ASP A  99      52.639   1.913  10.404  1.00 20.30           C  
ANISOU  649  C   ASP A  99     2415   2688   2610    -18   -206   -102       C  
ATOM    650  O   ASP A  99      53.768   2.367  10.611  1.00 24.60           O  
ANISOU  650  O   ASP A  99     2920   3243   3182    -28   -230   -116       O  
ATOM    651  CB  ASP A  99      50.643   2.020  11.913  1.00 36.01           C  
ANISOU  651  CB  ASP A  99     4469   4703   4511     -8   -217   -108       C  
ATOM    652  CG  ASP A  99      51.255   2.305  13.254  1.00 48.27           C  
ANISOU  652  CG  ASP A  99     6010   6294   6037     -1   -263   -125       C  
ATOM    653  OD1 ASP A  99      51.508   1.339  14.007  1.00 60.90           O  
ANISOU  653  OD1 ASP A  99     7608   7920   7611     23   -282    -99       O  
ATOM    654  OD2 ASP A  99      51.476   3.498  13.551  1.00 45.13           O  
ANISOU  654  OD2 ASP A  99     5607   5897   5643    -20   -283   -165       O  
ATOM    655  N   GLN A 100      52.420   0.724   9.850  1.00 15.48           N  
ANISOU  655  N   GLN A 100     1814   2067   2001      2   -183    -72       N  
ATOM    656  CA  GLN A 100      53.485  -0.160   9.395  1.00 18.84           C  
ANISOU  656  CA  GLN A 100     2209   2491   2459     20   -180    -52       C  
ATOM    657  C   GLN A 100      54.425   0.551   8.421  1.00 28.37           C  
ANISOU  657  C   GLN A 100     3380   3687   3714      3   -162    -65       C  
ATOM    658  O   GLN A 100      55.648   0.493   8.553  1.00 29.31           O  
ANISOU  658  O   GLN A 100     3452   3821   3864      7   -178    -64       O  
ATOM    659  CB  GLN A 100      52.864  -1.388   8.734  1.00  8.84           C  
ANISOU  659  CB  GLN A 100      969   1201   1190     40   -151    -26       C  
ATOM    660  CG  GLN A 100      53.843  -2.369   8.127  1.00 10.18           C  
ANISOU  660  CG  GLN A 100     1113   1362   1393     65   -140     -9       C  
ATOM    661  CD  GLN A 100      53.137  -3.473   7.336  1.00 24.52           C  
ANISOU  661  CD  GLN A 100     2961   3145   3208     81   -111      6       C  
ATOM    662  OE1 GLN A 100      51.907  -3.489   7.229  1.00 24.14           O  
ANISOU  662  OE1 GLN A 100     2950   3084   3138     70   -100      5       O  
ATOM    663  NE2 GLN A 100      53.917  -4.397   6.776  1.00 21.91           N  
ANISOU  663  NE2 GLN A 100     2616   2803   2907    108    -99     17       N  
ATOM    664  N   LEU A 101      53.836   1.234   7.449  1.00 20.21           N  
ANISOU  664  N   LEU A 101     2365   2628   2686    -15   -129    -73       N  
ATOM    665  CA  LEU A 101      54.593   1.953   6.437  1.00 14.31           C  
ANISOU  665  CA  LEU A 101     1589   1867   1981    -32   -103    -78       C  
ATOM    666  C   LEU A 101      55.355   3.149   7.017  1.00 22.44           C  
ANISOU  666  C   LEU A 101     2584   2905   3037    -62   -129   -101       C  
ATOM    667  O   LEU A 101      56.477   3.450   6.603  1.00 20.33           O  
ANISOU  667  O   LEU A 101     2270   2640   2815    -73   -122    -99       O  
ATOM    668  CB  LEU A 101      53.649   2.429   5.340  1.00 11.35           C  
ANISOU  668  CB  LEU A 101     1251   1466   1597    -41    -64    -78       C  
ATOM    669  CG  LEU A 101      54.206   3.288   4.211  1.00 17.27           C  
ANISOU  669  CG  LEU A 101     1983   2199   2381    -58    -29    -76       C  
ATOM    670  CD1 LEU A 101      55.321   2.532   3.500  1.00 15.88           C  
ANISOU  670  CD1 LEU A 101     1771   2031   2234    -40     -6    -59       C  
ATOM    671  CD2 LEU A 101      53.085   3.654   3.246  1.00 12.59           C  
ANISOU  671  CD2 LEU A 101     1435   1585   1766    -59      2    -73       C  
ATOM    672  N   MET A 102      54.730   3.845   7.956  1.00 25.12           N  
ANISOU  672  N   MET A 102     2945   3249   3350    -75   -159   -123       N  
ATOM    673  CA  MET A 102      55.347   5.017   8.548  1.00 27.32           C  
ANISOU  673  CA  MET A 102     3198   3530   3653   -105   -189   -153       C  
ATOM    674  C   MET A 102      56.632   4.592   9.252  1.00 24.36           C  
ANISOU  674  C   MET A 102     2769   3187   3299   -100   -228   -155       C  
ATOM    675  O   MET A 102      57.661   5.240   9.129  1.00 24.26           O  
ANISOU  675  O   MET A 102     2709   3174   3336   -125   -237   -167       O  
ATOM    676  CB  MET A 102      54.388   5.704   9.521  1.00 24.05           C  
ANISOU  676  CB  MET A 102     2823   3118   3199   -111   -215   -183       C  
ATOM    677  CG  MET A 102      55.046   6.802  10.353  1.00 35.01           C  
ANISOU  677  CG  MET A 102     4186   4509   4606   -139   -258   -223       C  
ATOM    678  SD  MET A 102      53.889   7.673  11.434  1.00 42.49           S  
ANISOU  678  SD  MET A 102     5184   5457   5503   -140   -284   -265       S  
ATOM    679  CE  MET A 102      54.946   8.073  12.826  1.00115.70           C  
ANISOU  679  CE  MET A 102    14423  14764  14776   -151   -355   -308       C  
ATOM    680  N   LYS A 103      56.557   3.472   9.960  1.00 21.62           N  
ANISOU  680  N   LYS A 103     2429   2868   2917    -66   -250   -139       N  
ATOM    681  CA  LYS A 103      57.687   2.946  10.699  1.00 20.84           C  
ANISOU  681  CA  LYS A 103     2284   2805   2830    -52   -292   -136       C  
ATOM    682  C   LYS A 103      58.814   2.483   9.781  1.00 22.60           C  
ANISOU  682  C   LYS A 103     2453   3025   3108    -45   -267   -115       C  
ATOM    683  O   LYS A 103      59.987   2.712  10.066  1.00 24.93           O  
ANISOU  683  O   LYS A 103     2689   3342   3442    -54   -295   -123       O  
ATOM    684  CB  LYS A 103      57.234   1.802  11.589  1.00 20.05           C  
ANISOU  684  CB  LYS A 103     2211   2730   2677    -12   -314   -115       C  
ATOM    685  CG  LYS A 103      58.362   1.058  12.231  1.00 31.20           C  
ANISOU  685  CG  LYS A 103     3579   4178   4099     14   -353   -101       C  
ATOM    686  CD  LYS A 103      57.863   0.123  13.301  1.00 37.18           C  
ANISOU  686  CD  LYS A 103     4368   4960   4797     50   -380    -78       C  
ATOM    687  CE  LYS A 103      59.022  -0.667  13.878  1.00 42.64           C  
ANISOU  687  CE  LYS A 103     5014   5687   5499     83   -420    -58       C  
ATOM    688  NZ  LYS A 103      58.603  -1.473  15.050  1.00 42.49           N  
ANISOU  688  NZ  LYS A 103     5028   5697   5418    119   -451    -33       N  
ATOM    689  N   ALA A 104      58.451   1.843   8.675  1.00 19.50           N  
ANISOU  689  N   ALA A 104     2081   2610   2719    -28   -215    -90       N  
ATOM    690  CA  ALA A 104      59.426   1.319   7.735  1.00 18.86           C  
ANISOU  690  CA  ALA A 104     1956   2527   2682    -14   -183    -70       C  
ATOM    691  C   ALA A 104      60.098   2.415   6.895  1.00 22.68           C  
ANISOU  691  C   ALA A 104     2400   2998   3219    -51   -154    -79       C  
ATOM    692  O   ALA A 104      61.257   2.279   6.495  1.00 19.68           O  
ANISOU  692  O   ALA A 104     1960   2632   2887    -48   -143    -69       O  
ATOM    693  CB  ALA A 104      58.767   0.282   6.826  1.00 16.68           C  
ANISOU  693  CB  ALA A 104     1721   2230   2388     17   -138    -48       C  
ATOM    694  N   ALA A 105      59.374   3.503   6.639  1.00 18.71           N  
ANISOU  694  N   ALA A 105     1929   2470   2710    -85   -141    -94       N  
ATOM    695  CA  ALA A 105      59.859   4.540   5.733  1.00 21.92           C  
ANISOU  695  CA  ALA A 105     2309   2855   3165   -120   -105    -94       C  
ATOM    696  C   ALA A 105      60.606   5.695   6.412  1.00 19.82           C  
ANISOU  696  C   ALA A 105     1997   2591   2943   -165   -143   -120       C  
ATOM    697  O   ALA A 105      61.466   6.330   5.792  1.00 21.46           O  
ANISOU  697  O   ALA A 105     2155   2789   3209   -193   -118   -113       O  
ATOM    698  CB  ALA A 105      58.716   5.072   4.865  1.00 13.97           C  
ANISOU  698  CB  ALA A 105     1361   1813   2134   -129    -63    -89       C  
ATOM    699  N   LEU A 106      60.262   5.967   7.669  1.00 15.40           N  
ANISOU  699  N   LEU A 106     1453   2042   2355   -171   -201   -151       N  
ATOM    700  CA  LEU A 106      60.923   7.017   8.455  1.00 25.93           C  
ANISOU  700  CA  LEU A 106     2748   3378   3726   -212   -248   -187       C  
ATOM    701  C   LEU A 106      62.461   7.010   8.383  1.00 31.69           C  
ANISOU  701  C   LEU A 106     3388   4129   4524   -228   -260   -182       C  
ATOM    702  O   LEU A 106      63.057   8.046   8.091  1.00 34.35           O  
ANISOU  702  O   LEU A 106     3685   4443   4922   -275   -254   -193       O  
ATOM    703  CB  LEU A 106      60.453   6.995   9.912  1.00 20.39           C  
ANISOU  703  CB  LEU A 106     2074   2700   2973   -202   -314   -220       C  
ATOM    704  CG  LEU A 106      59.334   7.977  10.273  1.00 19.44           C  
ANISOU  704  CG  LEU A 106     2014   2551   2821   -220   -320   -252       C  
ATOM    705  CD1 LEU A 106      58.867   7.789  11.718  1.00 16.53           C  
ANISOU  705  CD1 LEU A 106     1675   2216   2389   -200   -379   -282       C  
ATOM    706  CD2 LEU A 106      59.768   9.410  10.037  1.00 16.15           C  
ANISOU  706  CD2 LEU A 106     1574   2095   2466   -274   -321   -280       C  
ATOM    707  N   PRO A 107      63.103   5.842   8.607  1.00 25.11           N  
ANISOU  707  N   PRO A 107     2520   3336   3686   -188   -274   -163       N  
ATOM    708  CA  PRO A 107      64.571   5.834   8.571  1.00 30.60           C  
ANISOU  708  CA  PRO A 107     3121   4056   4448   -200   -287   -159       C  
ATOM    709  C   PRO A 107      65.143   6.240   7.220  1.00 33.88           C  
ANISOU  709  C   PRO A 107     3498   4449   4927   -223   -217   -133       C  
ATOM    710  O   PRO A 107      66.322   6.597   7.137  1.00 33.46           O  
ANISOU  710  O   PRO A 107     3368   4410   4937   -248   -221   -132       O  
ATOM    711  CB  PRO A 107      64.928   4.374   8.860  1.00 28.42           C  
ANISOU  711  CB  PRO A 107     2831   3821   4148   -140   -301   -135       C  
ATOM    712  CG  PRO A 107      63.692   3.783   9.505  1.00 25.67           C  
ANISOU  712  CG  PRO A 107     2565   3471   3717   -108   -319   -137       C  
ATOM    713  CD  PRO A 107      62.557   4.491   8.866  1.00 16.55           C  
ANISOU  713  CD  PRO A 107     1474   2271   2541   -132   -276   -142       C  
ATOM    714  N   PHE A 108      64.324   6.191   6.178  1.00 27.27           N  
ANISOU  714  N   PHE A 108     2717   3581   4065   -213   -153   -110       N  
ATOM    715  CA  PHE A 108      64.756   6.646   4.865  1.00 20.31           C  
ANISOU  715  CA  PHE A 108     1808   2678   3230   -233    -81    -82       C  
ATOM    716  C   PHE A 108      64.517   8.141   4.680  1.00 25.32           C  
ANISOU  716  C   PHE A 108     2453   3268   3897   -293    -72    -94       C  
ATOM    717  O   PHE A 108      64.771   8.673   3.603  1.00 24.54           O  
ANISOU  717  O   PHE A 108     2342   3148   3836   -313    -10    -66       O  
ATOM    718  CB  PHE A 108      64.022   5.890   3.767  1.00 14.90           C  
ANISOU  718  CB  PHE A 108     1180   1984   2499   -191    -18    -51       C  
ATOM    719  CG  PHE A 108      64.457   4.467   3.610  1.00 30.33           C  
ANISOU  719  CG  PHE A 108     3116   3970   4440   -134     -8    -34       C  
ATOM    720  CD1 PHE A 108      65.365   4.111   2.607  1.00 32.00           C  
ANISOU  720  CD1 PHE A 108     3276   4196   4689   -118     48     -7       C  
ATOM    721  CD2 PHE A 108      63.957   3.474   4.444  1.00 27.38           C  
ANISOU  721  CD2 PHE A 108     2776   3611   4016    -95    -52    -43       C  
ATOM    722  CE1 PHE A 108      65.763   2.791   2.434  1.00 25.34           C  
ANISOU  722  CE1 PHE A 108     2417   3376   3834    -60     59      6       C  
ATOM    723  CE2 PHE A 108      64.360   2.141   4.286  1.00 25.76           C  
ANISOU  723  CE2 PHE A 108     2557   3428   3804    -41    -43    -26       C  
ATOM    724  CZ  PHE A 108      65.262   1.800   3.277  1.00 26.00           C  
ANISOU  724  CZ  PHE A 108     2537   3468   3872    -22     12     -4       C  
ATOM    725  N   GLY A 109      64.018   8.817   5.714  1.00 24.37           N  
ANISOU  725  N   GLY A 109     2361   3135   3763   -317   -130   -134       N  
ATOM    726  CA  GLY A 109      63.607  10.208   5.573  1.00 23.18           C  
ANISOU  726  CA  GLY A 109     2236   2933   3639   -367   -123   -150       C  
ATOM    727  C   GLY A 109      62.371  10.374   4.680  1.00 28.73           C  
ANISOU  727  C   GLY A 109     3019   3600   4296   -351    -69   -127       C  
ATOM    728  O   GLY A 109      62.218  11.373   3.970  1.00 26.13           O  
ANISOU  728  O   GLY A 109     2702   3227   3998   -383    -30   -114       O  
ATOM    729  N   LEU A 110      61.487   9.382   4.705  1.00 26.95           N  
ANISOU  729  N   LEU A 110     2847   3393   3998   -301    -67   -121       N  
ATOM    730  CA  LEU A 110      60.247   9.447   3.945  1.00 21.76           C  
ANISOU  730  CA  LEU A 110     2264   2711   3294   -283    -26   -105       C  
ATOM    731  C   LEU A 110      59.030   9.480   4.868  1.00 24.77           C  
ANISOU  731  C   LEU A 110     2707   3087   3617   -270    -68   -136       C  
ATOM    732  O   LEU A 110      58.979   8.774   5.874  1.00 27.01           O  
ANISOU  732  O   LEU A 110     2991   3404   3869   -249   -114   -155       O  
ATOM    733  CB  LEU A 110      60.149   8.270   2.982  1.00 13.28           C  
ANISOU  733  CB  LEU A 110     1201   1657   2188   -237     21    -70       C  
ATOM    734  CG  LEU A 110      61.292   8.150   1.985  1.00 16.56           C  
ANISOU  734  CG  LEU A 110     1559   2083   2652   -241     73    -37       C  
ATOM    735  CD1 LEU A 110      61.011   7.010   1.020  1.00 18.23           C  
ANISOU  735  CD1 LEU A 110     1796   2310   2820   -190    119    -11       C  
ATOM    736  CD2 LEU A 110      61.519   9.456   1.235  1.00 14.49           C  
ANISOU  736  CD2 LEU A 110     1287   1783   2438   -285    114    -19       C  
ATOM    737  N   TRP A 111      58.052  10.301   4.500  1.00 23.52           N  
ANISOU  737  N   TRP A 111     2601   2890   3444   -279    -49   -138       N  
ATOM    738  CA  TRP A 111      56.868  10.549   5.318  1.00 23.28           C  
ANISOU  738  CA  TRP A 111     2627   2854   3366   -269    -82   -168       C  
ATOM    739  C   TRP A 111      55.616  10.161   4.535  1.00 20.84           C  
ANISOU  739  C   TRP A 111     2377   2537   3006   -236    -44   -145       C  
ATOM    740  O   TRP A 111      55.493  10.493   3.359  1.00 14.68           O  
ANISOU  740  O   TRP A 111     1607   1733   2237   -238      3   -116       O  
ATOM    741  CB  TRP A 111      56.804  12.040   5.656  1.00 22.59           C  
ANISOU  741  CB  TRP A 111     2547   2722   3316   -309    -98   -197       C  
ATOM    742  CG  TRP A 111      55.751  12.436   6.645  1.00 25.48           C  
ANISOU  742  CG  TRP A 111     2962   3082   3638   -299   -135   -238       C  
ATOM    743  CD1 TRP A 111      54.613  13.154   6.394  1.00 25.43           C  
ANISOU  743  CD1 TRP A 111     3009   3040   3612   -293   -118   -242       C  
ATOM    744  CD2 TRP A 111      55.748  12.163   8.050  1.00 21.16           C  
ANISOU  744  CD2 TRP A 111     2414   2568   3059   -291   -194   -279       C  
ATOM    745  NE1 TRP A 111      53.899  13.331   7.551  1.00 24.32           N  
ANISOU  745  NE1 TRP A 111     2900   2909   3432   -281   -159   -284       N  
ATOM    746  CE2 TRP A 111      54.575  12.734   8.583  1.00 24.69           C  
ANISOU  746  CE2 TRP A 111     2915   2998   3466   -279   -205   -308       C  
ATOM    747  CE3 TRP A 111      56.617  11.484   8.907  1.00 21.13           C  
ANISOU  747  CE3 TRP A 111     2367   2609   3052   -287   -238   -292       C  
ATOM    748  CZ2 TRP A 111      54.256  12.651   9.937  1.00 25.42           C  
ANISOU  748  CZ2 TRP A 111     3024   3121   3514   -266   -255   -350       C  
ATOM    749  CZ3 TRP A 111      56.297  11.403  10.253  1.00 25.29           C  
ANISOU  749  CZ3 TRP A 111     2912   3164   3531   -274   -291   -332       C  
ATOM    750  CH2 TRP A 111      55.128  11.979  10.753  1.00 23.35           C  
ANISOU  750  CH2 TRP A 111     2723   2904   3244   -263   -297   -361       C  
ATOM    751  N   VAL A 112      54.695   9.452   5.174  1.00 15.93           N  
ANISOU  751  N   VAL A 112     1789   1937   2326   -207    -67   -157       N  
ATOM    752  CA  VAL A 112      53.446   9.093   4.510  1.00 19.04           C  
ANISOU  752  CA  VAL A 112     2234   2325   2675   -180    -38   -140       C  
ATOM    753  C   VAL A 112      52.723  10.384   4.090  1.00 18.97           C  
ANISOU  753  C   VAL A 112     2258   2275   2675   -194    -22   -144       C  
ATOM    754  O   VAL A 112      52.456  11.247   4.919  1.00 22.62           O  
ANISOU  754  O   VAL A 112     2731   2721   3143   -208    -50   -176       O  
ATOM    755  CB  VAL A 112      52.561   8.196   5.407  1.00 16.21           C  
ANISOU  755  CB  VAL A 112     1902   1996   2262   -152    -66   -152       C  
ATOM    756  CG1 VAL A 112      51.247   7.910   4.746  1.00 16.10           C  
ANISOU  756  CG1 VAL A 112     1933   1975   2210   -130    -41   -138       C  
ATOM    757  CG2 VAL A 112      53.275   6.886   5.713  1.00 11.50           C  
ANISOU  757  CG2 VAL A 112     1277   1433   1660   -133    -78   -140       C  
ATOM    758  N   PRO A 113      52.440  10.525   2.785  1.00 17.52           N  
ANISOU  758  N   PRO A 113     2091   2073   2492   -187     23   -112       N  
ATOM    759  CA  PRO A 113      52.066  11.817   2.191  1.00 17.30           C  
ANISOU  759  CA  PRO A 113     2086   2001   2486   -202     45   -104       C  
ATOM    760  C   PRO A 113      50.672  12.317   2.592  1.00 16.02           C  
ANISOU  760  C   PRO A 113     1971   1824   2290   -186     30   -123       C  
ATOM    761  O   PRO A 113      50.430  13.521   2.605  1.00 23.26           O  
ANISOU  761  O   PRO A 113     2905   2701   3232   -200     31   -131       O  
ATOM    762  CB  PRO A 113      52.161  11.550   0.681  1.00 19.81           C  
ANISOU  762  CB  PRO A 113     2409   2318   2799   -188     97    -59       C  
ATOM    763  CG  PRO A 113      51.948  10.097   0.546  1.00 24.83           C  
ANISOU  763  CG  PRO A 113     3047   2994   3392   -157     96    -56       C  
ATOM    764  CD  PRO A 113      52.570   9.469   1.765  1.00 17.56           C  
ANISOU  764  CD  PRO A 113     2094   2099   2479   -163     57    -81       C  
ATOM    765  N   VAL A 114      49.779  11.397   2.926  1.00 20.67           N  
ANISOU  765  N   VAL A 114     2580   2446   2828   -157     17   -130       N  
ATOM    766  CA  VAL A 114      48.459  11.740   3.434  1.00 19.35           C  
ANISOU  766  CA  VAL A 114     2448   2274   2628   -139      3   -149       C  
ATOM    767  C   VAL A 114      48.164  10.848   4.641  1.00 23.66           C  
ANISOU  767  C   VAL A 114     2991   2859   3138   -127    -29   -172       C  
ATOM    768  O   VAL A 114      48.168   9.626   4.532  1.00 21.97           O  
ANISOU  768  O   VAL A 114     2770   2675   2902   -113    -27   -157       O  
ATOM    769  CB  VAL A 114      47.370  11.576   2.342  1.00 14.57           C  
ANISOU  769  CB  VAL A 114     1875   1667   1994   -113     30   -122       C  
ATOM    770  CG1 VAL A 114      45.963  11.720   2.933  1.00  9.67           C  
ANISOU  770  CG1 VAL A 114     1281   1053   1339    -91     15   -141       C  
ATOM    771  CG2 VAL A 114      47.584  12.592   1.198  1.00 14.73           C  
ANISOU  771  CG2 VAL A 114     1905   1648   2043   -121     62    -95       C  
ATOM    772  N   LEU A 115      47.940  11.467   5.795  1.00 24.70           N  
ANISOU  772  N   LEU A 115     3130   2990   3266   -131    -57   -207       N  
ATOM    773  CA  LEU A 115      47.650  10.737   7.025  1.00 24.97           C  
ANISOU  773  CA  LEU A 115     3164   3063   3259   -118    -86   -227       C  
ATOM    774  C   LEU A 115      46.285  11.107   7.603  1.00 24.43           C  
ANISOU  774  C   LEU A 115     3128   3000   3155    -96    -89   -245       C  
ATOM    775  O   LEU A 115      46.036  12.263   7.946  1.00 31.88           O  
ANISOU  775  O   LEU A 115     4087   3918   4110    -99    -96   -274       O  
ATOM    776  CB  LEU A 115      48.751  10.979   8.058  1.00 29.81           C  
ANISOU  776  CB  LEU A 115     3752   3686   3889   -137   -123   -256       C  
ATOM    777  CG  LEU A 115      50.060  10.257   7.722  1.00 34.37           C  
ANISOU  777  CG  LEU A 115     4288   4277   4495   -150   -124   -236       C  
ATOM    778  CD1 LEU A 115      51.231  10.840   8.494  1.00 37.12           C  
ANISOU  778  CD1 LEU A 115     4604   4624   4877   -177   -160   -266       C  
ATOM    779  CD2 LEU A 115      49.922   8.749   7.979  1.00 23.97           C  
ANISOU  779  CD2 LEU A 115     2967   3001   3140   -126   -127   -214       C  
ATOM    780  N   PRO A 116      45.393  10.118   7.707  1.00 19.56           N  
ANISOU  780  N   PRO A 116     2519   2414   2498    -74    -82   -229       N  
ATOM    781  CA  PRO A 116      44.062  10.347   8.262  1.00 20.97           C  
ANISOU  781  CA  PRO A 116     2721   2605   2642    -52    -79   -242       C  
ATOM    782  C   PRO A 116      44.132  10.341   9.797  1.00 23.02           C  
ANISOU  782  C   PRO A 116     2983   2896   2870    -46   -106   -273       C  
ATOM    783  O   PRO A 116      45.226  10.189  10.358  1.00 21.81           O  
ANISOU  783  O   PRO A 116     2813   2752   2723    -60   -131   -284       O  
ATOM    784  CB  PRO A 116      43.282   9.133   7.760  1.00 22.38           C  
ANISOU  784  CB  PRO A 116     2899   2807   2798    -38    -62   -209       C  
ATOM    785  CG  PRO A 116      44.319   8.024   7.736  1.00 16.50           C  
ANISOU  785  CG  PRO A 116     2133   2076   2059    -48    -70   -191       C  
ATOM    786  CD  PRO A 116      45.635   8.693   7.410  1.00 17.30           C  
ANISOU  786  CD  PRO A 116     2220   2154   2201    -69    -76   -199       C  
ATOM    787  N   GLY A 117      42.984  10.476  10.457  1.00 16.25           N  
ANISOU  787  N   GLY A 117     2142   2057   1976    -23   -101   -285       N  
ATOM    788  CA  GLY A 117      42.922  10.462  11.910  1.00 17.42           C  
ANISOU  788  CA  GLY A 117     2297   2241   2082    -11   -121   -313       C  
ATOM    789  C   GLY A 117      43.356   9.187  12.623  1.00 20.51           C  
ANISOU  789  C   GLY A 117     2675   2676   2441     -8   -134   -291       C  
ATOM    790  O   GLY A 117      43.514   9.182  13.844  1.00 26.85           O  
ANISOU  790  O   GLY A 117     3484   3512   3205      2   -156   -312       O  
ATOM    791  N   THR A 118      43.535   8.102  11.881  1.00 18.85           N  
ANISOU  791  N   THR A 118     2451   2467   2245    -15   -122   -250       N  
ATOM    792  CA  THR A 118      44.073   6.872  12.448  1.00 15.33           C  
ANISOU  792  CA  THR A 118     1993   2052   1779    -12   -135   -224       C  
ATOM    793  C   THR A 118      44.999   6.205  11.427  1.00 21.97           C  
ANISOU  793  C   THR A 118     2814   2873   2662    -27   -132   -199       C  
ATOM    794  O   THR A 118      44.704   6.200  10.236  1.00 29.15           O  
ANISOU  794  O   THR A 118     3723   3755   3597    -32   -109   -185       O  
ATOM    795  CB  THR A 118      42.934   5.895  12.878  1.00 19.08           C  
ANISOU  795  CB  THR A 118     2476   2557   2215      6   -114   -194       C  
ATOM    796  OG1 THR A 118      43.497   4.684  13.402  1.00 20.74           O  
ANISOU  796  OG1 THR A 118     2678   2792   2411      9   -126   -164       O  
ATOM    797  CG2 THR A 118      42.032   5.541  11.696  1.00 22.78           C  
ANISOU  797  CG2 THR A 118     2943   3004   2707      2    -84   -170       C  
ATOM    798  N   ARG A 119      46.112   5.641  11.885  1.00 27.78           N  
ANISOU  798  N   ARG A 119     3531   3625   3400    -29   -156   -192       N  
ATOM    799  CA  ARG A 119      47.066   4.974  10.985  1.00 30.21           C  
ANISOU  799  CA  ARG A 119     3816   3917   3747    -37   -152   -169       C  
ATOM    800  C   ARG A 119      46.705   3.521  10.755  1.00 26.20           C  
ANISOU  800  C   ARG A 119     3310   3415   3229    -24   -137   -130       C  
ATOM    801  O   ARG A 119      47.369   2.819   9.997  1.00 23.10           O  
ANISOU  801  O   ARG A 119     2903   3008   2864    -24   -130   -111       O  
ATOM    802  CB  ARG A 119      48.475   5.021  11.559  1.00 36.92           C  
ANISOU  802  CB  ARG A 119     4638   4779   4609    -43   -186   -181       C  
ATOM    803  CG  ARG A 119      49.113   6.385  11.563  1.00 45.10           C  
ANISOU  803  CG  ARG A 119     5664   5799   5675    -65   -203   -220       C  
ATOM    804  CD  ARG A 119      50.281   6.397  12.539  1.00 48.42           C  
ANISOU  804  CD  ARG A 119     6056   6245   6094    -69   -249   -238       C  
ATOM    805  NE  ARG A 119      49.894   6.905  13.854  1.00 52.12           N  
ANISOU  805  NE  ARG A 119     6545   6741   6515    -60   -279   -272       N  
ATOM    806  CZ  ARG A 119      50.724   7.003  14.888  1.00 60.74           C  
ANISOU  806  CZ  ARG A 119     7621   7864   7591    -58   -327   -296       C  
ATOM    807  NH1 ARG A 119      51.987   6.615  14.770  1.00 63.34           N  
ANISOU  807  NH1 ARG A 119     7909   8201   7955    -66   -350   -287       N  
ATOM    808  NH2 ARG A 119      50.292   7.490  16.041  1.00 66.04           N  
ANISOU  808  NH2 ARG A 119     8317   8563   8212    -46   -352   -331       N  
ATOM    809  N   GLN A 120      45.659   3.065  11.432  1.00 22.69           N  
ANISOU  809  N   GLN A 120     2883   2990   2746    -12   -130   -118       N  
ATOM    810  CA  GLN A 120      45.200   1.701  11.260  1.00 21.54           C  
ANISOU  810  CA  GLN A 120     2742   2844   2598     -4   -115    -79       C  
ATOM    811  C   GLN A 120      44.270   1.562  10.059  1.00 21.26           C  
ANISOU  811  C   GLN A 120     2714   2782   2581    -11    -87    -74       C  
ATOM    812  O   GLN A 120      43.144   1.095  10.191  1.00 19.28           O  
ANISOU  812  O   GLN A 120     2473   2537   2316     -9    -72    -59       O  
ATOM    813  CB  GLN A 120      44.541   1.194  12.542  1.00 26.24           C  
ANISOU  813  CB  GLN A 120     3349   3473   3147     10   -118    -61       C  
ATOM    814  CG  GLN A 120      45.544   0.912  13.645  1.00 24.42           C  
ANISOU  814  CG  GLN A 120     3112   3272   2893     23   -150    -56       C  
ATOM    815  CD  GLN A 120      46.560  -0.145  13.229  1.00 39.46           C  
ANISOU  815  CD  GLN A 120     5000   5162   4829     28   -158    -29       C  
ATOM    816  OE1 GLN A 120      46.202  -1.300  12.971  1.00 46.12           O  
ANISOU  816  OE1 GLN A 120     5850   5992   5683     34   -141      7       O  
ATOM    817  NE2 GLN A 120      47.833   0.248  13.149  1.00 37.85           N  
ANISOU  817  NE2 GLN A 120     4774   4960   4647     26   -183    -47       N  
ATOM    818  N   VAL A 121      44.756   1.990   8.891  1.00 19.45           N  
ANISOU  818  N   VAL A 121     2478   2526   2384    -19    -80    -85       N  
ATOM    819  CA  VAL A 121      44.075   1.763   7.625  1.00 17.56           C  
ANISOU  819  CA  VAL A 121     2248   2265   2161    -22    -58    -79       C  
ATOM    820  C   VAL A 121      45.052   1.143   6.637  1.00 16.82           C  
ANISOU  820  C   VAL A 121     2145   2152   2096    -21    -53    -71       C  
ATOM    821  O   VAL A 121      46.254   1.385   6.707  1.00 17.66           O  
ANISOU  821  O   VAL A 121     2234   2258   2217    -22    -61    -75       O  
ATOM    822  CB  VAL A 121      43.455   3.063   7.021  1.00 18.34           C  
ANISOU  822  CB  VAL A 121     2354   2352   2260    -27    -48   -100       C  
ATOM    823  CG1 VAL A 121      42.652   3.830   8.067  1.00 14.96           C  
ANISOU  823  CG1 VAL A 121     1934   1943   1806    -22    -53   -115       C  
ATOM    824  CG2 VAL A 121      44.506   3.953   6.449  1.00 18.60           C  
ANISOU  824  CG2 VAL A 121     2380   2368   2318    -34    -49   -113       C  
ATOM    825  N   THR A 122      44.537   0.334   5.718  1.00 14.68           N  
ANISOU  825  N   THR A 122     1882   1865   1832    -19    -39    -62       N  
ATOM    826  CA  THR A 122      45.388  -0.270   4.711  1.00 14.10           C  
ANISOU  826  CA  THR A 122     1804   1774   1780    -12    -30    -59       C  
ATOM    827  C   THR A 122      45.575   0.679   3.539  1.00 15.43           C  
ANISOU  827  C   THR A 122     1974   1932   1955    -15    -14    -72       C  
ATOM    828  O   THR A 122      44.727   1.534   3.294  1.00 14.57           O  
ANISOU  828  O   THR A 122     1877   1823   1835    -20    -10    -80       O  
ATOM    829  CB  THR A 122      44.808  -1.607   4.181  1.00 15.79           C  
ANISOU  829  CB  THR A 122     2031   1971   1999     -7    -24    -50       C  
ATOM    830  OG1 THR A 122      43.592  -1.356   3.465  1.00 14.49           O  
ANISOU  830  OG1 THR A 122     1880   1802   1825    -13    -18    -60       O  
ATOM    831  CG2 THR A 122      44.551  -2.588   5.335  1.00 10.56           C  
ANISOU  831  CG2 THR A 122     1367   1312   1332     -5    -35    -29       C  
ATOM    832  N   VAL A 123      46.683   0.516   2.819  1.00 15.98           N  
ANISOU  832  N   VAL A 123     2033   1994   2044     -9     -2    -70       N  
ATOM    833  CA  VAL A 123      46.910   1.220   1.561  1.00 16.37           C  
ANISOU  833  CA  VAL A 123     2087   2035   2098     -8     20    -73       C  
ATOM    834  C   VAL A 123      45.743   1.047   0.569  1.00 18.14           C  
ANISOU  834  C   VAL A 123     2338   2253   2302     -2     28    -78       C  
ATOM    835  O   VAL A 123      45.320   2.011  -0.078  1.00 16.77           O  
ANISOU  835  O   VAL A 123     2176   2077   2120     -3     38    -80       O  
ATOM    836  CB  VAL A 123      48.239   0.785   0.913  1.00 19.44           C  
ANISOU  836  CB  VAL A 123     2458   2422   2508      3     38    -68       C  
ATOM    837  CG1 VAL A 123      48.390   1.414  -0.486  1.00 12.63           C  
ANISOU  837  CG1 VAL A 123     1603   1553   1641      7     68    -66       C  
ATOM    838  CG2 VAL A 123      49.408   1.177   1.820  1.00 15.00           C  
ANISOU  838  CG2 VAL A 123     1861   1869   1969     -6     26    -65       C  
ATOM    839  N   GLY A 124      45.215  -0.172   0.474  1.00 10.00           N  
ANISOU  839  N   GLY A 124     1317   1217   1266      5     22    -80       N  
ATOM    840  CA  GLY A 124      44.049  -0.443  -0.347  1.00  7.33           C  
ANISOU  840  CA  GLY A 124      999    874    911      8     20    -89       C  
ATOM    841  C   GLY A 124      42.833   0.364   0.064  1.00 17.18           C  
ANISOU  841  C   GLY A 124     2251   2131   2146     -2     10    -90       C  
ATOM    842  O   GLY A 124      42.160   0.955  -0.782  1.00 15.01           O  
ANISOU  842  O   GLY A 124     1987   1858   1856      3     13    -95       O  
ATOM    843  N   GLY A 125      42.554   0.405   1.367  1.00 19.45           N  
ANISOU  843  N   GLY A 125     2528   2428   2436    -12     -1    -85       N  
ATOM    844  CA  GLY A 125      41.481   1.234   1.888  1.00 16.03           C  
ANISOU  844  CA  GLY A 125     2095   2006   1991    -16     -7    -87       C  
ATOM    845  C   GLY A 125      41.739   2.720   1.692  1.00 18.81           C  
ANISOU  845  C   GLY A 125     2449   2356   2340    -14      0    -92       C  
ATOM    846  O   GLY A 125      40.803   3.509   1.495  1.00 16.89           O  
ANISOU  846  O   GLY A 125     2213   2117   2088    -10      0    -97       O  
ATOM    847  N   ALA A 126      43.013   3.105   1.747  1.00 12.27           N  
ANISOU  847  N   ALA A 126     1614   1522   1525    -17      6    -91       N  
ATOM    848  CA  ALA A 126      43.393   4.504   1.571  1.00 13.39           C  
ANISOU  848  CA  ALA A 126     1758   1655   1676    -20     14    -94       C  
ATOM    849  C   ALA A 126      43.117   4.967   0.138  1.00 15.86           C  
ANISOU  849  C   ALA A 126     2087   1958   1983    -10     30    -87       C  
ATOM    850  O   ALA A 126      42.643   6.076  -0.086  1.00 16.64           O  
ANISOU  850  O   ALA A 126     2195   2047   2079     -7     34    -86       O  
ATOM    851  CB  ALA A 126      44.862   4.716   1.933  1.00 13.02           C  
ANISOU  851  CB  ALA A 126     1692   1603   1652    -30     15    -93       C  
ATOM    852  N   ILE A 127      43.406   4.097  -0.822  1.00 11.00           N  
ANISOU  852  N   ILE A 127     1476   1343   1361     -2     39    -82       N  
ATOM    853  CA  ILE A 127      43.189   4.399  -2.223  1.00 14.16           C  
ANISOU  853  CA  ILE A 127     1894   1741   1746     12     54    -75       C  
ATOM    854  C   ILE A 127      41.698   4.317  -2.587  1.00 15.87           C  
ANISOU  854  C   ILE A 127     2125   1967   1939     22     39    -81       C  
ATOM    855  O   ILE A 127      41.144   5.226  -3.210  1.00 14.50           O  
ANISOU  855  O   ILE A 127     1964   1791   1753     33     42    -74       O  
ATOM    856  CB  ILE A 127      43.988   3.436  -3.115  1.00 14.48           C  
ANISOU  856  CB  ILE A 127     1937   1784   1782     22     69    -74       C  
ATOM    857  CG1 ILE A 127      45.480   3.582  -2.841  1.00 15.74           C  
ANISOU  857  CG1 ILE A 127     2074   1938   1967     14     87    -65       C  
ATOM    858  CG2 ILE A 127      43.653   3.664  -4.595  1.00 19.71           C  
ANISOU  858  CG2 ILE A 127     2624   2451   2415     41     83    -68       C  
ATOM    859  CD1 ILE A 127      46.365   2.649  -3.694  1.00  7.64           C  
ANISOU  859  CD1 ILE A 127     1047    917    940     30    107    -64       C  
ATOM    860  N   ALA A 128      41.059   3.224  -2.184  1.00 10.71           N  
ANISOU  860  N   ALA A 128     1466   1321   1283     18     21    -93       N  
ATOM    861  CA  ALA A 128      39.649   2.998  -2.462  1.00 11.47           C  
ANISOU  861  CA  ALA A 128     1566   1428   1365     23      4   -101       C  
ATOM    862  C   ALA A 128      38.717   4.100  -1.933  1.00 14.68           C  
ANISOU  862  C   ALA A 128     1968   1840   1770     26     -2    -98       C  
ATOM    863  O   ALA A 128      37.682   4.361  -2.523  1.00 17.71           O  
ANISOU  863  O   ALA A 128     2355   2233   2140     38    -13   -100       O  
ATOM    864  CB  ALA A 128      39.223   1.645  -1.937  1.00  4.96           C  
ANISOU  864  CB  ALA A 128      731    604    549     11    -10   -109       C  
ATOM    865  N   CYS A 129      39.062   4.735  -0.821  1.00 16.23           N  
ANISOU  865  N   CYS A 129     2155   2031   1979     18      3    -96       N  
ATOM    866  CA  CYS A 129      38.238   5.830  -0.309  1.00  5.87           C  
ANISOU  866  CA  CYS A 129      841    722    666     26      0    -98       C  
ATOM    867  C   CYS A 129      38.877   7.195  -0.563  1.00  6.31           C  
ANISOU  867  C   CYS A 129      911    757    731     32     12    -92       C  
ATOM    868  O   CYS A 129      38.360   8.213  -0.097  1.00 12.92           O  
ANISOU  868  O   CYS A 129     1751   1587   1572     41     12    -97       O  
ATOM    869  CB  CYS A 129      37.958   5.667   1.198  1.00  9.40           C  
ANISOU  869  CB  CYS A 129     1274   1181   1117     17     -5   -106       C  
ATOM    870  SG  CYS A 129      36.684   4.453   1.604  1.00 18.96           S  
ANISOU  870  SG  CYS A 129     2466   2415   2323     12    -15   -106       S  
ATOM    871  N   ASP A 130      39.982   7.191  -1.311  1.00 12.77           N  
ANISOU  871  N   ASP A 130     1736   1561   1554     28     26    -82       N  
ATOM    872  CA  ASP A 130      40.761   8.391  -1.638  1.00 10.37           C  
ANISOU  872  CA  ASP A 130     1442   1233   1266     27     43    -70       C  
ATOM    873  C   ASP A 130      40.874   9.316  -0.431  1.00 10.27           C  
ANISOU  873  C   ASP A 130     1424   1205   1274     17     38    -83       C  
ATOM    874  O   ASP A 130      40.519  10.491  -0.500  1.00  9.77           O  
ANISOU  874  O   ASP A 130     1372   1120   1219     26     42    -81       O  
ATOM    875  CB  ASP A 130      40.149   9.113  -2.837  1.00 12.96           C  
ANISOU  875  CB  ASP A 130     1791   1555   1579     49     51    -52       C  
ATOM    876  CG  ASP A 130      41.068  10.180  -3.420  1.00 19.64           C  
ANISOU  876  CG  ASP A 130     2648   2371   2441     46     75    -29       C  
ATOM    877  OD1 ASP A 130      42.283  10.188  -3.109  1.00 21.15           O  
ANISOU  877  OD1 ASP A 130     2827   2550   2657     24     88    -28       O  
ATOM    878  OD2 ASP A 130      40.566  11.012  -4.208  1.00 21.04           O  
ANISOU  878  OD2 ASP A 130     2847   2538   2610     66     82     -9       O  
ATOM    879  N   ILE A 131      41.364   8.764   0.676  1.00 13.70           N  
ANISOU  879  N   ILE A 131     1841   1649   1715      1     28    -98       N  
ATOM    880  CA  ILE A 131      41.304   9.441   1.974  1.00 13.41           C  
ANISOU  880  CA  ILE A 131     1800   1607   1686     -5     17   -119       C  
ATOM    881  C   ILE A 131      42.043  10.777   1.998  1.00 15.22           C  
ANISOU  881  C   ILE A 131     2036   1800   1945    -15     22   -124       C  
ATOM    882  O   ILE A 131      42.981  10.998   1.221  1.00 14.57           O  
ANISOU  882  O   ILE A 131     1951   1700   1883    -27     37   -107       O  
ATOM    883  CB  ILE A 131      41.854   8.564   3.107  1.00 10.44           C  
ANISOU  883  CB  ILE A 131     1407   1252   1306    -17      3   -131       C  
ATOM    884  CG1 ILE A 131      43.353   8.306   2.908  1.00 13.35           C  
ANISOU  884  CG1 ILE A 131     1762   1613   1698    -35      6   -124       C  
ATOM    885  CG2 ILE A 131      41.060   7.261   3.219  1.00 13.92           C  
ANISOU  885  CG2 ILE A 131     1843   1721   1724    -10     -1   -124       C  
ATOM    886  CD1 ILE A 131      43.987   7.566   4.071  1.00 14.09           C  
ANISOU  886  CD1 ILE A 131     1838   1727   1788    -44    -12   -134       C  
ATOM    887  N   HIS A 132      41.602  11.654   2.900  1.00 13.47           N  
ANISOU  887  N   HIS A 132     1822   1569   1728    -10     12   -147       N  
ATOM    888  CA  HIS A 132      42.173  12.989   3.058  1.00 14.45           C  
ANISOU  888  CA  HIS A 132     1953   1650   1885    -22     13   -159       C  
ATOM    889  C   HIS A 132      42.761  13.130   4.442  1.00 16.39           C  
ANISOU  889  C   HIS A 132     2190   1900   2138    -38     -8   -194       C  
ATOM    890  O   HIS A 132      42.414  12.382   5.346  1.00 13.33           O  
ANISOU  890  O   HIS A 132     1796   1550   1721    -31    -22   -209       O  
ATOM    891  CB  HIS A 132      41.096  14.066   2.859  1.00 18.67           C  
ANISOU  891  CB  HIS A 132     2511   2160   2421      4     18   -162       C  
ATOM    892  CG  HIS A 132      39.864  13.841   3.675  1.00 18.29           C  
ANISOU  892  CG  HIS A 132     2465   2142   2343     28      8   -182       C  
ATOM    893  ND1 HIS A 132      38.834  13.019   3.259  1.00 16.03           N  
ANISOU  893  ND1 HIS A 132     2173   1891   2029     48     11   -166       N  
ATOM    894  CD2 HIS A 132      39.508  14.298   4.898  1.00 12.58           C  
ANISOU  894  CD2 HIS A 132     1746   1423   1613     37     -3   -218       C  
ATOM    895  CE1 HIS A 132      37.891  13.001   4.182  1.00 15.18           C  
ANISOU  895  CE1 HIS A 132     2061   1806   1901     65      5   -187       C  
ATOM    896  NE2 HIS A 132      38.277  13.766   5.191  1.00 13.38           N  
ANISOU  896  NE2 HIS A 132     1841   1561   1682     62     -1   -218       N  
ATOM    897  N   GLY A 133      43.640  14.106   4.613  1.00 18.73           N  
ANISOU  897  N   GLY A 133     2485   2159   2473    -59    -13   -209       N  
ATOM    898  CA  GLY A 133      44.240  14.331   5.903  1.00 13.22           C  
ANISOU  898  CA  GLY A 133     1778   1464   1780    -75    -40   -249       C  
ATOM    899  C   GLY A 133      44.304  15.803   6.227  1.00 20.01           C  
ANISOU  899  C   GLY A 133     2655   2273   2674    -82    -47   -279       C  
ATOM    900  O   GLY A 133      43.782  16.640   5.497  1.00 22.13           O  
ANISOU  900  O   GLY A 133     2944   2502   2961    -71    -29   -265       O  
ATOM    901  N   LYS A 134      44.966  16.108   7.335  1.00 20.14           N  
ANISOU  901  N   LYS A 134     2664   2290   2700   -100    -77   -322       N  
ATOM    902  CA  LYS A 134      45.105  17.461   7.832  1.00 17.15           C  
ANISOU  902  CA  LYS A 134     2302   1860   2355   -110    -91   -363       C  
ATOM    903  C   LYS A 134      45.830  18.365   6.820  1.00 18.02           C  
ANISOU  903  C   LYS A 134     2409   1906   2533   -140    -73   -340       C  
ATOM    904  O   LYS A 134      45.714  19.593   6.862  1.00 20.02           O  
ANISOU  904  O   LYS A 134     2684   2100   2823   -144    -74   -361       O  
ATOM    905  CB  LYS A 134      45.839  17.401   9.173  1.00 18.09           C  
ANISOU  905  CB  LYS A 134     2408   2001   2466   -127   -133   -414       C  
ATOM    906  CG  LYS A 134      45.789  18.655   9.989  1.00 28.47           C  
ANISOU  906  CG  LYS A 134     3745   3274   3800   -129   -156   -474       C  
ATOM    907  CD  LYS A 134      46.222  18.364  11.413  1.00 34.35           C  
ANISOU  907  CD  LYS A 134     4481   4061   4509   -132   -200   -527       C  
ATOM    908  CE  LYS A 134      46.395  19.647  12.218  1.00 30.74           C  
ANISOU  908  CE  LYS A 134     4045   3569   4065   -139   -220   -572       C  
ATOM    909  NZ  LYS A 134      46.870  19.353  13.600  1.00 29.17           N  
ANISOU  909  NZ  LYS A 134     3839   3423   3820   -138   -258   -607       N  
ATOM    910  N   ASN A 135      46.555  17.749   5.893  1.00 11.10           N  
ANISOU  910  N   ASN A 135     1508   1039   1671   -158    -53   -294       N  
ATOM    911  CA  ASN A 135      47.293  18.500   4.883  1.00 13.01           C  
ANISOU  911  CA  ASN A 135     1743   1227   1973   -187    -29   -262       C  
ATOM    912  C   ASN A 135      46.646  18.536   3.499  1.00 16.70           C  
ANISOU  912  C   ASN A 135     2231   1682   2432   -163     13   -206       C  
ATOM    913  O   ASN A 135      47.338  18.779   2.514  1.00 22.08           O  
ANISOU  913  O   ASN A 135     2903   2339   3149   -183     41   -165       O  
ATOM    914  CB  ASN A 135      48.713  17.936   4.751  1.00 16.81           C  
ANISOU  914  CB  ASN A 135     2177   1726   2483   -224    -30   -249       C  
ATOM    915  CG  ASN A 135      48.719  16.496   4.263  1.00 25.09           C  
ANISOU  915  CG  ASN A 135     3210   2835   3488   -205    -16   -215       C  
ATOM    916  OD1 ASN A 135      47.693  15.802   4.331  1.00 23.15           O  
ANISOU  916  OD1 ASN A 135     2985   2624   3189   -170    -16   -212       O  
ATOM    917  ND2 ASN A 135      49.868  16.037   3.773  1.00 19.77           N  
ANISOU  917  ND2 ASN A 135     2498   2172   2841   -229     -3   -190       N  
ATOM    918  N   HIS A 136      45.339  18.292   3.416  1.00 16.36           N  
ANISOU  918  N   HIS A 136     2214   1661   2341   -121     16   -203       N  
ATOM    919  CA  HIS A 136      44.672  18.210   2.115  1.00 12.31           C  
ANISOU  919  CA  HIS A 136     1719   1147   1811    -94     47   -152       C  
ATOM    920  C   HIS A 136      44.800  19.456   1.240  1.00 20.85           C  
ANISOU  920  C   HIS A 136     2822   2162   2939   -100     72   -120       C  
ATOM    921  O   HIS A 136      44.938  19.357   0.018  1.00 24.13           O  
ANISOU  921  O   HIS A 136     3241   2576   3352    -95    103    -68       O  
ATOM    922  CB  HIS A 136      43.187  17.878   2.243  1.00 12.53           C  
ANISOU  922  CB  HIS A 136     1766   1206   1789    -49     41   -159       C  
ATOM    923  CG  HIS A 136      42.523  17.712   0.917  1.00 19.37           C  
ANISOU  923  CG  HIS A 136     2646   2079   2633    -22     64   -111       C  
ATOM    924  ND1 HIS A 136      41.968  18.771   0.222  1.00 21.80           N  
ANISOU  924  ND1 HIS A 136     2983   2343   2957      0     79    -87       N  
ATOM    925  CD2 HIS A 136      42.399  16.628   0.112  1.00 14.31           C  
ANISOU  925  CD2 HIS A 136     1998   1483   1957    -12     74    -83       C  
ATOM    926  CE1 HIS A 136      41.505  18.339  -0.936  1.00 18.99           C  
ANISOU  926  CE1 HIS A 136     2634   2010   2570     23     94    -45       C  
ATOM    927  NE2 HIS A 136      41.756  17.042  -1.030  1.00 18.25           N  
ANISOU  927  NE2 HIS A 136     2520   1970   2446     15     91    -45       N  
ATOM    928  N   HIS A 137      44.722  20.627   1.857  1.00 19.26           N  
ANISOU  928  N   HIS A 137     2636   1904   2776   -106     60   -151       N  
ATOM    929  CA  HIS A 137      44.789  21.870   1.098  1.00 27.43           C  
ANISOU  929  CA  HIS A 137     3696   2867   3861   -110     84   -119       C  
ATOM    930  C   HIS A 137      46.181  22.053   0.470  1.00 29.91           C  
ANISOU  930  C   HIS A 137     3985   3152   4226   -159    108    -84       C  
ATOM    931  O   HIS A 137      46.349  22.862  -0.441  1.00 33.21           O  
ANISOU  931  O   HIS A 137     4420   3519   4681   -164    139    -36       O  
ATOM    932  CB  HIS A 137      44.433  23.071   1.984  1.00 22.79           C  
ANISOU  932  CB  HIS A 137     3132   2217   3309   -107     63   -167       C  
ATOM    933  CG  HIS A 137      45.439  23.330   3.060  1.00 30.16           C  
ANISOU  933  CG  HIS A 137     4044   3131   4283   -154     35   -222       C  
ATOM    934  ND1 HIS A 137      45.572  22.512   4.163  1.00 23.61           N  
ANISOU  934  ND1 HIS A 137     3194   2360   3418   -157      2   -271       N  
ATOM    935  CD2 HIS A 137      46.391  24.285   3.181  1.00 30.99           C  
ANISOU  935  CD2 HIS A 137     4144   3167   4464   -200     32   -233       C  
ATOM    936  CE1 HIS A 137      46.554  22.962   4.923  1.00 28.84           C  
ANISOU  936  CE1 HIS A 137     3838   2993   4125   -200    -24   -314       C  
ATOM    937  NE2 HIS A 137      47.066  24.038   4.351  1.00 30.27           N  
ANISOU  937  NE2 HIS A 137     4028   3106   4369   -227     -8   -289       N  
ATOM    938  N   SER A 138      47.171  21.298   0.946  1.00 25.99           N  
ANISOU  938  N   SER A 138     3448   2693   3735   -192     95   -103       N  
ATOM    939  CA  SER A 138      48.518  21.368   0.369  1.00 22.66           C  
ANISOU  939  CA  SER A 138     2992   2255   3363   -238    120    -69       C  
ATOM    940  C   SER A 138      48.963  20.107  -0.382  1.00 26.74           C  
ANISOU  940  C   SER A 138     3482   2837   3841   -231    143    -32       C  
ATOM    941  O   SER A 138      49.810  20.187  -1.261  1.00 26.79           O  
ANISOU  941  O   SER A 138     3469   2833   3876   -253    180     14       O  
ATOM    942  CB  SER A 138      49.564  21.733   1.437  1.00 21.72           C  
ANISOU  942  CB  SER A 138     2839   2113   3301   -288     88   -119       C  
ATOM    943  OG  SER A 138      49.757  20.687   2.377  1.00 25.90           O  
ANISOU  943  OG  SER A 138     3342   2707   3792   -286     52   -161       O  
ATOM    944  N   ALA A 139      48.407  18.948  -0.037  1.00 24.83           N  
ANISOU  944  N   ALA A 139     3239   2658   3536   -202    123    -52       N  
ATOM    945  CA  ALA A 139      48.878  17.687  -0.613  1.00 18.65           C  
ANISOU  945  CA  ALA A 139     2431   1933   2721   -196    140    -27       C  
ATOM    946  C   ALA A 139      47.834  16.959  -1.456  1.00 23.00           C  
ANISOU  946  C   ALA A 139     3010   2521   3207   -150    154     -2       C  
ATOM    947  O   ALA A 139      48.127  15.912  -2.035  1.00 24.67           O  
ANISOU  947  O   ALA A 139     3208   2776   3389   -140    168     17       O  
ATOM    948  CB  ALA A 139      49.388  16.758   0.494  1.00 17.84           C  
ANISOU  948  CB  ALA A 139     2294   1874   2610   -208    104    -70       C  
ATOM    949  N   GLY A 140      46.622  17.502  -1.514  1.00 15.83           N  
ANISOU  949  N   GLY A 140     2140   1596   2278   -120    147     -3       N  
ATOM    950  CA  GLY A 140      45.507  16.787  -2.103  1.00 17.13           C  
ANISOU  950  CA  GLY A 140     2326   1800   2382    -77    147      9       C  
ATOM    951  C   GLY A 140      45.171  15.565  -1.263  1.00 17.52           C  
ANISOU  951  C   GLY A 140     2360   1903   2395    -70    118    -28       C  
ATOM    952  O   GLY A 140      45.501  15.499  -0.067  1.00 19.32           O  
ANISOU  952  O   GLY A 140     2570   2133   2638    -88     92    -66       O  
ATOM    953  N   SER A 141      44.521  14.588  -1.880  1.00 12.35           N  
ANISOU  953  N   SER A 141     1711   1289   1692    -43    120    -16       N  
ATOM    954  CA  SER A 141      44.179  13.361  -1.168  1.00 14.35           C  
ANISOU  954  CA  SER A 141     1950   1587   1915    -37     96    -43       C  
ATOM    955  C   SER A 141      45.133  12.209  -1.516  1.00 19.32           C  
ANISOU  955  C   SER A 141     2557   2245   2539    -47    106    -34       C  
ATOM    956  O   SER A 141      46.086  12.389  -2.274  1.00 17.37           O  
ANISOU  956  O   SER A 141     2301   1987   2310    -59    133     -9       O  
ATOM    957  CB  SER A 141      42.723  12.972  -1.421  1.00 18.72           C  
ANISOU  957  CB  SER A 141     2521   2164   2426     -4     85    -45       C  
ATOM    958  OG  SER A 141      42.435  12.972  -2.805  1.00 19.78           O  
ANISOU  958  OG  SER A 141     2674   2303   2539     17    104    -11       O  
ATOM    959  N   PHE A 142      44.867  11.030  -0.957  1.00 19.79           N  
ANISOU  959  N   PHE A 142     2605   2339   2574    -42     87    -53       N  
ATOM    960  CA  PHE A 142      45.791   9.907  -1.067  1.00 18.95           C  
ANISOU  960  CA  PHE A 142     2477   2255   2467    -49     92    -50       C  
ATOM    961  C   PHE A 142      46.034   9.515  -2.522  1.00 19.90           C  
ANISOU  961  C   PHE A 142     2606   2383   2571    -34    122    -22       C  
ATOM    962  O   PHE A 142      47.165   9.204  -2.918  1.00 14.94           O  
ANISOU  962  O   PHE A 142     1959   1759   1959    -42    143    -10       O  
ATOM    963  CB  PHE A 142      45.279   8.712  -0.269  1.00 12.23           C  
ANISOU  963  CB  PHE A 142     1620   1434   1592    -41     67    -70       C  
ATOM    964  CG  PHE A 142      46.339   7.710   0.065  1.00 16.45           C  
ANISOU  964  CG  PHE A 142     2128   1984   2137    -49     65    -72       C  
ATOM    965  CD1 PHE A 142      46.589   6.645  -0.776  1.00 16.78           C  
ANISOU  965  CD1 PHE A 142     2169   2039   2166    -36     79    -61       C  
ATOM    966  CD2 PHE A 142      47.091   7.838   1.219  1.00 16.37           C  
ANISOU  966  CD2 PHE A 142     2095   1976   2149    -67     46    -87       C  
ATOM    967  CE1 PHE A 142      47.557   5.713  -0.472  1.00 13.08           C  
ANISOU  967  CE1 PHE A 142     1677   1583   1710    -38     77    -62       C  
ATOM    968  CE2 PHE A 142      48.069   6.917   1.527  1.00 16.75           C  
ANISOU  968  CE2 PHE A 142     2117   2041   2208    -69     41    -86       C  
ATOM    969  CZ  PHE A 142      48.303   5.844   0.675  1.00 10.93           C  
ANISOU  969  CZ  PHE A 142     1377   1313   1461    -54     58    -72       C  
ATOM    970  N   GLY A 143      44.970   9.559  -3.315  1.00 15.43           N  
ANISOU  970  N   GLY A 143     2068   1822   1972    -10    124    -13       N  
ATOM    971  CA  GLY A 143      45.069   9.295  -4.739  1.00 15.62           C  
ANISOU  971  CA  GLY A 143     2108   1857   1970      9    150     11       C  
ATOM    972  C   GLY A 143      46.073  10.151  -5.488  1.00 15.76           C  
ANISOU  972  C   GLY A 143     2124   1855   2008      1    188     44       C  
ATOM    973  O   GLY A 143      46.661   9.684  -6.459  1.00 20.88           O  
ANISOU  973  O   GLY A 143     2774   2519   2639     12    217     62       O  
ATOM    974  N   ASN A 144      46.281  11.391  -5.041  1.00 17.08           N  
ANISOU  974  N   ASN A 144     2288   1987   2213    -19    192     52       N  
ATOM    975  CA  ASN A 144      47.213  12.301  -5.716  1.00 23.61           C  
ANISOU  975  CA  ASN A 144     3112   2788   3070    -32    231     89       C  
ATOM    976  C   ASN A 144      48.649  11.778  -5.652  1.00 27.17           C  
ANISOU  976  C   ASN A 144     3523   3250   3550    -54    252     92       C  
ATOM    977  O   ASN A 144      49.509  12.252  -6.374  1.00 20.07           O  
ANISOU  977  O   ASN A 144     2614   2341   2671    -64    292    127       O  
ATOM    978  CB  ASN A 144      47.176  13.734  -5.130  1.00 17.38           C  
ANISOU  978  CB  ASN A 144     2326   1949   2328    -54    226     92       C  
ATOM    979  CG  ASN A 144      45.789  14.384  -5.205  1.00 22.43           C  
ANISOU  979  CG  ASN A 144     3003   2575   2945    -28    209     92       C  
ATOM    980  OD1 ASN A 144      44.788  13.799  -4.786  1.00 16.84           O  
ANISOU  980  OD1 ASN A 144     2302   1891   2205     -9    179     65       O  
ATOM    981  ND2 ASN A 144      45.736  15.609  -5.740  1.00 20.03           N  
ANISOU  981  ND2 ASN A 144     2720   2229   2661    -27    230    126       N  
ATOM    982  N   HIS A 145      48.901  10.798  -4.790  1.00 24.35           N  
ANISOU  982  N   HIS A 145     3141   2915   3195    -59    226     59       N  
ATOM    983  CA  HIS A 145      50.268  10.372  -4.527  1.00 24.25           C  
ANISOU  983  CA  HIS A 145     3084   2911   3217    -79    238     59       C  
ATOM    984  C   HIS A 145      50.501   8.939  -4.972  1.00 25.20           C  
ANISOU  984  C   HIS A 145     3199   3069   3306    -53    245     53       C  
ATOM    985  O   HIS A 145      51.574   8.372  -4.758  1.00 18.89           O  
ANISOU  985  O   HIS A 145     2363   2284   2532    -60    253     51       O  
ATOM    986  CB  HIS A 145      50.613  10.566  -3.045  1.00 19.80           C  
ANISOU  986  CB  HIS A 145     2492   2338   2692   -107    199     27       C  
ATOM    987  CG  HIS A 145      50.398  11.972  -2.571  1.00 21.39           C  
ANISOU  987  CG  HIS A 145     2702   2498   2927   -131    190     23       C  
ATOM    988  ND1 HIS A 145      51.394  12.921  -2.589  1.00 17.46           N  
ANISOU  988  ND1 HIS A 145     2178   1970   2487   -166    207     37       N  
ATOM    989  CD2 HIS A 145      49.288  12.595  -2.105  1.00 17.89           C  
ANISOU  989  CD2 HIS A 145     2290   2035   2471   -125    166      7       C  
ATOM    990  CE1 HIS A 145      50.912  14.069  -2.140  1.00 22.44           C  
ANISOU  990  CE1 HIS A 145     2827   2558   3140   -180    192     27       C  
ATOM    991  NE2 HIS A 145      49.640  13.897  -1.836  1.00 23.01           N  
ANISOU  991  NE2 HIS A 145     2935   2639   3169   -153    168      8       N  
ATOM    992  N   VAL A 146      49.494   8.356  -5.607  1.00 19.14           N  
ANISOU  992  N   VAL A 146     2469   2317   2487    -23    241     49       N  
ATOM    993  CA  VAL A 146      49.650   7.014  -6.137  1.00 14.24           C  
ANISOU  993  CA  VAL A 146     1850   1725   1836      3    248     40       C  
ATOM    994  C   VAL A 146      50.319   7.118  -7.493  1.00 21.04           C  
ANISOU  994  C   VAL A 146     2715   2597   2682     20    299     70       C  
ATOM    995  O   VAL A 146      49.827   7.797  -8.395  1.00 22.54           O  
ANISOU  995  O   VAL A 146     2936   2784   2844     32    318     94       O  
ATOM    996  CB  VAL A 146      48.302   6.288  -6.264  1.00 12.82           C  
ANISOU  996  CB  VAL A 146     1705   1556   1611     25    218     18       C  
ATOM    997  CG1 VAL A 146      48.496   4.921  -6.915  1.00  9.96           C  
ANISOU  997  CG1 VAL A 146     1348   1215   1221     51    226      5       C  
ATOM    998  CG2 VAL A 146      47.665   6.137  -4.906  1.00 12.41           C  
ANISOU  998  CG2 VAL A 146     1645   1498   1573     10    175     -6       C  
ATOM    999  N   ARG A 147      51.458   6.456  -7.630  1.00 19.65           N  
ANISOU  999  N   ARG A 147     2507   2436   2522     24    323     72       N  
ATOM   1000  CA  ARG A 147      52.205   6.512  -8.871  1.00 23.80           C  
ANISOU 1000  CA  ARG A 147     3032   2977   3033     42    379    101       C  
ATOM   1001  C   ARG A 147      51.883   5.324  -9.767  1.00 21.21           C  
ANISOU 1001  C   ARG A 147     2734   2676   2648     85    387     83       C  
ATOM   1002  O   ARG A 147      51.878   5.438 -10.988  1.00 29.62           O  
ANISOU 1002  O   ARG A 147     3825   3759   3670    111    424    102       O  
ATOM   1003  CB  ARG A 147      53.694   6.627  -8.566  1.00 37.22           C  
ANISOU 1003  CB  ARG A 147     4673   4679   4788     22    408    115       C  
ATOM   1004  CG  ARG A 147      54.045   8.026  -8.031  1.00 56.26           C  
ANISOU 1004  CG  ARG A 147     7061   7060   7255    -23    410    138       C  
ATOM   1005  CD  ARG A 147      54.351   8.971  -9.182  1.00 56.65           C  
ANISOU 1005  CD  ARG A 147     7120   7103   7300    -24    468    188       C  
ATOM   1006  NE  ARG A 147      55.444   8.401  -9.969  1.00 50.07           N  
ANISOU 1006  NE  ARG A 147     6257   6301   6465     -5    522    206       N  
ATOM   1007  CZ  ARG A 147      56.722   8.749  -9.839  1.00 42.92           C  
ANISOU 1007  CZ  ARG A 147     5292   5395   5620    -32    555    228       C  
ATOM   1008  NH1 ARG A 147      57.075   9.698  -8.978  1.00 23.37           N  
ANISOU 1008  NH1 ARG A 147     2783   2886   3211    -81    537    233       N  
ATOM   1009  NH2 ARG A 147      57.645   8.157 -10.587  1.00 48.55           N  
ANISOU 1009  NH2 ARG A 147     5979   6142   6327     -8    607    244       N  
ATOM   1010  N   SER A 148      51.580   4.187  -9.158  1.00 17.10           N  
ANISOU 1010  N   SER A 148     2213   2158   2125     93    350     45       N  
ATOM   1011  CA  SER A 148      51.042   3.071  -9.922  1.00 20.69           C  
ANISOU 1011  CA  SER A 148     2703   2629   2529    130    345     19       C  
ATOM   1012  C   SER A 148      50.302   2.133  -9.000  1.00 17.56           C  
ANISOU 1012  C   SER A 148     2312   2222   2140    125    293    -17       C  
ATOM   1013  O   SER A 148      50.465   2.180  -7.781  1.00 25.42           O  
ANISOU 1013  O   SER A 148     3279   3204   3176    100    267    -19       O  
ATOM   1014  CB  SER A 148      52.145   2.322 -10.696  1.00 22.33           C  
ANISOU 1014  CB  SER A 148     2897   2857   2729    160    390     19       C  
ATOM   1015  OG  SER A 148      52.912   1.495  -9.840  1.00 24.82           O  
ANISOU 1015  OG  SER A 148     3175   3168   3088    158    380      3       O  
ATOM   1016  N   MET A 149      49.469   1.288  -9.578  1.00 21.98           N  
ANISOU 1016  N   MET A 149     2907   2786   2658    148    275    -44       N  
ATOM   1017  CA  MET A 149      48.819   0.259  -8.787  1.00 21.02           C  
ANISOU 1017  CA  MET A 149     2788   2650   2548    143    231    -75       C  
ATOM   1018  C   MET A 149      48.486  -0.962  -9.617  1.00 21.39           C  
ANISOU 1018  C   MET A 149     2865   2700   2561    173    226   -109       C  
ATOM   1019  O   MET A 149      48.252  -0.860 -10.819  1.00 23.48           O  
ANISOU 1019  O   MET A 149     3161   2982   2779    197    242   -114       O  
ATOM   1020  CB  MET A 149      47.581   0.793  -8.073  1.00 22.81           C  
ANISOU 1020  CB  MET A 149     3024   2868   2776    119    192    -76       C  
ATOM   1021  CG  MET A 149      46.458   1.292  -8.964  1.00 29.17           C  
ANISOU 1021  CG  MET A 149     3864   3683   3536    129    183    -77       C  
ATOM   1022  SD  MET A 149      45.148   1.886  -7.869  1.00 27.17           S  
ANISOU 1022  SD  MET A 149     3607   3419   3298    101    140    -78       S  
ATOM   1023  CE  MET A 149      44.547   3.337  -8.717  1.00 16.43           C  
ANISOU 1023  CE  MET A 149     2269   2067   1906    111    150    -52       C  
ATOM   1024  N   ASP A 150      48.508  -2.119  -8.963  1.00 18.26           N  
ANISOU 1024  N   ASP A 150     2462   2285   2190    174    204   -131       N  
ATOM   1025  CA  ASP A 150      48.149  -3.376  -9.588  1.00 15.52           C  
ANISOU 1025  CA  ASP A 150     2144   1929   1822    198    192   -170       C  
ATOM   1026  C   ASP A 150      46.751  -3.743  -9.164  1.00 16.74           C  
ANISOU 1026  C   ASP A 150     2315   2068   1977    176    144   -189       C  
ATOM   1027  O   ASP A 150      46.481  -3.977  -7.983  1.00 18.74           O  
ANISOU 1027  O   ASP A 150     2550   2304   2267    152    120   -182       O  
ATOM   1028  CB  ASP A 150      49.128  -4.484  -9.191  1.00 26.78           C  
ANISOU 1028  CB  ASP A 150     3552   3338   3283    214    202   -180       C  
ATOM   1029  CG  ASP A 150      50.520  -4.273  -9.774  1.00 27.83           C  
ANISOU 1029  CG  ASP A 150     3666   3491   3417    241    253   -166       C  
ATOM   1030  OD1 ASP A 150      50.680  -3.364 -10.616  1.00 31.11           O  
ANISOU 1030  OD1 ASP A 150     4088   3933   3800    248    285   -149       O  
ATOM   1031  OD2 ASP A 150      51.446  -5.027  -9.401  1.00 29.42           O  
ANISOU 1031  OD2 ASP A 150     3844   3683   3651    258    264   -168       O  
ATOM   1032  N   LEU A 151      45.857  -3.786 -10.141  1.00 24.01           N  
ANISOU 1032  N   LEU A 151     3269   2999   2855    187    129   -212       N  
ATOM   1033  CA  LEU A 151      44.460  -4.073  -9.886  1.00 21.15           C  
ANISOU 1033  CA  LEU A 151     2917   2626   2492    166     84   -231       C  
ATOM   1034  C   LEU A 151      44.087  -5.440 -10.426  1.00 22.90           C  
ANISOU 1034  C   LEU A 151     3164   2829   2710    178     62   -278       C  
ATOM   1035  O   LEU A 151      44.205  -5.701 -11.624  1.00 23.07           O  
ANISOU 1035  O   LEU A 151     3214   2863   2688    209     70   -306       O  
ATOM   1036  CB  LEU A 151      43.587  -2.999 -10.527  1.00 20.27           C  
ANISOU 1036  CB  LEU A 151     2819   2542   2340    167     74   -222       C  
ATOM   1037  CG  LEU A 151      42.074  -3.105 -10.375  1.00 17.41           C  
ANISOU 1037  CG  LEU A 151     2461   2178   1975    148     27   -239       C  
ATOM   1038  CD1 LEU A 151      41.669  -2.879  -8.930  1.00 17.66           C  
ANISOU 1038  CD1 LEU A 151     2462   2196   2053    114     14   -218       C  
ATOM   1039  CD2 LEU A 151      41.411  -2.089 -11.292  1.00 17.11           C  
ANISOU 1039  CD2 LEU A 151     2440   2172   1888    163     22   -230       C  
ATOM   1040  N   LEU A 152      43.646  -6.317  -9.531  1.00 21.29           N  
ANISOU 1040  N   LEU A 152     2949   2591   2548    155     34   -287       N  
ATOM   1041  CA  LEU A 152      43.056  -7.585  -9.939  1.00 16.22           C  
ANISOU 1041  CA  LEU A 152     2330   1921   1913    156      6   -333       C  
ATOM   1042  C   LEU A 152      41.626  -7.325 -10.404  1.00 21.12           C  
ANISOU 1042  C   LEU A 152     2959   2555   2509    139    -33   -353       C  
ATOM   1043  O   LEU A 152      40.756  -6.949  -9.604  1.00 16.41           O  
ANISOU 1043  O   LEU A 152     2341   1961   1934    108    -54   -333       O  
ATOM   1044  CB  LEU A 152      43.064  -8.590  -8.780  1.00 14.78           C  
ANISOU 1044  CB  LEU A 152     2131   1694   1790    134     -7   -327       C  
ATOM   1045  CG  LEU A 152      42.333  -9.919  -9.017  1.00 18.37           C  
ANISOU 1045  CG  LEU A 152     2605   2106   2267    124    -40   -371       C  
ATOM   1046  CD1 LEU A 152      42.892 -10.649 -10.258  1.00 13.80           C  
ANISOU 1046  CD1 LEU A 152     2063   1518   1662    164    -32   -420       C  
ATOM   1047  CD2 LEU A 152      42.429 -10.789  -7.771  1.00 15.02           C  
ANISOU 1047  CD2 LEU A 152     2165   1638   1904    103    -45   -349       C  
ATOM   1048  N   THR A 153      41.396  -7.521 -11.701  1.00 15.55           N  
ANISOU 1048  N   THR A 153     2286   1865   1757    164    -44   -392       N  
ATOM   1049  CA  THR A 153      40.103  -7.243 -12.316  1.00 14.85           C  
ANISOU 1049  CA  THR A 153     2207   1798   1638    156    -85   -414       C  
ATOM   1050  C   THR A 153      39.309  -8.516 -12.504  1.00 17.64           C  
ANISOU 1050  C   THR A 153     2571   2118   2015    139   -129   -468       C  
ATOM   1051  O   THR A 153      39.816  -9.609 -12.262  1.00 17.85           O  
ANISOU 1051  O   THR A 153     2604   2101   2077    138   -124   -487       O  
ATOM   1052  CB  THR A 153      40.241  -6.487 -13.661  1.00 14.31           C  
ANISOU 1052  CB  THR A 153     2168   1776   1493    195    -74   -421       C  
ATOM   1053  OG1 THR A 153      41.315  -7.048 -14.423  1.00 21.51           O  
ANISOU 1053  OG1 THR A 153     3101   2687   2386    227    -41   -437       O  
ATOM   1054  CG2 THR A 153      40.543  -5.028 -13.403  1.00 10.77           C  
ANISOU 1054  CG2 THR A 153     1704   1357   1031    198    -43   -363       C  
ATOM   1055  N   ALA A 154      38.061  -8.357 -12.931  1.00 19.75           N  
ANISOU 1055  N   ALA A 154     2832   2404   2268    122   -171   -483       N  
ATOM   1056  CA  ALA A 154      37.093  -9.448 -13.009  1.00 18.52           C  
ANISOU 1056  CA  ALA A 154     2668   2220   2149     89   -213   -518       C  
ATOM   1057  C   ALA A 154      37.508 -10.542 -13.979  1.00 23.24           C  
ANISOU 1057  C   ALA A 154     3294   2800   2737    105   -211   -559       C  
ATOM   1058  O   ALA A 154      37.103 -11.693 -13.832  1.00 23.48           O  
ANISOU 1058  O   ALA A 154     3322   2787   2812     79   -233   -587       O  
ATOM   1059  CB  ALA A 154      35.718  -8.897 -13.388  1.00 18.53           C  
ANISOU 1059  CB  ALA A 154     2651   2257   2132     73   -255   -522       C  
ATOM   1060  N   ASP A 155      38.320 -10.176 -14.967  1.00 26.40           N  
ANISOU 1060  N   ASP A 155     3720   3232   3080    147   -182   -562       N  
ATOM   1061  CA  ASP A 155      38.853 -11.143 -15.926  1.00 30.36           C  
ANISOU 1061  CA  ASP A 155     4250   3721   3566    169   -174   -602       C  
ATOM   1062  C   ASP A 155      39.959 -12.028 -15.332  1.00 33.43           C  
ANISOU 1062  C   ASP A 155     4643   4060   3998    178   -142   -604       C  
ATOM   1063  O   ASP A 155      40.439 -12.949 -15.987  1.00 37.94           O  
ANISOU 1063  O   ASP A 155     5236   4612   4566    196   -133   -639       O  
ATOM   1064  CB  ASP A 155      39.328 -10.446 -17.219  1.00 30.98           C  
ANISOU 1064  CB  ASP A 155     4351   3853   3565    212   -152   -600       C  
ATOM   1065  CG  ASP A 155      40.331  -9.328 -16.963  1.00 39.52           C  
ANISOU 1065  CG  ASP A 155     5429   4963   4624    239   -102   -551       C  
ATOM   1066  OD1 ASP A 155      40.392  -8.382 -17.789  1.00 49.28           O  
ANISOU 1066  OD1 ASP A 155     6677   6247   5800    264    -89   -531       O  
ATOM   1067  OD2 ASP A 155      41.056  -9.393 -15.943  1.00 35.10           O  
ANISOU 1067  OD2 ASP A 155     4856   4375   4106    235    -75   -529       O  
ATOM   1068  N   GLY A 156      40.357 -11.744 -14.095  1.00 31.45           N  
ANISOU 1068  N   GLY A 156     4372   3790   3788    168   -124   -568       N  
ATOM   1069  CA  GLY A 156      41.389 -12.516 -13.421  1.00 29.16           C  
ANISOU 1069  CA  GLY A 156     4083   3454   3543    179    -96   -563       C  
ATOM   1070  C   GLY A 156      42.785 -12.039 -13.761  1.00 31.41           C  
ANISOU 1070  C   GLY A 156     4374   3766   3796    225    -44   -546       C  
ATOM   1071  O   GLY A 156      43.764 -12.628 -13.319  1.00 36.92           O  
ANISOU 1071  O   GLY A 156     5069   4432   4526    244    -17   -541       O  
ATOM   1072  N   GLU A 157      42.878 -10.979 -14.557  1.00 34.90           N  
ANISOU 1072  N   GLU A 157     4821   4264   4176    245    -28   -533       N  
ATOM   1073  CA  GLU A 157      44.163 -10.363 -14.876  1.00 42.68           C  
ANISOU 1073  CA  GLU A 157     5805   5279   5130    284     27   -507       C  
ATOM   1074  C   GLU A 157      44.546  -9.288 -13.855  1.00 42.00           C  
ANISOU 1074  C   GLU A 157     5695   5204   5057    279     49   -457       C  
ATOM   1075  O   GLU A 157      43.693  -8.541 -13.367  1.00 36.80           O  
ANISOU 1075  O   GLU A 157     5027   4556   4398    252     25   -438       O  
ATOM   1076  CB  GLU A 157      44.126  -9.729 -16.272  1.00 44.11           C  
ANISOU 1076  CB  GLU A 157     6006   5515   5239    308     39   -511       C  
ATOM   1077  N   ILE A 158      45.836  -9.207 -13.550  1.00 34.73           N  
ANISOU 1077  N   ILE A 158     4763   4284   4151    305     95   -435       N  
ATOM   1078  CA  ILE A 158      46.355  -8.137 -12.720  1.00 30.54           C  
ANISOU 1078  CA  ILE A 158     4193   3771   3639    288    121   -375       C  
ATOM   1079  C   ILE A 158      46.863  -7.004 -13.610  1.00 40.37           C  
ANISOU 1079  C   ILE A 158     5443   5067   4830    312    162   -350       C  
ATOM   1080  O   ILE A 158      47.858  -7.149 -14.319  1.00 44.14           O  
ANISOU 1080  O   ILE A 158     5927   5560   5285    350    206   -355       O  
ATOM   1081  CB  ILE A 158      47.457  -8.644 -11.786  1.00 31.39           C  
ANISOU 1081  CB  ILE A 158     4269   3853   3803    292    143   -354       C  
ATOM   1082  CG1 ILE A 158      46.862  -9.696 -10.841  1.00 31.93           C  
ANISOU 1082  CG1 ILE A 158     4336   3871   3926    266    103   -367       C  
ATOM   1083  CG2 ILE A 158      48.089  -7.474 -11.014  1.00 28.83           C  
ANISOU 1083  CG2 ILE A 158     3904   3553   3498    274    168   -297       C  
ATOM   1084  CD1 ILE A 158      47.797 -10.181  -9.762  1.00 31.59           C  
ANISOU 1084  CD1 ILE A 158     4263   3803   3939    269    116   -340       C  
ATOM   1085  N   ARG A 159      46.158  -5.881 -13.569  1.00 39.24           N  
ANISOU 1085  N   ARG A 159     5295   4946   4667    289    150   -322       N  
ATOM   1086  CA  ARG A 159      46.392  -4.763 -14.474  1.00 34.47           C  
ANISOU 1086  CA  ARG A 159     4703   4386   4010    309    184   -294       C  
ATOM   1087  C   ARG A 159      47.249  -3.694 -13.824  1.00 30.69           C  
ANISOU 1087  C   ARG A 159     4185   3914   3561    293    222   -237       C  
ATOM   1088  O   ARG A 159      46.875  -3.147 -12.784  1.00 33.67           O  
ANISOU 1088  O   ARG A 159     4537   4278   3978    256    201   -212       O  
ATOM   1089  CB  ARG A 159      45.056  -4.129 -14.823  1.00 35.28           C  
ANISOU 1089  CB  ARG A 159     4824   4504   4075    297    144   -296       C  
ATOM   1090  CG  ARG A 159      44.940  -3.663 -16.222  1.00 44.61           C  
ANISOU 1090  CG  ARG A 159     6037   5726   5185    328    157   -295       C  
ATOM   1091  CD  ARG A 159      43.866  -4.465 -16.907  1.00 53.14           C  
ANISOU 1091  CD  ARG A 159     7138   6808   6246    325    103   -343       C  
ATOM   1092  NE  ARG A 159      42.867  -3.603 -17.518  1.00 55.76           N  
ANISOU 1092  NE  ARG A 159     7482   7171   6535    326     77   -328       N  
ATOM   1093  CZ  ARG A 159      41.631  -3.995 -17.785  1.00 61.94           C  
ANISOU 1093  CZ  ARG A 159     8271   7954   7310    313     20   -361       C  
ATOM   1094  NH1 ARG A 159      41.252  -5.236 -17.485  1.00 60.62           N  
ANISOU 1094  NH1 ARG A 159     8100   7755   7178    294    -14   -408       N  
ATOM   1095  NH2 ARG A 159      40.776  -3.146 -18.341  1.00 64.88           N  
ANISOU 1095  NH2 ARG A 159     8651   8358   7644    319     -3   -343       N  
ATOM   1096  N   HIS A 160      48.382  -3.378 -14.444  1.00 27.29           N  
ANISOU 1096  N   HIS A 160     3749   3505   3114    320    278   -216       N  
ATOM   1097  CA  HIS A 160      49.234  -2.290 -13.972  1.00 30.98           C  
ANISOU 1097  CA  HIS A 160     4178   3981   3613    302    316   -162       C  
ATOM   1098  C   HIS A 160      48.692  -0.940 -14.448  1.00 32.36           C  
ANISOU 1098  C   HIS A 160     4366   4175   3752    294    322   -125       C  
ATOM   1099  O   HIS A 160      48.685  -0.644 -15.648  1.00 41.89           O  
ANISOU 1099  O   HIS A 160     5605   5413   4899    325    349   -119       O  
ATOM   1100  CB  HIS A 160      50.668  -2.486 -14.459  1.00 32.47           C  
ANISOU 1100  CB  HIS A 160     4348   4187   3804    333    377   -151       C  
ATOM   1101  CG  HIS A 160      51.657  -1.547 -13.836  1.00 34.73           C  
ANISOU 1101  CG  HIS A 160     4583   4475   4138    308    412   -100       C  
ATOM   1102  ND1 HIS A 160      52.195  -1.754 -12.582  1.00 35.15           N  
ANISOU 1102  ND1 HIS A 160     4591   4505   4259    283    397    -95       N  
ATOM   1103  CD2 HIS A 160      52.216  -0.404 -14.299  1.00 30.24           C  
ANISOU 1103  CD2 HIS A 160     4001   3926   3561    304    459    -53       C  
ATOM   1104  CE1 HIS A 160      53.046  -0.784 -12.304  1.00 34.36           C  
ANISOU 1104  CE1 HIS A 160     4450   4414   4192    263    429    -52       C  
ATOM   1105  NE2 HIS A 160      53.077   0.051 -13.328  1.00 32.09           N  
ANISOU 1105  NE2 HIS A 160     4180   4149   3864    273    469    -25       N  
ATOM   1106  N   LEU A 161      48.244  -0.123 -13.501  1.00 20.79           N  
ANISOU 1106  N   LEU A 161     2881   2694   2325    256    299   -101       N  
ATOM   1107  CA  LEU A 161      47.627   1.166 -13.816  1.00 23.18           C  
ANISOU 1107  CA  LEU A 161     3198   3007   2605    248    299    -66       C  
ATOM   1108  C   LEU A 161      48.499   2.349 -13.410  1.00 24.25           C  
ANISOU 1108  C   LEU A 161     3300   3134   2779    226    338    -15       C  
ATOM   1109  O   LEU A 161      49.162   2.335 -12.367  1.00 18.49           O  
ANISOU 1109  O   LEU A 161     2530   2386   2108    199    338    -11       O  
ATOM   1110  CB  LEU A 161      46.264   1.288 -13.113  1.00 27.52           C  
ANISOU 1110  CB  LEU A 161     3752   3541   3164    225    241    -81       C  
ATOM   1111  CG  LEU A 161      45.274   0.119 -13.225  1.00 28.80           C  
ANISOU 1111  CG  LEU A 161     3934   3700   3307    232    193   -132       C  
ATOM   1112  CD1 LEU A 161      43.957   0.466 -12.577  1.00 24.25           C  
ANISOU 1112  CD1 LEU A 161     3355   3116   2744    208    144   -135       C  
ATOM   1113  CD2 LEU A 161      45.060  -0.285 -14.681  1.00 30.33           C  
ANISOU 1113  CD2 LEU A 161     4170   3922   3430    272    197   -155       C  
ATOM   1114  N   THR A 162      48.467   3.389 -14.227  1.00 24.62           N  
ANISOU 1114  N   THR A 162     3366   3195   2794    236    367     24       N  
ATOM   1115  CA  THR A 162      49.188   4.620 -13.938  1.00 19.66           C  
ANISOU 1115  CA  THR A 162     2711   2553   2206    211    403     74       C  
ATOM   1116  C   THR A 162      48.232   5.795 -14.136  1.00 24.71           C  
ANISOU 1116  C   THR A 162     3377   3184   2828    207    389    103       C  
ATOM   1117  O   THR A 162      47.239   5.681 -14.859  1.00 25.32           O  
ANISOU 1117  O   THR A 162     3494   3280   2848    234    366     93       O  
ATOM   1118  CB  THR A 162      50.455   4.772 -14.838  1.00 32.41           C  
ANISOU 1118  CB  THR A 162     4316   4190   3809    230    475    108       C  
ATOM   1119  OG1 THR A 162      50.077   4.877 -16.215  1.00 24.29           O  
ANISOU 1119  OG1 THR A 162     3335   3193   2701    270    497    121       O  
ATOM   1120  CG2 THR A 162      51.395   3.574 -14.671  1.00 23.56           C  
ANISOU 1120  CG2 THR A 162     3167   3079   2706    242    490     77       C  
ATOM   1121  N   PRO A 163      48.510   6.926 -13.473  1.00 26.73           N  
ANISOU 1121  N   PRO A 163     3609   3411   3136    174    398    137       N  
ATOM   1122  CA  PRO A 163      47.565   8.053 -13.528  1.00 25.01           C  
ANISOU 1122  CA  PRO A 163     3416   3177   2910    171    381    162       C  
ATOM   1123  C   PRO A 163      47.543   8.853 -14.849  1.00 27.97           C  
ANISOU 1123  C   PRO A 163     3826   3565   3235    200    421    213       C  
ATOM   1124  O   PRO A 163      46.663   9.691 -15.038  1.00 30.07           O  
ANISOU 1124  O   PRO A 163     4118   3821   3486    208    404    234       O  
ATOM   1125  CB  PRO A 163      48.007   8.936 -12.357  1.00 21.04           C  
ANISOU 1125  CB  PRO A 163     2878   2633   2484    127    380    175       C  
ATOM   1126  CG  PRO A 163      49.455   8.572 -12.125  1.00 17.20           C  
ANISOU 1126  CG  PRO A 163     2349   2149   2038    109    416    178       C  
ATOM   1127  CD  PRO A 163      49.558   7.118 -12.451  1.00 18.27           C  
ANISOU 1127  CD  PRO A 163     2487   2316   2138    136    411    141       C  
ATOM   1128  N   THR A 164      48.477   8.595 -15.755  1.00 31.57           N  
ANISOU 1128  N   THR A 164     4284   4048   3664    219    475    234       N  
ATOM   1129  CA  THR A 164      48.510   9.321 -17.022  1.00 34.13           C  
ANISOU 1129  CA  THR A 164     4644   4390   3934    249    519    289       C  
ATOM   1130  C   THR A 164      48.634   8.379 -18.198  1.00 43.24           C  
ANISOU 1130  C   THR A 164     5827   5596   5007    297    538    272       C  
ATOM   1131  O   THR A 164      48.665   8.816 -19.343  1.00 55.94           O  
ANISOU 1131  O   THR A 164     7456   7224   6575    320    555    303       O  
ATOM   1132  CB  THR A 164      49.707  10.272 -17.105  1.00 33.47           C  
ANISOU 1132  CB  THR A 164     4533   4286   3898    224    586    350       C  
ATOM   1133  OG1 THR A 164      50.920   9.515 -17.010  1.00 37.92           O  
ANISOU 1133  OG1 THR A 164     5056   4865   4485    217    623    336       O  
ATOM   1134  CG2 THR A 164      49.669  11.302 -15.985  1.00 35.02           C  
ANISOU 1134  CG2 THR A 164     4703   4425   4178    175    568    363       C  
ATOM   1135  N   GLY A 165      48.719   7.086 -17.919  1.00 38.55           N  
ANISOU 1135  N   GLY A 165     5223   5017   4410    303    515    213       N  
ATOM   1136  CA  GLY A 165      48.907   6.105 -18.971  1.00 43.47           C  
ANISOU 1136  CA  GLY A 165     5863   5678   4976    340    517    181       C  
ATOM   1137  C   GLY A 165      47.683   5.855 -19.831  1.00 46.82           C  
ANISOU 1137  C   GLY A 165     6332   6127   5331    371    466    156       C  
ATOM   1138  O   GLY A 165      46.781   6.694 -19.947  1.00 49.15           O  
ANISOU 1138  O   GLY A 165     6648   6417   5609    374    442    181       O  
ATOM   1139  N   GLU A 166      47.661   4.684 -20.454  1.00 46.79           N  
ANISOU 1139  N   GLU A 166     6340   6148   5291    395    448    105       N  
ATOM   1140  CA  GLU A 166      46.553   4.307 -21.317  1.00 44.92           C  
ANISOU 1140  CA  GLU A 166     6139   5936   4992    421    395     72       C  
ATOM   1141  C   GLU A 166      45.362   3.897 -20.460  1.00 43.10           C  
ANISOU 1141  C   GLU A 166     5911   5688   4777    406    329     29       C  
ATOM   1142  O   GLU A 166      44.217   3.993 -20.891  1.00 44.03           O  
ANISOU 1142  O   GLU A 166     6049   5819   4860    418    280     16       O  
ATOM   1143  CB  GLU A 166      46.969   3.156 -22.244  1.00 41.48           C  
ANISOU 1143  CB  GLU A 166     5715   5527   4518    448    399     28       C  
ATOM   1144  N   ASP A 167      45.642   3.445 -19.239  1.00 37.88           N  
ANISOU 1144  N   ASP A 167     5224   5000   4171    379    328      8       N  
ATOM   1145  CA  ASP A 167      44.596   3.000 -18.335  1.00 45.14           C  
ANISOU 1145  CA  ASP A 167     6141   5901   5110    362    269    -33       C  
ATOM   1146  C   ASP A 167      44.242   4.065 -17.284  1.00 35.92           C  
ANISOU 1146  C   ASP A 167     4950   4703   3994    328    260      3       C  
ATOM   1147  O   ASP A 167      43.698   3.742 -16.227  1.00 27.05           O  
ANISOU 1147  O   ASP A 167     3803   3555   2921    298    219    -23       O  
ATOM   1148  CB  ASP A 167      44.994   1.681 -17.661  1.00 54.98           C  
ANISOU 1148  CB  ASP A 167     7370   7129   6392    350    259    -86       C  
ATOM   1149  CG  ASP A 167      44.288   0.467 -18.266  1.00 66.61           C  
ANISOU 1149  CG  ASP A 167     8859   8610   7839    361    208   -147       C  
ATOM   1150  OD1 ASP A 167      43.105   0.582 -18.669  1.00 67.14           O  
ANISOU 1150  OD1 ASP A 167     8941   8690   7878    363    159   -160       O  
ATOM   1151  OD2 ASP A 167      44.919  -0.612 -18.329  1.00 70.29           O  
ANISOU 1151  OD2 ASP A 167     9320   9068   8318    366    218   -182       O  
ATOM   1152  N   ALA A 168      44.537   5.327 -17.589  1.00 22.99           N  
ANISOU 1152  N   ALA A 168     3318   3065   2352    332    297     63       N  
ATOM   1153  CA  ALA A 168      44.270   6.430 -16.662  1.00 28.24           C  
ANISOU 1153  CA  ALA A 168     3961   3694   3074    300    290     97       C  
ATOM   1154  C   ALA A 168      42.817   6.472 -16.194  1.00 23.88           C  
ANISOU 1154  C   ALA A 168     3411   3138   2526    295    225     72       C  
ATOM   1155  O   ALA A 168      42.532   6.768 -15.039  1.00 23.03           O  
ANISOU 1155  O   ALA A 168     3275   2999   2475    263    205     68       O  
ATOM   1156  CB  ALA A 168      44.648   7.769 -17.300  1.00 23.86           C  
ANISOU 1156  CB  ALA A 168     3422   3137   2506    311    337    166       C  
ATOM   1157  N   GLU A 169      41.909   6.186 -17.113  1.00 17.58           N  
ANISOU 1157  N   GLU A 169     2645   2373   1662    329    192     55       N  
ATOM   1158  CA  GLU A 169      40.491   6.211 -16.824  1.00 23.95           C  
ANISOU 1158  CA  GLU A 169     3449   3183   2468    329    130     33       C  
ATOM   1159  C   GLU A 169      40.147   5.202 -15.728  1.00 23.85           C  
ANISOU 1159  C   GLU A 169     3404   3152   2506    295     94    -19       C  
ATOM   1160  O   GLU A 169      39.472   5.529 -14.753  1.00 15.84           O  
ANISOU 1160  O   GLU A 169     2364   2119   1536    272     68    -21       O  
ATOM   1161  CB  GLU A 169      39.717   5.913 -18.098  1.00 24.61           C  
ANISOU 1161  CB  GLU A 169     3570   3312   2469    372    100     17       C  
ATOM   1162  CG  GLU A 169      38.226   5.928 -17.946  1.00 32.70           C  
ANISOU 1162  CG  GLU A 169     4588   4347   3490    376     33     -6       C  
ATOM   1163  CD  GLU A 169      37.535   5.625 -19.259  1.00 36.74           C  
ANISOU 1163  CD  GLU A 169     5118   4899   3944    407     -2    -23       C  
ATOM   1164  OE1 GLU A 169      37.473   4.434 -19.647  1.00 34.02           O  
ANISOU 1164  OE1 GLU A 169     4771   4566   3589    401    -26    -76       O  
ATOM   1165  OE2 GLU A 169      37.080   6.583 -19.914  1.00 38.22           O  
ANISOU 1165  OE2 GLU A 169     5319   5100   4102    434     -6     17       O  
ATOM   1166  N   LEU A 170      40.641   3.982 -15.887  1.00 21.26           N  
ANISOU 1166  N   LEU A 170     3077   2830   2171    293     96    -59       N  
ATOM   1167  CA  LEU A 170      40.396   2.934 -14.920  1.00 19.35           C  
ANISOU 1167  CA  LEU A 170     2808   2568   1976    263     66   -103       C  
ATOM   1168  C   LEU A 170      41.114   3.256 -13.601  1.00 25.08           C  
ANISOU 1168  C   LEU A 170     3499   3260   2772    228     90    -83       C  
ATOM   1169  O   LEU A 170      40.582   3.032 -12.507  1.00 24.10           O  
ANISOU 1169  O   LEU A 170     3348   3117   2691    200     63    -97       O  
ATOM   1170  CB  LEU A 170      40.841   1.586 -15.490  1.00 17.25           C  
ANISOU 1170  CB  LEU A 170     2558   2310   1688    275     66   -148       C  
ATOM   1171  CG  LEU A 170      40.691   0.379 -14.562  1.00 20.37           C  
ANISOU 1171  CG  LEU A 170     2929   2677   2133    246     39   -190       C  
ATOM   1172  CD1 LEU A 170      39.279   0.288 -14.006  1.00  8.96           C  
ANISOU 1172  CD1 LEU A 170     1466   1228    708    224    -16   -208       C  
ATOM   1173  CD2 LEU A 170      41.068  -0.907 -15.287  1.00 16.78           C  
ANISOU 1173  CD2 LEU A 170     2497   2226   1653    265     37   -238       C  
ATOM   1174  N   PHE A 171      42.311   3.812 -13.717  1.00 18.43           N  
ANISOU 1174  N   PHE A 171     2655   2411   1938    229    142    -48       N  
ATOM   1175  CA  PHE A 171      43.095   4.185 -12.555  1.00 20.40           C  
ANISOU 1175  CA  PHE A 171     2870   2632   2250    197    162    -31       C  
ATOM   1176  C   PHE A 171      42.310   5.170 -11.696  1.00 19.88           C  
ANISOU 1176  C   PHE A 171     2791   2548   2213    178    140    -15       C  
ATOM   1177  O   PHE A 171      42.200   5.014 -10.479  1.00 19.39           O  
ANISOU 1177  O   PHE A 171     2703   2468   2196    151    124    -28       O  
ATOM   1178  CB  PHE A 171      44.425   4.799 -13.009  1.00 22.04           C  
ANISOU 1178  CB  PHE A 171     3076   2839   2460    202    221      8       C  
ATOM   1179  CG  PHE A 171      45.291   5.304 -11.882  1.00 18.22           C  
ANISOU 1179  CG  PHE A 171     2554   2327   2042    168    239     25       C  
ATOM   1180  CD1 PHE A 171      46.357   4.553 -11.424  1.00 13.29           C  
ANISOU 1180  CD1 PHE A 171     1902   1698   1449    157    256     13       C  
ATOM   1181  CD2 PHE A 171      45.049   6.550 -11.300  1.00 22.12           C  
ANISOU 1181  CD2 PHE A 171     3041   2798   2567    148    237     52       C  
ATOM   1182  CE1 PHE A 171      47.158   5.021 -10.393  1.00 17.98           C  
ANISOU 1182  CE1 PHE A 171     2459   2271   2101    126    266     26       C  
ATOM   1183  CE2 PHE A 171      45.832   7.016 -10.270  1.00 20.18           C  
ANISOU 1183  CE2 PHE A 171     2762   2527   2379    116    247     61       C  
ATOM   1184  CZ  PHE A 171      46.903   6.254  -9.823  1.00 19.26           C  
ANISOU 1184  CZ  PHE A 171     2615   2412   2292    104    260     48       C  
ATOM   1185  N   TRP A 172      41.767   6.193 -12.333  1.00 16.15           N  
ANISOU 1185  N   TRP A 172     2340   2083   1714    197    142     13       N  
ATOM   1186  CA  TRP A 172      41.076   7.228 -11.592  1.00 17.79           C  
ANISOU 1186  CA  TRP A 172     2538   2270   1951    186    126     29       C  
ATOM   1187  C   TRP A 172      39.654   6.836 -11.152  1.00 17.22           C  
ANISOU 1187  C   TRP A 172     2458   2208   1877    186     75     -1       C  
ATOM   1188  O   TRP A 172      39.083   7.466 -10.263  1.00 17.28           O  
ANISOU 1188  O   TRP A 172     2449   2200   1915    175     61      1       O  
ATOM   1189  CB  TRP A 172      41.124   8.555 -12.350  1.00 18.13           C  
ANISOU 1189  CB  TRP A 172     2606   2308   1977    206    151     78       C  
ATOM   1190  CG  TRP A 172      42.482   9.181 -12.300  1.00 20.63           C  
ANISOU 1190  CG  TRP A 172     2915   2601   2324    190    203    112       C  
ATOM   1191  CD1 TRP A 172      43.408   9.225 -13.309  1.00 19.46           C  
ANISOU 1191  CD1 TRP A 172     2781   2465   2148    204    248    142       C  
ATOM   1192  CD2 TRP A 172      43.083   9.841 -11.172  1.00 19.43           C  
ANISOU 1192  CD2 TRP A 172     2736   2411   2237    154    214    119       C  
ATOM   1193  NE1 TRP A 172      44.539   9.879 -12.881  1.00 19.96           N  
ANISOU 1193  NE1 TRP A 172     2823   2499   2263    176    288    169       N  
ATOM   1194  CE2 TRP A 172      44.372  10.265 -11.577  1.00 19.44           C  
ANISOU 1194  CE2 TRP A 172     2731   2401   2253    145    265    153       C  
ATOM   1195  CE3 TRP A 172      42.655  10.122  -9.867  1.00  9.92           C  
ANISOU 1195  CE3 TRP A 172     1510   1183   1076    131    187     98       C  
ATOM   1196  CZ2 TRP A 172      45.241  10.957 -10.720  1.00 23.72           C  
ANISOU 1196  CZ2 TRP A 172     3246   2907   2860    108    283    165       C  
ATOM   1197  CZ3 TRP A 172      43.519  10.813  -9.015  1.00 15.05           C  
ANISOU 1197  CZ3 TRP A 172     2138   1799   1781     99    204    106       C  
ATOM   1198  CH2 TRP A 172      44.797  11.225  -9.446  1.00 21.36           C  
ANISOU 1198  CH2 TRP A 172     2930   2585   2601     86    249    138       C  
ATOM   1199  N   ALA A 173      39.101   5.778 -11.738  1.00 14.39           N  
ANISOU 1199  N   ALA A 173     2108   1875   1485    198     47    -33       N  
ATOM   1200  CA  ALA A 173      37.853   5.226 -11.220  1.00 14.56           C  
ANISOU 1200  CA  ALA A 173     2110   1904   1516    189      0    -64       C  
ATOM   1201  C   ALA A 173      38.109   4.308 -10.013  1.00 15.76           C  
ANISOU 1201  C   ALA A 173     2235   2039   1715    154     -4    -89       C  
ATOM   1202  O   ALA A 173      37.230   4.122  -9.170  1.00 15.95           O  
ANISOU 1202  O   ALA A 173     2236   2062   1763    139    -29   -102       O  
ATOM   1203  CB  ALA A 173      37.100   4.491 -12.303  1.00 11.93           C  
ANISOU 1203  CB  ALA A 173     1795   1602   1135    211    -33    -91       C  
ATOM   1204  N   THR A 174      39.317   3.750  -9.943  1.00 12.71           N  
ANISOU 1204  N   THR A 174     1849   1642   1339    146     24    -91       N  
ATOM   1205  CA  THR A 174      39.759   2.943  -8.807  1.00 14.01           C  
ANISOU 1205  CA  THR A 174     1989   1788   1545    118     24   -106       C  
ATOM   1206  C   THR A 174      40.048   3.792  -7.559  1.00 19.28           C  
ANISOU 1206  C   THR A 174     2636   2439   2252     98     35    -86       C  
ATOM   1207  O   THR A 174      39.645   3.445  -6.444  1.00 11.96           O  
ANISOU 1207  O   THR A 174     1687   1505   1351     79     19    -96       O  
ATOM   1208  CB  THR A 174      41.016   2.130  -9.181  1.00 11.78           C  
ANISOU 1208  CB  THR A 174     1713   1500   1261    123     50   -113       C  
ATOM   1209  OG1 THR A 174      40.718   1.297 -10.312  1.00 11.96           O  
ANISOU 1209  OG1 THR A 174     1761   1539   1246    144     37   -139       O  
ATOM   1210  CG2 THR A 174      41.456   1.259  -8.026  1.00  5.96           C  
ANISOU 1210  CG2 THR A 174      952    745    566    100     46   -124       C  
ATOM   1211  N   VAL A 175      40.766   4.897  -7.749  1.00 15.30           N  
ANISOU 1211  N   VAL A 175     2137   1926   1751    103     63    -59       N  
ATOM   1212  CA  VAL A 175      40.875   5.899  -6.708  1.00 11.64           C  
ANISOU 1212  CA  VAL A 175     1658   1444   1320     86     68    -45       C  
ATOM   1213  C   VAL A 175      39.457   6.351  -6.332  1.00 18.82           C  
ANISOU 1213  C   VAL A 175     2566   2359   2226     92     40    -51       C  
ATOM   1214  O   VAL A 175      38.680   6.753  -7.207  1.00 10.38           O  
ANISOU 1214  O   VAL A 175     1513   1301   1129    115     31    -44       O  
ATOM   1215  CB  VAL A 175      41.659   7.112  -7.209  1.00 15.97           C  
ANISOU 1215  CB  VAL A 175     2217   1977   1873     91    100    -14       C  
ATOM   1216  CG1 VAL A 175      41.561   8.253  -6.216  1.00  5.92           C  
ANISOU 1216  CG1 VAL A 175      934    680    634     76     98     -7       C  
ATOM   1217  CG2 VAL A 175      43.105   6.724  -7.465  1.00 15.62           C  
ANISOU 1217  CG2 VAL A 175     2164   1930   1839     83    132     -6       C  
ATOM   1218  N   GLY A 176      39.112   6.237  -5.047  1.00 16.93           N  
ANISOU 1218  N   GLY A 176     2305   2116   2012     74     27    -64       N  
ATOM   1219  CA  GLY A 176      37.772   6.554  -4.566  1.00 14.74           C  
ANISOU 1219  CA  GLY A 176     2019   1848   1734     80      5    -71       C  
ATOM   1220  C   GLY A 176      36.680   5.585  -5.012  1.00 18.24           C  
ANISOU 1220  C   GLY A 176     2456   2314   2160     85    -21    -87       C  
ATOM   1221  O   GLY A 176      35.490   5.823  -4.791  1.00 19.65           O  
ANISOU 1221  O   GLY A 176     2622   2506   2339     93    -39    -91       O  
ATOM   1222  N   GLY A 177      37.079   4.480  -5.630  1.00 12.69           N  
ANISOU 1222  N   GLY A 177     1760   1616   1447     81    -24    -98       N  
ATOM   1223  CA  GLY A 177      36.124   3.556  -6.207  1.00 12.91           C  
ANISOU 1223  CA  GLY A 177     1784   1660   1460     84    -53   -119       C  
ATOM   1224  C   GLY A 177      35.519   2.536  -5.257  1.00 16.31           C  
ANISOU 1224  C   GLY A 177     2188   2091   1917     58    -69   -134       C  
ATOM   1225  O   GLY A 177      34.738   1.682  -5.682  1.00 15.77           O  
ANISOU 1225  O   GLY A 177     2113   2031   1847     53    -94   -153       O  
ATOM   1226  N   ASN A 178      35.883   2.612  -3.981  1.00 10.06           N  
ANISOU 1226  N   ASN A 178     1382   1289   1150     42    -55   -125       N  
ATOM   1227  CA  ASN A 178      35.313   1.726  -2.972  1.00 20.28           C  
ANISOU 1227  CA  ASN A 178     2653   2586   2468     20    -63   -131       C  
ATOM   1228  C   ASN A 178      35.375   0.232  -3.337  1.00 17.72           C  
ANISOU 1228  C   ASN A 178     2330   2249   2152      5    -76   -146       C  
ATOM   1229  O   ASN A 178      34.451  -0.531  -3.044  1.00 10.06           O  
ANISOU 1229  O   ASN A 178     1340   1282   1200    -13    -92   -153       O  
ATOM   1230  CB  ASN A 178      33.874   2.141  -2.661  1.00 17.67           C  
ANISOU 1230  CB  ASN A 178     2299   2275   2141     22    -77   -131       C  
ATOM   1231  CG  ASN A 178      33.784   3.499  -1.962  1.00 17.71           C  
ANISOU 1231  CG  ASN A 178     2300   2285   2144     36    -63   -119       C  
ATOM   1232  OD1 ASN A 178      33.817   3.577  -0.739  1.00 20.36           O  
ANISOU 1232  OD1 ASN A 178     2624   2621   2491     26    -51   -114       O  
ATOM   1233  ND2 ASN A 178      33.653   4.568  -2.743  1.00 16.77           N  
ANISOU 1233  ND2 ASN A 178     2196   2167   2009     61    -64   -114       N  
ATOM   1234  N   GLY A 179      36.462  -0.166  -3.998  1.00 11.97           N  
ANISOU 1234  N   GLY A 179     1624   1508   1417     13    -66   -152       N  
ATOM   1235  CA  GLY A 179      36.719  -1.559  -4.313  1.00  8.73           C  
ANISOU 1235  CA  GLY A 179     1221   1080   1018      4    -74   -169       C  
ATOM   1236  C   GLY A 179      35.922  -2.074  -5.491  1.00 14.07           C  
ANISOU 1236  C   GLY A 179     1906   1761   1678      8   -102   -198       C  
ATOM   1237  O   GLY A 179      36.023  -3.236  -5.871  1.00 13.81           O  
ANISOU 1237  O   GLY A 179     1883   1710   1656      1   -113   -220       O  
ATOM   1238  N   LEU A 180      35.118  -1.210  -6.083  1.00 14.56           N  
ANISOU 1238  N   LEU A 180     1966   1848   1717     22   -116   -198       N  
ATOM   1239  CA  LEU A 180      34.177  -1.676  -7.080  1.00 11.70           C  
ANISOU 1239  CA  LEU A 180     1607   1498   1342     24   -151   -227       C  
ATOM   1240  C   LEU A 180      34.745  -1.729  -8.493  1.00 14.03           C  
ANISOU 1240  C   LEU A 180     1938   1799   1592     53   -154   -246       C  
ATOM   1241  O   LEU A 180      33.989  -1.919  -9.428  1.00 16.47           O  
ANISOU 1241  O   LEU A 180     2253   2125   1878     62   -186   -271       O  
ATOM   1242  CB  LEU A 180      32.896  -0.851  -7.038  1.00 11.48           C  
ANISOU 1242  CB  LEU A 180     1554   1498   1309     28   -171   -220       C  
ATOM   1243  CG  LEU A 180      32.065  -1.018  -5.770  1.00 20.06           C  
ANISOU 1243  CG  LEU A 180     2601   2585   2437      1   -172   -208       C  
ATOM   1244  CD1 LEU A 180      30.997   0.093  -5.670  1.00 13.60           C  
ANISOU 1244  CD1 LEU A 180     1759   1798   1613     16   -181   -196       C  
ATOM   1245  CD2 LEU A 180      31.419  -2.432  -5.709  1.00  8.19           C  
ANISOU 1245  CD2 LEU A 180     1078   1067    967    -32   -197   -231       C  
ATOM   1246  N   THR A 181      36.061  -1.565  -8.656  1.00 19.95           N  
ANISOU 1246  N   THR A 181     2711   2540   2331     68   -119   -235       N  
ATOM   1247  CA  THR A 181      36.693  -1.848  -9.960  1.00 24.75           C  
ANISOU 1247  CA  THR A 181     3354   3154   2897     95   -115   -254       C  
ATOM   1248  C   THR A 181      37.517  -3.131  -9.914  1.00 22.75           C  
ANISOU 1248  C   THR A 181     3110   2871   2662     90   -105   -278       C  
ATOM   1249  O   THR A 181      38.004  -3.606 -10.938  1.00 15.55           O  
ANISOU 1249  O   THR A 181     2228   1962   1719    113   -102   -303       O  
ATOM   1250  CB  THR A 181      37.604  -0.710 -10.482  1.00 19.61           C  
ANISOU 1250  CB  THR A 181     2721   2517   2211    123    -78   -224       C  
ATOM   1251  OG1 THR A 181      38.694  -0.490  -9.575  1.00 22.59           O  
ANISOU 1251  OG1 THR A 181     3087   2876   2621    112    -41   -198       O  
ATOM   1252  CG2 THR A 181      36.813   0.575 -10.691  1.00 17.58           C  
ANISOU 1252  CG2 THR A 181     2462   2284   1934    136    -87   -199       C  
ATOM   1253  N   GLY A 182      37.656  -3.689  -8.718  1.00 18.23           N  
ANISOU 1253  N   GLY A 182     2515   2272   2138     63   -101   -268       N  
ATOM   1254  CA  GLY A 182      38.483  -4.857  -8.512  1.00 16.51           C  
ANISOU 1254  CA  GLY A 182     2305   2022   1946     60    -90   -282       C  
ATOM   1255  C   GLY A 182      39.321  -4.749  -7.246  1.00 16.86           C  
ANISOU 1255  C   GLY A 182     2329   2051   2024     50    -63   -248       C  
ATOM   1256  O   GLY A 182      39.158  -3.830  -6.434  1.00 10.31           O  
ANISOU 1256  O   GLY A 182     1480   1235   1201     39    -56   -218       O  
ATOM   1257  N   ILE A 183      40.226  -5.703  -7.085  1.00 12.18           N  
ANISOU 1257  N   ILE A 183     1743   1431   1452     55    -50   -255       N  
ATOM   1258  CA  ILE A 183      41.034  -5.788  -5.884  1.00 13.83           C  
ANISOU 1258  CA  ILE A 183     1932   1627   1694     48    -32   -225       C  
ATOM   1259  C   ILE A 183      42.396  -5.169  -6.126  1.00 17.88           C  
ANISOU 1259  C   ILE A 183     2446   2153   2194     72      2   -210       C  
ATOM   1260  O   ILE A 183      43.126  -5.584  -7.024  1.00 17.04           O  
ANISOU 1260  O   ILE A 183     2357   2044   2074     98     17   -228       O  
ATOM   1261  CB  ILE A 183      41.138  -7.251  -5.408  1.00 19.11           C  
ANISOU 1261  CB  ILE A 183     2603   2255   2402     39    -41   -234       C  
ATOM   1262  CG1 ILE A 183      39.736  -7.730  -5.019  1.00 19.76           C  
ANISOU 1262  CG1 ILE A 183     2677   2325   2506      7    -71   -240       C  
ATOM   1263  CG2 ILE A 183      42.101  -7.389  -4.213  1.00 14.20           C  
ANISOU 1263  CG2 ILE A 183     1964   1624   1809     39    -24   -201       C  
ATOM   1264  CD1 ILE A 183      39.624  -9.183  -4.918  1.00 27.42           C  
ANISOU 1264  CD1 ILE A 183     3656   3249   3514     -4    -84   -257       C  
ATOM   1265  N   ILE A 184      42.716  -4.134  -5.357  1.00 16.71           N  
ANISOU 1265  N   ILE A 184     2278   2022   2050     63     14   -179       N  
ATOM   1266  CA  ILE A 184      44.038  -3.558  -5.437  1.00 13.90           C  
ANISOU 1266  CA  ILE A 184     1913   1675   1694     78     44   -163       C  
ATOM   1267  C   ILE A 184      44.960  -4.532  -4.709  1.00 14.00           C  
ANISOU 1267  C   ILE A 184     1912   1668   1740     83     49   -158       C  
ATOM   1268  O   ILE A 184      44.707  -4.888  -3.568  1.00 19.08           O  
ANISOU 1268  O   ILE A 184     2542   2300   2406     66     33   -146       O  
ATOM   1269  CB  ILE A 184      44.087  -2.159  -4.820  1.00 13.17           C  
ANISOU 1269  CB  ILE A 184     1803   1599   1601     65     51   -137       C  
ATOM   1270  CG1 ILE A 184      43.022  -1.253  -5.465  1.00 13.45           C  
ANISOU 1270  CG1 ILE A 184     1853   1650   1608     64     43   -139       C  
ATOM   1271  CG2 ILE A 184      45.484  -1.574  -4.976  1.00  7.68           C  
ANISOU 1271  CG2 ILE A 184     1094    911    913     75     82   -120       C  
ATOM   1272  CD1 ILE A 184      42.618  -0.056  -4.623  1.00 10.25           C  
ANISOU 1272  CD1 ILE A 184     1434   1252   1209     48     39   -120       C  
ATOM   1273  N   MET A 185      45.993  -5.005  -5.399  1.00 12.95           N  
ANISOU 1273  N   MET A 185     1783   1531   1607    109     71   -167       N  
ATOM   1274  CA  MET A 185      46.874  -6.029  -4.866  1.00 12.70           C  
ANISOU 1274  CA  MET A 185     1739   1478   1607    122     75   -164       C  
ATOM   1275  C   MET A 185      48.100  -5.370  -4.246  1.00 19.46           C  
ANISOU 1275  C   MET A 185     2561   2351   2480    125     94   -137       C  
ATOM   1276  O   MET A 185      48.634  -5.819  -3.228  1.00 18.42           O  
ANISOU 1276  O   MET A 185     2409   2212   2378    124     84   -122       O  
ATOM   1277  CB  MET A 185      47.309  -6.975  -5.987  1.00 15.92           C  
ANISOU 1277  CB  MET A 185     2170   1873   2007    155     90   -195       C  
ATOM   1278  CG  MET A 185      46.168  -7.814  -6.621  1.00 17.04           C  
ANISOU 1278  CG  MET A 185     2346   1991   2137    152     65   -231       C  
ATOM   1279  SD  MET A 185      45.329  -8.897  -5.416  1.00 18.60           S  
ANISOU 1279  SD  MET A 185     2541   2147   2379    123     30   -226       S  
ATOM   1280  CE  MET A 185      46.469 -10.265  -5.318  1.00 25.05           C  
ANISOU 1280  CE  MET A 185     3362   2924   3232    157     42   -233       C  
ATOM   1281  N   ARG A 186      48.506  -4.262  -4.854  1.00 15.83           N  
ANISOU 1281  N   ARG A 186     2095   1916   2004    126    117   -129       N  
ATOM   1282  CA  ARG A 186      49.836  -3.738  -4.666  1.00 15.18           C  
ANISOU 1282  CA  ARG A 186     1978   1848   1941    132    142   -110       C  
ATOM   1283  C   ARG A 186      49.857  -2.343  -5.262  1.00 19.20           C  
ANISOU 1283  C   ARG A 186     2485   2377   2432    121    163    -97       C  
ATOM   1284  O   ARG A 186      49.146  -2.067  -6.229  1.00 23.43           O  
ANISOU 1284  O   ARG A 186     3052   2918   2932    127    170   -106       O  
ATOM   1285  CB  ARG A 186      50.817  -4.655  -5.398  1.00 13.54           C  
ANISOU 1285  CB  ARG A 186     1767   1637   1740    169    168   -121       C  
ATOM   1286  CG  ARG A 186      52.273  -4.274  -5.286  1.00 15.61           C  
ANISOU 1286  CG  ARG A 186     1985   1917   2028    179    197   -102       C  
ATOM   1287  CD  ARG A 186      53.114  -5.482  -5.683  1.00 20.19           C  
ANISOU 1287  CD  ARG A 186     2561   2488   2622    220    215   -115       C  
ATOM   1288  NE  ARG A 186      54.523  -5.152  -5.798  1.00 24.33           N  
ANISOU 1288  NE  ARG A 186     3038   3035   3170    235    249    -97       N  
ATOM   1289  CZ  ARG A 186      55.495  -6.050  -5.897  1.00 28.95           C  
ANISOU 1289  CZ  ARG A 186     3602   3618   3779    272    265   -102       C  
ATOM   1290  NH1 ARG A 186      55.210  -7.350  -5.878  1.00 23.99           N  
ANISOU 1290  NH1 ARG A 186     3002   2960   3154    299    250   -124       N  
ATOM   1291  NH2 ARG A 186      56.757  -5.640  -6.003  1.00 20.88           N  
ANISOU 1291  NH2 ARG A 186     2529   2622   2782    283    298    -84       N  
ATOM   1292  N   ALA A 187      50.649  -1.449  -4.683  1.00 13.63           N  
ANISOU 1292  N   ALA A 187     1745   1681   1751    105    171    -76       N  
ATOM   1293  CA  ALA A 187      50.704  -0.085  -5.194  1.00 16.42           C  
ANISOU 1293  CA  ALA A 187     2098   2045   2096     91    193    -59       C  
ATOM   1294  C   ALA A 187      52.056   0.549  -4.938  1.00 19.00           C  
ANISOU 1294  C   ALA A 187     2379   2380   2460     82    216    -40       C  
ATOM   1295  O   ALA A 187      52.778   0.162  -4.014  1.00 13.85           O  
ANISOU 1295  O   ALA A 187     1692   1729   1841     78    201    -39       O  
ATOM   1296  CB  ALA A 187      49.576   0.783  -4.585  1.00  8.70           C  
ANISOU 1296  CB  ALA A 187     1134   1060   1110     65    165    -58       C  
ATOM   1297  N   THR A 188      52.385   1.523  -5.780  1.00 17.98           N  
ANISOU 1297  N   THR A 188     2248   2257   2326     78    252    -21       N  
ATOM   1298  CA  THR A 188      53.577   2.342  -5.603  1.00 18.48           C  
ANISOU 1298  CA  THR A 188     2265   2325   2431     59    275      2       C  
ATOM   1299  C   THR A 188      53.185   3.766  -5.222  1.00 18.14           C  
ANISOU 1299  C   THR A 188     2224   2267   2400     24    266     14       C  
ATOM   1300  O   THR A 188      52.514   4.450  -5.984  1.00 17.73           O  
ANISOU 1300  O   THR A 188     2205   2210   2322     25    281     26       O  
ATOM   1301  CB  THR A 188      54.430   2.349  -6.881  1.00 22.00           C  
ANISOU 1301  CB  THR A 188     2701   2787   2869     81    334     20       C  
ATOM   1302  OG1 THR A 188      54.984   1.042  -7.074  1.00 17.44           O  
ANISOU 1302  OG1 THR A 188     2115   2221   2291    116    342      4       O  
ATOM   1303  CG2 THR A 188      55.553   3.347  -6.752  1.00 18.47           C  
ANISOU 1303  CG2 THR A 188     2204   2343   2471     54    361     48       C  
ATOM   1304  N   ILE A 189      53.576   4.189  -4.023  1.00 20.55           N  
ANISOU 1304  N   ILE A 189     2497   2567   2746     -5    237      9       N  
ATOM   1305  CA  ILE A 189      53.210   5.506  -3.495  1.00 18.59           C  
ANISOU 1305  CA  ILE A 189     2251   2298   2514    -38    222     12       C  
ATOM   1306  C   ILE A 189      54.423   6.444  -3.484  1.00 20.07           C  
ANISOU 1306  C   ILE A 189     2393   2479   2755    -67    244     30       C  
ATOM   1307  O   ILE A 189      55.506   6.041  -3.080  1.00 17.49           O  
ANISOU 1307  O   ILE A 189     2018   2166   2463    -71    242     29       O  
ATOM   1308  CB  ILE A 189      52.698   5.402  -2.037  1.00 17.25           C  
ANISOU 1308  CB  ILE A 189     2081   2125   2348    -51    168    -13       C  
ATOM   1309  CG1 ILE A 189      51.580   4.358  -1.892  1.00 17.00           C  
ANISOU 1309  CG1 ILE A 189     2085   2100   2274    -27    146    -28       C  
ATOM   1310  CG2 ILE A 189      52.279   6.772  -1.505  1.00 15.71           C  
ANISOU 1310  CG2 ILE A 189     1894   1908   2168    -80    153    -17       C  
ATOM   1311  CD1 ILE A 189      50.354   4.634  -2.738  1.00 18.58           C  
ANISOU 1311  CD1 ILE A 189     2331   2293   2436    -16    155    -26       C  
ATOM   1312  N   GLU A 190      54.248   7.687  -3.925  1.00 21.26           N  
ANISOU 1312  N   GLU A 190     2555   2606   2917    -87    264     49       N  
ATOM   1313  CA  GLU A 190      55.304   8.686  -3.772  1.00 17.70           C  
ANISOU 1313  CA  GLU A 190     2059   2139   2526   -125    280     65       C  
ATOM   1314  C   GLU A 190      55.243   9.344  -2.395  1.00 20.87           C  
ANISOU 1314  C   GLU A 190     2447   2522   2961   -159    228     36       C  
ATOM   1315  O   GLU A 190      54.287  10.047  -2.066  1.00 19.41           O  
ANISOU 1315  O   GLU A 190     2299   2312   2763   -165    208     25       O  
ATOM   1316  CB  GLU A 190      55.254   9.744  -4.876  1.00 14.19           C  
ANISOU 1316  CB  GLU A 190     1634   1673   2087   -134    329    104       C  
ATOM   1317  CG  GLU A 190      56.255  10.867  -4.631  1.00 24.49           C  
ANISOU 1317  CG  GLU A 190     2892   2951   3464   -181    342    120       C  
ATOM   1318  CD  GLU A 190      56.480  11.781  -5.827  1.00 32.57           C  
ANISOU 1318  CD  GLU A 190     3924   3953   4498   -190    403    171       C  
ATOM   1319  OE1 GLU A 190      57.276  12.738  -5.697  1.00 32.94           O  
ANISOU 1319  OE1 GLU A 190     3933   3972   4612   -233    419    189       O  
ATOM   1320  OE2 GLU A 190      55.877  11.548  -6.894  1.00 38.61           O  
ANISOU 1320  OE2 GLU A 190     4732   4730   5207   -154    435    194       O  
ATOM   1321  N   MET A 191      56.264   9.095  -1.584  1.00 25.98           N  
ANISOU 1321  N   MET A 191     3040   3182   3648   -175    206     22       N  
ATOM   1322  CA  MET A 191      56.322   9.630  -0.229  1.00 15.51           C  
ANISOU 1322  CA  MET A 191     1698   1845   2349   -204    152    -11       C  
ATOM   1323  C   MET A 191      56.780  11.088  -0.190  1.00 22.19           C  
ANISOU 1323  C   MET A 191     2526   2652   3254   -251    158     -7       C  
ATOM   1324  O   MET A 191      57.244  11.647  -1.188  1.00 25.12           O  
ANISOU 1324  O   MET A 191     2886   3007   3654   -264    208     28       O  
ATOM   1325  CB  MET A 191      57.253   8.784   0.614  1.00 12.64           C  
ANISOU 1325  CB  MET A 191     1284   1515   2003   -201    121    -27       C  
ATOM   1326  CG  MET A 191      56.929   7.316   0.539  1.00 14.83           C  
ANISOU 1326  CG  MET A 191     1578   1824   2234   -156    119    -27       C  
ATOM   1327  SD  MET A 191      55.443   6.900   1.481  1.00 20.13           S  
ANISOU 1327  SD  MET A 191     2306   2495   2845   -138     73    -53       S  
ATOM   1328  CE  MET A 191      56.098   6.793   3.142  1.00 14.15           C  
ANISOU 1328  CE  MET A 191     1510   1759   2106   -151     10    -82       C  
ATOM   1329  N   THR A 192      56.631  11.705   0.972  1.00 20.69           N  
ANISOU 1329  N   THR A 192     2335   2446   3080   -275    108    -45       N  
ATOM   1330  CA  THR A 192      57.096  13.058   1.168  1.00 22.17           C  
ANISOU 1330  CA  THR A 192     2504   2590   3331   -323    104    -51       C  
ATOM   1331  C   THR A 192      58.417  13.018   1.945  1.00 29.37           C  
ANISOU 1331  C   THR A 192     3343   3518   4298   -355     72    -72       C  
ATOM   1332  O   THR A 192      58.533  12.320   2.965  1.00 22.82           O  
ANISOU 1332  O   THR A 192     2499   2723   3447   -342     23   -103       O  
ATOM   1333  CB  THR A 192      56.014  13.907   1.870  1.00 24.86           C  
ANISOU 1333  CB  THR A 192     2895   2896   3654   -327     71    -85       C  
ATOM   1334  OG1 THR A 192      54.854  13.935   1.042  1.00 20.17           O  
ANISOU 1334  OG1 THR A 192     2359   2290   3014   -296    102    -61       O  
ATOM   1335  CG2 THR A 192      56.474  15.357   2.120  1.00 10.08           C  
ANISOU 1335  CG2 THR A 192     1009    968   1853   -378     63    -98       C  
ATOM   1336  N   PRO A 193      59.432  13.719   1.423  1.00 27.83           N  
ANISOU 1336  N   PRO A 193     3099   3301   4174   -395    102    -49       N  
ATOM   1337  CA  PRO A 193      60.738  13.853   2.072  1.00 29.94           C  
ANISOU 1337  CA  PRO A 193     3288   3580   4508   -433     73    -67       C  
ATOM   1338  C   PRO A 193      60.590  14.611   3.374  1.00 33.87           C  
ANISOU 1338  C   PRO A 193     3791   4055   5023   -463      3   -125       C  
ATOM   1339  O   PRO A 193      59.916  15.646   3.413  1.00 32.45           O  
ANISOU 1339  O   PRO A 193     3659   3825   4848   -479      1   -137       O  
ATOM   1340  CB  PRO A 193      61.541  14.711   1.083  1.00 30.27           C  
ANISOU 1340  CB  PRO A 193     3298   3591   4614   -470    129    -24       C  
ATOM   1341  CG  PRO A 193      60.832  14.572  -0.218  1.00 35.41           C  
ANISOU 1341  CG  PRO A 193     3994   4231   5228   -441    198     26       C  
ATOM   1342  CD  PRO A 193      59.385  14.406   0.123  1.00 32.70           C  
ANISOU 1342  CD  PRO A 193     3731   3883   4811   -405    170      1       C  
ATOM   1343  N   THR A 194      61.206  14.099   4.432  1.00 28.67           N  
ANISOU 1343  N   THR A 194     3093   3437   4363   -462    -55   -160       N  
ATOM   1344  CA  THR A 194      61.233  14.805   5.702  1.00 27.06           C  
ANISOU 1344  CA  THR A 194     2902   3226   4153   -480   -123   -214       C  
ATOM   1345  C   THR A 194      62.574  14.506   6.354  1.00 32.78           C  
ANISOU 1345  C   THR A 194     3559   3994   4901   -492   -162   -226       C  
ATOM   1346  O   THR A 194      63.220  13.503   6.028  1.00 35.24           O  
ANISOU 1346  O   THR A 194     3823   4349   5219   -472   -147   -200       O  
ATOM   1347  CB  THR A 194      60.106  14.349   6.633  1.00 21.92           C  
ANISOU 1347  CB  THR A 194     2301   2591   3437   -448   -167   -255       C  
ATOM   1348  OG1 THR A 194      60.069  15.183   7.799  1.00 19.26           O  
ANISOU 1348  OG1 THR A 194     1985   2244   3088   -463   -224   -306       O  
ATOM   1349  CG2 THR A 194      60.317  12.885   7.063  1.00 16.05           C  
ANISOU 1349  CG2 THR A 194     1535   1914   2649   -407   -189   -251       C  
ATOM   1350  N   SER A 195      63.000  15.374   7.265  1.00 26.79           N  
ANISOU 1350  N   SER A 195     2797   3224   4157   -521   -211   -265       N  
ATOM   1351  CA  SER A 195      64.263  15.154   7.970  1.00 32.86           C  
ANISOU 1351  CA  SER A 195     3503   4036   4947   -534   -255   -280       C  
ATOM   1352  C   SER A 195      63.988  14.885   9.436  1.00 33.62           C  
ANISOU 1352  C   SER A 195     3620   4167   4988   -514   -331   -333       C  
ATOM   1353  O   SER A 195      64.882  14.486  10.187  1.00 34.76           O  
ANISOU 1353  O   SER A 195     3718   4357   5131   -513   -377   -347       O  
ATOM   1354  CB  SER A 195      65.211  16.348   7.806  1.00 32.37           C  
ANISOU 1354  CB  SER A 195     3408   3941   4952   -589   -251   -281       C  
ATOM   1355  OG  SER A 195      64.549  17.578   8.075  1.00 37.14           O  
ANISOU 1355  OG  SER A 195     4066   4485   5558   -613   -261   -310       O  
ATOM   1356  N   THR A 196      62.743  15.124   9.843  1.00 31.11           N  
ANISOU 1356  N   THR A 196     3373   3829   4621   -497   -342   -359       N  
ATOM   1357  CA  THR A 196      62.306  14.765  11.186  1.00 33.00           C  
ANISOU 1357  CA  THR A 196     3641   4105   4792   -469   -404   -403       C  
ATOM   1358  C   THR A 196      60.911  14.174  11.185  1.00 33.18           C  
ANISOU 1358  C   THR A 196     3724   4132   4752   -427   -391   -402       C  
ATOM   1359  O   THR A 196      60.169  14.280  10.208  1.00 32.95           O  
ANISOU 1359  O   THR A 196     3720   4065   4732   -425   -340   -378       O  
ATOM   1360  CB  THR A 196      62.283  15.958  12.162  1.00 35.26           C  
ANISOU 1360  CB  THR A 196     3957   4368   5074   -494   -448   -456       C  
ATOM   1361  OG1 THR A 196      61.057  16.686  12.005  1.00 36.09           O  
ANISOU 1361  OG1 THR A 196     4130   4423   5158   -489   -426   -470       O  
ATOM   1362  CG2 THR A 196      63.481  16.880  11.943  1.00 29.32           C  
ANISOU 1362  CG2 THR A 196     3155   3589   4397   -547   -450   -457       C  
ATOM   1363  N   ALA A 197      60.564  13.563  12.309  1.00 34.98           N  
ANISOU 1363  N   ALA A 197     3973   4406   4912   -394   -439   -428       N  
ATOM   1364  CA  ALA A 197      59.259  12.956  12.498  1.00 34.69           C  
ANISOU 1364  CA  ALA A 197     3991   4381   4808   -353   -433   -430       C  
ATOM   1365  C   ALA A 197      58.379  13.835  13.378  1.00 33.63           C  
ANISOU 1365  C   ALA A 197     3919   4230   4628   -349   -455   -475       C  
ATOM   1366  O   ALA A 197      57.447  13.345  14.005  1.00 39.18           O  
ANISOU 1366  O   ALA A 197     4665   4960   5260   -311   -466   -485       O  
ATOM   1367  CB  ALA A 197      59.415  11.575  13.119  1.00 29.00           C  
ANISOU 1367  CB  ALA A 197     3254   3727   4037   -312   -464   -418       C  
ATOM   1368  N   TYR A 198      58.684  15.129  13.424  1.00 29.78           N  
ANISOU 1368  N   TYR A 198     3436   3697   4181   -385   -458   -500       N  
ATOM   1369  CA  TYR A 198      57.953  16.067  14.274  1.00 26.22           C  
ANISOU 1369  CA  TYR A 198     3042   3227   3694   -381   -478   -546       C  
ATOM   1370  C   TYR A 198      57.368  17.234  13.487  1.00 28.53           C  
ANISOU 1370  C   TYR A 198     3367   3445   4029   -402   -438   -547       C  
ATOM   1371  O   TYR A 198      57.833  17.580  12.398  1.00 30.27           O  
ANISOU 1371  O   TYR A 198     3560   3625   4317   -433   -402   -515       O  
ATOM   1372  CB  TYR A 198      58.855  16.618  15.384  1.00 28.01           C  
ANISOU 1372  CB  TYR A 198     3251   3470   3922   -401   -534   -588       C  
ATOM   1373  CG  TYR A 198      59.416  15.557  16.301  1.00 29.41           C  
ANISOU 1373  CG  TYR A 198     3401   3722   4052   -376   -580   -588       C  
ATOM   1374  CD1 TYR A 198      58.808  15.267  17.515  1.00 34.65           C  
ANISOU 1374  CD1 TYR A 198     4107   4428   4631   -339   -612   -615       C  
ATOM   1375  CD2 TYR A 198      60.553  14.845  15.951  1.00 32.59           C  
ANISOU 1375  CD2 TYR A 198     3737   4153   4492   -386   -587   -558       C  
ATOM   1376  CE1 TYR A 198      59.316  14.289  18.356  1.00 39.80           C  
ANISOU 1376  CE1 TYR A 198     4738   5147   5236   -313   -653   -608       C  
ATOM   1377  CE2 TYR A 198      61.069  13.864  16.782  1.00 39.78           C  
ANISOU 1377  CE2 TYR A 198     4624   5132   5360   -359   -630   -553       C  
ATOM   1378  CZ  TYR A 198      60.450  13.595  17.981  1.00 41.13           C  
ANISOU 1378  CZ  TYR A 198     4841   5342   5446   -323   -663   -577       C  
ATOM   1379  OH  TYR A 198      60.968  12.628  18.800  1.00 46.11           O  
ANISOU 1379  OH  TYR A 198     5450   6037   6031   -293   -704   -566       O  
ATOM   1380  N   PHE A 199      56.339  17.841  14.061  1.00 28.32           N  
ANISOU 1380  N   PHE A 199     3400   3402   3960   -383   -442   -580       N  
ATOM   1381  CA  PHE A 199      55.731  19.026  13.494  1.00 24.68           C  
ANISOU 1381  CA  PHE A 199     2975   2870   3533   -396   -410   -586       C  
ATOM   1382  C   PHE A 199      56.106  20.232  14.340  1.00 33.57           C  
ANISOU 1382  C   PHE A 199     4114   3968   4674   -419   -445   -636       C  
ATOM   1383  O   PHE A 199      56.310  20.116  15.557  1.00 36.07           O  
ANISOU 1383  O   PHE A 199     4434   4326   4945   -409   -492   -676       O  
ATOM   1384  CB  PHE A 199      54.202  18.887  13.492  1.00 24.49           C  
ANISOU 1384  CB  PHE A 199     3009   2845   3452   -351   -386   -588       C  
ATOM   1385  CG  PHE A 199      53.685  17.815  12.575  1.00 28.28           C  
ANISOU 1385  CG  PHE A 199     3483   3342   3920   -330   -350   -542       C  
ATOM   1386  CD1 PHE A 199      53.344  18.115  11.260  1.00 25.30           C  
ANISOU 1386  CD1 PHE A 199     3111   2914   3588   -340   -300   -505       C  
ATOM   1387  CD2 PHE A 199      53.532  16.514  13.027  1.00 25.69           C  
ANISOU 1387  CD2 PHE A 199     3146   3080   3535   -300   -364   -534       C  
ATOM   1388  CE1 PHE A 199      52.873  17.139  10.416  1.00 29.59           C  
ANISOU 1388  CE1 PHE A 199     3650   3472   4119   -322   -268   -467       C  
ATOM   1389  CE2 PHE A 199      53.055  15.536  12.190  1.00 32.15           C  
ANISOU 1389  CE2 PHE A 199     3959   3910   4344   -283   -333   -496       C  
ATOM   1390  CZ  PHE A 199      52.727  15.843  10.880  1.00 32.29           C  
ANISOU 1390  CZ  PHE A 199     3985   3881   4403   -292   -281   -459       C  
ATOM   1391  N   ILE A 200      56.192  21.390  13.700  1.00 34.49           N  
ANISOU 1391  N   ILE A 200     4239   4013   4853   -451   -423   -634       N  
ATOM   1392  CA  ILE A 200      56.178  22.640  14.437  1.00 34.56           C  
ANISOU 1392  CA  ILE A 200     4277   3982   4873   -466   -449   -686       C  
ATOM   1393  C   ILE A 200      54.826  23.323  14.220  1.00 34.81           C  
ANISOU 1393  C   ILE A 200     4373   3968   4886   -437   -417   -693       C  
ATOM   1394  O   ILE A 200      54.458  23.681  13.100  1.00 30.83           O  
ANISOU 1394  O   ILE A 200     3879   3413   4422   -442   -372   -654       O  
ATOM   1395  CB  ILE A 200      57.375  23.549  14.087  1.00 40.42           C  
ANISOU 1395  CB  ILE A 200     4981   4676   5700   -526   -455   -686       C  
ATOM   1396  CG1 ILE A 200      57.206  24.918  14.742  1.00 43.83           C  
ANISOU 1396  CG1 ILE A 200     5453   5055   6148   -541   -477   -740       C  
ATOM   1397  CG2 ILE A 200      57.552  23.670  12.583  1.00 39.15           C  
ANISOU 1397  CG2 ILE A 200     4801   4471   5605   -549   -399   -622       C  
ATOM   1398  CD1 ILE A 200      58.426  25.804  14.602  1.00 53.28           C  
ANISOU 1398  CD1 ILE A 200     6610   6207   7426   -603   -493   -749       C  
ATOM   1399  N   ALA A 201      54.089  23.489  15.313  1.00 36.93           N  
ANISOU 1399  N   ALA A 201     4684   4257   5092   -403   -440   -741       N  
ATOM   1400  CA  ALA A 201      52.680  23.861  15.256  1.00 33.65           C  
ANISOU 1400  CA  ALA A 201     4326   3818   4642   -362   -411   -747       C  
ATOM   1401  C   ALA A 201      52.378  25.263  15.783  1.00 42.45           C  
ANISOU 1401  C   ALA A 201     5482   4876   5772   -366   -421   -797       C  
ATOM   1402  O   ALA A 201      53.009  25.735  16.732  1.00 46.83           O  
ANISOU 1402  O   ALA A 201     6034   5435   6325   -385   -463   -847       O  
ATOM   1403  CB  ALA A 201      51.849  22.827  16.019  1.00 26.63           C  
ANISOU 1403  CB  ALA A 201     3453   3003   3660   -310   -417   -755       C  
ATOM   1404  N   ASP A 202      51.402  25.919  15.159  1.00 40.37           N  
ANISOU 1404  N   ASP A 202     5259   4558   5522   -346   -382   -785       N  
ATOM   1405  CA  ASP A 202      50.835  27.156  15.692  1.00 42.16           C  
ANISOU 1405  CA  ASP A 202     5534   4734   5751   -335   -385   -833       C  
ATOM   1406  C   ASP A 202      49.354  26.938  16.021  1.00 47.65           C  
ANISOU 1406  C   ASP A 202     6273   5454   6378   -271   -362   -841       C  
ATOM   1407  O   ASP A 202      48.596  26.451  15.179  1.00 47.43           O  
ANISOU 1407  O   ASP A 202     6249   5429   6342   -245   -324   -796       O  
ATOM   1408  CB  ASP A 202      50.964  28.317  14.693  1.00 40.32           C  
ANISOU 1408  CB  ASP A 202     5313   4405   5600   -364   -359   -810       C  
ATOM   1409  CG  ASP A 202      52.410  28.709  14.409  1.00 43.51           C  
ANISOU 1409  CG  ASP A 202     5674   4778   6079   -431   -378   -804       C  
ATOM   1410  OD1 ASP A 202      53.322  28.302  15.164  1.00 44.39           O  
ANISOU 1410  OD1 ASP A 202     5751   4937   6180   -454   -420   -831       O  
ATOM   1411  OD2 ASP A 202      52.629  29.442  13.422  1.00 41.21           O  
ANISOU 1411  OD2 ASP A 202     5383   4417   5856   -459   -349   -768       O  
ATOM   1412  N   GLY A 203      48.947  27.310  17.236  1.00 47.74           N  
ANISOU 1412  N   GLY A 203     6314   5485   6340   -246   -384   -900       N  
ATOM   1413  CA  GLY A 203      47.557  27.216  17.660  1.00 41.44           C  
ANISOU 1413  CA  GLY A 203     5555   4712   5479   -185   -360   -912       C  
ATOM   1414  C   GLY A 203      46.824  28.548  17.801  1.00 42.79           C  
ANISOU 1414  C   GLY A 203     5774   4815   5668   -166   -345   -948       C  
ATOM   1415  O   GLY A 203      47.396  29.550  18.224  1.00 45.22           O  
ANISOU 1415  O   GLY A 203     6095   5075   6011   -193   -370   -993       O  
ATOM   1416  N   ASP A 204      45.546  28.558  17.436  1.00 40.31           N  
ANISOU 1416  N   ASP A 204     5485   4498   5333   -117   -304   -930       N  
ATOM   1417  CA  ASP A 204      44.701  29.734  17.603  1.00 35.94           C  
ANISOU 1417  CA  ASP A 204     4978   3888   4791    -87   -285   -962       C  
ATOM   1418  C   ASP A 204      43.295  29.327  17.998  1.00 42.45           C  
ANISOU 1418  C   ASP A 204     5820   4763   5548    -21   -256   -964       C  
ATOM   1419  O   ASP A 204      42.777  28.308  17.545  1.00 46.28           O  
ANISOU 1419  O   ASP A 204     6284   5296   6002      0   -235   -918       O  
ATOM   1420  CB  ASP A 204      44.654  30.551  16.320  1.00 38.12           C  
ANISOU 1420  CB  ASP A 204     5265   4074   5146   -102   -258   -923       C  
ATOM   1421  CG  ASP A 204      45.986  31.159  15.983  1.00 50.03           C  
ANISOU 1421  CG  ASP A 204     6759   5525   6727   -168   -282   -923       C  
ATOM   1422  OD1 ASP A 204      46.532  31.872  16.849  1.00 61.21           O  
ANISOU 1422  OD1 ASP A 204     8186   6919   8151   -190   -315   -982       O  
ATOM   1423  OD2 ASP A 204      46.499  30.911  14.871  1.00 50.78           O  
ANISOU 1423  OD2 ASP A 204     6828   5597   6869   -199   -268   -866       O  
ATOM   1424  N   VAL A 205      42.678  30.128  18.851  1.00 42.29           N  
ANISOU 1424  N   VAL A 205     5835   4729   5505     12   -254  -1017       N  
ATOM   1425  CA  VAL A 205      41.314  29.874  19.266  1.00 38.58           C  
ANISOU 1425  CA  VAL A 205     5379   4305   4976     76   -222  -1021       C  
ATOM   1426  C   VAL A 205      40.449  31.038  18.822  1.00 43.51           C  
ANISOU 1426  C   VAL A 205     6037   4854   5640    107   -190  -1029       C  
ATOM   1427  O   VAL A 205      40.802  32.197  19.041  1.00 49.95           O  
ANISOU 1427  O   VAL A 205     6882   5600   6496     92   -202  -1071       O  
ATOM   1428  CB  VAL A 205      41.219  29.697  20.779  1.00 45.38           C  
ANISOU 1428  CB  VAL A 205     6252   5230   5762     97   -243  -1076       C  
ATOM   1429  CG1 VAL A 205      39.785  29.404  21.186  1.00 52.71           C  
ANISOU 1429  CG1 VAL A 205     7189   6208   6630    163   -204  -1074       C  
ATOM   1430  CG2 VAL A 205      42.142  28.576  21.228  1.00 43.13           C  
ANISOU 1430  CG2 VAL A 205     5934   5015   5439     68   -277  -1066       C  
ATOM   1431  N   THR A 206      39.336  30.720  18.166  1.00 40.87           N  
ANISOU 1431  N   THR A 206     5698   4533   5298    150   -149   -987       N  
ATOM   1432  CA  THR A 206      38.390  31.721  17.697  1.00 35.00           C  
ANISOU 1432  CA  THR A 206     4982   3726   4590    189   -116   -986       C  
ATOM   1433  C   THR A 206      37.200  31.748  18.634  1.00 36.11           C  
ANISOU 1433  C   THR A 206     5134   3916   4672    252    -95  -1020       C  
ATOM   1434  O   THR A 206      37.031  30.849  19.459  1.00 37.49           O  
ANISOU 1434  O   THR A 206     5292   4177   4776    264   -100  -1029       O  
ATOM   1435  CB  THR A 206      37.886  31.406  16.287  1.00 34.62           C  
ANISOU 1435  CB  THR A 206     4917   3660   4576    201    -86   -915       C  
ATOM   1436  OG1 THR A 206      37.182  30.155  16.305  1.00 34.54           O  
ANISOU 1436  OG1 THR A 206     4876   3739   4508    230    -71   -884       O  
ATOM   1437  CG2 THR A 206      39.057  31.338  15.303  1.00 30.94           C  
ANISOU 1437  CG2 THR A 206     4440   3149   4166    141   -102   -875       C  
ATOM   1438  N   ALA A 207      36.363  32.769  18.493  1.00 35.33           N  
ANISOU 1438  N   ALA A 207     5062   3763   4601    292    -68  -1035       N  
ATOM   1439  CA  ALA A 207      35.286  32.995  19.443  1.00 37.27           C  
ANISOU 1439  CA  ALA A 207     5319   4045   4796    351    -46  -1076       C  
ATOM   1440  C   ALA A 207      33.938  32.819  18.775  1.00 39.90           C  
ANISOU 1440  C   ALA A 207     5635   4394   5132    407     -3  -1032       C  
ATOM   1441  O   ALA A 207      32.896  32.854  19.431  1.00 40.66           O  
ANISOU 1441  O   ALA A 207     5731   4532   5187    461     21  -1053       O  
ATOM   1442  CB  ALA A 207      35.405  34.385  20.041  1.00 38.17           C  
ANISOU 1442  CB  ALA A 207     5478   4086   4938    358    -53  -1142       C  
ATOM   1443  N   SER A 208      33.961  32.611  17.465  1.00 41.64           N  
ANISOU 1443  N   SER A 208     5838   4585   5398    395      6   -970       N  
ATOM   1444  CA  SER A 208      32.729  32.553  16.703  1.00 40.18           C  
ANISOU 1444  CA  SER A 208     5636   4407   5225    447     41   -927       C  
ATOM   1445  C   SER A 208      32.944  31.926  15.347  1.00 39.20           C  
ANISOU 1445  C   SER A 208     5487   4276   5131    425     42   -857       C  
ATOM   1446  O   SER A 208      34.063  31.888  14.841  1.00 40.34           O  
ANISOU 1446  O   SER A 208     5636   4383   5308    371     21   -841       O  
ATOM   1447  CB  SER A 208      32.192  33.960  16.487  1.00 39.69           C  
ANISOU 1447  CB  SER A 208     5605   4259   5216    483     61   -946       C  
ATOM   1448  OG  SER A 208      33.032  34.660  15.589  1.00 46.48           O  
ANISOU 1448  OG  SER A 208     6487   5025   6147    443     51   -925       O  
ATOM   1449  N   LEU A 209      31.845  31.464  14.759  1.00 34.88           N  
ANISOU 1449  N   LEU A 209     4912   3766   4576    469     66   -815       N  
ATOM   1450  CA  LEU A 209      31.843  30.915  13.414  1.00 33.77           C  
ANISOU 1450  CA  LEU A 209     4749   3621   4462    460     68   -748       C  
ATOM   1451  C   LEU A 209      32.445  31.892  12.411  1.00 37.81           C  
ANISOU 1451  C   LEU A 209     5287   4030   5050    440     67   -725       C  
ATOM   1452  O   LEU A 209      33.270  31.503  11.588  1.00 38.88           O  
ANISOU 1452  O   LEU A 209     5418   4147   5207    397     55   -686       O  
ATOM   1453  CB  LEU A 209      30.415  30.538  13.009  1.00 29.78           C  
ANISOU 1453  CB  LEU A 209     4212   3164   3940    520     92   -715       C  
ATOM   1454  CG  LEU A 209      30.160  29.964  11.617  1.00 32.56           C  
ANISOU 1454  CG  LEU A 209     4539   3521   4312    524     93   -647       C  
ATOM   1455  CD1 LEU A 209      31.131  28.834  11.285  1.00 33.77           C  
ANISOU 1455  CD1 LEU A 209     4679   3705   4446    470     73   -623       C  
ATOM   1456  CD2 LEU A 209      28.737  29.472  11.551  1.00 29.16           C  
ANISOU 1456  CD2 LEU A 209     4073   3158   3850    581    111   -627       C  
ATOM   1457  N   ASP A 210      32.042  33.158  12.489  1.00 44.60           N  
ANISOU 1457  N   ASP A 210     6175   4821   5948    470     81   -746       N  
ATOM   1458  CA  ASP A 210      32.530  34.177  11.554  1.00 41.22           C  
ANISOU 1458  CA  ASP A 210     5777   4290   5595    454     86   -718       C  
ATOM   1459  C   ASP A 210      34.035  34.358  11.654  1.00 32.44           C  
ANISOU 1459  C   ASP A 210     4690   3132   4503    382     62   -731       C  
ATOM   1460  O   ASP A 210      34.704  34.576  10.655  1.00 37.08           O  
ANISOU 1460  O   ASP A 210     5289   3665   5136    350     62   -684       O  
ATOM   1461  CB  ASP A 210      31.832  35.520  11.774  1.00 40.13           C  
ANISOU 1461  CB  ASP A 210     5669   4085   5495    501    107   -744       C  
ATOM   1462  CG  ASP A 210      30.388  35.503  11.327  1.00 46.39           C  
ANISOU 1462  CG  ASP A 210     6433   4905   6287    572    129   -715       C  
ATOM   1463  OD1 ASP A 210      29.983  34.520  10.676  1.00 47.91           O  
ANISOU 1463  OD1 ASP A 210     6587   5160   6457    582    127   -667       O  
ATOM   1464  OD2 ASP A 210      29.659  36.476  11.617  1.00 49.17           O  
ANISOU 1464  OD2 ASP A 210     6802   5218   6664    620    147   -739       O  
ATOM   1465  N   GLU A 211      34.557  34.256  12.867  1.00 31.96           N  
ANISOU 1465  N   GLU A 211     4635   3100   4407    357     40   -793       N  
ATOM   1466  CA  GLU A 211      35.991  34.368  13.119  1.00 37.20           C  
ANISOU 1466  CA  GLU A 211     5313   3735   5087    288      8   -813       C  
ATOM   1467  C   GLU A 211      36.748  33.140  12.575  1.00 38.53           C  
ANISOU 1467  C   GLU A 211     5446   3954   5240    244     -8   -770       C  
ATOM   1468  O   GLU A 211      37.805  33.270  11.947  1.00 35.80           O  
ANISOU 1468  O   GLU A 211     5103   3563   4936    191    -21   -743       O  
ATOM   1469  CB  GLU A 211      36.206  34.521  14.623  1.00 43.31           C  
ANISOU 1469  CB  GLU A 211     6097   4538   5820    283    -13   -892       C  
ATOM   1470  CG  GLU A 211      37.577  34.985  15.053  1.00 55.64           C  
ANISOU 1470  CG  GLU A 211     7676   6057   7407    219    -50   -928       C  
ATOM   1471  CD  GLU A 211      37.591  35.389  16.518  1.00 63.10           C  
ANISOU 1471  CD  GLU A 211     8640   7019   8315    227    -69  -1011       C  
ATOM   1472  OE1 GLU A 211      36.548  35.881  17.003  1.00 67.38           O  
ANISOU 1472  OE1 GLU A 211     9201   7562   8839    284    -45  -1041       O  
ATOM   1473  OE2 GLU A 211      38.633  35.208  17.185  1.00 64.34           O  
ANISOU 1473  OE2 GLU A 211     8792   7193   8460    180   -107  -1045       O  
ATOM   1474  N   THR A 212      36.191  31.954  12.816  1.00 26.25           N  
ANISOU 1474  N   THR A 212     3856   2491   3626    265     -5   -761       N  
ATOM   1475  CA  THR A 212      36.735  30.714  12.274  1.00 28.75           C  
ANISOU 1475  CA  THR A 212     4139   2859   3927    233    -16   -720       C  
ATOM   1476  C   THR A 212      36.879  30.807  10.751  1.00 36.19           C  
ANISOU 1476  C   THR A 212     5081   3750   4921    224     -2   -652       C  
ATOM   1477  O   THR A 212      37.928  30.464  10.185  1.00 35.42           O  
ANISOU 1477  O   THR A 212     4974   3639   4846    174    -16   -624       O  
ATOM   1478  CB  THR A 212      35.826  29.515  12.618  1.00 30.16           C  
ANISOU 1478  CB  THR A 212     4285   3136   4038    270     -8   -713       C  
ATOM   1479  OG1 THR A 212      35.779  29.332  14.039  1.00 25.14           O  
ANISOU 1479  OG1 THR A 212     3651   2554   3348    276    -20   -768       O  
ATOM   1480  CG2 THR A 212      36.330  28.240  11.956  1.00 29.49           C  
ANISOU 1480  CG2 THR A 212     4169   3096   3941    240    -17   -669       C  
ATOM   1481  N   ILE A 213      35.824  31.286  10.095  1.00 30.43           N  
ANISOU 1481  N   ILE A 213     4359   2994   4209    276     25   -624       N  
ATOM   1482  CA  ILE A 213      35.817  31.428   8.647  1.00 28.28           C  
ANISOU 1482  CA  ILE A 213     4090   2676   3979    279     41   -555       C  
ATOM   1483  C   ILE A 213      36.765  32.524   8.172  1.00 36.15           C  
ANISOU 1483  C   ILE A 213     5126   3575   5036    240     39   -539       C  
ATOM   1484  O   ILE A 213      37.370  32.411   7.103  1.00 37.76           O  
ANISOU 1484  O   ILE A 213     5333   3750   5266    213     39   -482       O  
ATOM   1485  CB  ILE A 213      34.410  31.725   8.146  1.00 32.65           C  
ANISOU 1485  CB  ILE A 213     4637   3230   4539    348     65   -530       C  
ATOM   1486  CG1 ILE A 213      33.488  30.550   8.486  1.00 32.76           C  
ANISOU 1486  CG1 ILE A 213     4611   3346   4489    383     62   -534       C  
ATOM   1487  CG2 ILE A 213      34.422  31.995   6.646  1.00 32.01           C  
ANISOU 1487  CG2 ILE A 213     4560   3098   4505    354     79   -456       C  
ATOM   1488  CD1 ILE A 213      32.063  30.798   8.124  1.00 37.17           C  
ANISOU 1488  CD1 ILE A 213     5157   3919   5046    452     78   -514       C  
ATOM   1489  N   ALA A 214      36.897  33.577   8.977  1.00 30.02           N  
ANISOU 1489  N   ALA A 214     4380   2748   4277    237     34   -590       N  
ATOM   1490  CA  ALA A 214      37.789  34.687   8.648  1.00 36.68           C  
ANISOU 1490  CA  ALA A 214     5263   3497   5178    199     26   -582       C  
ATOM   1491  C   ALA A 214      39.235  34.221   8.687  1.00 37.31           C  
ANISOU 1491  C   ALA A 214     5321   3585   5268    122     -4   -582       C  
ATOM   1492  O   ALA A 214      40.033  34.552   7.808  1.00 41.56           O  
ANISOU 1492  O   ALA A 214     5865   4072   5853     83     -7   -535       O  
ATOM   1493  CB  ALA A 214      37.579  35.861   9.620  1.00 32.98           C  
ANISOU 1493  CB  ALA A 214     4829   2977   4724    213     25   -647       C  
ATOM   1494  N   LEU A 215      39.557  33.449   9.719  1.00 30.14           N  
ANISOU 1494  N   LEU A 215     4385   2748   4319    103    -26   -632       N  
ATOM   1495  CA  LEU A 215      40.887  32.890   9.883  1.00 33.55           C  
ANISOU 1495  CA  LEU A 215     4788   3203   4759     36    -55   -637       C  
ATOM   1496  C   LEU A 215      41.239  31.922   8.754  1.00 36.08           C  
ANISOU 1496  C   LEU A 215     5075   3550   5082     17    -46   -568       C  
ATOM   1497  O   LEU A 215      42.412  31.741   8.433  1.00 45.14           O  
ANISOU 1497  O   LEU A 215     6200   4690   6262    -41    -59   -549       O  
ATOM   1498  CB  LEU A 215      41.001  32.205  11.253  1.00 38.28           C  
ANISOU 1498  CB  LEU A 215     5366   3879   5300     32    -80   -700       C  
ATOM   1499  CG  LEU A 215      42.268  31.426  11.618  1.00 38.88           C  
ANISOU 1499  CG  LEU A 215     5405   3999   5371    -27   -113   -710       C  
ATOM   1500  CD1 LEU A 215      42.543  31.573  13.091  1.00 40.65           C  
ANISOU 1500  CD1 LEU A 215     5632   4253   5560    -33   -145   -785       C  
ATOM   1501  CD2 LEU A 215      42.142  29.946  11.265  1.00 38.77           C  
ANISOU 1501  CD2 LEU A 215     5352   4065   5314    -20   -109   -674       C  
ATOM   1502  N   HIS A 216      40.230  31.303   8.148  1.00 33.63           N  
ANISOU 1502  N   HIS A 216     4760   3275   4743     66    -24   -531       N  
ATOM   1503  CA  HIS A 216      40.483  30.369   7.053  1.00 35.17           C  
ANISOU 1503  CA  HIS A 216     4928   3497   4940     54    -15   -468       C  
ATOM   1504  C   HIS A 216      40.442  31.035   5.687  1.00 39.18           C  
ANISOU 1504  C   HIS A 216     5457   3938   5493     60      4   -398       C  
ATOM   1505  O   HIS A 216      40.732  30.398   4.680  1.00 43.64           O  
ANISOU 1505  O   HIS A 216     6000   4517   6064     47     14   -341       O  
ATOM   1506  CB  HIS A 216      39.511  29.191   7.092  1.00 27.63           C  
ANISOU 1506  CB  HIS A 216     3950   2621   3926     98     -7   -465       C  
ATOM   1507  CG  HIS A 216      39.842  28.176   8.136  1.00 27.44           C  
ANISOU 1507  CG  HIS A 216     3896   2675   3855     79    -29   -510       C  
ATOM   1508  ND1 HIS A 216      39.464  28.314   9.456  1.00 35.50           N  
ANISOU 1508  ND1 HIS A 216     4923   3729   4838     97    -41   -571       N  
ATOM   1509  CD2 HIS A 216      40.530  27.012   8.063  1.00 26.80           C  
ANISOU 1509  CD2 HIS A 216     3780   2646   3756     47    -42   -498       C  
ATOM   1510  CE1 HIS A 216      39.902  27.280  10.148  1.00 31.63           C  
ANISOU 1510  CE1 HIS A 216     4404   3308   4305     77    -62   -592       C  
ATOM   1511  NE2 HIS A 216      40.550  26.472   9.324  1.00 32.85           N  
ANISOU 1511  NE2 HIS A 216     4534   3474   4473     47    -63   -549       N  
ATOM   1512  N   SER A 217      40.102  32.318   5.653  1.00 39.79           N  
ANISOU 1512  N   SER A 217     5575   3942   5599     80     10   -401       N  
ATOM   1513  CA  SER A 217      40.004  33.032   4.385  1.00 43.03           C  
ANISOU 1513  CA  SER A 217     6009   4290   6050     92     22   -331       C  
ATOM   1514  C   SER A 217      40.936  34.244   4.333  1.00 47.51           C  
ANISOU 1514  C   SER A 217     6598   4772   6680     45     17   -329       C  
ATOM   1515  O   SER A 217      40.825  35.082   3.438  1.00 49.84           O  
ANISOU 1515  O   SER A 217     6918   5005   7012     56     27   -277       O  
ATOM   1516  CB  SER A 217      38.565  33.495   4.131  1.00 45.57           C  
ANISOU 1516  CB  SER A 217     6363   4599   6353    174     33   -320       C  
ATOM   1517  OG  SER A 217      37.607  32.606   4.681  1.00 45.15           O  
ANISOU 1517  OG  SER A 217     6290   4622   6244    217     45   -349       O  
ATOM   1518  N   ASP A 218      41.851  34.351   5.288  1.00 41.08           N  
ANISOU 1518  N   ASP A 218     5771   3957   5879     -8      0   -385       N  
ATOM   1519  CA  ASP A 218      42.682  35.546   5.358  1.00 38.64           C  
ANISOU 1519  CA  ASP A 218     5483   3565   5632    -53     -7   -393       C  
ATOM   1520  C   ASP A 218      44.044  35.352   4.710  1.00 41.45           C  
ANISOU 1520  C   ASP A 218     5801   3915   6033   -126     -5   -349       C  
ATOM   1521  O   ASP A 218      44.922  36.204   4.836  1.00 48.07           O  
ANISOU 1521  O   ASP A 218     6643   4694   6926   -176    -12   -357       O  
ATOM   1522  CB  ASP A 218      42.833  36.039   6.802  1.00 34.45           C  
ANISOU 1522  CB  ASP A 218     4966   3026   5098    -65    -31   -484       C  
ATOM   1523  CG  ASP A 218      43.574  35.060   7.689  1.00 46.31           C  
ANISOU 1523  CG  ASP A 218     6423   4603   6570   -104    -56   -530       C  
ATOM   1524  OD1 ASP A 218      44.141  34.070   7.176  1.00 47.75           O  
ANISOU 1524  OD1 ASP A 218     6562   4836   6746   -131    -54   -492       O  
ATOM   1525  OD2 ASP A 218      43.597  35.290   8.917  1.00 52.57           O  
ANISOU 1525  OD2 ASP A 218     7223   5407   7345   -106    -78   -605       O  
ATOM   1526  N   GLY A 219      44.218  34.215   4.046  1.00 36.53           N  
ANISOU 1526  N   GLY A 219     5139   3354   5387   -131      8   -303       N  
ATOM   1527  CA  GLY A 219      45.462  33.900   3.366  1.00 27.98           C  
ANISOU 1527  CA  GLY A 219     4014   2276   4340   -193     20   -256       C  
ATOM   1528  C   GLY A 219      46.486  33.169   4.216  1.00 35.87           C  
ANISOU 1528  C   GLY A 219     4966   3327   5335   -244     -4   -304       C  
ATOM   1529  O   GLY A 219      47.541  32.802   3.711  1.00 48.22           O  
ANISOU 1529  O   GLY A 219     6489   4905   6926   -293      7   -268       O  
ATOM   1530  N   SER A 220      46.194  32.951   5.497  1.00 30.13           N  
ANISOU 1530  N   SER A 220     4243   2633   4571   -231    -35   -381       N  
ATOM   1531  CA  SER A 220      47.161  32.298   6.388  1.00 29.69           C  
ANISOU 1531  CA  SER A 220     4144   2629   4507   -275    -65   -428       C  
ATOM   1532  C   SER A 220      47.265  30.783   6.173  1.00 35.42           C  
ANISOU 1532  C   SER A 220     4826   3440   5190   -271    -61   -407       C  
ATOM   1533  O   SER A 220      48.298  30.184   6.480  1.00 39.56           O  
ANISOU 1533  O   SER A 220     5306   4003   5721   -314    -78   -418       O  
ATOM   1534  CB  SER A 220      46.860  32.589   7.864  1.00 33.50           C  
ANISOU 1534  CB  SER A 220     4646   3123   4959   -261   -101   -517       C  
ATOM   1535  OG  SER A 220      45.632  32.012   8.278  1.00 39.76           O  
ANISOU 1535  OG  SER A 220     5457   3965   5685   -198    -98   -538       O  
ATOM   1536  N   GLU A 221      46.205  30.165   5.662  1.00 27.02           N  
ANISOU 1536  N   GLU A 221     3776   2405   4084   -219    -41   -379       N  
ATOM   1537  CA  GLU A 221      46.243  28.731   5.372  1.00 32.86           C  
ANISOU 1537  CA  GLU A 221     4479   3219   4787   -214    -34   -357       C  
ATOM   1538  C   GLU A 221      47.446  28.382   4.480  1.00 40.39           C  
ANISOU 1538  C   GLU A 221     5392   4175   5782   -265    -14   -302       C  
ATOM   1539  O   GLU A 221      48.085  27.332   4.651  1.00 36.53           O  
ANISOU 1539  O   GLU A 221     4859   3742   5277   -286    -22   -306       O  
ATOM   1540  CB  GLU A 221      44.923  28.258   4.743  1.00 26.51           C  
ANISOU 1540  CB  GLU A 221     3696   2433   3942   -153    -10   -327       C  
ATOM   1541  CG  GLU A 221      43.796  28.022   5.748  1.00 32.40           C  
ANISOU 1541  CG  GLU A 221     4462   3217   4633   -102    -28   -384       C  
ATOM   1542  CD  GLU A 221      44.013  26.771   6.593  1.00 36.56           C  
ANISOU 1542  CD  GLU A 221     4955   3826   5111   -109    -50   -421       C  
ATOM   1543  OE1 GLU A 221      44.503  26.893   7.732  1.00 34.51           O  
ANISOU 1543  OE1 GLU A 221     4690   3583   4840   -129    -81   -476       O  
ATOM   1544  OE2 GLU A 221      43.696  25.657   6.115  1.00 33.41           O  
ANISOU 1544  OE2 GLU A 221     4537   3475   4683    -93    -38   -395       O  
ATOM   1545  N   ALA A 222      47.776  29.287   3.562  1.00 38.97           N  
ANISOU 1545  N   ALA A 222     5222   3932   5651   -283     12   -251       N  
ATOM   1546  CA  ALA A 222      48.907  29.087   2.653  1.00 37.42           C  
ANISOU 1546  CA  ALA A 222     4987   3737   5494   -329     40   -193       C  
ATOM   1547  C   ALA A 222      50.258  28.948   3.363  1.00 33.12           C  
ANISOU 1547  C   ALA A 222     4394   3211   4980   -388     14   -227       C  
ATOM   1548  O   ALA A 222      51.223  28.463   2.783  1.00 32.73           O  
ANISOU 1548  O   ALA A 222     4300   3184   4952   -422     34   -188       O  
ATOM   1549  CB  ALA A 222      48.965  30.210   1.647  1.00 32.60           C  
ANISOU 1549  CB  ALA A 222     4402   3057   4929   -335     73   -133       C  
ATOM   1550  N   ARG A 223      50.319  29.376   4.617  1.00 38.96           N  
ANISOU 1550  N   ARG A 223     5142   3943   5717   -396    -30   -301       N  
ATOM   1551  CA  ARG A 223      51.553  29.324   5.392  1.00 38.19           C  
ANISOU 1551  CA  ARG A 223     5001   3864   5647   -448    -62   -339       C  
ATOM   1552  C   ARG A 223      51.757  27.984   6.083  1.00 37.35           C  
ANISOU 1552  C   ARG A 223     4857   3843   5490   -441    -89   -370       C  
ATOM   1553  O   ARG A 223      52.816  27.736   6.653  1.00 41.01           O  
ANISOU 1553  O   ARG A 223     5278   4335   5971   -479   -116   -395       O  
ATOM   1554  CB  ARG A 223      51.569  30.426   6.457  1.00 44.20           C  
ANISOU 1554  CB  ARG A 223     5790   4580   6426   -460   -100   -406       C  
ATOM   1555  CG  ARG A 223      51.820  31.836   5.926  1.00 49.69           C  
ANISOU 1555  CG  ARG A 223     6509   5184   7188   -488    -82   -383       C  
ATOM   1556  CD  ARG A 223      52.240  32.781   7.052  1.00 51.23           C  
ANISOU 1556  CD  ARG A 223     6715   5340   7410   -517   -125   -455       C  
ATOM   1557  NE  ARG A 223      51.140  33.166   7.939  1.00 56.15           N  
ANISOU 1557  NE  ARG A 223     7393   5953   7990   -469   -146   -515       N  
ATOM   1558  CZ  ARG A 223      50.267  34.134   7.663  1.00 62.89           C  
ANISOU 1558  CZ  ARG A 223     8302   6738   8854   -438   -128   -508       C  
ATOM   1559  NH1 ARG A 223      50.353  34.803   6.517  1.00 64.52           N  
ANISOU 1559  NH1 ARG A 223     8521   6882   9112   -450    -92   -442       N  
ATOM   1560  NH2 ARG A 223      49.303  34.434   8.529  1.00 61.12           N  
ANISOU 1560  NH2 ARG A 223     8122   6512   8588   -392   -144   -566       N  
ATOM   1561  N   TYR A 224      50.741  27.131   6.065  1.00 30.57           N  
ANISOU 1561  N   TYR A 224     4016   3027   4573   -392    -82   -369       N  
ATOM   1562  CA  TYR A 224      50.852  25.839   6.728  1.00 24.47           C  
ANISOU 1562  CA  TYR A 224     3214   2334   3751   -383   -107   -396       C  
ATOM   1563  C   TYR A 224      50.507  24.714   5.771  1.00 28.55           C  
ANISOU 1563  C   TYR A 224     3717   2886   4244   -361    -72   -344       C  
ATOM   1564  O   TYR A 224      49.567  24.817   4.993  1.00 36.45           O  
ANISOU 1564  O   TYR A 224     4750   3865   5233   -328    -40   -310       O  
ATOM   1565  CB  TYR A 224      49.923  25.772   7.936  1.00 26.01           C  
ANISOU 1565  CB  TYR A 224     3441   2555   3885   -342   -140   -460       C  
ATOM   1566  CG  TYR A 224      50.068  26.917   8.909  1.00 26.32           C  
ANISOU 1566  CG  TYR A 224     3504   2557   3939   -355   -171   -517       C  
ATOM   1567  CD1 TYR A 224      51.080  26.924   9.864  1.00 31.99           C  
ANISOU 1567  CD1 TYR A 224     4193   3299   4664   -390   -213   -560       C  
ATOM   1568  CD2 TYR A 224      49.184  27.977   8.891  1.00 25.07           C  
ANISOU 1568  CD2 TYR A 224     3397   2341   3786   -329   -160   -528       C  
ATOM   1569  CE1 TYR A 224      51.208  27.960  10.768  1.00 27.47           C  
ANISOU 1569  CE1 TYR A 224     3644   2692   4103   -401   -242   -616       C  
ATOM   1570  CE2 TYR A 224      49.299  29.021   9.791  1.00 31.38           C  
ANISOU 1570  CE2 TYR A 224     4221   3104   4599   -339   -186   -584       C  
ATOM   1571  CZ  TYR A 224      50.311  29.011  10.727  1.00 34.92           C  
ANISOU 1571  CZ  TYR A 224     4641   3575   5053   -376   -228   -629       C  
ATOM   1572  OH  TYR A 224      50.418  30.062  11.619  1.00 38.42           O  
ANISOU 1572  OH  TYR A 224     5110   3979   5509   -387   -256   -688       O  
ATOM   1573  N   THR A 225      51.276  23.636   5.830  1.00 31.89           N  
ANISOU 1573  N   THR A 225     4093   3365   4660   -378    -79   -339       N  
ATOM   1574  CA  THR A 225      51.006  22.472   5.007  1.00 28.22           C  
ANISOU 1574  CA  THR A 225     3615   2937   4172   -359    -47   -296       C  
ATOM   1575  C   THR A 225      49.888  21.645   5.631  1.00 24.72           C  
ANISOU 1575  C   THR A 225     3195   2538   3661   -313    -65   -330       C  
ATOM   1576  O   THR A 225      49.184  20.940   4.936  1.00 20.68           O  
ANISOU 1576  O   THR A 225     2695   2059   3102   -278    -37   -289       O  
ATOM   1577  CB  THR A 225      52.247  21.604   4.882  1.00 29.12           C  
ANISOU 1577  CB  THR A 225     3668   3093   4303   -391    -48   -280       C  
ATOM   1578  OG1 THR A 225      52.921  21.590   6.146  1.00 31.49           O  
ANISOU 1578  OG1 THR A 225     3944   3422   4599   -409   -101   -335       O  
ATOM   1579  CG2 THR A 225      53.183  22.176   3.828  1.00 25.61           C  
ANISOU 1579  CG2 THR A 225     3198   2613   3919   -427     -8   -224       C  
ATOM   1580  N   TYR A 226      49.736  21.756   6.946  1.00 21.08           N  
ANISOU 1580  N   TYR A 226     2741   2100   3166   -304   -110   -390       N  
ATOM   1581  CA  TYR A 226      48.754  21.001   7.711  1.00 20.70           C  
ANISOU 1581  CA  TYR A 226     2713   2104   3049   -261   -129   -423       C  
ATOM   1582  C   TYR A 226      47.874  21.946   8.513  1.00 19.74           C  
ANISOU 1582  C   TYR A 226     2636   1961   2903   -233   -143   -466       C  
ATOM   1583  O   TYR A 226      48.382  22.831   9.193  1.00 26.39           O  
ANISOU 1583  O   TYR A 226     3483   2779   3765   -254   -167   -499       O  
ATOM   1584  CB  TYR A 226      49.467  20.100   8.719  1.00 24.15           C  
ANISOU 1584  CB  TYR A 226     3116   2606   3454   -271   -169   -453       C  
ATOM   1585  CG  TYR A 226      50.171  18.899   8.137  1.00 27.73           C  
ANISOU 1585  CG  TYR A 226     3527   3106   3904   -281   -155   -408       C  
ATOM   1586  CD1 TYR A 226      49.663  17.615   8.329  1.00 22.93           C  
ANISOU 1586  CD1 TYR A 226     2920   2566   3227   -246   -154   -391       C  
ATOM   1587  CD2 TYR A 226      51.353  19.042   7.412  1.00 24.41           C  
ANISOU 1587  CD2 TYR A 226     3066   2662   3548   -323   -141   -378       C  
ATOM   1588  CE1 TYR A 226      50.305  16.513   7.810  1.00 21.40           C  
ANISOU 1588  CE1 TYR A 226     2690   2411   3028   -250   -141   -350       C  
ATOM   1589  CE2 TYR A 226      52.007  17.944   6.884  1.00 19.06           C  
ANISOU 1589  CE2 TYR A 226     2349   2030   2861   -325   -124   -336       C  
ATOM   1590  CZ  TYR A 226      51.481  16.679   7.090  1.00 24.36           C  
ANISOU 1590  CZ  TYR A 226     3027   2766   3464   -287   -126   -325       C  
ATOM   1591  OH  TYR A 226      52.120  15.578   6.568  1.00 21.32           O  
ANISOU 1591  OH  TYR A 226     2607   2421   3073   -285   -110   -287       O  
ATOM   1592  N   SER A 227      46.562  21.740   8.473  1.00 23.66           N  
ANISOU 1592  N   SER A 227     3164   2470   3357   -185   -129   -467       N  
ATOM   1593  CA  SER A 227      45.642  22.533   9.292  1.00 21.55           C  
ANISOU 1593  CA  SER A 227     2936   2193   3061   -151   -138   -508       C  
ATOM   1594  C   SER A 227      44.306  21.815   9.479  1.00 22.07           C  
ANISOU 1594  C   SER A 227     3017   2306   3063    -97   -127   -511       C  
ATOM   1595  O   SER A 227      43.737  21.299   8.516  1.00 21.07           O  
ANISOU 1595  O   SER A 227     2888   2190   2927    -79    -98   -462       O  
ATOM   1596  CB  SER A 227      45.403  23.907   8.657  1.00 22.10           C  
ANISOU 1596  CB  SER A 227     3035   2180   3181   -152   -117   -494       C  
ATOM   1597  OG  SER A 227      44.249  24.534   9.197  1.00 25.91           O  
ANISOU 1597  OG  SER A 227     3557   2654   3634   -106   -115   -524       O  
ATOM   1598  N   SER A 228      43.822  21.780  10.720  1.00 18.08           N  
ANISOU 1598  N   SER A 228     2525   1843   2504    -72   -145   -554       N  
ATOM   1599  CA  SER A 228      42.481  21.290  11.037  1.00 21.83           C  
ANISOU 1599  CA  SER A 228     3013   2363   2918    -20   -131   -557       C  
ATOM   1600  C   SER A 228      41.985  21.991  12.296  1.00 25.01           C  
ANISOU 1600  C   SER A 228     3440   2777   3287      5   -140   -605       C  
ATOM   1601  O   SER A 228      42.768  22.604  13.012  1.00 26.36           O  
ANISOU 1601  O   SER A 228     3615   2932   3470    -21   -165   -639       O  
ATOM   1602  CB  SER A 228      42.457  19.771  11.229  1.00 16.88           C  
ANISOU 1602  CB  SER A 228     2360   1812   2240    -15   -135   -541       C  
ATOM   1603  OG  SER A 228      43.262  19.381  12.322  1.00 21.77           O  
ANISOU 1603  OG  SER A 228     2966   2472   2832    -33   -167   -568       O  
ATOM   1604  N   ALA A 229      40.691  21.901  12.579  1.00 20.88           N  
ANISOU 1604  N   ALA A 229     2931   2283   2721     54   -120   -609       N  
ATOM   1605  CA  ALA A 229      40.160  22.587  13.745  1.00 16.21           C  
ANISOU 1605  CA  ALA A 229     2362   1701   2097     80   -123   -654       C  
ATOM   1606  C   ALA A 229      39.146  21.761  14.513  1.00 21.72           C  
ANISOU 1606  C   ALA A 229     3054   2476   2722    122   -109   -655       C  
ATOM   1607  O   ALA A 229      38.367  21.016  13.937  1.00 26.85           O  
ANISOU 1607  O   ALA A 229     3691   3156   3356    144    -87   -620       O  
ATOM   1608  CB  ALA A 229      39.562  23.922  13.345  1.00 17.93           C  
ANISOU 1608  CB  ALA A 229     2607   1849   2355    101   -104   -663       C  
ATOM   1609  N   TRP A 230      39.180  21.904  15.830  1.00 27.52           N  
ANISOU 1609  N   TRP A 230     3799   3245   3413    131   -122   -694       N  
ATOM   1610  CA  TRP A 230      38.160  21.353  16.698  1.00 29.79           C  
ANISOU 1610  CA  TRP A 230     4086   3601   3634    172   -103   -696       C  
ATOM   1611  C   TRP A 230      37.090  22.433  16.869  1.00 33.02           C  
ANISOU 1611  C   TRP A 230     4517   3982   4048    213    -79   -720       C  
ATOM   1612  O   TRP A 230      37.393  23.571  17.208  1.00 37.66           O  
ANISOU 1612  O   TRP A 230     5129   4520   4661    209    -90   -760       O  
ATOM   1613  CB  TRP A 230      38.770  20.981  18.039  1.00 38.71           C  
ANISOU 1613  CB  TRP A 230     5217   4780   4711    164   -129   -723       C  
ATOM   1614  CG  TRP A 230      37.998  19.933  18.743  1.00 55.14           C  
ANISOU 1614  CG  TRP A 230     7287   6941   6721    194   -110   -703       C  
ATOM   1615  CD1 TRP A 230      37.109  20.114  19.781  1.00 60.53           C  
ANISOU 1615  CD1 TRP A 230     7983   7663   7352    233    -91   -723       C  
ATOM   1616  CD2 TRP A 230      38.014  18.534  18.469  1.00 57.46           C  
ANISOU 1616  CD2 TRP A 230     7555   7285   6990    187   -104   -656       C  
ATOM   1617  NE1 TRP A 230      36.592  18.915  20.167  1.00 63.24           N  
ANISOU 1617  NE1 TRP A 230     8309   8077   7642    249    -72   -688       N  
ATOM   1618  CE2 TRP A 230      37.126  17.923  19.381  1.00 64.41           C  
ANISOU 1618  CE2 TRP A 230     8434   8232   7805    221    -81   -646       C  
ATOM   1619  CE3 TRP A 230      38.695  17.732  17.548  1.00 52.63           C  
ANISOU 1619  CE3 TRP A 230     6923   6668   6406    156   -115   -622       C  
ATOM   1620  CZ2 TRP A 230      36.901  16.535  19.393  1.00 64.60           C  
ANISOU 1620  CZ2 TRP A 230     8437   8314   7793    222    -68   -600       C  
ATOM   1621  CZ3 TRP A 230      38.472  16.368  17.559  1.00 53.69           C  
ANISOU 1621  CZ3 TRP A 230     7037   6859   6502    160   -105   -581       C  
ATOM   1622  CH2 TRP A 230      37.582  15.779  18.469  1.00 56.55           C  
ANISOU 1622  CH2 TRP A 230     7399   7285   6803    192    -81   -569       C  
ATOM   1623  N   PHE A 231      35.837  22.058  16.663  1.00 29.35           N  
ANISOU 1623  N   PHE A 231     4041   3549   3560    254    -46   -696       N  
ATOM   1624  CA  PHE A 231      34.770  22.998  16.339  1.00 24.25           C  
ANISOU 1624  CA  PHE A 231     3407   2869   2938    294    -19   -703       C  
ATOM   1625  C   PHE A 231      33.583  22.848  17.311  1.00 23.67           C  
ANISOU 1625  C   PHE A 231     3330   2856   2809    342      9   -714       C  
ATOM   1626  O   PHE A 231      33.182  21.735  17.656  1.00 27.11           O  
ANISOU 1626  O   PHE A 231     3741   3362   3196    349     21   -689       O  
ATOM   1627  CB  PHE A 231      34.373  22.658  14.896  1.00 30.97           C  
ANISOU 1627  CB  PHE A 231     4240   3701   3825    298     -5   -654       C  
ATOM   1628  CG  PHE A 231      33.296  23.500  14.306  1.00 28.49           C  
ANISOU 1628  CG  PHE A 231     3931   3351   3541    341     19   -647       C  
ATOM   1629  CD1 PHE A 231      33.606  24.495  13.398  1.00 32.86           C  
ANISOU 1629  CD1 PHE A 231     4504   3823   4158    334     15   -643       C  
ATOM   1630  CD2 PHE A 231      31.961  23.235  14.573  1.00 31.33           C  
ANISOU 1630  CD2 PHE A 231     4273   3762   3868    389     48   -638       C  
ATOM   1631  CE1 PHE A 231      32.595  25.255  12.801  1.00 29.97           C  
ANISOU 1631  CE1 PHE A 231     4143   3424   3821    378     36   -630       C  
ATOM   1632  CE2 PHE A 231      30.954  23.981  13.989  1.00 26.14           C  
ANISOU 1632  CE2 PHE A 231     3616   3076   3242    431     68   -629       C  
ATOM   1633  CZ  PHE A 231      31.270  24.993  13.103  1.00 26.13           C  
ANISOU 1633  CZ  PHE A 231     3636   2992   3301    428     61   -625       C  
ATOM   1634  N   ASP A 232      33.029  23.970  17.758  1.00 27.28           N  
ANISOU 1634  N   ASP A 232     3809   3284   3274    374     20   -751       N  
ATOM   1635  CA  ASP A 232      31.894  23.971  18.683  1.00 33.36           C  
ANISOU 1635  CA  ASP A 232     4574   4106   3995    421     50   -765       C  
ATOM   1636  C   ASP A 232      30.591  23.972  17.894  1.00 27.97           C  
ANISOU 1636  C   ASP A 232     3868   3428   3332    462     84   -732       C  
ATOM   1637  O   ASP A 232      30.325  24.904  17.147  1.00 28.93           O  
ANISOU 1637  O   ASP A 232     3999   3487   3505    477     88   -734       O  
ATOM   1638  CB  ASP A 232      31.959  25.230  19.562  1.00 36.88           C  
ANISOU 1638  CB  ASP A 232     5056   4514   4441    438     45   -827       C  
ATOM   1639  CG  ASP A 232      30.884  25.270  20.661  1.00 34.32           C  
ANISOU 1639  CG  ASP A 232     4732   4247   4062    488     76   -848       C  
ATOM   1640  OD1 ASP A 232      29.798  24.648  20.543  1.00 33.20           O  
ANISOU 1640  OD1 ASP A 232     4558   4156   3898    519    110   -813       O  
ATOM   1641  OD2 ASP A 232      31.142  25.961  21.662  1.00 29.99           O  
ANISOU 1641  OD2 ASP A 232     4213   3690   3491    495     67   -902       O  
ATOM   1642  N   ALA A 233      29.771  22.946  18.090  1.00 30.17           N  
ANISOU 1642  N   ALA A 233     4114   3781   3569    480    108   -699       N  
ATOM   1643  CA  ALA A 233      28.515  22.801  17.344  1.00 32.19           C  
ANISOU 1643  CA  ALA A 233     4337   4052   3842    516    138   -664       C  
ATOM   1644  C   ALA A 233      27.306  22.795  18.262  1.00 31.04           C  
ANISOU 1644  C   ALA A 233     4175   3964   3656    562    175   -672       C  
ATOM   1645  O   ALA A 233      26.187  22.515  17.834  1.00 31.69           O  
ANISOU 1645  O   ALA A 233     4221   4075   3745    592    201   -641       O  
ATOM   1646  CB  ALA A 233      28.534  21.521  16.515  1.00 29.03           C  
ANISOU 1646  CB  ALA A 233     3903   3687   3439    494    136   -611       C  
ATOM   1647  N   ILE A 234      27.535  23.089  19.532  1.00 31.59           N  
ANISOU 1647  N   ILE A 234     4269   4050   3684    568    176   -713       N  
ATOM   1648  CA  ILE A 234      26.471  23.014  20.518  1.00 34.85           C  
ANISOU 1648  CA  ILE A 234     4668   4523   4052    610    213   -720       C  
ATOM   1649  C   ILE A 234      26.103  24.391  21.055  1.00 37.82           C  
ANISOU 1649  C   ILE A 234     5073   4859   4437    649    223   -775       C  
ATOM   1650  O   ILE A 234      24.923  24.682  21.266  1.00 36.63           O  
ANISOU 1650  O   ILE A 234     4904   4732   4283    696    258   -775       O  
ATOM   1651  CB  ILE A 234      26.862  22.073  21.665  1.00 33.13           C  
ANISOU 1651  CB  ILE A 234     4452   4372   3765    593    215   -717       C  
ATOM   1652  CG1 ILE A 234      27.091  20.665  21.108  1.00 29.55           C  
ANISOU 1652  CG1 ILE A 234     3966   3956   3305    558    212   -659       C  
ATOM   1653  CG2 ILE A 234      25.787  22.060  22.739  1.00 31.96           C  
ANISOU 1653  CG2 ILE A 234     4292   4283   3567    637    258   -725       C  
ATOM   1654  CD1 ILE A 234      27.595  19.665  22.132  1.00 32.92           C  
ANISOU 1654  CD1 ILE A 234     4396   4444   3669    538    210   -648       C  
ATOM   1655  N   SER A 235      27.114  25.237  21.249  1.00 36.80           N  
ANISOU 1655  N   SER A 235     4988   4669   4325    629    191   -821       N  
ATOM   1656  CA  SER A 235      26.913  26.557  21.842  1.00 36.50           C  
ANISOU 1656  CA  SER A 235     4984   4588   4295    661    196   -880       C  
ATOM   1657  C   SER A 235      25.974  27.428  21.027  1.00 40.20           C  
ANISOU 1657  C   SER A 235     5444   5009   4820    702    217   -874       C  
ATOM   1658  O   SER A 235      26.030  27.452  19.795  1.00 32.49           O  
ANISOU 1658  O   SER A 235     4455   3993   3898    690    207   -839       O  
ATOM   1659  CB  SER A 235      28.247  27.282  22.048  1.00 31.45           C  
ANISOU 1659  CB  SER A 235     4391   3885   3675    623    154   -926       C  
ATOM   1660  OG  SER A 235      29.060  26.586  22.976  1.00 30.34           O  
ANISOU 1660  OG  SER A 235     4259   3793   3477    594    132   -939       O  
ATOM   1661  N   ALA A 236      25.094  28.128  21.733  1.00 51.78           N  
ANISOU 1661  N   ALA A 236     6916   6484   6272    754    246   -908       N  
ATOM   1662  CA  ALA A 236      24.251  29.134  21.113  1.00 55.46           C  
ANISOU 1662  CA  ALA A 236     7380   6900   6794    798    264   -912       C  
ATOM   1663  C   ALA A 236      25.159  30.178  20.473  1.00 46.16           C  
ANISOU 1663  C   ALA A 236     6243   5617   5679    775    233   -936       C  
ATOM   1664  O   ALA A 236      26.232  30.475  21.012  1.00 40.62           O  
ANISOU 1664  O   ALA A 236     5580   4886   4968    739    205   -976       O  
ATOM   1665  CB  ALA A 236      23.349  29.778  22.162  1.00 56.18           C  
ANISOU 1665  CB  ALA A 236     7479   7012   6855    855    299   -957       C  
ATOM   1666  N   PRO A 237      24.750  30.720  19.312  1.00 42.30           N  
ANISOU 1666  N   PRO A 237     5745   5073   5255    792    236   -907       N  
ATOM   1667  CA  PRO A 237      25.492  31.843  18.732  1.00 44.16           C  
ANISOU 1667  CA  PRO A 237     6021   5202   5555    775    214   -926       C  
ATOM   1668  C   PRO A 237      25.539  33.008  19.737  1.00 53.24           C  
ANISOU 1668  C   PRO A 237     7216   6309   6705    798    220   -999       C  
ATOM   1669  O   PRO A 237      24.660  33.106  20.602  1.00 55.87           O  
ANISOU 1669  O   PRO A 237     7542   6688   6999    846    249  -1027       O  
ATOM   1670  CB  PRO A 237      24.666  32.209  17.483  1.00 35.12           C  
ANISOU 1670  CB  PRO A 237     4853   4023   4469    810    227   -879       C  
ATOM   1671  CG  PRO A 237      23.885  31.000  17.160  1.00 33.61           C  
ANISOU 1671  CG  PRO A 237     4607   3919   4246    821    240   -827       C  
ATOM   1672  CD  PRO A 237      23.598  30.329  18.482  1.00 42.47           C  
ANISOU 1672  CD  PRO A 237     5718   5126   5294    828    258   -853       C  
ATOM   1673  N   PRO A 238      26.563  33.871  19.644  1.00 52.76           N  
ANISOU 1673  N   PRO A 238     7200   6162   6686    765    195  -1032       N  
ATOM   1674  CA  PRO A 238      27.584  33.887  18.596  1.00 51.26           C  
ANISOU 1674  CA  PRO A 238     7018   5910   6548    711    167   -998       C  
ATOM   1675  C   PRO A 238      28.770  32.967  18.890  1.00 46.77           C  
ANISOU 1675  C   PRO A 238     6450   5379   5944    646    134   -997       C  
ATOM   1676  O   PRO A 238      29.738  32.979  18.135  1.00 42.95           O  
ANISOU 1676  O   PRO A 238     5973   4846   5500    597    110   -975       O  
ATOM   1677  CB  PRO A 238      28.038  35.348  18.592  1.00 49.56           C  
ANISOU 1677  CB  PRO A 238     6853   5585   6392    709    161  -1042       C  
ATOM   1678  CG  PRO A 238      27.777  35.838  20.007  1.00 50.13           C  
ANISOU 1678  CG  PRO A 238     6951   5676   6419    738    169  -1117       C  
ATOM   1679  CD  PRO A 238      26.883  34.836  20.710  1.00 54.12           C  
ANISOU 1679  CD  PRO A 238     7419   6296   6849    772    191  -1109       C  
ATOM   1680  N   LYS A 239      28.699  32.179  19.958  1.00 49.15           N  
ANISOU 1680  N   LYS A 239     6740   5766   6170    648    134  -1016       N  
ATOM   1681  CA  LYS A 239      29.800  31.271  20.287  1.00 49.68           C  
ANISOU 1681  CA  LYS A 239     6803   5871   6201    592    103  -1013       C  
ATOM   1682  C   LYS A 239      29.789  30.025  19.393  1.00 42.90           C  
ANISOU 1682  C   LYS A 239     5903   5059   5339    571    102   -943       C  
ATOM   1683  O   LYS A 239      30.792  29.322  19.289  1.00 38.54           O  
ANISOU 1683  O   LYS A 239     5345   4520   4777    520     75   -928       O  
ATOM   1684  CB  LYS A 239      29.806  30.908  21.782  1.00 49.60           C  
ANISOU 1684  CB  LYS A 239     6801   5932   6111    601    101  -1057       C  
ATOM   1685  CG  LYS A 239      30.094  32.103  22.697  1.00 59.57           C  
ANISOU 1685  CG  LYS A 239     8112   7147   7375    611     91  -1135       C  
ATOM   1686  CD  LYS A 239      31.419  32.781  22.331  1.00 63.53           C  
ANISOU 1686  CD  LYS A 239     8643   7564   7932    555     50  -1157       C  
ATOM   1687  CE  LYS A 239      31.374  34.297  22.524  1.00 64.21           C  
ANISOU 1687  CE  LYS A 239     8773   7559   8064    573     52  -1215       C  
ATOM   1688  NZ  LYS A 239      31.654  34.727  23.924  1.00 62.52           N  
ANISOU 1688  NZ  LYS A 239     8593   7361   7801    580     36  -1293       N  
ATOM   1689  N   LEU A 240      28.652  29.768  18.749  1.00 40.19           N  
ANISOU 1689  N   LEU A 240     5528   4738   5003    611    132   -901       N  
ATOM   1690  CA  LEU A 240      28.548  28.713  17.750  1.00 38.10           C  
ANISOU 1690  CA  LEU A 240     5226   4507   4744    595    132   -836       C  
ATOM   1691  C   LEU A 240      29.618  28.893  16.669  1.00 34.49           C  
ANISOU 1691  C   LEU A 240     4782   3981   4344    548    104   -814       C  
ATOM   1692  O   LEU A 240      29.831  29.994  16.170  1.00 40.30           O  
ANISOU 1692  O   LEU A 240     5544   4633   5137    549    101   -824       O  
ATOM   1693  CB  LEU A 240      27.151  28.705  17.119  1.00 35.39           C  
ANISOU 1693  CB  LEU A 240     4850   4183   4415    649    163   -801       C  
ATOM   1694  CG  LEU A 240      26.959  27.692  15.983  1.00 37.98           C  
ANISOU 1694  CG  LEU A 240     5139   4540   4751    637    160   -735       C  
ATOM   1695  CD1 LEU A 240      27.175  26.257  16.476  1.00 38.39           C  
ANISOU 1695  CD1 LEU A 240     5166   4676   4744    609    159   -718       C  
ATOM   1696  CD2 LEU A 240      25.594  27.840  15.328  1.00 34.85           C  
ANISOU 1696  CD2 LEU A 240     4710   4156   4375    691    185   -703       C  
ATOM   1697  N   GLY A 241      30.319  27.818  16.339  1.00 27.57           N  
ANISOU 1697  N   GLY A 241     3887   3137   3451    505     87   -782       N  
ATOM   1698  CA  GLY A 241      31.327  27.872  15.296  1.00 30.81           C  
ANISOU 1698  CA  GLY A 241     4305   3489   3911    460     64   -757       C  
ATOM   1699  C   GLY A 241      32.722  28.301  15.723  1.00 29.12           C  
ANISOU 1699  C   GLY A 241     4120   3232   3713    408     34   -792       C  
ATOM   1700  O   GLY A 241      33.638  28.297  14.910  1.00 36.20           O  
ANISOU 1700  O   GLY A 241     5019   4084   4650    366     17   -769       O  
ATOM   1701  N   ARG A 242      32.894  28.691  16.979  1.00 29.75           N  
ANISOU 1701  N   ARG A 242     4219   3324   3760    411     26   -848       N  
ATOM   1702  CA  ARG A 242      34.233  28.975  17.486  1.00 35.28           C  
ANISOU 1702  CA  ARG A 242     4941   3996   4469    360    -10   -883       C  
ATOM   1703  C   ARG A 242      35.055  27.700  17.397  1.00 36.44           C  
ANISOU 1703  C   ARG A 242     5061   4196   4589    317    -31   -854       C  
ATOM   1704  O   ARG A 242      34.513  26.600  17.473  1.00 35.35           O  
ANISOU 1704  O   ARG A 242     4895   4131   4404    334    -19   -825       O  
ATOM   1705  CB  ARG A 242      34.192  29.454  18.938  1.00 38.77           C  
ANISOU 1705  CB  ARG A 242     5406   4457   4866    376    -17   -949       C  
ATOM   1706  CG  ARG A 242      33.725  28.401  19.925  1.00 44.48           C  
ANISOU 1706  CG  ARG A 242     6110   5282   5507    397     -9   -950       C  
ATOM   1707  CD  ARG A 242      33.824  28.884  21.360  1.00 44.34           C  
ANISOU 1707  CD  ARG A 242     6120   5283   5443    411    -20  -1016       C  
ATOM   1708  NE  ARG A 242      33.088  28.007  22.263  1.00 41.74           N  
ANISOU 1708  NE  ARG A 242     5775   5049   5035    445      0  -1010       N  
ATOM   1709  CZ  ARG A 242      32.908  28.246  23.557  1.00 43.38           C  
ANISOU 1709  CZ  ARG A 242     6004   5293   5187    469      1  -1059       C  
ATOM   1710  NH1 ARG A 242      33.422  29.337  24.116  1.00 48.96           N  
ANISOU 1710  NH1 ARG A 242     6748   5948   5908    464    -22  -1123       N  
ATOM   1711  NH2 ARG A 242      32.214  27.389  24.292  1.00 38.18           N  
ANISOU 1711  NH2 ARG A 242     5329   4721   4459    499     24  -1044       N  
ATOM   1712  N   ALA A 243      36.362  27.843  17.247  1.00 30.58           N  
ANISOU 1712  N   ALA A 243     4324   3416   3878    263    -64   -862       N  
ATOM   1713  CA  ALA A 243      37.198  26.684  16.997  1.00 26.86           C  
ANISOU 1713  CA  ALA A 243     3825   2986   3393    223    -84   -830       C  
ATOM   1714  C   ALA A 243      38.590  26.771  17.615  1.00 32.49           C  
ANISOU 1714  C   ALA A 243     4542   3693   4110    173   -126   -862       C  
ATOM   1715  O   ALA A 243      39.143  27.852  17.808  1.00 35.56           O  
ANISOU 1715  O   ALA A 243     4953   4019   4537    154   -142   -899       O  
ATOM   1716  CB  ALA A 243      37.310  26.445  15.492  1.00 22.66           C  
ANISOU 1716  CB  ALA A 243     3278   2418   2913    207    -73   -774       C  
ATOM   1717  N   ALA A 244      39.142  25.605  17.923  1.00 31.58           N  
ANISOU 1717  N   ALA A 244     4402   3642   3957    153   -144   -846       N  
ATOM   1718  CA  ALA A 244      40.532  25.475  18.320  1.00 29.12           C  
ANISOU 1718  CA  ALA A 244     4080   3330   3652    104   -186   -864       C  
ATOM   1719  C   ALA A 244      41.289  24.919  17.116  1.00 32.32           C  
ANISOU 1719  C   ALA A 244     4458   3716   4106     64   -190   -814       C  
ATOM   1720  O   ALA A 244      41.181  23.734  16.788  1.00 34.65           O  
ANISOU 1720  O   ALA A 244     4728   4062   4375     67   -183   -775       O  
ATOM   1721  CB  ALA A 244      40.666  24.552  19.520  1.00 28.69           C  
ANISOU 1721  CB  ALA A 244     4016   3362   3521    113   -204   -877       C  
ATOM   1722  N   VAL A 245      42.050  25.798  16.469  1.00 27.96           N  
ANISOU 1722  N   VAL A 245     3910   3088   3625     27   -200   -816       N  
ATOM   1723  CA  VAL A 245      42.728  25.516  15.214  1.00 17.73           C  
ANISOU 1723  CA  VAL A 245     2592   1760   2385    -10   -196   -768       C  
ATOM   1724  C   VAL A 245      44.177  25.117  15.441  1.00 32.25           C  
ANISOU 1724  C   VAL A 245     4401   3613   4239    -63   -233   -772       C  
ATOM   1725  O   VAL A 245      44.937  25.842  16.101  1.00 39.27           O  
ANISOU 1725  O   VAL A 245     5295   4478   5146    -89   -263   -813       O  
ATOM   1726  CB  VAL A 245      42.702  26.759  14.330  1.00 20.49           C  
ANISOU 1726  CB  VAL A 245     2964   2016   2807    -20   -180   -759       C  
ATOM   1727  CG1 VAL A 245      43.230  26.447  12.962  1.00 22.37           C  
ANISOU 1727  CG1 VAL A 245     3180   2223   3096    -50   -167   -700       C  
ATOM   1728  CG2 VAL A 245      41.277  27.296  14.242  1.00 23.48           C  
ANISOU 1728  CG2 VAL A 245     3372   2378   3172     37   -146   -761       C  
ATOM   1729  N   SER A 246      44.550  23.960  14.899  1.00 30.93           N  
ANISOU 1729  N   SER A 246     4201   3485   4067    -76   -233   -730       N  
ATOM   1730  CA  SER A 246      45.912  23.447  14.989  1.00 28.08           C  
ANISOU 1730  CA  SER A 246     3804   3143   3724   -122   -264   -726       C  
ATOM   1731  C   SER A 246      46.532  23.470  13.599  1.00 23.80           C  
ANISOU 1731  C   SER A 246     3238   2553   3252   -158   -248   -678       C  
ATOM   1732  O   SER A 246      46.046  22.813  12.688  1.00 24.61           O  
ANISOU 1732  O   SER A 246     3334   2663   3354   -144   -220   -635       O  
ATOM   1733  CB  SER A 246      45.919  22.018  15.557  1.00 27.20           C  
ANISOU 1733  CB  SER A 246     3670   3118   3546   -106   -276   -715       C  
ATOM   1734  OG  SER A 246      47.234  21.465  15.570  1.00 33.07           O  
ANISOU 1734  OG  SER A 246     4375   3881   4310   -146   -306   -707       O  
ATOM   1735  N   ARG A 247      47.586  24.254  13.424  1.00 23.00           N  
ANISOU 1735  N   ARG A 247     3124   2401   3212   -204   -263   -685       N  
ATOM   1736  CA  ARG A 247      48.226  24.364  12.117  1.00 24.32           C  
ANISOU 1736  CA  ARG A 247     3270   2523   3449   -240   -241   -635       C  
ATOM   1737  C   ARG A 247      49.741  24.270  12.235  1.00 28.24           C  
ANISOU 1737  C   ARG A 247     3720   3024   3985   -294   -269   -637       C  
ATOM   1738  O   ARG A 247      50.317  24.620  13.263  1.00 31.17           O  
ANISOU 1738  O   ARG A 247     4088   3407   4350   -309   -307   -683       O  
ATOM   1739  CB  ARG A 247      47.833  25.671  11.422  1.00 21.87           C  
ANISOU 1739  CB  ARG A 247     2993   2127   3191   -241   -215   -625       C  
ATOM   1740  CG  ARG A 247      46.335  25.960  11.448  1.00 25.93           C  
ANISOU 1740  CG  ARG A 247     3551   2632   3667   -184   -192   -631       C  
ATOM   1741  CD  ARG A 247      45.929  27.038  10.461  1.00 32.24           C  
ANISOU 1741  CD  ARG A 247     4380   3350   4521   -179   -161   -601       C  
ATOM   1742  NE  ARG A 247      46.266  28.376  10.927  1.00 33.18           N  
ANISOU 1742  NE  ARG A 247     4524   3406   4678   -199   -175   -638       N  
ATOM   1743  CZ  ARG A 247      45.906  29.498  10.306  1.00 38.61           C  
ANISOU 1743  CZ  ARG A 247     5244   4015   5410   -192   -153   -621       C  
ATOM   1744  NH1 ARG A 247      45.187  29.447   9.192  1.00 29.11           N  
ANISOU 1744  NH1 ARG A 247     4054   2791   4216   -164   -117   -566       N  
ATOM   1745  NH2 ARG A 247      46.261  30.680  10.805  1.00 42.32           N  
ANISOU 1745  NH2 ARG A 247     5737   4427   5916   -213   -168   -660       N  
ATOM   1746  N   GLY A 248      50.387  23.796  11.180  1.00 25.22           N  
ANISOU 1746  N   GLY A 248     3301   2636   3644   -321   -249   -585       N  
ATOM   1747  CA  GLY A 248      51.825  23.670  11.200  1.00 26.85           C  
ANISOU 1747  CA  GLY A 248     3458   2851   3894   -369   -269   -581       C  
ATOM   1748  C   GLY A 248      52.388  22.978   9.984  1.00 36.21           C  
ANISOU 1748  C   GLY A 248     4602   4040   5116   -389   -237   -519       C  
ATOM   1749  O   GLY A 248      51.748  22.890   8.932  1.00 41.23           O  
ANISOU 1749  O   GLY A 248     5253   4651   5759   -373   -194   -475       O  
ATOM   1750  N   ARG A 249      53.604  22.475  10.148  1.00 33.68           N  
ANISOU 1750  N   ARG A 249     4228   3752   4816   -421   -257   -515       N  
ATOM   1751  CA  ARG A 249      54.346  21.843   9.076  1.00 33.90           C  
ANISOU 1751  CA  ARG A 249     4210   3788   4883   -443   -226   -459       C  
ATOM   1752  C   ARG A 249      55.396  20.928   9.688  1.00 32.22           C  
ANISOU 1752  C   ARG A 249     3942   3638   4662   -456   -261   -470       C  
ATOM   1753  O   ARG A 249      55.653  20.990  10.890  1.00 31.01           O  
ANISOU 1753  O   ARG A 249     3788   3513   4481   -455   -310   -519       O  
ATOM   1754  CB  ARG A 249      55.031  22.904   8.228  1.00 41.55           C  
ANISOU 1754  CB  ARG A 249     5166   4692   5929   -485   -197   -428       C  
ATOM   1755  CG  ARG A 249      55.775  23.946   9.039  1.00 50.98           C  
ANISOU 1755  CG  ARG A 249     6353   5858   7158   -522   -235   -472       C  
ATOM   1756  CD  ARG A 249      56.731  24.744   8.172  1.00 61.23           C  
ANISOU 1756  CD  ARG A 249     7622   7106   8537   -571   -207   -433       C  
ATOM   1757  NE  ARG A 249      56.294  24.783   6.781  1.00 67.90           N  
ANISOU 1757  NE  ARG A 249     8481   7919   9400   -562   -145   -365       N  
ATOM   1758  CZ  ARG A 249      55.332  25.577   6.324  1.00 66.46           C  
ANISOU 1758  CZ  ARG A 249     8354   7681   9218   -543   -120   -352       C  
ATOM   1759  NH1 ARG A 249      54.699  26.393   7.160  1.00 76.50           N  
ANISOU 1759  NH1 ARG A 249     9671   8921  10476   -531   -149   -404       N  
ATOM   1760  NH2 ARG A 249      54.999  25.544   5.038  1.00 49.79           N  
ANISOU 1760  NH2 ARG A 249     6253   5548   7117   -532    -64   -286       N  
ATOM   1761  N   LEU A 250      56.000  20.075   8.867  1.00 29.94           N  
ANISOU 1761  N   LEU A 250     3609   3374   4395   -464   -235   -424       N  
ATOM   1762  CA  LEU A 250      57.051  19.198   9.359  1.00 24.86           C  
ANISOU 1762  CA  LEU A 250     2908   2789   3749   -473   -266   -429       C  
ATOM   1763  C   LEU A 250      58.257  20.023   9.787  1.00 31.89           C  
ANISOU 1763  C   LEU A 250     3762   3664   4691   -518   -294   -449       C  
ATOM   1764  O   LEU A 250      58.654  20.974   9.106  1.00 28.86           O  
ANISOU 1764  O   LEU A 250     3372   3226   4368   -552   -267   -429       O  
ATOM   1765  CB  LEU A 250      57.437  18.153   8.306  1.00 24.63           C  
ANISOU 1765  CB  LEU A 250     2838   2785   3737   -469   -225   -374       C  
ATOM   1766  CG  LEU A 250      56.384  17.042   8.131  1.00 32.12           C  
ANISOU 1766  CG  LEU A 250     3813   3764   4628   -425   -212   -364       C  
ATOM   1767  CD1 LEU A 250      56.713  16.130   6.958  1.00 33.76           C  
ANISOU 1767  CD1 LEU A 250     3988   3989   4849   -419   -163   -306       C  
ATOM   1768  CD2 LEU A 250      56.232  16.224   9.404  1.00 33.17           C  
ANISOU 1768  CD2 LEU A 250     3947   3957   4697   -397   -266   -403       C  
ATOM   1769  N   ALA A 251      58.821  19.667  10.934  1.00 35.41           N  
ANISOU 1769  N   ALA A 251     4185   4158   5110   -516   -350   -488       N  
ATOM   1770  CA  ALA A 251      59.993  20.357  11.452  1.00 38.83           C  
ANISOU 1770  CA  ALA A 251     4580   4584   5589   -559   -385   -513       C  
ATOM   1771  C   ALA A 251      61.277  19.890  10.761  1.00 42.47           C  
ANISOU 1771  C   ALA A 251     4966   5066   6106   -586   -368   -471       C  
ATOM   1772  O   ALA A 251      61.431  18.707  10.427  1.00 36.45           O  
ANISOU 1772  O   ALA A 251     4174   4351   5326   -563   -355   -440       O  
ATOM   1773  CB  ALA A 251      60.094  20.161  12.956  1.00 33.60           C  
ANISOU 1773  CB  ALA A 251     3925   3969   4872   -544   -452   -569       C  
ATOM   1774  N   THR A 252      62.187  20.834  10.537  1.00 42.53           N  
ANISOU 1774  N   THR A 252     4942   5036   6182   -636   -366   -470       N  
ATOM   1775  CA  THR A 252      63.552  20.514  10.134  1.00 45.49           C  
ANISOU 1775  CA  THR A 252     5238   5437   6610   -665   -359   -440       C  
ATOM   1776  C   THR A 252      64.333  20.219  11.402  1.00 40.26           C  
ANISOU 1776  C   THR A 252     4541   4827   5930   -669   -431   -486       C  
ATOM   1777  O   THR A 252      63.886  20.549  12.502  1.00 38.27           O  
ANISOU 1777  O   THR A 252     4328   4577   5634   -659   -480   -540       O  
ATOM   1778  CB  THR A 252      64.215  21.682   9.402  1.00 44.00           C  
ANISOU 1778  CB  THR A 252     5028   5187   6502   -719   -327   -419       C  
ATOM   1779  OG1 THR A 252      64.105  22.859  10.206  1.00 43.44           O  
ANISOU 1779  OG1 THR A 252     4989   5072   6443   -746   -367   -472       O  
ATOM   1780  CG2 THR A 252      63.537  21.925   8.060  1.00 36.75           C  
ANISOU 1780  CG2 THR A 252     4142   4222   5600   -712   -253   -363       C  
ATOM   1781  N   VAL A 253      65.489  19.589  11.267  1.00 35.25           N  
ANISOU 1781  N   VAL A 253     3833   4237   5324   -680   -436   -464       N  
ATOM   1782  CA  VAL A 253      66.210  19.168  12.462  1.00 40.95           C  
ANISOU 1782  CA  VAL A 253     4520   5017   6023   -676   -506   -502       C  
ATOM   1783  C   VAL A 253      66.741  20.351  13.307  1.00 41.25           C  
ANISOU 1783  C   VAL A 253     4556   5029   6090   -722   -557   -557       C  
ATOM   1784  O   VAL A 253      66.737  20.277  14.540  1.00 32.52           O  
ANISOU 1784  O   VAL A 253     3462   3956   4936   -709   -621   -606       O  
ATOM   1785  CB  VAL A 253      67.271  18.077  12.155  1.00 52.20           C  
ANISOU 1785  CB  VAL A 253     5867   6503   7466   -667   -502   -464       C  
ATOM   1786  CG1 VAL A 253      67.711  18.152  10.700  1.00 50.29           C  
ANISOU 1786  CG1 VAL A 253     5586   6234   7287   -688   -427   -405       C  
ATOM   1787  CG2 VAL A 253      68.451  18.168  13.128  1.00 52.76           C  
ANISOU 1787  CG2 VAL A 253     5880   6613   7552   -690   -568   -498       C  
ATOM   1788  N   GLU A 254      67.118  21.451  12.647  1.00 47.30           N  
ANISOU 1788  N   GLU A 254     5310   5732   6930   -772   -527   -547       N  
ATOM   1789  CA  GLU A 254      67.534  22.681  13.337  1.00 53.95           C  
ANISOU 1789  CA  GLU A 254     6154   6535   7809   -820   -571   -599       C  
ATOM   1790  C   GLU A 254      66.432  23.259  14.223  1.00 57.64           C  
ANISOU 1790  C   GLU A 254     6705   6976   8220   -799   -602   -656       C  
ATOM   1791  O   GLU A 254      66.715  24.029  15.144  1.00 55.64           O  
ANISOU 1791  O   GLU A 254     6459   6710   7973   -824   -655   -713       O  
ATOM   1792  CB  GLU A 254      67.974  23.753  12.335  1.00 52.49           C  
ANISOU 1792  CB  GLU A 254     5951   6278   7713   -875   -523   -569       C  
ATOM   1793  N   GLN A 255      65.182  22.896  13.932  1.00 51.83           N  
ANISOU 1793  N   GLN A 255     6030   6233   7432   -753   -569   -640       N  
ATOM   1794  CA  GLN A 255      64.033  23.374  14.704  1.00 47.94           C  
ANISOU 1794  CA  GLN A 255     5616   5719   6880   -725   -590   -689       C  
ATOM   1795  C   GLN A 255      63.742  22.497  15.918  1.00 44.47           C  
ANISOU 1795  C   GLN A 255     5191   5353   6351   -679   -642   -724       C  
ATOM   1796  O   GLN A 255      62.928  22.855  16.765  1.00 40.52           O  
ANISOU 1796  O   GLN A 255     4750   4848   5796   -655   -666   -770       O  
ATOM   1797  CB  GLN A 255      62.785  23.464  13.821  1.00 47.79           C  
ANISOU 1797  CB  GLN A 255     5653   5657   6847   -697   -528   -655       C  
ATOM   1798  CG  GLN A 255      62.895  24.466  12.684  1.00 55.05           C  
ANISOU 1798  CG  GLN A 255     6573   6498   7845   -737   -476   -620       C  
ATOM   1799  CD  GLN A 255      61.691  24.435  11.763  1.00 54.62           C  
ANISOU 1799  CD  GLN A 255     6571   6409   7772   -705   -417   -581       C  
ATOM   1800  OE1 GLN A 255      61.193  23.365  11.418  1.00 59.21           O  
ANISOU 1800  OE1 GLN A 255     7155   7032   8310   -665   -396   -550       O  
ATOM   1801  NE2 GLN A 255      61.208  25.611  11.373  1.00 48.98           N  
ANISOU 1801  NE2 GLN A 255     5899   5618   7092   -720   -393   -581       N  
ATOM   1802  N   LEU A 256      64.404  21.347  16.001  1.00 44.70           N  
ANISOU 1802  N   LEU A 256     5168   5450   6364   -664   -656   -699       N  
ATOM   1803  CA  LEU A 256      64.159  20.423  17.103  1.00 50.92           C  
ANISOU 1803  CA  LEU A 256     5971   6311   7067   -617   -702   -721       C  
ATOM   1804  C   LEU A 256      64.853  20.888  18.378  1.00 63.03           C  
ANISOU 1804  C   LEU A 256     7493   7868   8587   -635   -776   -781       C  
ATOM   1805  O   LEU A 256      65.963  21.426  18.322  1.00 64.62           O  
ANISOU 1805  O   LEU A 256     7640   8057   8855   -685   -797   -790       O  
ATOM   1806  CB  LEU A 256      64.615  19.000  16.747  1.00 43.24           C  
ANISOU 1806  CB  LEU A 256     4948   5400   6081   -590   -693   -671       C  
ATOM   1807  CG  LEU A 256      63.812  18.218  15.701  1.00 44.07           C  
ANISOU 1807  CG  LEU A 256     5071   5501   6174   -558   -631   -617       C  
ATOM   1808  CD1 LEU A 256      64.349  16.800  15.563  1.00 41.37           C  
ANISOU 1808  CD1 LEU A 256     4678   5223   5816   -529   -633   -577       C  
ATOM   1809  CD2 LEU A 256      62.325  18.201  16.039  1.00 41.77           C  
ANISOU 1809  CD2 LEU A 256     4860   5201   5812   -518   -620   -634       C  
ATOM   1810  N   PRO A 257      64.197  20.681  19.534  1.00 66.86           N  
ANISOU 1810  N   PRO A 257     8027   8389   8986   -595   -814   -820       N  
ATOM   1811  CA  PRO A 257      64.852  20.911  20.825  1.00 67.56           C  
ANISOU 1811  CA  PRO A 257     8106   8516   9047   -603   -888   -875       C  
ATOM   1812  C   PRO A 257      66.100  20.047  20.911  1.00 71.39           C  
ANISOU 1812  C   PRO A 257     8513   9063   9550   -610   -920   -849       C  
ATOM   1813  O   PRO A 257      66.116  18.957  20.331  1.00 70.09           O  
ANISOU 1813  O   PRO A 257     8322   8930   9377   -583   -891   -794       O  
ATOM   1814  CB  PRO A 257      63.809  20.438  21.843  1.00 68.24           C  
ANISOU 1814  CB  PRO A 257     8259   8646   9025   -543   -905   -898       C  
ATOM   1815  CG  PRO A 257      62.872  19.561  21.072  1.00 69.92           C  
ANISOU 1815  CG  PRO A 257     8494   8863   9210   -503   -846   -843       C  
ATOM   1816  CD  PRO A 257      62.838  20.137  19.690  1.00 68.14           C  
ANISOU 1816  CD  PRO A 257     8255   8566   9069   -539   -788   -812       C  
ATOM   1817  N   ALA A 258      67.120  20.536  21.610  1.00 70.51           N  
ANISOU 1817  N   ALA A 258     8363   8966   9464   -645   -979   -889       N  
ATOM   1818  CA  ALA A 258      68.433  19.898  21.637  1.00 66.99           C  
ANISOU 1818  CA  ALA A 258     7832   8572   9049   -659  -1012   -867       C  
ATOM   1819  C   ALA A 258      68.380  18.388  21.873  1.00 60.65           C  
ANISOU 1819  C   ALA A 258     7018   7846   8181   -600  -1018   -824       C  
ATOM   1820  O   ALA A 258      69.004  17.625  21.135  1.00 60.72           O  
ANISOU 1820  O   ALA A 258     6967   7878   8228   -599   -994   -772       O  
ATOM   1821  CB  ALA A 258      69.325  20.572  22.668  1.00 67.42           C  
ANISOU 1821  CB  ALA A 258     7861   8643   9114   -694  -1089   -927       C  
ATOM   1822  N   LYS A 259      67.622  17.971  22.886  1.00 55.10           N  
ANISOU 1822  N   LYS A 259     6373   7182   7380   -551  -1046   -845       N  
ATOM   1823  CA  LYS A 259      67.526  16.564  23.271  1.00 55.82           C  
ANISOU 1823  CA  LYS A 259     6461   7345   7402   -493  -1057   -805       C  
ATOM   1824  C   LYS A 259      67.116  15.644  22.117  1.00 68.29           C  
ANISOU 1824  C   LYS A 259     8032   8919   8997   -468   -990   -738       C  
ATOM   1825  O   LYS A 259      67.600  14.516  22.005  1.00 73.07           O  
ANISOU 1825  O   LYS A 259     8596   9573   9594   -440   -994   -693       O  
ATOM   1826  CB  LYS A 259      66.537  16.406  24.429  1.00 51.19           C  
ANISOU 1826  CB  LYS A 259     5952   6789   6708   -445  -1080   -835       C  
ATOM   1827  N   LEU A 260      66.235  16.146  21.256  1.00 64.71           N  
ANISOU 1827  N   LEU A 260     7617   8402   8566   -478   -930   -732       N  
ATOM   1828  CA  LEU A 260      65.599  15.335  20.222  1.00 52.53           C  
ANISOU 1828  CA  LEU A 260     6082   6851   7026   -451   -867   -676       C  
ATOM   1829  C   LEU A 260      66.381  15.284  18.915  1.00 50.88           C  
ANISOU 1829  C   LEU A 260     5807   6617   6909   -484   -825   -634       C  
ATOM   1830  O   LEU A 260      66.060  14.486  18.031  1.00 51.02           O  
ANISOU 1830  O   LEU A 260     5819   6636   6932   -461   -776   -586       O  
ATOM   1831  CB  LEU A 260      64.185  15.855  19.955  1.00 51.21           C  
ANISOU 1831  CB  LEU A 260     5991   6635   6831   -441   -824   -688       C  
ATOM   1832  CG  LEU A 260      63.033  15.197  20.714  1.00 61.80           C  
ANISOU 1832  CG  LEU A 260     7397   8011   8071   -383   -828   -690       C  
ATOM   1833  CD1 LEU A 260      63.473  14.719  22.093  1.00 69.09           C  
ANISOU 1833  CD1 LEU A 260     8319   9003   8928   -357   -893   -710       C  
ATOM   1834  CD2 LEU A 260      61.862  16.162  20.831  1.00 59.44           C  
ANISOU 1834  CD2 LEU A 260     7170   7664   7750   -383   -805   -726       C  
ATOM   1835  N   ARG A 261      67.399  16.132  18.789  1.00 45.83           N  
ANISOU 1835  N   ARG A 261     5117   5957   6341   -538   -841   -653       N  
ATOM   1836  CA  ARG A 261      68.213  16.184  17.573  1.00 52.80           C  
ANISOU 1836  CA  ARG A 261     5934   6816   7312   -572   -796   -612       C  
ATOM   1837  C   ARG A 261      69.029  14.906  17.372  1.00 53.93           C  
ANISOU 1837  C   ARG A 261     6010   7022   7458   -543   -799   -566       C  
ATOM   1838  O   ARG A 261      69.618  14.691  16.311  1.00 52.05           O  
ANISOU 1838  O   ARG A 261     5718   6775   7282   -558   -752   -524       O  
ATOM   1839  CB  ARG A 261      69.166  17.381  17.604  1.00 58.33           C  
ANISOU 1839  CB  ARG A 261     6593   7484   8087   -637   -817   -642       C  
ATOM   1840  CG  ARG A 261      68.542  18.743  17.349  1.00 59.93           C  
ANISOU 1840  CG  ARG A 261     6846   7606   8318   -675   -794   -672       C  
ATOM   1841  CD  ARG A 261      69.639  19.726  16.964  1.00 61.75           C  
ANISOU 1841  CD  ARG A 261     7018   7800   8644   -743   -795   -679       C  
ATOM   1842  NE  ARG A 261      69.158  21.079  16.708  1.00 67.31           N  
ANISOU 1842  NE  ARG A 261     7767   8422   9386   -782   -775   -705       N  
ATOM   1843  CZ  ARG A 261      69.116  22.040  17.626  1.00 74.71           C  
ANISOU 1843  CZ  ARG A 261     8734   9335  10317   -805   -825   -769       C  
ATOM   1844  NH1 ARG A 261      69.512  21.794  18.870  1.00 74.61           N  
ANISOU 1844  NH1 ARG A 261     8713   9378  10259   -794   -899   -814       N  
ATOM   1845  NH2 ARG A 261      68.673  23.247  17.302  1.00 76.04           N  
ANISOU 1845  NH2 ARG A 261     8943   9424  10525   -838   -802   -787       N  
ATOM   1846  N   SER A 262      69.070  14.074  18.408  1.00 57.35           N  
ANISOU 1846  N   SER A 262     6449   7518   7823   -501   -851   -573       N  
ATOM   1847  CA  SER A 262      69.779  12.800  18.381  1.00 60.90           C  
ANISOU 1847  CA  SER A 262     6843   8028   8267   -464   -860   -530       C  
ATOM   1848  C   SER A 262      69.158  11.802  17.399  1.00 58.96           C  
ANISOU 1848  C   SER A 262     6610   7779   8015   -424   -798   -477       C  
ATOM   1849  O   SER A 262      69.830  11.323  16.486  1.00 52.97           O  
ANISOU 1849  O   SER A 262     5791   7026   7309   -424   -760   -436       O  
ATOM   1850  CB  SER A 262      69.811  12.204  19.789  1.00 65.73           C  
ANISOU 1850  CB  SER A 262     7473   8704   8799   -424   -931   -548       C  
ATOM   1851  OG  SER A 262      70.239  10.855  19.764  1.00 71.03           O  
ANISOU 1851  OG  SER A 262     8106   9429   9453   -376   -935   -499       O  
ATOM   1852  N   GLU A 263      67.883  11.475  17.605  1.00 60.58           N  
ANISOU 1852  N   GLU A 263     6889   7976   8153   -389   -786   -479       N  
ATOM   1853  CA  GLU A 263      67.122  10.690  16.628  1.00 61.24           C  
ANISOU 1853  CA  GLU A 263     6993   8045   8232   -358   -725   -436       C  
ATOM   1854  C   GLU A 263      65.919  11.491  16.120  1.00 46.78           C  
ANISOU 1854  C   GLU A 263     5226   6151   6397   -375   -683   -453       C  
ATOM   1855  O   GLU A 263      64.806  11.392  16.644  1.00 40.13           O  
ANISOU 1855  O   GLU A 263     4452   5310   5488   -348   -689   -468       O  
ATOM   1856  CB  GLU A 263      66.710   9.327  17.192  1.00 68.00           C  
ANISOU 1856  CB  GLU A 263     7870   8951   9016   -293   -744   -411       C  
ATOM   1857  CG  GLU A 263      66.314   9.353  18.654  1.00 79.73           C  
ANISOU 1857  CG  GLU A 263     9403  10470  10419   -272   -804   -442       C  
ATOM   1858  CD  GLU A 263      66.016   7.971  19.204  1.00 85.42           C  
ANISOU 1858  CD  GLU A 263    10142  11242  11073   -209   -820   -407       C  
ATOM   1859  OE1 GLU A 263      65.434   7.142  18.466  1.00 85.59           O  
ANISOU 1859  OE1 GLU A 263    10175  11254  11091   -179   -776   -369       O  
ATOM   1860  OE2 GLU A 263      66.368   7.717  20.376  1.00 85.41           O  
ANISOU 1860  OE2 GLU A 263    10142  11287  11021   -188   -877   -415       O  
ATOM   1861  N   PRO A 264      66.155  12.307  15.091  1.00 36.40           N  
ANISOU 1861  N   PRO A 264     3892   4785   5155   -419   -638   -446       N  
ATOM   1862  CA  PRO A 264      65.127  13.222  14.605  1.00 36.08           C  
ANISOU 1862  CA  PRO A 264     3909   4681   5118   -439   -600   -460       C  
ATOM   1863  C   PRO A 264      63.999  12.497  13.868  1.00 37.12           C  
ANISOU 1863  C   PRO A 264     4082   4803   5221   -403   -551   -429       C  
ATOM   1864  O   PRO A 264      62.920  13.065  13.732  1.00 41.58           O  
ANISOU 1864  O   PRO A 264     4706   5327   5765   -405   -531   -444       O  
ATOM   1865  CB  PRO A 264      65.905  14.137  13.656  1.00 35.86           C  
ANISOU 1865  CB  PRO A 264     3838   4608   5180   -493   -564   -448       C  
ATOM   1866  CG  PRO A 264      67.026  13.285  13.155  1.00 36.52           C  
ANISOU 1866  CG  PRO A 264     3843   4731   5301   -486   -551   -408       C  
ATOM   1867  CD  PRO A 264      67.395  12.380  14.296  1.00 35.92           C  
ANISOU 1867  CD  PRO A 264     3751   4723   5173   -449   -614   -419       C  
ATOM   1868  N   LEU A 265      64.247  11.273  13.411  1.00 33.27           N  
ANISOU 1868  N   LEU A 265     3561   4349   4732   -371   -534   -389       N  
ATOM   1869  CA  LEU A 265      63.255  10.510  12.663  1.00 31.50           C  
ANISOU 1869  CA  LEU A 265     3368   4115   4485   -338   -489   -360       C  
ATOM   1870  C   LEU A 265      62.626   9.415  13.521  1.00 38.05           C  
ANISOU 1870  C   LEU A 265     4230   4992   5236   -285   -523   -360       C  
ATOM   1871  O   LEU A 265      62.148   8.407  13.001  1.00 42.15           O  
ANISOU 1871  O   LEU A 265     4755   5521   5741   -251   -497   -330       O  
ATOM   1872  CB  LEU A 265      63.882   9.911  11.400  1.00 24.81           C  
ANISOU 1872  CB  LEU A 265     2466   3265   3694   -336   -435   -312       C  
ATOM   1873  CG  LEU A 265      64.321  10.952  10.362  1.00 26.34           C  
ANISOU 1873  CG  LEU A 265     2638   3411   3961   -385   -385   -300       C  
ATOM   1874  CD1 LEU A 265      65.355  10.386   9.398  1.00 16.32           C  
ANISOU 1874  CD1 LEU A 265     1299   2157   2744   -383   -341   -255       C  
ATOM   1875  CD2 LEU A 265      63.118  11.473   9.593  1.00 26.91           C  
ANISOU 1875  CD2 LEU A 265     2769   3429   4028   -393   -337   -295       C  
ATOM   1876  N   LYS A 266      62.617   9.630  14.835  1.00 38.00           N  
ANISOU 1876  N   LYS A 266     4247   5015   5178   -278   -579   -393       N  
ATOM   1877  CA  LYS A 266      62.100   8.646  15.782  1.00 39.44           C  
ANISOU 1877  CA  LYS A 266     4461   5245   5279   -227   -612   -387       C  
ATOM   1878  C   LYS A 266      60.630   8.313  15.538  1.00 38.53           C  
ANISOU 1878  C   LYS A 266     4410   5116   5116   -201   -580   -381       C  
ATOM   1879  O   LYS A 266      59.828   9.192  15.248  1.00 32.63           O  
ANISOU 1879  O   LYS A 266     3703   4326   4370   -222   -556   -404       O  
ATOM   1880  CB  LYS A 266      62.266   9.137  17.222  1.00 40.10           C  
ANISOU 1880  CB  LYS A 266     4567   5358   5313   -228   -670   -426       C  
ATOM   1881  CG  LYS A 266      62.086   8.028  18.252  1.00 47.23           C  
ANISOU 1881  CG  LYS A 266     5489   6319   6137   -175   -706   -408       C  
ATOM   1882  CD  LYS A 266      61.485   8.539  19.554  1.00 51.85           C  
ANISOU 1882  CD  LYS A 266     6132   6922   6646   -166   -740   -445       C  
ATOM   1883  CE  LYS A 266      61.376   7.420  20.593  1.00 51.03           C  
ANISOU 1883  CE  LYS A 266     6047   6878   6463   -113   -772   -419       C  
ATOM   1884  N   PHE A 267      60.279   7.042  15.692  1.00 42.19           N  
ANISOU 1884  N   PHE A 267     4882   5614   5535   -154   -582   -349       N  
ATOM   1885  CA  PHE A 267      58.931   6.577  15.390  1.00 44.90           C  
ANISOU 1885  CA  PHE A 267     5289   5943   5829   -129   -538   -326       C  
ATOM   1886  C   PHE A 267      57.929   6.757  16.547  1.00 58.21           C  
ANISOU 1886  C   PHE A 267     7035   7652   7432   -109   -565   -353       C  
ATOM   1887  O   PHE A 267      58.243   6.453  17.703  1.00 53.69           O  
ANISOU 1887  O   PHE A 267     6463   7125   6810    -87   -612   -359       O  
ATOM   1888  CB  PHE A 267      58.971   5.119  14.894  1.00 42.20           C  
ANISOU 1888  CB  PHE A 267     4942   5612   5479    -89   -505   -265       C  
ATOM   1889  CG  PHE A 267      57.605   4.494  14.707  1.00 50.43           C  
ANISOU 1889  CG  PHE A 267     6051   6643   6468    -63   -461   -235       C  
ATOM   1890  CD1 PHE A 267      56.677   5.051  13.828  1.00 48.98           C  
ANISOU 1890  CD1 PHE A 267     5902   6414   6294    -81   -410   -237       C  
ATOM   1891  CD2 PHE A 267      57.251   3.338  15.404  1.00 51.61           C  
ANISOU 1891  CD2 PHE A 267     6224   6825   6561    -20   -472   -203       C  
ATOM   1892  CE1 PHE A 267      55.419   4.474  13.658  1.00 47.01           C  
ANISOU 1892  CE1 PHE A 267     5706   6156   6000    -60   -373   -212       C  
ATOM   1893  CE2 PHE A 267      55.992   2.750  15.237  1.00 46.81           C  
ANISOU 1893  CE2 PHE A 267     5670   6203   5912     -1   -431   -174       C  
ATOM   1894  CZ  PHE A 267      55.079   3.319  14.363  1.00 46.22           C  
ANISOU 1894  CZ  PHE A 267     5625   6087   5849    -22   -383   -181       C  
ATOM   1895  N   ASP A 268      56.746   7.281  16.194  1.00 71.02           N  
ANISOU 1895  N   ASP A 268     8709   9239   9036   -116   -523   -360       N  
ATOM   1896  CA  ASP A 268      55.534   7.377  17.039  1.00 73.56           C  
ANISOU 1896  CA  ASP A 268     9093   9577   9280    -92   -525   -375       C  
ATOM   1897  C   ASP A 268      55.393   8.692  17.820  1.00 76.05           C  
ANISOU 1897  C   ASP A 268     9431   9884   9581   -112   -552   -435       C  
ATOM   1898  O   ASP A 268      54.295   9.259  17.914  1.00 74.23           O  
ANISOU 1898  O   ASP A 268     9248   9635   9320   -107   -528   -454       O  
ATOM   1899  CB  ASP A 268      55.342   6.150  17.957  1.00 65.89           C  
ANISOU 1899  CB  ASP A 268     8137   8662   8236    -46   -543   -341       C  
ATOM   1900  N   ARG A 298      41.156  27.059  28.005  1.00 86.50           N  
ANISOU 1900  N   ARG A 298    11495  10857  10516    218   -337  -1243       N  
ATOM   1901  CA  ARG A 298      40.020  27.571  27.246  1.00 89.74           C  
ANISOU 1901  CA  ARG A 298    11913  11223  10961    246   -285  -1228       C  
ATOM   1902  C   ARG A 298      40.469  28.417  26.052  1.00 88.35           C  
ANISOU 1902  C   ARG A 298    11735  10948  10886    207   -290  -1225       C  
ATOM   1903  O   ARG A 298      40.050  28.170  24.919  1.00 83.67           O  
ANISOU 1903  O   ARG A 298    11124  10331  10335    205   -259  -1172       O  
ATOM   1904  CB  ARG A 298      39.095  28.388  28.154  1.00 90.56           C  
ANISOU 1904  CB  ARG A 298    12055  11330  11023    297   -263  -1285       C  
ATOM   1905  N   LYS A 299      41.314  29.414  26.317  1.00 89.08           N  
ANISOU 1905  N   LYS A 299    11847  10984  11017    175   -329  -1282       N  
ATOM   1906  CA  LYS A 299      41.795  30.335  25.284  1.00 86.06           C  
ANISOU 1906  CA  LYS A 299    11466  10501  10732    135   -333  -1281       C  
ATOM   1907  C   LYS A 299      43.292  30.618  25.419  1.00 86.47           C  
ANISOU 1907  C   LYS A 299    11507  10524  10822     73   -391  -1309       C  
ATOM   1908  O   LYS A 299      43.854  31.481  24.729  1.00 82.02           O  
ANISOU 1908  O   LYS A 299    10947   9876  10341     33   -401  -1316       O  
ATOM   1909  CB  LYS A 299      41.017  31.647  25.314  1.00 83.93           C  
ANISOU 1909  CB  LYS A 299    11238  10161  10490    165   -309  -1325       C  
ATOM   1910  N   SER A 300      43.941  29.892  26.319  1.00 87.98           N  
ANISOU 1910  N   SER A 300    11684  10787  10956     65   -429  -1323       N  
ATOM   1911  CA  SER A 300      45.392  29.770  26.244  1.00 85.80           C  
ANISOU 1911  CA  SER A 300    11379  10503  10717      4   -481  -1327       C  
ATOM   1912  C   SER A 300      45.771  28.531  25.439  1.00 84.64           C  
ANISOU 1912  C   SER A 300    11186  10395  10579    -15   -474  -1250       C  
ATOM   1913  O   SER A 300      46.852  27.971  25.623  1.00 86.68           O  
ANISOU 1913  O   SER A 300    11413  10685  10838    -49   -515  -1244       O  
ATOM   1914  CB  SER A 300      46.035  29.721  27.635  1.00 83.37           C  
ANISOU 1914  CB  SER A 300    11080  10247  10349      4   -534  -1386       C  
ATOM   1915  OG  SER A 300      46.078  30.988  28.241  1.00 80.90           O  
ANISOU 1915  OG  SER A 300    10805   9882  10050      2   -553  -1464       O  
ATOM   1916  N   GLY A 301      44.876  28.109  24.549  1.00 73.88           N  
ANISOU 1916  N   GLY A 301     9818   9029   9224      9   -424  -1194       N  
ATOM   1917  CA  GLY A 301      45.199  27.094  23.566  1.00 58.99           C  
ANISOU 1917  CA  GLY A 301     7892   7162   7361    -12   -414  -1124       C  
ATOM   1918  C   GLY A 301      45.725  27.861  22.372  1.00 52.39           C  
ANISOU 1918  C   GLY A 301     7047   6235   6624    -56   -410  -1108       C  
ATOM   1919  O   GLY A 301      45.498  27.467  21.235  1.00 46.37           O  
ANISOU 1919  O   GLY A 301     6267   5457   5896    -61   -379  -1051       O  
ATOM   1920  N   THR A 302      46.380  28.992  22.639  1.00 56.17           N  
ANISOU 1920  N   THR A 302     7540   6654   7148    -88   -439  -1159       N  
ATOM   1921  CA  THR A 302      46.995  29.828  21.610  1.00 51.12           C  
ANISOU 1921  CA  THR A 302     6894   5924   6606   -135   -437  -1146       C  
ATOM   1922  C   THR A 302      48.495  29.804  21.827  1.00 49.33           C  
ANISOU 1922  C   THR A 302     6632   5697   6413   -195   -488  -1162       C  
ATOM   1923  O   THR A 302      48.955  30.067  22.932  1.00 55.40           O  
ANISOU 1923  O   THR A 302     7410   6488   7153   -200   -531  -1220       O  
ATOM   1924  CB  THR A 302      46.513  31.309  21.689  1.00 59.92           C  
ANISOU 1924  CB  THR A 302     8055   6954   7758   -127   -426  -1193       C  
ATOM   1925  OG1 THR A 302      45.106  31.407  21.408  1.00 60.27           O  
ANISOU 1925  OG1 THR A 302     8128   6993   7779    -70   -376  -1176       O  
ATOM   1926  CG2 THR A 302      47.267  32.193  20.674  1.00 56.46           C  
ANISOU 1926  CG2 THR A 302     7611   6419   7423   -182   -426  -1176       C  
ATOM   1927  N   TYR A 303      49.255  29.471  20.788  1.00 36.89           N  
ANISOU 1927  N   TYR A 303     5016   4102   4898   -237   -485  -1109       N  
ATOM   1928  CA  TYR A 303      50.706  29.303  20.921  1.00 40.40           C  
ANISOU 1928  CA  TYR A 303     5417   4557   5378   -293   -530  -1115       C  
ATOM   1929  C   TYR A 303      51.418  29.393  19.573  1.00 41.41           C  
ANISOU 1929  C   TYR A 303     5508   4632   5593   -341   -512  -1059       C  
ATOM   1930  O   TYR A 303      50.781  29.349  18.519  1.00 41.35           O  
ANISOU 1930  O   TYR A 303     5508   4593   5609   -328   -465  -1009       O  
ATOM   1931  CB  TYR A 303      51.038  27.960  21.583  1.00 43.15           C  
ANISOU 1931  CB  TYR A 303     5735   5006   5656   -278   -556  -1104       C  
ATOM   1932  CG  TYR A 303      50.342  26.794  20.914  1.00 53.50           C  
ANISOU 1932  CG  TYR A 303     7034   6360   6933   -245   -515  -1039       C  
ATOM   1933  CD1 TYR A 303      50.830  26.250  19.723  1.00 54.54           C  
ANISOU 1933  CD1 TYR A 303     7125   6480   7116   -273   -496   -978       C  
ATOM   1934  CD2 TYR A 303      49.193  26.243  21.464  1.00 56.71           C  
ANISOU 1934  CD2 TYR A 303     7469   6821   7259   -187   -494  -1039       C  
ATOM   1935  CE1 TYR A 303      50.192  25.186  19.104  1.00 52.92           C  
ANISOU 1935  CE1 TYR A 303     6912   6314   6883   -244   -462   -923       C  
ATOM   1936  CE2 TYR A 303      48.550  25.180  20.856  1.00 57.20           C  
ANISOU 1936  CE2 TYR A 303     7520   6921   7294   -160   -458   -982       C  
ATOM   1937  CZ  TYR A 303      49.053  24.656  19.675  1.00 56.27           C  
ANISOU 1937  CZ  TYR A 303     7364   6788   7227   -189   -444   -926       C  
ATOM   1938  OH  TYR A 303      48.413  23.600  19.071  1.00 54.69           O  
ANISOU 1938  OH  TYR A 303     7155   6624   7001   -163   -412   -874       O  
ATOM   1939  N   ARG A 304      52.742  29.506  19.615  1.00 40.02           N  
ANISOU 1939  N   ARG A 304     5291   4450   5466   -397   -549  -1067       N  
ATOM   1940  CA  ARG A 304      53.538  29.616  18.402  1.00 44.76           C  
ANISOU 1940  CA  ARG A 304     5851   5004   6152   -446   -531  -1015       C  
ATOM   1941  C   ARG A 304      54.777  28.729  18.485  1.00 50.47           C  
ANISOU 1941  C   ARG A 304     6509   5784   6882   -480   -563   -997       C  
ATOM   1942  O   ARG A 304      55.441  28.669  19.526  1.00 51.66           O  
ANISOU 1942  O   ARG A 304     6645   5972   7009   -491   -615  -1045       O  
ATOM   1943  CB  ARG A 304      53.956  31.070  18.170  1.00 41.51           C  
ANISOU 1943  CB  ARG A 304     5454   4496   5821   -491   -535  -1040       C  
ATOM   1944  CG  ARG A 304      52.818  32.003  17.810  1.00 41.48           C  
ANISOU 1944  CG  ARG A 304     5511   4422   5829   -461   -496  -1043       C  
ATOM   1945  CD  ARG A 304      52.317  31.730  16.398  1.00 46.79           C  
ANISOU 1945  CD  ARG A 304     6180   5069   6529   -450   -439   -964       C  
ATOM   1946  NE  ARG A 304      51.146  32.539  16.066  1.00 43.44           N  
ANISOU 1946  NE  ARG A 304     5813   4584   6107   -412   -403   -963       N  
ATOM   1947  CZ  ARG A 304      49.901  32.216  16.411  1.00 40.30           C  
ANISOU 1947  CZ  ARG A 304     5451   4220   5641   -349   -385   -973       C  
ATOM   1948  NH1 ARG A 304      49.669  31.102  17.098  1.00 36.69           N  
ANISOU 1948  NH1 ARG A 304     4980   3855   5107   -319   -398   -982       N  
ATOM   1949  NH2 ARG A 304      48.888  33.004  16.072  1.00 35.24           N  
ANISOU 1949  NH2 ARG A 304     4858   3522   5010   -315   -351   -971       N  
ATOM   1950  N   GLY A 305      55.077  28.042  17.386  1.00 46.39           N  
ANISOU 1950  N   GLY A 305     5954   5274   6398   -493   -532   -929       N  
ATOM   1951  CA  GLY A 305      56.297  27.261  17.264  1.00 37.21           C  
ANISOU 1951  CA  GLY A 305     4725   4157   5257   -526   -554   -905       C  
ATOM   1952  C   GLY A 305      56.450  26.112  18.245  1.00 43.58           C  
ANISOU 1952  C   GLY A 305     5515   5058   5986   -497   -592   -921       C  
ATOM   1953  O   GLY A 305      57.570  25.711  18.566  1.00 47.35           O  
ANISOU 1953  O   GLY A 305     5942   5573   6477   -525   -629   -925       O  
ATOM   1954  N   LYS A 306      55.332  25.582  18.734  1.00 38.80           N  
ANISOU 1954  N   LYS A 306     4951   4494   5299   -440   -581   -928       N  
ATOM   1955  CA  LYS A 306      55.374  24.407  19.594  1.00 36.15           C  
ANISOU 1955  CA  LYS A 306     4603   4248   4885   -408   -609   -931       C  
ATOM   1956  C   LYS A 306      55.790  23.187  18.760  1.00 44.86           C  
ANISOU 1956  C   LYS A 306     5657   5387   5999   -410   -591   -866       C  
ATOM   1957  O   LYS A 306      55.408  23.056  17.595  1.00 45.13           O  
ANISOU 1957  O   LYS A 306     5690   5391   6068   -411   -543   -818       O  
ATOM   1958  CB  LYS A 306      54.013  24.192  20.265  1.00 44.70           C  
ANISOU 1958  CB  LYS A 306     5742   5361   5881   -348   -595   -948       C  
ATOM   1959  CG  LYS A 306      53.941  22.980  21.183  1.00 52.19           C  
ANISOU 1959  CG  LYS A 306     6685   6401   6742   -310   -618   -945       C  
ATOM   1960  CD  LYS A 306      52.540  22.778  21.765  1.00 54.93           C  
ANISOU 1960  CD  LYS A 306     7085   6778   7008   -252   -593   -954       C  
ATOM   1961  CE  LYS A 306      52.208  23.814  22.834  1.00 58.35           C  
ANISOU 1961  CE  LYS A 306     7562   7197   7412   -240   -615  -1023       C  
ATOM   1962  NZ  LYS A 306      50.907  23.526  23.515  1.00 58.52           N  
ANISOU 1962  NZ  LYS A 306     7628   7259   7348   -180   -590  -1031       N  
ATOM   1963  N   VAL A 307      56.592  22.308  19.350  1.00 44.75           N  
ANISOU 1963  N   VAL A 307     5606   5440   5958   -410   -629   -864       N  
ATOM   1964  CA  VAL A 307      57.112  21.153  18.631  1.00 39.70           C  
ANISOU 1964  CA  VAL A 307     4916   4835   5332   -413   -616   -807       C  
ATOM   1965  C   VAL A 307      56.378  19.901  19.098  1.00 44.15           C  
ANISOU 1965  C   VAL A 307     5498   5469   5809   -358   -613   -789       C  
ATOM   1966  O   VAL A 307      56.284  19.634  20.300  1.00 49.06           O  
ANISOU 1966  O   VAL A 307     6137   6142   6362   -332   -649   -819       O  
ATOM   1967  CB  VAL A 307      58.645  21.021  18.811  1.00 47.80           C  
ANISOU 1967  CB  VAL A 307     5876   5882   6402   -453   -658   -810       C  
ATOM   1968  CG1 VAL A 307      59.014  21.076  20.285  1.00 63.55           C  
ANISOU 1968  CG1 VAL A 307     7879   7925   8343   -444   -721   -863       C  
ATOM   1969  CG2 VAL A 307      59.176  19.748  18.163  1.00 43.74           C  
ANISOU 1969  CG2 VAL A 307     5310   5411   5896   -447   -645   -753       C  
ATOM   1970  N   GLN A 308      55.823  19.152  18.149  1.00 35.83           N  
ANISOU 1970  N   GLN A 308     4442   4416   4756   -341   -568   -739       N  
ATOM   1971  CA  GLN A 308      54.972  18.019  18.495  1.00 35.99           C  
ANISOU 1971  CA  GLN A 308     4484   4493   4697   -291   -559   -718       C  
ATOM   1972  C   GLN A 308      55.273  16.808  17.628  1.00 36.62           C  
ANISOU 1972  C   GLN A 308     4525   4598   4793   -288   -539   -663       C  
ATOM   1973  O   GLN A 308      55.596  16.949  16.446  1.00 40.10           O  
ANISOU 1973  O   GLN A 308     4938   4997   5300   -315   -509   -634       O  
ATOM   1974  CB  GLN A 308      53.494  18.394  18.340  1.00 38.60           C  
ANISOU 1974  CB  GLN A 308     4872   4799   4997   -260   -519   -723       C  
ATOM   1975  CG  GLN A 308      53.062  19.605  19.154  1.00 40.54           C  
ANISOU 1975  CG  GLN A 308     5160   5017   5226   -256   -531   -779       C  
ATOM   1976  CD  GLN A 308      51.575  19.877  19.054  1.00 42.73           C  
ANISOU 1976  CD  GLN A 308     5489   5278   5468   -218   -491   -780       C  
ATOM   1977  OE1 GLN A 308      51.079  20.328  18.024  1.00 42.64           O  
ANISOU 1977  OE1 GLN A 308     5488   5214   5501   -225   -452   -761       O  
ATOM   1978  NE2 GLN A 308      50.857  19.603  20.130  1.00 46.63           N  
ANISOU 1978  NE2 GLN A 308     6015   5821   5882   -177   -497   -801       N  
ATOM   1979  N   ASN A 309      55.170  15.617  18.211  1.00 30.33           N  
ANISOU 1979  N   ASN A 309     3724   3866   3932   -253   -554   -645       N  
ATOM   1980  CA  ASN A 309      55.176  14.413  17.395  1.00 33.58           C  
ANISOU 1980  CA  ASN A 309     4111   4300   4350   -241   -531   -594       C  
ATOM   1981  C   ASN A 309      53.781  14.222  16.812  1.00 34.99           C  
ANISOU 1981  C   ASN A 309     4330   4461   4502   -215   -484   -577       C  
ATOM   1982  O   ASN A 309      52.880  15.007  17.112  1.00 36.12           O  
ANISOU 1982  O   ASN A 309     4519   4582   4623   -204   -471   -603       O  
ATOM   1983  CB  ASN A 309      55.670  13.179  18.166  1.00 32.82           C  
ANISOU 1983  CB  ASN A 309     3993   4275   4204   -214   -565   -576       C  
ATOM   1984  CG  ASN A 309      54.843  12.876  19.400  1.00 42.36           C  
ANISOU 1984  CG  ASN A 309     5249   5529   5318   -172   -579   -589       C  
ATOM   1985  OD1 ASN A 309      53.640  13.136  19.443  1.00 43.34           O  
ANISOU 1985  OD1 ASN A 309     5420   5641   5407   -152   -548   -596       O  
ATOM   1986  ND2 ASN A 309      55.490  12.306  20.415  1.00 40.34           N  
ANISOU 1986  ND2 ASN A 309     4979   5328   5020   -156   -622   -589       N  
ATOM   1987  N   LEU A 310      53.611  13.192  15.987  1.00 33.90           N  
ANISOU 1987  N   LEU A 310     4175   4335   4369   -204   -459   -535       N  
ATOM   1988  CA  LEU A 310      52.368  12.979  15.245  1.00 32.19           C  
ANISOU 1988  CA  LEU A 310     3991   4101   4138   -185   -414   -517       C  
ATOM   1989  C   LEU A 310      51.138  12.873  16.148  1.00 37.46           C  
ANISOU 1989  C   LEU A 310     4710   4799   4724   -145   -410   -530       C  
ATOM   1990  O   LEU A 310      50.096  13.471  15.874  1.00 40.33           O  
ANISOU 1990  O   LEU A 310     5109   5133   5081   -135   -379   -539       O  
ATOM   1991  CB  LEU A 310      52.476  11.735  14.363  1.00 30.67           C  
ANISOU 1991  CB  LEU A 310     3776   3925   3952   -175   -382   -455       C  
ATOM   1992  CG  LEU A 310      51.198  11.351  13.615  1.00 34.52           C  
ANISOU 1992  CG  LEU A 310     4300   4401   4416   -151   -327   -416       C  
ATOM   1993  CD1 LEU A 310      50.671  12.514  12.766  1.00 36.14           C  
ANISOU 1993  CD1 LEU A 310     4525   4544   4661   -168   -295   -425       C  
ATOM   1994  CD2 LEU A 310      51.444  10.125  12.752  1.00 30.48           C  
ANISOU 1994  CD2 LEU A 310     3767   3901   3914   -143   -297   -356       C  
ATOM   1995  N   THR A 311      51.267  12.122  17.229  1.00 35.78           N  
ANISOU 1995  N   THR A 311     4500   4647   4450   -120   -437   -526       N  
ATOM   1996  CA  THR A 311      50.157  11.934  18.148  1.00 38.63           C  
ANISOU 1996  CA  THR A 311     4904   5043   4731    -81   -427   -530       C  
ATOM   1997  C   THR A 311      49.697  13.251  18.794  1.00 39.20           C  
ANISOU 1997  C   THR A 311     5011   5090   4793    -80   -428   -578       C  
ATOM   1998  O   THR A 311      48.497  13.547  18.845  1.00 32.20           O  
ANISOU 1998  O   THR A 311     4160   4198   3878    -57   -396   -582       O  
ATOM   1999  CB  THR A 311      50.512  10.885  19.216  1.00 44.77           C  
ANISOU 1999  CB  THR A 311     5676   5888   5446    -55   -456   -511       C  
ATOM   2000  OG1 THR A 311      50.670   9.608  18.583  1.00 47.01           O  
ANISOU 2000  OG1 THR A 311     5937   6192   5734    -46   -448   -463       O  
ATOM   2001  CG2 THR A 311      49.413  10.791  20.262  1.00 47.06           C  
ANISOU 2001  CG2 THR A 311     6012   6215   5655    -17   -442   -514       C  
ATOM   2002  N   GLN A 312      50.653  14.039  19.278  1.00 37.83           N  
ANISOU 2002  N   GLN A 312     4825   4903   4646   -105   -465   -613       N  
ATOM   2003  CA  GLN A 312      50.353  15.322  19.900  1.00 37.68           C  
ANISOU 2003  CA  GLN A 312     4838   4857   4623   -107   -471   -663       C  
ATOM   2004  C   GLN A 312      49.748  16.302  18.902  1.00 39.78           C  
ANISOU 2004  C   GLN A 312     5119   5053   4943   -121   -435   -670       C  
ATOM   2005  O   GLN A 312      48.768  16.990  19.208  1.00 35.49           O  
ANISOU 2005  O   GLN A 312     4614   4494   4376    -99   -415   -693       O  
ATOM   2006  CB  GLN A 312      51.620  15.934  20.493  1.00 37.20           C  
ANISOU 2006  CB  GLN A 312     4755   4791   4589   -138   -521   -699       C  
ATOM   2007  CG  GLN A 312      52.281  15.081  21.542  1.00 38.71           C  
ANISOU 2007  CG  GLN A 312     4931   5050   4727   -123   -562   -694       C  
ATOM   2008  CD  GLN A 312      53.666  15.580  21.891  1.00 47.27           C  
ANISOU 2008  CD  GLN A 312     5980   6129   5851   -158   -613   -723       C  
ATOM   2009  OE1 GLN A 312      54.346  16.195  21.067  1.00 52.62           O  
ANISOU 2009  OE1 GLN A 312     6628   6756   6608   -200   -613   -728       O  
ATOM   2010  NE2 GLN A 312      54.088  15.328  23.121  1.00 47.49           N  
ANISOU 2010  NE2 GLN A 312     6011   6209   5823   -143   -656   -742       N  
ATOM   2011  N   PHE A 313      50.342  16.363  17.712  1.00 35.12           N  
ANISOU 2011  N   PHE A 313     4498   4421   4425   -154   -425   -648       N  
ATOM   2012  CA  PHE A 313      49.903  17.293  16.684  1.00 30.05           C  
ANISOU 2012  CA  PHE A 313     3869   3709   3840   -169   -391   -647       C  
ATOM   2013  C   PHE A 313      48.482  16.989  16.224  1.00 32.29           C  
ANISOU 2013  C   PHE A 313     4182   3994   4092   -133   -348   -627       C  
ATOM   2014  O   PHE A 313      47.743  17.891  15.826  1.00 37.66           O  
ANISOU 2014  O   PHE A 313     4890   4626   4791   -126   -323   -637       O  
ATOM   2015  CB  PHE A 313      50.853  17.259  15.487  1.00 27.07           C  
ANISOU 2015  CB  PHE A 313     3450   3294   3542   -210   -384   -618       C  
ATOM   2016  CG  PHE A 313      50.519  18.264  14.425  1.00 27.18           C  
ANISOU 2016  CG  PHE A 313     3478   3234   3617   -228   -349   -610       C  
ATOM   2017  CD1 PHE A 313      50.463  19.619  14.728  1.00 28.15           C  
ANISOU 2017  CD1 PHE A 313     3626   3307   3764   -239   -354   -646       C  
ATOM   2018  CD2 PHE A 313      50.256  17.860  13.122  1.00 27.06           C  
ANISOU 2018  CD2 PHE A 313     3453   3196   3633   -231   -310   -567       C  
ATOM   2019  CE1 PHE A 313      50.154  20.559  13.749  1.00 32.06           C  
ANISOU 2019  CE1 PHE A 313     4136   3730   4315   -252   -322   -633       C  
ATOM   2020  CE2 PHE A 313      49.952  18.790  12.139  1.00 26.98           C  
ANISOU 2020  CE2 PHE A 313     3458   3117   3675   -243   -277   -553       C  
ATOM   2021  CZ  PHE A 313      49.897  20.148  12.456  1.00 28.57           C  
ANISOU 2021  CZ  PHE A 313     3685   3268   3901   -253   -283   -584       C  
ATOM   2022  N   TYR A 314      48.106  15.716  16.285  1.00 27.05           N  
ANISOU 2022  N   TYR A 314     3514   3385   3381   -108   -340   -597       N  
ATOM   2023  CA  TYR A 314      46.784  15.295  15.850  1.00 29.95           C  
ANISOU 2023  CA  TYR A 314     3902   3760   3717    -76   -301   -574       C  
ATOM   2024  C   TYR A 314      45.789  15.178  17.014  1.00 35.98           C  
ANISOU 2024  C   TYR A 314     4697   4571   4404    -35   -295   -588       C  
ATOM   2025  O   TYR A 314      44.615  14.912  16.783  1.00 34.43           O  
ANISOU 2025  O   TYR A 314     4516   4385   4180     -6   -260   -571       O  
ATOM   2026  CB  TYR A 314      46.862  13.972  15.068  1.00 27.74           C  
ANISOU 2026  CB  TYR A 314     3597   3505   3437    -76   -286   -524       C  
ATOM   2027  CG  TYR A 314      47.070  14.103  13.558  1.00 34.20           C  
ANISOU 2027  CG  TYR A 314     4401   4274   4322   -100   -253   -483       C  
ATOM   2028  CD1 TYR A 314      46.263  13.407  12.662  1.00 35.05           C  
ANISOU 2028  CD1 TYR A 314     4511   4385   4420    -84   -211   -431       C  
ATOM   2029  CD2 TYR A 314      48.079  14.905  13.028  1.00 42.36           C  
ANISOU 2029  CD2 TYR A 314     5414   5257   5424   -138   -264   -495       C  
ATOM   2030  CE1 TYR A 314      46.451  13.510  11.279  1.00 36.58           C  
ANISOU 2030  CE1 TYR A 314     4695   4540   4664   -101   -182   -394       C  
ATOM   2031  CE2 TYR A 314      48.276  15.015  11.635  1.00 36.97           C  
ANISOU 2031  CE2 TYR A 314     4719   4534   4795   -157   -228   -452       C  
ATOM   2032  CZ  TYR A 314      47.459  14.316  10.772  1.00 38.59           C  
ANISOU 2032  CZ  TYR A 314     4933   4749   4981   -135   -188   -403       C  
ATOM   2033  OH  TYR A 314      47.642  14.417   9.402  1.00 36.34           O  
ANISOU 2033  OH  TYR A 314     4640   4429   4739   -148   -154   -362       O  
ATOM   2034  N   HIS A 315      46.254  15.375  18.251  1.00 40.71           N  
ANISOU 2034  N   HIS A 315     5302   5199   4968    -31   -326   -616       N  
ATOM   2035  CA  HIS A 315      45.391  15.303  19.449  1.00 48.27           C  
ANISOU 2035  CA  HIS A 315     6288   6203   5850      7   -319   -629       C  
ATOM   2036  C   HIS A 315      44.152  16.204  19.340  1.00 52.67           C  
ANISOU 2036  C   HIS A 315     6875   6731   6406     31   -283   -647       C  
ATOM   2037  O   HIS A 315      44.262  17.357  18.901  1.00 47.66           O  
ANISOU 2037  O   HIS A 315     6249   6035   5823     16   -284   -675       O  
ATOM   2038  CB  HIS A 315      46.196  15.650  20.713  1.00 52.38           C  
ANISOU 2038  CB  HIS A 315     6812   6747   6343      3   -362   -667       C  
ATOM   2039  CG  HIS A 315      45.365  15.781  21.957  1.00 59.72           C  
ANISOU 2039  CG  HIS A 315     7775   7718   7200     42   -354   -687       C  
ATOM   2040  ND1 HIS A 315      45.050  14.707  22.763  1.00 64.60           N  
ANISOU 2040  ND1 HIS A 315     8396   8404   7746     71   -349   -657       N  
ATOM   2041  CD2 HIS A 315      44.792  16.866  22.534  1.00 58.58           C  
ANISOU 2041  CD2 HIS A 315     7661   7556   7043     58   -347   -731       C  
ATOM   2042  CE1 HIS A 315      44.312  15.124  23.780  1.00 61.38           C  
ANISOU 2042  CE1 HIS A 315     8017   8021   7284    102   -338   -682       C  
ATOM   2043  NE2 HIS A 315      44.140  16.428  23.663  1.00 57.86           N  
ANISOU 2043  NE2 HIS A 315     7588   7525   6872     96   -337   -730       N  
ATOM   2044  N   PRO A 316      42.970  15.691  19.751  1.00 54.09           N  
ANISOU 2044  N   PRO A 316     7069   6953   6530     70   -251   -630       N  
ATOM   2045  CA  PRO A 316      42.695  14.426  20.444  1.00 49.90           C  
ANISOU 2045  CA  PRO A 316     6533   6493   5933     92   -245   -595       C  
ATOM   2046  C   PRO A 316      42.040  13.368  19.559  1.00 49.81           C  
ANISOU 2046  C   PRO A 316     6506   6496   5922     98   -212   -543       C  
ATOM   2047  O   PRO A 316      41.183  12.626  20.055  1.00 43.50           O  
ANISOU 2047  O   PRO A 316     5711   5746   5071    125   -185   -515       O  
ATOM   2048  CB  PRO A 316      41.659  14.856  21.482  1.00 50.05           C  
ANISOU 2048  CB  PRO A 316     6579   6540   5897    129   -223   -616       C  
ATOM   2049  CG  PRO A 316      40.881  16.004  20.761  1.00 55.51           C  
ANISOU 2049  CG  PRO A 316     7283   7174   6633    136   -197   -639       C  
ATOM   2050  CD  PRO A 316      41.716  16.442  19.563  1.00 55.28           C  
ANISOU 2050  CD  PRO A 316     7241   7082   6682     97   -214   -641       C  
ATOM   2051  N   LEU A 317      42.421  13.302  18.286  1.00 46.31           N  
ANISOU 2051  N   LEU A 317     6046   6013   5537     73   -212   -530       N  
ATOM   2052  CA  LEU A 317      41.786  12.373  17.353  1.00 52.93           C  
ANISOU 2052  CA  LEU A 317     6872   6861   6378     78   -183   -487       C  
ATOM   2053  C   LEU A 317      42.010  10.896  17.720  1.00 56.10           C  
ANISOU 2053  C   LEU A 317     7257   7313   6743     79   -183   -435       C  
ATOM   2054  O   LEU A 317      41.093  10.069  17.585  1.00 50.02           O  
ANISOU 2054  O   LEU A 317     6483   6567   5955     92   -148   -390       O  
ATOM   2055  CB  LEU A 317      42.227  12.654  15.910  1.00 49.89           C  
ANISOU 2055  CB  LEU A 317     6470   6414   6070     47   -177   -467       C  
ATOM   2056  CG  LEU A 317      41.835  14.033  15.369  1.00 50.01           C  
ANISOU 2056  CG  LEU A 317     6502   6371   6126     48   -167   -501       C  
ATOM   2057  CD1 LEU A 317      42.389  14.257  13.968  1.00 50.02           C  
ANISOU 2057  CD1 LEU A 317     6489   6317   6198     17   -160   -474       C  
ATOM   2058  CD2 LEU A 317      40.325  14.205  15.385  1.00 48.32           C  
ANISOU 2058  CD2 LEU A 317     6304   6170   5887     85   -131   -496       C  
ATOM   2059  N   ASP A 318      43.216  10.570  18.186  1.00 54.21           N  
ANISOU 2059  N   ASP A 318     7009   7091   6500     66   -223   -442       N  
ATOM   2060  CA  ASP A 318      43.544   9.182  18.521  1.00 55.52           C  
ANISOU 2060  CA  ASP A 318     7160   7298   6636     69   -227   -391       C  
ATOM   2061  C   ASP A 318      42.833   8.670  19.771  1.00 57.69           C  
ANISOU 2061  C   ASP A 318     7455   7637   6829    104   -217   -381       C  
ATOM   2062  O   ASP A 318      42.403   7.513  19.803  1.00 57.89           O  
ANISOU 2062  O   ASP A 318     7473   7687   6835    112   -192   -323       O  
ATOM   2063  CB  ASP A 318      45.057   8.957  18.627  1.00 54.54           C  
ANISOU 2063  CB  ASP A 318     7014   7174   6533     49   -274   -396       C  
ATOM   2064  CG  ASP A 318      45.742   8.935  17.266  1.00 55.22           C  
ANISOU 2064  CG  ASP A 318     7073   7209   6699     17   -268   -377       C  
ATOM   2065  OD1 ASP A 318      45.606   7.924  16.534  1.00 48.51           O  
ANISOU 2065  OD1 ASP A 318     6211   6355   5867     14   -243   -324       O  
ATOM   2066  OD2 ASP A 318      46.420   9.929  16.933  1.00 55.18           O  
ANISOU 2066  OD2 ASP A 318     7061   7167   6739     -7   -289   -416       O  
ATOM   2067  N   MET A 319      42.695   9.519  20.789  1.00 55.11           N  
ANISOU 2067  N   MET A 319     7147   7319   6471    118   -224   -418       N  
ATOM   2068  CA  MET A 319      42.058   9.075  22.027  1.00 60.53           C  
ANISOU 2068  CA  MET A 319     7851   8059   7087    149   -207   -399       C  
ATOM   2069  C   MET A 319      40.536   8.936  21.908  1.00 51.30           C  
ANISOU 2069  C   MET A 319     6689   6904   5900    170   -151   -376       C  
ATOM   2070  O   MET A 319      39.915   8.219  22.687  1.00 47.95           O  
ANISOU 2070  O   MET A 319     6270   6526   5424    191   -125   -340       O  
ATOM   2071  CB  MET A 319      42.458   9.949  23.229  1.00 70.90           C  
ANISOU 2071  CB  MET A 319     9185   9384   8371    158   -235   -446       C  
ATOM   2072  CG  MET A 319      41.937  11.376  23.221  1.00 74.17           C  
ANISOU 2072  CG  MET A 319     9615   9762   8804    161   -225   -502       C  
ATOM   2073  SD  MET A 319      42.193  12.187  24.822  1.00 91.07           S  
ANISOU 2073  SD  MET A 319    11783  11928  10889    180   -252   -553       S  
ATOM   2074  CE  MET A 319      41.213  11.140  25.901  1.00 86.92           C  
ANISOU 2074  CE  MET A 319    11270  11478  10278    220   -213   -504       C  
ATOM   2075  N   PHE A 320      39.947   9.601  20.914  1.00 49.65           N  
ANISOU 2075  N   PHE A 320     6476   6654   5736    164   -131   -394       N  
ATOM   2076  CA  PHE A 320      38.504   9.532  20.689  1.00 52.29           C  
ANISOU 2076  CA  PHE A 320     6807   6999   6061    183    -80   -375       C  
ATOM   2077  C   PHE A 320      38.109   8.700  19.466  1.00 55.65           C  
ANISOU 2077  C   PHE A 320     7210   7411   6525    167    -57   -328       C  
ATOM   2078  O   PHE A 320      36.925   8.612  19.130  1.00 52.90           O  
ANISOU 2078  O   PHE A 320     6851   7066   6183    177    -17   -308       O  
ATOM   2079  CB  PHE A 320      37.907  10.935  20.559  1.00 57.01           C  
ANISOU 2079  CB  PHE A 320     7417   7562   6683    195    -69   -423       C  
ATOM   2080  CG  PHE A 320      37.782  11.664  21.864  1.00 64.00           C  
ANISOU 2080  CG  PHE A 320     8325   8466   7526    218    -73   -458       C  
ATOM   2081  CD1 PHE A 320      37.008  11.141  22.890  1.00 66.29           C  
ANISOU 2081  CD1 PHE A 320     8620   8813   7756    245    -43   -434       C  
ATOM   2082  CD2 PHE A 320      38.425  12.879  22.063  1.00 64.58           C  
ANISOU 2082  CD2 PHE A 320     8415   8500   7621    210   -105   -516       C  
ATOM   2083  CE1 PHE A 320      36.888  11.810  24.095  1.00 69.51           C  
ANISOU 2083  CE1 PHE A 320     9050   9241   8121    268    -46   -470       C  
ATOM   2084  CE2 PHE A 320      38.307  13.554  23.264  1.00 64.06           C  
ANISOU 2084  CE2 PHE A 320     8372   8453   7514    232   -110   -553       C  
ATOM   2085  CZ  PHE A 320      37.538  13.020  24.281  1.00 67.23           C  
ANISOU 2085  CZ  PHE A 320     8780   8914   7851    262    -81   -531       C  
ATOM   2086  N   GLY A 321      39.095   8.098  18.804  1.00 50.74           N  
ANISOU 2086  N   GLY A 321     6574   6762   5943    137    -81   -304       N  
ATOM   2087  CA  GLY A 321      38.839   7.308  17.614  1.00 48.85           C  
ANISOU 2087  CA  GLY A 321     6312   6493   5755    114    -61   -256       C  
ATOM   2088  C   GLY A 321      37.966   6.084  17.846  1.00 49.94           C  
ANISOU 2088  C   GLY A 321     6439   6664   5873    119    -27   -198       C  
ATOM   2089  O   GLY A 321      37.190   5.697  16.973  1.00 41.38           O  
ANISOU 2089  O   GLY A 321     5338   5561   4823    109     -2   -171       O  
ATOM   2090  N   GLU A 322      38.084   5.472  19.022  1.00 58.57           N  
ANISOU 2090  N   GLU A 322     7541   7805   6908    135    -27   -178       N  
ATOM   2091  CA  GLU A 322      37.329   4.252  19.310  1.00 60.25           C  
ANISOU 2091  CA  GLU A 322     7744   8046   7104    136      7   -116       C  
ATOM   2092  C   GLU A 322      35.874   4.523  19.726  1.00 59.66           C  
ANISOU 2092  C   GLU A 322     7663   8003   7001    157     53   -112       C  
ATOM   2093  O   GLU A 322      35.074   3.591  19.845  1.00 64.27           O  
ANISOU 2093  O   GLU A 322     8231   8604   7582    153     89    -59       O  
ATOM   2094  CB  GLU A 322      38.044   3.400  20.367  1.00 59.90           C  
ANISOU 2094  CB  GLU A 322     7711   8039   7009    147     -8    -84       C  
ATOM   2095  CG  GLU A 322      38.321   1.960  19.929  1.00 65.58           C  
ANISOU 2095  CG  GLU A 322     8416   8739   7762    127     -4    -19       C  
ATOM   2096  CD  GLU A 322      39.813   1.677  19.762  1.00 73.10           C  
ANISOU 2096  CD  GLU A 322     9370   9673   8732    119    -51    -23       C  
ATOM   2097  OE1 GLU A 322      40.574   1.904  20.731  1.00 72.29           O  
ANISOU 2097  OE1 GLU A 322     9282   9605   8581    138    -82    -39       O  
ATOM   2098  OE2 GLU A 322      40.226   1.236  18.662  1.00 71.01           O  
ANISOU 2098  OE2 GLU A 322     9090   9360   8529     96    -58    -12       O  
ATOM   2099  N   TRP A 323      35.539   5.798  19.914  1.00 49.34           N  
ANISOU 2099  N   TRP A 323     6368   6700   5680    178     54   -168       N  
ATOM   2100  CA  TRP A 323      34.243   6.225  20.454  1.00 48.70           C  
ANISOU 2100  CA  TRP A 323     6284   6656   5565    208     97   -174       C  
ATOM   2101  C   TRP A 323      32.990   5.527  19.889  1.00 48.36           C  
ANISOU 2101  C   TRP A 323     6205   6614   5555    197    142   -125       C  
ATOM   2102  O   TRP A 323      32.229   4.893  20.633  1.00 39.10           O  
ANISOU 2102  O   TRP A 323     5021   5488   4346    208    181    -85       O  
ATOM   2103  CB  TRP A 323      34.090   7.735  20.288  1.00 54.06           C  
ANISOU 2103  CB  TRP A 323     6975   7314   6251    228     88   -244       C  
ATOM   2104  CG  TRP A 323      33.029   8.321  21.156  1.00 59.62           C  
ANISOU 2104  CG  TRP A 323     7681   8045   6925    260    123   -257       C  
ATOM   2105  CD1 TRP A 323      31.711   8.494  20.842  1.00 60.93           C  
ANISOU 2105  CD1 TRP A 323     7823   8221   7107    276    165   -247       C  
ATOM   2106  CD2 TRP A 323      33.193   8.812  22.489  1.00 62.16           C  
ANISOU 2106  CD2 TRP A 323     8029   8390   7200    282    117   -282       C  
ATOM   2107  NE1 TRP A 323      31.045   9.063  21.899  1.00 61.96           N  
ANISOU 2107  NE1 TRP A 323     7962   8378   7203    306    188   -264       N  
ATOM   2108  CE2 TRP A 323      31.933   9.269  22.923  1.00 61.38           C  
ANISOU 2108  CE2 TRP A 323     7921   8312   7088    311    160   -286       C  
ATOM   2109  CE3 TRP A 323      34.285   8.907  23.361  1.00 60.75           C  
ANISOU 2109  CE3 TRP A 323     7876   8217   6987    281     78   -302       C  
ATOM   2110  CZ2 TRP A 323      31.734   9.815  24.187  1.00 55.56           C  
ANISOU 2110  CZ2 TRP A 323     7205   7603   6303    339    167   -312       C  
ATOM   2111  CZ3 TRP A 323      34.087   9.448  24.610  1.00 57.29           C  
ANISOU 2111  CZ3 TRP A 323     7459   7806   6501    307     83   -328       C  
ATOM   2112  CH2 TRP A 323      32.821   9.895  25.013  1.00 58.80           C  
ANISOU 2112  CH2 TRP A 323     7645   8018   6677    336    129   -333       C  
ATOM   2113  N   ASN A 324      32.760   5.663  18.586  1.00 48.09           N  
ANISOU 2113  N   ASN A 324     6152   6533   5588    175    136   -127       N  
ATOM   2114  CA  ASN A 324      31.565   5.078  17.990  1.00 45.61           C  
ANISOU 2114  CA  ASN A 324     5801   6221   5309    163    170    -89       C  
ATOM   2115  C   ASN A 324      31.564   3.564  18.062  1.00 42.51           C  
ANISOU 2115  C   ASN A 324     5392   5833   4925    135    182    -24       C  
ATOM   2116  O   ASN A 324      30.507   2.956  18.252  1.00 39.33           O  
ANISOU 2116  O   ASN A 324     4961   5455   4526    131    220     15       O  
ATOM   2117  CB  ASN A 324      31.345   5.565  16.554  1.00 43.61           C  
ANISOU 2117  CB  ASN A 324     5533   5918   5119    150    155   -107       C  
ATOM   2118  CG  ASN A 324      30.520   6.829  16.500  1.00 43.22           C  
ANISOU 2118  CG  ASN A 324     5480   5873   5068    183    169   -148       C  
ATOM   2119  OD1 ASN A 324      30.510   7.602  17.455  1.00 41.96           O  
ANISOU 2119  OD1 ASN A 324     5340   5739   4863    216    177   -181       O  
ATOM   2120  ND2 ASN A 324      29.812   7.043  15.389  1.00 42.19           N  
ANISOU 2120  ND2 ASN A 324     5326   5720   4987    178    170   -146       N  
ATOM   2121  N   ARG A 325      32.752   2.974  17.925  1.00 28.15           N  
ANISOU 2121  N   ARG A 325     3592   3990   3114    116    149    -13       N  
ATOM   2122  CA  ARG A 325      32.916   1.528  18.026  1.00 31.79           C  
ANISOU 2122  CA  ARG A 325     4046   4448   3586     93    156     47       C  
ATOM   2123  C   ARG A 325      32.674   1.031  19.467  1.00 36.29           C  
ANISOU 2123  C   ARG A 325     4623   5073   4091    112    185     85       C  
ATOM   2124  O   ARG A 325      32.064  -0.022  19.674  1.00 40.86           O  
ANISOU 2124  O   ARG A 325     5184   5660   4679     97    217    144       O  
ATOM   2125  CB  ARG A 325      34.292   1.090  17.476  1.00 26.38           C  
ANISOU 2125  CB  ARG A 325     3375   3720   2926     76    114     46       C  
ATOM   2126  CG  ARG A 325      34.685  -0.342  17.803  1.00 31.85           C  
ANISOU 2126  CG  ARG A 325     4070   4409   3622     62    116    104       C  
ATOM   2127  CD  ARG A 325      35.650  -0.915  16.765  1.00 34.03           C  
ANISOU 2127  CD  ARG A 325     4348   4632   3951     40     84    105       C  
ATOM   2128  NE  ARG A 325      34.909  -1.453  15.629  1.00 47.50           N  
ANISOU 2128  NE  ARG A 325     6031   6300   5715     12     96    117       N  
ATOM   2129  CZ  ARG A 325      34.878  -2.738  15.287  1.00 48.46           C  
ANISOU 2129  CZ  ARG A 325     6147   6393   5874    -10    101    158       C  
ATOM   2130  NH1 ARG A 325      35.574  -3.630  15.973  1.00 36.73           N  
ANISOU 2130  NH1 ARG A 325     4675   4906   4373     -6     97    197       N  
ATOM   2131  NH2 ARG A 325      34.166  -3.128  14.237  1.00 59.45           N  
ANISOU 2131  NH2 ARG A 325     7518   7752   7317    -35    106    158       N  
ATOM   2132  N   ALA A 326      33.122   1.806  20.454  1.00 34.15           N  
ANISOU 2132  N   ALA A 326     4380   4840   3756    146    176     53       N  
ATOM   2133  CA  ALA A 326      32.931   1.454  21.865  1.00 33.63           C  
ANISOU 2133  CA  ALA A 326     4328   4835   3614    172    203     85       C  
ATOM   2134  C   ALA A 326      31.467   1.502  22.301  1.00 40.74           C  
ANISOU 2134  C   ALA A 326     5205   5779   4498    185    263    107       C  
ATOM   2135  O   ALA A 326      31.043   0.693  23.133  1.00 41.86           O  
ANISOU 2135  O   ALA A 326     5343   5949   4614    186    297    163       O  
ATOM   2136  CB  ALA A 326      33.778   2.339  22.769  1.00 26.56           C  
ANISOU 2136  CB  ALA A 326     3469   3971   2651    206    171     34       C  
ATOM   2137  N   TYR A 327      30.695   2.437  21.742  1.00 39.51           N  
ANISOU 2137  N   TYR A 327     5030   5615   4367    193    274     64       N  
ATOM   2138  CA  TYR A 327      29.301   2.609  22.162  1.00 42.58           C  
ANISOU 2138  CA  TYR A 327     5391   6041   4748    208    329     77       C  
ATOM   2139  C   TYR A 327      28.305   2.264  21.075  1.00 43.89           C  
ANISOU 2139  C   TYR A 327     5507   6185   4985    180    350    100       C  
ATOM   2140  O   TYR A 327      27.102   2.403  21.278  1.00 41.24           O  
ANISOU 2140  O   TYR A 327     5137   5883   4651    192    396    112       O  
ATOM   2141  CB  TYR A 327      29.043   4.042  22.642  1.00 49.71           C  
ANISOU 2141  CB  TYR A 327     6311   6952   5626    247    324      9       C  
ATOM   2142  CG  TYR A 327      30.019   4.507  23.693  1.00 52.77           C  
ANISOU 2142  CG  TYR A 327     6746   7347   5958    268    292    -24       C  
ATOM   2143  CD1 TYR A 327      30.072   3.888  24.940  1.00 50.51           C  
ANISOU 2143  CD1 TYR A 327     6474   7097   5620    278    307     13       C  
ATOM   2144  CD2 TYR A 327      30.893   5.561  23.439  1.00 52.08           C  
ANISOU 2144  CD2 TYR A 327     6685   7229   5872    277    244    -92       C  
ATOM   2145  CE1 TYR A 327      30.967   4.304  25.902  1.00 57.02           C  
ANISOU 2145  CE1 TYR A 327     7339   7933   6393    297    274    -19       C  
ATOM   2146  CE2 TYR A 327      31.793   5.985  24.397  1.00 54.23           C  
ANISOU 2146  CE2 TYR A 327     6995   7509   6100    291    211   -124       C  
ATOM   2147  CZ  TYR A 327      31.827   5.353  25.627  1.00 60.68           C  
ANISOU 2147  CZ  TYR A 327     7825   8367   6862    303    224    -89       C  
ATOM   2148  OH  TYR A 327      32.721   5.767  26.588  1.00 64.66           O  
ANISOU 2148  OH  TYR A 327     8364   8882   7320    318    188   -123       O  
ATOM   2149  N   GLY A 328      28.803   1.833  19.917  1.00 44.56           N  
ANISOU 2149  N   GLY A 328     5587   6210   5135    143    313    101       N  
ATOM   2150  CA  GLY A 328      27.937   1.473  18.806  1.00 41.61           C  
ANISOU 2150  CA  GLY A 328     5169   5807   4835    112    320    116       C  
ATOM   2151  C   GLY A 328      27.315   0.103  18.985  1.00 48.05           C  
ANISOU 2151  C   GLY A 328     5953   6629   5676     78    353    187       C  
ATOM   2152  O   GLY A 328      27.749  -0.667  19.851  1.00 46.32           O  
ANISOU 2152  O   GLY A 328     5752   6425   5421     76    367    231       O  
ATOM   2153  N   PRO A 329      26.301  -0.218  18.162  1.00 49.58           N  
ANISOU 2153  N   PRO A 329     6097   6808   5932     51    365    200       N  
ATOM   2154  CA  PRO A 329      25.814   0.632  17.067  1.00 49.97           C  
ANISOU 2154  CA  PRO A 329     6125   6838   6022     56    344    152       C  
ATOM   2155  C   PRO A 329      24.780   1.654  17.525  1.00 50.29           C  
ANISOU 2155  C   PRO A 329     6140   6929   6039     96    379    130       C  
ATOM   2156  O   PRO A 329      24.310   2.442  16.700  1.00 43.32           O  
ANISOU 2156  O   PRO A 329     5239   6035   5186    108    364     93       O  
ATOM   2157  CB  PRO A 329      25.113  -0.377  16.155  1.00 46.49           C  
ANISOU 2157  CB  PRO A 329     5639   6369   5655      8    342    183       C  
ATOM   2158  CG  PRO A 329      24.520  -1.361  17.122  1.00 43.72           C  
ANISOU 2158  CG  PRO A 329     5264   6050   5299     -9    392    248       C  
ATOM   2159  CD  PRO A 329      25.559  -1.493  18.230  1.00 46.50           C  
ANISOU 2159  CD  PRO A 329     5669   6417   5583     12    397    265       C  
ATOM   2160  N   ALA A 330      24.432   1.629  18.810  1.00 54.92           N  
ANISOU 2160  N   ALA A 330     6725   7571   6569    121    427    154       N  
ATOM   2161  CA  ALA A 330      23.240   2.319  19.307  1.00 63.13           C  
ANISOU 2161  CA  ALA A 330     7728   8665   7591    157    475    146       C  
ATOM   2162  C   ALA A 330      23.530   3.698  19.886  1.00 57.91           C  
ANISOU 2162  C   ALA A 330     7109   8021   6874    213    469     84       C  
ATOM   2163  O   ALA A 330      22.611   4.441  20.230  1.00 58.53           O  
ANISOU 2163  O   ALA A 330     7170   8120   6950    245    493     64       O  
ATOM   2164  CB  ALA A 330      22.531   1.451  20.355  1.00 68.12           C  
ANISOU 2164  CB  ALA A 330     8340   9332   8212    145    526    206       C  
ATOM   2165  N   GLY A 331      24.811   4.032  19.995  1.00 52.23           N  
ANISOU 2165  N   GLY A 331     6446   7281   6119    222    431     53       N  
ATOM   2166  CA  GLY A 331      25.213   5.245  20.676  1.00 41.95           C  
ANISOU 2166  CA  GLY A 331     5189   5978   4771    265    415     -6       C  
ATOM   2167  C   GLY A 331      25.205   6.479  19.800  1.00 35.17           C  
ANISOU 2167  C   GLY A 331     4335   5089   3939    288    389    -68       C  
ATOM   2168  O   GLY A 331      24.557   7.478  20.126  1.00 32.66           O  
ANISOU 2168  O   GLY A 331     4017   4777   3616    325    401   -102       O  
ATOM   2169  N   PHE A 332      25.928   6.419  18.687  1.00 30.45           N  
ANISOU 2169  N   PHE A 332     3747   4440   3384    260    344    -78       N  
ATOM   2170  CA  PHE A 332      26.252   7.636  17.946  1.00 30.39           C  
ANISOU 2170  CA  PHE A 332     3760   4387   3400    278    310   -134       C  
ATOM   2171  C   PHE A 332      26.233   7.463  16.434  1.00 31.81           C  
ANISOU 2171  C   PHE A 332     3920   4516   3650    247    278   -126       C  
ATOM   2172  O   PHE A 332      26.604   6.419  15.911  1.00 32.89           O  
ANISOU 2172  O   PHE A 332     4049   4634   3814    204    263    -91       O  
ATOM   2173  CB  PHE A 332      27.624   8.166  18.377  1.00 25.79           C  
ANISOU 2173  CB  PHE A 332     3234   3781   2782    284    273   -175       C  
ATOM   2174  CG  PHE A 332      27.700   8.525  19.820  1.00 31.96           C  
ANISOU 2174  CG  PHE A 332     4044   4601   3500    314    289   -194       C  
ATOM   2175  CD1 PHE A 332      27.474   9.832  20.232  1.00 36.13           C  
ANISOU 2175  CD1 PHE A 332     4593   5115   4021    349    285   -246       C  
ATOM   2176  CD2 PHE A 332      27.986   7.556  20.776  1.00 32.95           C  
ANISOU 2176  CD2 PHE A 332     4177   4761   3583    302    301   -153       C  
ATOM   2177  CE1 PHE A 332      27.529  10.168  21.570  1.00 33.38           C  
ANISOU 2177  CE1 PHE A 332     4270   4789   3622    370    293   -263       C  
ATOM   2178  CE2 PHE A 332      28.032   7.877  22.113  1.00 34.56           C  
ANISOU 2178  CE2 PHE A 332     4407   4990   3735    325    308   -167       C  
ATOM   2179  CZ  PHE A 332      27.811   9.189  22.514  1.00 38.40           C  
ANISOU 2179  CZ  PHE A 332     4912   5465   4212    359    304   -224       C  
ATOM   2180  N   LEU A 333      25.802   8.507  15.739  1.00 32.80           N  
ANISOU 2180  N   LEU A 333     4041   4620   3803    272    269   -159       N  
ATOM   2181  CA  LEU A 333      25.845   8.524  14.285  1.00 27.40           C  
ANISOU 2181  CA  LEU A 333     3346   3889   3175    251    236   -156       C  
ATOM   2182  C   LEU A 333      26.810   9.610  13.841  1.00 28.14           C  
ANISOU 2182  C   LEU A 333     3486   3931   3273    262    202   -199       C  
ATOM   2183  O   LEU A 333      26.596  10.793  14.125  1.00 25.70           O  
ANISOU 2183  O   LEU A 333     3194   3617   2954    304    207   -237       O  
ATOM   2184  CB  LEU A 333      24.457   8.780  13.693  1.00 28.08           C  
ANISOU 2184  CB  LEU A 333     3382   3992   3295    270    252   -149       C  
ATOM   2185  CG  LEU A 333      24.372   8.774  12.162  1.00 27.41           C  
ANISOU 2185  CG  LEU A 333     3285   3869   3262    253    216   -144       C  
ATOM   2186  CD1 LEU A 333      24.513   7.364  11.619  1.00 22.67           C  
ANISOU 2186  CD1 LEU A 333     2664   3263   2686    199    202   -106       C  
ATOM   2187  CD2 LEU A 333      23.076   9.406  11.685  1.00 31.70           C  
ANISOU 2187  CD2 LEU A 333     3785   4429   3831    288    225   -149       C  
ATOM   2188  N   GLN A 334      27.882   9.187  13.173  1.00 14.03           N  
ANISOU 2188  N   GLN A 334     1721   2106   1505    226    169   -191       N  
ATOM   2189  CA  GLN A 334      28.848  10.089  12.579  1.00 18.20           C  
ANISOU 2189  CA  GLN A 334     2287   2582   2048    227    138   -222       C  
ATOM   2190  C   GLN A 334      28.206  10.680  11.337  1.00 25.89           C  
ANISOU 2190  C   GLN A 334     3246   3528   3062    240    129   -222       C  
ATOM   2191  O   GLN A 334      27.340  10.053  10.726  1.00 30.79           O  
ANISOU 2191  O   GLN A 334     3830   4167   3703    233    133   -194       O  
ATOM   2192  CB  GLN A 334      30.123   9.334  12.191  1.00 21.69           C  
ANISOU 2192  CB  GLN A 334     2746   2997   2498    185    111   -207       C  
ATOM   2193  CG  GLN A 334      29.972   8.424  10.959  1.00 31.96           C  
ANISOU 2193  CG  GLN A 334     4025   4283   3836    155    100   -173       C  
ATOM   2194  CD  GLN A 334      29.061   7.207  11.180  1.00 36.23           C  
ANISOU 2194  CD  GLN A 334     4526   4861   4377    140    120   -136       C  
ATOM   2195  OE1 GLN A 334      28.976   6.665  12.293  1.00 32.74           O  
ANISOU 2195  OE1 GLN A 334     4080   4453   3906    139    141   -122       O  
ATOM   2196  NE2 GLN A 334      28.381   6.770  10.107  1.00 25.30           N  
ANISOU 2196  NE2 GLN A 334     3114   3470   3028    127    112   -120       N  
ATOM   2197  N   TYR A 335      28.613  11.892  10.976  1.00 23.36           N  
ANISOU 2197  N   TYR A 335     2956   3166   2754    260    115   -252       N  
ATOM   2198  CA  TYR A 335      28.055  12.572   9.817  1.00 24.98           C  
ANISOU 2198  CA  TYR A 335     3155   3344   2994    280    105   -249       C  
ATOM   2199  C   TYR A 335      29.067  13.565   9.274  1.00 23.03           C  
ANISOU 2199  C   TYR A 335     2950   3035   2764    279     84   -268       C  
ATOM   2200  O   TYR A 335      29.404  14.538   9.937  1.00 27.08           O  
ANISOU 2200  O   TYR A 335     3491   3526   3271    299     86   -304       O  
ATOM   2201  CB  TYR A 335      26.746  13.289  10.178  1.00 22.42           C  
ANISOU 2201  CB  TYR A 335     2807   3044   2667    330    129   -262       C  
ATOM   2202  CG  TYR A 335      25.965  13.781   8.969  1.00 23.09           C  
ANISOU 2202  CG  TYR A 335     2874   3113   2786    354    118   -249       C  
ATOM   2203  CD1 TYR A 335      25.133  12.918   8.258  1.00 26.26           C  
ANISOU 2203  CD1 TYR A 335     3230   3545   3202    341    113   -217       C  
ATOM   2204  CD2 TYR A 335      26.066  15.101   8.537  1.00 18.33           C  
ANISOU 2204  CD2 TYR A 335     2301   2462   2201    388    109   -269       C  
ATOM   2205  CE1 TYR A 335      24.412  13.356   7.153  1.00 25.92           C  
ANISOU 2205  CE1 TYR A 335     3169   3494   3185    366     97   -206       C  
ATOM   2206  CE2 TYR A 335      25.365  15.550   7.429  1.00 18.34           C  
ANISOU 2206  CE2 TYR A 335     2288   2451   2229    414     97   -252       C  
ATOM   2207  CZ  TYR A 335      24.530  14.674   6.743  1.00 26.79           C  
ANISOU 2207  CZ  TYR A 335     3311   3560   3307    405     89   -221       C  
ATOM   2208  OH  TYR A 335      23.818  15.108   5.648  1.00 23.56           O  
ANISOU 2208  OH  TYR A 335     2886   3146   2920    434     72   -205       O  
ATOM   2209  N   GLN A 336      29.537  13.308   8.061  1.00 18.99           N  
ANISOU 2209  N   GLN A 336     2443   2497   2277    256     65   -245       N  
ATOM   2210  CA  GLN A 336      30.556  14.131   7.430  1.00 21.42           C  
ANISOU 2210  CA  GLN A 336     2786   2746   2605    248     50   -252       C  
ATOM   2211  C   GLN A 336      30.068  14.710   6.103  1.00 20.44           C  
ANISOU 2211  C   GLN A 336     2664   2596   2506    269     43   -233       C  
ATOM   2212  O   GLN A 336      29.446  14.019   5.295  1.00 17.24           O  
ANISOU 2212  O   GLN A 336     2233   2215   2102    267     37   -206       O  
ATOM   2213  CB  GLN A 336      31.855  13.328   7.220  1.00 13.90           C  
ANISOU 2213  CB  GLN A 336     1844   1784   1654    202     37   -240       C  
ATOM   2214  CG  GLN A 336      32.945  14.151   6.555  1.00 15.88           C  
ANISOU 2214  CG  GLN A 336     2125   1978   1930    190     26   -243       C  
ATOM   2215  CD  GLN A 336      34.328  13.556   6.683  1.00 22.00           C  
ANISOU 2215  CD  GLN A 336     2908   2746   2707    150     16   -241       C  
ATOM   2216  OE1 GLN A 336      34.528  12.493   7.285  1.00 22.69           O  
ANISOU 2216  OE1 GLN A 336     2980   2868   2773    132     15   -237       O  
ATOM   2217  NE2 GLN A 336      35.306  14.252   6.118  1.00 18.12           N  
ANISOU 2217  NE2 GLN A 336     2435   2207   2242    136     10   -242       N  
ATOM   2218  N   PHE A 337      30.347  15.988   5.886  1.00 17.82           N  
ANISOU 2218  N   PHE A 337     2362   2214   2195    290     41   -246       N  
ATOM   2219  CA  PHE A 337      29.984  16.626   4.628  1.00 23.58           C  
ANISOU 2219  CA  PHE A 337     3099   2914   2945    313     34   -221       C  
ATOM   2220  C   PHE A 337      30.927  17.781   4.298  1.00 18.93           C  
ANISOU 2220  C   PHE A 337     2553   2256   2385    311     32   -226       C  
ATOM   2221  O   PHE A 337      31.617  18.310   5.172  1.00 17.15           O  
ANISOU 2221  O   PHE A 337     2348   2003   2167    300     35   -259       O  
ATOM   2222  CB  PHE A 337      28.521  17.100   4.665  1.00 21.75           C  
ANISOU 2222  CB  PHE A 337     2846   2705   2716    365     41   -223       C  
ATOM   2223  CG  PHE A 337      28.262  18.191   5.671  1.00 22.29           C  
ANISOU 2223  CG  PHE A 337     2930   2751   2789    402     55   -262       C  
ATOM   2224  CD1 PHE A 337      28.385  19.535   5.314  1.00 23.55           C  
ANISOU 2224  CD1 PHE A 337     3123   2847   2978    432     54   -268       C  
ATOM   2225  CD2 PHE A 337      27.910  17.879   6.971  1.00 21.17           C  
ANISOU 2225  CD2 PHE A 337     2772   2650   2623    408     71   -292       C  
ATOM   2226  CE1 PHE A 337      28.154  20.535   6.240  1.00 24.04           C  
ANISOU 2226  CE1 PHE A 337     3204   2884   3047    467     65   -310       C  
ATOM   2227  CE2 PHE A 337      27.676  18.877   7.913  1.00 19.03           C  
ANISOU 2227  CE2 PHE A 337     2519   2361   2351    445     84   -334       C  
ATOM   2228  CZ  PHE A 337      27.799  20.201   7.551  1.00 20.72           C  
ANISOU 2228  CZ  PHE A 337     2768   2509   2597    475     80   -347       C  
ATOM   2229  N   VAL A 338      30.971  18.150   3.024  1.00 19.79           N  
ANISOU 2229  N   VAL A 338     2674   2337   2509    319     27   -192       N  
ATOM   2230  CA  VAL A 338      31.759  19.291   2.577  1.00 16.61           C  
ANISOU 2230  CA  VAL A 338     2310   1864   2138    318     30   -185       C  
ATOM   2231  C   VAL A 338      30.868  20.176   1.720  1.00 23.66           C  
ANISOU 2231  C   VAL A 338     3212   2733   3043    369     30   -160       C  
ATOM   2232  O   VAL A 338      30.116  19.676   0.891  1.00 18.96           O  
ANISOU 2232  O   VAL A 338     2597   2175   2430    387     21   -131       O  
ATOM   2233  CB  VAL A 338      33.021  18.865   1.767  1.00 16.52           C  
ANISOU 2233  CB  VAL A 338     2310   1836   2132    273     29   -157       C  
ATOM   2234  CG1 VAL A 338      32.654  17.955   0.610  1.00  9.51           C  
ANISOU 2234  CG1 VAL A 338     1406    987   1219    275     23   -119       C  
ATOM   2235  CG2 VAL A 338      33.788  20.096   1.261  1.00 16.37           C  
ANISOU 2235  CG2 VAL A 338     2327   1741   2152    270     37   -143       C  
ATOM   2236  N   ILE A 339      30.935  21.483   1.957  1.00 22.94           N  
ANISOU 2236  N   ILE A 339     3152   2580   2986    393     36   -173       N  
ATOM   2237  CA  ILE A 339      30.196  22.481   1.191  1.00 21.83           C  
ANISOU 2237  CA  ILE A 339     3027   2404   2864    445     37   -146       C  
ATOM   2238  C   ILE A 339      31.209  23.306   0.391  1.00 22.08           C  
ANISOU 2238  C   ILE A 339     3099   2361   2928    428     44   -114       C  
ATOM   2239  O   ILE A 339      32.217  23.730   0.940  1.00 20.68           O  
ANISOU 2239  O   ILE A 339     2942   2135   2779    392     50   -137       O  
ATOM   2240  CB  ILE A 339      29.425  23.419   2.137  1.00 21.20           C  
ANISOU 2240  CB  ILE A 339     2953   2302   2801    493     43   -187       C  
ATOM   2241  CG1 ILE A 339      28.486  22.621   3.050  1.00 15.28           C  
ANISOU 2241  CG1 ILE A 339     2160   1628   2018    508     45   -218       C  
ATOM   2242  CG2 ILE A 339      28.674  24.510   1.365  1.00 20.47           C  
ANISOU 2242  CG2 ILE A 339     2879   2166   2733    554     43   -157       C  
ATOM   2243  CD1 ILE A 339      27.504  21.754   2.326  1.00 13.47           C  
ANISOU 2243  CD1 ILE A 339     1888   1465   1763    525     35   -184       C  
ATOM   2244  N   PRO A 340      30.956  23.513  -0.915  1.00 18.98           N  
ANISOU 2244  N   PRO A 340     2718   1962   2533    451     42    -59       N  
ATOM   2245  CA  PRO A 340      31.879  24.259  -1.783  1.00 22.59           C  
ANISOU 2245  CA  PRO A 340     3213   2352   3018    436     55    -16       C  
ATOM   2246  C   PRO A 340      32.234  25.613  -1.193  1.00 27.50           C  
ANISOU 2246  C   PRO A 340     3869   2883   3696    441     65    -36       C  
ATOM   2247  O   PRO A 340      31.355  26.274  -0.628  1.00 25.52           O  
ANISOU 2247  O   PRO A 340     3622   2617   3459    488     62    -64       O  
ATOM   2248  CB  PRO A 340      31.077  24.445  -3.081  1.00 18.86           C  
ANISOU 2248  CB  PRO A 340     2748   1893   2526    486     49     42       C  
ATOM   2249  CG  PRO A 340      30.138  23.293  -3.103  1.00 21.30           C  
ANISOU 2249  CG  PRO A 340     3013   2292   2787    499     29     30       C  
ATOM   2250  CD  PRO A 340      29.775  23.032  -1.655  1.00 22.19           C  
ANISOU 2250  CD  PRO A 340     3099   2427   2906    494     28    -32       C  
ATOM   2251  N   THR A 341      33.506  25.989  -1.316  1.00 25.83           N  
ANISOU 2251  N   THR A 341     3680   2616   3520    392     78    -26       N  
ATOM   2252  CA  THR A 341      34.060  27.222  -0.757  1.00 30.12           C  
ANISOU 2252  CA  THR A 341     4254   3065   4125    381     86    -50       C  
ATOM   2253  C   THR A 341      33.159  28.439  -0.926  1.00 32.65           C  
ANISOU 2253  C   THR A 341     4596   3333   4475    440     86    -39       C  
ATOM   2254  O   THR A 341      32.931  29.194   0.023  1.00 36.39           O  
ANISOU 2254  O   THR A 341     5070   3776   4981    447     79    -91       O  
ATOM   2255  CB  THR A 341      35.392  27.572  -1.450  1.00 34.50           C  
ANISOU 2255  CB  THR A 341     4827   3563   4718    329    105     -8       C  
ATOM   2256  OG1 THR A 341      36.206  26.395  -1.571  1.00 30.58           O  
ANISOU 2256  OG1 THR A 341     4301   3126   4191    279    105     -4       O  
ATOM   2257  CG2 THR A 341      36.138  28.676  -0.684  1.00 31.52           C  
ANISOU 2257  CG2 THR A 341     4466   3100   4409    296    103    -46       C  
ATOM   2258  N   GLU A 342      32.654  28.622  -2.144  1.00 29.58           N  
ANISOU 2258  N   GLU A 342     4215   2952   4073    475     89     27       N  
ATOM   2259  CA  GLU A 342      31.894  29.819  -2.496  1.00 31.19           C  
ANISOU 2259  CA  GLU A 342     4429   3115   4306    521     85     50       C  
ATOM   2260  C   GLU A 342      30.531  29.862  -1.811  1.00 33.87           C  
ANISOU 2260  C   GLU A 342     4746   3493   4631    578     72      9       C  
ATOM   2261  O   GLU A 342      29.882  30.905  -1.786  1.00 39.32           O  
ANISOU 2261  O   GLU A 342     5441   4146   5354    616     69     10       O  
ATOM   2262  CB  GLU A 342      31.727  29.928  -4.020  1.00 27.35           C  
ANISOU 2262  CB  GLU A 342     3955   2636   3799    543     90    134       C  
ATOM   2263  N   ALA A 343      30.104  28.728  -1.258  1.00 26.27           N  
ANISOU 2263  N   ALA A 343     3755   2606   3622    584     66    -25       N  
ATOM   2264  CA  ALA A 343      28.803  28.617  -0.596  1.00 23.79           C  
ANISOU 2264  CA  ALA A 343     3409   2342   3288    634     57    -61       C  
ATOM   2265  C   ALA A 343      28.933  28.723   0.922  1.00 26.44           C  
ANISOU 2265  C   ALA A 343     3737   2674   3636    617     62   -139       C  
ATOM   2266  O   ALA A 343      28.275  28.006   1.677  1.00 28.99           O  
ANISOU 2266  O   ALA A 343     4029   3064   3924    632     60   -176       O  
ATOM   2267  CB  ALA A 343      28.110  27.316  -0.995  1.00 20.74           C  
ANISOU 2267  CB  ALA A 343     2988   2048   2842    654     45    -46       C  
ATOM   2268  N   VAL A 344      29.782  29.643   1.356  1.00 30.19           N  
ANISOU 2268  N   VAL A 344     4239   3072   4161    585     68   -163       N  
ATOM   2269  CA  VAL A 344      30.088  29.815   2.767  1.00 31.06           C  
ANISOU 2269  CA  VAL A 344     4348   3174   4280    563     71   -237       C  
ATOM   2270  C   VAL A 344      28.854  30.197   3.597  1.00 33.30           C  
ANISOU 2270  C   VAL A 344     4612   3486   4555    616     78   -277       C  
ATOM   2271  O   VAL A 344      28.706  29.775   4.748  1.00 33.01           O  
ANISOU 2271  O   VAL A 344     4560   3493   4488    611     82   -331       O  
ATOM   2272  CB  VAL A 344      31.242  30.840   2.944  1.00 39.79           C  
ANISOU 2272  CB  VAL A 344     5483   4185   5450    517     74   -253       C  
ATOM   2273  CG1 VAL A 344      30.884  32.179   2.308  1.00 33.43           C  
ANISOU 2273  CG1 VAL A 344     4696   3304   4701    550     76   -221       C  
ATOM   2274  CG2 VAL A 344      31.606  30.998   4.404  1.00 41.73           C  
ANISOU 2274  CG2 VAL A 344     5730   4428   5697    492     78   -331       C  
ATOM   2275  N   ASP A 345      27.953  30.971   3.004  1.00 34.29           N  
ANISOU 2275  N   ASP A 345     4737   3589   4703    669     80   -246       N  
ATOM   2276  CA  ASP A 345      26.714  31.348   3.685  1.00 37.58           C  
ANISOU 2276  CA  ASP A 345     5133   4034   5114    724     88   -278       C  
ATOM   2277  C   ASP A 345      25.809  30.144   3.943  1.00 32.05           C  
ANISOU 2277  C   ASP A 345     4386   3438   4352    745     87   -281       C  
ATOM   2278  O   ASP A 345      25.274  29.978   5.041  1.00 33.81           O  
ANISOU 2278  O   ASP A 345     4589   3703   4553    759     99   -329       O  
ATOM   2279  CB  ASP A 345      25.966  32.408   2.880  1.00 50.46           C  
ANISOU 2279  CB  ASP A 345     6770   5619   6784    777     87   -238       C  
ATOM   2280  CG  ASP A 345      26.208  33.812   3.401  1.00 63.36           C  
ANISOU 2280  CG  ASP A 345     8433   7160   8480    781     97   -271       C  
ATOM   2281  OD1 ASP A 345      27.275  34.061   4.010  1.00 61.58           O  
ANISOU 2281  OD1 ASP A 345     8232   6888   8279    731    102   -309       O  
ATOM   2282  OD2 ASP A 345      25.320  34.669   3.203  1.00 71.26           O  
ANISOU 2282  OD2 ASP A 345     9431   8135   9509    836    100   -261       O  
ATOM   2283  N   GLU A 346      25.647  29.309   2.923  1.00 28.90           N  
ANISOU 2283  N   GLU A 346     3971   3083   3927    747     74   -229       N  
ATOM   2284  CA  GLU A 346      24.907  28.062   3.055  1.00 36.14           C  
ANISOU 2284  CA  GLU A 346     4841   4098   4793    758     70   -229       C  
ATOM   2285  C   GLU A 346      25.543  27.175   4.118  1.00 38.75           C  
ANISOU 2285  C   GLU A 346     5165   4465   5093    713     77   -276       C  
ATOM   2286  O   GLU A 346      24.846  26.470   4.857  1.00 35.07           O  
ANISOU 2286  O   GLU A 346     4661   4071   4594    724     85   -299       O  
ATOM   2287  CB  GLU A 346      24.867  27.323   1.721  1.00 33.46           C  
ANISOU 2287  CB  GLU A 346     4492   3789   4433    759     52   -169       C  
ATOM   2288  CG  GLU A 346      24.022  27.999   0.662  1.00 46.95           C  
ANISOU 2288  CG  GLU A 346     6195   5486   6156    810     41   -119       C  
ATOM   2289  CD  GLU A 346      24.794  29.027  -0.154  1.00 58.84           C  
ANISOU 2289  CD  GLU A 346     7752   6904   7700    801     40    -81       C  
ATOM   2290  OE1 GLU A 346      24.559  29.096  -1.382  1.00 62.99           O  
ANISOU 2290  OE1 GLU A 346     8281   7433   8218    822     27    -22       O  
ATOM   2291  OE2 GLU A 346      25.626  29.764   0.425  1.00 54.30           O  
ANISOU 2291  OE2 GLU A 346     7210   6258   7161    773     53   -109       O  
ATOM   2292  N   PHE A 347      26.870  27.219   4.193  1.00 34.59           N  
ANISOU 2292  N   PHE A 347     4674   3890   4578    661     73   -286       N  
ATOM   2293  CA  PHE A 347      27.593  26.454   5.190  1.00 27.43           C  
ANISOU 2293  CA  PHE A 347     3765   3014   3644    616     75   -328       C  
ATOM   2294  C   PHE A 347      27.273  26.939   6.615  1.00 28.83           C  
ANISOU 2294  C   PHE A 347     3940   3199   3816    625     89   -388       C  
ATOM   2295  O   PHE A 347      27.019  26.131   7.509  1.00 26.53           O  
ANISOU 2295  O   PHE A 347     3624   2975   3482    620     96   -415       O  
ATOM   2296  CB  PHE A 347      29.098  26.499   4.924  1.00 29.79           C  
ANISOU 2296  CB  PHE A 347     4100   3257   3964    558     66   -325       C  
ATOM   2297  CG  PHE A 347      29.917  25.912   6.037  1.00 31.58           C  
ANISOU 2297  CG  PHE A 347     4325   3507   4167    511     63   -373       C  
ATOM   2298  CD1 PHE A 347      29.948  24.532   6.238  1.00 27.31           C  
ANISOU 2298  CD1 PHE A 347     3757   3039   3579    494     58   -373       C  
ATOM   2299  CD2 PHE A 347      30.641  26.733   6.894  1.00 26.84           C  
ANISOU 2299  CD2 PHE A 347     3749   2857   3592    484     63   -419       C  
ATOM   2300  CE1 PHE A 347      30.689  23.981   7.273  1.00 26.23           C  
ANISOU 2300  CE1 PHE A 347     3618   2929   3419    453     53   -412       C  
ATOM   2301  CE2 PHE A 347      31.382  26.190   7.931  1.00 30.60           C  
ANISOU 2301  CE2 PHE A 347     4222   3363   4040    443     55   -461       C  
ATOM   2302  CZ  PHE A 347      31.406  24.813   8.122  1.00 28.28           C  
ANISOU 2302  CZ  PHE A 347     3902   3144   3698    429     50   -455       C  
ATOM   2303  N   LYS A 348      27.285  28.254   6.819  1.00 28.82           N  
ANISOU 2303  N   LYS A 348     3967   3129   3856    641     95   -408       N  
ATOM   2304  CA  LYS A 348      26.871  28.842   8.103  1.00 32.22           C  
ANISOU 2304  CA  LYS A 348     4399   3563   4280    660    111   -464       C  
ATOM   2305  C   LYS A 348      25.455  28.424   8.488  1.00 30.18           C  
ANISOU 2305  C   LYS A 348     4098   3382   3988    711    126   -465       C  
ATOM   2306  O   LYS A 348      25.200  28.025   9.623  1.00 32.90           O  
ANISOU 2306  O   LYS A 348     4429   3779   4294    711    139   -502       O  
ATOM   2307  CB  LYS A 348      27.018  30.374   8.083  1.00 34.74           C  
ANISOU 2307  CB  LYS A 348     4755   3788   4657    675    116   -480       C  
ATOM   2308  CG  LYS A 348      28.485  30.828   8.119  1.00 41.79           C  
ANISOU 2308  CG  LYS A 348     5687   4608   5584    615    107   -496       C  
ATOM   2309  CD  LYS A 348      28.736  32.159   7.417  1.00 44.99           C  
ANISOU 2309  CD  LYS A 348     6123   4910   6062    622    110   -477       C  
ATOM   2310  CE  LYS A 348      28.264  33.330   8.255  1.00 55.61           C  
ANISOU 2310  CE  LYS A 348     7488   6212   7431    655    126   -526       C  
ATOM   2311  NZ  LYS A 348      29.058  34.566   7.987  1.00 58.70           N  
ANISOU 2311  NZ  LYS A 348     7919   6492   7891    632    131   -529       N  
ATOM   2312  N   LYS A 349      24.542  28.481   7.529  1.00 25.98           N  
ANISOU 2312  N   LYS A 349     3542   2859   3469    752    124   -420       N  
ATOM   2313  CA  LYS A 349      23.157  28.099   7.784  1.00 30.84           C  
ANISOU 2313  CA  LYS A 349     4109   3549   4061    798    138   -415       C  
ATOM   2314  C   LYS A 349      23.007  26.646   8.247  1.00 31.97           C  
ANISOU 2314  C   LYS A 349     4212   3783   4151    775    143   -416       C  
ATOM   2315  O   LYS A 349      22.244  26.364   9.167  1.00 33.08           O  
ANISOU 2315  O   LYS A 349     4322   3981   4265    794    164   -437       O  
ATOM   2316  CB  LYS A 349      22.267  28.398   6.567  1.00 42.48           C  
ANISOU 2316  CB  LYS A 349     5561   5019   5560    844    128   -364       C  
ATOM   2317  CG  LYS A 349      22.065  29.908   6.317  1.00 59.67           C  
ANISOU 2317  CG  LYS A 349     7769   7115   7789    882    131   -365       C  
ATOM   2318  CD  LYS A 349      21.084  30.179   5.174  1.00 66.35           C  
ANISOU 2318  CD  LYS A 349     8590   7967   8653    931    119   -311       C  
ATOM   2319  N   ILE A 350      23.744  25.732   7.626  1.00 28.72           N  
ANISOU 2319  N   ILE A 350     3801   3384   3727    735    125   -390       N  
ATOM   2320  CA  ILE A 350      23.715  24.336   8.039  1.00 28.61           C  
ANISOU 2320  CA  ILE A 350     3752   3449   3669    708    129   -389       C  
ATOM   2321  C   ILE A 350      24.225  24.173   9.474  1.00 30.10           C  
ANISOU 2321  C   ILE A 350     3955   3655   3827    682    143   -437       C  
ATOM   2322  O   ILE A 350      23.641  23.436  10.272  1.00 33.23           O  
ANISOU 2322  O   ILE A 350     4317   4122   4187    685    162   -444       O  
ATOM   2323  CB  ILE A 350      24.536  23.463   7.096  1.00 37.23           C  
ANISOU 2323  CB  ILE A 350     4849   4540   4756    670    108   -357       C  
ATOM   2324  CG1 ILE A 350      23.865  23.415   5.721  1.00 37.25           C  
ANISOU 2324  CG1 ILE A 350     4830   4547   4775    701     92   -307       C  
ATOM   2325  CG2 ILE A 350      24.723  22.057   7.681  1.00 36.83           C  
ANISOU 2325  CG2 ILE A 350     4769   4560   4663    636    113   -363       C  
ATOM   2326  CD1 ILE A 350      24.548  22.476   4.735  1.00 34.28           C  
ANISOU 2326  CD1 ILE A 350     4453   4181   4389    655     72   -268       C  
ATOM   2327  N   ILE A 351      25.301  24.876   9.803  1.00 21.22           N  
ANISOU 2327  N   ILE A 351     2879   2467   2717    655    134   -467       N  
ATOM   2328  CA  ILE A 351      25.813  24.865  11.163  1.00 26.77           C  
ANISOU 2328  CA  ILE A 351     3599   3183   3390    632    142   -514       C  
ATOM   2329  C   ILE A 351      24.751  25.376  12.142  1.00 34.09           C  
ANISOU 2329  C   ILE A 351     4513   4138   4301    678    169   -543       C  
ATOM   2330  O   ILE A 351      24.523  24.768  13.196  1.00 32.52           O  
ANISOU 2330  O   ILE A 351     4299   4001   4056    675    185   -560       O  
ATOM   2331  CB  ILE A 351      27.098  25.702  11.301  1.00 24.90           C  
ANISOU 2331  CB  ILE A 351     3413   2868   3181    597    124   -544       C  
ATOM   2332  CG1 ILE A 351      28.160  25.195  10.331  1.00 27.74           C  
ANISOU 2332  CG1 ILE A 351     3782   3200   3557    552    101   -513       C  
ATOM   2333  CG2 ILE A 351      27.623  25.624  12.727  1.00 23.71           C  
ANISOU 2333  CG2 ILE A 351     3278   2740   2992    575    126   -593       C  
ATOM   2334  CD1 ILE A 351      28.525  23.732  10.530  1.00 25.47           C  
ANISOU 2334  CD1 ILE A 351     3472   2981   3226    518     96   -502       C  
ATOM   2335  N   GLY A 352      24.099  26.483  11.779  1.00 32.17           N  
ANISOU 2335  N   GLY A 352     4276   3849   4096    722    175   -544       N  
ATOM   2336  CA  GLY A 352      23.022  27.040  12.581  1.00 32.52           C  
ANISOU 2336  CA  GLY A 352     4307   3917   4133    772    203   -570       C  
ATOM   2337  C   GLY A 352      21.890  26.049  12.797  1.00 29.57           C  
ANISOU 2337  C   GLY A 352     3873   3636   3725    793    225   -545       C  
ATOM   2338  O   GLY A 352      21.431  25.859  13.923  1.00 34.05           O  
ANISOU 2338  O   GLY A 352     4429   4253   4256    805    250   -570       O  
ATOM   2339  N   VAL A 353      21.455  25.408  11.717  1.00 27.63           N  
ANISOU 2339  N   VAL A 353     3591   3416   3493    795    215   -496       N  
ATOM   2340  CA  VAL A 353      20.430  24.367  11.782  1.00 30.31           C  
ANISOU 2340  CA  VAL A 353     3867   3842   3808    806    232   -468       C  
ATOM   2341  C   VAL A 353      20.849  23.217  12.701  1.00 28.14           C  
ANISOU 2341  C   VAL A 353     3582   3626   3482    765    244   -475       C  
ATOM   2342  O   VAL A 353      20.040  22.695  13.476  1.00 28.02           O  
ANISOU 2342  O   VAL A 353     3529   3678   3440    776    274   -473       O  
ATOM   2343  CB  VAL A 353      20.113  23.823  10.374  1.00 34.25           C  
ANISOU 2343  CB  VAL A 353     4332   4352   4330    805    210   -417       C  
ATOM   2344  CG1 VAL A 353      19.106  22.697  10.441  1.00 29.47           C  
ANISOU 2344  CG1 VAL A 353     3656   3835   3707    807    226   -389       C  
ATOM   2345  CG2 VAL A 353      19.590  24.939   9.505  1.00 40.20           C  
ANISOU 2345  CG2 VAL A 353     5091   5053   5128    851    199   -403       C  
ATOM   2346  N   ILE A 354      22.119  22.833  12.634  1.00 30.66           N  
ANISOU 2346  N   ILE A 354     3936   3921   3791    717    223   -480       N  
ATOM   2347  CA  ILE A 354      22.603  21.747  13.480  1.00 30.03           C  
ANISOU 2347  CA  ILE A 354     3852   3895   3664    678    230   -482       C  
ATOM   2348  C   ILE A 354      22.520  22.130  14.948  1.00 29.03           C  
ANISOU 2348  C   ILE A 354     3743   3786   3500    690    253   -523       C  
ATOM   2349  O   ILE A 354      22.010  21.362  15.763  1.00 31.69           O  
ANISOU 2349  O   ILE A 354     4051   4192   3799    690    280   -514       O  
ATOM   2350  CB  ILE A 354      24.040  21.327  13.141  1.00 27.12           C  
ANISOU 2350  CB  ILE A 354     3517   3494   3292    626    200   -483       C  
ATOM   2351  CG1 ILE A 354      24.061  20.479  11.868  1.00 27.66           C  
ANISOU 2351  CG1 ILE A 354     3559   3573   3379    609    184   -438       C  
ATOM   2352  CG2 ILE A 354      24.650  20.536  14.298  1.00 28.01           C  
ANISOU 2352  CG2 ILE A 354     3638   3650   3355    592    206   -496       C  
ATOM   2353  CD1 ILE A 354      25.460  20.132  11.370  1.00 17.90           C  
ANISOU 2353  CD1 ILE A 354     2355   2299   2147    562    156   -437       C  
ATOM   2354  N   GLN A 355      23.010  23.318  15.286  1.00 26.94           N  
ANISOU 2354  N   GLN A 355     3527   3460   3250    700    244   -566       N  
ATOM   2355  CA  GLN A 355      22.953  23.779  16.675  1.00 34.80           C  
ANISOU 2355  CA  GLN A 355     4544   4470   4209    716    263   -610       C  
ATOM   2356  C   GLN A 355      21.516  23.854  17.221  1.00 35.71           C  
ANISOU 2356  C   GLN A 355     4621   4638   4311    766    304   -608       C  
ATOM   2357  O   GLN A 355      21.260  23.472  18.362  1.00 32.44           O  
ANISOU 2357  O   GLN A 355     4200   4278   3847    771    329   -620       O  
ATOM   2358  CB  GLN A 355      23.668  25.123  16.837  1.00 33.73           C  
ANISOU 2358  CB  GLN A 355     4464   4252   4099    719    245   -659       C  
ATOM   2359  CG  GLN A 355      23.973  25.479  18.288  1.00 33.56           C  
ANISOU 2359  CG  GLN A 355     4474   4243   4034    722    253   -712       C  
ATOM   2360  CD  GLN A 355      22.764  26.042  19.015  1.00 33.90           C  
ANISOU 2360  CD  GLN A 355     4505   4313   4063    780    290   -733       C  
ATOM   2361  OE1 GLN A 355      21.899  26.656  18.395  1.00 30.93           O  
ANISOU 2361  OE1 GLN A 355     4112   3914   3728    820    303   -724       O  
ATOM   2362  NE2 GLN A 355      22.693  25.825  20.332  1.00 31.55           N  
ANISOU 2362  NE2 GLN A 355     4216   4066   3707    787    309   -761       N  
ATOM   2363  N   ALA A 356      20.587  24.332  16.394  1.00 35.44           N  
ANISOU 2363  N   ALA A 356     4558   4588   4319    804    311   -589       N  
ATOM   2364  CA  ALA A 356      19.197  24.512  16.809  1.00 35.16           C  
ANISOU 2364  CA  ALA A 356     4481   4597   4280    855    349   -587       C  
ATOM   2365  C   ALA A 356      18.402  23.213  16.868  1.00 40.93           C  
ANISOU 2365  C   ALA A 356     5147   5415   4989    845    373   -542       C  
ATOM   2366  O   ALA A 356      17.284  23.200  17.383  1.00 43.05           O  
ANISOU 2366  O   ALA A 356     5377   5732   5250    880    409   -538       O  
ATOM   2367  CB  ALA A 356      18.493  25.504  15.891  1.00 26.09           C  
ANISOU 2367  CB  ALA A 356     3323   3402   3189    900    344   -581       C  
ATOM   2368  N   SER A 357      18.970  22.131  16.340  1.00 37.30           N  
ANISOU 2368  N   SER A 357     4675   4973   4523    798    354   -508       N  
ATOM   2369  CA  SER A 357      18.229  20.877  16.177  1.00 33.02           C  
ANISOU 2369  CA  SER A 357     4068   4505   3974    783    373   -460       C  
ATOM   2370  C   SER A 357      17.899  20.151  17.476  1.00 29.22           C  
ANISOU 2370  C   SER A 357     3570   4092   3442    776    413   -457       C  
ATOM   2371  O   SER A 357      16.924  19.403  17.544  1.00 36.81           O  
ANISOU 2371  O   SER A 357     4469   5112   4404    778    442   -422       O  
ATOM   2372  CB  SER A 357      18.971  19.919  15.232  1.00 32.94           C  
ANISOU 2372  CB  SER A 357     4052   4491   3974    735    342   -427       C  
ATOM   2373  OG  SER A 357      20.204  19.478  15.788  1.00 33.37           O  
ANISOU 2373  OG  SER A 357     4150   4537   3992    693    330   -441       O  
ATOM   2374  N   GLY A 358      18.705  20.355  18.507  1.00 24.32           N  
ANISOU 2374  N   GLY A 358     3001   3463   2777    767    414   -491       N  
ATOM   2375  CA  GLY A 358      18.556  19.550  19.712  1.00 15.35           C  
ANISOU 2375  CA  GLY A 358     1855   2392   1586    756    447   -481       C  
ATOM   2376  C   GLY A 358      19.470  18.335  19.700  1.00 32.87           C  
ANISOU 2376  C   GLY A 358     4080   4630   3781    700    431   -452       C  
ATOM   2377  O   GLY A 358      19.556  17.602  20.688  1.00 35.41           O  
ANISOU 2377  O   GLY A 358     4401   4999   4053    685    454   -439       O  
ATOM   2378  N   HIS A 359      20.149  18.115  18.572  1.00 27.30           N  
ANISOU 2378  N   HIS A 359     3379   3886   3109    671    393   -439       N  
ATOM   2379  CA  HIS A 359      21.114  17.023  18.452  1.00 26.72           C  
ANISOU 2379  CA  HIS A 359     3314   3821   3016    619    374   -415       C  
ATOM   2380  C   HIS A 359      22.523  17.565  18.656  1.00 29.23           C  
ANISOU 2380  C   HIS A 359     3698   4088   3322    601    336   -455       C  
ATOM   2381  O   HIS A 359      23.017  18.367  17.868  1.00 29.83           O  
ANISOU 2381  O   HIS A 359     3799   4100   3434    603    305   -477       O  
ATOM   2382  CB  HIS A 359      20.956  16.318  17.105  1.00 19.79           C  
ANISOU 2382  CB  HIS A 359     2395   2942   2182    597    359   -375       C  
ATOM   2383  CG  HIS A 359      19.564  15.821  16.861  1.00 24.99           C  
ANISOU 2383  CG  HIS A 359     2983   3651   2862    610    391   -338       C  
ATOM   2384  ND1 HIS A 359      19.034  14.746  17.544  1.00 31.45           N  
ANISOU 2384  ND1 HIS A 359     3761   4532   3658    590    427   -301       N  
ATOM   2385  CD2 HIS A 359      18.582  16.267  16.041  1.00 22.23           C  
ANISOU 2385  CD2 HIS A 359     2591   3297   2557    639    391   -330       C  
ATOM   2386  CE1 HIS A 359      17.792  14.541  17.142  1.00 29.33           C  
ANISOU 2386  CE1 HIS A 359     3427   4295   3423    603    448   -274       C  
ATOM   2387  NE2 HIS A 359      17.493  15.452  16.231  1.00 28.75           N  
ANISOU 2387  NE2 HIS A 359     3350   4184   3390    634    425   -292       N  
ATOM   2388  N   TYR A 360      23.165  17.129  19.730  1.00 28.73           N  
ANISOU 2388  N   TYR A 360     3661   4050   3207    583    338   -462       N  
ATOM   2389  CA  TYR A 360      24.336  17.832  20.235  1.00 29.35           C  
ANISOU 2389  CA  TYR A 360     3797   4086   3268    574    305   -509       C  
ATOM   2390  C   TYR A 360      25.611  17.003  20.117  1.00 28.76           C  
ANISOU 2390  C   TYR A 360     3740   4006   3180    525    272   -495       C  
ATOM   2391  O   TYR A 360      25.740  15.951  20.728  1.00 30.53           O  
ANISOU 2391  O   TYR A 360     3954   4280   3364    507    284   -465       O  
ATOM   2392  CB  TYR A 360      24.073  18.279  21.683  1.00 29.40           C  
ANISOU 2392  CB  TYR A 360     3825   4122   3223    603    327   -541       C  
ATOM   2393  CG  TYR A 360      22.855  19.196  21.813  1.00 29.05           C  
ANISOU 2393  CG  TYR A 360     3766   4079   3194    655    360   -561       C  
ATOM   2394  CD1 TYR A 360      22.685  20.274  20.951  1.00 37.32           C  
ANISOU 2394  CD1 TYR A 360     4820   5064   4296    676    346   -584       C  
ATOM   2395  CD2 TYR A 360      21.871  18.968  22.778  1.00 30.47           C  
ANISOU 2395  CD2 TYR A 360     3922   4320   3334    685    407   -552       C  
ATOM   2396  CE1 TYR A 360      21.588  21.111  21.050  1.00 41.69           C  
ANISOU 2396  CE1 TYR A 360     5359   5615   4865    726    374   -601       C  
ATOM   2397  CE2 TYR A 360      20.758  19.810  22.892  1.00 28.77           C  
ANISOU 2397  CE2 TYR A 360     3691   4106   3135    735    438   -571       C  
ATOM   2398  CZ  TYR A 360      20.630  20.878  22.022  1.00 36.40           C  
ANISOU 2398  CZ  TYR A 360     4665   5010   4157    756    420   -596       C  
ATOM   2399  OH  TYR A 360      19.546  21.723  22.094  1.00 39.28           O  
ANISOU 2399  OH  TYR A 360     5012   5372   4540    808    448   -613       O  
ATOM   2400  N   SER A 361      26.551  17.496  19.319  1.00 28.15           N  
ANISOU 2400  N   SER A 361     3689   3868   3141    505    233   -515       N  
ATOM   2401  CA  SER A 361      27.804  16.801  19.071  1.00 22.43           C  
ANISOU 2401  CA  SER A 361     2979   3132   2412    459    200   -504       C  
ATOM   2402  C   SER A 361      29.006  17.564  19.635  1.00 26.11           C  
ANISOU 2402  C   SER A 361     3492   3558   2871    444    163   -552       C  
ATOM   2403  O   SER A 361      29.189  18.743  19.347  1.00 26.34           O  
ANISOU 2403  O   SER A 361     3545   3529   2935    453    149   -589       O  
ATOM   2404  CB  SER A 361      27.980  16.577  17.562  1.00 18.80           C  
ANISOU 2404  CB  SER A 361     2503   2636   2004    440    184   -480       C  
ATOM   2405  OG  SER A 361      29.304  16.202  17.237  1.00 18.86           O  
ANISOU 2405  OG  SER A 361     2531   2619   2018    399    148   -481       O  
ATOM   2406  N   PHE A 362      29.819  16.865  20.428  1.00 25.96           N  
ANISOU 2406  N   PHE A 362     3484   3569   2810    421    148   -548       N  
ATOM   2407  CA  PHE A 362      31.068  17.387  20.978  1.00 26.85           C  
ANISOU 2407  CA  PHE A 362     3634   3653   2914    400    108   -589       C  
ATOM   2408  C   PHE A 362      32.269  17.094  20.086  1.00 35.83           C  
ANISOU 2408  C   PHE A 362     4773   4751   4089    356     70   -580       C  
ATOM   2409  O   PHE A 362      33.223  17.867  20.052  1.00 42.01           O  
ANISOU 2409  O   PHE A 362     5580   5484   4896    337     36   -617       O  
ATOM   2410  CB  PHE A 362      31.347  16.768  22.348  1.00 33.17           C  
ANISOU 2410  CB  PHE A 362     4443   4512   3646    402    108   -588       C  
ATOM   2411  CG  PHE A 362      30.648  17.453  23.475  1.00 54.56           C  
ANISOU 2411  CG  PHE A 362     7169   7246   6316    442    131   -622       C  
ATOM   2412  CD1 PHE A 362      31.164  18.622  24.022  1.00 60.99           C  
ANISOU 2412  CD1 PHE A 362     8019   8024   7130    448    106   -683       C  
ATOM   2413  CD2 PHE A 362      29.471  16.931  23.998  1.00 62.79           C  
ANISOU 2413  CD2 PHE A 362     8188   8347   7321    472    179   -592       C  
ATOM   2414  CE1 PHE A 362      30.517  19.263  25.071  1.00 62.28           C  
ANISOU 2414  CE1 PHE A 362     8199   8210   7253    488    128   -719       C  
ATOM   2415  CE2 PHE A 362      28.817  17.565  25.048  1.00 61.37           C  
ANISOU 2415  CE2 PHE A 362     8023   8191   7102    511    203   -624       C  
ATOM   2416  CZ  PHE A 362      29.343  18.731  25.584  1.00 61.34           C  
ANISOU 2416  CZ  PHE A 362     8059   8152   7095    521    177   -689       C  
ATOM   2417  N   LEU A 363      32.245  15.958  19.396  1.00 35.62           N  
ANISOU 2417  N   LEU A 363     4720   4746   4067    338     76   -532       N  
ATOM   2418  CA  LEU A 363      33.374  15.571  18.555  1.00 32.43           C  
ANISOU 2418  CA  LEU A 363     4316   4311   3695    298     43   -522       C  
ATOM   2419  C   LEU A 363      33.193  16.099  17.131  1.00 32.75           C  
ANISOU 2419  C   LEU A 363     4352   4296   3798    296     43   -519       C  
ATOM   2420  O   LEU A 363      32.583  15.440  16.280  1.00 29.08           O  
ANISOU 2420  O   LEU A 363     3861   3844   3344    299     61   -483       O  
ATOM   2421  CB  LEU A 363      33.547  14.055  18.557  1.00 33.51           C  
ANISOU 2421  CB  LEU A 363     4432   4498   3804    280     48   -474       C  
ATOM   2422  CG  LEU A 363      33.490  13.407  19.947  1.00 42.10           C  
ANISOU 2422  CG  LEU A 363     5523   5647   4826    290     57   -462       C  
ATOM   2423  CD1 LEU A 363      33.376  11.877  19.859  1.00 37.30           C  
ANISOU 2423  CD1 LEU A 363     4890   5085   4196    277     73   -404       C  
ATOM   2424  CD2 LEU A 363      34.689  13.825  20.809  1.00 38.29           C  
ANISOU 2424  CD2 LEU A 363     5068   5156   4325    277     16   -499       C  
ATOM   2425  N   ASN A 364      33.706  17.303  16.884  1.00 21.21           N  
ANISOU 2425  N   ASN A 364     2913   2770   2375    291     23   -555       N  
ATOM   2426  CA  ASN A 364      33.570  17.922  15.574  1.00 23.39           C  
ANISOU 2426  CA  ASN A 364     3189   2987   2709    292     23   -549       C  
ATOM   2427  C   ASN A 364      34.931  18.312  15.008  1.00 26.22           C  
ANISOU 2427  C   ASN A 364     3564   3287   3113    251    -11   -561       C  
ATOM   2428  O   ASN A 364      35.702  19.027  15.645  1.00 28.75           O  
ANISOU 2428  O   ASN A 364     3903   3581   3439    235    -33   -596       O  
ATOM   2429  CB  ASN A 364      32.662  19.147  15.637  1.00 22.46           C  
ANISOU 2429  CB  ASN A 364     3084   2839   2610    331     41   -573       C  
ATOM   2430  CG  ASN A 364      31.440  18.913  16.477  1.00 28.37           C  
ANISOU 2430  CG  ASN A 364     3818   3647   3314    370     74   -570       C  
ATOM   2431  OD1 ASN A 364      30.578  18.112  16.120  1.00 30.40           O  
ANISOU 2431  OD1 ASN A 364     4043   3947   3560    384     98   -534       O  
ATOM   2432  ND2 ASN A 364      31.354  19.608  17.610  1.00 26.11           N  
ANISOU 2432  ND2 ASN A 364     3552   3366   3002    387     77   -610       N  
ATOM   2433  N   VAL A 365      35.223  17.818  13.813  1.00 22.38           N  
ANISOU 2433  N   VAL A 365     3065   2782   2657    232    -15   -530       N  
ATOM   2434  CA  VAL A 365      36.460  18.153  13.138  1.00 26.26           C  
ANISOU 2434  CA  VAL A 365     3565   3217   3197    193    -41   -532       C  
ATOM   2435  C   VAL A 365      36.135  18.975  11.907  1.00 26.45           C  
ANISOU 2435  C   VAL A 365     3596   3179   3275    199    -29   -512       C  
ATOM   2436  O   VAL A 365      35.254  18.638  11.134  1.00 29.96           O  
ANISOU 2436  O   VAL A 365     4025   3637   3721    217     -8   -471       O  
ATOM   2437  CB  VAL A 365      37.236  16.901  12.736  1.00 26.21           C  
ANISOU 2437  CB  VAL A 365     3533   3239   3188    153    -49   -487       C  
ATOM   2438  CG1 VAL A 365      38.666  17.267  12.358  1.00 26.02           C  
ANISOU 2438  CG1 VAL A 365     3511   3165   3208    109    -75   -494       C  
ATOM   2439  CG2 VAL A 365      37.242  15.932  13.880  1.00 29.85           C  
ANISOU 2439  CG2 VAL A 365     3985   3767   3588    156    -53   -491       C  
ATOM   2440  N   PHE A 366      36.868  20.056  11.732  1.00 24.91           N  
ANISOU 2440  N   PHE A 366     3423   2915   3127    184    -44   -539       N  
ATOM   2441  CA  PHE A 366      36.610  20.984  10.661  1.00 23.64           C  
ANISOU 2441  CA  PHE A 366     3276   2687   3018    194    -33   -521       C  
ATOM   2442  C   PHE A 366      37.897  21.220   9.869  1.00 26.69           C  
ANISOU 2442  C   PHE A 366     3663   3020   3458    143    -45   -500       C  
ATOM   2443  O   PHE A 366      38.988  21.217  10.427  1.00 25.40           O  
ANISOU 2443  O   PHE A 366     3497   2849   3304    107    -69   -528       O  
ATOM   2444  CB  PHE A 366      36.104  22.276  11.289  1.00 24.25           C  
ANISOU 2444  CB  PHE A 366     3378   2729   3105    221    -27   -558       C  
ATOM   2445  CG  PHE A 366      36.114  23.462  10.373  1.00 26.08           C  
ANISOU 2445  CG  PHE A 366     3631   2877   3400    226    -20   -546       C  
ATOM   2446  CD1 PHE A 366      37.239  24.262  10.261  1.00 26.15           C  
ANISOU 2446  CD1 PHE A 366     3657   2822   3459    184    -34   -556       C  
ATOM   2447  CD2 PHE A 366      34.980  23.812   9.669  1.00 32.79           C  
ANISOU 2447  CD2 PHE A 366     4485   3715   4259    273      1   -521       C  
ATOM   2448  CE1 PHE A 366      37.237  25.367   9.430  1.00 28.61           C  
ANISOU 2448  CE1 PHE A 366     3990   3052   3827    187    -23   -538       C  
ATOM   2449  CE2 PHE A 366      34.975  24.923   8.847  1.00 34.13           C  
ANISOU 2449  CE2 PHE A 366     4676   3806   4484    281      8   -503       C  
ATOM   2450  CZ  PHE A 366      36.100  25.696   8.729  1.00 31.42           C  
ANISOU 2450  CZ  PHE A 366     4353   3395   4191    238     -1   -511       C  
ATOM   2451  N   LYS A 367      37.760  21.440   8.570  1.00 26.15           N  
ANISOU 2451  N   LYS A 367     3595   2918   3424    143    -29   -449       N  
ATOM   2452  CA  LYS A 367      38.905  21.731   7.726  1.00 25.36           C  
ANISOU 2452  CA  LYS A 367     3495   2767   3375     99    -31   -422       C  
ATOM   2453  C   LYS A 367      38.450  22.398   6.444  1.00 28.78           C  
ANISOU 2453  C   LYS A 367     3944   3151   3842    118     -9   -375       C  
ATOM   2454  O   LYS A 367      37.343  22.140   5.961  1.00 29.73           O  
ANISOU 2454  O   LYS A 367     4061   3300   3936    157      5   -348       O  
ATOM   2455  CB  LYS A 367      39.650  20.448   7.367  1.00 26.51           C  
ANISOU 2455  CB  LYS A 367     3609   2961   3502     64    -32   -387       C  
ATOM   2456  CG  LYS A 367      41.076  20.695   6.972  1.00 30.75           C  
ANISOU 2456  CG  LYS A 367     4139   3458   4089     13    -38   -377       C  
ATOM   2457  CD  LYS A 367      41.594  19.716   5.956  1.00 26.69           C  
ANISOU 2457  CD  LYS A 367     3600   2970   3570     -7    -24   -321       C  
ATOM   2458  CE  LYS A 367      42.738  20.354   5.183  1.00 27.13           C  
ANISOU 2458  CE  LYS A 367     3653   2969   3686    -46    -15   -298       C  
ATOM   2459  NZ  LYS A 367      43.425  21.413   6.007  1.00 20.98           N  
ANISOU 2459  NZ  LYS A 367     2882   2136   2954    -73    -36   -348       N  
ATOM   2460  N   LEU A 368      39.302  23.253   5.891  1.00 25.11           N  
ANISOU 2460  N   LEU A 368     3492   2615   3435     88     -6   -363       N  
ATOM   2461  CA  LEU A 368      39.062  23.780   4.559  1.00 25.76           C  
ANISOU 2461  CA  LEU A 368     3588   2653   3545    101     17   -305       C  
ATOM   2462  C   LEU A 368      39.848  22.942   3.564  1.00 26.65           C  
ANISOU 2462  C   LEU A 368     3679   2792   3655     67     29   -250       C  
ATOM   2463  O   LEU A 368      41.080  22.996   3.543  1.00 25.72           O  
ANISOU 2463  O   LEU A 368     3550   2651   3571     19     28   -249       O  
ATOM   2464  CB  LEU A 368      39.492  25.243   4.477  1.00 27.29           C  
ANISOU 2464  CB  LEU A 368     3813   2748   3808     91     19   -316       C  
ATOM   2465  CG  LEU A 368      39.474  25.912   3.097  1.00 26.97           C  
ANISOU 2465  CG  LEU A 368     3791   2651   3805     98     45   -248       C  
ATOM   2466  CD1 LEU A 368      38.071  25.940   2.522  1.00 17.15           C  
ANISOU 2466  CD1 LEU A 368     2560   1429   2528    163     56   -218       C  
ATOM   2467  CD2 LEU A 368      40.059  27.320   3.178  1.00 20.11           C  
ANISOU 2467  CD2 LEU A 368     2950   1683   3008     77     45   -259       C  
ATOM   2468  N   PHE A 369      39.139  22.148   2.764  1.00 17.94           N  
ANISOU 2468  N   PHE A 369     2567   1738   2510     93     41   -208       N  
ATOM   2469  CA  PHE A 369      39.771  21.341   1.718  1.00 16.92           C  
ANISOU 2469  CA  PHE A 369     2423   1636   2371     71     55   -157       C  
ATOM   2470  C   PHE A 369      40.362  22.227   0.629  1.00 26.62           C  
ANISOU 2470  C   PHE A 369     3670   2801   3644     58     78   -109       C  
ATOM   2471  O   PHE A 369      39.889  23.340   0.392  1.00 32.86           O  
ANISOU 2471  O   PHE A 369     4488   3534   4462     83     85   -100       O  
ATOM   2472  CB  PHE A 369      38.759  20.384   1.071  1.00 13.31           C  
ANISOU 2472  CB  PHE A 369     1956   1241   1859    105     57   -130       C  
ATOM   2473  CG  PHE A 369      38.437  19.163   1.899  1.00 22.45           C  
ANISOU 2473  CG  PHE A 369     3088   2467   2975    103     42   -159       C  
ATOM   2474  CD1 PHE A 369      39.292  18.734   2.897  1.00 23.87           C  
ANISOU 2474  CD1 PHE A 369     3252   2660   3157     69     29   -193       C  
ATOM   2475  CD2 PHE A 369      37.278  18.430   1.657  1.00 21.05           C  
ANISOU 2475  CD2 PHE A 369     2901   2342   2757    135     39   -149       C  
ATOM   2476  CE1 PHE A 369      38.993  17.596   3.655  1.00 23.45           C  
ANISOU 2476  CE1 PHE A 369     3178   2668   3064     70     17   -212       C  
ATOM   2477  CE2 PHE A 369      36.978  17.303   2.395  1.00 21.39           C  
ANISOU 2477  CE2 PHE A 369     2919   2442   2766    130     28   -169       C  
ATOM   2478  CZ  PHE A 369      37.837  16.881   3.402  1.00 24.19           C  
ANISOU 2478  CZ  PHE A 369     3262   2807   3121     99     20   -198       C  
ATOM   2479  N   GLY A 370      41.394  21.732  -0.044  1.00 27.70           N  
ANISOU 2479  N   GLY A 370     3791   2948   3788     24     94    -76       N  
ATOM   2480  CA  GLY A 370      41.937  22.425  -1.202  1.00 17.24           C  
ANISOU 2480  CA  GLY A 370     2481   1574   2495     14    124    -19       C  
ATOM   2481  C   GLY A 370      41.394  21.865  -2.509  1.00 20.90           C  
ANISOU 2481  C   GLY A 370     2953   2078   2911     47    142     37       C  
ATOM   2482  O   GLY A 370      40.340  21.225  -2.542  1.00 24.08           O  
ANISOU 2482  O   GLY A 370     3355   2531   3263     84    127     29       O  
ATOM   2483  N   PRO A 371      42.115  22.110  -3.609  1.00 22.69           N  
ANISOU 2483  N   PRO A 371     3186   2283   3151     34    174     94       N  
ATOM   2484  CA  PRO A 371      41.704  21.644  -4.940  1.00 21.30           C  
ANISOU 2484  CA  PRO A 371     3023   2145   2924     66    192    147       C  
ATOM   2485  C   PRO A 371      41.456  20.137  -4.980  1.00 22.06           C  
ANISOU 2485  C   PRO A 371     3097   2325   2961     74    177    128       C  
ATOM   2486  O   PRO A 371      42.148  19.386  -4.297  1.00 23.11           O  
ANISOU 2486  O   PRO A 371     3201   2482   3100     41    169     96       O  
ATOM   2487  CB  PRO A 371      42.905  22.018  -5.820  1.00 23.60           C  
ANISOU 2487  CB  PRO A 371     3315   2406   3245     36    234    201       C  
ATOM   2488  CG  PRO A 371      43.505  23.237  -5.113  1.00 20.96           C  
ANISOU 2488  CG  PRO A 371     2984   1989   2992      0    237    188       C  
ATOM   2489  CD  PRO A 371      43.354  22.914  -3.653  1.00 24.63           C  
ANISOU 2489  CD  PRO A 371     3427   2466   3464    -14    197    111       C  
ATOM   2490  N   ARG A 372      40.466  19.718  -5.764  1.00 19.69           N  
ANISOU 2490  N   ARG A 372     2810   2065   2607    117    170    148       N  
ATOM   2491  CA  ARG A 372      40.137  18.310  -5.922  1.00 21.43           C  
ANISOU 2491  CA  ARG A 372     3012   2356   2774    125    154    130       C  
ATOM   2492  C   ARG A 372      41.040  17.658  -6.960  1.00 26.32           C  
ANISOU 2492  C   ARG A 372     3631   3001   3371    114    182    164       C  
ATOM   2493  O   ARG A 372      41.814  18.344  -7.641  1.00 25.57           O  
ANISOU 2493  O   ARG A 372     3548   2872   3295    104    216    207       O  
ATOM   2494  CB  ARG A 372      38.670  18.144  -6.334  1.00 19.26           C  
ANISOU 2494  CB  ARG A 372     2749   2115   2456    174    131    132       C  
ATOM   2495  CG  ARG A 372      38.302  18.807  -7.667  1.00 23.86           C  
ANISOU 2495  CG  ARG A 372     3363   2687   3015    213    144    189       C  
ATOM   2496  CD  ARG A 372      37.019  18.217  -8.254  1.00 27.85           C  
ANISOU 2496  CD  ARG A 372     3869   3247   3465    257    115    188       C  
ATOM   2497  NE  ARG A 372      37.208  16.789  -8.508  1.00 35.36           N  
ANISOU 2497  NE  ARG A 372     4802   4255   4377    243    106    167       N  
ATOM   2498  CZ  ARG A 372      36.280  15.848  -8.366  1.00 29.48           C  
ANISOU 2498  CZ  ARG A 372     4038   3560   3602    255     73    136       C  
ATOM   2499  NH1 ARG A 372      35.048  16.163  -7.982  1.00 21.37           N  
ANISOU 2499  NH1 ARG A 372     3002   2540   2577    283     47    122       N  
ATOM   2500  NH2 ARG A 372      36.596  14.580  -8.611  1.00 27.37           N  
ANISOU 2500  NH2 ARG A 372     3759   3332   3307    238     68    118       N  
ATOM   2501  N   ASN A 373      40.942  16.333  -7.069  1.00 22.05           N  
ANISOU 2501  N   ASN A 373     3073   2515   2789    116    169    143       N  
ATOM   2502  CA  ASN A 373      41.684  15.582  -8.084  1.00 21.93           C  
ANISOU 2502  CA  ASN A 373     3059   2531   2743    114    193    167       C  
ATOM   2503  C   ASN A 373      40.738  15.056  -9.160  1.00 19.53           C  
ANISOU 2503  C   ASN A 373     2775   2270   2374    157    181    179       C  
ATOM   2504  O   ASN A 373      39.570  15.420  -9.187  1.00 20.06           O  
ANISOU 2504  O   ASN A 373     2855   2341   2427    186    155    178       O  
ATOM   2505  CB  ASN A 373      42.539  14.462  -7.463  1.00 17.88           C  
ANISOU 2505  CB  ASN A 373     2513   2041   2239     82    191    134       C  
ATOM   2506  CG  ASN A 373      41.697  13.353  -6.816  1.00 15.82           C  
ANISOU 2506  CG  ASN A 373     2238   1818   1953     89    153     90       C  
ATOM   2507  OD1 ASN A 373      40.582  13.059  -7.240  1.00 13.76           O  
ANISOU 2507  OD1 ASN A 373     1990   1583   1655    118    133     86       O  
ATOM   2508  ND2 ASN A 373      42.243  12.736  -5.795  1.00  9.53           N  
ANISOU 2508  ND2 ASN A 373     1415   1027   1180     61    144     59       N  
ATOM   2509  N   GLN A 374      41.228  14.190 -10.036  1.00 23.01           N  
ANISOU 2509  N   GLN A 374     3220   2747   2776    162    196    188       N  
ATOM   2510  CA  GLN A 374      40.446  13.815 -11.209  1.00 24.01           C  
ANISOU 2510  CA  GLN A 374     3371   2914   2837    204    184    201       C  
ATOM   2511  C   GLN A 374      39.593  12.544 -11.099  1.00 22.50           C  
ANISOU 2511  C   GLN A 374     3168   2769   2612    213    142    154       C  
ATOM   2512  O   GLN A 374      38.927  12.178 -12.065  1.00 27.89           O  
ANISOU 2512  O   GLN A 374     3870   3487   3241    245    125    157       O  
ATOM   2513  CB  GLN A 374      41.324  13.800 -12.475  1.00 29.11           C  
ANISOU 2513  CB  GLN A 374     4039   3574   3449    216    227    243       C  
ATOM   2514  CG  GLN A 374      42.569  12.949 -12.381  1.00 40.00           C  
ANISOU 2514  CG  GLN A 374     5396   4964   4839    188    255    230       C  
ATOM   2515  CD  GLN A 374      43.662  13.365 -13.375  1.00 42.30           C  
ANISOU 2515  CD  GLN A 374     5699   5252   5119    191    313    282       C  
ATOM   2516  OE1 GLN A 374      43.518  13.205 -14.591  1.00 40.66           O  
ANISOU 2516  OE1 GLN A 374     5522   5078   4848    227    328    307       O  
ATOM   2517  NE2 GLN A 374      44.767  13.889 -12.849  1.00 30.74           N  
ANISOU 2517  NE2 GLN A 374     4210   3752   3716    153    347    298       N  
ATOM   2518  N   ALA A 375      39.600  11.886  -9.938  1.00 22.22           N  
ANISOU 2518  N   ALA A 375     3103   2732   2608    184    124    112       N  
ATOM   2519  CA  ALA A 375      38.743  10.707  -9.709  1.00 18.69           C  
ANISOU 2519  CA  ALA A 375     2641   2319   2140    187     86     71       C  
ATOM   2520  C   ALA A 375      37.283  11.120  -9.642  1.00 20.36           C  
ANISOU 2520  C   ALA A 375     2853   2541   2343    212     51     67       C  
ATOM   2521  O   ALA A 375      36.910  11.919  -8.776  1.00 23.23           O  
ANISOU 2521  O   ALA A 375     3206   2880   2740    208     47     66       O  
ATOM   2522  CB  ALA A 375      39.133   9.991  -8.403  1.00  6.56           C  
ANISOU 2522  CB  ALA A 375     1074    777    643    151     80     37       C  
ATOM   2523  N   PRO A 376      36.453  10.579 -10.550  1.00 21.13           N  
ANISOU 2523  N   PRO A 376     2959   2676   2394    238     24     60       N  
ATOM   2524  CA  PRO A 376      35.034  10.937 -10.624  1.00 16.76           C  
ANISOU 2524  CA  PRO A 376     2399   2139   1830    266    -12     57       C  
ATOM   2525  C   PRO A 376      34.362  10.855  -9.268  1.00 14.80           C  
ANISOU 2525  C   PRO A 376     2116   1884   1623    247    -29     30       C  
ATOM   2526  O   PRO A 376      33.586  11.753  -8.956  1.00 15.78           O  
ANISOU 2526  O   PRO A 376     2235   1999   1761    268    -37     39       O  
ATOM   2527  CB  PRO A 376      34.447   9.865 -11.549  1.00 18.83           C  
ANISOU 2527  CB  PRO A 376     2664   2447   2044    280    -45     35       C  
ATOM   2528  CG  PRO A 376      35.559   9.481 -12.420  1.00 20.27           C  
ANISOU 2528  CG  PRO A 376     2874   2633   2195    281    -17     45       C  
ATOM   2529  CD  PRO A 376      36.817   9.593 -11.579  1.00 24.18           C  
ANISOU 2529  CD  PRO A 376     3360   3093   2735    246     24     51       C  
ATOM   2530  N   LEU A 377      34.654   9.821  -8.476  1.00 15.23           N  
ANISOU 2530  N   LEU A 377     2147   1942   1696    213    -31     -2       N  
ATOM   2531  CA  LEU A 377      33.950   9.633  -7.199  1.00 18.28           C  
ANISOU 2531  CA  LEU A 377     2501   2330   2115    197    -45    -25       C  
ATOM   2532  C   LEU A 377      34.717  10.072  -5.974  1.00 13.95           C  
ANISOU 2532  C   LEU A 377     1947   1751   1604    174    -20    -28       C  
ATOM   2533  O   LEU A 377      34.344   9.702  -4.861  1.00 16.48           O  
ANISOU 2533  O   LEU A 377     2242   2076   1942    158    -27    -48       O  
ATOM   2534  CB  LEU A 377      33.577   8.178  -6.957  1.00 16.48           C  
ANISOU 2534  CB  LEU A 377     2249   2127   1885    175    -66    -56       C  
ATOM   2535  CG  LEU A 377      32.309   7.544  -7.471  1.00 22.12           C  
ANISOU 2535  CG  LEU A 377     2945   2876   2583    186   -104    -72       C  
ATOM   2536  CD1 LEU A 377      31.922   6.490  -6.443  1.00 21.20           C  
ANISOU 2536  CD1 LEU A 377     2795   2766   2495    153   -113    -97       C  
ATOM   2537  CD2 LEU A 377      31.234   8.569  -7.686  1.00 16.96           C  
ANISOU 2537  CD2 LEU A 377     2285   2234   1925    221   -120    -58       C  
ATOM   2538  N   SER A 378      35.795  10.816  -6.165  1.00 16.72           N  
ANISOU 2538  N   SER A 378     2319   2071   1964    170      7     -7       N  
ATOM   2539  CA  SER A 378      36.532  11.356  -5.030  1.00 20.33           C  
ANISOU 2539  CA  SER A 378     2770   2497   2458    147     24    -13       C  
ATOM   2540  C   SER A 378      35.634  12.233  -4.131  1.00 15.93           C  
ANISOU 2540  C   SER A 378     2204   1928   1919    161     15    -24       C  
ATOM   2541  O   SER A 378      34.890  13.077  -4.619  1.00 19.97           O  
ANISOU 2541  O   SER A 378     2728   2434   2427    193     11     -8       O  
ATOM   2542  CB  SER A 378      37.742  12.155  -5.526  1.00 17.66           C  
ANISOU 2542  CB  SER A 378     2452   2124   2133    140     54     14       C  
ATOM   2543  OG  SER A 378      38.571  12.548  -4.444  1.00 17.04           O  
ANISOU 2543  OG  SER A 378     2364   2018   2093    112     65      2       O  
ATOM   2544  N   PHE A 379      35.694  12.022  -2.823  1.00 12.36           N  
ANISOU 2544  N   PHE A 379     1734   1476   1485    142     13    -49       N  
ATOM   2545  CA  PHE A 379      34.912  12.849  -1.893  1.00 13.01           C  
ANISOU 2545  CA  PHE A 379     1810   1550   1582    158     10    -64       C  
ATOM   2546  C   PHE A 379      35.333  14.337  -1.785  1.00 15.49           C  
ANISOU 2546  C   PHE A 379     2148   1814   1923    167     23    -57       C  
ATOM   2547  O   PHE A 379      34.485  15.214  -1.902  1.00 15.19           O  
ANISOU 2547  O   PHE A 379     2118   1764   1889    200     20    -53       O  
ATOM   2548  CB  PHE A 379      34.803  12.187  -0.504  1.00 12.98           C  
ANISOU 2548  CB  PHE A 379     1784   1567   1582    139      5    -93       C  
ATOM   2549  CG  PHE A 379      34.375  13.133   0.602  1.00 16.07           C  
ANISOU 2549  CG  PHE A 379     2174   1945   1986    154      9   -114       C  
ATOM   2550  CD1 PHE A 379      33.064  13.620   0.662  1.00 17.96           C  
ANISOU 2550  CD1 PHE A 379     2405   2197   2222    189      4   -117       C  
ATOM   2551  CD2 PHE A 379      35.279  13.523   1.596  1.00 13.49           C  
ANISOU 2551  CD2 PHE A 379     1855   1597   1675    134     14   -134       C  
ATOM   2552  CE1 PHE A 379      32.666  14.500   1.683  1.00 18.21           C  
ANISOU 2552  CE1 PHE A 379     2438   2216   2264    208     10   -141       C  
ATOM   2553  CE2 PHE A 379      34.892  14.406   2.628  1.00 11.07           C  
ANISOU 2553  CE2 PHE A 379     1553   1278   1376    150     16   -161       C  
ATOM   2554  CZ  PHE A 379      33.584  14.890   2.667  1.00 15.66           C  
ANISOU 2554  CZ  PHE A 379     2129   1870   1952    189     16   -165       C  
ATOM   2555  N   PRO A 380      36.629  14.625  -1.551  1.00 15.63           N  
ANISOU 2555  N   PRO A 380     2175   1800   1963    139     37    -58       N  
ATOM   2556  CA  PRO A 380      36.986  16.038  -1.330  1.00 17.49           C  
ANISOU 2556  CA  PRO A 380     2432   1982   2233    142     48    -56       C  
ATOM   2557  C   PRO A 380      36.768  16.962  -2.519  1.00 18.43           C  
ANISOU 2557  C   PRO A 380     2576   2070   2356    168     59    -17       C  
ATOM   2558  O   PRO A 380      37.052  16.618  -3.662  1.00 18.00           O  
ANISOU 2558  O   PRO A 380     2529   2027   2282    170     68     17       O  
ATOM   2559  CB  PRO A 380      38.481  15.970  -0.980  1.00 19.25           C  
ANISOU 2559  CB  PRO A 380     2650   2183   2481     99     58    -62       C  
ATOM   2560  CG  PRO A 380      38.635  14.577  -0.344  1.00 17.75           C  
ANISOU 2560  CG  PRO A 380     2434   2041   2269     81     46    -83       C  
ATOM   2561  CD  PRO A 380      37.754  13.723  -1.224  1.00 16.77           C  
ANISOU 2561  CD  PRO A 380     2306   1955   2109    102     41    -66       C  
ATOM   2562  N   ILE A 381      36.225  18.133  -2.224  1.00 20.47           N  
ANISOU 2562  N   ILE A 381     2850   2290   2637    193     59    -20       N  
ATOM   2563  CA  ILE A 381      36.194  19.248  -3.155  1.00 23.89           C  
ANISOU 2563  CA  ILE A 381     3314   2678   3087    216     72     20       C  
ATOM   2564  C   ILE A 381      36.618  20.456  -2.343  1.00 20.85           C  
ANISOU 2564  C   ILE A 381     2943   2226   2753    206     79      0       C  
ATOM   2565  O   ILE A 381      36.509  20.437  -1.123  1.00 21.85           O  
ANISOU 2565  O   ILE A 381     3059   2355   2889    198     68    -48       O  
ATOM   2566  CB  ILE A 381      34.796  19.469  -3.761  1.00 22.27           C  
ANISOU 2566  CB  ILE A 381     3113   2493   2856    271     59     37       C  
ATOM   2567  CG1 ILE A 381      33.783  19.822  -2.672  1.00 20.82           C  
ANISOU 2567  CG1 ILE A 381     2916   2312   2683    297     45     -2       C  
ATOM   2568  CG2 ILE A 381      34.364  18.244  -4.565  1.00 12.39           C  
ANISOU 2568  CG2 ILE A 381     1845   1308   1556    277     45     49       C  
ATOM   2569  CD1 ILE A 381      32.389  20.135  -3.209  1.00 19.14           C  
ANISOU 2569  CD1 ILE A 381     2701   2118   2453    354     31     15       C  
ATOM   2570  N   PRO A 382      37.150  21.491  -2.999  1.00 18.81           N  
ANISOU 2570  N   PRO A 382     2712   1906   2527    205     98     36       N  
ATOM   2571  CA  PRO A 382      37.578  22.638  -2.196  1.00 22.81           C  
ANISOU 2571  CA  PRO A 382     3234   2341   3091    191    102     11       C  
ATOM   2572  C   PRO A 382      36.384  23.217  -1.457  1.00 21.44           C  
ANISOU 2572  C   PRO A 382     3068   2159   2919    235     86    -23       C  
ATOM   2573  O   PRO A 382      35.328  23.402  -2.051  1.00 21.81           O  
ANISOU 2573  O   PRO A 382     3123   2219   2947    285     83      1       O  
ATOM   2574  CB  PRO A 382      38.125  23.630  -3.245  1.00 22.73           C  
ANISOU 2574  CB  PRO A 382     3254   2267   3116    189    128     69       C  
ATOM   2575  CG  PRO A 382      37.613  23.137  -4.567  1.00 19.92           C  
ANISOU 2575  CG  PRO A 382     2904   1956   2710    222    135    124       C  
ATOM   2576  CD  PRO A 382      37.465  21.655  -4.427  1.00 19.93           C  
ANISOU 2576  CD  PRO A 382     2874   2040   2660    213    119    100       C  
ATOM   2577  N   GLY A 383      36.534  23.468  -0.165  1.00 20.41           N  
ANISOU 2577  N   GLY A 383     2933   2013   2810    221     75    -81       N  
ATOM   2578  CA  GLY A 383      35.403  23.921   0.605  1.00 18.66           C  
ANISOU 2578  CA  GLY A 383     2716   1792   2584    267     65   -119       C  
ATOM   2579  C   GLY A 383      35.398  23.543   2.070  1.00 30.04           C  
ANISOU 2579  C   GLY A 383     4140   3262   4012    255     51   -186       C  
ATOM   2580  O   GLY A 383      36.384  23.027   2.626  1.00 25.28           O  
ANISOU 2580  O   GLY A 383     3525   2671   3410    208     45   -208       O  
ATOM   2581  N   TRP A 384      34.254  23.808   2.692  1.00 28.21           N  
ANISOU 2581  N   TRP A 384     3907   3046   3767    303     47   -215       N  
ATOM   2582  CA  TRP A 384      34.107  23.716   4.134  1.00 26.45           C  
ANISOU 2582  CA  TRP A 384     3677   2844   3530    304     38   -280       C  
ATOM   2583  C   TRP A 384      33.736  22.306   4.574  1.00 22.22           C  
ANISOU 2583  C   TRP A 384     3104   2399   2940    297     34   -285       C  
ATOM   2584  O   TRP A 384      32.628  21.843   4.345  1.00 23.90           O  
ANISOU 2584  O   TRP A 384     3295   2660   3125    332     38   -269       O  
ATOM   2585  CB  TRP A 384      33.083  24.753   4.587  1.00 24.86           C  
ANISOU 2585  CB  TRP A 384     3493   2611   3341    363     42   -309       C  
ATOM   2586  CG  TRP A 384      33.408  26.085   3.985  1.00 30.47           C  
ANISOU 2586  CG  TRP A 384     4242   3225   4110    372     47   -293       C  
ATOM   2587  CD1 TRP A 384      32.799  26.674   2.920  1.00 25.85           C  
ANISOU 2587  CD1 TRP A 384     3671   2608   3541    412     56   -242       C  
ATOM   2588  CD2 TRP A 384      34.468  26.963   4.378  1.00 30.09           C  
ANISOU 2588  CD2 TRP A 384     4222   3099   4113    334     44   -322       C  
ATOM   2589  NE1 TRP A 384      33.397  27.876   2.641  1.00 28.58           N  
ANISOU 2589  NE1 TRP A 384     4048   2863   3947    399     62   -233       N  
ATOM   2590  CE2 TRP A 384      34.426  28.076   3.519  1.00 26.54           C  
ANISOU 2590  CE2 TRP A 384     3794   2576   3715    347     55   -282       C  
ATOM   2591  CE3 TRP A 384      35.441  26.921   5.384  1.00 32.79           C  
ANISOU 2591  CE3 TRP A 384     4560   3437   4462    284     32   -373       C  
ATOM   2592  CZ2 TRP A 384      35.318  29.139   3.631  1.00 31.80           C  
ANISOU 2592  CZ2 TRP A 384     4476   3161   4447    310     58   -293       C  
ATOM   2593  CZ3 TRP A 384      36.326  27.978   5.499  1.00 33.37           C  
ANISOU 2593  CZ3 TRP A 384     4655   3434   4589    247     36   -384       C  
ATOM   2594  CH2 TRP A 384      36.262  29.073   4.624  1.00 31.37           C  
ANISOU 2594  CH2 TRP A 384     4427   3103   4389    259     54   -343       C  
ATOM   2595  N   ASN A 385      34.685  21.622   5.194  1.00 21.61           N  
ANISOU 2595  N   ASN A 385     3016   2343   2851    251     26   -304       N  
ATOM   2596  CA  ASN A 385      34.483  20.234   5.562  1.00 23.33           C  
ANISOU 2596  CA  ASN A 385     3202   2640   3023    239     23   -302       C  
ATOM   2597  C   ASN A 385      34.301  20.045   7.061  1.00 23.63           C  
ANISOU 2597  C   ASN A 385     3235   2712   3032    245     19   -353       C  
ATOM   2598  O   ASN A 385      35.078  20.559   7.869  1.00 18.43           O  
ANISOU 2598  O   ASN A 385     2594   2026   2385    228      8   -395       O  
ATOM   2599  CB  ASN A 385      35.656  19.375   5.078  1.00 24.82           C  
ANISOU 2599  CB  ASN A 385     3379   2837   3212    188     18   -276       C  
ATOM   2600  CG  ASN A 385      35.611  17.964   5.650  1.00 25.97           C  
ANISOU 2600  CG  ASN A 385     3497   3054   3317    173     14   -278       C  
ATOM   2601  OD1 ASN A 385      36.209  17.689   6.684  1.00 36.57           O  
ANISOU 2601  OD1 ASN A 385     4836   4411   4648    153      4   -309       O  
ATOM   2602  ND2 ASN A 385      34.880  17.078   4.994  1.00 11.37           N  
ANISOU 2602  ND2 ASN A 385     1628   1246   1446    183     18   -246       N  
ATOM   2603  N   ILE A 386      33.291  19.278   7.440  1.00 20.51           N  
ANISOU 2603  N   ILE A 386     2814   2380   2598    269     27   -351       N  
ATOM   2604  CA  ILE A 386      33.119  18.985   8.848  1.00 20.99           C  
ANISOU 2604  CA  ILE A 386     2870   2483   2623    276     28   -392       C  
ATOM   2605  C   ILE A 386      32.555  17.597   9.111  1.00 21.99           C  
ANISOU 2605  C   ILE A 386     2961   2685   2709    271     36   -368       C  
ATOM   2606  O   ILE A 386      31.623  17.141   8.443  1.00 22.81           O  
ANISOU 2606  O   ILE A 386     3040   2815   2810    287     46   -336       O  
ATOM   2607  CB  ILE A 386      32.274  20.072   9.585  1.00 26.71           C  
ANISOU 2607  CB  ILE A 386     3610   3192   3345    328     38   -436       C  
ATOM   2608  CG1 ILE A 386      32.307  19.840  11.101  1.00 36.71           C  
ANISOU 2608  CG1 ILE A 386     4879   4502   4568    334     39   -483       C  
ATOM   2609  CG2 ILE A 386      30.849  20.065   9.104  1.00 24.32           C  
ANISOU 2609  CG2 ILE A 386     3286   2916   3040    374     56   -411       C  
ATOM   2610  CD1 ILE A 386      31.939  21.062  11.938  1.00 43.52           C  
ANISOU 2610  CD1 ILE A 386     5764   5338   5434    363     45   -527       C  
ATOM   2611  N   CYS A 387      33.133  16.926  10.098  1.00 20.87           N  
ANISOU 2611  N   CYS A 387     2816   2577   2536    249     30   -385       N  
ATOM   2612  CA  CYS A 387      32.556  15.697  10.591  1.00 20.39           C  
ANISOU 2612  CA  CYS A 387     2726   2583   2437    247     42   -365       C  
ATOM   2613  C   CYS A 387      32.001  15.960  11.985  1.00 20.67           C  
ANISOU 2613  C   CYS A 387     2766   2655   2432    280     56   -403       C  
ATOM   2614  O   CYS A 387      32.686  16.514  12.835  1.00 20.29           O  
ANISOU 2614  O   CYS A 387     2743   2593   2371    279     44   -446       O  
ATOM   2615  CB  CYS A 387      33.585  14.556  10.598  1.00 21.72           C  
ANISOU 2615  CB  CYS A 387     2887   2768   2597    202     29   -343       C  
ATOM   2616  SG  CYS A 387      32.944  12.948  11.244  1.00 34.74           S  
ANISOU 2616  SG  CYS A 387     4504   4493   4205    196     45   -312       S  
ATOM   2617  N   VAL A 388      30.741  15.594  12.195  1.00 21.06           N  
ANISOU 2617  N   VAL A 388     2787   2751   2462    308     82   -389       N  
ATOM   2618  CA  VAL A 388      30.125  15.681  13.507  1.00 18.00           C  
ANISOU 2618  CA  VAL A 388     2400   2411   2030    342    104   -417       C  
ATOM   2619  C   VAL A 388      29.673  14.289  13.942  1.00 23.49           C  
ANISOU 2619  C   VAL A 388     3061   3173   2693    327    123   -378       C  
ATOM   2620  O   VAL A 388      29.645  13.350  13.134  1.00 20.31           O  
ANISOU 2620  O   VAL A 388     2633   2774   2310    296    118   -333       O  
ATOM   2621  CB  VAL A 388      28.905  16.639  13.509  1.00 31.15           C  
ANISOU 2621  CB  VAL A 388     4059   4074   3704    398    126   -437       C  
ATOM   2622  CG1 VAL A 388      29.322  18.058  13.115  1.00 28.78           C  
ANISOU 2622  CG1 VAL A 388     3795   3697   3442    411    109   -470       C  
ATOM   2623  CG2 VAL A 388      27.832  16.120  12.579  1.00 24.22           C  
ANISOU 2623  CG2 VAL A 388     3137   3218   2849    404    140   -390       C  
ATOM   2624  N   ASP A 389      29.309  14.158  15.214  1.00 24.77           N  
ANISOU 2624  N   ASP A 389     3223   3385   2804    350    145   -394       N  
ATOM   2625  CA  ASP A 389      28.926  12.862  15.764  1.00 23.98           C  
ANISOU 2625  CA  ASP A 389     3093   3346   2671    336    168   -353       C  
ATOM   2626  C   ASP A 389      27.722  12.985  16.702  1.00 25.15           C  
ANISOU 2626  C   ASP A 389     3222   3549   2784    378    211   -356       C  
ATOM   2627  O   ASP A 389      27.869  13.360  17.862  1.00 24.00           O  
ANISOU 2627  O   ASP A 389     3100   3415   2603    389    215   -377       O  
ATOM   2628  CB  ASP A 389      30.129  12.250  16.489  1.00 26.36           C  
ANISOU 2628  CB  ASP A 389     3419   3658   2938    308    147   -353       C  
ATOM   2629  CG  ASP A 389      29.984  10.753  16.730  1.00 28.70           C  
ANISOU 2629  CG  ASP A 389     3689   3998   3217    281    163   -297       C  
ATOM   2630  OD1 ASP A 389      29.145  10.097  16.073  1.00 27.42           O  
ANISOU 2630  OD1 ASP A 389     3489   3845   3083    270    181   -256       O  
ATOM   2631  OD2 ASP A 389      30.742  10.234  17.580  1.00 33.13           O  
ANISOU 2631  OD2 ASP A 389     4268   4583   3738    271    154   -293       O  
ATOM   2632  N   PHE A 390      26.534  12.674  16.188  1.00 26.56           N  
ANISOU 2632  N   PHE A 390     3354   3753   2984    390    238   -327       N  
ATOM   2633  CA  PHE A 390      25.295  12.804  16.957  1.00 31.89           C  
ANISOU 2633  CA  PHE A 390     4002   4473   3643    422    279   -320       C  
ATOM   2634  C   PHE A 390      25.025  11.603  17.851  1.00 35.47           C  
ANISOU 2634  C   PHE A 390     4433   4987   4058    404    310   -277       C  
ATOM   2635  O   PHE A 390      25.176  10.459  17.426  1.00 39.08           O  
ANISOU 2635  O   PHE A 390     4866   5461   4522    371    312   -236       O  
ATOM   2636  CB  PHE A 390      24.082  12.980  16.035  1.00 25.38           C  
ANISOU 2636  CB  PHE A 390     3128   3654   2862    444    294   -304       C  
ATOM   2637  CG  PHE A 390      24.204  14.122  15.082  1.00 26.86           C  
ANISOU 2637  CG  PHE A 390     3335   3783   3090    466    267   -335       C  
ATOM   2638  CD1 PHE A 390      24.247  15.424  15.544  1.00 27.82           C  
ANISOU 2638  CD1 PHE A 390     3492   3867   3210    497    262   -377       C  
ATOM   2639  CD2 PHE A 390      24.259  13.899  13.719  1.00 31.30           C  
ANISOU 2639  CD2 PHE A 390     3881   4312   3698    443    240   -311       C  
ATOM   2640  CE1 PHE A 390      24.355  16.483  14.665  1.00 27.16           C  
ANISOU 2640  CE1 PHE A 390     3428   3723   3168    517    239   -398       C  
ATOM   2641  CE2 PHE A 390      24.363  14.953  12.836  1.00 30.14           C  
ANISOU 2641  CE2 PHE A 390     3755   4110   3587    464    216   -330       C  
ATOM   2642  CZ  PHE A 390      24.407  16.246  13.311  1.00 28.84           C  
ANISOU 2642  CZ  PHE A 390     3625   3915   3416    509    220   -377       C  
ATOM   2643  N   PRO A 391      24.610  11.863  19.095  1.00 30.16           N  
ANISOU 2643  N   PRO A 391     3769   4344   3347    427    336   -285       N  
ATOM   2644  CA  PRO A 391      24.010  10.811  19.920  1.00 29.51           C  
ANISOU 2644  CA  PRO A 391     3658   4320   3236    417    377   -236       C  
ATOM   2645  C   PRO A 391      22.734  10.330  19.238  1.00 32.34           C  
ANISOU 2645  C   PRO A 391     3948   4703   3636    415    408   -198       C  
ATOM   2646  O   PRO A 391      21.968  11.156  18.742  1.00 38.53           O  
ANISOU 2646  O   PRO A 391     4713   5476   4452    444    411   -219       O  
ATOM   2647  CB  PRO A 391      23.655  11.542  21.215  1.00 21.86           C  
ANISOU 2647  CB  PRO A 391     2711   3372   2223    454    398   -264       C  
ATOM   2648  CG  PRO A 391      24.562  12.724  21.251  1.00 29.67           C  
ANISOU 2648  CG  PRO A 391     3754   4311   3208    468    358   -327       C  
ATOM   2649  CD  PRO A 391      24.762  13.132  19.821  1.00 25.57           C  
ANISOU 2649  CD  PRO A 391     3229   3741   2747    460    329   -338       C  
ATOM   2650  N   ILE A 392      22.504   9.025  19.195  1.00 28.88           N  
ANISOU 2650  N   ILE A 392     3474   4295   3204    379    427   -141       N  
ATOM   2651  CA  ILE A 392      21.292   8.530  18.568  1.00 36.18           C  
ANISOU 2651  CA  ILE A 392     4329   5243   4177    369    453   -105       C  
ATOM   2652  C   ILE A 392      20.087   8.824  19.458  1.00 37.26           C  
ANISOU 2652  C   ILE A 392     4437   5417   4303    398    499    -98       C  
ATOM   2653  O   ILE A 392      20.066   8.465  20.629  1.00 39.02           O  
ANISOU 2653  O   ILE A 392     4674   5670   4481    399    528    -81       O  
ATOM   2654  CB  ILE A 392      21.404   7.040  18.196  1.00 39.92           C  
ANISOU 2654  CB  ILE A 392     4769   5728   4671    314    458    -46       C  
ATOM   2655  CG1 ILE A 392      22.441   6.879  17.086  1.00 37.62           C  
ANISOU 2655  CG1 ILE A 392     4504   5380   4410    282    402    -57       C  
ATOM   2656  CG2 ILE A 392      20.049   6.490  17.734  1.00 36.61           C  
ANISOU 2656  CG2 ILE A 392     4270   5333   4306    298    484     -8       C  
ATOM   2657  CD1 ILE A 392      22.687   5.456  16.690  1.00 43.47           C  
ANISOU 2657  CD1 ILE A 392     5229   6105   5183    221    391     -6       C  
ATOM   2658  N   LYS A 393      19.107   9.521  18.888  1.00 40.66           N  
ANISOU 2658  N   LYS A 393     4829   5847   4773    426    504   -114       N  
ATOM   2659  CA  LYS A 393      17.945  10.004  19.617  1.00 43.70           C  
ANISOU 2659  CA  LYS A 393     5187   6265   5153    462    546   -117       C  
ATOM   2660  C   LYS A 393      16.742  10.023  18.698  1.00 44.03           C  
ANISOU 2660  C   LYS A 393     5155   6316   5257    465    552   -101       C  
ATOM   2661  O   LYS A 393      16.891  10.023  17.470  1.00 36.66           O  
ANISOU 2661  O   LYS A 393     4205   5356   4367    453    515   -104       O  
ATOM   2662  CB  LYS A 393      18.171  11.437  20.094  1.00 45.53           C  
ANISOU 2662  CB  LYS A 393     5470   6475   5355    514    537   -178       C  
ATOM   2663  CG  LYS A 393      18.956  11.586  21.369  1.00 53.45           C  
ANISOU 2663  CG  LYS A 393     6535   7485   6291    522    542   -198       C  
ATOM   2664  CD  LYS A 393      18.597  12.893  22.065  1.00 63.27           C  
ANISOU 2664  CD  LYS A 393     7804   8724   7511    577    554   -250       C  
ATOM   2665  CE  LYS A 393      18.295  14.022  21.073  1.00 66.51           C  
ANISOU 2665  CE  LYS A 393     8210   9090   7971    607    530   -286       C  
ATOM   2666  NZ  LYS A 393      16.833  14.211  20.809  1.00 65.73           N  
ANISOU 2666  NZ  LYS A 393     8046   9018   7910    634    564   -271       N  
ATOM   2667  N   ASP A 394      15.553  10.067  19.293  1.00 45.61           N  
ANISOU 2667  N   ASP A 394     5310   6555   5463    484    597    -87       N  
ATOM   2668  CA  ASP A 394      14.323  10.160  18.521  1.00 47.76           C  
ANISOU 2668  CA  ASP A 394     5509   6840   5797    491    601    -75       C  
ATOM   2669  C   ASP A 394      14.375  11.382  17.619  1.00 41.41           C  
ANISOU 2669  C   ASP A 394     4720   5997   5017    533    562   -120       C  
ATOM   2670  O   ASP A 394      14.748  12.473  18.052  1.00 42.36           O  
ANISOU 2670  O   ASP A 394     4895   6095   5106    576    558   -165       O  
ATOM   2671  CB  ASP A 394      13.093  10.203  19.435  1.00 57.07           C  
ANISOU 2671  CB  ASP A 394     6644   8066   6974    512    658    -61       C  
ATOM   2672  CG  ASP A 394      12.829   8.869  20.126  1.00 63.75           C  
ANISOU 2672  CG  ASP A 394     7459   8948   7814    464    698     -4       C  
ATOM   2673  OD1 ASP A 394      13.234   7.810  19.593  1.00 61.93           O  
ANISOU 2673  OD1 ASP A 394     7216   8706   7608    408    680     31       O  
ATOM   2674  OD2 ASP A 394      12.212   8.879  21.209  1.00 69.80           O  
ANISOU 2674  OD2 ASP A 394     8216   9753   8552    482    750      6       O  
ATOM   2675  N   GLY A 395      14.037  11.178  16.351  1.00 40.56           N  
ANISOU 2675  N   GLY A 395     4566   5879   4964    519    530   -108       N  
ATOM   2676  CA  GLY A 395      14.040  12.252  15.374  1.00 39.65           C  
ANISOU 2676  CA  GLY A 395     4463   5726   4875    558    490   -142       C  
ATOM   2677  C   GLY A 395      15.338  12.419  14.602  1.00 37.02           C  
ANISOU 2677  C   GLY A 395     4187   5344   4535    547    441   -161       C  
ATOM   2678  O   GLY A 395      15.392  13.206  13.658  1.00 41.20           O  
ANISOU 2678  O   GLY A 395     4727   5839   5089    574    406   -181       O  
ATOM   2679  N   LEU A 396      16.381  11.688  14.987  1.00 28.59           N  
ANISOU 2679  N   LEU A 396     3157   4273   3433    508    440   -153       N  
ATOM   2680  CA  LEU A 396      17.689  11.888  14.367  1.00 29.25           C  
ANISOU 2680  CA  LEU A 396     3297   4309   3506    498    398   -176       C  
ATOM   2681  C   LEU A 396      17.688  11.518  12.885  1.00 31.51           C  
ANISOU 2681  C   LEU A 396     3550   4583   3839    479    358   -162       C  
ATOM   2682  O   LEU A 396      18.190  12.277  12.054  1.00 32.19           O  
ANISOU 2682  O   LEU A 396     3677   4617   3939    494    317   -184       O  
ATOM   2683  CB  LEU A 396      18.794  11.126  15.106  1.00 24.84           C  
ANISOU 2683  CB  LEU A 396     2782   3752   2903    460    404   -168       C  
ATOM   2684  CG  LEU A 396      20.230  11.373  14.605  1.00 26.59           C  
ANISOU 2684  CG  LEU A 396     3068   3923   3114    448    362   -194       C  
ATOM   2685  CD1 LEU A 396      20.614  12.847  14.730  1.00 23.76           C  
ANISOU 2685  CD1 LEU A 396     2765   3519   2745    493    347   -246       C  
ATOM   2686  CD2 LEU A 396      21.260  10.493  15.321  1.00 21.07           C  
ANISOU 2686  CD2 LEU A 396     2404   3225   2375    405    363   -179       C  
ATOM   2687  N   GLY A 397      17.121  10.361  12.560  1.00 27.95           N  
ANISOU 2687  N   GLY A 397     3041   4160   3419    432    359   -121       N  
ATOM   2688  CA  GLY A 397      17.143   9.873  11.191  1.00 29.54           C  
ANISOU 2688  CA  GLY A 397     3226   4332   3666    394    306   -107       C  
ATOM   2689  C   GLY A 397      16.488  10.846  10.236  1.00 30.22           C  
ANISOU 2689  C   GLY A 397     3292   4409   3782    441    278   -123       C  
ATOM   2690  O   GLY A 397      16.997  11.136   9.160  1.00 31.48           O  
ANISOU 2690  O   GLY A 397     3485   4523   3954    437    230   -132       O  
ATOM   2691  N   LYS A 398      15.344  11.357  10.657  1.00 36.90           N  
ANISOU 2691  N   LYS A 398     4084   5300   4637    490    312   -126       N  
ATOM   2692  CA  LYS A 398      14.598  12.335   9.896  1.00 39.52           C  
ANISOU 2692  CA  LYS A 398     4398   5619   4998    539    287   -138       C  
ATOM   2693  C   LYS A 398      15.422  13.620   9.764  1.00 38.80           C  
ANISOU 2693  C   LYS A 398     4387   5471   4885    585    271   -173       C  
ATOM   2694  O   LYS A 398      15.494  14.228   8.683  1.00 34.85           O  
ANISOU 2694  O   LYS A 398     3899   4938   4404    610    230   -178       O  
ATOM   2695  CB  LYS A 398      13.279  12.608  10.618  1.00 44.06           C  
ANISOU 2695  CB  LYS A 398     4922   6230   5587    564    327   -130       C  
ATOM   2696  CG  LYS A 398      12.208  13.232   9.766  1.00 50.04           C  
ANISOU 2696  CG  LYS A 398     5633   6991   6387    602    301   -129       C  
ATOM   2697  CD  LYS A 398      11.286  14.090  10.621  1.00 57.37           C  
ANISOU 2697  CD  LYS A 398     6548   7935   7316    652    343   -140       C  
ATOM   2698  CE  LYS A 398      10.075  14.562   9.828  1.00 62.65           C  
ANISOU 2698  CE  LYS A 398     7157   8616   8032    686    320   -133       C  
ATOM   2699  NZ  LYS A 398       9.467  15.792  10.411  1.00 66.97           N  
ANISOU 2699  NZ  LYS A 398     7713   9155   8576    752    349   -154       N  
ATOM   2700  N   PHE A 399      16.059  14.027  10.862  1.00 29.47           N  
ANISOU 2700  N   PHE A 399     3260   4273   3662    594    301   -196       N  
ATOM   2701  CA  PHE A 399      16.902  15.217  10.829  1.00 19.70           C  
ANISOU 2701  CA  PHE A 399     2100   2974   2410    627    286   -232       C  
ATOM   2702  C   PHE A 399      18.089  15.124   9.866  1.00 27.96           C  
ANISOU 2702  C   PHE A 399     3193   3971   3459    601    242   -234       C  
ATOM   2703  O   PHE A 399      18.381  16.090   9.168  1.00 29.41           O  
ANISOU 2703  O   PHE A 399     3414   4103   3657    631    216   -247       O  
ATOM   2704  CB  PHE A 399      17.426  15.593  12.215  1.00 21.62           C  
ANISOU 2704  CB  PHE A 399     2396   3210   2611    631    318   -259       C  
ATOM   2705  CG  PHE A 399      18.357  16.785  12.194  1.00 25.38           C  
ANISOU 2705  CG  PHE A 399     2949   3616   3078    654    298   -299       C  
ATOM   2706  CD1 PHE A 399      17.873  18.055  11.882  1.00 30.05           C  
ANISOU 2706  CD1 PHE A 399     3552   4170   3695    703    291   -316       C  
ATOM   2707  CD2 PHE A 399      19.707  16.639  12.459  1.00 23.99           C  
ANISOU 2707  CD2 PHE A 399     2830   3408   2875    622    284   -316       C  
ATOM   2708  CE1 PHE A 399      18.718  19.160  11.843  1.00 22.90           C  
ANISOU 2708  CE1 PHE A 399     2716   3194   2792    718    273   -349       C  
ATOM   2709  CE2 PHE A 399      20.564  17.739  12.419  1.00 21.07           C  
ANISOU 2709  CE2 PHE A 399     2527   2970   2508    635    264   -351       C  
ATOM   2710  CZ  PHE A 399      20.064  19.000  12.113  1.00 23.02           C  
ANISOU 2710  CZ  PHE A 399     2785   3177   2783    681    259   -367       C  
ATOM   2711  N   VAL A 400      18.788  13.985   9.840  1.00 28.25           N  
ANISOU 2711  N   VAL A 400     3238   4010   3486    534    232   -213       N  
ATOM   2712  CA  VAL A 400      19.946  13.859   8.948  1.00 29.08           C  
ANISOU 2712  CA  VAL A 400     3395   4059   3596    495    189   -209       C  
ATOM   2713  C   VAL A 400      19.530  13.773   7.473  1.00 25.95           C  
ANISOU 2713  C   VAL A 400     2974   3652   3234    492    148   -188       C  
ATOM   2714  O   VAL A 400      20.286  14.175   6.574  1.00 21.78           O  
ANISOU 2714  O   VAL A 400     2492   3074   2711    487    115   -188       O  
ATOM   2715  CB  VAL A 400      20.915  12.705   9.341  1.00 35.10           C  
ANISOU 2715  CB  VAL A 400     4178   4821   4338    430    188   -197       C  
ATOM   2716  CG1 VAL A 400      21.445  12.914  10.742  1.00 30.66           C  
ANISOU 2716  CG1 VAL A 400     3648   4266   3734    438    221   -220       C  
ATOM   2717  CG2 VAL A 400      20.234  11.365   9.232  1.00 40.32           C  
ANISOU 2717  CG2 VAL A 400     4778   5527   5014    388    193   -162       C  
ATOM   2718  N   SER A 401      18.319  13.279   7.226  1.00 21.46           N  
ANISOU 2718  N   SER A 401     2333   3133   2687    496    149   -169       N  
ATOM   2719  CA  SER A 401      17.764  13.314   5.876  1.00 23.61           C  
ANISOU 2719  CA  SER A 401     2577   3404   2988    505    106   -154       C  
ATOM   2720  C   SER A 401      17.555  14.764   5.451  1.00 23.69           C  
ANISOU 2720  C   SER A 401     2611   3384   3005    574     97   -167       C  
ATOM   2721  O   SER A 401      17.721  15.118   4.287  1.00 31.13           O  
ANISOU 2721  O   SER A 401     3574   4298   3956    585     57   -157       O  
ATOM   2722  CB  SER A 401      16.459  12.526   5.798  1.00 31.65           C  
ANISOU 2722  CB  SER A 401     3505   4486   4034    495    108   -136       C  
ATOM   2723  OG  SER A 401      16.724  11.134   5.889  1.00 38.48           O  
ANISOU 2723  OG  SER A 401     4354   5364   4902    424    106   -120       O  
ATOM   2724  N   GLU A 402      17.216  15.609   6.408  1.00 26.91           N  
ANISOU 2724  N   GLU A 402     3021   3797   3407    625    134   -189       N  
ATOM   2725  CA  GLU A 402      17.091  17.028   6.127  1.00 27.24           C  
ANISOU 2725  CA  GLU A 402     3093   3799   3458    693    129   -203       C  
ATOM   2726  C   GLU A 402      18.464  17.641   5.807  1.00 26.80           C  
ANISOU 2726  C   GLU A 402     3125   3666   3391    680    112   -214       C  
ATOM   2727  O   GLU A 402      18.594  18.436   4.865  1.00 26.78           O  
ANISOU 2727  O   GLU A 402     3152   3619   3404    709     86   -204       O  
ATOM   2728  CB  GLU A 402      16.386  17.748   7.287  1.00 30.94           C  
ANISOU 2728  CB  GLU A 402     3553   4280   3924    733    173   -224       C  
ATOM   2729  CG  GLU A 402      16.225  19.254   7.099  1.00 50.53           C  
ANISOU 2729  CG  GLU A 402     6074   6705   6421    787    168   -238       C  
ATOM   2730  CD  GLU A 402      15.470  19.628   5.823  1.00 64.35           C  
ANISOU 2730  CD  GLU A 402     7796   8453   8202    820    131   -210       C  
ATOM   2731  OE1 GLU A 402      14.676  18.800   5.315  1.00 70.56           O  
ANISOU 2731  OE1 GLU A 402     8514   9294   9000    807    115   -186       O  
ATOM   2732  OE2 GLU A 402      15.678  20.758   5.326  1.00 63.42           O  
ANISOU 2732  OE2 GLU A 402     7724   8276   8098    856    116   -211       O  
ATOM   2733  N   LEU A 403      19.489  17.259   6.569  1.00 20.27           N  
ANISOU 2733  N   LEU A 403     2338   2824   2541    636    127   -229       N  
ATOM   2734  CA  LEU A 403      20.841  17.727   6.280  1.00 22.23           C  
ANISOU 2734  CA  LEU A 403     2659   3003   2784    614    111   -238       C  
ATOM   2735  C   LEU A 403      21.255  17.289   4.881  1.00 24.46           C  
ANISOU 2735  C   LEU A 403     2950   3268   3076    581     72   -204       C  
ATOM   2736  O   LEU A 403      21.800  18.091   4.121  1.00 24.03           O  
ANISOU 2736  O   LEU A 403     2941   3158   3032    595     54   -198       O  
ATOM   2737  CB  LEU A 403      21.852  17.233   7.315  1.00 22.37           C  
ANISOU 2737  CB  LEU A 403     2708   3018   2774    569    128   -258       C  
ATOM   2738  CG  LEU A 403      21.656  17.762   8.737  1.00 32.29           C  
ANISOU 2738  CG  LEU A 403     3972   4288   4010    602    165   -297       C  
ATOM   2739  CD1 LEU A 403      22.708  17.183   9.677  1.00 31.26           C  
ANISOU 2739  CD1 LEU A 403     3871   4160   3845    556    173   -313       C  
ATOM   2740  CD2 LEU A 403      21.662  19.296   8.775  1.00 25.97           C  
ANISOU 2740  CD2 LEU A 403     3212   3431   3225    660    166   -328       C  
ATOM   2741  N   ASP A 404      20.988  16.024   4.554  1.00 19.64           N  
ANISOU 2741  N   ASP A 404     2298   2702   2461    539     60   -184       N  
ATOM   2742  CA  ASP A 404      21.312  15.462   3.243  1.00 21.38           C  
ANISOU 2742  CA  ASP A 404     2523   2914   2684    509     22   -158       C  
ATOM   2743  C   ASP A 404      20.819  16.378   2.143  1.00 24.27           C  
ANISOU 2743  C   ASP A 404     2895   3262   3064    560     -3   -142       C  
ATOM   2744  O   ASP A 404      21.572  16.753   1.244  1.00 28.86           O  
ANISOU 2744  O   ASP A 404     3523   3800   3642    557    -22   -128       O  
ATOM   2745  CB  ASP A 404      20.626  14.109   3.063  1.00 25.37           C  
ANISOU 2745  CB  ASP A 404     2969   3477   3194    472     12   -144       C  
ATOM   2746  CG  ASP A 404      21.366  12.967   3.737  1.00 24.12           C  
ANISOU 2746  CG  ASP A 404     2817   3326   3023    411     26   -146       C  
ATOM   2747  OD1 ASP A 404      22.320  13.202   4.504  1.00 24.24           O  
ANISOU 2747  OD1 ASP A 404     2876   3313   3022    399     45   -161       O  
ATOM   2748  OD2 ASP A 404      20.973  11.817   3.494  1.00 23.77           O  
ANISOU 2748  OD2 ASP A 404     2732   3313   2985    374     14   -134       O  
ATOM   2749  N   ARG A 405      19.547  16.750   2.240  1.00 23.02           N  
ANISOU 2749  N   ARG A 405     2687   3139   2921    609      0   -142       N  
ATOM   2750  CA  ARG A 405      18.910  17.610   1.249  1.00 33.12           C  
ANISOU 2750  CA  ARG A 405     3963   4409   4214    667    -27   -124       C  
ATOM   2751  C   ARG A 405      19.640  18.953   1.113  1.00 30.83           C  
ANISOU 2751  C   ARG A 405     3743   4043   3928    703    -20   -126       C  
ATOM   2752  O   ARG A 405      19.872  19.430   0.001  1.00 24.29           O  
ANISOU 2752  O   ARG A 405     2945   3184   3099    720    -46    -99       O  
ATOM   2753  CB  ARG A 405      17.434  17.817   1.610  1.00 43.96           C  
ANISOU 2753  CB  ARG A 405     5264   5833   5605    719    -19   -128       C  
ATOM   2754  CG  ARG A 405      16.573  18.410   0.500  1.00 55.97           C  
ANISOU 2754  CG  ARG A 405     6762   7364   7139    777    -56   -105       C  
ATOM   2755  CD  ARG A 405      15.124  18.551   0.950  1.00 60.10           C  
ANISOU 2755  CD  ARG A 405     7212   7938   7686    811    -44   -108       C  
ATOM   2756  N   ARG A 406      20.023  19.540   2.244  1.00 24.64           N  
ANISOU 2756  N   ARG A 406     2986   3229   3146    711     15   -156       N  
ATOM   2757  CA  ARG A 406      20.708  20.833   2.243  1.00 28.33           C  
ANISOU 2757  CA  ARG A 406     3519   3618   3627    740     22   -164       C  
ATOM   2758  C   ARG A 406      22.107  20.743   1.670  1.00 28.30           C  
ANISOU 2758  C   ARG A 406     3572   3564   3616    689     11   -150       C  
ATOM   2759  O   ARG A 406      22.512  21.587   0.872  1.00 32.90           O  
ANISOU 2759  O   ARG A 406     4198   4091   4212    709      1   -128       O  
ATOM   2760  CB  ARG A 406      20.768  21.437   3.652  1.00 26.72           C  
ANISOU 2760  CB  ARG A 406     3330   3397   3427    760     58   -209       C  
ATOM   2761  CG  ARG A 406      19.395  21.718   4.227  1.00 32.90           C  
ANISOU 2761  CG  ARG A 406     4061   4223   4218    804     76   -219       C  
ATOM   2762  CD  ARG A 406      19.444  22.438   5.564  1.00 37.17           C  
ANISOU 2762  CD  ARG A 406     4624   4742   4758    813    110   -261       C  
ATOM   2763  NE  ARG A 406      18.181  22.247   6.271  1.00 49.09           N  
ANISOU 2763  NE  ARG A 406     6073   6314   6264    837    134   -268       N  
ATOM   2764  CZ  ARG A 406      17.487  23.219   6.855  1.00 56.74           C  
ANISOU 2764  CZ  ARG A 406     7042   7270   7248    879    155   -287       C  
ATOM   2765  NH1 ARG A 406      17.938  24.468   6.827  1.00 57.71           N  
ANISOU 2765  NH1 ARG A 406     7221   7315   7391    900    153   -302       N  
ATOM   2766  NH2 ARG A 406      16.340  22.939   7.470  1.00 56.48           N  
ANISOU 2766  NH2 ARG A 406     6950   7298   7212    899    179   -289       N  
ATOM   2767  N   VAL A 407      22.846  19.723   2.096  1.00 26.40           N  
ANISOU 2767  N   VAL A 407     3331   3342   3357    625     16   -160       N  
ATOM   2768  CA  VAL A 407      24.178  19.479   1.578  1.00 22.56           C  
ANISOU 2768  CA  VAL A 407     2888   2818   2864    574      8   -147       C  
ATOM   2769  C   VAL A 407      24.090  19.330   0.060  1.00 18.08           C  
ANISOU 2769  C   VAL A 407     2324   2253   2292    579    -20   -105       C  
ATOM   2770  O   VAL A 407      24.848  19.947  -0.689  1.00 16.30           O  
ANISOU 2770  O   VAL A 407     2145   1977   2072    579    -24    -82       O  
ATOM   2771  CB  VAL A 407      24.791  18.208   2.202  1.00 19.95           C  
ANISOU 2771  CB  VAL A 407     2545   2522   2514    511     14   -160       C  
ATOM   2772  CG1 VAL A 407      26.004  17.749   1.408  1.00 13.07           C  
ANISOU 2772  CG1 VAL A 407     1706   1626   1636    463      2   -140       C  
ATOM   2773  CG2 VAL A 407      25.152  18.457   3.664  1.00 15.98           C  
ANISOU 2773  CG2 VAL A 407     2053   2010   2008    505     40   -201       C  
ATOM   2774  N   LEU A 408      23.134  18.522  -0.372  1.00 17.64           N  
ANISOU 2774  N   LEU A 408     2218   2260   2225    584    -40    -94       N  
ATOM   2775  CA  LEU A 408      22.881  18.285  -1.779  1.00 18.95           C  
ANISOU 2775  CA  LEU A 408     2381   2442   2378    594    -73    -60       C  
ATOM   2776  C   LEU A 408      22.622  19.586  -2.554  1.00 22.60           C  
ANISOU 2776  C   LEU A 408     2873   2865   2850    655    -82    -32       C  
ATOM   2777  O   LEU A 408      23.364  19.929  -3.480  1.00 17.51           O  
ANISOU 2777  O   LEU A 408     2274   2183   2196    652    -88     -2       O  
ATOM   2778  CB  LEU A 408      21.702  17.321  -1.922  1.00 25.00           C  
ANISOU 2778  CB  LEU A 408     3079   3282   3139    594    -95    -62       C  
ATOM   2779  CG  LEU A 408      21.079  17.190  -3.308  1.00 38.51           C  
ANISOU 2779  CG  LEU A 408     4774   5021   4836    619   -138    -35       C  
ATOM   2780  CD1 LEU A 408      22.150  16.797  -4.309  1.00 41.17           C  
ANISOU 2780  CD1 LEU A 408     5159   5338   5145    585   -152    -17       C  
ATOM   2781  CD2 LEU A 408      19.951  16.172  -3.285  1.00 41.32           C  
ANISOU 2781  CD2 LEU A 408     5055   5448   5195    608   -161    -46       C  
ATOM   2782  N   GLU A 409      21.590  20.318  -2.153  1.00 23.73           N  
ANISOU 2782  N   GLU A 409     2990   3013   3013    713    -78    -39       N  
ATOM   2783  CA  GLU A 409      21.225  21.558  -2.829  1.00 23.30           C  
ANISOU 2783  CA  GLU A 409     2961   2920   2972    780    -87    -11       C  
ATOM   2784  C   GLU A 409      22.339  22.599  -2.837  1.00 27.02           C  
ANISOU 2784  C   GLU A 409     3504   3301   3459    778    -65     -1       C  
ATOM   2785  O   GLU A 409      22.448  23.399  -3.774  1.00 21.86           O  
ANISOU 2785  O   GLU A 409     2888   2608   2810    813    -75     39       O  
ATOM   2786  CB  GLU A 409      19.941  22.148  -2.225  1.00 25.28           C  
ANISOU 2786  CB  GLU A 409     3168   3192   3246    846    -82    -26       C  
ATOM   2787  CG  GLU A 409      18.697  21.262  -2.393  1.00 33.32           C  
ANISOU 2787  CG  GLU A 409     4106   4298   4257    855   -107    -27       C  
ATOM   2788  CD  GLU A 409      18.291  21.037  -3.851  1.00 48.25           C  
ANISOU 2788  CD  GLU A 409     5986   6218   6127    867   -154     12       C  
ATOM   2789  OE1 GLU A 409      18.872  21.673  -4.772  1.00 54.38           O  
ANISOU 2789  OE1 GLU A 409     6820   6949   6893    879   -164     46       O  
ATOM   2790  OE2 GLU A 409      17.375  20.213  -4.072  1.00 47.21           O  
ANISOU 2790  OE2 GLU A 409     5790   6158   5992    861   -180      8       O  
ATOM   2791  N   PHE A 410      23.176  22.589  -1.803  1.00 25.31           N  
ANISOU 2791  N   PHE A 410     3309   3054   3254    737    -38    -36       N  
ATOM   2792  CA  PHE A 410      24.222  23.606  -1.703  1.00 27.51           C  
ANISOU 2792  CA  PHE A 410     3650   3244   3558    730    -19    -34       C  
ATOM   2793  C   PHE A 410      25.466  23.171  -2.444  1.00 28.55           C  
ANISOU 2793  C   PHE A 410     3814   3358   3675    673    -20     -7       C  
ATOM   2794  O   PHE A 410      26.500  23.834  -2.376  1.00 28.62           O  
ANISOU 2794  O   PHE A 410     3869   3298   3707    651     -3     -4       O  
ATOM   2795  CB  PHE A 410      24.540  23.950  -0.245  1.00 26.66           C  
ANISOU 2795  CB  PHE A 410     3551   3109   3471    718      7    -89       C  
ATOM   2796  CG  PHE A 410      23.361  24.492   0.511  1.00 35.14           C  
ANISOU 2796  CG  PHE A 410     4596   4197   4557    778     16   -117       C  
ATOM   2797  CD1 PHE A 410      22.337  25.156  -0.162  1.00 38.23           C  
ANISOU 2797  CD1 PHE A 410     4971   4592   4961    828      4    -87       C  
ATOM   2798  CD2 PHE A 410      23.255  24.323   1.889  1.00 40.10           C  
ANISOU 2798  CD2 PHE A 410     5208   4846   5182    767     37   -170       C  
ATOM   2799  CE1 PHE A 410      21.238  25.657   0.527  1.00 44.32           C  
ANISOU 2799  CE1 PHE A 410     5709   5383   5747    867     15   -110       C  
ATOM   2800  CE2 PHE A 410      22.153  24.823   2.589  1.00 44.75           C  
ANISOU 2800  CE2 PHE A 410     5766   5457   5781    806     50   -192       C  
ATOM   2801  CZ  PHE A 410      21.146  25.489   1.907  1.00 47.16           C  
ANISOU 2801  CZ  PHE A 410     6053   5761   6103    856     40   -163       C  
ATOM   2802  N   GLY A 411      25.357  22.044  -3.148  1.00 24.33           N  
ANISOU 2802  N   GLY A 411     3254   2885   3106    649    -40     10       N  
ATOM   2803  CA  GLY A 411      26.435  21.566  -3.991  1.00 23.64           C  
ANISOU 2803  CA  GLY A 411     3194   2789   2998    604    -40     37       C  
ATOM   2804  C   GLY A 411      27.488  20.742  -3.267  1.00 25.48           C  
ANISOU 2804  C   GLY A 411     3427   3026   3230    536    -25      7       C  
ATOM   2805  O   GLY A 411      28.557  20.478  -3.818  1.00 22.44           O  
ANISOU 2805  O   GLY A 411     3067   2623   2836    498    -19     26       O  
ATOM   2806  N   GLY A 412      27.187  20.332  -2.037  1.00 20.49           N  
ANISOU 2806  N   GLY A 412     2765   2418   2603    523    -19    -37       N  
ATOM   2807  CA  GLY A 412      28.097  19.498  -1.279  1.00 20.92           C  
ANISOU 2807  CA  GLY A 412     2816   2482   2652    464     -9    -63       C  
ATOM   2808  C   GLY A 412      27.892  17.999  -1.459  1.00 21.68           C  
ANISOU 2808  C   GLY A 412     2875   2644   2719    432    -23    -65       C  
ATOM   2809  O   GLY A 412      27.090  17.560  -2.276  1.00 15.30           O  
ANISOU 2809  O   GLY A 412     2045   1875   1894    451    -44    -47       O  
ATOM   2810  N   ARG A 413      28.627  17.213  -0.683  1.00 19.19           N  
ANISOU 2810  N   ARG A 413     2554   2338   2399    384    -13    -87       N  
ATOM   2811  CA  ARG A 413      28.490  15.765  -0.702  1.00 20.22           C  
ANISOU 2811  CA  ARG A 413     2653   2521   2509    351    -24    -91       C  
ATOM   2812  C   ARG A 413      28.776  15.140   0.668  1.00 18.65           C  
ANISOU 2812  C   ARG A 413     2438   2338   2309    320    -10   -121       C  
ATOM   2813  O   ARG A 413      29.409  15.745   1.534  1.00 17.99           O  
ANISOU 2813  O   ARG A 413     2374   2223   2236    314      5   -141       O  
ATOM   2814  CB  ARG A 413      29.441  15.146  -1.740  1.00 14.10           C  
ANISOU 2814  CB  ARG A 413     1897   1740   1719    321    -30    -69       C  
ATOM   2815  CG  ARG A 413      30.925  15.446  -1.486  1.00 14.49           C  
ANISOU 2815  CG  ARG A 413     1980   1744   1781    289    -12    -70       C  
ATOM   2816  CD  ARG A 413      31.435  16.586  -2.400  1.00 16.79           C  
ANISOU 2816  CD  ARG A 413     2311   1986   2084    307     -4    -40       C  
ATOM   2817  NE  ARG A 413      31.074  16.317  -3.787  1.00 16.33           N  
ANISOU 2817  NE  ARG A 413     2257   1949   1999    326    -18     -8       N  
ATOM   2818  CZ  ARG A 413      31.756  15.503  -4.588  1.00 22.34           C  
ANISOU 2818  CZ  ARG A 413     3025   2725   2738    302    -19      5       C  
ATOM   2819  NH1 ARG A 413      32.853  14.900  -4.144  1.00 19.44           N  
ANISOU 2819  NH1 ARG A 413     2658   2351   2377    259     -5     -7       N  
ATOM   2820  NH2 ARG A 413      31.337  15.281  -5.828  1.00 18.40           N  
ANISOU 2820  NH2 ARG A 413     2533   2251   2208    325    -35     29       N  
ATOM   2821  N   LEU A 414      28.298  13.913   0.825  1.00 17.47           N  
ANISOU 2821  N   LEU A 414     2253   2237   2148    299    -17   -122       N  
ATOM   2822  CA  LEU A 414      28.719  12.999   1.872  1.00 17.72           C  
ANISOU 2822  CA  LEU A 414     2272   2286   2173    262     -6   -138       C  
ATOM   2823  C   LEU A 414      29.892  12.141   1.389  1.00 19.04           C  
ANISOU 2823  C   LEU A 414     2457   2444   2335    221    -12   -129       C  
ATOM   2824  O   LEU A 414      30.224  12.119   0.199  1.00 22.89           O  
ANISOU 2824  O   LEU A 414     2959   2918   2819    220    -23   -111       O  
ATOM   2825  CB  LEU A 414      27.561  12.070   2.214  1.00 17.64           C  
ANISOU 2825  CB  LEU A 414     2214   2330   2160    260     -8   -138       C  
ATOM   2826  CG  LEU A 414      26.276  12.790   2.592  1.00 21.59           C  
ANISOU 2826  CG  LEU A 414     2685   2851   2668    305     -1   -144       C  
ATOM   2827  CD1 LEU A 414      25.131  11.807   2.736  1.00 22.83           C  
ANISOU 2827  CD1 LEU A 414     2785   3061   2827    297     -4   -139       C  
ATOM   2828  CD2 LEU A 414      26.489  13.562   3.873  1.00 24.44           C  
ANISOU 2828  CD2 LEU A 414     3062   3200   3026    321     24   -169       C  
ATOM   2829  N   TYR A 415      30.468  11.397   2.323  1.00 20.37           N  
ANISOU 2829  N   TYR A 415     2620   2620   2498    190     -3   -139       N  
ATOM   2830  CA  TYR A 415      31.664  10.583   2.120  1.00 17.32           C  
ANISOU 2830  CA  TYR A 415     2248   2224   2110    153     -6   -133       C  
ATOM   2831  C   TYR A 415      31.290   9.119   2.363  1.00 17.32           C  
ANISOU 2831  C   TYR A 415     2219   2257   2104    129    -10   -129       C  
ATOM   2832  O   TYR A 415      30.766   8.778   3.435  1.00 22.28           O  
ANISOU 2832  O   TYR A 415     2826   2911   2729    126      0   -135       O  
ATOM   2833  CB  TYR A 415      32.674  11.027   3.172  1.00 16.45           C  
ANISOU 2833  CB  TYR A 415     2155   2093   2002    142      5   -150       C  
ATOM   2834  CG  TYR A 415      34.069  10.450   3.120  1.00 19.93           C  
ANISOU 2834  CG  TYR A 415     2608   2519   2445    109      3   -146       C  
ATOM   2835  CD1 TYR A 415      34.551   9.789   1.996  1.00 15.41           C  
ANISOU 2835  CD1 TYR A 415     2039   1941   1873     96     -2   -129       C  
ATOM   2836  CD2 TYR A 415      34.908  10.569   4.227  1.00 14.09           C  
ANISOU 2836  CD2 TYR A 415     1874   1774   1705     95      6   -163       C  
ATOM   2837  CE1 TYR A 415      35.839   9.282   1.972  1.00 13.25           C  
ANISOU 2837  CE1 TYR A 415     1773   1656   1604     71      0   -126       C  
ATOM   2838  CE2 TYR A 415      36.185  10.071   4.215  1.00 13.07           C  
ANISOU 2838  CE2 TYR A 415     1749   1634   1581     69      3   -159       C  
ATOM   2839  CZ  TYR A 415      36.655   9.431   3.090  1.00 18.78           C  
ANISOU 2839  CZ  TYR A 415     2474   2351   2310     57      2   -140       C  
ATOM   2840  OH  TYR A 415      37.945   8.944   3.101  1.00 19.29           O  
ANISOU 2840  OH  TYR A 415     2540   2407   2383     35      1   -136       O  
ATOM   2841  N   THR A 416      31.555   8.247   1.394  1.00  9.45           N  
ANISOU 2841  N   THR A 416     1223   1260   1106    112    -23   -119       N  
ATOM   2842  CA  THR A 416      31.230   6.825   1.559  1.00 14.04           C  
ANISOU 2842  CA  THR A 416     1781   1862   1690     86    -28   -116       C  
ATOM   2843  C   THR A 416      31.868   6.185   2.793  1.00 16.53           C  
ANISOU 2843  C   THR A 416     2095   2180   2005     64    -15   -116       C  
ATOM   2844  O   THR A 416      31.349   5.202   3.321  1.00 17.61           O  
ANISOU 2844  O   THR A 416     2209   2337   2146     47    -12   -109       O  
ATOM   2845  CB  THR A 416      31.648   5.966   0.343  1.00 13.94           C  
ANISOU 2845  CB  THR A 416     1778   1842   1676     72    -45   -113       C  
ATOM   2846  OG1 THR A 416      33.037   6.182   0.048  1.00 19.67           O  
ANISOU 2846  OG1 THR A 416     2536   2541   2398     67    -37   -110       O  
ATOM   2847  CG2 THR A 416      30.793   6.276  -0.868  1.00 16.34           C  
ANISOU 2847  CG2 THR A 416     2078   2156   1974     93    -65   -112       C  
ATOM   2848  N   ALA A 417      32.999   6.725   3.239  1.00 16.99           N  
ANISOU 2848  N   ALA A 417     2177   2219   2059     63     -8   -121       N  
ATOM   2849  CA  ALA A 417      33.704   6.166   4.398  1.00 15.85           C  
ANISOU 2849  CA  ALA A 417     2033   2079   1909     46      0   -121       C  
ATOM   2850  C   ALA A 417      32.974   6.469   5.692  1.00 15.63           C  
ANISOU 2850  C   ALA A 417     1992   2078   1868     57     13   -127       C  
ATOM   2851  O   ALA A 417      33.305   5.917   6.735  1.00 16.49           O  
ANISOU 2851  O   ALA A 417     2098   2201   1964     47     19   -123       O  
ATOM   2852  CB  ALA A 417      35.136   6.688   4.467  1.00 12.36           C  
ANISOU 2852  CB  ALA A 417     1615   1613   1470     41     -2   -128       C  
ATOM   2853  N   LYS A 418      31.967   7.336   5.610  1.00 18.28           N  
ANISOU 2853  N   LYS A 418     2319   2423   2204     83     17   -135       N  
ATOM   2854  CA  LYS A 418      31.253   7.807   6.790  1.00 20.69           C  
ANISOU 2854  CA  LYS A 418     2613   2754   2494    102     35   -145       C  
ATOM   2855  C   LYS A 418      29.755   7.552   6.720  1.00 25.71           C  
ANISOU 2855  C   LYS A 418     3212   3423   3136    113     44   -135       C  
ATOM   2856  O   LYS A 418      28.995   8.049   7.550  1.00 29.59           O  
ANISOU 2856  O   LYS A 418     3689   3938   3615    137     62   -143       O  
ATOM   2857  CB  LYS A 418      31.518   9.299   6.988  1.00 15.37           C  
ANISOU 2857  CB  LYS A 418     1964   2059   1818    129     36   -171       C  
ATOM   2858  CG  LYS A 418      32.939   9.596   7.439  1.00 21.86           C  
ANISOU 2858  CG  LYS A 418     2813   2856   2635    115     28   -185       C  
ATOM   2859  CD  LYS A 418      33.173   9.099   8.851  1.00 24.56           C  
ANISOU 2859  CD  LYS A 418     3154   3228   2950    110     35   -191       C  
ATOM   2860  CE  LYS A 418      34.446   9.676   9.451  1.00 32.30           C  
ANISOU 2860  CE  LYS A 418     4160   4189   3924    103     22   -215       C  
ATOM   2861  NZ  LYS A 418      34.276  11.067   9.952  1.00 29.74           N  
ANISOU 2861  NZ  LYS A 418     3853   3850   3595    130     24   -252       N  
ATOM   2862  N   ASP A 419      29.327   6.775   5.734  1.00 27.69           N  
ANISOU 2862  N   ASP A 419     3443   3673   3404     97     30   -121       N  
ATOM   2863  CA  ASP A 419      27.903   6.621   5.480  1.00 20.26           C  
ANISOU 2863  CA  ASP A 419     2461   2762   2476    107     31   -114       C  
ATOM   2864  C   ASP A 419      27.432   5.185   5.266  1.00 24.20           C  
ANISOU 2864  C   ASP A 419     2929   3273   2993     71     26    -96       C  
ATOM   2865  O   ASP A 419      28.035   4.434   4.501  1.00 30.42           O  
ANISOU 2865  O   ASP A 419     3730   4038   3789     47      7    -93       O  
ATOM   2866  CB  ASP A 419      27.496   7.439   4.256  1.00 20.02           C  
ANISOU 2866  CB  ASP A 419     2433   2719   2455    132     11   -121       C  
ATOM   2867  CG  ASP A 419      26.085   7.113   3.788  1.00 25.23           C  
ANISOU 2867  CG  ASP A 419     3044   3411   3132    137      2   -114       C  
ATOM   2868  OD1 ASP A 419      25.113   7.542   4.451  1.00 20.39           O  
ANISOU 2868  OD1 ASP A 419     2399   2827   2522    160     20   -115       O  
ATOM   2869  OD2 ASP A 419      25.949   6.410   2.767  1.00 21.38           O  
ANISOU 2869  OD2 ASP A 419     2548   2920   2656    119    -24   -110       O  
ATOM   2870  N   SER A 420      26.329   4.822   5.915  1.00 21.85           N  
ANISOU 2870  N   SER A 420     2587   3010   2703     69     44    -84       N  
ATOM   2871  CA  SER A 420      25.604   3.619   5.526  1.00 26.87           C  
ANISOU 2871  CA  SER A 420     3185   3657   3369     36     35    -69       C  
ATOM   2872  C   SER A 420      24.094   3.854   5.560  1.00 28.02           C  
ANISOU 2872  C   SER A 420     3273   3840   3532     49     43    -65       C  
ATOM   2873  O   SER A 420      23.313   2.902   5.622  1.00 27.39           O  
ANISOU 2873  O   SER A 420     3148   3776   3480     19     45    -49       O  
ATOM   2874  CB  SER A 420      26.003   2.406   6.379  1.00 26.11           C  
ANISOU 2874  CB  SER A 420     3089   3557   3275      0     53    -45       C  
ATOM   2875  OG  SER A 420      25.728   2.618   7.753  1.00 25.49           O  
ANISOU 2875  OG  SER A 420     3000   3509   3176     12     91    -32       O  
ATOM   2876  N   ARG A 421      23.687   5.120   5.495  1.00 22.82           N  
ANISOU 2876  N   ARG A 421     2614   3194   2863     94     45    -79       N  
ATOM   2877  CA  ARG A 421      22.275   5.465   5.667  1.00 20.03           C  
ANISOU 2877  CA  ARG A 421     2203   2882   2526    116     57    -76       C  
ATOM   2878  C   ARG A 421      21.597   6.227   4.522  1.00 20.06           C  
ANISOU 2878  C   ARG A 421     2190   2890   2542    148     25    -89       C  
ATOM   2879  O   ARG A 421      20.392   6.077   4.347  1.00 25.98           O  
ANISOU 2879  O   ARG A 421     2879   3674   3317    152     21    -84       O  
ATOM   2880  CB  ARG A 421      22.051   6.201   6.993  1.00 22.08           C  
ANISOU 2880  CB  ARG A 421     2461   3168   2762    150    101    -78       C  
ATOM   2881  CG  ARG A 421      23.002   7.359   7.220  1.00 30.35           C  
ANISOU 2881  CG  ARG A 421     3568   4187   3778    183    102   -101       C  
ATOM   2882  CD  ARG A 421      22.334   8.508   7.959  1.00 34.70           C  
ANISOU 2882  CD  ARG A 421     4108   4761   4316    237    131   -116       C  
ATOM   2883  NE  ARG A 421      21.199   9.058   7.214  1.00 37.22           N  
ANISOU 2883  NE  ARG A 421     4385   5097   4660    269    118   -118       N  
ATOM   2884  CZ  ARG A 421      21.291   9.956   6.236  1.00 30.44           C  
ANISOU 2884  CZ  ARG A 421     3547   4209   3808    299     89   -130       C  
ATOM   2885  NH1 ARG A 421      22.476  10.429   5.852  1.00 26.09           N  
ANISOU 2885  NH1 ARG A 421     3059   3610   3244    297     73   -141       N  
ATOM   2886  NH2 ARG A 421      20.185  10.381   5.638  1.00 23.08           N  
ANISOU 2886  NH2 ARG A 421     2573   3300   2898    332     78   -128       N  
ATOM   2887  N   THR A 422      22.346   7.028   3.757  1.00 18.77           N  
ANISOU 2887  N   THR A 422     2076   2694   2362    171      3   -102       N  
ATOM   2888  CA  THR A 422      21.758   7.835   2.667  1.00 22.39           C  
ANISOU 2888  CA  THR A 422     2527   3155   2826    209    -27   -108       C  
ATOM   2889  C   THR A 422      21.213   7.005   1.496  1.00 22.75           C  
ANISOU 2889  C   THR A 422     2542   3213   2891    186    -70   -107       C  
ATOM   2890  O   THR A 422      21.462   5.807   1.408  1.00 24.66           O  
ANISOU 2890  O   THR A 422     2779   3449   3143    138    -78   -105       O  
ATOM   2891  CB  THR A 422      22.725   8.944   2.151  1.00 21.58           C  
ANISOU 2891  CB  THR A 422     2487   3009   2701    239    -35   -116       C  
ATOM   2892  OG1 THR A 422      21.962  10.042   1.638  1.00 22.46           O  
ANISOU 2892  OG1 THR A 422     2588   3129   2818    292    -47   -117       O  
ATOM   2893  CG2 THR A 422      23.644   8.422   1.055  1.00 12.30           C  
ANISOU 2893  CG2 THR A 422     1350   1806   1518    213    -64   -114       C  
ATOM   2894  N   THR A 423      20.452   7.641   0.607  1.00 20.84           N  
ANISOU 2894  N   THR A 423     2279   2986   2652    222   -100   -110       N  
ATOM   2895  CA  THR A 423      19.804   6.924  -0.509  1.00 12.24           C  
ANISOU 2895  CA  THR A 423     1156   1916   1578    205   -147   -114       C  
ATOM   2896  C   THR A 423      20.585   7.027  -1.815  1.00 13.60           C  
ANISOU 2896  C   THR A 423     1382   2062   1722    211   -184   -120       C  
ATOM   2897  O   THR A 423      21.399   7.937  -2.004  1.00 20.21           O  
ANISOU 2897  O   THR A 423     2275   2870   2535    240   -174   -115       O  
ATOM   2898  CB  THR A 423      18.387   7.498  -0.799  1.00 25.37           C  
ANISOU 2898  CB  THR A 423     2755   3623   3259    245   -166   -112       C  
ATOM   2899  OG1 THR A 423      18.500   8.881  -1.177  1.00 20.45           O  
ANISOU 2899  OG1 THR A 423     2166   2988   2615    307   -169   -109       O  
ATOM   2900  CG2 THR A 423      17.488   7.388   0.427  1.00 17.73           C  
ANISOU 2900  CG2 THR A 423     1725   2691   2321    243   -126   -105       C  
ATOM   2901  N   ALA A 424      20.310   6.108  -2.729  1.00 18.44           N  
ANISOU 2901  N   ALA A 424     1979   2685   2341    184   -226   -131       N  
ATOM   2902  CA  ALA A 424      20.919   6.133  -4.058  1.00 15.26           C  
ANISOU 2902  CA  ALA A 424     1624   2267   1905    194   -263   -138       C  
ATOM   2903  C   ALA A 424      20.648   7.462  -4.766  1.00 20.64           C  
ANISOU 2903  C   ALA A 424     2321   2957   2563    257   -278   -127       C  
ATOM   2904  O   ALA A 424      21.530   8.031  -5.410  1.00 22.77           O  
ANISOU 2904  O   ALA A 424     2651   3200   2799    279   -278   -118       O  
ATOM   2905  CB  ALA A 424      20.412   4.983  -4.882  1.00 14.58           C  
ANISOU 2905  CB  ALA A 424     1509   2199   1830    161   -311   -159       C  
ATOM   2906  N   GLU A 425      19.428   7.960  -4.627  1.00 21.71           N  
ANISOU 2906  N   GLU A 425     2401   3128   2718    289   -289   -123       N  
ATOM   2907  CA  GLU A 425      19.050   9.219  -5.250  1.00 22.42           C  
ANISOU 2907  CA  GLU A 425     2501   3226   2790    354   -305   -108       C  
ATOM   2908  C   GLU A 425      19.873  10.386  -4.701  1.00 23.69           C  
ANISOU 2908  C   GLU A 425     2717   3343   2940    385   -260    -92       C  
ATOM   2909  O   GLU A 425      20.408  11.192  -5.457  1.00 22.10           O  
ANISOU 2909  O   GLU A 425     2567   3118   2711    419   -267    -77       O  
ATOM   2910  CB  GLU A 425      17.576   9.484  -5.015  1.00 25.79           C  
ANISOU 2910  CB  GLU A 425     2850   3700   3248    383   -320   -107       C  
ATOM   2911  CG  GLU A 425      17.091  10.809  -5.546  1.00 41.66           C  
ANISOU 2911  CG  GLU A 425     4866   5718   5246    458   -335    -90       C  
ATOM   2912  CD  GLU A 425      15.631  11.026  -5.224  1.00 53.17           C  
ANISOU 2912  CD  GLU A 425     6237   7225   6739    488   -346    -90       C  
ATOM   2913  OE1 GLU A 425      15.324  12.008  -4.515  1.00 55.52           O  
ANISOU 2913  OE1 GLU A 425     6528   7518   7051    534   -311    -80       O  
ATOM   2914  OE2 GLU A 425      14.798  10.195  -5.658  1.00 52.68           O  
ANISOU 2914  OE2 GLU A 425     6113   7207   6695    464   -388   -103       O  
ATOM   2915  N   THR A 426      19.984  10.459  -3.381  1.00 17.63           N  
ANISOU 2915  N   THR A 426     1939   2566   2193    372   -215    -96       N  
ATOM   2916  CA  THR A 426      20.763  11.509  -2.741  1.00 17.74           C  
ANISOU 2916  CA  THR A 426     2002   2538   2200    396   -175    -90       C  
ATOM   2917  C   THR A 426      22.243  11.438  -3.122  1.00 21.01           C  
ANISOU 2917  C   THR A 426     2486   2907   2591    371   -168    -86       C  
ATOM   2918  O   THR A 426      22.851  12.450  -3.473  1.00 24.45           O  
ANISOU 2918  O   THR A 426     2971   3306   3015    401   -160    -73       O  
ATOM   2919  CB  THR A 426      20.597  11.464  -1.206  1.00 19.86           C  
ANISOU 2919  CB  THR A 426     2246   2812   2488    385   -131   -100       C  
ATOM   2920  OG1 THR A 426      19.244  11.778  -0.879  1.00 20.52           O  
ANISOU 2920  OG1 THR A 426     2266   2936   2593    420   -130   -100       O  
ATOM   2921  CG2 THR A 426      21.503  12.476  -0.529  1.00 16.27           C  
ANISOU 2921  CG2 THR A 426     1846   2310   2025    403    -96   -103       C  
ATOM   2922  N   PHE A 427      22.817  10.243  -3.072  1.00 13.35           N  
ANISOU 2922  N   PHE A 427     1519   1937   1618    318   -169    -95       N  
ATOM   2923  CA  PHE A 427      24.229  10.096  -3.374  1.00 12.94           C  
ANISOU 2923  CA  PHE A 427     1524   1846   1546    295   -159    -93       C  
ATOM   2924  C   PHE A 427      24.517  10.417  -4.841  1.00 18.95           C  
ANISOU 2924  C   PHE A 427     2322   2601   2279    318   -186    -80       C  
ATOM   2925  O   PHE A 427      25.469  11.139  -5.142  1.00 20.30           O  
ANISOU 2925  O   PHE A 427     2543   2736   2436    329   -170    -65       O  
ATOM   2926  CB  PHE A 427      24.721   8.689  -3.025  1.00 15.65           C  
ANISOU 2926  CB  PHE A 427     1861   2191   1894    238   -156   -105       C  
ATOM   2927  CG  PHE A 427      26.194   8.478  -3.284  1.00 19.36           C  
ANISOU 2927  CG  PHE A 427     2383   2624   2347    216   -143   -103       C  
ATOM   2928  CD1 PHE A 427      27.135   8.756  -2.289  1.00 17.64           C  
ANISOU 2928  CD1 PHE A 427     2188   2379   2135    203   -109   -103       C  
ATOM   2929  CD2 PHE A 427      26.642   7.999  -4.511  1.00 16.35           C  
ANISOU 2929  CD2 PHE A 427     2027   2241   1943    211   -166   -104       C  
ATOM   2930  CE1 PHE A 427      28.493   8.557  -2.518  1.00 16.29           C  
ANISOU 2930  CE1 PHE A 427     2057   2178   1953    184    -98   -100       C  
ATOM   2931  CE2 PHE A 427      28.000   7.801  -4.745  1.00 14.50           C  
ANISOU 2931  CE2 PHE A 427     1837   1978   1696    194   -150   -101       C  
ATOM   2932  CZ  PHE A 427      28.926   8.084  -3.742  1.00 10.52           C  
ANISOU 2932  CZ  PHE A 427     1348   1445   1204    180   -116    -98       C  
ATOM   2933  N   HIS A 428      23.703   9.884  -5.752  1.00 16.62           N  
ANISOU 2933  N   HIS A 428     2000   2342   1973    324   -228    -84       N  
ATOM   2934  CA  HIS A 428      23.932  10.133  -7.172  1.00 19.78           C  
ANISOU 2934  CA  HIS A 428     2435   2744   2335    350   -257    -72       C  
ATOM   2935  C   HIS A 428      23.865  11.638  -7.422  1.00 20.71           C  
ANISOU 2935  C   HIS A 428     2580   2844   2447    406   -247    -43       C  
ATOM   2936  O   HIS A 428      24.683  12.196  -8.149  1.00 20.30           O  
ANISOU 2936  O   HIS A 428     2580   2765   2368    422   -239    -20       O  
ATOM   2937  CB  HIS A 428      22.917   9.392  -8.059  1.00 15.12           C  
ANISOU 2937  CB  HIS A 428     1808   2202   1735    352   -311    -87       C  
ATOM   2938  CG  HIS A 428      23.236   7.942  -8.287  1.00 17.93           C  
ANISOU 2938  CG  HIS A 428     2161   2564   2089    301   -327   -115       C  
ATOM   2939  ND1 HIS A 428      23.307   7.385  -9.547  1.00 19.62           N  
ANISOU 2939  ND1 HIS A 428     2394   2795   2266    303   -367   -128       N  
ATOM   2940  CD2 HIS A 428      23.489   6.937  -7.413  1.00 11.68           C  
ANISOU 2940  CD2 HIS A 428     1350   1761   1327    249   -308   -133       C  
ATOM   2941  CE1 HIS A 428      23.583   6.095  -9.441  1.00 17.42           C  
ANISOU 2941  CE1 HIS A 428     2109   2512   1998    254   -373   -157       C  
ATOM   2942  NE2 HIS A 428      23.696   5.800  -8.159  1.00 20.72           N  
ANISOU 2942  NE2 HIS A 428     2503   2911   2458    220   -338   -157       N  
ATOM   2943  N   ALA A 429      22.905  12.307  -6.799  1.00 12.07           N  
ANISOU 2943  N   ALA A 429     1448   1759   1377    437   -245    -41       N  
ATOM   2944  CA  ALA A 429      22.787  13.736  -7.035  1.00 18.09           C  
ANISOU 2944  CA  ALA A 429     2236   2497   2138    494   -237    -13       C  
ATOM   2945  C   ALA A 429      24.023  14.516  -6.520  1.00 19.83           C  
ANISOU 2945  C   ALA A 429     2512   2656   2367    486   -192     -2       C  
ATOM   2946  O   ALA A 429      24.436  15.496  -7.127  1.00 18.63           O  
ANISOU 2946  O   ALA A 429     2403   2470   2204    519   -185     27       O  
ATOM   2947  CB  ALA A 429      21.493  14.264  -6.452  1.00 15.36           C  
ANISOU 2947  CB  ALA A 429     1838   2176   1821    533   -243    -17       C  
ATOM   2948  N   MET A 430      24.627  14.041  -5.434  1.00 18.88           N  
ANISOU 2948  N   MET A 430     2388   2520   2264    442   -163    -25       N  
ATOM   2949  CA  MET A 430      25.829  14.651  -4.845  1.00 17.22           C  
ANISOU 2949  CA  MET A 430     2222   2255   2065    426   -125    -22       C  
ATOM   2950  C   MET A 430      27.109  14.431  -5.657  1.00 18.68           C  
ANISOU 2950  C   MET A 430     2453   2416   2228    401   -118     -6       C  
ATOM   2951  O   MET A 430      28.107  15.133  -5.469  1.00 17.86           O  
ANISOU 2951  O   MET A 430     2386   2264   2135    395    -91      5       O  
ATOM   2952  CB  MET A 430      26.051  14.113  -3.431  1.00 15.54           C  
ANISOU 2952  CB  MET A 430     1988   2044   1872    389   -101    -52       C  
ATOM   2953  CG  MET A 430      24.985  14.511  -2.413  1.00 12.22           C  
ANISOU 2953  CG  MET A 430     1529   1642   1473    415    -93    -67       C  
ATOM   2954  SD  MET A 430      25.252  13.704  -0.824  1.00 20.72           S  
ANISOU 2954  SD  MET A 430     2583   2732   2558    370    -65    -96       S  
ATOM   2955  CE  MET A 430      24.229  14.753   0.215  1.00 17.89           C  
ANISOU 2955  CE  MET A 430     2200   2379   2217    421    -45   -111       C  
ATOM   2956  N   TYR A 431      27.083  13.449  -6.548  1.00 18.71           N  
ANISOU 2956  N   TYR A 431     2452   2453   2204    387   -142     -6       N  
ATOM   2957  CA  TYR A 431      28.244  13.146  -7.375  1.00 17.95           C  
ANISOU 2957  CA  TYR A 431     2396   2341   2082    369   -134      7       C  
ATOM   2958  C   TYR A 431      27.907  13.251  -8.866  1.00 23.18           C  
ANISOU 2958  C   TYR A 431     3078   3028   2703    404   -161     31       C  
ATOM   2959  O   TYR A 431      27.600  12.247  -9.518  1.00 29.68           O  
ANISOU 2959  O   TYR A 431     3888   3890   3498    395   -191     15       O  
ATOM   2960  CB  TYR A 431      28.775  11.752  -7.038  1.00 16.93           C  
ANISOU 2960  CB  TYR A 431     2254   2227   1953    318   -133    -20       C  
ATOM   2961  CG  TYR A 431      29.507  11.695  -5.714  1.00 18.97           C  
ANISOU 2961  CG  TYR A 431     2509   2458   2242    284   -102    -34       C  
ATOM   2962  CD1 TYR A 431      28.804  11.691  -4.511  1.00 13.28           C  
ANISOU 2962  CD1 TYR A 431     1754   1746   1546    280    -98    -53       C  
ATOM   2963  CD2 TYR A 431      30.907  11.644  -5.664  1.00 15.11           C  
ANISOU 2963  CD2 TYR A 431     2049   1937   1754    257    -76    -29       C  
ATOM   2964  CE1 TYR A 431      29.456  11.653  -3.299  1.00 14.43           C  
ANISOU 2964  CE1 TYR A 431     1899   1872   1710    253    -73    -67       C  
ATOM   2965  CE2 TYR A 431      31.578  11.599  -4.443  1.00 18.32           C  
ANISOU 2965  CE2 TYR A 431     2451   2324   2186    228    -54    -44       C  
ATOM   2966  CZ  TYR A 431      30.843  11.606  -3.266  1.00 19.87           C  
ANISOU 2966  CZ  TYR A 431     2618   2532   2401    227    -55    -63       C  
ATOM   2967  OH  TYR A 431      31.479  11.563  -2.055  1.00 15.21           O  
ANISOU 2967  OH  TYR A 431     2026   1927   1828    203    -36    -78       O  
ATOM   2968  N   PRO A 432      27.955  14.473  -9.415  1.00 19.81           N  
ANISOU 2968  N   PRO A 432     2683   2576   2269    446   -153     69       N  
ATOM   2969  CA  PRO A 432      27.583  14.686 -10.824  1.00 13.25           C  
ANISOU 2969  CA  PRO A 432     1873   1770   1391    488   -180     98       C  
ATOM   2970  C   PRO A 432      28.394  13.846 -11.805  1.00 16.08           C  
ANISOU 2970  C   PRO A 432     2259   2147   1702    470   -180     99       C  
ATOM   2971  O   PRO A 432      27.982  13.701 -12.958  1.00 18.74           O  
ANISOU 2971  O   PRO A 432     2608   2520   1990    501   -211    110       O  
ATOM   2972  CB  PRO A 432      27.838  16.182 -11.045  1.00 10.77           C  
ANISOU 2972  CB  PRO A 432     1598   1409   1086    527   -155    145       C  
ATOM   2973  CG  PRO A 432      28.513  16.671  -9.796  1.00 19.45           C  
ANISOU 2973  CG  PRO A 432     2698   2453   2238    497   -116    133       C  
ATOM   2974  CD  PRO A 432      28.189  15.735  -8.698  1.00 18.09           C  
ANISOU 2974  CD  PRO A 432     2480   2305   2088    460   -123     84       C  
ATOM   2975  N   ARG A 433      29.511  13.286 -11.353  1.00 13.83           N  
ANISOU 2975  N   ARG A 433     1984   1841   1431    423   -148     84       N  
ATOM   2976  CA  ARG A 433      30.331  12.437 -12.218  1.00 18.89           C  
ANISOU 2976  CA  ARG A 433     2648   2497   2030    408   -144     81       C  
ATOM   2977  C   ARG A 433      30.057  10.942 -12.031  1.00 20.33           C  
ANISOU 2977  C   ARG A 433     2802   2714   2211    374   -171     31       C  
ATOM   2978  O   ARG A 433      30.736  10.108 -12.624  1.00 16.29           O  
ANISOU 2978  O   ARG A 433     2308   2212   1670    360   -168     18       O  
ATOM   2979  CB  ARG A 433      31.815  12.755 -12.058  1.00 10.21           C  
ANISOU 2979  CB  ARG A 433     1579   1355    945    383    -91    102       C  
ATOM   2980  CG  ARG A 433      32.162  14.155 -12.540  1.00 14.82           C  
ANISOU 2980  CG  ARG A 433     2200   1905   1528    414    -63    157       C  
ATOM   2981  CD  ARG A 433      33.631  14.481 -12.400  1.00 12.53           C  
ANISOU 2981  CD  ARG A 433     1930   1571   1258    384    -11    178       C  
ATOM   2982  NE  ARG A 433      34.452  13.641 -13.257  1.00 24.50           N  
ANISOU 2982  NE  ARG A 433     3464   3113   2732    375      3    179       N  
ATOM   2983  CZ  ARG A 433      35.771  13.521 -13.132  1.00 25.72           C  
ANISOU 2983  CZ  ARG A 433     3625   3245   2903    344     46    187       C  
ATOM   2984  NH1 ARG A 433      36.407  14.200 -12.185  1.00 24.68           N  
ANISOU 2984  NH1 ARG A 433     3484   3063   2830    315     73    194       N  
ATOM   2985  NH2 ARG A 433      36.454  12.721 -13.947  1.00 18.87           N  
ANISOU 2985  NH2 ARG A 433     2771   2405   1993    342     60    185       N  
ATOM   2986  N   VAL A 434      29.028  10.616 -11.250  1.00 15.05           N  
ANISOU 2986  N   VAL A 434     2087   2060   1573    365   -197      4       N  
ATOM   2987  CA  VAL A 434      28.698   9.218 -10.976  1.00 18.72           C  
ANISOU 2987  CA  VAL A 434     2518   2548   2045    329   -222    -40       C  
ATOM   2988  C   VAL A 434      28.370   8.370 -12.217  1.00 23.53           C  
ANISOU 2988  C   VAL A 434     3137   3197   2608    339   -264    -60       C  
ATOM   2989  O   VAL A 434      28.793   7.218 -12.295  1.00 27.39           O  
ANISOU 2989  O   VAL A 434     3626   3687   3093    307   -267    -91       O  
ATOM   2990  CB  VAL A 434      27.598   9.065  -9.898  1.00 18.36           C  
ANISOU 2990  CB  VAL A 434     2417   2513   2044    316   -237    -58       C  
ATOM   2991  CG1 VAL A 434      26.229   9.483 -10.434  1.00  8.70           C  
ANISOU 2991  CG1 VAL A 434     1168   1328    811    356   -280    -55       C  
ATOM   2992  CG2 VAL A 434      27.564   7.636  -9.386  1.00 13.42           C  
ANISOU 2992  CG2 VAL A 434     1763   1895   1440    268   -246    -95       C  
ATOM   2993  N   ASP A 435      27.651   8.921 -13.195  1.00 26.33           N  
ANISOU 2993  N   ASP A 435     3499   3581   2923    384   -296    -45       N  
ATOM   2994  CA  ASP A 435      27.352   8.143 -14.412  1.00 25.10           C  
ANISOU 2994  CA  ASP A 435     3355   3467   2714    397   -341    -69       C  
ATOM   2995  C   ASP A 435      28.609   7.873 -15.248  1.00 19.77           C  
ANISOU 2995  C   ASP A 435     2736   2785   1991    400   -313    -63       C  
ATOM   2996  O   ASP A 435      28.752   6.811 -15.844  1.00 24.24           O  
ANISOU 2996  O   ASP A 435     3312   3370   2528    388   -335   -101       O  
ATOM   2997  CB  ASP A 435      26.261   8.805 -15.266  1.00 23.42           C  
ANISOU 2997  CB  ASP A 435     3137   3296   2466    450   -389    -53       C  
ATOM   2998  CG  ASP A 435      24.882   8.805 -14.580  1.00 31.75           C  
ANISOU 2998  CG  ASP A 435     4125   4370   3567    447   -426    -70       C  
ATOM   2999  OD1 ASP A 435      24.599   7.914 -13.756  1.00 30.35           O  
ANISOU 2999  OD1 ASP A 435     3905   4190   3436    400   -430   -105       O  
ATOM   3000  OD2 ASP A 435      24.066   9.696 -14.875  1.00 37.14           O  
ANISOU 3000  OD2 ASP A 435     4796   5074   4241    494   -449    -44       O  
ATOM   3001  N   GLU A 436      29.515   8.839 -15.293  1.00 21.04           N  
ANISOU 3001  N   GLU A 436     2932   2917   2145    415   -263    -16       N  
ATOM   3002  CA  GLU A 436      30.823   8.637 -15.907  1.00 18.99           C  
ANISOU 3002  CA  GLU A 436     2718   2647   1851    413   -223     -5       C  
ATOM   3003  C   GLU A 436      31.525   7.478 -15.199  1.00 15.22           C  
ANISOU 3003  C   GLU A 436     2225   2149   1408    363   -207    -45       C  
ATOM   3004  O   GLU A 436      31.992   6.534 -15.835  1.00 17.55           O  
ANISOU 3004  O   GLU A 436     2539   2458   1670    359   -210    -73       O  
ATOM   3005  CB  GLU A 436      31.647   9.928 -15.795  1.00 16.32           C  
ANISOU 3005  CB  GLU A 436     2407   2272   1523    427   -168     54       C  
ATOM   3006  CG  GLU A 436      33.107   9.812 -16.168  1.00 24.44           C  
ANISOU 3006  CG  GLU A 436     3469   3283   2534    416   -115     72       C  
ATOM   3007  CD  GLU A 436      33.920  11.017 -15.709  1.00 27.05           C  
ANISOU 3007  CD  GLU A 436     3811   3565   2902    411    -61    123       C  
ATOM   3008  OE1 GLU A 436      33.323  12.080 -15.448  1.00 26.72           O  
ANISOU 3008  OE1 GLU A 436     3767   3506   2881    430    -66    153       O  
ATOM   3009  OE2 GLU A 436      35.160  10.903 -15.602  1.00 29.15           O  
ANISOU 3009  OE2 GLU A 436     4086   3809   3180    388    -14    133       O  
ATOM   3010  N   TRP A 437      31.576   7.553 -13.872  1.00 15.04           N  
ANISOU 3010  N   TRP A 437     2170   2095   1449    329   -189    -47       N  
ATOM   3011  CA  TRP A 437      32.210   6.510 -13.068  1.00 19.03           C  
ANISOU 3011  CA  TRP A 437     2659   2579   1991    284   -174    -78       C  
ATOM   3012  C   TRP A 437      31.573   5.128 -13.313  1.00 21.99           C  
ANISOU 3012  C   TRP A 437     3018   2977   2361    267   -218   -130       C  
ATOM   3013  O   TRP A 437      32.278   4.147 -13.577  1.00 21.08           O  
ANISOU 3013  O   TRP A 437     2918   2856   2237    252   -211   -155       O  
ATOM   3014  CB  TRP A 437      32.194   6.870 -11.577  1.00 13.44           C  
ANISOU 3014  CB  TRP A 437     1919   1841   1345    255   -154    -72       C  
ATOM   3015  CG  TRP A 437      32.868   5.829 -10.749  1.00 18.64           C  
ANISOU 3015  CG  TRP A 437     2565   2481   2038    214   -140    -96       C  
ATOM   3016  CD1 TRP A 437      34.193   5.767 -10.431  1.00 17.64           C  
ANISOU 3016  CD1 TRP A 437     2452   2328   1923    198    -99    -87       C  
ATOM   3017  CD2 TRP A 437      32.261   4.671 -10.165  1.00 18.09           C  
ANISOU 3017  CD2 TRP A 437     2463   2416   1994    184   -165   -132       C  
ATOM   3018  NE1 TRP A 437      34.450   4.651  -9.678  1.00 13.19           N  
ANISOU 3018  NE1 TRP A 437     1870   1754   1389    165   -100   -113       N  
ATOM   3019  CE2 TRP A 437      33.282   3.956  -9.505  1.00 13.08           C  
ANISOU 3019  CE2 TRP A 437     1830   1756   1385    154   -139   -139       C  
ATOM   3020  CE3 TRP A 437      30.954   4.172 -10.134  1.00  7.31           C  
ANISOU 3020  CE3 TRP A 437     1066   1074    639    178   -208   -155       C  
ATOM   3021  CZ2 TRP A 437      33.040   2.774  -8.821  1.00  6.64           C  
ANISOU 3021  CZ2 TRP A 437      989    933    600    122   -152   -165       C  
ATOM   3022  CZ3 TRP A 437      30.717   2.998  -9.456  1.00 13.72           C  
ANISOU 3022  CZ3 TRP A 437     1850   1878   1486    140   -219   -182       C  
ATOM   3023  CH2 TRP A 437      31.754   2.315  -8.803  1.00 13.97           C  
ANISOU 3023  CH2 TRP A 437     1889   1880   1539    113   -190   -185       C  
ATOM   3024  N   ILE A 438      30.249   5.062 -13.242  1.00 17.12           N  
ANISOU 3024  N   ILE A 438     2368   2383   1753    270   -264   -145       N  
ATOM   3025  CA  ILE A 438      29.530   3.820 -13.501  1.00 19.77           C  
ANISOU 3025  CA  ILE A 438     2682   2738   2091    250   -312   -194       C  
ATOM   3026  C   ILE A 438      29.878   3.247 -14.882  1.00 24.81           C  
ANISOU 3026  C   ILE A 438     3362   3399   2667    272   -332   -220       C  
ATOM   3027  O   ILE A 438      30.050   2.038 -15.039  1.00 24.42           O  
ANISOU 3027  O   ILE A 438     3316   3343   2621    248   -347   -263       O  
ATOM   3028  CB  ILE A 438      27.999   4.016 -13.350  1.00 18.31           C  
ANISOU 3028  CB  ILE A 438     2450   2582   1925    254   -360   -202       C  
ATOM   3029  CG1 ILE A 438      27.621   4.112 -11.865  1.00 18.14           C  
ANISOU 3029  CG1 ILE A 438     2381   2540   1970    223   -340   -193       C  
ATOM   3030  CG2 ILE A 438      27.213   2.883 -14.047  1.00 10.57           C  
ANISOU 3030  CG2 ILE A 438     1454   1629    934    242   -421   -254       C  
ATOM   3031  CD1 ILE A 438      26.171   4.554 -11.624  1.00 15.39           C  
ANISOU 3031  CD1 ILE A 438     1982   2222   1643    235   -375   -191       C  
ATOM   3032  N   SER A 439      30.019   4.121 -15.873  1.00 17.11           N  
ANISOU 3032  N   SER A 439     2423   2447   1632    319   -329   -191       N  
ATOM   3033  CA  SER A 439      30.391   3.695 -17.218  1.00 14.65           C  
ANISOU 3033  CA  SER A 439     2147   2153   1267    337   -331   -204       C  
ATOM   3034  C   SER A 439      31.739   2.990 -17.237  1.00 24.78           C  
ANISOU 3034  C   SER A 439     3458   3411   2545    323   -288   -216       C  
ATOM   3035  O   SER A 439      31.906   1.974 -17.909  1.00 24.20           O  
ANISOU 3035  O   SER A 439     3395   3340   2461    315   -298   -254       O  
ATOM   3036  CB  SER A 439      30.462   4.891 -18.162  1.00 21.39           C  
ANISOU 3036  CB  SER A 439     3031   3026   2069    386   -317   -154       C  
ATOM   3037  OG  SER A 439      29.384   4.862 -19.060  1.00 37.92           O  
ANISOU 3037  OG  SER A 439     5113   5155   4139    404   -366   -167       O  
ATOM   3038  N   VAL A 440      32.707   3.556 -16.520  1.00 21.40           N  
ANISOU 3038  N   VAL A 440     3042   2958   2132    321   -237   -183       N  
ATOM   3039  CA  VAL A 440      34.024   2.941 -16.413  1.00 20.75           C  
ANISOU 3039  CA  VAL A 440     2977   2851   2055    307   -192   -190       C  
ATOM   3040  C   VAL A 440      33.901   1.588 -15.722  1.00 22.24           C  
ANISOU 3040  C   VAL A 440     3141   3018   2293    266   -212   -241       C  
ATOM   3041  O   VAL A 440      34.492   0.604 -16.162  1.00 22.58           O  
ANISOU 3041  O   VAL A 440     3201   3053   2324    264   -206   -274       O  
ATOM   3042  CB  VAL A 440      35.021   3.854 -15.675  1.00 12.49           C  
ANISOU 3042  CB  VAL A 440     1928   1774   1044    298   -131   -139       C  
ATOM   3043  CG1 VAL A 440      36.404   3.221 -15.632  1.00  9.13           C  
ANISOU 3043  CG1 VAL A 440     1515   1329    625    287    -85   -146       C  
ATOM   3044  CG2 VAL A 440      35.077   5.205 -16.366  1.00 13.66           C  
ANISOU 3044  CG2 VAL A 440     2102   1936   1151    335   -111    -85       C  
ATOM   3045  N   ARG A 441      33.090   1.531 -14.670  1.00 22.64           N  
ANISOU 3045  N   ARG A 441     3147   3054   2400    234   -233   -244       N  
ATOM   3046  CA  ARG A 441      32.907   0.291 -13.933  1.00 19.32           C  
ANISOU 3046  CA  ARG A 441     2701   2608   2030    193   -249   -282       C  
ATOM   3047  C   ARG A 441      32.285  -0.806 -14.795  1.00 22.70           C  
ANISOU 3047  C   ARG A 441     3138   3051   2437    193   -301   -339       C  
ATOM   3048  O   ARG A 441      32.640  -1.983 -14.673  1.00 29.24           O  
ANISOU 3048  O   ARG A 441     3968   3851   3290    169   -301   -373       O  
ATOM   3049  CB  ARG A 441      32.074   0.523 -12.679  1.00 24.68           C  
ANISOU 3049  CB  ARG A 441     3331   3277   2768    162   -258   -268       C  
ATOM   3050  CG  ARG A 441      31.337  -0.709 -12.224  1.00 31.66           C  
ANISOU 3050  CG  ARG A 441     4185   4149   3696    124   -293   -307       C  
ATOM   3051  CD  ARG A 441      30.935  -0.636 -10.783  1.00 27.70           C  
ANISOU 3051  CD  ARG A 441     3640   3630   3255     91   -279   -286       C  
ATOM   3052  NE  ARG A 441      30.061  -1.752 -10.456  1.00 37.40           N  
ANISOU 3052  NE  ARG A 441     4834   4850   4525     54   -314   -317       N  
ATOM   3053  CZ  ARG A 441      30.467  -3.012 -10.300  1.00 37.46           C  
ANISOU 3053  CZ  ARG A 441     4849   4825   4561     26   -314   -344       C  
ATOM   3054  NH1 ARG A 441      31.741  -3.332 -10.439  1.00 25.53           N  
ANISOU 3054  NH1 ARG A 441     3375   3290   3036     36   -283   -344       N  
ATOM   3055  NH2 ARG A 441      29.589  -3.956  -9.993  1.00 46.36           N  
ANISOU 3055  NH2 ARG A 441     5943   5939   5732    -11   -345   -367       N  
ATOM   3056  N   ARG A 442      31.366  -0.413 -15.669  1.00 21.22           N  
ANISOU 3056  N   ARG A 442     2946   2898   2217    212   -336   -340       N  
ATOM   3057  CA  ARG A 442      30.758  -1.342 -16.619  1.00 29.39           C  
ANISOU 3057  CA  ARG A 442     3981   3943   3243    206   -376   -382       C  
ATOM   3058  C   ARG A 442      31.778  -1.896 -17.620  1.00 26.39           C  
ANISOU 3058  C   ARG A 442     3645   3560   2822    225   -350   -397       C  
ATOM   3059  O   ARG A 442      31.759  -3.081 -17.909  1.00 25.07           O  
ANISOU 3059  O   ARG A 442     3481   3375   2668    206   -367   -441       O  
ATOM   3060  CB  ARG A 442      29.588  -0.680 -17.367  1.00 33.61           C  
ANISOU 3060  CB  ARG A 442     4502   4520   3749    228   -418   -374       C  
ATOM   3061  CG  ARG A 442      28.466  -0.152 -16.463  1.00 35.00           C  
ANISOU 3061  CG  ARG A 442     4628   4706   3966    214   -445   -361       C  
ATOM   3062  CD  ARG A 442      27.352  -1.150 -16.276  1.00 30.89           C  
ANISOU 3062  CD  ARG A 442     4063   4183   3493    174   -494   -401       C  
ATOM   3063  NE  ARG A 442      26.258  -0.616 -15.471  1.00 28.05           N  
ANISOU 3063  NE  ARG A 442     3647   3838   3172    163   -516   -386       N  
ATOM   3064  CZ  ARG A 442      26.077  -0.905 -14.184  1.00 40.71           C  
ANISOU 3064  CZ  ARG A 442     5212   5421   4836    127   -509   -386       C  
ATOM   3065  NH1 ARG A 442      26.926  -1.727 -13.562  1.00 36.87           N  
ANISOU 3065  NH1 ARG A 442     4739   4892   4377     97   -481   -400       N  
ATOM   3066  NH2 ARG A 442      25.052  -0.375 -13.520  1.00 36.08           N  
ANISOU 3066  NH2 ARG A 442     4571   4855   4282    123   -526   -371       N  
ATOM   3067  N   LYS A 443      32.662  -1.049 -18.148  1.00 20.89           N  
ANISOU 3067  N   LYS A 443     2982   2878   2078    262   -309   -361       N  
ATOM   3068  CA  LYS A 443      33.704  -1.535 -19.047  1.00 24.02           C  
ANISOU 3068  CA  LYS A 443     3415   3274   2436    282   -277   -372       C  
ATOM   3069  C   LYS A 443      34.537  -2.614 -18.364  1.00 26.19           C  
ANISOU 3069  C   LYS A 443     3689   3507   2755    256   -254   -399       C  
ATOM   3070  O   LYS A 443      34.843  -3.640 -18.968  1.00 33.66           O  
ANISOU 3070  O   LYS A 443     4652   4444   3695    256   -257   -438       O  
ATOM   3071  CB  LYS A 443      34.631  -0.413 -19.529  1.00 31.10           C  
ANISOU 3071  CB  LYS A 443     4342   4189   3287    320   -225   -319       C  
ATOM   3072  CG  LYS A 443      34.051   0.514 -20.599  1.00 41.55           C  
ANISOU 3072  CG  LYS A 443     5679   5553   4553    356   -241   -292       C  
ATOM   3073  CD  LYS A 443      34.969   1.726 -20.832  1.00 53.00           C  
ANISOU 3073  CD  LYS A 443     7154   7011   5973    386   -183   -229       C  
ATOM   3074  CE  LYS A 443      34.248   2.862 -21.562  1.00 63.96           C  
ANISOU 3074  CE  LYS A 443     8551   8431   7319    420   -199   -189       C  
ATOM   3075  NZ  LYS A 443      34.500   4.208 -20.943  1.00 64.07           N  
ANISOU 3075  NZ  LYS A 443     8565   8432   7346    429   -165   -126       N  
ATOM   3076  N   VAL A 444      34.878  -2.392 -17.097  1.00 19.25           N  
ANISOU 3076  N   VAL A 444     2793   2602   1921    235   -233   -379       N  
ATOM   3077  CA  VAL A 444      35.866  -3.230 -16.435  1.00 18.82           C  
ANISOU 3077  CA  VAL A 444     2740   2508   1903    220   -202   -393       C  
ATOM   3078  C   VAL A 444      35.270  -4.450 -15.706  1.00 21.84           C  
ANISOU 3078  C   VAL A 444     3098   2854   2346    178   -237   -433       C  
ATOM   3079  O   VAL A 444      35.944  -5.455 -15.511  1.00 22.01           O  
ANISOU 3079  O   VAL A 444     3127   2841   2394    169   -222   -455       O  
ATOM   3080  CB  VAL A 444      36.746  -2.392 -15.482  1.00 19.14           C  
ANISOU 3080  CB  VAL A 444     2778   2538   1958    222   -155   -350       C  
ATOM   3081  CG1 VAL A 444      36.024  -2.127 -14.172  1.00 21.39           C  
ANISOU 3081  CG1 VAL A 444     3022   2805   2300    186   -172   -333       C  
ATOM   3082  CG2 VAL A 444      38.068  -3.102 -15.228  1.00 23.01           C  
ANISOU 3082  CG2 VAL A 444     3278   2999   2466    224   -113   -357       C  
ATOM   3083  N   ASP A 445      34.001  -4.366 -15.328  1.00 13.65           N  
ANISOU 3083  N   ASP A 445     2031   1823   1333    154   -281   -439       N  
ATOM   3084  CA  ASP A 445      33.351  -5.441 -14.601  1.00 15.36           C  
ANISOU 3084  CA  ASP A 445     2219   2004   1612    110   -311   -468       C  
ATOM   3085  C   ASP A 445      31.931  -5.680 -15.150  1.00 22.44           C  
ANISOU 3085  C   ASP A 445     3094   2922   2512     94   -366   -493       C  
ATOM   3086  O   ASP A 445      30.928  -5.440 -14.464  1.00 19.97           O  
ANISOU 3086  O   ASP A 445     2740   2614   2233     69   -393   -485       O  
ATOM   3087  CB  ASP A 445      33.327  -5.114 -13.105  1.00 10.62           C  
ANISOU 3087  CB  ASP A 445     1590   1384   1061     85   -299   -442       C  
ATOM   3088  CG  ASP A 445      32.739  -6.227 -12.273  1.00 18.91           C  
ANISOU 3088  CG  ASP A 445     2609   2394   2181     37   -321   -462       C  
ATOM   3089  OD1 ASP A 445      32.645  -7.360 -12.799  1.00 18.33           O  
ANISOU 3089  OD1 ASP A 445     2545   2297   2121     24   -338   -498       O  
ATOM   3090  OD2 ASP A 445      32.375  -5.976 -11.095  1.00 16.63           O  
ANISOU 3090  OD2 ASP A 445     2283   2098   1939      9   -308   -425       O  
ATOM   3091  N   PRO A 446      31.847  -6.160 -16.399  1.00 24.01           N  
ANISOU 3091  N   PRO A 446     3316   3133   2673    110   -384   -524       N  
ATOM   3092  CA  PRO A 446      30.543  -6.316 -17.055  1.00 23.70           C  
ANISOU 3092  CA  PRO A 446     3258   3119   2628    100   -439   -549       C  
ATOM   3093  C   PRO A 446      29.631  -7.312 -16.338  1.00 25.75           C  
ANISOU 3093  C   PRO A 446     3477   3345   2960     46   -473   -575       C  
ATOM   3094  O   PRO A 446      28.416  -7.175 -16.406  1.00 23.90           O  
ANISOU 3094  O   PRO A 446     3208   3133   2741     30   -514   -580       O  
ATOM   3095  CB  PRO A 446      30.909  -6.823 -18.464  1.00 21.15           C  
ANISOU 3095  CB  PRO A 446     2976   2808   2251    128   -445   -583       C  
ATOM   3096  CG  PRO A 446      32.275  -7.438 -18.316  1.00 26.18           C  
ANISOU 3096  CG  PRO A 446     3644   3410   2893    135   -398   -589       C  
ATOM   3097  CD  PRO A 446      32.964  -6.605 -17.258  1.00 27.53           C  
ANISOU 3097  CD  PRO A 446     3806   3574   3080    139   -354   -540       C  
ATOM   3098  N   LEU A 447      30.202  -8.289 -15.647  1.00 26.66           N  
ANISOU 3098  N   LEU A 447     3596   3408   3125     19   -453   -586       N  
ATOM   3099  CA  LEU A 447      29.385  -9.293 -14.975  1.00 24.76           C  
ANISOU 3099  CA  LEU A 447     3321   3130   2958    -34   -479   -604       C  
ATOM   3100  C   LEU A 447      29.090  -8.928 -13.532  1.00 29.16           C  
ANISOU 3100  C   LEU A 447     3835   3675   3569    -63   -466   -567       C  
ATOM   3101  O   LEU A 447      28.430  -9.691 -12.822  1.00 31.67           O  
ANISOU 3101  O   LEU A 447     4118   3962   3952   -111   -480   -571       O  
ATOM   3102  CB  LEU A 447      30.074 -10.653 -15.025  1.00 28.25           C  
ANISOU 3102  CB  LEU A 447     3790   3516   3428    -48   -467   -636       C  
ATOM   3103  CG  LEU A 447      30.328 -11.217 -16.426  1.00 36.79           C  
ANISOU 3103  CG  LEU A 447     4912   4604   4463    -23   -481   -682       C  
ATOM   3104  CD1 LEU A 447      31.100 -12.520 -16.327  1.00 36.37           C  
ANISOU 3104  CD1 LEU A 447     4885   4491   4443    -33   -463   -709       C  
ATOM   3105  CD2 LEU A 447      29.005 -11.416 -17.170  1.00 30.73           C  
ANISOU 3105  CD2 LEU A 447     4124   3861   3691    -41   -539   -714       C  
ATOM   3106  N   ARG A 448      29.584  -7.770 -13.101  1.00 22.17           N  
ANISOU 3106  N   ARG A 448     2954   2815   2657    -36   -438   -530       N  
ATOM   3107  CA  ARG A 448      29.423  -7.342 -11.711  1.00 26.07           C  
ANISOU 3107  CA  ARG A 448     3411   3301   3195    -58   -423   -496       C  
ATOM   3108  C   ARG A 448      30.002  -8.403 -10.773  1.00 25.55           C  
ANISOU 3108  C   ARG A 448     3346   3174   3188    -91   -401   -496       C  
ATOM   3109  O   ARG A 448      29.355  -8.847  -9.824  1.00 22.18           O  
ANISOU 3109  O   ARG A 448     2878   2725   2823   -134   -407   -485       O  
ATOM   3110  CB  ARG A 448      27.948  -7.066 -11.390  1.00 29.03           C  
ANISOU 3110  CB  ARG A 448     3728   3702   3601    -85   -458   -491       C  
ATOM   3111  CG  ARG A 448      27.268  -6.080 -12.347  1.00 35.54           C  
ANISOU 3111  CG  ARG A 448     4548   4584   4370    -50   -486   -490       C  
ATOM   3112  CD  ARG A 448      25.759  -6.131 -12.199  1.00 44.47           C  
ANISOU 3112  CD  ARG A 448     5619   5737   5541    -78   -526   -493       C  
ATOM   3113  NE  ARG A 448      25.118  -4.861 -12.531  1.00 57.21           N  
ANISOU 3113  NE  ARG A 448     7214   7406   7116    -42   -542   -473       N  
ATOM   3114  CZ  ARG A 448      23.881  -4.529 -12.155  1.00 57.88           C  
ANISOU 3114  CZ  ARG A 448     7239   7520   7235    -56   -566   -462       C  
ATOM   3115  NH1 ARG A 448      23.152  -5.381 -11.434  1.00 55.73           N  
ANISOU 3115  NH1 ARG A 448     6916   7226   7032   -110   -574   -469       N  
ATOM   3116  NH2 ARG A 448      23.372  -3.347 -12.496  1.00 46.27           N  
ANISOU 3116  NH2 ARG A 448     5756   6097   5728    -15   -578   -442       N  
ATOM   3117  N   VAL A 449      31.221  -8.832 -11.075  1.00 20.36           N  
ANISOU 3117  N   VAL A 449     2733   2491   2512    -69   -373   -505       N  
ATOM   3118  CA  VAL A 449      31.971  -9.695 -10.177  1.00 19.15           C  
ANISOU 3118  CA  VAL A 449     2587   2281   2409    -88   -348   -497       C  
ATOM   3119  C   VAL A 449      32.240  -8.957  -8.851  1.00 25.66           C  
ANISOU 3119  C   VAL A 449     3385   3113   3251    -94   -304   -431       C  
ATOM   3120  O   VAL A 449      32.283  -9.567  -7.778  1.00 19.44           O  
ANISOU 3120  O   VAL A 449     2580   2291   2516   -124   -287   -405       O  
ATOM   3121  CB  VAL A 449      33.298 -10.138 -10.828  1.00 24.06           C  
ANISOU 3121  CB  VAL A 449     3258   2884   3000    -52   -320   -513       C  
ATOM   3122  CG1 VAL A 449      34.268 -10.683  -9.803  1.00 25.20           C  
ANISOU 3122  CG1 VAL A 449     3407   2980   3187    -58   -285   -489       C  
ATOM   3123  CG2 VAL A 449      33.037 -11.166 -11.921  1.00 24.55           C  
ANISOU 3123  CG2 VAL A 449     3339   2932   3057    -54   -343   -558       C  
ATOM   3124  N   PHE A 450      32.405  -7.639  -8.926  1.00 17.45           N  
ANISOU 3124  N   PHE A 450     2345   2120   2166    -65   -286   -403       N  
ATOM   3125  CA  PHE A 450      32.603  -6.859  -7.716  1.00 12.42           C  
ANISOU 3125  CA  PHE A 450     1684   1492   1541    -69   -250   -349       C  
ATOM   3126  C   PHE A 450      31.338  -6.180  -7.220  1.00 17.45           C  
ANISOU 3126  C   PHE A 450     2278   2162   2192    -86   -264   -330       C  
ATOM   3127  O   PHE A 450      30.639  -5.520  -7.977  1.00 23.71           O  
ANISOU 3127  O   PHE A 450     3065   2990   2955    -70   -290   -343       O  
ATOM   3128  CB  PHE A 450      33.786  -5.916  -7.885  1.00 10.71           C  
ANISOU 3128  CB  PHE A 450     1494   1292   1282    -31   -214   -326       C  
ATOM   3129  CG  PHE A 450      35.036  -6.650  -8.243  1.00 16.00           C  
ANISOU 3129  CG  PHE A 450     2199   1933   1948    -15   -195   -342       C  
ATOM   3130  CD1 PHE A 450      35.737  -7.346  -7.273  1.00 10.28           C  
ANISOU 3130  CD1 PHE A 450     1471   1173   1263    -29   -172   -323       C  
ATOM   3131  CD2 PHE A 450      35.466  -6.717  -9.562  1.00 14.32           C  
ANISOU 3131  CD2 PHE A 450     2022   1730   1690     16   -201   -375       C  
ATOM   3132  CE1 PHE A 450      36.868  -8.052  -7.602  1.00 20.32           C  
ANISOU 3132  CE1 PHE A 450     2770   2417   2535     -9   -156   -337       C  
ATOM   3133  CE2 PHE A 450      36.598  -7.425  -9.901  1.00 11.50           C  
ANISOU 3133  CE2 PHE A 450     1693   1347   1329     35   -181   -392       C  
ATOM   3134  CZ  PHE A 450      37.302  -8.093  -8.927  1.00 18.73           C  
ANISOU 3134  CZ  PHE A 450     2602   2226   2290     23   -158   -373       C  
ATOM   3135  N   ALA A 451      31.035  -6.393  -5.944  1.00 20.37           N  
ANISOU 3135  N   ALA A 451     2616   2519   2605   -115   -246   -298       N  
ATOM   3136  CA  ALA A 451      29.793  -5.897  -5.356  1.00 18.77           C  
ANISOU 3136  CA  ALA A 451     2365   2345   2420   -131   -253   -280       C  
ATOM   3137  C   ALA A 451      29.912  -5.789  -3.843  1.00 15.80           C  
ANISOU 3137  C   ALA A 451     1969   1965   2070   -146   -214   -235       C  
ATOM   3138  O   ALA A 451      30.653  -6.539  -3.215  1.00 18.70           O  
ANISOU 3138  O   ALA A 451     2350   2298   2458   -158   -194   -221       O  
ATOM   3139  CB  ALA A 451      28.648  -6.805  -5.719  1.00 18.66           C  
ANISOU 3139  CB  ALA A 451     2321   2323   2445   -167   -293   -309       C  
ATOM   3140  N   SER A 452      29.177  -4.851  -3.265  1.00 14.66           N  
ANISOU 3140  N   SER A 452     1793   1857   1922   -141   -205   -212       N  
ATOM   3141  CA  SER A 452      29.207  -4.621  -1.828  1.00 13.38           C  
ANISOU 3141  CA  SER A 452     1612   1699   1772   -149   -168   -172       C  
ATOM   3142  C   SER A 452      27.818  -4.189  -1.406  1.00 16.57           C  
ANISOU 3142  C   SER A 452     1965   2139   2192   -158   -171   -162       C  
ATOM   3143  O   SER A 452      26.993  -3.851  -2.252  1.00 18.12           O  
ANISOU 3143  O   SER A 452     2142   2358   2384   -151   -202   -183       O  
ATOM   3144  CB  SER A 452      30.195  -3.512  -1.495  1.00 11.55           C  
ANISOU 3144  CB  SER A 452     1407   1479   1501   -115   -142   -157       C  
ATOM   3145  OG  SER A 452      29.792  -2.288  -2.101  1.00 15.14           O  
ANISOU 3145  OG  SER A 452     1860   1965   1927    -85   -151   -164       O  
ATOM   3146  N   ASP A 453      27.555  -4.200  -0.106  1.00 15.09           N  
ANISOU 3146  N   ASP A 453     1753   1960   2022   -171   -139   -128       N  
ATOM   3147  CA  ASP A 453      26.284  -3.695   0.398  1.00 17.42           C  
ANISOU 3147  CA  ASP A 453     1996   2294   2329   -173   -132   -114       C  
ATOM   3148  C   ASP A 453      26.064  -2.257  -0.059  1.00 15.41           C  
ANISOU 3148  C   ASP A 453     1743   2074   2038   -130   -139   -125       C  
ATOM   3149  O   ASP A 453      24.965  -1.884  -0.474  1.00 17.22           O  
ANISOU 3149  O   ASP A 453     1935   2333   2276   -124   -159   -134       O  
ATOM   3150  CB  ASP A 453      26.239  -3.770   1.926  1.00 12.69           C  
ANISOU 3150  CB  ASP A 453     1382   1704   1738   -182    -88    -74       C  
ATOM   3151  CG  ASP A 453      26.040  -5.172   2.430  1.00 16.72           C  
ANISOU 3151  CG  ASP A 453     1875   2185   2293   -228    -79    -54       C  
ATOM   3152  OD1 ASP A 453      26.019  -6.113   1.604  1.00 15.76           O  
ANISOU 3152  OD1 ASP A 453     1758   2029   2201   -254   -109    -76       O  
ATOM   3153  OD2 ASP A 453      25.919  -5.328   3.661  1.00 21.83           O  
ANISOU 3153  OD2 ASP A 453     2508   2842   2944   -236    -42    -16       O  
ATOM   3154  N   MET A 454      27.128  -1.463   0.034  1.00  9.46           N  
ANISOU 3154  N   MET A 454     1032   1314   1247   -100   -123   -122       N  
ATOM   3155  CA  MET A 454      27.123  -0.072  -0.394  1.00 14.37           C  
ANISOU 3155  CA  MET A 454     1667   1957   1837    -58   -126   -128       C  
ATOM   3156  C   MET A 454      26.707   0.059  -1.873  1.00 17.05           C  
ANISOU 3156  C   MET A 454     2009   2303   2167    -45   -167   -153       C  
ATOM   3157  O   MET A 454      25.816   0.851  -2.195  1.00 16.51           O  
ANISOU 3157  O   MET A 454     1916   2265   2093    -22   -181   -155       O  
ATOM   3158  CB  MET A 454      28.509   0.545  -0.139  1.00 11.22           C  
ANISOU 3158  CB  MET A 454     1315   1538   1410    -39   -105   -122       C  
ATOM   3159  CG  MET A 454      28.617   2.070  -0.333  1.00 18.05           C  
ANISOU 3159  CG  MET A 454     2195   2414   2248      1    -99   -122       C  
ATOM   3160  SD  MET A 454      28.786   2.582  -2.056  1.00 43.15           S  
ANISOU 3160  SD  MET A 454     5403   5591   5403     27   -129   -137       S  
ATOM   3161  CE  MET A 454      30.513   2.276  -2.356  1.00 24.13           C  
ANISOU 3161  CE  MET A 454     3043   3148   2979     22   -116   -138       C  
ATOM   3162  N   ALA A 455      27.343  -0.712  -2.760  1.00 11.68           N  
ANISOU 3162  N   ALA A 455     1358   1599   1482    -56   -188   -172       N  
ATOM   3163  CA  ALA A 455      27.035  -0.635  -4.185  1.00 13.85           C  
ANISOU 3163  CA  ALA A 455     1642   1884   1736    -40   -228   -198       C  
ATOM   3164  C   ALA A 455      25.539  -0.869  -4.466  1.00 19.55           C  
ANISOU 3164  C   ALA A 455     2310   2635   2482    -52   -263   -211       C  
ATOM   3165  O   ALA A 455      24.952  -0.193  -5.315  1.00 22.19           O  
ANISOU 3165  O   ALA A 455     2639   2998   2796    -23   -292   -220       O  
ATOM   3166  CB  ALA A 455      27.892  -1.613  -4.986  1.00  9.44           C  
ANISOU 3166  CB  ALA A 455     1122   1296   1169    -51   -241   -222       C  
ATOM   3167  N   ARG A 456      24.932  -1.810  -3.739  1.00 15.88           N  
ANISOU 3167  N   ARG A 456     1805   2164   2065    -94   -259   -207       N  
ATOM   3168  CA  ARG A 456      23.512  -2.126  -3.914  1.00 21.91           C  
ANISOU 3168  CA  ARG A 456     2507   2954   2863   -113   -290   -218       C  
ATOM   3169  C   ARG A 456      22.625  -1.021  -3.356  1.00 19.25           C  
ANISOU 3169  C   ARG A 456     2128   2660   2526    -86   -276   -196       C  
ATOM   3170  O   ARG A 456      21.662  -0.607  -4.001  1.00 22.67           O  
ANISOU 3170  O   ARG A 456     2526   3127   2961    -69   -310   -208       O  
ATOM   3171  CB  ARG A 456      23.149  -3.507  -3.329  1.00 16.45           C  
ANISOU 3171  CB  ARG A 456     1783   2237   2229   -171   -288   -217       C  
ATOM   3172  CG  ARG A 456      23.658  -4.682  -4.205  1.00 29.34           C  
ANISOU 3172  CG  ARG A 456     3449   3829   3871   -197   -321   -253       C  
ATOM   3173  CD  ARG A 456      23.298  -6.084  -3.655  1.00 22.98           C  
ANISOU 3173  CD  ARG A 456     2615   2987   3131   -257   -319   -250       C  
ATOM   3174  NE  ARG A 456      24.026  -6.338  -2.426  1.00 31.81           N  
ANISOU 3174  NE  ARG A 456     3749   4080   4259   -266   -265   -210       N  
ATOM   3175  CZ  ARG A 456      25.160  -7.028  -2.342  1.00 28.23           C  
ANISOU 3175  CZ  ARG A 456     3345   3580   3802   -271   -252   -210       C  
ATOM   3176  NH1 ARG A 456      25.689  -7.593  -3.415  1.00 21.16           N  
ANISOU 3176  NH1 ARG A 456     2487   2655   2898   -269   -285   -251       N  
ATOM   3177  NH2 ARG A 456      25.753  -7.164  -1.166  1.00 28.34           N  
ANISOU 3177  NH2 ARG A 456     3368   3579   3820   -275   -206   -169       N  
ATOM   3178  N   ARG A 457      22.975  -0.510  -2.183  1.00 16.13           N  
ANISOU 3178  N   ARG A 457     1737   2263   2127    -77   -226   -166       N  
ATOM   3179  CA  ARG A 457      22.189   0.545  -1.547  1.00 21.37           C  
ANISOU 3179  CA  ARG A 457     2365   2965   2791    -47   -206   -149       C  
ATOM   3180  C   ARG A 457      22.204   1.831  -2.384  1.00 25.80           C  
ANISOU 3180  C   ARG A 457     2948   3540   3313      8   -225   -156       C  
ATOM   3181  O   ARG A 457      21.170   2.463  -2.596  1.00 23.42           O  
ANISOU 3181  O   ARG A 457     2605   3274   3018     34   -240   -155       O  
ATOM   3182  CB  ARG A 457      22.697   0.800  -0.119  1.00 16.77           C  
ANISOU 3182  CB  ARG A 457     1793   2376   2204    -45   -150   -122       C  
ATOM   3183  CG  ARG A 457      21.964   1.880   0.652  1.00 12.66           C  
ANISOU 3183  CG  ARG A 457     1240   1890   1678    -10   -123   -108       C  
ATOM   3184  CD  ARG A 457      22.498   2.032   2.110  1.00 16.42           C  
ANISOU 3184  CD  ARG A 457     1732   2364   2143    -10    -70    -87       C  
ATOM   3185  NE  ARG A 457      23.954   2.196   2.185  1.00 20.09           N  
ANISOU 3185  NE  ARG A 457     2262   2793   2578     -5    -62    -90       N  
ATOM   3186  CZ  ARG A 457      24.590   3.367   2.116  1.00 22.41           C  
ANISOU 3186  CZ  ARG A 457     2595   3078   2841     33    -57    -96       C  
ATOM   3187  NH1 ARG A 457      23.902   4.487   1.963  1.00 18.30           N  
ANISOU 3187  NH1 ARG A 457     2060   2578   2315     73    -58   -101       N  
ATOM   3188  NH2 ARG A 457      25.919   3.422   2.191  1.00 15.78           N  
ANISOU 3188  NH2 ARG A 457     1806   2207   1981     30    -50    -98       N  
ATOM   3189  N   LEU A 458      23.378   2.192  -2.886  1.00 21.46           N  
ANISOU 3189  N   LEU A 458     2462   2965   2727     26   -223   -159       N  
ATOM   3190  CA  LEU A 458      23.535   3.441  -3.614  1.00 16.61           C  
ANISOU 3190  CA  LEU A 458     1877   2357   2077     77   -232   -157       C  
ATOM   3191  C   LEU A 458      23.465   3.250  -5.121  1.00 16.52           C  
ANISOU 3191  C   LEU A 458     1883   2353   2042     88   -281   -176       C  
ATOM   3192  O   LEU A 458      23.697   4.192  -5.871  1.00 22.64           O  
ANISOU 3192  O   LEU A 458     2689   3131   2783    130   -289   -169       O  
ATOM   3193  CB  LEU A 458      24.860   4.100  -3.233  1.00 16.43           C  
ANISOU 3193  CB  LEU A 458     1910   2302   2030     91   -197   -144       C  
ATOM   3194  CG  LEU A 458      24.964   4.406  -1.738  1.00 15.94           C  
ANISOU 3194  CG  LEU A 458     1838   2238   1982     86   -153   -130       C  
ATOM   3195  CD1 LEU A 458      26.265   5.121  -1.417  1.00  9.77           C  
ANISOU 3195  CD1 LEU A 458     1108   1425   1179     99   -126   -124       C  
ATOM   3196  CD2 LEU A 458      23.750   5.233  -1.300  1.00 10.86           C  
ANISOU 3196  CD2 LEU A 458     1150   1627   1350    117   -148   -124       C  
ATOM   3197  N   GLU A 459      23.168   2.029  -5.557  1.00 16.38           N  
ANISOU 3197  N   GLU A 459     1847   2336   2042     51   -312   -199       N  
ATOM   3198  CA  GLU A 459      22.948   1.746  -6.972  1.00 20.94           C  
ANISOU 3198  CA  GLU A 459     2436   2927   2595     61   -365   -226       C  
ATOM   3199  C   GLU A 459      24.148   2.131  -7.815  1.00 23.60           C  
ANISOU 3199  C   GLU A 459     2844   3245   2879     88   -359   -225       C  
ATOM   3200  O   GLU A 459      24.016   2.804  -8.839  1.00 29.07           O  
ANISOU 3200  O   GLU A 459     3556   3958   3531    129   -385   -225       O  
ATOM   3201  CB  GLU A 459      21.698   2.459  -7.478  1.00 16.42           C  
ANISOU 3201  CB  GLU A 459     1820   2399   2019     94   -402   -225       C  
ATOM   3202  CG  GLU A 459      20.412   1.781  -7.040  1.00 21.37           C  
ANISOU 3202  CG  GLU A 459     2368   3051   2700     60   -423   -236       C  
ATOM   3203  CD  GLU A 459      19.179   2.599  -7.361  1.00 28.36           C  
ANISOU 3203  CD  GLU A 459     3201   3985   3588     99   -454   -231       C  
ATOM   3204  OE1 GLU A 459      19.217   3.395  -8.333  1.00 31.12           O  
ANISOU 3204  OE1 GLU A 459     3581   4352   3893    148   -482   -230       O  
ATOM   3205  OE2 GLU A 459      18.182   2.457  -6.623  1.00 32.24           O  
ANISOU 3205  OE2 GLU A 459     3622   4499   4127     82   -448   -225       O  
ATOM   3206  N   LEU A 460      25.318   1.720  -7.345  1.00 13.69           N  
ANISOU 3206  N   LEU A 460     1624   1953   1625     68   -323   -221       N  
ATOM   3207  CA  LEU A 460      26.561   1.856  -8.080  1.00 25.77           C  
ANISOU 3207  CA  LEU A 460     3216   3463   3113     86   -311   -221       C  
ATOM   3208  C   LEU A 460      26.888   0.522  -8.730  1.00 31.48           C  
ANISOU 3208  C   LEU A 460     3955   4172   3834     60   -335   -256       C  
ATOM   3209  O   LEU A 460      27.747   0.448  -9.610  1.00 27.97           O  
ANISOU 3209  O   LEU A 460     3558   3720   3350     77   -334   -266       O  
ATOM   3210  CB  LEU A 460      27.703   2.238  -7.127  1.00 16.14           C  
ANISOU 3210  CB  LEU A 460     2020   2212   1899     82   -258   -196       C  
ATOM   3211  CG  LEU A 460      27.541   3.561  -6.392  1.00 20.73           C  
ANISOU 3211  CG  LEU A 460     2594   2798   2484    106   -232   -167       C  
ATOM   3212  CD1 LEU A 460      28.787   3.846  -5.544  1.00 16.73           C  
ANISOU 3212  CD1 LEU A 460     2115   2261   1983     98   -187   -151       C  
ATOM   3213  CD2 LEU A 460      27.287   4.670  -7.416  1.00  9.34           C  
ANISOU 3213  CD2 LEU A 460     1171   1373   1006    154   -248   -156       C  
ATOM   3214  N   LEU A 461      26.216  -0.531  -8.263  1.00 36.31           N  
ANISOU 3214  N   LEU A 461     4527   4777   4492     18   -352   -275       N  
ATOM   3215  CA  LEU A 461      26.476  -1.904  -8.713  1.00 37.24           C  
ANISOU 3215  CA  LEU A 461     4657   4870   4621    -13   -374   -312       C  
ATOM   3216  C   LEU A 461      26.312  -2.014 -10.217  1.00 33.59           C  
ANISOU 3216  C   LEU A 461     4221   4429   4113     11   -421   -348       C  
ATOM   3217  O   LEU A 461      27.028  -2.778 -10.851  1.00 31.14           O  
ANISOU 3217  O   LEU A 461     3949   4097   3784      8   -427   -377       O  
ATOM   3218  CB  LEU A 461      25.534  -2.891  -8.012  1.00 32.53           C  
ANISOU 3218  CB  LEU A 461     4007   4264   4089    -63   -388   -322       C  
ATOM   3219  CG  LEU A 461      25.552  -4.337  -8.498  1.00 37.36           C  
ANISOU 3219  CG  LEU A 461     4625   4845   4725   -100   -420   -364       C  
ATOM   3220  CD1 LEU A 461      26.753  -5.032  -7.943  1.00 28.79           C  
ANISOU 3220  CD1 LEU A 461     3576   3710   3652   -114   -380   -356       C  
ATOM   3221  CD2 LEU A 461      24.265  -5.115  -8.164  1.00 42.42           C  
ANISOU 3221  CD2 LEU A 461     5202   5486   5428   -147   -451   -378       C  
ATOM   3222  OXT LEU A 461      25.481  -1.328 -10.824  1.00 37.25           O  
ANISOU 3222  OXT LEU A 461     4668   4933   4553     38   -455   -349       O  
TER    3223      LEU A 461                                                      
HETATM 3224  PA  FAD A 900      37.992  -0.850   4.941  1.00 10.46           P  
ANISOU 3224  PA  FAD A 900     1360   1341   1273    -44    -17    -51       P  
HETATM 3225  O1A FAD A 900      37.181  -0.053   5.918  1.00 13.94           O  
ANISOU 3225  O1A FAD A 900     1792   1810   1695    -40    -10    -50       O  
HETATM 3226  O2A FAD A 900      38.287  -2.299   5.183  1.00 14.17           O  
ANISOU 3226  O2A FAD A 900     1830   1793   1759    -53    -18    -32       O  
HETATM 3227  O5B FAD A 900      37.333  -0.726   3.477  1.00 12.03           O  
ANISOU 3227  O5B FAD A 900     1562   1530   1480    -44    -22    -68       O  
HETATM 3228  C5B FAD A 900      37.028   0.577   2.960  1.00 14.06           C  
ANISOU 3228  C5B FAD A 900     1822   1795   1724    -32    -22    -83       C  
HETATM 3229  C4B FAD A 900      36.864   0.553   1.439  1.00 16.49           C  
ANISOU 3229  C4B FAD A 900     2140   2092   2034    -26    -29    -96       C  
HETATM 3230  O4B FAD A 900      38.130   0.253   0.807  1.00 14.27           O  
ANISOU 3230  O4B FAD A 900     1874   1794   1756    -22    -25    -98       O  
HETATM 3231  C3B FAD A 900      35.893  -0.525   0.979  1.00 17.27           C  
ANISOU 3231  C3B FAD A 900     2229   2188   2145    -39    -41    -99       C  
HETATM 3232  O3B FAD A 900      35.137  -0.061  -0.150  1.00 11.38           O  
ANISOU 3232  O3B FAD A 900     1484   1449   1389    -29    -54   -114       O  
HETATM 3233  C2B FAD A 900      36.824  -1.647   0.552  1.00 15.69           C  
ANISOU 3233  C2B FAD A 900     2043   1963   1956    -43    -43   -102       C  
HETATM 3234  O2B FAD A 900      36.191  -2.483  -0.403  1.00 13.39           O  
ANISOU 3234  O2B FAD A 900     1754   1661   1674    -50    -59   -119       O  
HETATM 3235  C1B FAD A 900      37.978  -0.871  -0.052  1.00 11.44           C  
ANISOU 3235  C1B FAD A 900     1521   1421   1404    -25    -34   -107       C  
HETATM 3236  N9A FAD A 900      39.243  -1.630  -0.078  1.00 13.84           N  
ANISOU 3236  N9A FAD A 900     1833   1707   1718    -23    -27   -105       N  
HETATM 3237  C8A FAD A 900      39.983  -1.963   0.990  1.00 11.12           C  
ANISOU 3237  C8A FAD A 900     1481   1359   1384    -26    -22    -89       C  
HETATM 3238  N7A FAD A 900      41.058  -2.664   0.579  1.00 12.24           N  
ANISOU 3238  N7A FAD A 900     1630   1485   1537    -17    -17    -91       N  
HETATM 3239  C5A FAD A 900      40.985  -2.759  -0.768  1.00 17.62           C  
ANISOU 3239  C5A FAD A 900     2326   2159   2211     -8    -16   -110       C  
HETATM 3240  C6A FAD A 900      41.794  -3.344  -1.734  1.00 11.66           C  
ANISOU 3240  C6A FAD A 900     1583   1390   1456      8     -8   -122       C  
HETATM 3241  N6A FAD A 900      42.914  -3.984  -1.358  1.00 13.86           N  
ANISOU 3241  N6A FAD A 900     1857   1656   1752     17      0   -114       N  
HETATM 3242  N1A FAD A 900      41.447  -3.275  -3.038  1.00 14.31           N  
ANISOU 3242  N1A FAD A 900     1937   1728   1773     19     -9   -143       N  
HETATM 3243  C2A FAD A 900      40.326  -2.637  -3.406  1.00 11.84           C  
ANISOU 3243  C2A FAD A 900     1626   1430   1443     14    -21   -148       C  
HETATM 3244  N3A FAD A 900      39.531  -2.054  -2.497  1.00 14.16           N  
ANISOU 3244  N3A FAD A 900     1904   1736   1741     -1    -29   -136       N  
HETATM 3245  C4A FAD A 900      39.836  -2.104  -1.176  1.00 14.87           C  
ANISOU 3245  C4A FAD A 900     1978   1824   1847    -12    -24   -117       C  
HETATM 3246  N1  FAD A 900      39.133   9.054   6.424  1.00 12.49           N  
ANISOU 3246  N1  FAD A 900     1670   1570   1505     17    -17   -181       N  
HETATM 3247  C2  FAD A 900      39.669  10.168   5.880  1.00 12.60           C  
ANISOU 3247  C2  FAD A 900     1696   1549   1544     14    -16   -189       C  
HETATM 3248  O2  FAD A 900      39.563  10.369   4.543  1.00 13.27           O  
ANISOU 3248  O2  FAD A 900     1786   1612   1643     17     -5   -169       O  
HETATM 3249  N3  FAD A 900      40.295  11.092   6.632  1.00 16.13           N  
ANISOU 3249  N3  FAD A 900     2150   1979   2002      8    -26   -217       N  
HETATM 3250  C4  FAD A 900      40.400  10.896   7.953  1.00 16.34           C  
ANISOU 3250  C4  FAD A 900     2173   2031   2005      9    -40   -238       C  
HETATM 3251  O4  FAD A 900      41.045  11.799   8.705  1.00 19.10           O  
ANISOU 3251  O4  FAD A 900     2530   2365   2363      3    -56   -272       O  
HETATM 3252  C4X FAD A 900      39.830   9.684   8.572  1.00 15.99           C  
ANISOU 3252  C4X FAD A 900     2119   2032   1927     17    -38   -224       C  
HETATM 3253  N5  FAD A 900      39.925   9.471   9.900  1.00 19.14           N  
ANISOU 3253  N5  FAD A 900     2517   2461   2295     21    -49   -240       N  
HETATM 3254  C5X FAD A 900      39.403   8.359  10.472  1.00 15.96           C  
ANISOU 3254  C5X FAD A 900     2106   2096   1861     27    -43   -219       C  
HETATM 3255  C6  FAD A 900      39.521   8.144  11.846  1.00 18.39           C  
ANISOU 3255  C6  FAD A 900     2417   2439   2130     36    -53   -231       C  
HETATM 3256  C7  FAD A 900      38.979   7.010  12.449  1.00 18.58           C  
ANISOU 3256  C7  FAD A 900     2434   2501   2124     42    -42   -201       C  
HETATM 3257  C7M FAD A 900      39.115   6.807  13.939  1.00 13.23           C  
ANISOU 3257  C7M FAD A 900     1763   1866   1397     55    -50   -208       C  
HETATM 3258  C8  FAD A 900      38.277   5.999  11.613  1.00 19.81           C  
ANISOU 3258  C8  FAD A 900     2576   2654   2297     34    -23   -163       C  
HETATM 3259  C8M FAD A 900      37.696   4.760  12.256  1.00  9.95           C  
ANISOU 3259  C8M FAD A 900     1317   1437   1025     35     -9   -128       C  
HETATM 3260  C9  FAD A 900      38.165   6.210  10.232  1.00 22.38           C  
ANISOU 3260  C9  FAD A 900     2898   2946   2660     26    -19   -160       C  
HETATM 3261  C9A FAD A 900      38.705   7.353   9.630  1.00 10.69           C  
ANISOU 3261  C9A FAD A 900     1427   1433   1201     25    -27   -184       C  
HETATM 3262  N10 FAD A 900      38.611   7.603   8.244  1.00 13.60           N  
ANISOU 3262  N10 FAD A 900     1796   1772   1601     20    -21   -176       N  
HETATM 3263  C10 FAD A 900      39.188   8.789   7.739  1.00 15.58           C  
ANISOU 3263  C10 FAD A 900     2057   1987   1873     18    -25   -194       C  
HETATM 3264  C1' FAD A 900      37.970   6.670   7.303  1.00 16.33           C  
ANISOU 3264  C1' FAD A 900     2132   2119   1953     17    -12   -150       C  
HETATM 3265  C2' FAD A 900      39.017   5.673   6.763  1.00 13.14           C  
ANISOU 3265  C2' FAD A 900     1725   1705   1564      0    -18   -133       C  
HETATM 3266  O2' FAD A 900      40.292   6.292   6.546  1.00 13.74           O  
ANISOU 3266  O2' FAD A 900     1804   1759   1656     -8    -25   -143       O  
HETATM 3267  C3' FAD A 900      38.613   5.059   5.430  1.00 11.96           C  
ANISOU 3267  C3' FAD A 900     1573   1544   1427     -2    -13   -118       C  
HETATM 3268  O3' FAD A 900      37.331   4.477   5.594  1.00 16.52           O  
ANISOU 3268  O3' FAD A 900     2141   2141   1996      1     -8   -110       O  
HETATM 3269  C4' FAD A 900      39.621   4.021   4.925  1.00 12.63           C  
ANISOU 3269  C4' FAD A 900     1655   1618   1524    -14    -15   -106       C  
HETATM 3270  O4' FAD A 900      39.193   3.537   3.633  1.00 14.33           O  
ANISOU 3270  O4' FAD A 900     1875   1824   1747    -13    -12   -100       O  
HETATM 3271  C5' FAD A 900      39.749   2.843   5.897  1.00 16.82           C  
ANISOU 3271  C5' FAD A 900     2178   2164   2048    -19    -20    -92       C  
HETATM 3272  O5' FAD A 900      40.710   1.889   5.410  1.00 17.22           O  
ANISOU 3272  O5' FAD A 900     2228   2201   2115    -24    -22    -82       O  
HETATM 3273  P   FAD A 900      40.549   0.306   5.641  1.00 12.63           P  
ANISOU 3273  P   FAD A 900     1643   1618   1538    -28    -23    -61       P  
HETATM 3274  O1P FAD A 900      41.803  -0.365   5.148  1.00 14.63           O  
ANISOU 3274  O1P FAD A 900     1896   1853   1809    -26    -26    -57       O  
HETATM 3275  O2P FAD A 900      40.146   0.093   7.072  1.00 12.98           O  
ANISOU 3275  O2P FAD A 900     1683   1685   1563    -28    -25    -47       O  
HETATM 3276  O3P FAD A 900      39.362  -0.047   4.609  1.00 13.24           O  
ANISOU 3276  O3P FAD A 900     1722   1685   1622    -33    -19    -64       O  
HETATM 3277  O38 0T5 A 901      36.204  15.472   9.439  1.00 57.03           O  
ANISOU 3277  O38 0T5 A 901     7393   7137   7141    140     -9   -349       O  
HETATM 3278  N8  0T5 A 901      37.332  15.052   8.758  1.00 61.73           N  
ANISOU 3278  N8  0T5 A 901     7983   7714   7759    103    -18   -327       N  
HETATM 3279  O10 0T5 A 901      37.360  15.066   7.369  1.00 69.45           O  
ANISOU 3279  O10 0T5 A 901     8958   8666   8763     97    -10   -290       O  
HETATM 3280  C2  0T5 A 901      38.440  14.598   9.468  1.00 61.51           C  
ANISOU 3280  C2  0T5 A 901     7949   7698   7723     76    -37   -340       C  
HETATM 3281  C1  0T5 A 901      39.702  15.139   9.227  1.00 63.13           C  
ANISOU 3281  C1  0T5 A 901     8159   7862   7965     46    -51   -350       C  
HETATM 3282  C6  0T5 A 901      40.805  14.676   9.939  1.00 64.72           C  
ANISOU 3282  C6  0T5 A 901     8348   8080   8160     21    -74   -364       C  
HETATM 3283  C7  0T5 A 901      42.162  15.279   9.659  1.00 69.90           C  
ANISOU 3283  C7  0T5 A 901     9001   8694   8865    -14    -90   -374       C  
HETATM 3284  F28 0T5 A 901      42.072  15.963   8.529  1.00 73.29           F  
ANISOU 3284  F28 0T5 A 901     9438   9075   9334    -18    -71   -353       F  
HETATM 3285  F27 0T5 A 901      42.526  16.099  10.636  1.00 72.52           F  
ANISOU 3285  F27 0T5 A 901     9344   9012   9200    -18   -114   -426       F  
HETATM 3286  F29 0T5 A 901      43.074  14.321   9.525  1.00 56.85           F  
ANISOU 3286  F29 0T5 A 901     7323   7063   7213    -37    -97   -352       F  
HETATM 3287  C5  0T5 A 901      40.626  13.670  10.895  1.00 58.20           C  
ANISOU 3287  C5  0T5 A 901     7515   7313   7288     29    -80   -365       C  
HETATM 3288  C3  0T5 A 901      38.260  13.595  10.408  1.00 54.66           C  
ANISOU 3288  C3  0T5 A 901     7071   6886   6812     79    -39   -340       C  
HETATM 3289  C4  0T5 A 901      39.354  13.129  11.125  1.00 55.96           C  
ANISOU 3289  C4  0T5 A 901     7230   7067   6967     57    -61   -350       C  
HETATM 3290  C14 0T5 A 901      39.127  12.035  12.131  1.00 51.53           C  
ANISOU 3290  C14 0T5 A 901     6659   6564   6355     65    -62   -342       C  
HETATM 3291  O15 0T5 A 901      40.008  11.729  12.914  1.00 47.82           O  
ANISOU 3291  O15 0T5 A 901     6188   6113   5868     54    -84   -354       O  
HETATM 3292  N13 0T5 A 901      37.950  11.410  12.125  1.00 51.78           N  
ANISOU 3292  N13 0T5 A 901     6682   6627   6363     84    -38   -317       N  
HETATM 3293  C12 0T5 A 901      37.598  10.413  13.127  1.00 47.18           C  
ANISOU 3293  C12 0T5 A 901     6093   6100   5734     92    -32   -302       C  
HETATM 3294  C13 0T5 A 901      36.316   9.665  12.737  1.00 42.20           C  
ANISOU 3294  C13 0T5 A 901     5444   5491   5098    102     -3   -266       C  
HETATM 3295  C20 0T5 A 901      37.454  11.052  14.458  1.00 46.91           C  
ANISOU 3295  C20 0T5 A 901     6075   6090   5656    116    -37   -344       C  
HETATM 3296  C25 0T5 A 901      36.569  12.115  14.633  1.00 42.46           C  
ANISOU 3296  C25 0T5 A 901     5525   5519   5089    145    -22   -376       C  
HETATM 3297  C24 0T5 A 901      36.450  12.703  15.888  1.00 48.45           C  
ANISOU 3297  C24 0T5 A 901     6303   6303   5803    171    -26   -421       C  
HETATM 3298  C23 0T5 A 901      37.207  12.238  16.965  1.00 47.28           C  
ANISOU 3298  C23 0T5 A 901     6162   6191   5610    167    -47   -431       C  
HETATM 3299  C22 0T5 A 901      38.091  11.172  16.789  1.00 46.41           C  
ANISOU 3299  C22 0T5 A 901     6038   6091   5506    138    -64   -394       C  
HETATM 3300  C21 0T5 A 901      38.215  10.581  15.532  1.00 45.93           C  
ANISOU 3300  C21 0T5 A 901     5957   6001   5494    113    -57   -351       C  
HETATM 3301  O   HOH A1001      28.781  -8.815   4.523  1.00 11.60           O  
HETATM 3302  O   HOH A1002      33.945   8.333  16.366  1.00 34.31           O  
HETATM 3303  O   HOH A1003      31.989  -1.005  -1.807  1.00  8.47           O  
HETATM 3304  O   HOH A1004      37.007  -5.613 -12.765  1.00 27.46           O  
HETATM 3305  O   HOH A1005      45.375  15.209   2.744  1.00 16.86           O  
HETATM 3306  O   HOH A1006      36.552   7.529  -8.552  1.00 14.51           O  
HETATM 3307  O   HOH A1007      38.393  11.339   1.053  1.00 15.07           O  
HETATM 3308  O   HOH A1008      29.905   3.018   2.240  1.00 23.15           O  
HETATM 3309  O   HOH A1009      43.556  -3.509   1.518  1.00 11.34           O  
HETATM 3310  O   HOH A1010      43.107 -12.724   1.616  1.00 23.17           O  
HETATM 3311  O   HOH A1011      25.321  19.895  17.679  1.00 22.22           O  
HETATM 3312  O   HOH A1012      44.637  14.535 -10.255  1.00 19.87           O  
HETATM 3313  O   HOH A1013      37.287  -5.058  -4.095  1.00 12.92           O  
HETATM 3314  O   HOH A1014      36.851   9.641  -1.881  1.00 13.38           O  
HETATM 3315  O   HOH A1015      37.146  11.654   7.464  1.00 28.42           O  
HETATM 3316  O   HOH A1016      57.114   7.549   7.304  1.00 32.12           O  
HETATM 3317  O   HOH A1017      25.651  18.353  -4.503  1.00 18.30           O  
HETATM 3318  O   HOH A1018      27.836  -1.455   7.935  1.00 17.25           O  
HETATM 3319  O   HOH A1019      27.882   0.423   8.342  1.00 29.10           O  
HETATM 3320  O   HOH A1020      30.053   2.283  11.702  1.00 21.06           O  
HETATM 3321  O   HOH A1021      22.540   8.901 -11.708  1.00 27.68           O  
HETATM 3322  O   HOH A1022      41.401  15.378  -3.231  1.00 11.54           O  
HETATM 3323  O   HOH A1023      32.880  -8.842 -15.057  1.00 20.44           O  
HETATM 3324  O   HOH A1024      57.355  -6.488   4.687  1.00 18.64           O  
HETATM 3325  O   HOH A1025      34.495  -1.067   7.194  1.00 15.37           O  
HETATM 3326  O   HOH A1026      29.789  13.771  19.643  1.00 28.37           O  
HETATM 3327  O   HOH A1027      55.903  11.243  15.143  1.00 30.55           O  
HETATM 3328  O   HOH A1028      48.161   9.787  -8.964  1.00 14.01           O  
HETATM 3329  O   HOH A1029      42.910  25.465   4.133  1.00 27.78           O  
HETATM 3330  O   HOH A1030      39.388  21.997  -7.546  1.00 21.36           O  
HETATM 3331  O   HOH A1031      33.047  12.997  14.526  1.00 31.35           O  
HETATM 3332  O   HOH A1032      25.684   5.739   8.480  1.00 28.02           O  
HETATM 3333  O   HOH A1033      34.549  -2.513  10.845  1.00 15.85           O  
HETATM 3334  O   HOH A1034      44.461  20.059  -2.468  1.00 24.64           O  
HETATM 3335  O   HOH A1035      23.015  -6.113   0.398  1.00 30.60           O  
HETATM 3336  O   HOH A1036      22.904  -0.618  -9.241  1.00 27.35           O  
HETATM 3337  O   HOH A1037      50.270  -8.101  -3.967  1.00 20.86           O  
HETATM 3338  O   HOH A1038      27.831  10.531   7.003  1.00 15.68           O  
HETATM 3339  O   HOH A1039      33.819  13.593  -7.157  1.00 11.04           O  
HETATM 3340  O   HOH A1040      59.808  -2.667  -6.269  1.00 15.86           O  
HETATM 3341  O   HOH A1041      43.185  16.640  -4.730  1.00 16.62           O  
HETATM 3342  O   HOH A1042      41.425   2.986 -18.792  1.00 28.69           O  
HETATM 3343  O   HOH A1043      62.224   3.775  -7.473  1.00 31.74           O  
HETATM 3344  O   HOH A1044      31.432 -19.364  10.303  1.00 18.15           O  
HETATM 3345  O   HOH A1045      32.287  -1.856   5.663  1.00 13.51           O  
HETATM 3346  O   HOH A1046      25.886  11.966 -13.191  1.00 26.28           O  
HETATM 3347  O   HOH A1047      26.069  17.556  -7.263  1.00 22.88           O  
HETATM 3348  O   HOH A1048      39.229  15.094  -4.739  1.00 15.53           O  
HETATM 3349  O   HOH A1049      38.495  -1.219  -6.888  1.00 13.10           O  
HETATM 3350  O   HOH A1050      29.701  11.433   5.189  1.00 19.07           O  
HETATM 3351  O   HOH A1051      31.049  13.525  -8.844  1.00 15.84           O  
HETATM 3352  O   HOH A1052      41.739  23.992   9.645  1.00 21.43           O  
HETATM 3353  O   HOH A1053      24.915  -3.970   5.508  1.00 15.77           O  
HETATM 3354  O   HOH A1054      50.788  13.335   5.896  1.00 21.77           O  
HETATM 3355  O   HOH A1055      60.527   1.471  -4.417  1.00 14.32           O  
HETATM 3356  O   HOH A1056      32.714   9.382  -1.079  1.00 16.06           O  
HETATM 3357  O   HOH A1057      46.367  19.708  -4.438  1.00 34.92           O  
HETATM 3358  O   HOH A1058      30.435  21.234  20.160  1.00 25.54           O  
HETATM 3359  O   HOH A1059      23.592  -1.786   4.445  1.00 18.24           O  
HETATM 3360  O   HOH A1060      29.976 -19.622  12.214  1.00 19.97           O  
HETATM 3361  O   HOH A1061      41.532  18.722  15.236  1.00 29.79           O  
HETATM 3362  O   HOH A1062      24.505  12.836 -10.604  1.00 25.96           O  
HETATM 3363  O   HOH A1063      41.394   2.913  14.544  1.00 26.58           O  
HETATM 3364  O   HOH A1064      38.605   2.145 -18.728  1.00 27.92           O  
HETATM 3365  O   HOH A1065      38.520   1.026  -5.400  1.00 13.86           O  
HETATM 3366  O   HOH A1066      38.595  -1.871 -19.281  1.00 26.65           O  
HETATM 3367  O   HOH A1067      62.542   0.079   7.032  1.00 22.69           O  
HETATM 3368  O   HOH A1068      23.993  15.454  -9.833  1.00 26.75           O  
HETATM 3369  O   HOH A1069      25.345   9.625   6.259  1.00 21.79           O  
HETATM 3370  O   HOH A1070      34.547   7.852  -2.952  1.00 18.54           O  
HETATM 3371  O   HOH A1071      55.339  20.011   5.936  1.00 28.30           O  
HETATM 3372  O   HOH A1072      54.145  12.788  -2.998  1.00 23.71           O  
HETATM 3373  O   HOH A1073      60.657   2.205  -6.632  1.00 23.32           O  
HETATM 3374  O   HOH A1074      27.790   3.558  16.348  1.00 32.93           O  
HETATM 3375  O   HOH A1075      52.156  -0.968  -8.429  1.00 31.65           O  
HETATM 3376  O   HOH A1076      44.522  18.029  14.895  1.00 28.03           O  
HETATM 3377  O   HOH A1077      47.573  -4.601   7.959  1.00 34.56           O  
HETATM 3378  O   HOH A1078      32.985  -6.589  11.336  1.00 24.45           O  
HETATM 3379  O   HOH A1079      28.977  18.088  -5.174  1.00 19.19           O  
HETATM 3380  O   HOH A1080      28.660  11.594 -15.192  1.00 30.51           O  
HETATM 3381  O   HOH A1081      22.407  -3.071   0.330  1.00 24.31           O  
HETATM 3382  O   HOH A1082      41.859  23.827   7.254  1.00 22.89           O  
HETATM 3383  O   HOH A1083      38.010   8.062 -14.284  1.00 20.98           O  
HETATM 3384  O   HOH A1084      25.451   8.449   8.399  1.00 27.85           O  
HETATM 3385  O   HOH A1085      19.575  11.268  -8.235  1.00 28.90           O  
HETATM 3386  O   HOH A1086      21.838  -4.591   8.279  1.00 30.17           O  
HETATM 3387  O   HOH A1087      25.010  -8.204  -6.283  1.00 27.87           O  
HETATM 3388  O   HOH A1088      30.483 -16.475  -1.955  1.00 27.83           O  
HETATM 3389  O   HOH A1089      21.384  13.579  19.255  1.00 36.76           O  
HETATM 3390  O   HOH A1090      32.267  -3.589   6.537  1.00 34.87           O  
HETATM 3391  O   HOH A1091      36.403   8.597 -16.190  1.00 30.57           O  
HETATM 3392  O   HOH A1092      16.055  10.310  -1.423  1.00 30.61           O  
HETATM 3393  O   HOH A1093      53.713  16.018   4.441  1.00 33.81           O  
HETATM 3394  O   HOH A1094      30.856  18.221  -7.344  1.00 17.47           O  
HETATM 3395  O   HOH A1095      50.928  -3.130  12.071  1.00 39.08           O  
HETATM 3396  O   HOH A1096      21.621  15.385  21.497  1.00 31.36           O  
HETATM 3397  O   HOH A1097      55.221   1.579 -12.397  1.00 37.86           O  
HETATM 3398  O   HOH A1098      51.943  18.730   2.777  1.00 27.60           O  
HETATM 3399  O   HOH A1099      60.925   3.558  12.375  1.00 34.31           O  
HETATM 3400  O   HOH A1100      25.562 -15.872 -11.521  1.00 42.16           O  
HETATM 3401  O   HOH A1101      19.162  23.544  20.687  1.00 46.63           O  
HETATM 3402  O   HOH A1102      50.661  -5.624   8.722  1.00 28.05           O  
HETATM 3403  O   HOH A1103      21.424  27.504  15.960  1.00 35.01           O  
HETATM 3404  O   HOH A1104      17.144   6.307  -3.729  1.00 31.69           O  
HETATM 3405  O   HOH A1105      29.824 -14.569  -4.072  1.00 30.56           O  
HETATM 3406  O   HOH A1106      22.802  -0.502  12.577  1.00 36.37           O  
HETATM 3407  O   HOH A1107      23.609 -11.214   5.353  1.00 32.64           O  
HETATM 3408  O   HOH A1108      27.357  19.909  -8.691  1.00 27.87           O  
HETATM 3409  O   HOH A1109      34.276  23.570  -4.371  1.00 30.24           O  
HETATM 3410  O   HOH A1110      32.835 -21.946  10.092  1.00 38.80           O  
HETATM 3411  O   HOH A1111      23.115   2.364   8.882  1.00 31.38           O  
HETATM 3412  O   HOH A1112      48.245  31.148  13.082  1.00 45.47           O  
HETATM 3413  O   HOH A1113      27.861   4.564  18.273  1.00 35.35           O  
HETATM 3414  O   HOH A1114      37.649  -7.499 -16.517  1.00 38.42           O  
HETATM 3415  O   HOH A1115      53.178 -10.413  -1.623  1.00 38.19           O  
HETATM 3416  O   HOH A1116      13.688  15.304  13.412  1.00 36.20           O  
HETATM 3417  O   HOH A1117      28.004  31.953  15.925  1.00 44.49           O  
HETATM 3418  O   HOH A1118      52.679  15.294   1.952  1.00 29.98           O  
HETATM 3419  O   HOH A1119      51.479 -14.284  -2.387  1.00 37.48           O  
HETATM 3420  O   HOH A1120      57.316  -1.678   9.613  1.00 30.82           O  
HETATM 3421  O   HOH A1121      54.850  14.948  -1.505  1.00 34.06           O  
HETATM 3422  O   HOH A1122      29.020   4.842  13.412  1.00 39.39           O  
HETATM 3423  O   HOH A1123      41.764   8.120  16.042  1.00 34.14           O  
HETATM 3424  O   HOH A1124      13.874  17.249  11.741  1.00 33.68           O  
HETATM 3425  O   HOH A1125      48.581  12.298 -10.094  1.00 32.25           O  
HETATM 3426  O   HOH A1126      44.587  34.079  17.664  1.00 36.45           O  
HETATM 3427  O   HOH A1127      20.845  -1.965  -6.464  1.00 31.91           O  
HETATM 3428  O   HOH A1128      35.632   8.479 -19.058  1.00 32.69           O  
HETATM 3429  O   HOH A1129      28.039  32.498   0.332  1.00 41.00           O  
HETATM 3430  O   HOH A1130      45.881  12.199  18.702  1.00 35.59           O  
HETATM 3431  O   HOH A1131      36.349  22.231  -8.241  1.00 32.90           O  
HETATM 3432  O   HOH A1132      34.709  -6.629  18.176  1.00 42.79           O  
HETATM 3433  O   HOH A1133      38.723 -11.579   8.394  1.00 35.71           O  
HETATM 3434  O   HOH A1134      16.826  13.786   1.814  1.00 34.38           O  
HETATM 3435  O   HOH A1135      42.821  21.035  16.849  1.00 39.14           O  
HETATM 3436  O   HOH A1136      21.999   0.333   5.637  1.00 27.14           O  
HETATM 3437  O   HOH A1137      33.824  -3.478 -21.938  1.00 41.47           O  
HETATM 3438  O   HOH A1138      58.443  13.781  -3.211  1.00 34.97           O  
HETATM 3439  O   HOH A1139      34.434  21.144  -6.913  1.00 34.45           O  
HETATM 3440  O   HOH A1140      32.127 -20.981   6.983  1.00 31.84           O  
HETATM 3441  O   HOH A1141      46.631  -9.677   9.576  1.00 38.94           O  
HETATM 3442  O   HOH A1142      68.162  10.348  -1.306  1.00 31.92           O  
HETATM 3443  O   HOH A1143      14.991   9.511  22.530  1.00 45.21           O  
HETATM 3444  O   HOH A1144      33.180   7.025 -18.793  1.00 37.62           O  
HETATM 3445  O   HOH A1145      68.080  21.701  10.277  1.00 47.52           O  
HETATM 3446  O   HOH A1146      59.797  -1.660   9.655  1.00 38.20           O  
HETATM 3447  O   HOH A1147      53.457  -1.474  -7.074  1.00 40.80           O  
HETATM 3448  O   HOH A1148      16.335  19.910  -6.321  1.00 29.63           O  
HETATM 3449  O   HOH A1149      47.284  -5.596   9.666  1.00 40.60           O  
HETATM 3450  O   HOH A1150      16.023   8.143  14.641  1.00 39.20           O  
HETATM 3451  O   HOH A1151      20.537  -2.615  -1.009  1.00 32.16           O  
HETATM 3452  O   HOH A1152      33.741  19.189  -7.978  1.00 36.51           O  
HETATM 3453  O   HOH A1153      30.809 -21.458   5.157  1.00 41.20           O  
HETATM 3454  O   HOH A1154      61.319  18.030   7.858  1.00 39.67           O  
HETATM 3455  O   HOH A1155      42.772   1.439  16.717  1.00 40.30           O  
HETATM 3456  O   HOH A1156      17.926   8.989   7.611  1.00 31.43           O  
HETATM 3457  O   HOH A1157      53.830  -1.012  12.924  1.00 40.04           O  
HETATM 3458  O   HOH A1158      31.935 -19.200   4.027  1.00 48.20           O  
HETATM 3459  O   HOH A1159      59.565  23.590   9.341  1.00 36.88           O  
HETATM 3460  O   HOH A1160      46.772  14.357  -8.913  1.00 37.73           O  
HETATM 3461  O   HOH A1161      39.527  10.849 -15.107  1.00 45.26           O  
HETATM 3462  O   HOH A1162      17.996   7.941   4.074  1.00 44.14           O  
HETATM 3463  O   HOH A1163      62.768   6.216  12.302  1.00 45.82           O  
HETATM 3464  O   HOH A1164      26.665  -9.259  -8.174  1.00 38.54           O  
HETATM 3465  O   HOH A1165      22.658   2.013 -11.523  1.00 46.52           O  
HETATM 3466  O   HOH A1166      16.113   5.699  -5.772  1.00 37.02           O  
HETATM 3467  O   HOH A1167      46.748  28.201  13.852  1.00 35.86           O  
HETATM 3468  O   HOH A1168      55.648  -2.861  11.454  1.00 40.60           O  
HETATM 3469  O   HOH A1169      13.942   9.539  12.958  1.00 39.28           O  
HETATM 3470  O   HOH A1170      42.550  -4.536  13.924  1.00 40.06           O  
HETATM 3471  O   HOH A1171      16.083  16.429  19.777  1.00 44.45           O  
HETATM 3472  O   HOH A1172      18.167   3.809  -2.050  1.00 40.26           O  
HETATM 3473  O   HOH A1173      59.116   1.585  -8.423  1.00 39.14           O  
HETATM 3474  O   HOH A1174      43.454  31.171   5.183  1.00 51.17           O  
HETATM 3475  O   HOH A1175      51.530   8.134 -14.835  1.00 43.35           O  
HETATM 3476  O   HOH A1176      23.393   4.160   9.973  1.00 44.29           O  
HETATM 3477  O   HOH A1177      62.211   0.190  10.494  1.00 45.09           O  
HETATM 3478  O   HOH A1178      59.523  -4.283  10.911  1.00 34.84           O  
HETATM 3479  O   HOH A1179      44.278  -3.134  14.271  1.00 42.50           O  
HETATM 3480  O   HOH A1180      45.420  34.247  10.842  1.00 40.78           O  
HETATM 3481  O   HOH A1181      44.697  18.653  -7.350  1.00 40.76           O  
HETATM 3482  O   HOH A1182      36.752  20.677 -10.918  1.00 37.18           O  
HETATM 3483  O   HOH A1183      59.811  -6.970   3.401  1.00 40.08           O  
HETATM 3484  O   HOH A1184      41.448  20.849  -9.313  1.00 36.09           O  
HETATM 3485  O   HOH A1185      15.065   7.940  -2.240  1.00 44.33           O  
HETATM 3486  O   HOH A1186      39.237  37.022   6.029  1.00 43.99           O  
HETATM 3487  O   HOH A1187      46.739  -1.744 -17.930  1.00 49.03           O  
HETATM 3488  O   HOH A1188      56.691  -4.285   7.622  1.00 36.09           O  
HETATM 3489  O   HOH A1189      41.740  10.767 -16.044  1.00 49.50           O  
HETATM 3490  O   HOH A1190      63.404  12.232  -7.884  1.00 44.99           O  
HETATM 3491  O   HOH A1191      62.542   4.953  15.484  1.00 40.96           O  
HETATM 3492  O   HOH A1192      53.341  26.163   3.682  1.00 48.87           O  
HETATM 3493  O   HOH A1193      33.618  35.507   8.358  1.00 47.41           O  
HETATM 3494  O   HOH A1194      31.283  -6.579  14.048  1.00 43.68           O  
CONECT 3224 3225 3226 3227 3276                                                 
CONECT 3225 3224                                                                
CONECT 3226 3224                                                                
CONECT 3227 3224 3228                                                           
CONECT 3228 3227 3229                                                           
CONECT 3229 3228 3230 3231                                                      
CONECT 3230 3229 3235                                                           
CONECT 3231 3229 3232 3233                                                      
CONECT 3232 3231                                                                
CONECT 3233 3231 3234 3235                                                      
CONECT 3234 3233                                                                
CONECT 3235 3230 3233 3236                                                      
CONECT 3236 3235 3237 3245                                                      
CONECT 3237 3236 3238                                                           
CONECT 3238 3237 3239                                                           
CONECT 3239 3238 3240 3245                                                      
CONECT 3240 3239 3241 3242                                                      
CONECT 3241 3240                                                                
CONECT 3242 3240 3243                                                           
CONECT 3243 3242 3244                                                           
CONECT 3244 3243 3245                                                           
CONECT 3245 3236 3239 3244                                                      
CONECT 3246 3247 3263                                                           
CONECT 3247 3246 3248 3249                                                      
CONECT 3248 3247                                                                
CONECT 3249 3247 3250                                                           
CONECT 3250 3249 3251 3252                                                      
CONECT 3251 3250                                                                
CONECT 3252 3250 3253 3263                                                      
CONECT 3253 3252 3254                                                           
CONECT 3254 3253 3255 3261                                                      
CONECT 3255 3254 3256                                                           
CONECT 3256 3255 3257 3258                                                      
CONECT 3257 3256                                                                
CONECT 3258 3256 3259 3260                                                      
CONECT 3259 3258                                                                
CONECT 3260 3258 3261                                                           
CONECT 3261 3254 3260 3262                                                      
CONECT 3262 3261 3263 3264                                                      
CONECT 3263 3246 3252 3262                                                      
CONECT 3264 3262 3265                                                           
CONECT 3265 3264 3266 3267                                                      
CONECT 3266 3265                                                                
CONECT 3267 3265 3268 3269                                                      
CONECT 3268 3267                                                                
CONECT 3269 3267 3270 3271                                                      
CONECT 3270 3269                                                                
CONECT 3271 3269 3272                                                           
CONECT 3272 3271 3273                                                           
CONECT 3273 3272 3274 3275 3276                                                 
CONECT 3274 3273                                                                
CONECT 3275 3273                                                                
CONECT 3276 3224 3273                                                           
CONECT 3277 3278                                                                
CONECT 3278 3277 3279 3280                                                      
CONECT 3279 3278                                                                
CONECT 3280 3278 3281 3288                                                      
CONECT 3281 3280 3282                                                           
CONECT 3282 3281 3283 3287                                                      
CONECT 3283 3282 3284 3285 3286                                                 
CONECT 3284 3283                                                                
CONECT 3285 3283                                                                
CONECT 3286 3283                                                                
CONECT 3287 3282 3289                                                           
CONECT 3288 3280 3289                                                           
CONECT 3289 3287 3288 3290                                                      
CONECT 3290 3289 3291 3292                                                      
CONECT 3291 3290                                                                
CONECT 3292 3290 3293                                                           
CONECT 3293 3292 3294 3295                                                      
CONECT 3294 3293                                                                
CONECT 3295 3293 3296 3300                                                      
CONECT 3296 3295 3297                                                           
CONECT 3297 3296 3298                                                           
CONECT 3298 3297 3299                                                           
CONECT 3299 3298 3300                                                           
CONECT 3300 3295 3299                                                           
MASTER      355    0    2   18   19    0   12    6 3493    1   77   37          
END                                                                             


A second structure was input as follows:


HEADER    OXIDOREDUCTASE/OXIDOREDUCTASE INHIBITOR 31-MAR-14   4P8L              
TITLE     CRYSTAL STRUCTURE OF M. TUBERCULOSIS DPRE1 IN COMPLEX WITH THE NON-   
TITLE    2 COVALENT INHIBITOR TY36C                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROBABLE DECAPRENYLPHOSPHORYL-BETA-D-RIBOSE OXIDASE;       
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: DPRE1;                                                      
COMPND   5 EC: 1.-.-.-;                                                         
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: DPRE1, RV3790, MT3898;                                         
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET28B                                    
KEYWDS    DPRE1, INHIBITOR, COMPLEX, NON-COVALENT, OXIDOREDUCTASE-              
KEYWDS   2 OXIDOREDUCTASE INHIBITOR COMPLEX                                     
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.NERES,F.POJER,S.T.COLE                                              
REVDAT   3   22-NOV-17 4P8L    1       SOURCE REMARK                            
REVDAT   2   01-APR-15 4P8L    1       JRNL                                     
REVDAT   1   10-DEC-14 4P8L    0                                                
JRNL        AUTH   J.NERES,R.C.HARTKOORN,L.R.CHIARELLI,R.GADUPUDI,M.R.PASCA,    
JRNL        AUTH 2 G.MORI,A.VENTURELLI,S.SAVINA,V.MAKAROV,G.S.KOLLY,E.MOLTENI,  
JRNL        AUTH 3 C.BINDA,N.DHAR,S.FERRARI,P.BRODIN,V.DELORME,V.LANDRY,        
JRNL        AUTH 4 A.L.DE JESUS LOPES RIBEIRO,D.FARINA,P.SAXENA,F.POJER,        
JRNL        AUTH 5 A.CARTA,R.LUCIANI,A.PORTA,G.ZANONI,E.DE ROSSI,M.P.COSTI,     
JRNL        AUTH 6 G.RICCARDI,S.T.COLE                                          
JRNL        TITL   2-CARBOXYQUINOXALINES KILL MYCOBACTERIUM TUBERCULOSIS        
JRNL        TITL 2 THROUGH NONCOVALENT INHIBITION OF DPRE1.                     
JRNL        REF    ACS CHEM.BIOL.                V.  10   705 2015              
JRNL        REFN                   ESSN 1554-8937                               
JRNL        PMID   25427196                                                     
JRNL        DOI    10.1021/CB5007163                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.02 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0117                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.02                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 49.10                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 61205                          
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) : 0.195                           
REMARK   3   R VALUE            (WORKING SET) : 0.193                           
REMARK   3   FREE R VALUE                     : 0.228                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 3264                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.02                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.08                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 4291                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 97.06                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 224                          
REMARK   3   BIN FREE R VALUE                    : 0.3490                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 6730                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 163                                     
REMARK   3   SOLVENT ATOMS            : 276                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 38.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.01000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.03000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.187         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.161         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.118         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 4.356         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.958                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.943                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  7066 ; 0.007 ; 0.020       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  9625 ; 1.221 ; 1.983       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   872 ; 5.767 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   298 ;32.599 ;22.685       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  1086 ;15.146 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    59 ;16.175 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):  1054 ; 0.079 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  5405 ; 0.005 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4P8L COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 04-APR-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000200932.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 24-JUN-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 7.2                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : SLS                                
REMARK 200  BEAMLINE                       : X06DA                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0                                
REMARK 200  MONOCHROMATOR                  : BARTELS MONOCHROMATOR WITH DUAL    
REMARK 200                                   CHANNEL CUT CRYSTALS               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : PSI PILATUS 6M                     
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : NULL                               
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 123579                             
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.020                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.100                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 97.3                               
REMARK 200  DATA REDUNDANCY                : 2.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 14.6900                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.02                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.15                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 96.5                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.20                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.650                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: NULL                         
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: RMEAS 0.055 (OVERALL), 0.453 (OUTER SHELL)                   
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 48.82                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.40                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 36% POLYPROPYLENEGLYCOL 400, 100 MM      
REMARK 280  IMIDAZOLE, PH 7.2, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE       
REMARK 280  291K                                                                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 1 21 1                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y+1/2,-Z                                             
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000       41.57450            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
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 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     GLY A   -18                                                      
REMARK 465     SER A   -17                                                      
REMARK 465     SER A   -16                                                      
REMARK 465     HIS A   -15                                                      
REMARK 465     HIS A   -14                                                      
REMARK 465     HIS A   -13                                                      
REMARK 465     HIS A   -12                                                      
REMARK 465     HIS A   -11                                                      
REMARK 465     HIS A   -10                                                      
REMARK 465     SER A    -9                                                      
REMARK 465     SER A    -8                                                      
REMARK 465     GLY A    -7                                                      
REMARK 465     LEU A    -6                                                      
REMARK 465     VAL A    -5                                                      
REMARK 465     PRO A    -4                                                      
REMARK 465     ARG A    -3                                                      
REMARK 465     GLY A    -2                                                      
REMARK 465     SER A    -1                                                      
REMARK 465     HIS A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     LEU A     2                                                      
REMARK 465     SER A     3                                                      
REMARK 465     VAL A     4                                                      
REMARK 465     GLY B   -18                                                      
REMARK 465     SER B   -17                                                      
REMARK 465     SER B   -16                                                      
REMARK 465     HIS B   -15                                                      
REMARK 465     HIS B   -14                                                      
REMARK 465     HIS B   -13                                                      
REMARK 465     HIS B   -12                                                      
REMARK 465     HIS B   -11                                                      
REMARK 465     HIS B   -10                                                      
REMARK 465     SER B    -9                                                      
REMARK 465     SER B    -8                                                      
REMARK 465     GLY B    -7                                                      
REMARK 465     LEU B    -6                                                      
REMARK 465     VAL B    -5                                                      
REMARK 465     PRO B    -4                                                      
REMARK 465     ARG B    -3                                                      
REMARK 465     GLY B    -2                                                      
REMARK 465     SER B    -1                                                      
REMARK 465     HIS B     0                                                      
REMARK 465     MET B     1                                                      
REMARK 465     LEU B     2                                                      
REMARK 465     SER B     3                                                      
REMARK 465     VAL B     4                                                      
REMARK 465     GLY B     5                                                      
REMARK 465     ALA B     6                                                      
REMARK 465     GLN B   271                                                      
REMARK 465     LEU B   272                                                      
REMARK 465     LEU B   273                                                      
REMARK 465     THR B   274                                                      
REMARK 465     LEU B   275                                                      
REMARK 465     PRO B   276                                                      
REMARK 465     ASP B   277                                                      
REMARK 465     VAL B   278                                                      
REMARK 465     PHE B   279                                                      
REMARK 465     PRO B   280                                                      
REMARK 465     ASN B   281                                                      
REMARK 465     GLY B   282                                                      
REMARK 465     LEU B   283                                                      
REMARK 465     ALA B   284                                                      
REMARK 465     ASN B   285                                                      
REMARK 465     LYS B   286                                                      
REMARK 465     TYR B   287                                                      
REMARK 465     THR B   288                                                      
REMARK 465     PHE B   289                                                      
REMARK 465     GLY B   290                                                      
REMARK 465     PRO B   291                                                      
REMARK 465     ILE B   292                                                      
REMARK 465     LEU B   317                                                      
REMARK 465     ASP B   318                                                      
REMARK 465     MET B   319                                                      
REMARK 465     PHE B   320                                                      
REMARK 465     GLY B   321                                                      
REMARK 465     GLU B   322                                                      
REMARK 465     TRP B   323                                                      
REMARK 465     ASN B   324                                                      
REMARK 465     ARG B   325                                                      
REMARK 465     ALA B   326                                                      
REMARK 465     TYR B   327                                                      
REMARK 465     GLY B   328                                                      
REMARK 465     PRO B   329                                                      
REMARK 465     ALA B   330                                                      
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    ALA A  20       61.62     38.77                                   
REMARK 500    ASN A  66       79.09   -153.07                                   
REMARK 500    LEU A 240      123.46    -38.53                                   
REMARK 500    TYR A 327      -14.23     73.15                                   
REMARK 500    GLU B 263       59.06   -141.48                                   
REMARK 500    ALA B 343       45.00    -90.39                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 36C A 502                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue IMD A 503                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue FAD B 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 36C B 502                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 4P8C   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8H   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8K   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8M   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8N   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8P   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8T   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 4P8Y   RELATED DB: PDB                                   
DBREF  4P8L A    1   461  UNP    P72056   DPRE1_MYCTU      1    461             
DBREF  4P8L B    1   461  UNP    P72056   DPRE1_MYCTU      1    461             
SEQADV 4P8L GLY A  -18  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER A  -17  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER A  -16  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A  -15  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A  -14  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A  -13  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A  -12  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A  -11  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A  -10  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER A   -9  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER A   -8  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L GLY A   -7  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L LEU A   -6  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L VAL A   -5  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L PRO A   -4  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L ARG A   -3  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L GLY A   -2  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER A   -1  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS A    0  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L GLY B  -18  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER B  -17  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER B  -16  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B  -15  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B  -14  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B  -13  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B  -12  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B  -11  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B  -10  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER B   -9  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER B   -8  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L GLY B   -7  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L LEU B   -6  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L VAL B   -5  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L PRO B   -4  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L ARG B   -3  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L GLY B   -2  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L SER B   -1  UNP  P72056              EXPRESSION TAG                 
SEQADV 4P8L HIS B    0  UNP  P72056              EXPRESSION TAG                 
SEQRES   1 A  480  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 A  480  VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA THR          
SEQRES   3 A  480  THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR ALA          
SEQRES   4 A  480  PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA GLU          
SEQRES   5 A  480  MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER GLY          
SEQRES   6 A  480  GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG SER          
SEQRES   7 A  480  TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL ILE          
SEQRES   8 A  480  ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP ALA          
SEQRES   9 A  480  ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN LEU          
SEQRES  10 A  480  ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU TRP          
SEQRES  11 A  480  VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL GLY          
SEQRES  12 A  480  GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS HIS          
SEQRES  13 A  480  SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET ASP          
SEQRES  14 A  480  LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR PRO          
SEQRES  15 A  480  THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL GLY          
SEQRES  16 A  480  GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR ILE          
SEQRES  17 A  480  GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA ASP          
SEQRES  18 A  480  GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA LEU          
SEQRES  19 A  480  HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER SER          
SEQRES  20 A  480  ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU GLY          
SEQRES  21 A  480  ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL GLU          
SEQRES  22 A  480  GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS PHE          
SEQRES  23 A  480  ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE PRO          
SEQRES  24 A  480  ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE GLY          
SEQRES  25 A  480  GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY LYS          
SEQRES  26 A  480  VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP MET          
SEQRES  27 A  480  PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY PHE          
SEQRES  28 A  480  LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL ASP          
SEQRES  29 A  480  GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER GLY          
SEQRES  30 A  480  HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY PRO          
SEQRES  31 A  480  ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY TRP          
SEQRES  32 A  480  ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU GLY          
SEQRES  33 A  480  LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU PHE          
SEQRES  34 A  480  GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR THR          
SEQRES  35 A  480  ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP GLU          
SEQRES  36 A  480  TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG VAL          
SEQRES  37 A  480  PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU              
SEQRES   1 B  480  GLY SER SER HIS HIS HIS HIS HIS HIS SER SER GLY LEU          
SEQRES   2 B  480  VAL PRO ARG GLY SER HIS MET LEU SER VAL GLY ALA THR          
SEQRES   3 B  480  THR THR ALA THR ARG LEU THR GLY TRP GLY ARG THR ALA          
SEQRES   4 B  480  PRO SER VAL ALA ASN VAL LEU ARG THR PRO ASP ALA GLU          
SEQRES   5 B  480  MET ILE VAL LYS ALA VAL ALA ARG VAL ALA GLU SER GLY          
SEQRES   6 B  480  GLY GLY ARG GLY ALA ILE ALA ARG GLY LEU GLY ARG SER          
SEQRES   7 B  480  TYR GLY ASP ASN ALA GLN ASN GLY GLY GLY LEU VAL ILE          
SEQRES   8 B  480  ASP MET THR PRO LEU ASN THR ILE HIS SER ILE ASP ALA          
SEQRES   9 B  480  ASP THR LYS LEU VAL ASP ILE ASP ALA GLY VAL ASN LEU          
SEQRES  10 B  480  ASP GLN LEU MET LYS ALA ALA LEU PRO PHE GLY LEU TRP          
SEQRES  11 B  480  VAL PRO VAL LEU PRO GLY THR ARG GLN VAL THR VAL GLY          
SEQRES  12 B  480  GLY ALA ILE ALA CYS ASP ILE HIS GLY LYS ASN HIS HIS          
SEQRES  13 B  480  SER ALA GLY SER PHE GLY ASN HIS VAL ARG SER MET ASP          
SEQRES  14 B  480  LEU LEU THR ALA ASP GLY GLU ILE ARG HIS LEU THR PRO          
SEQRES  15 B  480  THR GLY GLU ASP ALA GLU LEU PHE TRP ALA THR VAL GLY          
SEQRES  16 B  480  GLY ASN GLY LEU THR GLY ILE ILE MET ARG ALA THR ILE          
SEQRES  17 B  480  GLU MET THR PRO THR SER THR ALA TYR PHE ILE ALA ASP          
SEQRES  18 B  480  GLY ASP VAL THR ALA SER LEU ASP GLU THR ILE ALA LEU          
SEQRES  19 B  480  HIS SER ASP GLY SER GLU ALA ARG TYR THR TYR SER SER          
SEQRES  20 B  480  ALA TRP PHE ASP ALA ILE SER ALA PRO PRO LYS LEU GLY          
SEQRES  21 B  480  ARG ALA ALA VAL SER ARG GLY ARG LEU ALA THR VAL GLU          
SEQRES  22 B  480  GLN LEU PRO ALA LYS LEU ARG SER GLU PRO LEU LYS PHE          
SEQRES  23 B  480  ASP ALA PRO GLN LEU LEU THR LEU PRO ASP VAL PHE PRO          
SEQRES  24 B  480  ASN GLY LEU ALA ASN LYS TYR THR PHE GLY PRO ILE GLY          
SEQRES  25 B  480  GLU LEU TRP TYR ARG LYS SER GLY THR TYR ARG GLY LYS          
SEQRES  26 B  480  VAL GLN ASN LEU THR GLN PHE TYR HIS PRO LEU ASP MET          
SEQRES  27 B  480  PHE GLY GLU TRP ASN ARG ALA TYR GLY PRO ALA GLY PHE          
SEQRES  28 B  480  LEU GLN TYR GLN PHE VAL ILE PRO THR GLU ALA VAL ASP          
SEQRES  29 B  480  GLU PHE LYS LYS ILE ILE GLY VAL ILE GLN ALA SER GLY          
SEQRES  30 B  480  HIS TYR SER PHE LEU ASN VAL PHE LYS LEU PHE GLY PRO          
SEQRES  31 B  480  ARG ASN GLN ALA PRO LEU SER PHE PRO ILE PRO GLY TRP          
SEQRES  32 B  480  ASN ILE CYS VAL ASP PHE PRO ILE LYS ASP GLY LEU GLY          
SEQRES  33 B  480  LYS PHE VAL SER GLU LEU ASP ARG ARG VAL LEU GLU PHE          
SEQRES  34 B  480  GLY GLY ARG LEU TYR THR ALA LYS ASP SER ARG THR THR          
SEQRES  35 B  480  ALA GLU THR PHE HIS ALA MET TYR PRO ARG VAL ASP GLU          
SEQRES  36 B  480  TRP ILE SER VAL ARG ARG LYS VAL ASP PRO LEU ARG VAL          
SEQRES  37 B  480  PHE ALA SER ASP MET ALA ARG ARG LEU GLU LEU LEU              
HET    FAD  A 501      53                                                       
HET    36C  A 502      26                                                       
HET    IMD  A 503       5                                                       
HET    FAD  B 501      53                                                       
HET    36C  B 502      26                                                       
HETNAM     FAD FLAVIN-ADENINE DINUCLEOTIDE                                      
HETNAM     36C 3-[(4-FLUOROBENZYL)AMINO]-6-(TRIFLUOROMETHYL)                    
HETNAM   2 36C  QUINOXALINE-2-CARBOXYLIC ACID                                   
HETNAM     IMD IMIDAZOLE                                                        
FORMUL   3  FAD    2(C27 H33 N9 O15 P2)                                         
FORMUL   4  36C    2(C17 H11 F4 N3 O2)                                          
FORMUL   5  IMD    C3 H5 N2 1+                                                  
FORMUL   8  HOH   *276(H2 O)                                                    
HELIX    1 AA1 ASP A   31  GLY A   46  1                                  16    
HELIX    2 AA2 ASN A   97  LEU A  106  1                                  10    
HELIX    3 AA3 THR A  122  CYS A  129  1                                   8    
HELIX    4 AA4 ASN A  135  GLY A  140  1                                   6    
HELIX    5 AA5 SER A  141  ASN A  144  5                                   4    
HELIX    6 AA6 ASP A  167  VAL A  175  1                                   9    
HELIX    7 AA7 SER A  208  ASP A  218  1                                  11    
HELIX    8 AA8 GLY A  219  TYR A  224  5                                   6    
HELIX    9 AA9 THR A  252  LEU A  256  5                                   5    
HELIX   10 AB1 PRO A  257  SER A  262  1                                   6    
HELIX   11 AB2 THR A  274  PHE A  279  1                                   6    
HELIX   12 AB3 GLY A  290  GLY A  301  1                                  12    
HELIX   13 AB4 ASN A  309  HIS A  315  1                                   7    
HELIX   14 AB5 PRO A  316  ASN A  324  5                                   9    
HELIX   15 AB6 ALA A  343  SER A  357  1                                  15    
HELIX   16 AB7 GLY A  395  PHE A  410  1                                  16    
HELIX   17 AB8 THR A  423  TYR A  431  1                                   9    
HELIX   18 AB9 ARG A  433  ASP A  445  1                                  13    
HELIX   19 AC1 SER A  452  LEU A  458  1                                   7    
HELIX   20 AC2 ASP B   31  GLY B   46  1                                  16    
HELIX   21 AC3 ASN B   97  LEU B  106  1                                  10    
HELIX   22 AC4 THR B  122  CYS B  129  1                                   8    
HELIX   23 AC5 ASN B  135  GLY B  140  1                                   6    
HELIX   24 AC6 SER B  141  ASN B  144  5                                   4    
HELIX   25 AC7 ASP B  167  VAL B  175  1                                   9    
HELIX   26 AC8 SER B  208  ASP B  218  1                                  11    
HELIX   27 AC9 GLY B  219  TYR B  224  5                                   6    
HELIX   28 AD1 THR B  252  LEU B  256  5                                   5    
HELIX   29 AD2 PRO B  257  SER B  262  1                                   6    
HELIX   30 AD3 GLU B  294  GLY B  301  1                                   8    
HELIX   31 AD4 ASN B  309  TYR B  314  1                                   6    
HELIX   32 AD5 ALA B  343  SER B  357  1                                  15    
HELIX   33 AD6 GLY B  395  PHE B  410  1                                  16    
HELIX   34 AD7 THR B  423  TYR B  431  1                                   9    
HELIX   35 AD8 ARG B  433  ASP B  445  1                                  13    
HELIX   36 AD9 SER B  452  LEU B  458  1                                   7    
SHEET    1 AA1 4 THR A   7  LEU A  13  0                                        
SHEET    2 AA1 4 SER A  22  ARG A  28 -1  O  VAL A  26   N  THR A   9           
SHEET    3 AA1 4 LEU A  70  ASP A  73  1  O  VAL A  71   N  LEU A  27           
SHEET    4 AA1 4 ALA A  51  ARG A  54  1  N  ILE A  52   O  ILE A  72           
SHEET    1 AA210 ILE A 158  LEU A 161  0                                        
SHEET    2 AA210 VAL A 146  LEU A 152 -1  N  MET A 149   O  LEU A 161           
SHEET    3 AA210 ILE A 183  GLU A 190 -1  O  ILE A 183   N  LEU A 152           
SHEET    4 AA210 LEU A  89  ASP A  93 -1  N  ILE A  92   O  ALA A 187           
SHEET    5 AA210 ILE A  80  ASP A  84 -1  N  SER A  82   O  ASP A  91           
SHEET    6 AA210 ILE B  80  ASP B  84 -1  O  ILE B  83   N  ILE A  83           
SHEET    7 AA210 LEU B  89  ASP B  93 -1  O  ASP B  91   N  SER B  82           
SHEET    8 AA210 ILE B 183  GLU B 190 -1  O  ALA B 187   N  ILE B  92           
SHEET    9 AA210 VAL B 146  LEU B 152 -1  N  LEU B 152   O  ILE B 183           
SHEET   10 AA210 ILE B 158  LEU B 161 -1  O  LEU B 161   N  MET B 149           
SHEET    1 AA3 2 LEU A 110  TRP A 111  0                                        
SHEET    2 AA3 2 THR A 192  PRO A 193 -1  O  THR A 192   N  TRP A 111           
SHEET    1 AA4 8 TYR A 303  GLN A 308  0                                        
SHEET    2 AA4 8 PHE A 199  VAL A 205 -1  N  PHE A 199   O  GLN A 308           
SHEET    3 AA4 8 ALA A 243  LEU A 250 -1  O  ARG A 247   N  ASP A 202           
SHEET    4 AA4 8 TYR A 226  PHE A 231 -1  N  SER A 228   O  SER A 246           
SHEET    5 AA4 8 VAL A 365  PHE A 369 -1  O  PHE A 366   N  ALA A 229           
SHEET    6 AA4 8 GLY A 383  PRO A 391 -1  O  ASN A 385   N  LYS A 367           
SHEET    7 AA4 8 PHE A 332  PRO A 340 -1  N  LEU A 333   O  PHE A 390           
SHEET    8 AA4 8 ARG A 413  LEU A 414 -1  O  ARG A 413   N  VAL A 338           
SHEET    1 AA5 4 THR B   9  LEU B  13  0                                        
SHEET    2 AA5 4 SER B  22  LEU B  27 -1  O  ALA B  24   N  THR B  11           
SHEET    3 AA5 4 LEU B  70  ASP B  73  1  O  VAL B  71   N  ASN B  25           
SHEET    4 AA5 4 ALA B  51  ARG B  54  1  N  ARG B  54   O  ILE B  72           
SHEET    1 AA6 2 LEU B 110  TRP B 111  0                                        
SHEET    2 AA6 2 THR B 192  PRO B 193 -1  O  THR B 192   N  TRP B 111           
SHEET    1 AA7 4 TYR B 226  PHE B 231  0                                        
SHEET    2 AA7 4 ALA B 243  LEU B 250 -1  O  SER B 246   N  SER B 228           
SHEET    3 AA7 4 PHE B 199  VAL B 205 -1  N  ASP B 204   O  VAL B 245           
SHEET    4 AA7 4 TYR B 303  GLN B 308 -1  O  LYS B 306   N  ALA B 201           
SHEET    1 AA8 4 VAL B 365  PHE B 369  0                                        
SHEET    2 AA8 4 GLY B 383  PRO B 391 -1  O  ASN B 385   N  LYS B 367           
SHEET    3 AA8 4 PHE B 332  PRO B 340 -1  N  ILE B 339   O  TRP B 384           
SHEET    4 AA8 4 ARG B 413  LEU B 414 -1  O  ARG B 413   N  VAL B 338           
CISPEP   1 SER A   45    GLY A   46          0       -15.72                     
CISPEP   2 PRO A  237    PRO A  238          0         7.89                     
CISPEP   3 GLY B   48    ARG B   49          0        11.20                     
CISPEP   4 PRO B  237    PRO B  238          0         4.60                     
CISPEP   5 HIS B  315    PRO B  316          0        -4.50                     
SITE     1 AC1 33 TRP A  16  ILE A  52  ALA A  53  GLY A  55                    
SITE     2 AC1 33 LEU A  56  GLY A  57  ARG A  58  SER A  59                    
SITE     3 AC1 33 TYR A  60  ASN A  63  ALA A  64  MET A  74                    
SITE     4 AC1 33 ALA A  94  PRO A 116  GLY A 117  THR A 118                    
SITE     5 AC1 33 VAL A 121  THR A 122  GLY A 124  GLY A 125                    
SITE     6 AC1 33 ALA A 128  CYS A 129  ILE A 131  HIS A 132                    
SITE     7 AC1 33 ASN A 178  GLY A 179  GLY A 182  ILE A 184                    
SITE     8 AC1 33 TYR A 415  ALA A 417  36C A 502  HOH A 658                    
SITE     9 AC1 33 HOH A 660                                                     
SITE     1 AC2 14 TYR A  60  HIS A 132  GLY A 133  LYS A 134                    
SITE     2 AC2 14 LEU A 317  ASN A 324  ARG A 325  GLN A 336                    
SITE     3 AC2 14 VAL A 365  LYS A 367  ASN A 385  CYS A 387                    
SITE     4 AC2 14 LYS A 418  FAD A 501                                          
SITE     1 AC3  4 SER A  82  ASP A  84  SER B  82  ASP B  84                    
SITE     1 AC4 33 TRP B  16  ILE B  52  ALA B  53  GLY B  55                    
SITE     2 AC4 33 LEU B  56  GLY B  57  ARG B  58  SER B  59                    
SITE     3 AC4 33 TYR B  60  ASN B  63  ALA B  64  MET B  74                    
SITE     4 AC4 33 ALA B  94  PRO B 116  GLY B 117  THR B 118                    
SITE     5 AC4 33 VAL B 121  THR B 122  GLY B 124  GLY B 125                    
SITE     6 AC4 33 ALA B 128  CYS B 129  ILE B 131  HIS B 132                    
SITE     7 AC4 33 ASN B 178  GLY B 179  GLY B 182  ILE B 184                    
SITE     8 AC4 33 TYR B 415  ALA B 417  36C B 502  HOH B 623                    
SITE     9 AC4 33 HOH B 650                                                     
SITE     1 AC5 11 TYR B  60  HIS B 132  GLY B 133  LYS B 134                    
SITE     2 AC5 11 TRP B 230  ASN B 364  VAL B 365  LYS B 367                    
SITE     3 AC5 11 CYS B 387  LYS B 418  FAD B 501                               
CRYST1   76.946   83.149   80.524  90.00 102.79  90.00 P 1 21 1      4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012996  0.000000  0.002950        0.00000                         
SCALE2      0.000000  0.012027  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012735        0.00000                         
ATOM      1  N   GLY A   5       8.283  -3.889   1.680  1.00 59.83           N  
ATOM      2  CA  GLY A   5       8.844  -3.507   0.351  1.00 61.35           C  
ATOM      3  C   GLY A   5       7.777  -3.287  -0.705  1.00 61.52           C  
ATOM      4  O   GLY A   5       7.197  -4.246  -1.220  1.00 62.70           O  
ATOM      5  N   ALA A   6       7.533  -2.020  -1.035  1.00 60.10           N  
ATOM      6  CA  ALA A   6       6.507  -1.631  -2.010  1.00 60.00           C  
ATOM      7  C   ALA A   6       6.805  -2.114  -3.429  1.00 60.18           C  
ATOM      8  O   ALA A   6       7.940  -2.010  -3.906  1.00 59.11           O  
ATOM      9  CB  ALA A   6       6.317  -0.120  -2.008  1.00 58.46           C  
ATOM     10  N   THR A   7       5.774  -2.641  -4.088  1.00 59.10           N  
ATOM     11  CA  THR A   7       5.841  -3.027  -5.501  1.00 57.90           C  
ATOM     12  C   THR A   7       4.584  -2.562  -6.248  1.00 59.24           C  
ATOM     13  O   THR A   7       3.473  -2.614  -5.704  1.00 54.64           O  
ATOM     14  CB  THR A   7       5.994  -4.558  -5.692  1.00 57.62           C  
ATOM     15  OG1 THR A   7       4.858  -5.237  -5.142  1.00 56.63           O  
ATOM     16  CG2 THR A   7       7.276  -5.087  -5.035  1.00 55.40           C  
ATOM     17  N   THR A   8       4.781  -2.092  -7.481  1.00 59.06           N  
ATOM     18  CA  THR A   8       3.692  -1.762  -8.406  1.00 60.01           C  
ATOM     19  C   THR A   8       3.844  -2.612  -9.663  1.00 60.90           C  
ATOM     20  O   THR A   8       4.817  -2.462 -10.409  1.00 60.51           O  
ATOM     21  CB  THR A   8       3.666  -0.263  -8.792  1.00 61.63           C  
ATOM     22  OG1 THR A   8       4.998   0.192  -9.074  1.00 64.23           O  
ATOM     23  CG2 THR A   8       3.069   0.584  -7.671  1.00 59.28           C  
ATOM     24  N   THR A   9       2.880  -3.503  -9.885  1.00 59.67           N  
ATOM     25  CA  THR A   9       2.965  -4.515 -10.938  1.00 60.74           C  
ATOM     26  C   THR A   9       1.677  -4.570 -11.757  1.00 60.00           C  
ATOM     27  O   THR A   9       0.581  -4.567 -11.195  1.00 62.60           O  
ATOM     28  CB  THR A   9       3.203  -5.918 -10.334  1.00 60.74           C  
ATOM     29  OG1 THR A   9       4.150  -5.831  -9.263  1.00 63.50           O  
ATOM     30  CG2 THR A   9       3.715  -6.898 -11.385  1.00 61.53           C  
ATOM     31  N   ALA A  10       1.813  -4.622 -13.081  1.00 57.47           N  
ATOM     32  CA  ALA A  10       0.674  -4.864 -13.961  1.00 54.96           C  
ATOM     33  C   ALA A  10       0.204  -6.300 -13.749  1.00 54.59           C  
ATOM     34  O   ALA A  10       0.993  -7.241 -13.868  1.00 54.16           O  
ATOM     35  CB  ALA A  10       1.055  -4.630 -15.412  1.00 53.71           C  
ATOM     36  N   THR A  11      -1.074  -6.466 -13.411  1.00 50.60           N  
ATOM     37  CA  THR A  11      -1.597  -7.788 -13.067  1.00 49.70           C  
ATOM     38  C   THR A  11      -2.992  -8.014 -13.641  1.00 49.75           C  
ATOM     39  O   THR A  11      -3.862  -7.140 -13.566  1.00 49.48           O  
ATOM     40  CB  THR A  11      -1.618  -8.006 -11.534  1.00 49.00           C  
ATOM     41  OG1 THR A  11      -0.403  -7.508 -10.960  1.00 45.92           O  
ATOM     42  CG2 THR A  11      -1.782  -9.485 -11.179  1.00 47.88           C  
ATOM     43  N   ARG A  12      -3.184  -9.194 -14.220  1.00 51.09           N  
ATOM     44  CA  ARG A  12      -4.475  -9.623 -14.728  1.00 51.31           C  
ATOM     45  C   ARG A  12      -5.305 -10.121 -13.550  1.00 49.60           C  
ATOM     46  O   ARG A  12      -4.947 -11.107 -12.897  1.00 49.19           O  
ATOM     47  CB  ARG A  12      -4.286 -10.738 -15.759  1.00 53.35           C  
ATOM     48  CG  ARG A  12      -5.573 -11.313 -16.328  1.00 55.37           C  
ATOM     49  CD  ARG A  12      -5.318 -12.723 -16.833  1.00 58.15           C  
ATOM     50  NE  ARG A  12      -6.180 -13.089 -17.953  1.00 59.70           N  
ATOM     51  CZ  ARG A  12      -7.202 -13.936 -17.880  1.00 60.96           C  
ATOM     52  NH1 ARG A  12      -7.517 -14.516 -16.727  1.00 64.43           N  
ATOM     53  NH2 ARG A  12      -7.915 -14.201 -18.968  1.00 61.81           N  
ATOM     54  N   LEU A  13      -6.410  -9.435 -13.277  1.00 46.44           N  
ATOM     55  CA  LEU A  13      -7.220  -9.764 -12.111  1.00 45.13           C  
ATOM     56  C   LEU A  13      -8.604 -10.254 -12.482  1.00 43.85           C  
ATOM     57  O   LEU A  13      -9.221  -9.757 -13.429  1.00 44.74           O  
ATOM     58  CB  LEU A  13      -7.333  -8.558 -11.181  1.00 43.79           C  
ATOM     59  CG  LEU A  13      -6.026  -7.918 -10.713  1.00 43.78           C  
ATOM     60  CD1 LEU A  13      -6.308  -6.515 -10.209  1.00 41.65           C  
ATOM     61  CD2 LEU A  13      -5.337  -8.772  -9.651  1.00 40.87           C  
ATOM     62  N   THR A  14      -9.065 -11.249 -11.730  1.00 43.95           N  
ATOM     63  CA  THR A  14     -10.457 -11.690 -11.738  1.00 44.40           C  
ATOM     64  C   THR A  14     -10.918 -11.796 -10.283  1.00 42.70           C  
ATOM     65  O   THR A  14     -10.093 -11.886  -9.375  1.00 42.66           O  
ATOM     66  CB  THR A  14     -10.650 -13.078 -12.413  1.00 44.89           C  
ATOM     67  OG1 THR A  14     -10.230 -14.128 -11.525  1.00 43.10           O  
ATOM     68  CG2 THR A  14      -9.897 -13.183 -13.748  1.00 45.52           C  
ATOM     69  N   GLY A  15     -12.230 -11.788 -10.062  1.00 42.58           N  
ATOM     70  CA  GLY A  15     -12.785 -12.170  -8.763  1.00 40.56           C  
ATOM     71  C   GLY A  15     -12.719 -13.682  -8.613  1.00 41.21           C  
ATOM     72  O   GLY A  15     -12.184 -14.383  -9.480  1.00 39.93           O  
ATOM     73  N   TRP A  16     -13.282 -14.191  -7.521  1.00 41.61           N  
ATOM     74  CA  TRP A  16     -13.297 -15.625  -7.240  1.00 40.68           C  
ATOM     75  C   TRP A  16     -13.899 -16.446  -8.356  1.00 42.91           C  
ATOM     76  O   TRP A  16     -13.531 -17.605  -8.538  1.00 42.76           O  
ATOM     77  CB  TRP A  16     -14.029 -15.889  -5.931  1.00 40.48           C  
ATOM     78  CG  TRP A  16     -13.586 -17.147  -5.228  1.00 40.19           C  
ATOM     79  CD1 TRP A  16     -14.336 -18.294  -4.982  1.00 37.39           C  
ATOM     80  CD2 TRP A  16     -12.255 -17.430  -4.657  1.00 40.80           C  
ATOM     81  NE1 TRP A  16     -13.590 -19.230  -4.310  1.00 40.44           N  
ATOM     82  CE2 TRP A  16     -12.334 -18.781  -4.088  1.00 41.05           C  
ATOM     83  CE3 TRP A  16     -11.055 -16.728  -4.570  1.00 42.84           C  
ATOM     84  CZ2 TRP A  16     -11.249 -19.381  -3.461  1.00 43.50           C  
ATOM     85  CZ3 TRP A  16      -9.964 -17.342  -3.935  1.00 44.75           C  
ATOM     86  CH2 TRP A  16     -10.061 -18.640  -3.395  1.00 44.86           C  
ATOM     87  N   GLY A  17     -14.813 -15.845  -9.121  1.00 45.14           N  
ATOM     88  CA  GLY A  17     -15.496 -16.513 -10.234  1.00 46.48           C  
ATOM     89  C   GLY A  17     -14.655 -16.785 -11.476  1.00 49.34           C  
ATOM     90  O   GLY A  17     -15.093 -17.504 -12.375  1.00 46.92           O  
ATOM     91  N   ARG A  18     -13.451 -16.212 -11.520  1.00 51.48           N  
ATOM     92  CA  ARG A  18     -12.515 -16.348 -12.654  1.00 54.94           C  
ATOM     93  C   ARG A  18     -13.080 -15.842 -13.996  1.00 54.47           C  
ATOM     94  O   ARG A  18     -12.728 -16.358 -15.057  1.00 55.43           O  
ATOM     95  CB  ARG A  18     -11.976 -17.790 -12.797  1.00 58.94           C  
ATOM     96  CG  ARG A  18     -11.687 -18.541 -11.500  1.00 62.55           C  
ATOM     97  CD  ARG A  18     -10.587 -17.904 -10.665  1.00 66.22           C  
ATOM     98  NE  ARG A  18     -10.485 -18.553  -9.358  1.00 70.57           N  
ATOM     99  CZ  ARG A  18      -9.884 -18.031  -8.291  1.00 70.61           C  
ATOM    100  NH1 ARG A  18      -9.316 -16.829  -8.349  1.00 68.03           N  
ATOM    101  NH2 ARG A  18      -9.858 -18.717  -7.155  1.00 70.13           N  
ATOM    102  N   THR A  19     -13.949 -14.833 -13.942  1.00 54.31           N  
ATOM    103  CA  THR A  19     -14.525 -14.233 -15.152  1.00 53.90           C  
ATOM    104  C   THR A  19     -14.144 -12.758 -15.274  1.00 50.57           C  
ATOM    105  O   THR A  19     -13.546 -12.191 -14.361  1.00 47.92           O  
ATOM    106  CB  THR A  19     -16.064 -14.383 -15.215  1.00 55.03           C  
ATOM    107  OG1 THR A  19     -16.651 -13.884 -14.005  1.00 58.47           O  
ATOM    108  CG2 THR A  19     -16.464 -15.841 -15.412  1.00 55.70           C  
ATOM    109  N   ALA A  20     -14.488 -12.158 -16.414  1.00 49.44           N  
ATOM    110  CA  ALA A  20     -14.189 -10.752 -16.725  1.00 50.21           C  
ATOM    111  C   ALA A  20     -12.805 -10.266 -16.249  1.00 49.22           C  
ATOM    112  O   ALA A  20     -12.720  -9.357 -15.419  1.00 46.27           O  
ATOM    113  CB  ALA A  20     -15.301  -9.846 -16.199  1.00 50.28           C  
ATOM    114  N   PRO A  21     -11.714 -10.878 -16.763  1.00 49.42           N  
ATOM    115  CA  PRO A  21     -10.374 -10.395 -16.395  1.00 48.44           C  
ATOM    116  C   PRO A  21     -10.088  -8.989 -16.923  1.00 48.78           C  
ATOM    117  O   PRO A  21     -10.568  -8.617 -17.995  1.00 51.28           O  
ATOM    118  CB  PRO A  21      -9.435 -11.411 -17.056  1.00 49.80           C  
ATOM    119  CG  PRO A  21     -10.239 -12.033 -18.149  1.00 49.43           C  
ATOM    120  CD  PRO A  21     -11.650 -12.063 -17.640  1.00 49.55           C  
ATOM    121  N   SER A  22      -9.329  -8.210 -16.161  1.00 47.09           N  
ATOM    122  CA  SER A  22      -8.867  -6.899 -16.613  1.00 45.70           C  
ATOM    123  C   SER A  22      -7.524  -6.577 -15.967  1.00 44.77           C  
ATOM    124  O   SER A  22      -7.241  -7.016 -14.849  1.00 45.69           O  
ATOM    125  CB  SER A  22      -9.901  -5.806 -16.315  1.00 44.10           C  
ATOM    126  OG  SER A  22     -10.029  -5.584 -14.923  1.00 41.85           O  
ATOM    127  N   VAL A  23      -6.699  -5.817 -16.680  1.00 44.55           N  
ATOM    128  CA  VAL A  23      -5.325  -5.567 -16.253  1.00 43.22           C  
ATOM    129  C   VAL A  23      -5.246  -4.237 -15.511  1.00 43.03           C  
ATOM    130  O   VAL A  23      -5.735  -3.215 -15.996  1.00 43.16           O  
ATOM    131  CB  VAL A  23      -4.325  -5.592 -17.442  1.00 42.41           C  
ATOM    132  CG1 VAL A  23      -2.890  -5.466 -16.944  1.00 40.89           C  
ATOM    133  CG2 VAL A  23      -4.478  -6.872 -18.252  1.00 40.46           C  
ATOM    134  N   ALA A  24      -4.639  -4.271 -14.329  1.00 43.57           N  
ATOM    135  CA  ALA A  24      -4.464  -3.084 -13.504  1.00 44.28           C  
ATOM    136  C   ALA A  24      -3.066  -3.044 -12.902  1.00 44.07           C  
ATOM    137  O   ALA A  24      -2.422  -4.084 -12.738  1.00 46.12           O  
ATOM    138  CB  ALA A  24      -5.506  -3.063 -12.396  1.00 42.58           C  
ATOM    139  N   ASN A  25      -2.599  -1.840 -12.579  1.00 44.52           N  
ATOM    140  CA  ASN A  25      -1.395  -1.684 -11.769  1.00 46.48           C  
ATOM    141  C   ASN A  25      -1.713  -2.013 -10.312  1.00 45.76           C  
ATOM    142  O   ASN A  25      -2.414  -1.248  -9.643  1.00 46.69           O  
ATOM    143  CB  ASN A  25      -0.841  -0.260 -11.880  1.00 48.87           C  
ATOM    144  CG  ASN A  25       0.064  -0.076 -13.083  1.00 55.34           C  
ATOM    145  OD1 ASN A  25       1.190  -0.586 -13.114  1.00 58.21           O  
ATOM    146  ND2 ASN A  25      -0.416   0.666 -14.077  1.00 53.51           N  
ATOM    147  N   VAL A  26      -1.207  -3.147  -9.830  1.00 43.27           N  
ATOM    148  CA  VAL A  26      -1.426  -3.562  -8.444  1.00 40.79           C  
ATOM    149  C   VAL A  26      -0.324  -3.049  -7.521  1.00 41.91           C  
ATOM    150  O   VAL A  26       0.823  -3.501  -7.597  1.00 44.31           O  
ATOM    151  CB  VAL A  26      -1.559  -5.096  -8.310  1.00 39.85           C  
ATOM    152  CG1 VAL A  26      -1.577  -5.520  -6.844  1.00 38.32           C  
ATOM    153  CG2 VAL A  26      -2.819  -5.590  -9.004  1.00 39.37           C  
ATOM    154  N   LEU A  27      -0.670  -2.088  -6.668  1.00 39.75           N  
ATOM    155  CA  LEU A  27       0.226  -1.661  -5.597  1.00 41.74           C  
ATOM    156  C   LEU A  27       0.127  -2.611  -4.406  1.00 42.98           C  
ATOM    157  O   LEU A  27      -0.969  -3.005  -3.989  1.00 43.02           O  
ATOM    158  CB  LEU A  27      -0.058  -0.214  -5.161  1.00 42.54           C  
ATOM    159  CG  LEU A  27       0.622   0.307  -3.880  1.00 43.86           C  
ATOM    160  CD1 LEU A  27       2.145   0.287  -3.979  1.00 42.51           C  
ATOM    161  CD2 LEU A  27       0.128   1.704  -3.530  1.00 42.14           C  
ATOM    162  N   ARG A  28       1.281  -2.976  -3.860  1.00 42.31           N  
ATOM    163  CA  ARG A  28       1.340  -3.855  -2.707  1.00 41.79           C  
ATOM    164  C   ARG A  28       2.429  -3.407  -1.741  1.00 43.19           C  
ATOM    165  O   ARG A  28       3.615  -3.675  -1.951  1.00 43.74           O  
ATOM    166  CB  ARG A  28       1.559  -5.292  -3.159  1.00 43.04           C  
ATOM    167  CG  ARG A  28       1.661  -6.293  -2.031  1.00 45.43           C  
ATOM    168  CD  ARG A  28       1.702  -7.705  -2.578  1.00 48.42           C  
ATOM    169  NE  ARG A  28       2.214  -8.626  -1.572  1.00 52.77           N  
ATOM    170  CZ  ARG A  28       1.461  -9.395  -0.793  1.00 54.38           C  
ATOM    171  NH1 ARG A  28       0.135  -9.380  -0.901  1.00 53.42           N  
ATOM    172  NH2 ARG A  28       2.043 -10.189   0.094  1.00 55.12           N  
ATOM    173  N   THR A  29       2.012  -2.722  -0.681  1.00 41.71           N  
ATOM    174  CA  THR A  29       2.939  -2.171   0.308  1.00 43.03           C  
ATOM    175  C   THR A  29       2.414  -2.362   1.729  1.00 42.79           C  
ATOM    176  O   THR A  29       1.213  -2.233   1.957  1.00 40.34           O  
ATOM    177  CB  THR A  29       3.219  -0.670   0.047  1.00 42.31           C  
ATOM    178  OG1 THR A  29       3.943  -0.109   1.149  1.00 44.67           O  
ATOM    179  CG2 THR A  29       1.924   0.121  -0.156  1.00 41.58           C  
ATOM    180  N   PRO A  30       3.309  -2.676   2.690  1.00 44.45           N  
ATOM    181  CA  PRO A  30       2.857  -2.716   4.084  1.00 43.63           C  
ATOM    182  C   PRO A  30       2.824  -1.332   4.721  1.00 44.74           C  
ATOM    183  O   PRO A  30       2.436  -1.191   5.882  1.00 44.22           O  
ATOM    184  CB  PRO A  30       3.901  -3.604   4.767  1.00 45.92           C  
ATOM    185  CG  PRO A  30       5.143  -3.427   3.949  1.00 44.65           C  
ATOM    186  CD  PRO A  30       4.706  -3.133   2.541  1.00 44.51           C  
ATOM    187  N   ASP A  31       3.207  -0.318   3.951  1.00 43.45           N  
ATOM    188  CA  ASP A  31       3.353   1.033   4.466  1.00 44.51           C  
ATOM    189  C   ASP A  31       2.110   1.894   4.176  1.00 43.89           C  
ATOM    190  O   ASP A  31       1.823   2.228   3.025  1.00 43.06           O  
ATOM    191  CB  ASP A  31       4.634   1.654   3.886  1.00 46.23           C  
ATOM    192  CG  ASP A  31       4.951   3.025   4.462  1.00 49.61           C  
ATOM    193  OD1 ASP A  31       4.166   3.561   5.279  1.00 49.23           O  
ATOM    194  OD2 ASP A  31       6.006   3.573   4.087  1.00 52.90           O  
ATOM    195  N   ALA A  32       1.383   2.247   5.233  1.00 44.01           N  
ATOM    196  CA  ALA A  32       0.191   3.097   5.128  1.00 45.20           C  
ATOM    197  C   ALA A  32       0.469   4.434   4.440  1.00 47.27           C  
ATOM    198  O   ALA A  32      -0.356   4.920   3.653  1.00 45.31           O  
ATOM    199  CB  ALA A  32      -0.417   3.332   6.503  1.00 45.08           C  
ATOM    200  N   GLU A  33       1.629   5.018   4.749  1.00 47.82           N  
ATOM    201  CA  GLU A  33       2.063   6.294   4.182  1.00 48.74           C  
ATOM    202  C   GLU A  33       2.154   6.246   2.655  1.00 46.37           C  
ATOM    203  O   GLU A  33       1.791   7.207   1.971  1.00 44.77           O  
ATOM    204  CB  GLU A  33       3.415   6.698   4.782  1.00 53.92           C  
ATOM    205  CG  GLU A  33       3.714   8.186   4.725  1.00 61.56           C  
ATOM    206  CD  GLU A  33       2.844   9.005   5.665  1.00 66.33           C  
ATOM    207  OE1 GLU A  33       3.027   8.896   6.900  1.00 69.36           O  
ATOM    208  OE2 GLU A  33       1.985   9.768   5.167  1.00 68.85           O  
ATOM    209  N   MET A  34       2.638   5.120   2.136  1.00 44.28           N  
ATOM    210  CA  MET A  34       2.734   4.891   0.696  1.00 44.68           C  
ATOM    211  C   MET A  34       1.349   4.816   0.043  1.00 43.83           C  
ATOM    212  O   MET A  34       1.114   5.412  -1.014  1.00 42.32           O  
ATOM    213  CB  MET A  34       3.525   3.610   0.421  1.00 45.76           C  
ATOM    214  CG  MET A  34       3.696   3.255  -1.047  1.00 50.33           C  
ATOM    215  SD  MET A  34       4.863   4.329  -1.913  1.00 59.66           S  
ATOM    216  CE  MET A  34       3.758   5.494  -2.697  1.00 53.45           C  
ATOM    217  N   ILE A  35       0.430   4.093   0.678  1.00 41.53           N  
ATOM    218  CA  ILE A  35      -0.944   4.026   0.187  1.00 40.71           C  
ATOM    219  C   ILE A  35      -1.522   5.440   0.054  1.00 39.71           C  
ATOM    220  O   ILE A  35      -2.061   5.787  -0.995  1.00 39.94           O  
ATOM    221  CB  ILE A  35      -1.825   3.111   1.071  1.00 40.31           C  
ATOM    222  CG1 ILE A  35      -1.309   1.675   1.000  1.00 39.13           C  
ATOM    223  CG2 ILE A  35      -3.295   3.189   0.654  1.00 40.72           C  
ATOM    224  CD1 ILE A  35      -1.884   0.761   2.063  1.00 42.06           C  
ATOM    225  N   VAL A  36      -1.368   6.257   1.099  1.00 40.94           N  
ATOM    226  CA  VAL A  36      -1.821   7.658   1.085  1.00 40.27           C  
ATOM    227  C   VAL A  36      -1.243   8.424  -0.110  1.00 42.18           C  
ATOM    228  O   VAL A  36      -1.973   9.149  -0.805  1.00 40.55           O  
ATOM    229  CB  VAL A  36      -1.480   8.391   2.405  1.00 40.19           C  
ATOM    230  CG1 VAL A  36      -1.721   9.895   2.281  1.00 39.31           C  
ATOM    231  CG2 VAL A  36      -2.292   7.818   3.558  1.00 39.83           C  
ATOM    232  N   LYS A  37       0.059   8.243  -0.347  1.00 43.28           N  
ATOM    233  CA  LYS A  37       0.754   8.915  -1.449  1.00 44.44           C  
ATOM    234  C   LYS A  37       0.191   8.569  -2.821  1.00 43.05           C  
ATOM    235  O   LYS A  37      -0.006   9.460  -3.653  1.00 43.10           O  
ATOM    236  CB  LYS A  37       2.253   8.628  -1.405  1.00 46.93           C  
ATOM    237  CG  LYS A  37       3.028   9.668  -0.628  1.00 51.83           C  
ATOM    238  CD  LYS A  37       4.296   9.094  -0.015  1.00 54.90           C  
ATOM    239  CE  LYS A  37       4.602   9.809   1.291  1.00 56.07           C  
ATOM    240  NZ  LYS A  37       3.340   9.990   2.071  1.00 57.56           N  
ATOM    241  N   ALA A  38      -0.064   7.277  -3.047  1.00 41.33           N  
ATOM    242  CA  ALA A  38      -0.653   6.801  -4.301  1.00 39.95           C  
ATOM    243  C   ALA A  38      -2.030   7.419  -4.560  1.00 39.16           C  
ATOM    244  O   ALA A  38      -2.330   7.843  -5.678  1.00 39.44           O  
ATOM    245  CB  ALA A  38      -0.729   5.281  -4.311  1.00 39.18           C  
ATOM    246  N   VAL A  39      -2.858   7.476  -3.519  1.00 38.28           N  
ATOM    247  CA  VAL A  39      -4.183   8.084  -3.626  1.00 37.68           C  
ATOM    248  C   VAL A  39      -4.063   9.589  -3.896  1.00 38.37           C  
ATOM    249  O   VAL A  39      -4.848  10.146  -4.667  1.00 36.61           O  
ATOM    250  CB  VAL A  39      -5.047   7.802  -2.376  1.00 36.99           C  
ATOM    251  CG1 VAL A  39      -6.383   8.534  -2.455  1.00 35.46           C  
ATOM    252  CG2 VAL A  39      -5.266   6.301  -2.220  1.00 36.95           C  
ATOM    253  N   ALA A  40      -3.067  10.228  -3.280  1.00 39.23           N  
ATOM    254  CA  ALA A  40      -2.788  11.648  -3.514  1.00 40.60           C  
ATOM    255  C   ALA A  40      -2.323  11.895  -4.952  1.00 41.58           C  
ATOM    256  O   ALA A  40      -2.674  12.910  -5.555  1.00 43.40           O  
ATOM    257  CB  ALA A  40      -1.763  12.164  -2.514  1.00 41.32           C  
ATOM    258  N   ARG A  41      -1.556  10.946  -5.487  1.00 42.41           N  
ATOM    259  CA  ARG A  41      -1.082  10.969  -6.865  1.00 45.71           C  
ATOM    260  C   ARG A  41      -2.233  10.850  -7.875  1.00 45.80           C  
ATOM    261  O   ARG A  41      -2.371  11.691  -8.771  1.00 44.37           O  
ATOM    262  CB  ARG A  41      -0.063   9.845  -7.080  1.00 49.71           C  
ATOM    263  CG  ARG A  41       0.871  10.059  -8.258  1.00 55.91           C  
ATOM    264  CD  ARG A  41       2.130  10.808  -7.843  1.00 62.46           C  
ATOM    265  NE  ARG A  41       2.882  11.287  -9.005  1.00 69.74           N  
ATOM    266  CZ  ARG A  41       3.670  10.527  -9.768  1.00 74.32           C  
ATOM    267  NH1 ARG A  41       3.827   9.227  -9.511  1.00 77.09           N  
ATOM    268  NH2 ARG A  41       4.303  11.070 -10.802  1.00 77.71           N  
ATOM    269  N   VAL A  42      -3.054   9.807  -7.725  1.00 44.06           N  
ATOM    270  CA  VAL A  42      -4.271   9.641  -8.531  1.00 42.53           C  
ATOM    271  C   VAL A  42      -5.152  10.897  -8.466  1.00 43.33           C  
ATOM    272  O   VAL A  42      -5.656  11.359  -9.491  1.00 45.41           O  
ATOM    273  CB  VAL A  42      -5.077   8.379  -8.111  1.00 42.36           C  
ATOM    274  CG1 VAL A  42      -6.417   8.308  -8.841  1.00 41.61           C  
ATOM    275  CG2 VAL A  42      -4.274   7.112  -8.376  1.00 41.30           C  
ATOM    276  N   ALA A  43      -5.304  11.463  -7.272  1.00 42.88           N  
ATOM    277  CA  ALA A  43      -6.166  12.631  -7.071  1.00 46.65           C  
ATOM    278  C   ALA A  43      -5.595  13.932  -7.649  1.00 51.47           C  
ATOM    279  O   ALA A  43      -6.344  14.878  -7.910  1.00 51.42           O  
ATOM    280  CB  ALA A  43      -6.479  12.807  -5.599  1.00 45.15           C  
ATOM    281  N   GLU A  44      -4.277  14.010  -7.748  1.00 54.69           N  
ATOM    282  CA  GLU A  44      -3.584  15.144  -8.335  1.00 57.74           C  
ATOM    283  C   GLU A  44      -3.719  15.201  -9.834  1.00 59.47           C  
ATOM    284  O   GLU A  44      -3.710  16.247 -10.443  1.00 58.59           O  
ATOM    285  CB  GLU A  44      -2.150  15.226  -7.852  1.00 57.66           C  
ATOM    286  CG  GLU A  44      -2.055  16.164  -6.679  1.00 60.20           C  
ATOM    287  CD  GLU A  44      -0.863  15.937  -5.780  1.00 62.67           C  
ATOM    288  OE1 GLU A  44      -0.173  14.923  -5.875  1.00 61.28           O  
ATOM    289  OE2 GLU A  44      -0.618  16.809  -4.950  1.00 64.51           O  
ATOM    290  N   SER A  45      -3.829  14.021 -10.402  1.00 62.12           N  
ATOM    291  CA  SER A  45      -3.920  13.827 -11.816  1.00 63.41           C  
ATOM    292  C   SER A  45      -5.153  14.465 -12.478  1.00 65.61           C  
ATOM    293  O   SER A  45      -5.015  14.994 -13.546  1.00 68.97           O  
ATOM    294  CB  SER A  45      -3.696  12.370 -12.174  1.00 62.26           C  
ATOM    295  OG  SER A  45      -4.898  11.718 -12.413  1.00 64.21           O  
ATOM    296  N   GLY A  46      -6.327  14.485 -11.863  1.00 64.99           N  
ATOM    297  CA  GLY A  46      -6.673  13.676 -10.725  1.00 68.16           C  
ATOM    298  C   GLY A  46      -7.925  12.872 -11.013  1.00 69.81           C  
ATOM    299  O   GLY A  46      -8.993  13.408 -11.231  1.00 71.39           O  
ATOM    300  N   GLY A  47      -7.760  11.562 -10.975  1.00 70.36           N  
ATOM    301  CA  GLY A  47      -8.776  10.594 -11.328  1.00 66.37           C  
ATOM    302  C   GLY A  47      -8.187   9.633 -12.340  1.00 65.51           C  
ATOM    303  O   GLY A  47      -7.744   8.559 -11.972  1.00 62.57           O  
ATOM    304  N   GLY A  48      -8.114  10.041 -13.609  1.00 63.52           N  
ATOM    305  CA  GLY A  48      -7.703   9.117 -14.658  1.00 58.07           C  
ATOM    306  C   GLY A  48      -8.663   7.956 -14.674  1.00 54.16           C  
ATOM    307  O   GLY A  48      -9.830   8.186 -14.764  1.00 54.17           O  
ATOM    308  N   ARG A  49      -8.164   6.733 -14.599  1.00 50.53           N  
ATOM    309  CA  ARG A  49      -8.982   5.552 -14.386  1.00 47.54           C  
ATOM    310  C   ARG A  49      -9.164   5.196 -12.922  1.00 44.88           C  
ATOM    311  O   ARG A  49      -9.730   4.175 -12.619  1.00 44.12           O  
ATOM    312  CB  ARG A  49      -8.388   4.350 -15.076  1.00 48.11           C  
ATOM    313  CG  ARG A  49      -8.637   4.283 -16.561  1.00 50.53           C  
ATOM    314  CD  ARG A  49     -10.095   4.106 -16.880  1.00 51.02           C  
ATOM    315  NE  ARG A  49     -10.436   2.705 -16.938  1.00 51.84           N  
ATOM    316  CZ  ARG A  49     -11.405   2.235 -17.678  1.00 51.01           C  
ATOM    317  NH1 ARG A  49     -12.111   3.073 -18.390  1.00 51.51           N  
ATOM    318  NH2 ARG A  49     -11.663   0.953 -17.694  1.00 49.12           N  
ATOM    319  N   GLY A  50      -8.608   6.004 -12.034  1.00 41.02           N  
ATOM    320  CA  GLY A  50      -8.795   5.883 -10.577  1.00 37.32           C  
ATOM    321  C   GLY A  50      -8.154   4.696  -9.874  1.00 34.51           C  
ATOM    322  O   GLY A  50      -7.267   4.032 -10.421  1.00 32.99           O  
ATOM    323  N   ALA A  51      -8.628   4.424  -8.656  1.00 32.74           N  
ATOM    324  CA  ALA A  51      -8.072   3.376  -7.790  1.00 31.65           C  
ATOM    325  C   ALA A  51      -9.160   2.631  -7.001  1.00 31.04           C  
ATOM    326  O   ALA A  51     -10.209   3.202  -6.693  1.00 30.83           O  
ATOM    327  CB  ALA A  51      -7.056   3.978  -6.827  1.00 30.24           C  
ATOM    328  N   ILE A  52      -8.903   1.366  -6.669  1.00 30.91           N  
ATOM    329  CA  ILE A  52      -9.806   0.597  -5.793  1.00 30.12           C  
ATOM    330  C   ILE A  52      -9.005  -0.291  -4.836  1.00 30.58           C  
ATOM    331  O   ILE A  52      -7.961  -0.837  -5.220  1.00 31.38           O  
ATOM    332  CB  ILE A  52     -10.851  -0.234  -6.601  1.00 28.82           C  
ATOM    333  CG1 ILE A  52     -12.050  -0.625  -5.728  1.00 28.87           C  
ATOM    334  CG2 ILE A  52     -10.238  -1.470  -7.240  1.00 28.40           C  
ATOM    335  CD1 ILE A  52     -13.045   0.500  -5.545  1.00 28.44           C  
ATOM    336  N   ALA A  53      -9.466  -0.420  -3.590  1.00 27.06           N  
ATOM    337  CA  ALA A  53      -8.884  -1.421  -2.696  1.00 27.20           C  
ATOM    338  C   ALA A  53      -9.208  -2.853  -3.130  1.00 26.89           C  
ATOM    339  O   ALA A  53     -10.240  -3.115  -3.755  1.00 27.42           O  
ATOM    340  CB  ALA A  53      -9.311  -1.188  -1.254  1.00 26.10           C  
ATOM    341  N   ARG A  54      -8.300  -3.766  -2.810  1.00 26.99           N  
ATOM    342  CA  ARG A  54      -8.537  -5.200  -2.945  1.00 27.75           C  
ATOM    343  C   ARG A  54      -8.153  -5.894  -1.648  1.00 26.39           C  
ATOM    344  O   ARG A  54      -7.130  -5.573  -1.041  1.00 26.08           O  
ATOM    345  CB  ARG A  54      -7.730  -5.770  -4.107  1.00 28.33           C  
ATOM    346  CG  ARG A  54      -7.901  -7.259  -4.350  1.00 29.80           C  
ATOM    347  CD  ARG A  54      -7.092  -7.651  -5.580  1.00 30.92           C  
ATOM    348  NE  ARG A  54      -7.317  -9.036  -5.969  1.00 32.75           N  
ATOM    349  CZ  ARG A  54      -8.253  -9.442  -6.827  1.00 32.67           C  
ATOM    350  NH1 ARG A  54      -9.081  -8.569  -7.396  1.00 34.48           N  
ATOM    351  NH2 ARG A  54      -8.364 -10.731  -7.116  1.00 31.33           N  
ATOM    352  N   GLY A  55      -8.993  -6.833  -1.221  1.00 27.46           N  
ATOM    353  CA  GLY A  55      -8.725  -7.644  -0.034  1.00 27.76           C  
ATOM    354  C   GLY A  55      -8.193  -9.006  -0.450  1.00 28.31           C  
ATOM    355  O   GLY A  55      -7.204  -9.091  -1.166  1.00 27.27           O  
ATOM    356  N   LEU A  56      -8.859 -10.075  -0.029  1.00 27.59           N  
ATOM    357  CA  LEU A  56      -8.400 -11.420  -0.374  1.00 27.55           C  
ATOM    358  C   LEU A  56      -8.967 -11.955  -1.694  1.00 28.07           C  
ATOM    359  O   LEU A  56      -8.738 -13.111  -2.047  1.00 28.26           O  
ATOM    360  CB  LEU A  56      -8.634 -12.394   0.791  1.00 26.79           C  
ATOM    361  CG  LEU A  56      -7.540 -12.296   1.869  1.00 27.36           C  
ATOM    362  CD1 LEU A  56      -8.015 -12.894   3.185  1.00 25.70           C  
ATOM    363  CD2 LEU A  56      -6.226 -12.945   1.434  1.00 25.21           C  
ATOM    364  N   GLY A  57      -9.711 -11.112  -2.412  1.00 28.58           N  
ATOM    365  CA  GLY A  57     -10.279 -11.485  -3.706  1.00 29.51           C  
ATOM    366  C   GLY A  57     -11.375 -12.541  -3.652  1.00 29.78           C  
ATOM    367  O   GLY A  57     -11.638 -13.213  -4.648  1.00 30.99           O  
ATOM    368  N   ARG A  58     -12.022 -12.696  -2.497  1.00 29.74           N  
ATOM    369  CA  ARG A  58     -13.093 -13.696  -2.356  1.00 28.85           C  
ATOM    370  C   ARG A  58     -14.438 -13.317  -2.981  1.00 27.87           C  
ATOM    371  O   ARG A  58     -15.295 -14.182  -3.146  1.00 28.87           O  
ATOM    372  CB  ARG A  58     -13.270 -14.146  -0.892  1.00 27.49           C  
ATOM    373  CG  ARG A  58     -12.558 -15.450  -0.560  1.00 29.31           C  
ATOM    374  CD  ARG A  58     -11.064 -15.369  -0.856  1.00 32.19           C  
ATOM    375  NE  ARG A  58     -10.358 -16.592  -0.474  1.00 33.76           N  
ATOM    376  CZ  ARG A  58      -9.037 -16.756  -0.535  1.00 34.78           C  
ATOM    377  NH1 ARG A  58      -8.246 -15.773  -0.962  1.00 33.73           N  
ATOM    378  NH2 ARG A  58      -8.506 -17.907  -0.152  1.00 36.57           N  
ATOM    379  N   SER A  59     -14.644 -12.045  -3.313  1.00 27.39           N  
ATOM    380  CA  SER A  59     -15.853 -11.680  -4.068  1.00 28.18           C  
ATOM    381  C   SER A  59     -15.782 -12.312  -5.455  1.00 28.69           C  
ATOM    382  O   SER A  59     -14.718 -12.321  -6.087  1.00 27.35           O  
ATOM    383  CB  SER A  59     -16.046 -10.165  -4.187  1.00 26.54           C  
ATOM    384  OG  SER A  59     -16.024  -9.559  -2.910  1.00 27.64           O  
ATOM    385  N   TYR A  60     -16.912 -12.835  -5.913  1.00 27.66           N  
ATOM    386  CA  TYR A  60     -16.949 -13.599  -7.155  1.00 29.08           C  
ATOM    387  C   TYR A  60     -16.845 -12.734  -8.399  1.00 29.41           C  
ATOM    388  O   TYR A  60     -16.390 -13.205  -9.431  1.00 29.16           O  
ATOM    389  CB  TYR A  60     -18.220 -14.448  -7.245  1.00 28.27           C  
ATOM    390  CG  TYR A  60     -18.277 -15.599  -6.277  1.00 30.28           C  
ATOM    391  CD1 TYR A  60     -18.087 -16.924  -6.710  1.00 31.25           C  
ATOM    392  CD2 TYR A  60     -18.530 -15.377  -4.919  1.00 30.01           C  
ATOM    393  CE1 TYR A  60     -18.153 -17.986  -5.811  1.00 31.65           C  
ATOM    394  CE2 TYR A  60     -18.593 -16.423  -4.022  1.00 31.31           C  
ATOM    395  CZ  TYR A  60     -18.411 -17.722  -4.463  1.00 32.01           C  
ATOM    396  OH  TYR A  60     -18.475 -18.733  -3.534  1.00 31.69           O  
ATOM    397  N   GLY A  61     -17.274 -11.479  -8.303  1.00 28.57           N  
ATOM    398  CA  GLY A  61     -17.362 -10.621  -9.474  1.00 30.02           C  
ATOM    399  C   GLY A  61     -16.228  -9.628  -9.576  1.00 29.98           C  
ATOM    400  O   GLY A  61     -15.094  -9.930  -9.227  1.00 30.37           O  
ATOM    401  N   ASP A  62     -16.562  -8.419 -10.003  1.00 30.03           N  
ATOM    402  CA  ASP A  62     -15.571  -7.442 -10.454  1.00 30.00           C  
ATOM    403  C   ASP A  62     -15.454  -6.200  -9.563  1.00 29.28           C  
ATOM    404  O   ASP A  62     -15.034  -5.137 -10.033  1.00 28.64           O  
ATOM    405  CB  ASP A  62     -15.912  -7.021 -11.895  1.00 29.19           C  
ATOM    406  CG  ASP A  62     -17.357  -6.540 -12.042  1.00 30.34           C  
ATOM    407  OD1 ASP A  62     -18.119  -6.594 -11.048  1.00 28.78           O  
ATOM    408  OD2 ASP A  62     -17.738  -6.111 -13.153  1.00 29.58           O  
ATOM    409  N   ASN A  63     -15.809  -6.316  -8.285  1.00 27.79           N  
ATOM    410  CA  ASN A  63     -15.749  -5.136  -7.413  1.00 27.84           C  
ATOM    411  C   ASN A  63     -14.358  -4.747  -6.909  1.00 27.76           C  
ATOM    412  O   ASN A  63     -14.175  -3.617  -6.441  1.00 27.49           O  
ATOM    413  CB  ASN A  63     -16.741  -5.229  -6.241  1.00 27.51           C  
ATOM    414  CG  ASN A  63     -16.550  -6.479  -5.402  1.00 28.16           C  
ATOM    415  OD1 ASN A  63     -15.679  -7.317  -5.682  1.00 31.15           O  
ATOM    416  ND2 ASN A  63     -17.374  -6.623  -4.370  1.00 26.07           N  
ATOM    417  N   ALA A  64     -13.396  -5.673  -7.007  1.00 28.55           N  
ATOM    418  CA  ALA A  64     -12.017  -5.460  -6.526  1.00 28.37           C  
ATOM    419  C   ALA A  64     -10.998  -5.443  -7.665  1.00 30.66           C  
ATOM    420  O   ALA A  64      -9.810  -5.787  -7.486  1.00 27.19           O  
ATOM    421  CB  ALA A  64     -11.635  -6.512  -5.488  1.00 28.02           C  
ATOM    422  N   GLN A  65     -11.466  -5.035  -8.836  1.00 30.86           N  
ATOM    423  CA  GLN A  65     -10.569  -4.816  -9.958  1.00 33.91           C  
ATOM    424  C   GLN A  65     -10.868  -3.501 -10.657  1.00 32.67           C  
ATOM    425  O   GLN A  65     -11.950  -2.931 -10.509  1.00 29.71           O  
ATOM    426  CB  GLN A  65     -10.601  -5.995 -10.923  1.00 34.29           C  
ATOM    427  CG  GLN A  65     -11.951  -6.257 -11.542  1.00 36.66           C  
ATOM    428  CD  GLN A  65     -11.992  -7.608 -12.207  1.00 38.46           C  
ATOM    429  OE1 GLN A  65     -12.196  -8.627 -11.549  1.00 39.72           O  
ATOM    430  NE2 GLN A  65     -11.791  -7.627 -13.520  1.00 39.43           N  
ATOM    431  N   ASN A  66      -9.892  -3.021 -11.414  1.00 31.55           N  
ATOM    432  CA  ASN A  66      -9.990  -1.712 -12.016  1.00 33.38           C  
ATOM    433  C   ASN A  66      -9.150  -1.658 -13.293  1.00 34.33           C  
ATOM    434  O   ASN A  66      -8.034  -1.131 -13.285  1.00 34.06           O  
ATOM    435  CB  ASN A  66      -9.544  -0.645 -11.013  1.00 32.81           C  
ATOM    436  CG  ASN A  66      -9.794   0.767 -11.506  1.00 34.94           C  
ATOM    437  OD1 ASN A  66     -10.612   0.990 -12.402  1.00 38.15           O  
ATOM    438  ND2 ASN A  66      -9.102   1.735 -10.909  1.00 32.95           N  
ATOM    439  N   GLY A  67      -9.708  -2.215 -14.371  1.00 33.88           N  
ATOM    440  CA  GLY A  67      -9.026  -2.330 -15.665  1.00 34.35           C  
ATOM    441  C   GLY A  67      -8.463  -1.015 -16.139  1.00 34.62           C  
ATOM    442  O   GLY A  67      -9.184  -0.021 -16.242  1.00 34.92           O  
ATOM    443  N   GLY A  68      -7.158  -1.007 -16.392  1.00 35.42           N  
ATOM    444  CA  GLY A  68      -6.454   0.191 -16.830  1.00 36.49           C  
ATOM    445  C   GLY A  68      -6.210   1.231 -15.758  1.00 37.44           C  
ATOM    446  O   GLY A  68      -5.921   2.386 -16.070  1.00 39.05           O  
ATOM    447  N   GLY A  69      -6.329   0.833 -14.493  1.00 37.90           N  
ATOM    448  CA  GLY A  69      -6.119   1.754 -13.382  1.00 37.08           C  
ATOM    449  C   GLY A  69      -5.341   1.127 -12.246  1.00 36.85           C  
ATOM    450  O   GLY A  69      -4.649   0.129 -12.437  1.00 36.40           O  
ATOM    451  N   LEU A  70      -5.470   1.708 -11.054  1.00 36.76           N  
ATOM    452  CA  LEU A  70      -4.734   1.234  -9.883  1.00 36.07           C  
ATOM    453  C   LEU A  70      -5.587   0.322  -8.988  1.00 36.58           C  
ATOM    454  O   LEU A  70      -6.762   0.610  -8.708  1.00 33.84           O  
ATOM    455  CB  LEU A  70      -4.175   2.422  -9.091  1.00 36.13           C  
ATOM    456  CG  LEU A  70      -3.311   2.182  -7.846  1.00 37.45           C  
ATOM    457  CD1 LEU A  70      -1.900   1.743  -8.211  1.00 38.42           C  
ATOM    458  CD2 LEU A  70      -3.260   3.434  -6.986  1.00 37.83           C  
ATOM    459  N   VAL A  71      -4.995  -0.800  -8.585  1.00 35.28           N  
ATOM    460  CA  VAL A  71      -5.560  -1.649  -7.538  1.00 34.58           C  
ATOM    461  C   VAL A  71      -4.591  -1.632  -6.363  1.00 35.03           C  
ATOM    462  O   VAL A  71      -3.385  -1.859  -6.538  1.00 35.26           O  
ATOM    463  CB  VAL A  71      -5.784  -3.101  -8.022  1.00 33.81           C  
ATOM    464  CG1 VAL A  71      -6.124  -4.022  -6.860  1.00 32.25           C  
ATOM    465  CG2 VAL A  71      -6.890  -3.150  -9.066  1.00 33.12           C  
ATOM    466  N   ILE A  72      -5.102  -1.355  -5.169  1.00 32.53           N  
ATOM    467  CA  ILE A  72      -4.258  -1.393  -3.980  1.00 32.71           C  
ATOM    468  C   ILE A  72      -4.537  -2.638  -3.142  1.00 33.74           C  
ATOM    469  O   ILE A  72      -5.601  -2.763  -2.514  1.00 31.88           O  
ATOM    470  CB  ILE A  72      -4.363  -0.100  -3.147  1.00 32.83           C  
ATOM    471  CG1 ILE A  72      -3.895   1.097  -3.981  1.00 33.21           C  
ATOM    472  CG2 ILE A  72      -3.531  -0.208  -1.869  1.00 33.09           C  
ATOM    473  CD1 ILE A  72      -4.339   2.443  -3.452  1.00 34.17           C  
ATOM    474  N   ASP A  73      -3.571  -3.560  -3.153  1.00 32.76           N  
ATOM    475  CA  ASP A  73      -3.654  -4.795  -2.383  1.00 33.40           C  
ATOM    476  C   ASP A  73      -3.451  -4.505  -0.890  1.00 33.45           C  
ATOM    477  O   ASP A  73      -2.359  -4.121  -0.463  1.00 30.87           O  
ATOM    478  CB  ASP A  73      -2.640  -5.822  -2.909  1.00 34.92           C  
ATOM    479  CG  ASP A  73      -2.551  -7.074  -2.043  1.00 36.99           C  
ATOM    480  OD1 ASP A  73      -3.336  -7.241  -1.088  1.00 34.33           O  
ATOM    481  OD2 ASP A  73      -1.671  -7.911  -2.321  1.00 40.06           O  
ATOM    482  N   MET A  74      -4.517  -4.697  -0.107  1.00 31.96           N  
ATOM    483  CA  MET A  74      -4.527  -4.289   1.295  1.00 31.27           C  
ATOM    484  C   MET A  74      -4.026  -5.358   2.260  1.00 30.54           C  
ATOM    485  O   MET A  74      -3.862  -5.082   3.454  1.00 30.72           O  
ATOM    486  CB  MET A  74      -5.941  -3.846   1.725  1.00 30.63           C  
ATOM    487  CG  MET A  74      -6.437  -2.558   1.087  1.00 30.42           C  
ATOM    488  SD  MET A  74      -5.353  -1.136   1.322  1.00 31.14           S  
ATOM    489  CE  MET A  74      -5.468  -0.821   3.083  1.00 28.58           C  
ATOM    490  N   THR A  75      -3.799  -6.569   1.754  1.00 29.45           N  
ATOM    491  CA  THR A  75      -3.388  -7.702   2.601  1.00 30.44           C  
ATOM    492  C   THR A  75      -2.106  -7.516   3.452  1.00 31.39           C  
ATOM    493  O   THR A  75      -2.001  -8.127   4.518  1.00 30.30           O  
ATOM    494  CB  THR A  75      -3.294  -9.035   1.817  1.00 31.33           C  
ATOM    495  OG1 THR A  75      -2.410  -8.873   0.706  1.00 31.58           O  
ATOM    496  CG2 THR A  75      -4.668  -9.487   1.308  1.00 30.93           C  
ATOM    497  N   PRO A  76      -1.134  -6.689   2.996  1.00 32.11           N  
ATOM    498  CA  PRO A  76       0.040  -6.451   3.858  1.00 33.00           C  
ATOM    499  C   PRO A  76      -0.229  -5.567   5.082  1.00 34.28           C  
ATOM    500  O   PRO A  76       0.564  -5.593   6.023  1.00 36.37           O  
ATOM    501  CB  PRO A  76       1.052  -5.753   2.924  1.00 32.64           C  
ATOM    502  CG  PRO A  76       0.548  -5.985   1.543  1.00 32.28           C  
ATOM    503  CD  PRO A  76      -0.940  -6.102   1.655  1.00 31.93           C  
ATOM    504  N   LEU A  77      -1.310  -4.783   5.076  1.00 32.90           N  
ATOM    505  CA  LEU A  77      -1.687  -4.016   6.272  1.00 33.03           C  
ATOM    506  C   LEU A  77      -2.520  -4.917   7.158  1.00 31.09           C  
ATOM    507  O   LEU A  77      -3.737  -4.874   7.097  1.00 30.56           O  
ATOM    508  CB  LEU A  77      -2.510  -2.780   5.907  1.00 34.89           C  
ATOM    509  CG  LEU A  77      -1.811  -1.444   5.717  1.00 38.31           C  
ATOM    510  CD1 LEU A  77      -1.040  -1.453   4.408  1.00 41.40           C  
ATOM    511  CD2 LEU A  77      -2.853  -0.340   5.721  1.00 37.00           C  
ATOM    512  N   ASN A  78      -1.861  -5.733   7.969  1.00 30.04           N  
ATOM    513  CA  ASN A  78      -2.526  -6.814   8.668  1.00 29.71           C  
ATOM    514  C   ASN A  78      -2.143  -6.879  10.147  1.00 28.99           C  
ATOM    515  O   ASN A  78      -2.114  -7.953  10.749  1.00 27.73           O  
ATOM    516  CB  ASN A  78      -2.226  -8.148   7.972  1.00 30.28           C  
ATOM    517  CG  ASN A  78      -0.786  -8.604   8.173  1.00 31.08           C  
ATOM    518  OD1 ASN A  78       0.092  -7.804   8.495  1.00 29.66           O  
ATOM    519  ND2 ASN A  78      -0.544  -9.898   7.994  1.00 31.07           N  
ATOM    520  N   THR A  79      -1.859  -5.719  10.720  1.00 27.98           N  
ATOM    521  CA  THR A  79      -1.505  -5.623  12.122  1.00 28.90           C  
ATOM    522  C   THR A  79      -2.759  -5.617  12.966  1.00 28.27           C  
ATOM    523  O   THR A  79      -3.694  -4.861  12.702  1.00 28.87           O  
ATOM    524  CB  THR A  79      -0.712  -4.335  12.411  1.00 28.49           C  
ATOM    525  OG1 THR A  79       0.452  -4.312  11.587  1.00 30.51           O  
ATOM    526  CG2 THR A  79      -0.288  -4.253  13.876  1.00 28.88           C  
ATOM    527  N   ILE A  80      -2.774  -6.487  13.963  1.00 27.88           N  
ATOM    528  CA  ILE A  80      -3.736  -6.396  15.037  1.00 27.06           C  
ATOM    529  C   ILE A  80      -3.120  -5.480  16.099  1.00 25.96           C  
ATOM    530  O   ILE A  80      -2.168  -5.862  16.772  1.00 24.98           O  
ATOM    531  CB  ILE A  80      -4.064  -7.789  15.616  1.00 27.22           C  
ATOM    532  CG1 ILE A  80      -4.752  -8.662  14.557  1.00 26.80           C  
ATOM    533  CG2 ILE A  80      -4.944  -7.671  16.856  1.00 27.02           C  
ATOM    534  CD1 ILE A  80      -4.778 -10.139  14.913  1.00 26.80           C  
ATOM    535  N   HIS A  81      -3.665  -4.269  16.240  1.00 26.29           N  
ATOM    536  CA  HIS A  81      -3.124  -3.305  17.199  1.00 26.40           C  
ATOM    537  C   HIS A  81      -3.451  -3.641  18.623  1.00 26.26           C  
ATOM    538  O   HIS A  81      -2.577  -3.601  19.497  1.00 25.09           O  
ATOM    539  CB  HIS A  81      -3.583  -1.898  16.848  1.00 27.51           C  
ATOM    540  CG  HIS A  81      -3.076  -1.430  15.515  1.00 28.53           C  
ATOM    541  ND1 HIS A  81      -3.797  -1.561  14.376  1.00 29.75           N  
ATOM    542  CD2 HIS A  81      -1.863  -0.856  15.154  1.00 27.24           C  
ATOM    543  CE1 HIS A  81      -3.084  -1.065  13.346  1.00 29.10           C  
ATOM    544  NE2 HIS A  81      -1.899  -0.640  13.823  1.00 28.63           N  
ATOM    545  N   SER A  82      -4.712  -3.977  18.887  1.00 25.75           N  
ATOM    546  CA  SER A  82      -5.085  -4.371  20.235  1.00 24.08           C  
ATOM    547  C   SER A  82      -6.376  -5.148  20.281  1.00 24.36           C  
ATOM    548  O   SER A  82      -7.216  -5.059  19.376  1.00 24.45           O  
ATOM    549  CB  SER A  82      -5.182  -3.147  21.167  1.00 25.35           C  
ATOM    550  OG  SER A  82      -6.332  -2.362  20.874  1.00 24.16           O  
ATOM    551  N   ILE A  83      -6.521  -5.907  21.365  1.00 23.43           N  
ATOM    552  CA  ILE A  83      -7.750  -6.590  21.694  1.00 23.13           C  
ATOM    553  C   ILE A  83      -7.971  -6.334  23.187  1.00 23.98           C  
ATOM    554  O   ILE A  83      -7.035  -6.415  23.988  1.00 24.37           O  
ATOM    555  CB  ILE A  83      -7.666  -8.108  21.394  1.00 22.89           C  
ATOM    556  CG1 ILE A  83      -7.474  -8.357  19.883  1.00 21.94           C  
ATOM    557  CG2 ILE A  83      -8.900  -8.836  21.924  1.00 21.74           C  
ATOM    558  CD1 ILE A  83      -7.571  -9.809  19.435  1.00 21.98           C  
ATOM    559  N   ASP A  84      -9.198  -6.018  23.569  1.00 25.43           N  
ATOM    560  CA  ASP A  84      -9.490  -5.737  24.977  1.00 25.99           C  
ATOM    561  C   ASP A  84     -10.706  -6.551  25.384  1.00 26.66           C  
ATOM    562  O   ASP A  84     -11.756  -6.388  24.792  1.00 26.99           O  
ATOM    563  CB  ASP A  84      -9.739  -4.234  25.151  1.00 26.80           C  
ATOM    564  CG  ASP A  84      -9.808  -3.805  26.609  1.00 27.69           C  
ATOM    565  OD1 ASP A  84     -10.623  -4.373  27.370  1.00 26.12           O  
ATOM    566  OD2 ASP A  84      -9.042  -2.889  26.980  1.00 28.63           O  
ATOM    567  N   ALA A  85     -10.556  -7.422  26.382  1.00 27.58           N  
ATOM    568  CA  ALA A  85     -11.640  -8.304  26.837  1.00 30.01           C  
ATOM    569  C   ALA A  85     -12.717  -7.552  27.615  1.00 30.83           C  
ATOM    570  O   ALA A  85     -13.876  -7.962  27.618  1.00 32.47           O  
ATOM    571  CB  ALA A  85     -11.097  -9.445  27.690  1.00 28.77           C  
ATOM    572  N   ASP A  86     -12.317  -6.465  28.273  1.00 31.07           N  
ATOM    573  CA  ASP A  86     -13.218  -5.680  29.107  1.00 33.26           C  
ATOM    574  C   ASP A  86     -14.151  -4.804  28.278  1.00 31.58           C  
ATOM    575  O   ASP A  86     -15.345  -4.774  28.527  1.00 30.41           O  
ATOM    576  CB  ASP A  86     -12.431  -4.818  30.109  1.00 34.65           C  
ATOM    577  CG  ASP A  86     -11.514  -5.644  30.995  1.00 36.51           C  
ATOM    578  OD1 ASP A  86     -11.960  -6.686  31.521  1.00 37.35           O  
ATOM    579  OD2 ASP A  86     -10.343  -5.242  31.166  1.00 36.38           O  
ATOM    580  N   THR A  87     -13.598  -4.086  27.305  1.00 30.01           N  
ATOM    581  CA  THR A  87     -14.409  -3.288  26.390  1.00 29.15           C  
ATOM    582  C   THR A  87     -14.943  -4.126  25.211  1.00 28.35           C  
ATOM    583  O   THR A  87     -15.827  -3.674  24.486  1.00 28.25           O  
ATOM    584  CB  THR A  87     -13.609  -2.100  25.834  1.00 29.84           C  
ATOM    585  OG1 THR A  87     -12.605  -2.594  24.940  1.00 26.88           O  
ATOM    586  CG2 THR A  87     -12.949  -1.312  26.971  1.00 29.79           C  
ATOM    587  N   LYS A  88     -14.395  -5.331  25.025  1.00 26.52           N  
ATOM    588  CA  LYS A  88     -14.740  -6.220  23.899  1.00 27.42           C  
ATOM    589  C   LYS A  88     -14.370  -5.674  22.518  1.00 26.49           C  
ATOM    590  O   LYS A  88     -14.850  -6.182  21.496  1.00 25.81           O  
ATOM    591  CB  LYS A  88     -16.219  -6.640  23.926  1.00 29.05           C  
ATOM    592  CG  LYS A  88     -16.635  -7.332  25.217  1.00 32.03           C  
ATOM    593  CD  LYS A  88     -18.136  -7.507  25.279  1.00 35.11           C  
ATOM    594  CE  LYS A  88     -18.825  -6.263  25.814  1.00 38.13           C  
ATOM    595  NZ  LYS A  88     -20.298  -6.472  25.810  1.00 41.03           N  
ATOM    596  N   LEU A  89     -13.508  -4.656  22.493  1.00 26.10           N  
ATOM    597  CA  LEU A  89     -13.108  -4.013  21.241  1.00 25.42           C  
ATOM    598  C   LEU A  89     -11.821  -4.594  20.685  1.00 25.00           C  
ATOM    599  O   LEU A  89     -10.906  -4.915  21.441  1.00 25.03           O  
ATOM    600  CB  LEU A  89     -12.932  -2.502  21.429  1.00 25.84           C  
ATOM    601  CG  LEU A  89     -14.130  -1.701  21.962  1.00 26.51           C  
ATOM    602  CD1 LEU A  89     -13.762  -0.226  22.044  1.00 26.95           C  
ATOM    603  CD2 LEU A  89     -15.368  -1.913  21.099  1.00 26.93           C  
ATOM    604  N   VAL A  90     -11.761  -4.720  19.360  1.00 23.72           N  
ATOM    605  CA  VAL A  90     -10.502  -5.014  18.674  1.00 23.90           C  
ATOM    606  C   VAL A  90     -10.160  -3.855  17.734  1.00 23.80           C  
ATOM    607  O   VAL A  90     -11.043  -3.335  17.050  1.00 25.01           O  
ATOM    608  CB  VAL A  90     -10.557  -6.353  17.891  1.00 24.12           C  
ATOM    609  CG1 VAL A  90     -10.822  -7.520  18.827  1.00 23.47           C  
ATOM    610  CG2 VAL A  90     -11.621  -6.320  16.798  1.00 23.94           C  
ATOM    611  N   ASP A  91      -8.889  -3.461  17.700  1.00 24.32           N  
ATOM    612  CA  ASP A  91      -8.404  -2.390  16.825  1.00 25.71           C  
ATOM    613  C   ASP A  91      -7.440  -2.995  15.814  1.00 26.49           C  
ATOM    614  O   ASP A  91      -6.338  -3.392  16.174  1.00 26.79           O  
ATOM    615  CB  ASP A  91      -7.697  -1.311  17.664  1.00 25.58           C  
ATOM    616  CG  ASP A  91      -7.098  -0.185  16.822  1.00 25.95           C  
ATOM    617  OD1 ASP A  91      -7.421  -0.052  15.623  1.00 26.11           O  
ATOM    618  OD2 ASP A  91      -6.289   0.585  17.377  1.00 27.40           O  
ATOM    619  N   ILE A  92      -7.859  -3.087  14.553  1.00 27.03           N  
ATOM    620  CA  ILE A  92      -7.079  -3.828  13.553  1.00 27.08           C  
ATOM    621  C   ILE A  92      -7.021  -3.120  12.206  1.00 27.79           C  
ATOM    622  O   ILE A  92      -7.971  -2.423  11.825  1.00 27.64           O  
ATOM    623  CB  ILE A  92      -7.571  -5.302  13.346  1.00 27.43           C  
ATOM    624  CG1 ILE A  92      -8.829  -5.393  12.443  1.00 28.64           C  
ATOM    625  CG2 ILE A  92      -7.693  -6.068  14.667  1.00 26.08           C  
ATOM    626  CD1 ILE A  92     -10.131  -4.862  13.026  1.00 27.17           C  
ATOM    627  N   ASP A  93      -5.897  -3.301  11.506  1.00 27.31           N  
ATOM    628  CA  ASP A  93      -5.733  -2.857  10.118  1.00 27.89           C  
ATOM    629  C   ASP A  93      -6.753  -3.566   9.245  1.00 25.87           C  
ATOM    630  O   ASP A  93      -7.141  -4.694   9.541  1.00 25.66           O  
ATOM    631  CB  ASP A  93      -4.336  -3.225   9.584  1.00 27.63           C  
ATOM    632  CG  ASP A  93      -3.233  -2.388  10.172  1.00 30.01           C  
ATOM    633  OD1 ASP A  93      -3.521  -1.334  10.775  1.00 29.10           O  
ATOM    634  OD2 ASP A  93      -2.049  -2.787  10.019  1.00 32.75           O  
ATOM    635  N   ALA A  94      -7.155  -2.912   8.158  1.00 25.74           N  
ATOM    636  CA  ALA A  94      -8.187  -3.446   7.260  1.00 25.19           C  
ATOM    637  C   ALA A  94      -7.770  -4.731   6.529  1.00 24.83           C  
ATOM    638  O   ALA A  94      -8.626  -5.496   6.076  1.00 23.24           O  
ATOM    639  CB  ALA A  94      -8.615  -2.385   6.263  1.00 26.06           C  
ATOM    640  N   GLY A  95      -6.466  -4.976   6.421  1.00 24.84           N  
ATOM    641  CA  GLY A  95      -5.971  -6.192   5.767  1.00 25.26           C  
ATOM    642  C   GLY A  95      -5.970  -7.452   6.619  1.00 25.69           C  
ATOM    643  O   GLY A  95      -5.716  -8.555   6.119  1.00 25.86           O  
ATOM    644  N   VAL A  96      -6.210  -7.293   7.915  1.00 25.06           N  
ATOM    645  CA  VAL A  96      -6.395  -8.430   8.807  1.00 24.90           C  
ATOM    646  C   VAL A  96      -7.557  -9.287   8.275  1.00 25.90           C  
ATOM    647  O   VAL A  96      -8.599  -8.761   7.874  1.00 25.90           O  
ATOM    648  CB  VAL A  96      -6.675  -7.950  10.254  1.00 25.19           C  
ATOM    649  CG1 VAL A  96      -7.159  -9.084  11.147  1.00 23.60           C  
ATOM    650  CG2 VAL A  96      -5.434  -7.298  10.856  1.00 24.68           C  
ATOM    651  N   ASN A  97      -7.381 -10.604   8.244  1.00 25.35           N  
ATOM    652  CA  ASN A  97      -8.468 -11.467   7.812  1.00 24.11           C  
ATOM    653  C   ASN A  97      -9.177 -12.093   9.011  1.00 23.84           C  
ATOM    654  O   ASN A  97      -8.646 -12.101  10.111  1.00 22.68           O  
ATOM    655  CB  ASN A  97      -7.975 -12.536   6.839  1.00 25.17           C  
ATOM    656  CG  ASN A  97      -7.187 -13.637   7.525  1.00 25.78           C  
ATOM    657  OD1 ASN A  97      -7.735 -14.419   8.300  1.00 27.48           O  
ATOM    658  ND2 ASN A  97      -5.903 -13.722   7.217  1.00 24.94           N  
ATOM    659  N   LEU A  98     -10.362 -12.646   8.775  1.00 24.72           N  
ATOM    660  CA  LEU A  98     -11.249 -13.079   9.860  1.00 25.57           C  
ATOM    661  C   LEU A  98     -10.815 -14.371  10.557  1.00 26.12           C  
ATOM    662  O   LEU A  98     -11.184 -14.613  11.708  1.00 25.10           O  
ATOM    663  CB  LEU A  98     -12.694 -13.161   9.358  1.00 24.13           C  
ATOM    664  CG  LEU A  98     -13.353 -11.831   8.954  1.00 23.36           C  
ATOM    665  CD1 LEU A  98     -14.798 -12.082   8.543  1.00 23.19           C  
ATOM    666  CD2 LEU A  98     -13.280 -10.777  10.056  1.00 23.47           C  
ATOM    667  N   ASP A  99     -10.030 -15.191   9.859  1.00 26.49           N  
ATOM    668  CA  ASP A  99      -9.410 -16.369  10.455  1.00 26.85           C  
ATOM    669  C   ASP A  99      -8.332 -15.952  11.459  1.00 25.76           C  
ATOM    670  O   ASP A  99      -8.336 -16.401  12.603  1.00 24.69           O  
ATOM    671  CB  ASP A  99      -8.799 -17.256   9.362  1.00 30.73           C  
ATOM    672  CG  ASP A  99      -8.339 -18.610   9.890  1.00 34.56           C  
ATOM    673  OD1 ASP A  99      -9.146 -19.313  10.543  1.00 35.00           O  
ATOM    674  OD2 ASP A  99      -7.165 -18.970   9.642  1.00 37.72           O  
ATOM    675  N   GLN A 100      -7.408 -15.100  11.010  1.00 25.42           N  
ATOM    676  CA  GLN A 100      -6.408 -14.470  11.871  1.00 25.92           C  
ATOM    677  C   GLN A 100      -7.050 -13.819  13.112  1.00 25.80           C  
ATOM    678  O   GLN A 100      -6.617 -14.051  14.251  1.00 26.17           O  
ATOM    679  CB  GLN A 100      -5.637 -13.429  11.055  1.00 26.25           C  
ATOM    680  CG  GLN A 100      -4.608 -12.599  11.813  1.00 26.13           C  
ATOM    681  CD  GLN A 100      -4.134 -11.405  10.992  1.00 26.17           C  
ATOM    682  OE1 GLN A 100      -4.617 -11.168   9.874  1.00 26.56           O  
ATOM    683  NE2 GLN A 100      -3.187 -10.652  11.535  1.00 25.46           N  
ATOM    684  N   LEU A 101      -8.100 -13.033  12.881  1.00 25.11           N  
ATOM    685  CA  LEU A 101      -8.814 -12.344  13.964  1.00 23.98           C  
ATOM    686  C   LEU A 101      -9.477 -13.323  14.936  1.00 24.69           C  
ATOM    687  O   LEU A 101      -9.320 -13.196  16.152  1.00 25.25           O  
ATOM    688  CB  LEU A 101      -9.836 -11.359  13.395  1.00 21.91           C  
ATOM    689  CG  LEU A 101     -10.562 -10.406  14.359  1.00 21.79           C  
ATOM    690  CD1 LEU A 101      -9.608  -9.750  15.346  1.00 19.92           C  
ATOM    691  CD2 LEU A 101     -11.322  -9.345  13.568  1.00 22.46           C  
ATOM    692  N   MET A 102     -10.195 -14.310  14.405  1.00 26.30           N  
ATOM    693  CA  MET A 102     -10.806 -15.341  15.248  1.00 27.22           C  
ATOM    694  C   MET A 102      -9.801 -16.002  16.190  1.00 26.73           C  
ATOM    695  O   MET A 102     -10.058 -16.118  17.391  1.00 25.23           O  
ATOM    696  CB  MET A 102     -11.509 -16.417  14.408  1.00 29.92           C  
ATOM    697  CG  MET A 102     -11.944 -17.631  15.236  1.00 32.49           C  
ATOM    698  SD  MET A 102     -12.622 -18.991  14.265  1.00 40.30           S  
ATOM    699  CE  MET A 102     -14.244 -18.349  13.889  1.00 38.49           C  
ATOM    700  N   LYS A 103      -8.664 -16.419  15.634  1.00 27.39           N  
ATOM    701  CA  LYS A 103      -7.589 -17.069  16.389  1.00 28.66           C  
ATOM    702  C   LYS A 103      -6.957 -16.165  17.444  1.00 27.13           C  
ATOM    703  O   LYS A 103      -6.679 -16.616  18.556  1.00 28.53           O  
ATOM    704  CB  LYS A 103      -6.508 -17.606  15.447  1.00 29.91           C  
ATOM    705  CG  LYS A 103      -7.005 -18.691  14.505  1.00 35.35           C  
ATOM    706  CD  LYS A 103      -5.894 -19.211  13.596  1.00 38.92           C  
ATOM    707  CE  LYS A 103      -6.420 -20.191  12.550  1.00 42.06           C  
ATOM    708  NZ  LYS A 103      -7.246 -21.291  13.131  1.00 45.02           N  
ATOM    709  N   ALA A 104      -6.735 -14.899  17.101  1.00 26.09           N  
ATOM    710  CA  ALA A 104      -6.189 -13.923  18.047  1.00 25.30           C  
ATOM    711  C   ALA A 104      -7.168 -13.574  19.169  1.00 25.14           C  
ATOM    712  O   ALA A 104      -6.749 -13.359  20.303  1.00 26.61           O  
ATOM    713  CB  ALA A 104      -5.757 -12.655  17.320  1.00 25.36           C  
ATOM    714  N   ALA A 105      -8.463 -13.536  18.861  1.00 24.63           N  
ATOM    715  CA  ALA A 105      -9.487 -13.104  19.843  1.00 24.83           C  
ATOM    716  C   ALA A 105      -9.975 -14.180  20.837  1.00 25.28           C  
ATOM    717  O   ALA A 105     -10.402 -13.860  21.958  1.00 26.79           O  
ATOM    718  CB  ALA A 105     -10.665 -12.471  19.124  1.00 24.50           C  
ATOM    719  N   LEU A 106      -9.927 -15.442  20.425  1.00 25.47           N  
ATOM    720  CA  LEU A 106     -10.389 -16.559  21.261  1.00 26.85           C  
ATOM    721  C   LEU A 106      -9.793 -16.603  22.681  1.00 27.66           C  
ATOM    722  O   LEU A 106     -10.540 -16.783  23.646  1.00 28.41           O  
ATOM    723  CB  LEU A 106     -10.224 -17.921  20.544  1.00 26.77           C  
ATOM    724  CG  LEU A 106     -11.402 -18.406  19.685  1.00 28.14           C  
ATOM    725  CD1 LEU A 106     -11.079 -19.741  19.027  1.00 29.12           C  
ATOM    726  CD2 LEU A 106     -12.684 -18.533  20.507  1.00 25.64           C  
ATOM    727  N   PRO A 107      -8.467 -16.411  22.828  1.00 28.11           N  
ATOM    728  CA  PRO A 107      -7.936 -16.395  24.203  1.00 28.83           C  
ATOM    729  C   PRO A 107      -8.518 -15.318  25.128  1.00 29.05           C  
ATOM    730  O   PRO A 107      -8.312 -15.396  26.337  1.00 31.16           O  
ATOM    731  CB  PRO A 107      -6.446 -16.146  23.993  1.00 28.70           C  
ATOM    732  CG  PRO A 107      -6.170 -16.731  22.646  1.00 29.74           C  
ATOM    733  CD  PRO A 107      -7.378 -16.392  21.831  1.00 28.99           C  
ATOM    734  N   PHE A 108      -9.199 -14.316  24.574  1.00 28.10           N  
ATOM    735  CA  PHE A 108      -9.812 -13.244  25.376  1.00 27.69           C  
ATOM    736  C   PHE A 108     -11.280 -13.545  25.675  1.00 27.87           C  
ATOM    737  O   PHE A 108     -11.988 -12.712  26.260  1.00 27.13           O  
ATOM    738  CB  PHE A 108      -9.734 -11.894  24.654  1.00 26.69           C  
ATOM    739  CG  PHE A 108      -8.334 -11.458  24.304  1.00 25.91           C  
ATOM    740  CD1 PHE A 108      -7.691 -10.468  25.052  1.00 26.30           C  
ATOM    741  CD2 PHE A 108      -7.657 -12.029  23.228  1.00 25.66           C  
ATOM    742  CE1 PHE A 108      -6.407 -10.051  24.729  1.00 25.50           C  
ATOM    743  CE2 PHE A 108      -6.377 -11.614  22.896  1.00 24.07           C  
ATOM    744  CZ  PHE A 108      -5.750 -10.629  23.654  1.00 24.76           C  
ATOM    745  N   GLY A 109     -11.745 -14.708  25.230  1.00 27.60           N  
ATOM    746  CA  GLY A 109     -13.174 -15.030  25.290  1.00 28.44           C  
ATOM    747  C   GLY A 109     -13.978 -14.120  24.375  1.00 27.88           C  
ATOM    748  O   GLY A 109     -15.078 -13.690  24.718  1.00 26.31           O  
ATOM    749  N   LEU A 110     -13.419 -13.813  23.207  1.00 27.21           N  
ATOM    750  CA  LEU A 110     -14.110 -12.958  22.228  1.00 26.31           C  
ATOM    751  C   LEU A 110     -14.369 -13.693  20.918  1.00 26.60           C  
ATOM    752  O   LEU A 110     -13.497 -14.425  20.426  1.00 26.96           O  
ATOM    753  CB  LEU A 110     -13.322 -11.672  21.968  1.00 25.31           C  
ATOM    754  CG  LEU A 110     -13.148 -10.717  23.152  1.00 26.91           C  
ATOM    755  CD1 LEU A 110     -12.407  -9.470  22.684  1.00 27.89           C  
ATOM    756  CD2 LEU A 110     -14.485 -10.333  23.772  1.00 25.31           C  
ATOM    757  N   TRP A 111     -15.558 -13.467  20.357  1.00 24.65           N  
ATOM    758  CA  TRP A 111     -16.018 -14.127  19.147  1.00 24.68           C  
ATOM    759  C   TRP A 111     -16.282 -13.115  18.054  1.00 24.48           C  
ATOM    760  O   TRP A 111     -17.000 -12.130  18.286  1.00 24.35           O  
ATOM    761  CB  TRP A 111     -17.283 -14.948  19.470  1.00 24.01           C  
ATOM    762  CG  TRP A 111     -17.655 -15.921  18.377  1.00 24.01           C  
ATOM    763  CD1 TRP A 111     -18.656 -15.784  17.426  1.00 22.86           C  
ATOM    764  CD2 TRP A 111     -17.005 -17.208  18.063  1.00 23.77           C  
ATOM    765  NE1 TRP A 111     -18.675 -16.860  16.581  1.00 23.69           N  
ATOM    766  CE2 TRP A 111     -17.714 -17.749  16.901  1.00 23.55           C  
ATOM    767  CE3 TRP A 111     -15.952 -17.940  18.615  1.00 24.45           C  
ATOM    768  CZ2 TRP A 111     -17.369 -18.974  16.323  1.00 23.79           C  
ATOM    769  CZ3 TRP A 111     -15.614 -19.172  18.028  1.00 23.70           C  
ATOM    770  CH2 TRP A 111     -16.314 -19.677  16.913  1.00 23.38           C  
ATOM    771  N   VAL A 112     -15.689 -13.329  16.867  1.00 23.88           N  
ATOM    772  CA  VAL A 112     -15.977 -12.506  15.666  1.00 24.73           C  
ATOM    773  C   VAL A 112     -17.498 -12.455  15.477  1.00 25.35           C  
ATOM    774  O   VAL A 112     -18.136 -13.502  15.349  1.00 26.08           O  
ATOM    775  CB  VAL A 112     -15.285 -13.062  14.386  1.00 24.32           C  
ATOM    776  CG1 VAL A 112     -15.689 -12.272  13.144  1.00 24.69           C  
ATOM    777  CG2 VAL A 112     -13.764 -13.040  14.528  1.00 24.34           C  
ATOM    778  N   PRO A 113     -18.093 -11.247  15.508  1.00 24.97           N  
ATOM    779  CA  PRO A 113     -19.573 -11.173  15.576  1.00 24.64           C  
ATOM    780  C   PRO A 113     -20.317 -11.624  14.309  1.00 23.81           C  
ATOM    781  O   PRO A 113     -21.449 -12.101  14.394  1.00 23.22           O  
ATOM    782  CB  PRO A 113     -19.837  -9.689  15.889  1.00 24.92           C  
ATOM    783  CG  PRO A 113     -18.620  -8.981  15.352  1.00 25.46           C  
ATOM    784  CD  PRO A 113     -17.477  -9.916  15.652  1.00 25.18           C  
ATOM    785  N   VAL A 114     -19.693 -11.493  13.141  1.00 23.28           N  
ATOM    786  CA  VAL A 114     -20.301 -11.968  11.896  1.00 22.35           C  
ATOM    787  C   VAL A 114     -19.258 -12.746  11.087  1.00 24.59           C  
ATOM    788  O   VAL A 114     -18.226 -12.182  10.693  1.00 22.57           O  
ATOM    789  CB  VAL A 114     -20.893 -10.795  11.074  1.00 22.61           C  
ATOM    790  CG1 VAL A 114     -21.435 -11.270   9.737  1.00 21.92           C  
ATOM    791  CG2 VAL A 114     -21.998 -10.073  11.856  1.00 21.96           C  
ATOM    792  N   LEU A 115     -19.519 -14.040  10.871  1.00 24.78           N  
ATOM    793  CA  LEU A 115     -18.646 -14.894  10.060  1.00 26.01           C  
ATOM    794  C   LEU A 115     -19.353 -15.384   8.796  1.00 26.30           C  
ATOM    795  O   LEU A 115     -20.459 -15.922   8.865  1.00 28.18           O  
ATOM    796  CB  LEU A 115     -18.138 -16.097  10.865  1.00 26.21           C  
ATOM    797  CG  LEU A 115     -17.210 -15.818  12.047  1.00 28.04           C  
ATOM    798  CD1 LEU A 115     -17.295 -16.968  13.040  1.00 27.74           C  
ATOM    799  CD2 LEU A 115     -15.775 -15.584  11.591  1.00 28.22           C  
ATOM    800  N   PRO A 116     -18.721 -15.190   7.635  1.00 25.80           N  
ATOM    801  CA  PRO A 116     -19.234 -15.699   6.371  1.00 25.65           C  
ATOM    802  C   PRO A 116     -18.837 -17.168   6.208  1.00 27.28           C  
ATOM    803  O   PRO A 116     -18.155 -17.718   7.074  1.00 28.52           O  
ATOM    804  CB  PRO A 116     -18.500 -14.837   5.341  1.00 25.13           C  
ATOM    805  CG  PRO A 116     -17.171 -14.581   5.978  1.00 24.98           C  
ATOM    806  CD  PRO A 116     -17.446 -14.465   7.459  1.00 26.07           C  
ATOM    807  N   GLY A 117     -19.237 -17.782   5.099  1.00 28.76           N  
ATOM    808  CA  GLY A 117     -18.985 -19.209   4.848  1.00 31.94           C  
ATOM    809  C   GLY A 117     -17.546 -19.586   4.521  1.00 33.29           C  
ATOM    810  O   GLY A 117     -17.247 -20.754   4.314  1.00 36.70           O  
ATOM    811  N   THR A 118     -16.660 -18.600   4.469  1.00 34.09           N  
ATOM    812  CA  THR A 118     -15.217 -18.837   4.359  1.00 35.38           C  
ATOM    813  C   THR A 118     -14.473 -17.861   5.264  1.00 36.39           C  
ATOM    814  O   THR A 118     -14.888 -16.710   5.407  1.00 37.86           O  
ATOM    815  CB  THR A 118     -14.707 -18.691   2.913  1.00 36.40           C  
ATOM    816  OG1 THR A 118     -13.292 -18.941   2.889  1.00 38.96           O  
ATOM    817  CG2 THR A 118     -14.973 -17.284   2.366  1.00 33.89           C  
ATOM    818  N   ARG A 119     -13.375 -18.299   5.872  1.00 37.64           N  
ATOM    819  CA  ARG A 119     -12.635 -17.414   6.788  1.00 39.09           C  
ATOM    820  C   ARG A 119     -11.572 -16.538   6.133  1.00 37.55           C  
ATOM    821  O   ARG A 119     -11.004 -15.653   6.787  1.00 35.69           O  
ATOM    822  CB  ARG A 119     -12.050 -18.198   7.960  1.00 43.79           C  
ATOM    823  CG  ARG A 119     -12.786 -17.959   9.274  1.00 48.80           C  
ATOM    824  CD  ARG A 119     -13.209 -19.259   9.951  1.00 53.04           C  
ATOM    825  NE  ARG A 119     -12.102 -20.090  10.448  1.00 56.20           N  
ATOM    826  CZ  ARG A 119     -11.539 -21.103   9.781  1.00 57.52           C  
ATOM    827  NH1 ARG A 119     -11.937 -21.417   8.551  1.00 58.99           N  
ATOM    828  NH2 ARG A 119     -10.555 -21.798  10.341  1.00 54.42           N  
ATOM    829  N   GLN A 120     -11.318 -16.759   4.846  1.00 33.45           N  
ATOM    830  CA  GLN A 120     -10.329 -15.957   4.133  1.00 33.48           C  
ATOM    831  C   GLN A 120     -10.940 -14.685   3.546  1.00 30.61           C  
ATOM    832  O   GLN A 120     -10.997 -14.516   2.329  1.00 30.67           O  
ATOM    833  CB  GLN A 120      -9.617 -16.783   3.045  1.00 35.54           C  
ATOM    834  CG  GLN A 120      -8.837 -17.990   3.557  1.00 36.99           C  
ATOM    835  CD  GLN A 120      -7.789 -17.633   4.598  1.00 41.19           C  
ATOM    836  OE1 GLN A 120      -6.983 -16.712   4.412  1.00 43.57           O  
ATOM    837  NE2 GLN A 120      -7.795 -18.362   5.704  1.00 42.03           N  
ATOM    838  N   VAL A 121     -11.424 -13.791   4.403  1.00 30.10           N  
ATOM    839  CA  VAL A 121     -11.839 -12.459   3.920  1.00 28.18           C  
ATOM    840  C   VAL A 121     -11.253 -11.391   4.828  1.00 26.64           C  
ATOM    841  O   VAL A 121     -11.089 -11.623   6.035  1.00 25.51           O  
ATOM    842  CB  VAL A 121     -13.375 -12.285   3.727  1.00 28.61           C  
ATOM    843  CG1 VAL A 121     -14.039 -13.527   3.140  1.00 26.92           C  
ATOM    844  CG2 VAL A 121     -14.071 -11.845   5.008  1.00 30.44           C  
ATOM    845  N   THR A 122     -10.898 -10.244   4.243  1.00 25.41           N  
ATOM    846  CA  THR A 122     -10.318  -9.150   5.017  1.00 23.61           C  
ATOM    847  C   THR A 122     -11.412  -8.410   5.782  1.00 23.58           C  
ATOM    848  O   THR A 122     -12.601  -8.519   5.460  1.00 23.70           O  
ATOM    849  CB  THR A 122      -9.530  -8.147   4.150  1.00 23.74           C  
ATOM    850  OG1 THR A 122     -10.388  -7.595   3.147  1.00 23.60           O  
ATOM    851  CG2 THR A 122      -8.305  -8.841   3.492  1.00 23.29           C  
ATOM    852  N   VAL A 123     -10.990  -7.671   6.801  1.00 23.23           N  
ATOM    853  CA  VAL A 123     -11.869  -6.782   7.540  1.00 22.12           C  
ATOM    854  C   VAL A 123     -12.394  -5.716   6.595  1.00 21.25           C  
ATOM    855  O   VAL A 123     -13.574  -5.401   6.604  1.00 19.70           O  
ATOM    856  CB  VAL A 123     -11.133  -6.176   8.751  1.00 22.89           C  
ATOM    857  CG1 VAL A 123     -11.774  -4.869   9.217  1.00 22.12           C  
ATOM    858  CG2 VAL A 123     -11.065  -7.207   9.881  1.00 22.84           C  
ATOM    859  N   GLY A 124     -11.529  -5.168   5.743  1.00 19.81           N  
ATOM    860  CA  GLY A 124     -12.010  -4.203   4.751  1.00 19.60           C  
ATOM    861  C   GLY A 124     -13.044  -4.780   3.783  1.00 19.89           C  
ATOM    862  O   GLY A 124     -14.010  -4.104   3.394  1.00 20.34           O  
ATOM    863  N   GLY A 125     -12.849  -6.034   3.377  1.00 19.50           N  
ATOM    864  CA  GLY A 125     -13.787  -6.672   2.443  1.00 19.50           C  
ATOM    865  C   GLY A 125     -15.094  -6.986   3.173  1.00 20.09           C  
ATOM    866  O   GLY A 125     -16.185  -6.903   2.599  1.00 19.55           O  
ATOM    867  N   ALA A 126     -14.963  -7.330   4.448  1.00 19.41           N  
ATOM    868  CA  ALA A 126     -16.118  -7.610   5.299  1.00 19.81           C  
ATOM    869  C   ALA A 126     -16.972  -6.348   5.462  1.00 19.38           C  
ATOM    870  O   ALA A 126     -18.192  -6.406   5.356  1.00 20.67           O  
ATOM    871  CB  ALA A 126     -15.653  -8.150   6.637  1.00 18.97           C  
ATOM    872  N   ILE A 127     -16.328  -5.199   5.643  1.00 19.95           N  
ATOM    873  CA  ILE A 127     -17.055  -3.922   5.775  1.00 20.02           C  
ATOM    874  C   ILE A 127     -17.644  -3.474   4.438  1.00 20.06           C  
ATOM    875  O   ILE A 127     -18.820  -3.109   4.348  1.00 18.62           O  
ATOM    876  CB  ILE A 127     -16.171  -2.797   6.382  1.00 19.24           C  
ATOM    877  CG1 ILE A 127     -15.686  -3.192   7.780  1.00 18.75           C  
ATOM    878  CG2 ILE A 127     -16.917  -1.456   6.389  1.00 19.46           C  
ATOM    879  CD1 ILE A 127     -14.605  -2.295   8.364  1.00 18.32           C  
ATOM    880  N   ALA A 128     -16.826  -3.535   3.395  1.00 21.04           N  
ATOM    881  CA  ALA A 128     -17.209  -3.005   2.089  1.00 21.12           C  
ATOM    882  C   ALA A 128     -18.363  -3.749   1.469  1.00 21.05           C  
ATOM    883  O   ALA A 128     -19.068  -3.185   0.627  1.00 21.47           O  
ATOM    884  CB  ALA A 128     -16.021  -2.997   1.135  1.00 21.70           C  
ATOM    885  N   CYS A 129     -18.550  -5.014   1.851  1.00 19.97           N  
ATOM    886  CA  CYS A 129     -19.657  -5.783   1.305  1.00 20.48           C  
ATOM    887  C   CYS A 129     -20.756  -5.970   2.341  1.00 19.53           C  
ATOM    888  O   CYS A 129     -21.761  -6.592   2.033  1.00 19.40           O  
ATOM    889  CB  CYS A 129     -19.203  -7.136   0.740  1.00 21.56           C  
ATOM    890  SG  CYS A 129     -18.315  -7.001  -0.844  1.00 24.96           S  
ATOM    891  N   ASP A 130     -20.530  -5.419   3.540  1.00 19.21           N  
ATOM    892  CA  ASP A 130     -21.429  -5.513   4.698  1.00 20.35           C  
ATOM    893  C   ASP A 130     -21.878  -6.987   4.835  1.00 20.26           C  
ATOM    894  O   ASP A 130     -23.065  -7.312   4.782  1.00 20.52           O  
ATOM    895  CB  ASP A 130     -22.597  -4.516   4.571  1.00 19.49           C  
ATOM    896  CG  ASP A 130     -23.476  -4.445   5.842  1.00 19.95           C  
ATOM    897  OD1 ASP A 130     -23.042  -4.897   6.922  1.00 19.22           O  
ATOM    898  OD2 ASP A 130     -24.611  -3.929   5.751  1.00 21.27           O  
ATOM    899  N   ILE A 131     -20.888  -7.867   4.968  1.00 20.56           N  
ATOM    900  CA  ILE A 131     -21.106  -9.301   4.809  1.00 21.08           C  
ATOM    901  C   ILE A 131     -22.046  -9.833   5.886  1.00 20.96           C  
ATOM    902  O   ILE A 131     -22.175  -9.245   6.950  1.00 20.63           O  
ATOM    903  CB  ILE A 131     -19.795 -10.112   4.854  1.00 20.81           C  
ATOM    904  CG1 ILE A 131     -19.173 -10.033   6.253  1.00 21.21           C  
ATOM    905  CG2 ILE A 131     -18.833  -9.654   3.755  1.00 19.79           C  
ATOM    906  CD1 ILE A 131     -18.070 -11.037   6.479  1.00 21.79           C  
ATOM    907  N   HIS A 132     -22.658 -10.974   5.610  1.00 21.15           N  
ATOM    908  CA  HIS A 132     -23.607 -11.565   6.551  1.00 20.79           C  
ATOM    909  C   HIS A 132     -23.212 -12.983   6.841  1.00 20.34           C  
ATOM    910  O   HIS A 132     -22.337 -13.552   6.179  1.00 19.57           O  
ATOM    911  CB  HIS A 132     -25.014 -11.496   5.975  1.00 20.99           C  
ATOM    912  CG  HIS A 132     -25.122 -12.079   4.594  1.00 21.89           C  
ATOM    913  ND1 HIS A 132     -25.280 -13.406   4.373  1.00 23.72           N  
ATOM    914  CD2 HIS A 132     -25.053 -11.478   3.347  1.00 21.36           C  
ATOM    915  CE1 HIS A 132     -25.327 -13.633   3.050  1.00 22.76           C  
ATOM    916  NE2 HIS A 132     -25.183 -12.453   2.422  1.00 24.36           N  
ATOM    917  N   GLY A 133     -23.852 -13.580   7.831  1.00 19.33           N  
ATOM    918  CA  GLY A 133     -23.566 -14.953   8.185  1.00 20.46           C  
ATOM    919  C   GLY A 133     -24.789 -15.679   8.701  1.00 22.29           C  
ATOM    920  O   GLY A 133     -25.915 -15.151   8.678  1.00 19.95           O  
ATOM    921  N   LYS A 134     -24.527 -16.884   9.187  1.00 22.97           N  
ATOM    922  CA  LYS A 134     -25.522 -17.796   9.738  1.00 25.72           C  
ATOM    923  C   LYS A 134     -26.314 -17.178  10.905  1.00 24.49           C  
ATOM    924  O   LYS A 134     -27.419 -17.608  11.202  1.00 26.02           O  
ATOM    925  CB  LYS A 134     -24.808 -19.076  10.188  1.00 27.01           C  
ATOM    926  CG  LYS A 134     -25.723 -20.240  10.514  1.00 30.46           C  
ATOM    927  CD  LYS A 134     -24.937 -21.534  10.710  1.00 32.44           C  
ATOM    928  CE  LYS A 134     -25.890 -22.715  10.848  1.00 30.39           C  
ATOM    929  NZ  LYS A 134     -25.117 -23.974  10.977  1.00 35.02           N  
ATOM    930  N   ASN A 135     -25.729 -16.187  11.570  1.00 23.80           N  
ATOM    931  CA  ASN A 135     -26.429 -15.466  12.633  1.00 23.19           C  
ATOM    932  C   ASN A 135     -27.056 -14.134  12.215  1.00 22.97           C  
ATOM    933  O   ASN A 135     -27.344 -13.317  13.089  1.00 23.35           O  
ATOM    934  CB  ASN A 135     -25.499 -15.235  13.835  1.00 22.14           C  
ATOM    935  CG  ASN A 135     -24.329 -14.317  13.499  1.00 20.75           C  
ATOM    936  OD1 ASN A 135     -24.067 -14.050  12.334  1.00 21.59           O  
ATOM    937  ND2 ASN A 135     -23.629 -13.842  14.507  1.00 18.75           N  
ATOM    938  N   HIS A 136     -27.298 -13.905  10.917  1.00 21.29           N  
ATOM    939  CA  HIS A 136     -27.839 -12.597  10.517  1.00 21.75           C  
ATOM    940  C   HIS A 136     -29.108 -12.234  11.234  1.00 22.43           C  
ATOM    941  O   HIS A 136     -29.289 -11.078  11.600  1.00 22.72           O  
ATOM    942  CB  HIS A 136     -28.071 -12.435   9.024  1.00 20.11           C  
ATOM    943  CG  HIS A 136     -28.601 -11.061   8.662  1.00 20.74           C  
ATOM    944  ND1 HIS A 136     -29.924 -10.785   8.585  1.00 19.82           N  
ATOM    945  CD2 HIS A 136     -27.930  -9.854   8.418  1.00 20.12           C  
ATOM    946  CE1 HIS A 136     -30.091  -9.487   8.290  1.00 21.03           C  
ATOM    947  NE2 HIS A 136     -28.867  -8.911   8.198  1.00 19.62           N  
ATOM    948  N   HIS A 137     -30.005 -13.201  11.425  1.00 22.57           N  
ATOM    949  CA  HIS A 137     -31.323 -12.891  11.994  1.00 24.66           C  
ATOM    950  C   HIS A 137     -31.266 -12.471  13.441  1.00 25.54           C  
ATOM    951  O   HIS A 137     -32.249 -11.930  13.964  1.00 27.27           O  
ATOM    952  CB  HIS A 137     -32.265 -14.082  11.851  1.00 23.81           C  
ATOM    953  CG  HIS A 137     -31.830 -15.276  12.661  1.00 25.64           C  
ATOM    954  ND1 HIS A 137     -30.765 -16.038  12.313  1.00 25.65           N  
ATOM    955  CD2 HIS A 137     -32.318 -15.802  13.854  1.00 25.84           C  
ATOM    956  CE1 HIS A 137     -30.578 -17.000  13.240  1.00 26.14           C  
ATOM    957  NE2 HIS A 137     -31.535 -16.867  14.177  1.00 27.98           N  
ATOM    958  N   SER A 138     -30.150 -12.751  14.114  1.00 24.92           N  
ATOM    959  CA  SER A 138     -29.972 -12.363  15.511  1.00 26.67           C  
ATOM    960  C   SER A 138     -28.917 -11.286  15.705  1.00 26.91           C  
ATOM    961  O   SER A 138     -28.947 -10.588  16.717  1.00 26.05           O  
ATOM    962  CB  SER A 138     -29.641 -13.575  16.403  1.00 27.39           C  
ATOM    963  OG  SER A 138     -28.327 -14.071  16.169  1.00 27.57           O  
ATOM    964  N   ALA A 139     -27.978 -11.149  14.761  1.00 25.66           N  
ATOM    965  CA  ALA A 139     -26.876 -10.190  14.964  1.00 24.51           C  
ATOM    966  C   ALA A 139     -26.673  -9.120  13.885  1.00 23.02           C  
ATOM    967  O   ALA A 139     -25.825  -8.238  14.052  1.00 21.76           O  
ATOM    968  CB  ALA A 139     -25.572 -10.926  15.247  1.00 25.89           C  
ATOM    969  N   GLY A 140     -27.457  -9.199  12.809  1.00 22.51           N  
ATOM    970  CA  GLY A 140     -27.351  -8.291  11.662  1.00 22.23           C  
ATOM    971  C   GLY A 140     -26.119  -8.636  10.851  1.00 22.01           C  
ATOM    972  O   GLY A 140     -25.608  -9.748  10.955  1.00 21.27           O  
ATOM    973  N   SER A 141     -25.659  -7.694  10.035  1.00 21.70           N  
ATOM    974  CA  SER A 141     -24.464  -7.908   9.214  1.00 23.05           C  
ATOM    975  C   SER A 141     -23.225  -7.266   9.840  1.00 23.16           C  
ATOM    976  O   SER A 141     -23.304  -6.648  10.904  1.00 21.88           O  
ATOM    977  CB  SER A 141     -24.693  -7.397   7.788  1.00 22.15           C  
ATOM    978  OG  SER A 141     -25.139  -6.049   7.802  1.00 22.06           O  
ATOM    979  N   PHE A 142     -22.080  -7.418   9.174  1.00 21.99           N  
ATOM    980  CA  PHE A 142     -20.812  -6.974   9.727  1.00 22.54           C  
ATOM    981  C   PHE A 142     -20.840  -5.496  10.143  1.00 22.87           C  
ATOM    982  O   PHE A 142     -20.319  -5.122  11.204  1.00 21.10           O  
ATOM    983  CB  PHE A 142     -19.681  -7.231   8.713  1.00 21.47           C  
ATOM    984  CG  PHE A 142     -18.326  -7.339   9.339  1.00 22.46           C  
ATOM    985  CD1 PHE A 142     -17.908  -8.534   9.919  1.00 21.97           C  
ATOM    986  CD2 PHE A 142     -17.452  -6.251   9.342  1.00 22.59           C  
ATOM    987  CE1 PHE A 142     -16.663  -8.638  10.513  1.00 22.21           C  
ATOM    988  CE2 PHE A 142     -16.204  -6.349   9.945  1.00 22.80           C  
ATOM    989  CZ  PHE A 142     -15.807  -7.542  10.526  1.00 22.48           C  
ATOM    990  N   GLY A 143     -21.467  -4.670   9.309  1.00 24.16           N  
ATOM    991  CA  GLY A 143     -21.524  -3.227   9.530  1.00 24.44           C  
ATOM    992  C   GLY A 143     -22.080  -2.844  10.888  1.00 24.61           C  
ATOM    993  O   GLY A 143     -21.634  -1.859  11.480  1.00 23.24           O  
ATOM    994  N   ASN A 144     -23.027  -3.648  11.383  1.00 24.59           N  
ATOM    995  CA  ASN A 144     -23.679  -3.430  12.677  1.00 24.58           C  
ATOM    996  C   ASN A 144     -22.700  -3.425  13.832  1.00 24.14           C  
ATOM    997  O   ASN A 144     -23.005  -2.907  14.892  1.00 23.42           O  
ATOM    998  CB  ASN A 144     -24.729  -4.515  12.956  1.00 23.75           C  
ATOM    999  CG  ASN A 144     -25.872  -4.514  11.955  1.00 24.55           C  
ATOM   1000  OD1 ASN A 144     -25.669  -4.498  10.741  1.00 24.57           O  
ATOM   1001  ND2 ASN A 144     -27.086  -4.587  12.465  1.00 24.27           N  
ATOM   1002  N   HIS A 145     -21.522  -4.003  13.620  1.00 22.54           N  
ATOM   1003  CA  HIS A 145     -20.584  -4.228  14.712  1.00 21.87           C  
ATOM   1004  C   HIS A 145     -19.352  -3.388  14.640  1.00 21.61           C  
ATOM   1005  O   HIS A 145     -18.489  -3.490  15.507  1.00 21.41           O  
ATOM   1006  CB  HIS A 145     -20.220  -5.711  14.793  1.00 22.38           C  
ATOM   1007  CG  HIS A 145     -21.412  -6.597  14.954  1.00 23.13           C  
ATOM   1008  ND1 HIS A 145     -21.948  -6.881  16.163  1.00 23.53           N  
ATOM   1009  CD2 HIS A 145     -22.210  -7.224  14.011  1.00 23.13           C  
ATOM   1010  CE1 HIS A 145     -23.020  -7.670  15.990  1.00 24.23           C  
ATOM   1011  NE2 HIS A 145     -23.177  -7.877  14.675  1.00 23.53           N  
ATOM   1012  N   VAL A 146     -19.246  -2.557  13.601  1.00 22.22           N  
ATOM   1013  CA  VAL A 146     -18.125  -1.632  13.474  1.00 22.38           C  
ATOM   1014  C   VAL A 146     -18.367  -0.397  14.358  1.00 23.27           C  
ATOM   1015  O   VAL A 146     -19.355   0.313  14.171  1.00 23.47           O  
ATOM   1016  CB  VAL A 146     -17.923  -1.214  12.010  1.00 22.31           C  
ATOM   1017  CG1 VAL A 146     -16.818  -0.170  11.892  1.00 22.25           C  
ATOM   1018  CG2 VAL A 146     -17.613  -2.439  11.141  1.00 22.76           C  
ATOM   1019  N   ARG A 147     -17.483  -0.151  15.318  1.00 23.03           N  
ATOM   1020  CA  ARG A 147     -17.643   1.016  16.195  1.00 25.09           C  
ATOM   1021  C   ARG A 147     -16.921   2.255  15.649  1.00 25.44           C  
ATOM   1022  O   ARG A 147     -17.330   3.374  15.916  1.00 23.96           O  
ATOM   1023  CB  ARG A 147     -17.241   0.704  17.649  1.00 25.53           C  
ATOM   1024  CG  ARG A 147     -18.067  -0.415  18.289  1.00 27.52           C  
ATOM   1025  CD  ARG A 147     -19.526  -0.011  18.544  1.00 28.64           C  
ATOM   1026  NE  ARG A 147     -20.376  -1.189  18.746  1.00 28.61           N  
ATOM   1027  CZ  ARG A 147     -21.236  -1.685  17.849  1.00 30.26           C  
ATOM   1028  NH1 ARG A 147     -21.408  -1.106  16.663  1.00 27.85           N  
ATOM   1029  NH2 ARG A 147     -21.941  -2.777  18.144  1.00 29.73           N  
ATOM   1030  N   SER A 148     -15.863   2.045  14.864  1.00 25.36           N  
ATOM   1031  CA  SER A 148     -15.227   3.133  14.136  1.00 27.16           C  
ATOM   1032  C   SER A 148     -14.422   2.568  12.972  1.00 26.87           C  
ATOM   1033  O   SER A 148     -14.108   1.375  12.958  1.00 25.86           O  
ATOM   1034  CB  SER A 148     -14.331   3.991  15.055  1.00 28.12           C  
ATOM   1035  OG  SER A 148     -13.059   3.404  15.258  1.00 30.65           O  
ATOM   1036  N   MET A 149     -14.115   3.423  12.000  1.00 26.35           N  
ATOM   1037  CA  MET A 149     -13.152   3.078  10.966  1.00 28.23           C  
ATOM   1038  C   MET A 149     -12.475   4.333  10.421  1.00 28.74           C  
ATOM   1039  O   MET A 149     -13.054   5.424  10.429  1.00 31.30           O  
ATOM   1040  CB  MET A 149     -13.791   2.223   9.848  1.00 29.19           C  
ATOM   1041  CG  MET A 149     -14.928   2.882   9.085  1.00 30.74           C  
ATOM   1042  SD  MET A 149     -15.712   1.784   7.876  1.00 33.95           S  
ATOM   1043  CE  MET A 149     -17.293   2.602   7.731  1.00 32.88           C  
ATOM   1044  N   ASP A 150     -11.239   4.161   9.980  1.00 28.49           N  
ATOM   1045  CA  ASP A 150     -10.443   5.226   9.396  1.00 29.14           C  
ATOM   1046  C   ASP A 150     -10.449   5.080   7.893  1.00 28.43           C  
ATOM   1047  O   ASP A 150      -9.922   4.105   7.348  1.00 30.27           O  
ATOM   1048  CB  ASP A 150      -9.020   5.178   9.937  1.00 30.55           C  
ATOM   1049  CG  ASP A 150      -8.972   5.366  11.443  1.00 33.73           C  
ATOM   1050  OD1 ASP A 150      -9.811   6.121  11.985  1.00 36.10           O  
ATOM   1051  OD2 ASP A 150      -8.103   4.755  12.089  1.00 35.60           O  
ATOM   1052  N   LEU A 151     -11.067   6.051   7.233  1.00 27.34           N  
ATOM   1053  CA  LEU A 151     -11.228   6.031   5.793  1.00 27.38           C  
ATOM   1054  C   LEU A 151     -10.310   7.040   5.104  1.00 28.00           C  
ATOM   1055  O   LEU A 151     -10.377   8.231   5.373  1.00 28.03           O  
ATOM   1056  CB  LEU A 151     -12.679   6.330   5.426  1.00 26.18           C  
ATOM   1057  CG  LEU A 151     -13.058   6.250   3.946  1.00 25.31           C  
ATOM   1058  CD1 LEU A 151     -13.080   4.799   3.474  1.00 25.40           C  
ATOM   1059  CD2 LEU A 151     -14.401   6.916   3.690  1.00 25.18           C  
ATOM   1060  N   LEU A 152      -9.469   6.547   4.201  1.00 29.30           N  
ATOM   1061  CA  LEU A 152      -8.656   7.406   3.350  1.00 31.13           C  
ATOM   1062  C   LEU A 152      -9.500   7.881   2.161  1.00 32.25           C  
ATOM   1063  O   LEU A 152      -9.853   7.090   1.276  1.00 33.47           O  
ATOM   1064  CB  LEU A 152      -7.403   6.648   2.876  1.00 30.24           C  
ATOM   1065  CG  LEU A 152      -6.522   7.309   1.802  1.00 31.35           C  
ATOM   1066  CD1 LEU A 152      -5.957   8.650   2.271  1.00 31.03           C  
ATOM   1067  CD2 LEU A 152      -5.402   6.358   1.381  1.00 30.04           C  
ATOM   1068  N   THR A 153      -9.835   9.169   2.153  1.00 33.10           N  
ATOM   1069  CA  THR A 153     -10.704   9.730   1.115  1.00 33.89           C  
ATOM   1070  C   THR A 153      -9.915  10.312  -0.068  1.00 35.51           C  
ATOM   1071  O   THR A 153      -8.673  10.356  -0.038  1.00 34.23           O  
ATOM   1072  CB  THR A 153     -11.756  10.711   1.695  1.00 35.02           C  
ATOM   1073  OG1 THR A 153     -11.121  11.674   2.548  1.00 35.32           O  
ATOM   1074  CG2 THR A 153     -12.776   9.944   2.521  1.00 34.05           C  
ATOM   1075  N   ALA A 154     -10.638  10.706  -1.118  1.00 35.35           N  
ATOM   1076  CA  ALA A 154     -10.040  11.192  -2.369  1.00 39.15           C  
ATOM   1077  C   ALA A 154      -9.173  12.439  -2.168  1.00 40.75           C  
ATOM   1078  O   ALA A 154      -8.176  12.620  -2.863  1.00 43.64           O  
ATOM   1079  CB  ALA A 154     -11.122  11.455  -3.410  1.00 37.22           C  
ATOM   1080  N   ASP A 155      -9.555  13.279  -1.207  1.00 42.70           N  
ATOM   1081  CA  ASP A 155      -8.792  14.481  -0.834  1.00 44.21           C  
ATOM   1082  C   ASP A 155      -7.459  14.178  -0.117  1.00 45.36           C  
ATOM   1083  O   ASP A 155      -6.740  15.097   0.285  1.00 44.65           O  
ATOM   1084  CB  ASP A 155      -9.663  15.416   0.019  1.00 44.03           C  
ATOM   1085  CG  ASP A 155     -10.072  14.799   1.356  1.00 45.51           C  
ATOM   1086  OD1 ASP A 155      -9.669  13.659   1.664  1.00 48.33           O  
ATOM   1087  OD2 ASP A 155     -10.803  15.458   2.118  1.00 46.93           O  
ATOM   1088  N   GLY A 156      -7.145  12.894   0.047  1.00 45.68           N  
ATOM   1089  CA  GLY A 156      -5.906  12.464   0.706  1.00 46.05           C  
ATOM   1090  C   GLY A 156      -5.925  12.492   2.226  1.00 45.18           C  
ATOM   1091  O   GLY A 156      -4.923  12.166   2.860  1.00 48.73           O  
ATOM   1092  N   GLU A 157      -7.052  12.883   2.815  1.00 44.93           N  
ATOM   1093  CA  GLU A 157      -7.208  12.890   4.272  1.00 46.34           C  
ATOM   1094  C   GLU A 157      -7.635  11.518   4.792  1.00 44.12           C  
ATOM   1095  O   GLU A 157      -8.187  10.709   4.041  1.00 43.24           O  
ATOM   1096  CB  GLU A 157      -8.252  13.927   4.707  1.00 50.81           C  
ATOM   1097  CG  GLU A 157      -8.055  15.333   4.152  1.00 57.32           C  
ATOM   1098  CD  GLU A 157      -6.948  16.104   4.849  1.00 62.85           C  
ATOM   1099  OE1 GLU A 157      -7.275  17.017   5.640  1.00 67.23           O  
ATOM   1100  OE2 GLU A 157      -5.758  15.799   4.610  1.00 62.83           O  
ATOM   1101  N   ILE A 158      -7.384  11.271   6.077  1.00 41.27           N  
ATOM   1102  CA  ILE A 158      -7.921  10.095   6.759  1.00 41.03           C  
ATOM   1103  C   ILE A 158      -8.986  10.508   7.772  1.00 41.50           C  
ATOM   1104  O   ILE A 158      -8.693  11.157   8.774  1.00 43.01           O  
ATOM   1105  CB  ILE A 158      -6.814   9.233   7.407  1.00 42.77           C  
ATOM   1106  CG1 ILE A 158      -5.864   8.706   6.314  1.00 41.11           C  
ATOM   1107  CG2 ILE A 158      -7.427   8.095   8.228  1.00 41.93           C  
ATOM   1108  CD1 ILE A 158      -4.747   7.808   6.802  1.00 42.31           C  
ATOM   1109  N   ARG A 159     -10.229  10.131   7.490  1.00 40.35           N  
ATOM   1110  CA  ARG A 159     -11.362  10.522   8.321  1.00 39.87           C  
ATOM   1111  C   ARG A 159     -11.761   9.412   9.272  1.00 38.96           C  
ATOM   1112  O   ARG A 159     -11.921   8.252   8.866  1.00 39.64           O  
ATOM   1113  CB  ARG A 159     -12.536  10.952   7.444  1.00 40.65           C  
ATOM   1114  CG  ARG A 159     -12.248  12.263   6.729  1.00 41.97           C  
ATOM   1115  CD  ARG A 159     -13.063  12.428   5.467  1.00 43.20           C  
ATOM   1116  NE  ARG A 159     -14.432  12.840   5.763  1.00 44.60           N  
ATOM   1117  CZ  ARG A 159     -15.211  13.495   4.906  1.00 43.31           C  
ATOM   1118  NH1 ARG A 159     -14.751  13.824   3.700  1.00 41.32           N  
ATOM   1119  NH2 ARG A 159     -16.446  13.824   5.259  1.00 41.59           N  
ATOM   1120  N   HIS A 160     -11.881   9.775  10.544  1.00 37.56           N  
ATOM   1121  CA  HIS A 160     -12.336   8.866  11.581  1.00 37.79           C  
ATOM   1122  C   HIS A 160     -13.844   8.851  11.571  1.00 37.51           C  
ATOM   1123  O   HIS A 160     -14.492   9.847  11.902  1.00 38.77           O  
ATOM   1124  CB  HIS A 160     -11.780   9.303  12.930  1.00 38.43           C  
ATOM   1125  CG  HIS A 160     -11.958   8.281  14.029  1.00 39.06           C  
ATOM   1126  ND1 HIS A 160     -11.209   7.168  14.109  1.00 40.02           N  
ATOM   1127  CD2 HIS A 160     -12.825   8.252  15.121  1.00 39.50           C  
ATOM   1128  CE1 HIS A 160     -11.575   6.457  15.190  1.00 40.11           C  
ATOM   1129  NE2 HIS A 160     -12.566   7.123  15.810  1.00 40.68           N  
ATOM   1130  N   LEU A 161     -14.420   7.729  11.150  1.00 34.14           N  
ATOM   1131  CA  LEU A 161     -15.869   7.624  10.993  1.00 31.60           C  
ATOM   1132  C   LEU A 161     -16.439   6.753  12.090  1.00 30.31           C  
ATOM   1133  O   LEU A 161     -15.824   5.756  12.474  1.00 28.28           O  
ATOM   1134  CB  LEU A 161     -16.235   7.022   9.631  1.00 31.92           C  
ATOM   1135  CG  LEU A 161     -15.579   7.524   8.339  1.00 32.82           C  
ATOM   1136  CD1 LEU A 161     -16.075   6.673   7.181  1.00 32.85           C  
ATOM   1137  CD2 LEU A 161     -15.853   8.999   8.074  1.00 32.50           C  
ATOM   1138  N   THR A 162     -17.615   7.136  12.586  1.00 28.52           N  
ATOM   1139  CA  THR A 162     -18.327   6.389  13.618  1.00 29.27           C  
ATOM   1140  C   THR A 162     -19.794   6.271  13.198  1.00 28.60           C  
ATOM   1141  O   THR A 162     -20.288   7.135  12.470  1.00 27.96           O  
ATOM   1142  CB  THR A 162     -18.254   7.100  14.988  1.00 30.74           C  
ATOM   1143  OG1 THR A 162     -18.855   8.392  14.877  1.00 33.97           O  
ATOM   1144  CG2 THR A 162     -16.804   7.255  15.466  1.00 31.22           C  
ATOM   1145  N   PRO A 163     -20.499   5.203  13.639  1.00 28.12           N  
ATOM   1146  CA  PRO A 163     -21.851   4.968  13.118  1.00 28.84           C  
ATOM   1147  C   PRO A 163     -22.862   6.070  13.465  1.00 30.34           C  
ATOM   1148  O   PRO A 163     -23.830   6.258  12.723  1.00 28.54           O  
ATOM   1149  CB  PRO A 163     -22.268   3.642  13.774  1.00 27.15           C  
ATOM   1150  CG  PRO A 163     -21.409   3.519  14.980  1.00 27.17           C  
ATOM   1151  CD  PRO A 163     -20.100   4.160  14.598  1.00 27.64           C  
ATOM   1152  N   THR A 164     -22.643   6.780  14.573  1.00 32.55           N  
ATOM   1153  CA  THR A 164     -23.613   7.802  15.024  1.00 35.86           C  
ATOM   1154  C   THR A 164     -22.974   9.157  15.227  1.00 37.70           C  
ATOM   1155  O   THR A 164     -23.628  10.082  15.698  1.00 41.08           O  
ATOM   1156  CB  THR A 164     -24.318   7.430  16.346  1.00 34.17           C  
ATOM   1157  OG1 THR A 164     -23.373   7.480  17.416  1.00 35.76           O  
ATOM   1158  CG2 THR A 164     -24.941   6.051  16.281  1.00 35.30           C  
ATOM   1159  N   GLY A 165     -21.699   9.275  14.869  1.00 39.44           N  
ATOM   1160  CA  GLY A 165     -21.003  10.549  14.948  1.00 42.69           C  
ATOM   1161  C   GLY A 165     -21.418  11.536  13.872  1.00 45.98           C  
ATOM   1162  O   GLY A 165     -22.466  11.390  13.228  1.00 45.67           O  
ATOM   1163  N   GLU A 166     -20.574  12.542  13.679  1.00 47.22           N  
ATOM   1164  CA  GLU A 166     -20.849  13.628  12.758  1.00 49.11           C  
ATOM   1165  C   GLU A 166     -20.727  13.144  11.316  1.00 46.35           C  
ATOM   1166  O   GLU A 166     -21.368  13.680  10.422  1.00 45.90           O  
ATOM   1167  CB  GLU A 166     -19.860  14.762  13.018  1.00 52.44           C  
ATOM   1168  CG  GLU A 166     -20.478  16.146  12.997  1.00 55.86           C  
ATOM   1169  CD  GLU A 166     -19.686  17.147  13.819  1.00 58.23           C  
ATOM   1170  OE1 GLU A 166     -18.438  17.052  13.857  1.00 57.47           O  
ATOM   1171  OE2 GLU A 166     -20.319  18.031  14.434  1.00 59.39           O  
ATOM   1172  N   ASP A 167     -19.899  12.124  11.112  1.00 45.48           N  
ATOM   1173  CA  ASP A 167     -19.660  11.530   9.798  1.00 43.37           C  
ATOM   1174  C   ASP A 167     -20.449  10.226   9.587  1.00 41.05           C  
ATOM   1175  O   ASP A 167     -19.992   9.337   8.862  1.00 41.63           O  
ATOM   1176  CB  ASP A 167     -18.160  11.248   9.630  1.00 45.72           C  
ATOM   1177  CG  ASP A 167     -17.438  12.312   8.817  1.00 48.96           C  
ATOM   1178  OD1 ASP A 167     -17.913  12.673   7.716  1.00 49.46           O  
ATOM   1179  OD2 ASP A 167     -16.364  12.761   9.270  1.00 52.30           O  
ATOM   1180  N   ALA A 168     -21.623  10.117  10.209  1.00 35.14           N  
ATOM   1181  CA  ALA A 168     -22.437   8.898  10.132  1.00 34.52           C  
ATOM   1182  C   ALA A 168     -22.905   8.564   8.716  1.00 33.01           C  
ATOM   1183  O   ALA A 168     -22.965   7.392   8.333  1.00 31.21           O  
ATOM   1184  CB  ALA A 168     -23.630   8.985  11.080  1.00 33.26           C  
ATOM   1185  N   GLU A 169     -23.237   9.600   7.944  1.00 32.23           N  
ATOM   1186  CA  GLU A 169     -23.666   9.440   6.561  1.00 30.79           C  
ATOM   1187  C   GLU A 169     -22.587   8.749   5.724  1.00 28.33           C  
ATOM   1188  O   GLU A 169     -22.872   7.805   4.980  1.00 26.88           O  
ATOM   1189  CB  GLU A 169     -24.020  10.804   5.957  1.00 33.21           C  
ATOM   1190  CG  GLU A 169     -24.537  10.737   4.532  1.00 33.74           C  
ATOM   1191  CD  GLU A 169     -24.844  12.117   3.954  1.00 37.13           C  
ATOM   1192  OE1 GLU A 169     -23.904  12.835   3.546  1.00 39.67           O  
ATOM   1193  OE2 GLU A 169     -26.032  12.476   3.886  1.00 35.52           O  
ATOM   1194  N   LEU A 170     -21.354   9.231   5.854  1.00 26.80           N  
ATOM   1195  CA  LEU A 170     -20.206   8.638   5.167  1.00 26.17           C  
ATOM   1196  C   LEU A 170     -19.864   7.241   5.712  1.00 25.31           C  
ATOM   1197  O   LEU A 170     -19.427   6.355   4.959  1.00 23.81           O  
ATOM   1198  CB  LEU A 170     -18.981   9.564   5.256  1.00 25.53           C  
ATOM   1199  CG  LEU A 170     -17.733   9.070   4.505  1.00 25.78           C  
ATOM   1200  CD1 LEU A 170     -18.074   8.746   3.055  1.00 25.06           C  
ATOM   1201  CD2 LEU A 170     -16.607  10.092   4.596  1.00 26.25           C  
ATOM   1202  N   PHE A 171     -20.042   7.064   7.018  1.00 24.23           N  
ATOM   1203  CA  PHE A 171     -19.853   5.764   7.651  1.00 25.42           C  
ATOM   1204  C   PHE A 171     -20.761   4.725   6.993  1.00 24.82           C  
ATOM   1205  O   PHE A 171     -20.304   3.666   6.561  1.00 24.74           O  
ATOM   1206  CB  PHE A 171     -20.147   5.831   9.158  1.00 24.87           C  
ATOM   1207  CG  PHE A 171     -19.954   4.521   9.872  1.00 24.23           C  
ATOM   1208  CD1 PHE A 171     -18.804   4.281  10.599  1.00 23.81           C  
ATOM   1209  CD2 PHE A 171     -20.936   3.528   9.818  1.00 24.50           C  
ATOM   1210  CE1 PHE A 171     -18.617   3.073  11.253  1.00 24.09           C  
ATOM   1211  CE2 PHE A 171     -20.754   2.318  10.470  1.00 24.09           C  
ATOM   1212  CZ  PHE A 171     -19.597   2.090  11.185  1.00 23.90           C  
ATOM   1213  N   TRP A 172     -22.050   5.038   6.934  1.00 24.64           N  
ATOM   1214  CA  TRP A 172     -23.047   4.100   6.432  1.00 25.14           C  
ATOM   1215  C   TRP A 172     -23.077   3.951   4.934  1.00 25.23           C  
ATOM   1216  O   TRP A 172     -23.681   3.010   4.424  1.00 25.42           O  
ATOM   1217  CB  TRP A 172     -24.422   4.422   7.015  1.00 25.06           C  
ATOM   1218  CG  TRP A 172     -24.459   4.055   8.471  1.00 24.61           C  
ATOM   1219  CD1 TRP A 172     -24.442   4.918   9.567  1.00 24.11           C  
ATOM   1220  CD2 TRP A 172     -24.485   2.697   9.046  1.00 24.72           C  
ATOM   1221  NE1 TRP A 172     -24.478   4.216  10.738  1.00 24.50           N  
ATOM   1222  CE2 TRP A 172     -24.498   2.873  10.501  1.00 25.02           C  
ATOM   1223  CE3 TRP A 172     -24.525   1.406   8.520  1.00 24.31           C  
ATOM   1224  CZ2 TRP A 172     -24.536   1.785  11.379  1.00 24.60           C  
ATOM   1225  CZ3 TRP A 172     -24.574   0.316   9.413  1.00 24.88           C  
ATOM   1226  CH2 TRP A 172     -24.572   0.504  10.805  1.00 25.14           C  
ATOM   1227  N   ALA A 173     -22.395   4.855   4.226  1.00 23.92           N  
ATOM   1228  CA  ALA A 173     -22.201   4.732   2.782  1.00 23.11           C  
ATOM   1229  C   ALA A 173     -20.970   3.878   2.463  1.00 23.03           C  
ATOM   1230  O   ALA A 173     -20.887   3.302   1.386  1.00 23.08           O  
ATOM   1231  CB  ALA A 173     -22.074   6.108   2.132  1.00 22.70           C  
ATOM   1232  N   THR A 174     -20.040   3.807   3.407  1.00 22.23           N  
ATOM   1233  CA  THR A 174     -18.816   3.006   3.277  1.00 23.35           C  
ATOM   1234  C   THR A 174     -19.162   1.536   3.573  1.00 23.20           C  
ATOM   1235  O   THR A 174     -18.716   0.613   2.875  1.00 22.62           O  
ATOM   1236  CB  THR A 174     -17.711   3.536   4.222  1.00 23.39           C  
ATOM   1237  OG1 THR A 174     -17.406   4.895   3.872  1.00 23.65           O  
ATOM   1238  CG2 THR A 174     -16.419   2.679   4.149  1.00 22.66           C  
ATOM   1239  N   VAL A 175     -19.999   1.336   4.586  1.00 22.12           N  
ATOM   1240  CA  VAL A 175     -20.595   0.034   4.839  1.00 22.45           C  
ATOM   1241  C   VAL A 175     -21.352  -0.366   3.584  1.00 20.99           C  
ATOM   1242  O   VAL A 175     -22.206   0.373   3.095  1.00 21.91           O  
ATOM   1243  CB  VAL A 175     -21.549   0.079   6.057  1.00 22.50           C  
ATOM   1244  CG1 VAL A 175     -22.360  -1.206   6.154  1.00 22.48           C  
ATOM   1245  CG2 VAL A 175     -20.756   0.296   7.338  1.00 22.55           C  
ATOM   1246  N   GLY A 176     -21.009  -1.521   3.035  1.00 21.65           N  
ATOM   1247  CA  GLY A 176     -21.644  -1.984   1.806  1.00 22.45           C  
ATOM   1248  C   GLY A 176     -21.292  -1.187   0.557  1.00 22.25           C  
ATOM   1249  O   GLY A 176     -21.917  -1.379  -0.479  1.00 21.99           O  
ATOM   1250  N   GLY A 177     -20.284  -0.310   0.643  1.00 23.50           N  
ATOM   1251  CA  GLY A 177     -19.927   0.593  -0.477  1.00 22.89           C  
ATOM   1252  C   GLY A 177     -18.969   0.058  -1.539  1.00 25.23           C  
ATOM   1253  O   GLY A 177     -18.625   0.771  -2.492  1.00 24.62           O  
ATOM   1254  N   ASN A 178     -18.536  -1.189  -1.388  1.00 24.13           N  
ATOM   1255  CA  ASN A 178     -17.647  -1.820  -2.357  1.00 24.98           C  
ATOM   1256  C   ASN A 178     -16.438  -0.945  -2.678  1.00 24.94           C  
ATOM   1257  O   ASN A 178     -16.076  -0.787  -3.843  1.00 23.79           O  
ATOM   1258  CB  ASN A 178     -18.390  -2.195  -3.661  1.00 25.15           C  
ATOM   1259  CG  ASN A 178     -19.467  -3.249  -3.441  1.00 25.86           C  
ATOM   1260  OD1 ASN A 178     -19.218  -4.441  -3.590  1.00 26.50           O  
ATOM   1261  ND2 ASN A 178     -20.666  -2.808  -3.091  1.00 25.45           N  
ATOM   1262  N   GLY A 179     -15.850  -0.355  -1.641  1.00 25.50           N  
ATOM   1263  CA  GLY A 179     -14.609   0.421  -1.776  1.00 26.59           C  
ATOM   1264  C   GLY A 179     -14.733   1.773  -2.452  1.00 27.56           C  
ATOM   1265  O   GLY A 179     -13.721   2.420  -2.723  1.00 28.35           O  
ATOM   1266  N   LEU A 180     -15.963   2.220  -2.708  1.00 25.96           N  
ATOM   1267  CA  LEU A 180     -16.171   3.404  -3.546  1.00 27.01           C  
ATOM   1268  C   LEU A 180     -16.325   4.740  -2.812  1.00 27.22           C  
ATOM   1269  O   LEU A 180     -16.667   5.755  -3.434  1.00 29.04           O  
ATOM   1270  CB  LEU A 180     -17.307   3.171  -4.549  1.00 26.59           C  
ATOM   1271  CG  LEU A 180     -16.999   2.086  -5.589  1.00 26.97           C  
ATOM   1272  CD1 LEU A 180     -18.285   1.560  -6.219  1.00 25.87           C  
ATOM   1273  CD2 LEU A 180     -16.030   2.610  -6.644  1.00 28.92           C  
ATOM   1274  N   THR A 181     -16.044   4.743  -1.513  1.00 25.39           N  
ATOM   1275  CA  THR A 181     -15.984   5.978  -0.735  1.00 26.44           C  
ATOM   1276  C   THR A 181     -14.552   6.244  -0.285  1.00 26.85           C  
ATOM   1277  O   THR A 181     -14.265   7.278   0.312  1.00 27.82           O  
ATOM   1278  CB  THR A 181     -16.898   5.933   0.503  1.00 25.46           C  
ATOM   1279  OG1 THR A 181     -16.429   4.919   1.403  1.00 24.90           O  
ATOM   1280  CG2 THR A 181     -18.312   5.627   0.083  1.00 26.30           C  
ATOM   1281  N   GLY A 182     -13.662   5.305  -0.592  1.00 27.54           N  
ATOM   1282  CA  GLY A 182     -12.261   5.419  -0.231  1.00 27.84           C  
ATOM   1283  C   GLY A 182     -11.652   4.122   0.272  1.00 27.87           C  
ATOM   1284  O   GLY A 182     -12.197   3.030   0.079  1.00 26.56           O  
ATOM   1285  N   ILE A 183     -10.505   4.245   0.923  1.00 29.08           N  
ATOM   1286  CA  ILE A 183      -9.796   3.074   1.394  1.00 29.84           C  
ATOM   1287  C   ILE A 183      -9.905   3.005   2.904  1.00 29.54           C  
ATOM   1288  O   ILE A 183      -9.441   3.905   3.605  1.00 28.44           O  
ATOM   1289  CB  ILE A 183      -8.320   3.081   0.940  1.00 31.29           C  
ATOM   1290  CG1 ILE A 183      -8.258   3.140  -0.594  1.00 32.69           C  
ATOM   1291  CG2 ILE A 183      -7.584   1.864   1.493  1.00 32.07           C  
ATOM   1292  CD1 ILE A 183      -6.910   2.814  -1.198  1.00 33.48           C  
ATOM   1293  N   ILE A 184     -10.548   1.942   3.392  1.00 28.13           N  
ATOM   1294  CA  ILE A 184     -10.614   1.674   4.815  1.00 27.02           C  
ATOM   1295  C   ILE A 184      -9.225   1.236   5.250  1.00 27.06           C  
ATOM   1296  O   ILE A 184      -8.698   0.242   4.750  1.00 27.19           O  
ATOM   1297  CB  ILE A 184     -11.651   0.579   5.157  1.00 26.24           C  
ATOM   1298  CG1 ILE A 184     -13.031   0.940   4.585  1.00 25.44           C  
ATOM   1299  CG2 ILE A 184     -11.685   0.347   6.660  1.00 26.09           C  
ATOM   1300  CD1 ILE A 184     -14.030  -0.208   4.545  1.00 23.82           C  
ATOM   1301  N   MET A 185      -8.623   1.990   6.160  1.00 26.54           N  
ATOM   1302  CA  MET A 185      -7.262   1.700   6.593  1.00 26.29           C  
ATOM   1303  C   MET A 185      -7.258   0.857   7.854  1.00 24.92           C  
ATOM   1304  O   MET A 185      -6.370   0.037   8.057  1.00 22.27           O  
ATOM   1305  CB  MET A 185      -6.474   3.001   6.854  1.00 28.38           C  
ATOM   1306  CG  MET A 185      -6.358   3.958   5.658  1.00 31.40           C  
ATOM   1307  SD  MET A 185      -5.468   3.299   4.223  1.00 34.97           S  
ATOM   1308  CE  MET A 185      -3.794   3.132   4.846  1.00 36.08           C  
ATOM   1309  N   ARG A 186      -8.266   1.067   8.704  1.00 24.93           N  
ATOM   1310  CA  ARG A 186      -8.208   0.609  10.080  1.00 24.15           C  
ATOM   1311  C   ARG A 186      -9.621   0.710  10.647  1.00 24.22           C  
ATOM   1312  O   ARG A 186     -10.389   1.602  10.270  1.00 23.27           O  
ATOM   1313  CB  ARG A 186      -7.274   1.534  10.865  1.00 24.61           C  
ATOM   1314  CG  ARG A 186      -6.799   1.014  12.207  1.00 25.07           C  
ATOM   1315  CD  ARG A 186      -5.663   1.875  12.743  1.00 24.77           C  
ATOM   1316  NE  ARG A 186      -5.436   1.629  14.165  1.00 25.69           N  
ATOM   1317  CZ  ARG A 186      -4.345   1.992  14.833  1.00 26.49           C  
ATOM   1318  NH1 ARG A 186      -3.363   2.619  14.206  1.00 25.52           N  
ATOM   1319  NH2 ARG A 186      -4.231   1.720  16.137  1.00 26.99           N  
ATOM   1320  N   ALA A 187      -9.956  -0.197  11.548  1.00 23.66           N  
ATOM   1321  CA  ALA A 187     -11.291  -0.199  12.149  1.00 24.31           C  
ATOM   1322  C   ALA A 187     -11.235  -0.759  13.547  1.00 25.18           C  
ATOM   1323  O   ALA A 187     -10.290  -1.477  13.899  1.00 24.42           O  
ATOM   1324  CB  ALA A 187     -12.263  -1.008  11.300  1.00 23.14           C  
ATOM   1325  N   THR A 188     -12.261  -0.408  14.329  1.00 25.14           N  
ATOM   1326  CA  THR A 188     -12.494  -0.944  15.654  1.00 25.26           C  
ATOM   1327  C   THR A 188     -13.828  -1.695  15.585  1.00 24.89           C  
ATOM   1328  O   THR A 188     -14.826  -1.149  15.097  1.00 25.28           O  
ATOM   1329  CB  THR A 188     -12.532   0.197  16.707  1.00 27.58           C  
ATOM   1330  OG1 THR A 188     -11.225   0.776  16.825  1.00 29.00           O  
ATOM   1331  CG2 THR A 188     -12.950  -0.312  18.080  1.00 27.93           C  
ATOM   1332  N   ILE A 189     -13.829  -2.949  16.033  1.00 24.04           N  
ATOM   1333  CA  ILE A 189     -15.000  -3.819  15.967  1.00 24.15           C  
ATOM   1334  C   ILE A 189     -15.343  -4.242  17.381  1.00 24.43           C  
ATOM   1335  O   ILE A 189     -14.447  -4.576  18.154  1.00 24.29           O  
ATOM   1336  CB  ILE A 189     -14.686  -5.126  15.179  1.00 24.68           C  
ATOM   1337  CG1 ILE A 189     -13.903  -4.854  13.880  1.00 25.02           C  
ATOM   1338  CG2 ILE A 189     -15.940  -5.952  14.925  1.00 24.22           C  
ATOM   1339  CD1 ILE A 189     -14.656  -4.122  12.800  1.00 24.68           C  
ATOM   1340  N   GLU A 190     -16.634  -4.242  17.719  1.00 24.58           N  
ATOM   1341  CA  GLU A 190     -17.071  -4.795  18.981  1.00 24.29           C  
ATOM   1342  C   GLU A 190     -17.339  -6.280  18.781  1.00 23.36           C  
ATOM   1343  O   GLU A 190     -18.118  -6.669  17.901  1.00 22.71           O  
ATOM   1344  CB  GLU A 190     -18.341  -4.099  19.489  1.00 25.38           C  
ATOM   1345  CG  GLU A 190     -18.901  -4.762  20.732  1.00 27.55           C  
ATOM   1346  CD  GLU A 190     -20.010  -3.966  21.411  1.00 29.22           C  
ATOM   1347  OE1 GLU A 190     -20.469  -2.937  20.872  1.00 31.33           O  
ATOM   1348  OE2 GLU A 190     -20.423  -4.388  22.501  1.00 31.27           O  
ATOM   1349  N   MET A 191     -16.705  -7.097  19.613  1.00 23.37           N  
ATOM   1350  CA  MET A 191     -16.774  -8.539  19.475  1.00 24.14           C  
ATOM   1351  C   MET A 191     -17.909  -9.061  20.338  1.00 24.57           C  
ATOM   1352  O   MET A 191     -18.482  -8.324  21.140  1.00 25.22           O  
ATOM   1353  CB  MET A 191     -15.435  -9.182  19.882  1.00 24.44           C  
ATOM   1354  CG  MET A 191     -14.238  -8.681  19.082  1.00 23.91           C  
ATOM   1355  SD  MET A 191     -14.189  -9.278  17.377  1.00 25.76           S  
ATOM   1356  CE  MET A 191     -13.402 -10.862  17.642  1.00 24.05           C  
ATOM   1357  N   THR A 192     -18.234 -10.332  20.158  1.00 24.26           N  
ATOM   1358  CA  THR A 192     -19.246 -10.998  20.955  1.00 23.94           C  
ATOM   1359  C   THR A 192     -18.546 -11.822  22.036  1.00 25.21           C  
ATOM   1360  O   THR A 192     -17.630 -12.598  21.725  1.00 25.23           O  
ATOM   1361  CB  THR A 192     -20.108 -11.885  20.038  1.00 23.63           C  
ATOM   1362  OG1 THR A 192     -20.752 -11.049  19.066  1.00 23.88           O  
ATOM   1363  CG2 THR A 192     -21.155 -12.688  20.823  1.00 21.98           C  
ATOM   1364  N   PRO A 193     -18.944 -11.649  23.314  1.00 25.88           N  
ATOM   1365  CA  PRO A 193     -18.272 -12.451  24.347  1.00 27.58           C  
ATOM   1366  C   PRO A 193     -18.667 -13.913  24.233  1.00 28.16           C  
ATOM   1367  O   PRO A 193     -19.774 -14.217  23.792  1.00 29.10           O  
ATOM   1368  CB  PRO A 193     -18.779 -11.865  25.676  1.00 26.04           C  
ATOM   1369  CG  PRO A 193     -19.644 -10.708  25.326  1.00 26.56           C  
ATOM   1370  CD  PRO A 193     -20.001 -10.781  23.871  1.00 26.06           C  
ATOM   1371  N   THR A 194     -17.749 -14.804  24.594  1.00 27.90           N  
ATOM   1372  CA  THR A 194     -18.005 -16.240  24.557  1.00 28.49           C  
ATOM   1373  C   THR A 194     -17.134 -16.928  25.607  1.00 29.50           C  
ATOM   1374  O   THR A 194     -16.023 -16.462  25.899  1.00 29.67           O  
ATOM   1375  CB  THR A 194     -17.752 -16.848  23.150  1.00 28.28           C  
ATOM   1376  OG1 THR A 194     -18.194 -18.214  23.121  1.00 28.54           O  
ATOM   1377  CG2 THR A 194     -16.268 -16.802  22.777  1.00 26.03           C  
ATOM   1378  N   SER A 195     -17.640 -18.021  26.177  1.00 28.70           N  
ATOM   1379  CA  SER A 195     -16.845 -18.812  27.116  1.00 29.58           C  
ATOM   1380  C   SER A 195     -16.214 -20.031  26.438  1.00 29.45           C  
ATOM   1381  O   SER A 195     -15.362 -20.692  27.027  1.00 30.46           O  
ATOM   1382  CB  SER A 195     -17.649 -19.206  28.365  1.00 30.00           C  
ATOM   1383  OG  SER A 195     -18.875 -19.837  28.034  1.00 31.54           O  
ATOM   1384  N   THR A 196     -16.611 -20.314  25.196  1.00 27.95           N  
ATOM   1385  CA  THR A 196     -16.087 -21.490  24.476  1.00 28.50           C  
ATOM   1386  C   THR A 196     -15.990 -21.269  22.969  1.00 26.51           C  
ATOM   1387  O   THR A 196     -16.602 -20.355  22.427  1.00 25.30           O  
ATOM   1388  CB  THR A 196     -16.963 -22.753  24.697  1.00 28.79           C  
ATOM   1389  OG1 THR A 196     -18.037 -22.768  23.753  1.00 27.62           O  
ATOM   1390  CG2 THR A 196     -17.545 -22.798  26.095  1.00 30.16           C  
ATOM   1391  N   ALA A 197     -15.252 -22.143  22.295  1.00 27.91           N  
ATOM   1392  CA  ALA A 197     -15.171 -22.119  20.829  1.00 28.44           C  
ATOM   1393  C   ALA A 197     -16.115 -23.139  20.169  1.00 28.98           C  
ATOM   1394  O   ALA A 197     -15.898 -23.551  19.031  1.00 31.71           O  
ATOM   1395  CB  ALA A 197     -13.727 -22.325  20.377  1.00 29.17           C  
ATOM   1396  N   TYR A 198     -17.178 -23.518  20.878  1.00 29.05           N  
ATOM   1397  CA  TYR A 198     -18.096 -24.563  20.420  1.00 28.97           C  
ATOM   1398  C   TYR A 198     -19.550 -24.102  20.314  1.00 29.09           C  
ATOM   1399  O   TYR A 198     -19.954 -23.131  20.962  1.00 27.17           O  
ATOM   1400  CB  TYR A 198     -18.039 -25.756  21.378  1.00 29.47           C  
ATOM   1401  CG  TYR A 198     -16.701 -26.436  21.418  1.00 32.22           C  
ATOM   1402  CD1 TYR A 198     -16.423 -27.511  20.576  1.00 32.90           C  
ATOM   1403  CD2 TYR A 198     -15.703 -26.001  22.291  1.00 32.26           C  
ATOM   1404  CE1 TYR A 198     -15.192 -28.138  20.606  1.00 34.74           C  
ATOM   1405  CE2 TYR A 198     -14.468 -26.622  22.333  1.00 33.71           C  
ATOM   1406  CZ  TYR A 198     -14.219 -27.690  21.494  1.00 36.16           C  
ATOM   1407  OH  TYR A 198     -12.992 -28.311  21.539  1.00 38.54           O  
ATOM   1408  N   PHE A 199     -20.324 -24.827  19.503  1.00 27.54           N  
ATOM   1409  CA  PHE A 199     -21.764 -24.623  19.371  1.00 27.26           C  
ATOM   1410  C   PHE A 199     -22.535 -25.815  19.950  1.00 28.41           C  
ATOM   1411  O   PHE A 199     -22.055 -26.955  19.911  1.00 27.48           O  
ATOM   1412  CB  PHE A 199     -22.160 -24.433  17.890  1.00 25.85           C  
ATOM   1413  CG  PHE A 199     -21.516 -23.233  17.224  1.00 26.93           C  
ATOM   1414  CD1 PHE A 199     -22.186 -22.018  17.150  1.00 26.58           C  
ATOM   1415  CD2 PHE A 199     -20.245 -23.325  16.656  1.00 28.03           C  
ATOM   1416  CE1 PHE A 199     -21.602 -20.915  16.536  1.00 28.01           C  
ATOM   1417  CE2 PHE A 199     -19.652 -22.222  16.042  1.00 28.33           C  
ATOM   1418  CZ  PHE A 199     -20.330 -21.013  15.990  1.00 28.11           C  
ATOM   1419  N   ILE A 200     -23.716 -25.531  20.494  1.00 28.59           N  
ATOM   1420  CA  ILE A 200     -24.743 -26.546  20.758  1.00 31.01           C  
ATOM   1421  C   ILE A 200     -25.766 -26.441  19.623  1.00 28.78           C  
ATOM   1422  O   ILE A 200     -26.349 -25.381  19.429  1.00 28.54           O  
ATOM   1423  CB  ILE A 200     -25.491 -26.301  22.096  1.00 32.95           C  
ATOM   1424  CG1 ILE A 200     -24.519 -26.053  23.259  1.00 35.16           C  
ATOM   1425  CG2 ILE A 200     -26.465 -27.441  22.396  1.00 32.61           C  
ATOM   1426  CD1 ILE A 200     -23.622 -27.228  23.613  1.00 36.38           C  
ATOM   1427  N   ALA A 201     -25.998 -27.542  18.913  1.00 27.55           N  
ATOM   1428  CA  ALA A 201     -26.780 -27.549  17.667  1.00 28.29           C  
ATOM   1429  C   ALA A 201     -27.990 -28.509  17.638  1.00 28.41           C  
ATOM   1430  O   ALA A 201     -27.939 -29.626  18.171  1.00 28.33           O  
ATOM   1431  CB  ALA A 201     -25.864 -27.873  16.494  1.00 27.37           C  
ATOM   1432  N   ASP A 202     -29.053 -28.058  16.978  1.00 27.06           N  
ATOM   1433  CA  ASP A 202     -30.190 -28.888  16.610  1.00 26.69           C  
ATOM   1434  C   ASP A 202     -30.254 -28.983  15.104  1.00 27.62           C  
ATOM   1435  O   ASP A 202     -30.105 -27.975  14.379  1.00 26.83           O  
ATOM   1436  CB  ASP A 202     -31.500 -28.307  17.156  1.00 27.14           C  
ATOM   1437  CG  ASP A 202     -31.504 -28.221  18.665  1.00 27.87           C  
ATOM   1438  OD1 ASP A 202     -30.615 -28.842  19.269  1.00 27.29           O  
ATOM   1439  OD2 ASP A 202     -32.390 -27.550  19.246  1.00 29.66           O  
ATOM   1440  N   GLY A 203     -30.442 -30.204  14.629  1.00 26.93           N  
ATOM   1441  CA  GLY A 203     -30.565 -30.443  13.202  1.00 27.43           C  
ATOM   1442  C   GLY A 203     -31.934 -30.983  12.878  1.00 28.50           C  
ATOM   1443  O   GLY A 203     -32.486 -31.788  13.639  1.00 28.72           O  
ATOM   1444  N   ASP A 204     -32.472 -30.544  11.744  1.00 28.27           N  
ATOM   1445  CA  ASP A 204     -33.729 -31.052  11.222  1.00 29.23           C  
ATOM   1446  C   ASP A 204     -33.638 -31.287   9.720  1.00 30.22           C  
ATOM   1447  O   ASP A 204     -32.903 -30.603   9.012  1.00 31.67           O  
ATOM   1448  CB  ASP A 204     -34.887 -30.107  11.556  1.00 29.20           C  
ATOM   1449  CG  ASP A 204     -35.137 -30.007  13.043  1.00 29.89           C  
ATOM   1450  OD1 ASP A 204     -35.976 -30.782  13.560  1.00 32.15           O  
ATOM   1451  OD2 ASP A 204     -34.472 -29.180  13.709  1.00 28.55           O  
ATOM   1452  N   VAL A 205     -34.358 -32.290   9.240  1.00 29.52           N  
ATOM   1453  CA  VAL A 205     -34.428 -32.555   7.810  1.00 29.47           C  
ATOM   1454  C   VAL A 205     -35.889 -32.470   7.418  1.00 29.81           C  
ATOM   1455  O   VAL A 205     -36.747 -33.078   8.056  1.00 31.71           O  
ATOM   1456  CB  VAL A 205     -33.806 -33.927   7.433  1.00 29.37           C  
ATOM   1457  CG1 VAL A 205     -33.967 -34.233   5.941  1.00 27.70           C  
ATOM   1458  CG2 VAL A 205     -32.335 -33.966   7.814  1.00 27.14           C  
ATOM   1459  N   THR A 206     -36.171 -31.674   6.394  1.00 29.97           N  
ATOM   1460  CA  THR A 206     -37.536 -31.501   5.894  1.00 29.46           C  
ATOM   1461  C   THR A 206     -37.704 -32.273   4.594  1.00 28.99           C  
ATOM   1462  O   THR A 206     -36.716 -32.643   3.954  1.00 26.92           O  
ATOM   1463  CB  THR A 206     -37.862 -30.020   5.635  1.00 29.10           C  
ATOM   1464  OG1 THR A 206     -37.079 -29.548   4.536  1.00 29.73           O  
ATOM   1465  CG2 THR A 206     -37.572 -29.182   6.868  1.00 28.97           C  
ATOM   1466  N   ALA A 207     -38.952 -32.487   4.192  1.00 29.01           N  
ATOM   1467  CA  ALA A 207     -39.269 -33.323   3.035  1.00 30.08           C  
ATOM   1468  C   ALA A 207     -39.547 -32.533   1.752  1.00 30.41           C  
ATOM   1469  O   ALA A 207     -39.553 -33.106   0.660  1.00 31.30           O  
ATOM   1470  CB  ALA A 207     -40.461 -34.223   3.359  1.00 30.06           C  
ATOM   1471  N   SER A 208     -39.781 -31.228   1.888  1.00 30.79           N  
ATOM   1472  CA  SER A 208     -40.246 -30.394   0.779  1.00 30.73           C  
ATOM   1473  C   SER A 208     -40.017 -28.919   1.082  1.00 29.89           C  
ATOM   1474  O   SER A 208     -39.784 -28.545   2.235  1.00 31.34           O  
ATOM   1475  CB  SER A 208     -41.747 -30.585   0.593  1.00 30.66           C  
ATOM   1476  OG  SER A 208     -42.433 -30.046   1.710  1.00 29.26           O  
ATOM   1477  N   LEU A 209     -40.133 -28.090   0.049  1.00 29.32           N  
ATOM   1478  CA  LEU A 209     -40.076 -26.633   0.194  1.00 28.13           C  
ATOM   1479  C   LEU A 209     -41.097 -26.103   1.211  1.00 27.64           C  
ATOM   1480  O   LEU A 209     -40.764 -25.286   2.067  1.00 27.08           O  
ATOM   1481  CB  LEU A 209     -40.286 -25.970  -1.171  1.00 27.51           C  
ATOM   1482  CG  LEU A 209     -40.292 -24.436  -1.230  1.00 27.10           C  
ATOM   1483  CD1 LEU A 209     -38.968 -23.855  -0.767  1.00 26.60           C  
ATOM   1484  CD2 LEU A 209     -40.633 -23.990  -2.648  1.00 26.92           C  
ATOM   1485  N   ASP A 210     -42.335 -26.584   1.126  1.00 27.66           N  
ATOM   1486  CA  ASP A 210     -43.396 -26.127   2.041  1.00 28.01           C  
ATOM   1487  C   ASP A 210     -43.026 -26.394   3.484  1.00 27.84           C  
ATOM   1488  O   ASP A 210     -43.295 -25.576   4.361  1.00 26.45           O  
ATOM   1489  CB  ASP A 210     -44.735 -26.789   1.716  1.00 29.33           C  
ATOM   1490  CG  ASP A 210     -45.417 -26.168   0.501  1.00 31.65           C  
ATOM   1491  OD1 ASP A 210     -44.991 -25.077   0.040  1.00 31.42           O  
ATOM   1492  OD2 ASP A 210     -46.388 -26.777   0.004  1.00 32.09           O  
ATOM   1493  N   GLU A 211     -42.396 -27.540   3.713  1.00 28.07           N  
ATOM   1494  CA  GLU A 211     -41.932 -27.936   5.034  1.00 29.34           C  
ATOM   1495  C   GLU A 211     -40.769 -27.065   5.508  1.00 27.16           C  
ATOM   1496  O   GLU A 211     -40.705 -26.688   6.668  1.00 25.58           O  
ATOM   1497  CB  GLU A 211     -41.475 -29.382   4.966  1.00 31.78           C  
ATOM   1498  CG  GLU A 211     -41.440 -30.111   6.286  1.00 38.79           C  
ATOM   1499  CD  GLU A 211     -41.631 -31.596   6.058  1.00 42.85           C  
ATOM   1500  OE1 GLU A 211     -42.751 -31.986   5.637  1.00 45.20           O  
ATOM   1501  OE2 GLU A 211     -40.659 -32.352   6.265  1.00 41.04           O  
ATOM   1502  N   THR A 212     -39.842 -26.770   4.604  1.00 27.78           N  
ATOM   1503  CA  THR A 212     -38.700 -25.898   4.917  1.00 26.32           C  
ATOM   1504  C   THR A 212     -39.177 -24.513   5.330  1.00 26.07           C  
ATOM   1505  O   THR A 212     -38.696 -23.952   6.312  1.00 25.67           O  
ATOM   1506  CB  THR A 212     -37.749 -25.785   3.716  1.00 25.89           C  
ATOM   1507  OG1 THR A 212     -37.304 -27.095   3.354  1.00 25.17           O  
ATOM   1508  CG2 THR A 212     -36.537 -24.885   4.034  1.00 24.84           C  
ATOM   1509  N   ILE A 213     -40.127 -23.971   4.577  1.00 27.32           N  
ATOM   1510  CA  ILE A 213     -40.729 -22.683   4.899  1.00 28.02           C  
ATOM   1511  C   ILE A 213     -41.474 -22.697   6.245  1.00 28.27           C  
ATOM   1512  O   ILE A 213     -41.323 -21.770   7.046  1.00 28.33           O  
ATOM   1513  CB  ILE A 213     -41.605 -22.178   3.727  1.00 28.17           C  
ATOM   1514  CG1 ILE A 213     -40.694 -21.759   2.564  1.00 28.04           C  
ATOM   1515  CG2 ILE A 213     -42.512 -21.024   4.155  1.00 28.09           C  
ATOM   1516  CD1 ILE A 213     -41.393 -21.673   1.227  1.00 28.65           C  
ATOM   1517  N   ALA A 214     -42.252 -23.749   6.505  1.00 29.06           N  
ATOM   1518  CA  ALA A 214     -43.009 -23.838   7.769  1.00 28.44           C  
ATOM   1519  C   ALA A 214     -42.094 -23.831   9.007  1.00 29.07           C  
ATOM   1520  O   ALA A 214     -42.347 -23.109   9.981  1.00 29.68           O  
ATOM   1521  CB  ALA A 214     -43.924 -25.057   7.767  1.00 28.00           C  
ATOM   1522  N   LEU A 215     -41.020 -24.616   8.950  1.00 28.84           N  
ATOM   1523  CA  LEU A 215     -40.021 -24.660  10.012  1.00 30.16           C  
ATOM   1524  C   LEU A 215     -39.407 -23.283  10.293  1.00 30.53           C  
ATOM   1525  O   LEU A 215     -39.075 -22.970  11.434  1.00 31.43           O  
ATOM   1526  CB  LEU A 215     -38.922 -25.672   9.662  1.00 30.36           C  
ATOM   1527  CG  LEU A 215     -37.748 -25.842  10.636  1.00 30.63           C  
ATOM   1528  CD1 LEU A 215     -37.254 -27.279  10.641  1.00 30.73           C  
ATOM   1529  CD2 LEU A 215     -36.613 -24.887  10.293  1.00 30.96           C  
ATOM   1530  N   HIS A 216     -39.237 -22.473   9.253  1.00 30.41           N  
ATOM   1531  CA  HIS A 216     -38.654 -21.146   9.426  1.00 32.06           C  
ATOM   1532  C   HIS A 216     -39.679 -20.121   9.828  1.00 32.94           C  
ATOM   1533  O   HIS A 216     -39.325 -19.002  10.173  1.00 33.75           O  
ATOM   1534  CB  HIS A 216     -37.911 -20.713   8.165  1.00 30.09           C  
ATOM   1535  CG  HIS A 216     -36.594 -21.429   7.960  1.00 29.96           C  
ATOM   1536  ND1 HIS A 216     -36.511 -22.658   7.414  1.00 29.57           N  
ATOM   1537  CD2 HIS A 216     -35.286 -21.040   8.247  1.00 30.28           C  
ATOM   1538  CE1 HIS A 216     -35.225 -23.041   7.354  1.00 28.80           C  
ATOM   1539  NE2 HIS A 216     -34.473 -22.050   7.863  1.00 30.49           N  
ATOM   1540  N   SER A 217     -40.954 -20.507   9.809  1.00 34.01           N  
ATOM   1541  CA  SER A 217     -42.058 -19.588  10.078  1.00 34.21           C  
ATOM   1542  C   SER A 217     -42.858 -19.945  11.331  1.00 35.28           C  
ATOM   1543  O   SER A 217     -43.818 -19.261  11.660  1.00 38.23           O  
ATOM   1544  CB  SER A 217     -43.023 -19.552   8.893  1.00 34.17           C  
ATOM   1545  OG  SER A 217     -42.352 -19.397   7.664  1.00 33.03           O  
ATOM   1546  N   ASP A 218     -42.478 -21.006  12.030  1.00 34.59           N  
ATOM   1547  CA  ASP A 218     -43.266 -21.453  13.173  1.00 36.39           C  
ATOM   1548  C   ASP A 218     -42.834 -20.810  14.488  1.00 36.25           C  
ATOM   1549  O   ASP A 218     -43.333 -21.180  15.547  1.00 37.48           O  
ATOM   1550  CB  ASP A 218     -43.260 -22.993  13.282  1.00 37.43           C  
ATOM   1551  CG  ASP A 218     -41.897 -23.561  13.700  1.00 39.91           C  
ATOM   1552  OD1 ASP A 218     -41.050 -22.808  14.225  1.00 41.40           O  
ATOM   1553  OD2 ASP A 218     -41.670 -24.773  13.501  1.00 41.24           O  
ATOM   1554  N   GLY A 219     -41.893 -19.870  14.414  1.00 37.13           N  
ATOM   1555  CA  GLY A 219     -41.398 -19.167  15.596  1.00 32.86           C  
ATOM   1556  C   GLY A 219     -40.086 -19.707  16.143  1.00 33.28           C  
ATOM   1557  O   GLY A 219     -39.440 -19.056  16.963  1.00 32.25           O  
ATOM   1558  N   SER A 220     -39.671 -20.889  15.681  1.00 32.46           N  
ATOM   1559  CA  SER A 220     -38.500 -21.553  16.265  1.00 32.22           C  
ATOM   1560  C   SER A 220     -37.177 -20.823  16.018  1.00 31.99           C  
ATOM   1561  O   SER A 220     -36.212 -21.037  16.748  1.00 29.90           O  
ATOM   1562  CB  SER A 220     -38.400 -23.015  15.813  1.00 31.53           C  
ATOM   1563  OG  SER A 220     -38.328 -23.119  14.410  1.00 32.16           O  
ATOM   1564  N   GLU A 221     -37.141 -19.951  15.007  1.00 31.57           N  
ATOM   1565  CA  GLU A 221     -35.908 -19.227  14.667  1.00 32.03           C  
ATOM   1566  C   GLU A 221     -35.396 -18.347  15.813  1.00 31.94           C  
ATOM   1567  O   GLU A 221     -34.186 -18.195  15.995  1.00 31.20           O  
ATOM   1568  CB  GLU A 221     -36.077 -18.424  13.368  1.00 30.47           C  
ATOM   1569  CG  GLU A 221     -36.081 -19.308  12.125  1.00 30.27           C  
ATOM   1570  CD  GLU A 221     -34.686 -19.752  11.704  1.00 30.35           C  
ATOM   1571  OE1 GLU A 221     -34.366 -20.953  11.799  1.00 28.08           O  
ATOM   1572  OE2 GLU A 221     -33.891 -18.886  11.293  1.00 32.66           O  
ATOM   1573  N   ALA A 222     -36.325 -17.806  16.595  1.00 32.27           N  
ATOM   1574  CA  ALA A 222     -36.013 -16.968  17.753  1.00 33.17           C  
ATOM   1575  C   ALA A 222     -35.244 -17.684  18.875  1.00 33.47           C  
ATOM   1576  O   ALA A 222     -34.651 -17.037  19.735  1.00 33.64           O  
ATOM   1577  CB  ALA A 222     -37.290 -16.353  18.300  1.00 34.15           C  
ATOM   1578  N   ARG A 223     -35.244 -19.013  18.851  1.00 32.91           N  
ATOM   1579  CA  ARG A 223     -34.564 -19.814  19.872  1.00 32.84           C  
ATOM   1580  C   ARG A 223     -33.112 -20.130  19.499  1.00 31.62           C  
ATOM   1581  O   ARG A 223     -32.395 -20.773  20.265  1.00 30.78           O  
ATOM   1582  CB  ARG A 223     -35.350 -21.109  20.133  1.00 34.48           C  
ATOM   1583  CG  ARG A 223     -36.720 -20.840  20.748  1.00 38.56           C  
ATOM   1584  CD  ARG A 223     -37.387 -22.098  21.288  1.00 39.51           C  
ATOM   1585  NE  ARG A 223     -38.254 -22.747  20.301  1.00 43.62           N  
ATOM   1586  CZ  ARG A 223     -37.933 -23.843  19.612  1.00 43.82           C  
ATOM   1587  NH1 ARG A 223     -36.757 -24.430  19.781  1.00 45.08           N  
ATOM   1588  NH2 ARG A 223     -38.794 -24.355  18.747  1.00 43.44           N  
ATOM   1589  N   TYR A 224     -32.686 -19.659  18.327  1.00 29.00           N  
ATOM   1590  CA  TYR A 224     -31.351 -19.932  17.822  1.00 28.59           C  
ATOM   1591  C   TYR A 224     -30.676 -18.657  17.326  1.00 27.76           C  
ATOM   1592  O   TYR A 224     -31.239 -17.918  16.510  1.00 27.08           O  
ATOM   1593  CB  TYR A 224     -31.417 -20.929  16.664  1.00 28.19           C  
ATOM   1594  CG  TYR A 224     -32.044 -22.263  16.994  1.00 29.10           C  
ATOM   1595  CD1 TYR A 224     -31.303 -23.263  17.627  1.00 30.08           C  
ATOM   1596  CD2 TYR A 224     -33.370 -22.535  16.643  1.00 29.05           C  
ATOM   1597  CE1 TYR A 224     -31.867 -24.494  17.917  1.00 31.33           C  
ATOM   1598  CE2 TYR A 224     -33.950 -23.760  16.941  1.00 30.82           C  
ATOM   1599  CZ  TYR A 224     -33.190 -24.730  17.577  1.00 31.87           C  
ATOM   1600  OH  TYR A 224     -33.734 -25.945  17.864  1.00 32.15           O  
ATOM   1601  N   THR A 225     -29.464 -18.414  17.811  1.00 26.02           N  
ATOM   1602  CA  THR A 225     -28.692 -17.285  17.336  1.00 26.27           C  
ATOM   1603  C   THR A 225     -28.153 -17.577  15.932  1.00 25.57           C  
ATOM   1604  O   THR A 225     -27.979 -16.658  15.144  1.00 26.46           O  
ATOM   1605  CB  THR A 225     -27.548 -16.899  18.302  1.00 26.00           C  
ATOM   1606  OG1 THR A 225     -26.890 -18.080  18.774  1.00 25.39           O  
ATOM   1607  CG2 THR A 225     -28.084 -16.091  19.509  1.00 26.14           C  
ATOM   1608  N   TYR A 226     -27.919 -18.855  15.622  1.00 25.31           N  
ATOM   1609  CA  TYR A 226     -27.377 -19.261  14.317  1.00 24.46           C  
ATOM   1610  C   TYR A 226     -28.301 -20.241  13.595  1.00 24.03           C  
ATOM   1611  O   TYR A 226     -28.775 -21.211  14.196  1.00 23.45           O  
ATOM   1612  CB  TYR A 226     -26.007 -19.914  14.471  1.00 25.24           C  
ATOM   1613  CG  TYR A 226     -24.903 -19.004  14.946  1.00 25.92           C  
ATOM   1614  CD1 TYR A 226     -23.888 -18.590  14.077  1.00 24.51           C  
ATOM   1615  CD2 TYR A 226     -24.849 -18.581  16.273  1.00 24.88           C  
ATOM   1616  CE1 TYR A 226     -22.869 -17.765  14.524  1.00 24.60           C  
ATOM   1617  CE2 TYR A 226     -23.845 -17.745  16.716  1.00 25.49           C  
ATOM   1618  CZ  TYR A 226     -22.851 -17.351  15.841  1.00 25.76           C  
ATOM   1619  OH  TYR A 226     -21.846 -16.530  16.308  1.00 27.74           O  
ATOM   1620  N   SER A 227     -28.528 -20.003  12.304  1.00 22.55           N  
ATOM   1621  CA  SER A 227     -29.441 -20.834  11.512  1.00 24.04           C  
ATOM   1622  C   SER A 227     -29.157 -20.721  10.011  1.00 24.55           C  
ATOM   1623  O   SER A 227     -29.097 -19.615   9.466  1.00 24.25           O  
ATOM   1624  CB  SER A 227     -30.907 -20.448  11.831  1.00 23.61           C  
ATOM   1625  OG  SER A 227     -31.837 -21.276  11.151  1.00 25.85           O  
ATOM   1626  N   SER A 228     -28.925 -21.867   9.361  1.00 25.74           N  
ATOM   1627  CA  SER A 228     -28.846 -21.959   7.900  1.00 24.64           C  
ATOM   1628  C   SER A 228     -29.239 -23.366   7.457  1.00 25.94           C  
ATOM   1629  O   SER A 228     -29.358 -24.273   8.283  1.00 25.37           O  
ATOM   1630  CB  SER A 228     -27.440 -21.622   7.376  1.00 24.88           C  
ATOM   1631  OG  SER A 228     -26.496 -22.543   7.867  1.00 25.16           O  
ATOM   1632  N   ALA A 229     -29.415 -23.546   6.150  1.00 24.98           N  
ATOM   1633  CA  ALA A 229     -29.864 -24.818   5.609  1.00 25.35           C  
ATOM   1634  C   ALA A 229     -29.262 -25.067   4.223  1.00 26.88           C  
ATOM   1635  O   ALA A 229     -28.968 -24.119   3.484  1.00 27.46           O  
ATOM   1636  CB  ALA A 229     -31.387 -24.839   5.538  1.00 21.52           C  
ATOM   1637  N   TRP A 230     -29.062 -26.336   3.879  1.00 28.43           N  
ATOM   1638  CA  TRP A 230     -28.829 -26.700   2.482  1.00 31.22           C  
ATOM   1639  C   TRP A 230     -30.128 -27.197   1.929  1.00 30.60           C  
ATOM   1640  O   TRP A 230     -30.840 -27.945   2.604  1.00 31.09           O  
ATOM   1641  CB  TRP A 230     -27.750 -27.773   2.335  1.00 35.45           C  
ATOM   1642  CG  TRP A 230     -27.730 -28.373   0.943  1.00 39.85           C  
ATOM   1643  CD1 TRP A 230     -26.952 -27.971  -0.146  1.00 39.62           C  
ATOM   1644  CD2 TRP A 230     -28.572 -29.477   0.424  1.00 41.71           C  
ATOM   1645  NE1 TRP A 230     -27.231 -28.728  -1.256  1.00 42.44           N  
ATOM   1646  CE2 TRP A 230     -28.187 -29.656  -0.985  1.00 43.28           C  
ATOM   1647  CE3 TRP A 230     -29.558 -30.303   0.965  1.00 41.22           C  
ATOM   1648  CZ2 TRP A 230     -28.778 -30.628  -1.794  1.00 43.14           C  
ATOM   1649  CZ3 TRP A 230     -30.144 -31.279   0.140  1.00 42.99           C  
ATOM   1650  CH2 TRP A 230     -29.761 -31.436  -1.204  1.00 42.85           C  
ATOM   1651  N   PHE A 231     -30.467 -26.794   0.708  1.00 28.32           N  
ATOM   1652  CA  PHE A 231     -31.681 -27.294   0.096  1.00 28.56           C  
ATOM   1653  C   PHE A 231     -31.467 -27.943  -1.268  1.00 29.31           C  
ATOM   1654  O   PHE A 231     -30.450 -27.724  -1.935  1.00 28.13           O  
ATOM   1655  CB  PHE A 231     -32.801 -26.238   0.080  1.00 30.40           C  
ATOM   1656  CG  PHE A 231     -32.647 -25.186  -0.975  1.00 29.76           C  
ATOM   1657  CD1 PHE A 231     -33.297 -25.314  -2.201  1.00 29.22           C  
ATOM   1658  CD2 PHE A 231     -31.869 -24.056  -0.741  1.00 30.50           C  
ATOM   1659  CE1 PHE A 231     -33.163 -24.342  -3.180  1.00 30.43           C  
ATOM   1660  CE2 PHE A 231     -31.731 -23.076  -1.714  1.00 30.26           C  
ATOM   1661  CZ  PHE A 231     -32.379 -23.215  -2.934  1.00 30.27           C  
ATOM   1662  N   ASP A 232     -32.446 -28.748  -1.660  1.00 28.74           N  
ATOM   1663  CA  ASP A 232     -32.449 -29.449  -2.941  1.00 28.75           C  
ATOM   1664  C   ASP A 232     -33.097 -28.525  -3.986  1.00 26.97           C  
ATOM   1665  O   ASP A 232     -34.276 -28.199  -3.882  1.00 25.92           O  
ATOM   1666  CB  ASP A 232     -33.221 -30.767  -2.749  1.00 29.17           C  
ATOM   1667  CG  ASP A 232     -33.307 -31.627  -3.999  1.00 29.92           C  
ATOM   1668  OD1 ASP A 232     -33.050 -31.154  -5.126  1.00 29.94           O  
ATOM   1669  OD2 ASP A 232     -33.680 -32.809  -3.828  1.00 30.28           O  
ATOM   1670  N   ALA A 233     -32.299 -28.090  -4.964  1.00 26.57           N  
ATOM   1671  CA  ALA A 233     -32.749 -27.223  -6.065  1.00 27.79           C  
ATOM   1672  C   ALA A 233     -32.962 -27.964  -7.394  1.00 28.63           C  
ATOM   1673  O   ALA A 233     -33.291 -27.337  -8.408  1.00 27.09           O  
ATOM   1674  CB  ALA A 233     -31.751 -26.083  -6.278  1.00 27.74           C  
ATOM   1675  N   ILE A 234     -32.789 -29.285  -7.381  1.00 30.56           N  
ATOM   1676  CA  ILE A 234     -32.833 -30.096  -8.609  1.00 31.35           C  
ATOM   1677  C   ILE A 234     -34.070 -30.995  -8.719  1.00 32.68           C  
ATOM   1678  O   ILE A 234     -34.667 -31.102  -9.794  1.00 34.17           O  
ATOM   1679  CB  ILE A 234     -31.534 -30.917  -8.791  1.00 32.02           C  
ATOM   1680  CG1 ILE A 234     -30.353 -29.962  -8.994  1.00 31.93           C  
ATOM   1681  CG2 ILE A 234     -31.660 -31.895  -9.967  1.00 31.96           C  
ATOM   1682  CD1 ILE A 234     -28.990 -30.614  -8.924  1.00 32.87           C  
ATOM   1683  N   SER A 235     -34.457 -31.628  -7.615  1.00 32.66           N  
ATOM   1684  CA  SER A 235     -35.595 -32.548  -7.620  1.00 34.46           C  
ATOM   1685  C   SER A 235     -36.908 -31.856  -7.952  1.00 33.96           C  
ATOM   1686  O   SER A 235     -37.184 -30.747  -7.488  1.00 32.16           O  
ATOM   1687  CB  SER A 235     -35.741 -33.259  -6.274  1.00 33.19           C  
ATOM   1688  OG  SER A 235     -34.554 -33.943  -5.911  1.00 34.60           O  
ATOM   1689  N   ALA A 236     -37.719 -32.542  -8.747  1.00 34.02           N  
ATOM   1690  CA  ALA A 236     -39.082 -32.122  -9.022  1.00 34.85           C  
ATOM   1691  C   ALA A 236     -39.853 -31.964  -7.709  1.00 33.02           C  
ATOM   1692  O   ALA A 236     -39.521 -32.613  -6.718  1.00 31.48           O  
ATOM   1693  CB  ALA A 236     -39.763 -33.142  -9.932  1.00 34.98           C  
ATOM   1694  N   PRO A 237     -40.873 -31.084  -7.689  1.00 32.92           N  
ATOM   1695  CA  PRO A 237     -41.777 -31.059  -6.540  1.00 32.38           C  
ATOM   1696  C   PRO A 237     -42.442 -32.437  -6.402  1.00 32.89           C  
ATOM   1697  O   PRO A 237     -42.753 -33.052  -7.416  1.00 33.39           O  
ATOM   1698  CB  PRO A 237     -42.837 -30.022  -6.948  1.00 33.03           C  
ATOM   1699  CG  PRO A 237     -42.195 -29.200  -8.012  1.00 32.34           C  
ATOM   1700  CD  PRO A 237     -41.296 -30.146  -8.744  1.00 32.09           C  
ATOM   1701  N   PRO A 238     -42.720 -32.896  -5.167  1.00 32.66           N  
ATOM   1702  CA  PRO A 238     -42.620 -32.196  -3.887  1.00 31.11           C  
ATOM   1703  C   PRO A 238     -41.252 -32.240  -3.196  1.00 29.98           C  
ATOM   1704  O   PRO A 238     -41.067 -31.572  -2.187  1.00 29.52           O  
ATOM   1705  CB  PRO A 238     -43.669 -32.915  -3.031  1.00 32.27           C  
ATOM   1706  CG  PRO A 238     -43.646 -34.315  -3.542  1.00 32.32           C  
ATOM   1707  CD  PRO A 238     -43.326 -34.233  -5.012  1.00 32.03           C  
ATOM   1708  N   LYS A 239     -40.305 -33.007  -3.726  1.00 29.05           N  
ATOM   1709  CA  LYS A 239     -38.980 -33.081  -3.125  1.00 30.12           C  
ATOM   1710  C   LYS A 239     -38.237 -31.742  -3.221  1.00 28.14           C  
ATOM   1711  O   LYS A 239     -37.480 -31.394  -2.321  1.00 26.71           O  
ATOM   1712  CB  LYS A 239     -38.153 -34.212  -3.746  1.00 32.68           C  
ATOM   1713  CG  LYS A 239     -38.668 -35.608  -3.412  1.00 37.23           C  
ATOM   1714  CD  LYS A 239     -37.846 -36.671  -4.125  1.00 40.43           C  
ATOM   1715  CE  LYS A 239     -38.454 -38.055  -3.962  1.00 42.98           C  
ATOM   1716  NZ  LYS A 239     -38.478 -38.444  -2.525  1.00 46.28           N  
ATOM   1717  N   LEU A 240     -38.466 -31.005  -4.309  1.00 26.64           N  
ATOM   1718  CA  LEU A 240     -37.952 -29.631  -4.462  1.00 26.28           C  
ATOM   1719  C   LEU A 240     -38.008 -28.839  -3.170  1.00 25.47           C  
ATOM   1720  O   LEU A 240     -39.077 -28.695  -2.567  1.00 24.34           O  
ATOM   1721  CB  LEU A 240     -38.740 -28.857  -5.529  1.00 25.94           C  
ATOM   1722  CG  LEU A 240     -38.255 -27.402  -5.746  1.00 25.59           C  
ATOM   1723  CD1 LEU A 240     -36.777 -27.384  -6.116  1.00 23.80           C  
ATOM   1724  CD2 LEU A 240     -39.089 -26.721  -6.823  1.00 25.29           C  
ATOM   1725  N   GLY A 241     -36.857 -28.329  -2.746  1.00 25.88           N  
ATOM   1726  CA  GLY A 241     -36.812 -27.442  -1.583  1.00 27.44           C  
ATOM   1727  C   GLY A 241     -36.769 -28.133  -0.228  1.00 28.16           C  
ATOM   1728  O   GLY A 241     -36.849 -27.459   0.820  1.00 26.90           O  
ATOM   1729  N   ARG A 242     -36.635 -29.464  -0.238  1.00 26.52           N  
ATOM   1730  CA  ARG A 242     -36.301 -30.198   0.987  1.00 27.69           C  
ATOM   1731  C   ARG A 242     -34.918 -29.746   1.451  1.00 26.88           C  
ATOM   1732  O   ARG A 242     -34.106 -29.283   0.637  1.00 30.09           O  
ATOM   1733  CB  ARG A 242     -36.360 -31.718   0.782  1.00 29.41           C  
ATOM   1734  CG  ARG A 242     -35.284 -32.301  -0.122  1.00 30.76           C  
ATOM   1735  CD  ARG A 242     -35.632 -33.738  -0.477  1.00 32.32           C  
ATOM   1736  NE  ARG A 242     -34.771 -34.274  -1.527  1.00 34.77           N  
ATOM   1737  CZ  ARG A 242     -34.610 -35.572  -1.782  1.00 38.03           C  
ATOM   1738  NH1 ARG A 242     -35.248 -36.495  -1.065  1.00 39.69           N  
ATOM   1739  NH2 ARG A 242     -33.807 -35.952  -2.760  1.00 40.45           N  
ATOM   1740  N   ALA A 243     -34.641 -29.880   2.739  1.00 25.28           N  
ATOM   1741  CA  ALA A 243     -33.504 -29.188   3.333  1.00 25.58           C  
ATOM   1742  C   ALA A 243     -32.896 -29.945   4.499  1.00 25.57           C  
ATOM   1743  O   ALA A 243     -33.614 -30.622   5.237  1.00 26.11           O  
ATOM   1744  CB  ALA A 243     -33.947 -27.802   3.806  1.00 24.70           C  
ATOM   1745  N   ALA A 244     -31.580 -29.818   4.666  1.00 24.55           N  
ATOM   1746  CA  ALA A 244     -30.932 -30.158   5.934  1.00 24.95           C  
ATOM   1747  C   ALA A 244     -30.630 -28.844   6.669  1.00 25.30           C  
ATOM   1748  O   ALA A 244     -29.827 -28.017   6.200  1.00 24.18           O  
ATOM   1749  CB  ALA A 244     -29.669 -30.969   5.711  1.00 25.14           C  
ATOM   1750  N   VAL A 245     -31.311 -28.649   7.795  1.00 23.01           N  
ATOM   1751  CA  VAL A 245     -31.249 -27.410   8.562  1.00 23.40           C  
ATOM   1752  C   VAL A 245     -30.334 -27.603   9.757  1.00 24.60           C  
ATOM   1753  O   VAL A 245     -30.436 -28.605  10.492  1.00 23.87           O  
ATOM   1754  CB  VAL A 245     -32.666 -26.996   9.071  1.00 23.04           C  
ATOM   1755  CG1 VAL A 245     -32.665 -25.556   9.568  1.00 22.73           C  
ATOM   1756  CG2 VAL A 245     -33.708 -27.161   7.968  1.00 21.82           C  
ATOM   1757  N   SER A 246     -29.440 -26.643   9.959  1.00 24.12           N  
ATOM   1758  CA  SER A 246     -28.517 -26.687  11.080  1.00 26.22           C  
ATOM   1759  C   SER A 246     -28.703 -25.408  11.896  1.00 27.27           C  
ATOM   1760  O   SER A 246     -28.517 -24.310  11.370  1.00 26.76           O  
ATOM   1761  CB  SER A 246     -27.079 -26.816  10.555  1.00 26.92           C  
ATOM   1762  OG  SER A 246     -26.124 -26.438  11.533  1.00 30.98           O  
ATOM   1763  N   ARG A 247     -29.101 -25.544  13.160  1.00 26.37           N  
ATOM   1764  CA  ARG A 247     -29.357 -24.364  14.001  1.00 26.36           C  
ATOM   1765  C   ARG A 247     -28.725 -24.536  15.371  1.00 26.42           C  
ATOM   1766  O   ARG A 247     -28.709 -25.632  15.923  1.00 28.67           O  
ATOM   1767  CB  ARG A 247     -30.866 -24.086  14.131  1.00 25.74           C  
ATOM   1768  CG  ARG A 247     -31.638 -24.201  12.822  1.00 27.02           C  
ATOM   1769  CD  ARG A 247     -33.051 -23.642  12.913  1.00 27.86           C  
ATOM   1770  NE  ARG A 247     -34.064 -24.565  13.444  1.00 27.62           N  
ATOM   1771  CZ  ARG A 247     -35.349 -24.241  13.568  1.00 29.01           C  
ATOM   1772  NH1 ARG A 247     -35.757 -23.025  13.205  1.00 27.09           N  
ATOM   1773  NH2 ARG A 247     -36.230 -25.115  14.062  1.00 27.76           N  
ATOM   1774  N   GLY A 248     -28.187 -23.461  15.924  1.00 26.00           N  
ATOM   1775  CA  GLY A 248     -27.596 -23.549  17.249  1.00 27.01           C  
ATOM   1776  C   GLY A 248     -27.291 -22.217  17.895  1.00 26.88           C  
ATOM   1777  O   GLY A 248     -27.835 -21.179  17.504  1.00 25.67           O  
ATOM   1778  N   ARG A 249     -26.417 -22.279  18.896  1.00 27.97           N  
ATOM   1779  CA  ARG A 249     -25.911 -21.119  19.617  1.00 28.47           C  
ATOM   1780  C   ARG A 249     -24.554 -21.504  20.175  1.00 27.87           C  
ATOM   1781  O   ARG A 249     -24.253 -22.691  20.304  1.00 27.41           O  
ATOM   1782  CB  ARG A 249     -26.870 -20.730  20.753  1.00 31.37           C  
ATOM   1783  CG  ARG A 249     -26.977 -21.770  21.856  1.00 34.70           C  
ATOM   1784  CD  ARG A 249     -28.207 -21.548  22.733  1.00 37.59           C  
ATOM   1785  NE  ARG A 249     -29.459 -21.753  21.994  1.00 43.52           N  
ATOM   1786  CZ  ARG A 249     -29.968 -22.943  21.650  1.00 45.44           C  
ATOM   1787  NH1 ARG A 249     -29.337 -24.077  21.961  1.00 45.29           N  
ATOM   1788  NH2 ARG A 249     -31.115 -23.001  20.981  1.00 44.18           N  
ATOM   1789  N   LEU A 250     -23.729 -20.515  20.505  1.00 27.13           N  
ATOM   1790  CA  LEU A 250     -22.442 -20.798  21.131  1.00 28.71           C  
ATOM   1791  C   LEU A 250     -22.663 -21.531  22.446  1.00 29.19           C  
ATOM   1792  O   LEU A 250     -23.584 -21.200  23.180  1.00 29.30           O  
ATOM   1793  CB  LEU A 250     -21.668 -19.516  21.389  1.00 27.31           C  
ATOM   1794  CG  LEU A 250     -21.166 -18.804  20.140  1.00 28.05           C  
ATOM   1795  CD1 LEU A 250     -20.846 -17.371  20.516  1.00 27.03           C  
ATOM   1796  CD2 LEU A 250     -19.947 -19.536  19.582  1.00 27.43           C  
ATOM   1797  N   ALA A 251     -21.831 -22.534  22.716  1.00 28.94           N  
ATOM   1798  CA  ALA A 251     -21.921 -23.319  23.950  1.00 31.61           C  
ATOM   1799  C   ALA A 251     -21.315 -22.542  25.119  1.00 32.17           C  
ATOM   1800  O   ALA A 251     -20.431 -21.713  24.912  1.00 28.95           O  
ATOM   1801  CB  ALA A 251     -21.193 -24.645  23.777  1.00 30.89           C  
ATOM   1802  N   THR A 252     -21.807 -22.808  26.331  1.00 32.70           N  
ATOM   1803  CA  THR A 252     -21.132 -22.376  27.562  1.00 35.46           C  
ATOM   1804  C   THR A 252     -20.259 -23.520  28.058  1.00 36.40           C  
ATOM   1805  O   THR A 252     -20.479 -24.673  27.686  1.00 37.89           O  
ATOM   1806  CB  THR A 252     -22.116 -22.004  28.694  1.00 36.98           C  
ATOM   1807  OG1 THR A 252     -22.878 -23.160  29.063  1.00 37.51           O  
ATOM   1808  CG2 THR A 252     -23.043 -20.868  28.282  1.00 35.57           C  
ATOM   1809  N   VAL A 253     -19.277 -23.198  28.900  1.00 38.22           N  
ATOM   1810  CA  VAL A 253     -18.319 -24.184  29.417  1.00 39.61           C  
ATOM   1811  C   VAL A 253     -18.988 -25.434  30.008  1.00 39.09           C  
ATOM   1812  O   VAL A 253     -18.600 -26.552  29.671  1.00 37.99           O  
ATOM   1813  CB  VAL A 253     -17.329 -23.561  30.429  1.00 40.37           C  
ATOM   1814  CG1 VAL A 253     -16.514 -24.638  31.136  1.00 40.88           C  
ATOM   1815  CG2 VAL A 253     -16.403 -22.584  29.724  1.00 40.57           C  
ATOM   1816  N   GLU A 254     -19.999 -25.252  30.854  1.00 40.88           N  
ATOM   1817  CA  GLU A 254     -20.652 -26.402  31.498  1.00 44.27           C  
ATOM   1818  C   GLU A 254     -21.420 -27.306  30.521  1.00 45.03           C  
ATOM   1819  O   GLU A 254     -21.685 -28.463  30.835  1.00 44.71           O  
ATOM   1820  CB  GLU A 254     -21.519 -25.980  32.703  1.00 47.44           C  
ATOM   1821  CG  GLU A 254     -22.733 -25.118  32.392  1.00 52.61           C  
ATOM   1822  CD  GLU A 254     -22.406 -23.641  32.215  1.00 57.20           C  
ATOM   1823  OE1 GLU A 254     -21.270 -23.219  32.543  1.00 59.20           O  
ATOM   1824  OE2 GLU A 254     -23.297 -22.894  31.745  1.00 57.15           O  
ATOM   1825  N   GLN A 255     -21.735 -26.791  29.329  1.00 42.34           N  
ATOM   1826  CA  GLN A 255     -22.403 -27.582  28.295  1.00 41.27           C  
ATOM   1827  C   GLN A 255     -21.441 -28.477  27.520  1.00 42.04           C  
ATOM   1828  O   GLN A 255     -21.859 -29.320  26.731  1.00 43.72           O  
ATOM   1829  CB  GLN A 255     -23.168 -26.676  27.334  1.00 41.89           C  
ATOM   1830  CG  GLN A 255     -24.376 -25.990  27.958  1.00 39.10           C  
ATOM   1831  CD  GLN A 255     -25.042 -25.022  27.000  1.00 40.99           C  
ATOM   1832  OE1 GLN A 255     -24.390 -24.152  26.420  1.00 40.25           O  
ATOM   1833  NE2 GLN A 255     -26.348 -25.172  26.825  1.00 40.80           N  
ATOM   1834  N   LEU A 256     -20.148 -28.293  27.747  1.00 41.52           N  
ATOM   1835  CA  LEU A 256     -19.143 -29.149  27.141  1.00 42.32           C  
ATOM   1836  C   LEU A 256     -19.021 -30.445  27.939  1.00 43.55           C  
ATOM   1837  O   LEU A 256     -19.176 -30.433  29.158  1.00 43.01           O  
ATOM   1838  CB  LEU A 256     -17.794 -28.426  27.126  1.00 41.55           C  
ATOM   1839  CG  LEU A 256     -17.394 -27.446  26.004  1.00 42.06           C  
ATOM   1840  CD1 LEU A 256     -18.530 -26.988  25.092  1.00 40.37           C  
ATOM   1841  CD2 LEU A 256     -16.657 -26.263  26.604  1.00 40.30           C  
ATOM   1842  N   PRO A 257     -18.742 -31.571  27.259  1.00 45.24           N  
ATOM   1843  CA  PRO A 257     -18.338 -32.761  28.008  1.00 47.44           C  
ATOM   1844  C   PRO A 257     -17.037 -32.475  28.761  1.00 49.06           C  
ATOM   1845  O   PRO A 257     -16.245 -31.636  28.308  1.00 48.00           O  
ATOM   1846  CB  PRO A 257     -18.103 -33.806  26.912  1.00 47.05           C  
ATOM   1847  CG  PRO A 257     -17.935 -33.028  25.648  1.00 47.44           C  
ATOM   1848  CD  PRO A 257     -18.813 -31.829  25.812  1.00 45.35           C  
ATOM   1849  N   ALA A 258     -16.824 -33.155  29.891  1.00 47.32           N  
ATOM   1850  CA  ALA A 258     -15.657 -32.906  30.754  1.00 48.42           C  
ATOM   1851  C   ALA A 258     -14.326 -32.906  29.987  1.00 48.50           C  
ATOM   1852  O   ALA A 258     -13.446 -32.087  30.255  1.00 48.63           O  
ATOM   1853  CB  ALA A 258     -15.621 -33.902  31.902  1.00 48.53           C  
ATOM   1854  N   LYS A 259     -14.219 -33.811  29.019  1.00 49.30           N  
ATOM   1855  CA  LYS A 259     -13.070 -33.932  28.121  1.00 51.61           C  
ATOM   1856  C   LYS A 259     -12.626 -32.600  27.507  1.00 52.84           C  
ATOM   1857  O   LYS A 259     -11.428 -32.339  27.379  1.00 53.66           O  
ATOM   1858  CB  LYS A 259     -13.426 -34.909  27.000  1.00 53.35           C  
ATOM   1859  CG  LYS A 259     -12.254 -35.605  26.338  1.00 54.45           C  
ATOM   1860  CD  LYS A 259     -12.743 -36.389  25.128  1.00 57.62           C  
ATOM   1861  CE  LYS A 259     -11.810 -37.537  24.780  1.00 60.93           C  
ATOM   1862  NZ  LYS A 259     -11.807 -38.600  25.827  1.00 63.46           N  
ATOM   1863  N   LEU A 260     -13.594 -31.764  27.134  1.00 51.46           N  
ATOM   1864  CA  LEU A 260     -13.315 -30.508  26.430  1.00 52.29           C  
ATOM   1865  C   LEU A 260     -13.266 -29.281  27.340  1.00 52.78           C  
ATOM   1866  O   LEU A 260     -12.910 -28.185  26.887  1.00 52.13           O  
ATOM   1867  CB  LEU A 260     -14.350 -30.288  25.323  1.00 51.96           C  
ATOM   1868  CG  LEU A 260     -14.119 -30.813  23.902  1.00 53.76           C  
ATOM   1869  CD1 LEU A 260     -13.551 -32.224  23.833  1.00 54.58           C  
ATOM   1870  CD2 LEU A 260     -15.420 -30.717  23.120  1.00 54.74           C  
ATOM   1871  N   ARG A 261     -13.618 -29.467  28.614  1.00 51.95           N  
ATOM   1872  CA  ARG A 261     -13.715 -28.360  29.571  1.00 50.86           C  
ATOM   1873  C   ARG A 261     -12.397 -27.714  29.978  1.00 49.40           C  
ATOM   1874  O   ARG A 261     -12.390 -26.574  30.445  1.00 47.81           O  
ATOM   1875  CB  ARG A 261     -14.453 -28.796  30.830  1.00 51.57           C  
ATOM   1876  CG  ARG A 261     -15.937 -28.537  30.766  1.00 52.38           C  
ATOM   1877  CD  ARG A 261     -16.576 -28.694  32.129  1.00 53.12           C  
ATOM   1878  NE  ARG A 261     -17.988 -29.013  31.973  1.00 55.83           N  
ATOM   1879  CZ  ARG A 261     -18.514 -30.215  32.182  1.00 54.32           C  
ATOM   1880  NH1 ARG A 261     -17.751 -31.222  32.585  1.00 52.38           N  
ATOM   1881  NH2 ARG A 261     -19.811 -30.405  31.993  1.00 54.83           N  
ATOM   1882  N   SER A 262     -11.295 -28.444  29.824  1.00 49.53           N  
ATOM   1883  CA  SER A 262      -9.981 -27.927  30.209  1.00 50.81           C  
ATOM   1884  C   SER A 262      -9.452 -26.884  29.221  1.00 49.19           C  
ATOM   1885  O   SER A 262      -8.686 -26.002  29.603  1.00 53.76           O  
ATOM   1886  CB  SER A 262      -8.977 -29.067  30.386  1.00 52.48           C  
ATOM   1887  OG  SER A 262      -8.816 -29.788  29.178  1.00 55.67           O  
ATOM   1888  N   GLU A 263      -9.861 -26.983  27.959  1.00 45.28           N  
ATOM   1889  CA  GLU A 263      -9.523 -25.964  26.963  1.00 44.80           C  
ATOM   1890  C   GLU A 263     -10.781 -25.512  26.226  1.00 38.08           C  
ATOM   1891  O   GLU A 263     -10.997 -25.903  25.087  1.00 35.27           O  
ATOM   1892  CB  GLU A 263      -8.488 -26.496  25.967  1.00 48.57           C  
ATOM   1893  CG  GLU A 263      -7.180 -26.953  26.597  1.00 58.23           C  
ATOM   1894  CD  GLU A 263      -6.086 -27.201  25.572  1.00 64.03           C  
ATOM   1895  OE1 GLU A 263      -4.907 -26.932  25.895  1.00 67.50           O  
ATOM   1896  OE2 GLU A 263      -6.400 -27.648  24.444  1.00 67.12           O  
ATOM   1897  N   PRO A 264     -11.624 -24.688  26.873  1.00 35.98           N  
ATOM   1898  CA  PRO A 264     -12.915 -24.475  26.207  1.00 35.93           C  
ATOM   1899  C   PRO A 264     -12.838 -23.560  24.979  1.00 34.01           C  
ATOM   1900  O   PRO A 264     -13.680 -23.654  24.094  1.00 33.64           O  
ATOM   1901  CB  PRO A 264     -13.797 -23.875  27.308  1.00 34.76           C  
ATOM   1902  CG  PRO A 264     -12.851 -23.322  28.321  1.00 35.23           C  
ATOM   1903  CD  PRO A 264     -11.568 -24.085  28.217  1.00 35.01           C  
ATOM   1904  N   LEU A 265     -11.809 -22.722  24.926  1.00 33.41           N  
ATOM   1905  CA  LEU A 265     -11.671 -21.703  23.885  1.00 36.05           C  
ATOM   1906  C   LEU A 265     -10.734 -22.124  22.755  1.00 39.33           C  
ATOM   1907  O   LEU A 265     -10.377 -21.315  21.899  1.00 43.68           O  
ATOM   1908  CB  LEU A 265     -11.216 -20.378  24.510  1.00 32.56           C  
ATOM   1909  CG  LEU A 265     -12.284 -19.727  25.401  1.00 32.12           C  
ATOM   1910  CD1 LEU A 265     -11.668 -18.754  26.391  1.00 31.76           C  
ATOM   1911  CD2 LEU A 265     -13.353 -19.041  24.564  1.00 31.06           C  
ATOM   1912  N   LYS A 266     -10.372 -23.402  22.734  1.00 42.51           N  
ATOM   1913  CA  LYS A 266      -9.405 -23.920  21.774  1.00 46.39           C  
ATOM   1914  C   LYS A 266     -10.025 -24.132  20.401  1.00 47.21           C  
ATOM   1915  O   LYS A 266     -11.137 -24.638  20.295  1.00 44.18           O  
ATOM   1916  CB  LYS A 266      -8.822 -25.243  22.289  1.00 50.00           C  
ATOM   1917  CG  LYS A 266      -7.353 -25.480  21.948  1.00 52.37           C  
ATOM   1918  CD  LYS A 266      -6.443 -24.351  22.431  1.00 54.60           C  
ATOM   1919  CE  LYS A 266      -6.396 -24.250  23.949  1.00 54.53           C  
ATOM   1920  NZ  LYS A 266      -5.910 -22.915  24.394  1.00 57.67           N  
ATOM   1921  N   PHE A 267      -9.314 -23.737  19.350  1.00 49.35           N  
ATOM   1922  CA  PHE A 267      -9.708 -24.162  18.011  1.00 58.10           C  
ATOM   1923  C   PHE A 267      -8.904 -25.382  17.558  1.00 59.40           C  
ATOM   1924  O   PHE A 267      -7.673 -25.360  17.555  1.00 60.76           O  
ATOM   1925  CB  PHE A 267      -9.610 -23.036  16.981  1.00 61.19           C  
ATOM   1926  CG  PHE A 267      -9.971 -23.476  15.590  1.00 64.72           C  
ATOM   1927  CD1 PHE A 267      -9.024 -23.456  14.570  1.00 66.42           C  
ATOM   1928  CD2 PHE A 267     -11.252 -23.954  15.307  1.00 66.91           C  
ATOM   1929  CE1 PHE A 267      -9.354 -23.878  13.287  1.00 67.22           C  
ATOM   1930  CE2 PHE A 267     -11.587 -24.378  14.029  1.00 69.00           C  
ATOM   1931  CZ  PHE A 267     -10.636 -24.338  13.017  1.00 67.62           C  
ATOM   1932  N   ASP A 268      -9.619 -26.441  17.183  1.00 64.85           N  
ATOM   1933  CA  ASP A 268      -9.006 -27.696  16.738  1.00 66.69           C  
ATOM   1934  C   ASP A 268      -8.432 -27.537  15.336  1.00 68.74           C  
ATOM   1935  O   ASP A 268      -8.993 -26.812  14.508  1.00 70.57           O  
ATOM   1936  CB  ASP A 268     -10.026 -28.845  16.728  1.00 68.30           C  
ATOM   1937  CG  ASP A 268     -11.363 -28.463  17.347  1.00 69.01           C  
ATOM   1938  OD1 ASP A 268     -11.962 -27.457  16.904  1.00 67.12           O  
ATOM   1939  OD2 ASP A 268     -11.827 -29.186  18.257  1.00 67.49           O  
ATOM   1940  N   ALA A 269      -7.322 -28.223  15.074  1.00 71.46           N  
ATOM   1941  CA  ALA A 269      -6.698 -28.228  13.750  1.00 72.64           C  
ATOM   1942  C   ALA A 269      -7.597 -28.922  12.718  1.00 72.97           C  
ATOM   1943  O   ALA A 269      -8.059 -30.043  12.963  1.00 69.38           O  
ATOM   1944  CB  ALA A 269      -5.333 -28.907  13.812  1.00 71.69           C  
ATOM   1945  N   PRO A 270      -7.875 -28.244  11.579  1.00 75.58           N  
ATOM   1946  CA  PRO A 270      -8.535 -28.907  10.449  1.00 75.74           C  
ATOM   1947  C   PRO A 270      -7.743 -30.149  10.053  1.00 76.94           C  
ATOM   1948  O   PRO A 270      -6.621 -30.024   9.559  1.00 77.82           O  
ATOM   1949  CB  PRO A 270      -8.469 -27.853   9.339  1.00 75.25           C  
ATOM   1950  CG  PRO A 270      -8.462 -26.551  10.064  1.00 74.13           C  
ATOM   1951  CD  PRO A 270      -7.704 -26.795  11.342  1.00 75.11           C  
ATOM   1952  N   GLN A 271      -8.318 -31.329  10.289  1.00 74.90           N  
ATOM   1953  CA  GLN A 271      -7.601 -32.603  10.120  1.00 74.76           C  
ATOM   1954  C   GLN A 271      -7.193 -32.915   8.671  1.00 73.39           C  
ATOM   1955  O   GLN A 271      -7.620 -32.236   7.730  1.00 72.74           O  
ATOM   1956  CB  GLN A 271      -8.381 -33.769  10.747  1.00 74.93           C  
ATOM   1957  CG  GLN A 271      -9.768 -34.004  10.167  1.00 76.86           C  
ATOM   1958  CD  GLN A 271     -10.663 -34.801  11.099  1.00 79.43           C  
ATOM   1959  OE1 GLN A 271     -11.207 -35.838  10.718  1.00 81.22           O  
ATOM   1960  NE2 GLN A 271     -10.821 -34.320  12.329  1.00 79.88           N  
ATOM   1961  N   LEU A 272      -6.361 -33.943   8.512  1.00 71.07           N  
ATOM   1962  CA  LEU A 272      -5.740 -34.264   7.226  1.00 70.17           C  
ATOM   1963  C   LEU A 272      -6.737 -34.811   6.204  1.00 68.35           C  
ATOM   1964  O   LEU A 272      -6.916 -34.232   5.127  1.00 66.08           O  
ATOM   1965  CB  LEU A 272      -4.593 -35.268   7.415  1.00 68.32           C  
ATOM   1966  CG  LEU A 272      -3.265 -35.053   6.670  1.00 68.49           C  
ATOM   1967  CD1 LEU A 272      -2.670 -36.388   6.248  1.00 66.90           C  
ATOM   1968  CD2 LEU A 272      -3.370 -34.098   5.486  1.00 66.98           C  
ATOM   1969  N   LEU A 273      -7.378 -35.924   6.554  1.00 65.81           N  
ATOM   1970  CA  LEU A 273      -8.243 -36.648   5.632  1.00 65.00           C  
ATOM   1971  C   LEU A 273      -9.636 -36.034   5.537  1.00 64.88           C  
ATOM   1972  O   LEU A 273     -10.274 -35.748   6.553  1.00 65.99           O  
ATOM   1973  CB  LEU A 273      -8.342 -38.128   6.028  1.00 63.47           C  
ATOM   1974  CG  LEU A 273      -7.052 -38.950   6.150  1.00 63.24           C  
ATOM   1975  CD1 LEU A 273      -7.364 -40.359   6.630  1.00 62.22           C  
ATOM   1976  CD2 LEU A 273      -6.278 -38.992   4.840  1.00 62.19           C  
ATOM   1977  N   THR A 274     -10.079 -35.825   4.299  1.00 62.09           N  
ATOM   1978  CA  THR A 274     -11.454 -35.436   3.996  1.00 59.98           C  
ATOM   1979  C   THR A 274     -12.154 -36.638   3.356  1.00 60.02           C  
ATOM   1980  O   THR A 274     -11.516 -37.665   3.093  1.00 57.59           O  
ATOM   1981  CB  THR A 274     -11.514 -34.208   3.058  1.00 57.66           C  
ATOM   1982  OG1 THR A 274     -10.889 -34.520   1.806  1.00 58.64           O  
ATOM   1983  CG2 THR A 274     -10.809 -33.012   3.686  1.00 58.41           C  
ATOM   1984  N   LEU A 275     -13.457 -36.515   3.105  1.00 59.12           N  
ATOM   1985  CA  LEU A 275     -14.240 -37.626   2.553  1.00 57.86           C  
ATOM   1986  C   LEU A 275     -13.761 -38.171   1.186  1.00 58.39           C  
ATOM   1987  O   LEU A 275     -13.771 -39.389   0.987  1.00 57.29           O  
ATOM   1988  CB  LEU A 275     -15.742 -37.305   2.544  1.00 58.17           C  
ATOM   1989  CG  LEU A 275     -16.450 -37.267   3.909  1.00 59.21           C  
ATOM   1990  CD1 LEU A 275     -17.832 -36.647   3.769  1.00 59.17           C  
ATOM   1991  CD2 LEU A 275     -16.546 -38.645   4.559  1.00 58.67           C  
ATOM   1992  N   PRO A 276     -13.341 -37.284   0.247  1.00 58.22           N  
ATOM   1993  CA  PRO A 276     -12.773 -37.784  -1.018  1.00 59.04           C  
ATOM   1994  C   PRO A 276     -11.544 -38.672  -0.826  1.00 59.59           C  
ATOM   1995  O   PRO A 276     -11.303 -39.579  -1.631  1.00 61.80           O  
ATOM   1996  CB  PRO A 276     -12.374 -36.505  -1.757  1.00 57.67           C  
ATOM   1997  CG  PRO A 276     -13.297 -35.471  -1.229  1.00 58.41           C  
ATOM   1998  CD  PRO A 276     -13.516 -35.818   0.216  1.00 57.86           C  
ATOM   1999  N   ASP A 277     -10.779 -38.405   0.228  1.00 58.19           N  
ATOM   2000  CA  ASP A 277      -9.600 -39.205   0.550  1.00 59.17           C  
ATOM   2001  C   ASP A 277      -9.998 -40.587   1.060  1.00 59.84           C  
ATOM   2002  O   ASP A 277      -9.375 -41.585   0.693  1.00 62.87           O  
ATOM   2003  CB  ASP A 277      -8.716 -38.484   1.575  1.00 55.92           C  
ATOM   2004  CG  ASP A 277      -8.436 -37.040   1.192  1.00 54.23           C  
ATOM   2005  OD1 ASP A 277      -8.175 -36.765   0.000  1.00 51.75           O  
ATOM   2006  OD2 ASP A 277      -8.482 -36.176   2.088  1.00 56.03           O  
ATOM   2007  N   VAL A 278     -11.047 -40.639   1.879  1.00 58.96           N  
ATOM   2008  CA  VAL A 278     -11.494 -41.893   2.499  1.00 60.39           C  
ATOM   2009  C   VAL A 278     -12.413 -42.714   1.587  1.00 59.89           C  
ATOM   2010  O   VAL A 278     -12.316 -43.942   1.547  1.00 58.83           O  
ATOM   2011  CB  VAL A 278     -12.164 -41.653   3.873  1.00 59.67           C  
ATOM   2012  CG1 VAL A 278     -12.461 -42.978   4.564  1.00 60.88           C  
ATOM   2013  CG2 VAL A 278     -11.269 -40.796   4.760  1.00 60.16           C  
ATOM   2014  N   PHE A 279     -13.295 -42.040   0.854  1.00 60.04           N  
ATOM   2015  CA  PHE A 279     -14.195 -42.724  -0.076  1.00 62.51           C  
ATOM   2016  C   PHE A 279     -14.059 -42.143  -1.488  1.00 64.54           C  
ATOM   2017  O   PHE A 279     -14.903 -41.349  -1.911  1.00 64.70           O  
ATOM   2018  CB  PHE A 279     -15.649 -42.648   0.414  1.00 63.10           C  
ATOM   2019  CG  PHE A 279     -15.826 -43.022   1.863  1.00 63.10           C  
ATOM   2020  CD1 PHE A 279     -15.931 -44.356   2.246  1.00 63.28           C  
ATOM   2021  CD2 PHE A 279     -15.888 -42.038   2.846  1.00 61.85           C  
ATOM   2022  CE1 PHE A 279     -16.095 -44.701   3.581  1.00 62.89           C  
ATOM   2023  CE2 PHE A 279     -16.049 -42.377   4.180  1.00 62.22           C  
ATOM   2024  CZ  PHE A 279     -16.151 -43.710   4.548  1.00 61.38           C  
ATOM   2025  N   PRO A 280     -12.996 -42.542  -2.226  1.00 63.52           N  
ATOM   2026  CA  PRO A 280     -12.703 -41.943  -3.536  1.00 61.41           C  
ATOM   2027  C   PRO A 280     -13.766 -42.236  -4.595  1.00 60.10           C  
ATOM   2028  O   PRO A 280     -13.959 -41.433  -5.507  1.00 58.89           O  
ATOM   2029  CB  PRO A 280     -11.363 -42.582  -3.934  1.00 61.22           C  
ATOM   2030  CG  PRO A 280     -10.816 -43.181  -2.683  1.00 62.97           C  
ATOM   2031  CD  PRO A 280     -12.018 -43.590  -1.885  1.00 62.96           C  
ATOM   2032  N   ASN A 281     -14.446 -43.372  -4.464  1.00 58.70           N  
ATOM   2033  CA  ASN A 281     -15.507 -43.758  -5.393  1.00 58.79           C  
ATOM   2034  C   ASN A 281     -16.865 -43.101  -5.098  1.00 58.74           C  
ATOM   2035  O   ASN A 281     -17.833 -43.311  -5.834  1.00 58.67           O  
ATOM   2036  CB  ASN A 281     -15.642 -45.285  -5.449  1.00 59.86           C  
ATOM   2037  CG  ASN A 281     -14.376 -45.971  -5.947  1.00 61.83           C  
ATOM   2038  OD1 ASN A 281     -13.902 -46.929  -5.339  1.00 63.83           O  
ATOM   2039  ND2 ASN A 281     -13.821 -45.479  -7.052  1.00 60.31           N  
ATOM   2040  N   GLY A 282     -16.932 -42.306  -4.030  1.00 57.54           N  
ATOM   2041  CA  GLY A 282     -18.155 -41.575  -3.680  1.00 58.13           C  
ATOM   2042  C   GLY A 282     -18.925 -42.181  -2.520  1.00 57.39           C  
ATOM   2043  O   GLY A 282     -18.472 -43.142  -1.893  1.00 57.83           O  
ATOM   2044  N   LEU A 283     -20.098 -41.621  -2.238  1.00 55.38           N  
ATOM   2045  CA  LEU A 283     -20.893 -42.043  -1.082  1.00 55.08           C  
ATOM   2046  C   LEU A 283     -22.136 -42.868  -1.438  1.00 51.86           C  
ATOM   2047  O   LEU A 283     -22.829 -43.355  -0.545  1.00 50.15           O  
ATOM   2048  CB  LEU A 283     -21.291 -40.828  -0.230  1.00 56.28           C  
ATOM   2049  CG  LEU A 283     -20.177 -40.060   0.493  1.00 58.86           C  
ATOM   2050  CD1 LEU A 283     -20.715 -38.745   1.036  1.00 58.10           C  
ATOM   2051  CD2 LEU A 283     -19.531 -40.886   1.603  1.00 58.72           C  
ATOM   2052  N   ALA A 284     -22.402 -43.032  -2.733  1.00 48.99           N  
ATOM   2053  CA  ALA A 284     -23.597 -43.738  -3.206  1.00 46.43           C  
ATOM   2054  C   ALA A 284     -23.500 -45.262  -3.072  1.00 45.27           C  
ATOM   2055  O   ALA A 284     -22.493 -45.875  -3.452  1.00 44.58           O  
ATOM   2056  CB  ALA A 284     -23.908 -43.349  -4.644  1.00 44.70           C  
ATOM   2057  N   ASN A 285     -24.550 -45.859  -2.506  1.00 41.06           N  
ATOM   2058  CA  ASN A 285     -24.725 -47.310  -2.499  1.00 37.94           C  
ATOM   2059  C   ASN A 285     -26.110 -47.644  -3.071  1.00 36.73           C  
ATOM   2060  O   ASN A 285     -26.783 -46.757  -3.605  1.00 35.70           O  
ATOM   2061  CB  ASN A 285     -24.479 -47.904  -1.098  1.00 36.95           C  
ATOM   2062  CG  ASN A 285     -25.356 -47.279  -0.017  1.00 39.84           C  
ATOM   2063  OD1 ASN A 285     -26.579 -47.153  -0.170  1.00 37.41           O  
ATOM   2064  ND2 ASN A 285     -24.734 -46.912   1.103  1.00 38.44           N  
ATOM   2065  N   LYS A 286     -26.542 -48.900  -2.979  1.00 34.87           N  
ATOM   2066  CA  LYS A 286     -27.800 -49.300  -3.625  1.00 34.58           C  
ATOM   2067  C   LYS A 286     -29.029 -48.749  -2.891  1.00 34.18           C  
ATOM   2068  O   LYS A 286     -30.136 -48.794  -3.422  1.00 35.41           O  
ATOM   2069  CB  LYS A 286     -27.898 -50.827  -3.785  1.00 33.67           C  
ATOM   2070  CG  LYS A 286     -27.943 -51.603  -2.473  1.00 35.01           C  
ATOM   2071  CD  LYS A 286     -28.238 -53.076  -2.732  1.00 34.95           C  
ATOM   2072  CE  LYS A 286     -28.322 -53.854  -1.436  1.00 34.73           C  
ATOM   2073  NZ  LYS A 286     -28.885 -55.208  -1.681  1.00 35.65           N  
ATOM   2074  N   TYR A 287     -28.814 -48.232  -1.682  1.00 33.12           N  
ATOM   2075  CA  TYR A 287     -29.893 -47.713  -0.835  1.00 35.66           C  
ATOM   2076  C   TYR A 287     -30.117 -46.210  -0.973  1.00 35.75           C  
ATOM   2077  O   TYR A 287     -31.187 -45.714  -0.629  1.00 35.82           O  
ATOM   2078  CB  TYR A 287     -29.594 -47.999   0.634  1.00 35.73           C  
ATOM   2079  CG  TYR A 287     -29.454 -49.454   0.991  1.00 36.56           C  
ATOM   2080  CD1 TYR A 287     -30.577 -50.229   1.266  1.00 35.86           C  
ATOM   2081  CD2 TYR A 287     -28.194 -50.047   1.089  1.00 36.54           C  
ATOM   2082  CE1 TYR A 287     -30.458 -51.561   1.608  1.00 37.69           C  
ATOM   2083  CE2 TYR A 287     -28.058 -51.382   1.431  1.00 38.82           C  
ATOM   2084  CZ  TYR A 287     -29.193 -52.133   1.691  1.00 39.75           C  
ATOM   2085  OH  TYR A 287     -29.068 -53.452   2.037  1.00 40.39           O  
ATOM   2086  N   THR A 288     -29.107 -45.499  -1.478  1.00 35.43           N  
ATOM   2087  CA  THR A 288     -29.036 -44.029  -1.413  1.00 35.40           C  
ATOM   2088  C   THR A 288     -30.268 -43.289  -1.936  1.00 35.44           C  
ATOM   2089  O   THR A 288     -30.724 -42.328  -1.317  1.00 37.41           O  
ATOM   2090  CB  THR A 288     -27.782 -43.491  -2.150  1.00 35.85           C  
ATOM   2091  OG1 THR A 288     -26.628 -44.224  -1.726  1.00 35.05           O  
ATOM   2092  CG2 THR A 288     -27.572 -41.993  -1.868  1.00 35.60           C  
ATOM   2093  N   PHE A 289     -30.794 -43.730  -3.072  1.00 36.75           N  
ATOM   2094  CA  PHE A 289     -31.851 -42.997  -3.754  1.00 37.69           C  
ATOM   2095  C   PHE A 289     -33.256 -43.559  -3.516  1.00 37.29           C  
ATOM   2096  O   PHE A 289     -34.224 -43.104  -4.124  1.00 37.56           O  
ATOM   2097  CB  PHE A 289     -31.531 -42.885  -5.248  1.00 40.14           C  
ATOM   2098  CG  PHE A 289     -30.212 -42.213  -5.526  1.00 44.24           C  
ATOM   2099  CD1 PHE A 289     -30.082 -40.830  -5.409  1.00 45.45           C  
ATOM   2100  CD2 PHE A 289     -29.093 -42.962  -5.879  1.00 45.22           C  
ATOM   2101  CE1 PHE A 289     -28.864 -40.207  -5.655  1.00 47.19           C  
ATOM   2102  CE2 PHE A 289     -27.874 -42.344  -6.128  1.00 45.25           C  
ATOM   2103  CZ  PHE A 289     -27.759 -40.967  -6.012  1.00 45.64           C  
ATOM   2104  N   GLY A 290     -33.366 -44.536  -2.622  1.00 34.35           N  
ATOM   2105  CA  GLY A 290     -34.657 -45.097  -2.292  1.00 31.67           C  
ATOM   2106  C   GLY A 290     -35.070 -44.782  -0.860  1.00 31.02           C  
ATOM   2107  O   GLY A 290     -34.408 -44.004  -0.161  1.00 30.07           O  
ATOM   2108  N   PRO A 291     -36.159 -45.412  -0.403  1.00 29.79           N  
ATOM   2109  CA  PRO A 291     -36.758 -45.145   0.907  1.00 29.42           C  
ATOM   2110  C   PRO A 291     -35.829 -45.361   2.100  1.00 29.26           C  
ATOM   2111  O   PRO A 291     -35.986 -44.679   3.108  1.00 27.66           O  
ATOM   2112  CB  PRO A 291     -37.961 -46.101   0.942  1.00 29.78           C  
ATOM   2113  CG  PRO A 291     -38.285 -46.334  -0.516  1.00 28.51           C  
ATOM   2114  CD  PRO A 291     -36.941 -46.398  -1.172  1.00 29.14           C  
ATOM   2115  N   ILE A 292     -34.866 -46.278   1.998  1.00 28.54           N  
ATOM   2116  CA  ILE A 292     -33.903 -46.471   3.095  1.00 29.54           C  
ATOM   2117  C   ILE A 292     -32.882 -45.325   3.138  1.00 29.34           C  
ATOM   2118  O   ILE A 292     -32.499 -44.887   4.219  1.00 30.51           O  
ATOM   2119  CB  ILE A 292     -33.219 -47.863   3.069  1.00 29.54           C  
ATOM   2120  CG1 ILE A 292     -34.219 -48.957   3.448  1.00 31.17           C  
ATOM   2121  CG2 ILE A 292     -32.040 -47.938   4.036  1.00 29.90           C  
ATOM   2122  CD1 ILE A 292     -33.745 -50.348   3.079  1.00 32.65           C  
ATOM   2123  N   GLY A 293     -32.479 -44.835   1.968  1.00 30.27           N  
ATOM   2124  CA  GLY A 293     -31.635 -43.634   1.859  1.00 30.61           C  
ATOM   2125  C   GLY A 293     -32.298 -42.403   2.442  1.00 30.87           C  
ATOM   2126  O   GLY A 293     -31.708 -41.703   3.273  1.00 29.72           O  
ATOM   2127  N   GLU A 294     -33.544 -42.157   2.038  1.00 31.33           N  
ATOM   2128  CA  GLU A 294     -34.314 -41.037   2.568  1.00 32.32           C  
ATOM   2129  C   GLU A 294     -34.376 -41.100   4.090  1.00 31.00           C  
ATOM   2130  O   GLU A 294     -34.103 -40.115   4.771  1.00 28.79           O  
ATOM   2131  CB  GLU A 294     -35.716 -40.983   1.940  1.00 35.23           C  
ATOM   2132  CG  GLU A 294     -35.701 -40.496   0.496  1.00 39.72           C  
ATOM   2133  CD  GLU A 294     -37.074 -40.423  -0.162  1.00 43.96           C  
ATOM   2134  OE1 GLU A 294     -38.111 -40.324   0.545  1.00 45.25           O  
ATOM   2135  OE2 GLU A 294     -37.113 -40.444  -1.416  1.00 46.23           O  
ATOM   2136  N   LEU A 295     -34.693 -42.282   4.613  1.00 30.11           N  
ATOM   2137  CA  LEU A 295     -34.790 -42.511   6.047  1.00 30.39           C  
ATOM   2138  C   LEU A 295     -33.460 -42.286   6.766  1.00 30.69           C  
ATOM   2139  O   LEU A 295     -33.418 -41.675   7.838  1.00 28.99           O  
ATOM   2140  CB  LEU A 295     -35.279 -43.937   6.302  1.00 30.65           C  
ATOM   2141  CG  LEU A 295     -36.095 -44.250   7.541  1.00 31.97           C  
ATOM   2142  CD1 LEU A 295     -37.125 -43.170   7.840  1.00 32.10           C  
ATOM   2143  CD2 LEU A 295     -36.766 -45.598   7.307  1.00 32.09           C  
ATOM   2144  N   TRP A 296     -32.380 -42.788   6.173  1.00 30.18           N  
ATOM   2145  CA  TRP A 296     -31.066 -42.648   6.770  1.00 33.06           C  
ATOM   2146  C   TRP A 296     -30.669 -41.197   6.874  1.00 33.17           C  
ATOM   2147  O   TRP A 296     -30.191 -40.744   7.923  1.00 31.02           O  
ATOM   2148  CB  TRP A 296     -30.028 -43.435   5.975  1.00 35.38           C  
ATOM   2149  CG  TRP A 296     -28.643 -43.341   6.565  1.00 39.31           C  
ATOM   2150  CD1 TRP A 296     -28.046 -44.204   7.485  1.00 41.31           C  
ATOM   2151  CD2 TRP A 296     -27.635 -42.302   6.307  1.00 40.68           C  
ATOM   2152  NE1 TRP A 296     -26.774 -43.783   7.795  1.00 40.83           N  
ATOM   2153  CE2 TRP A 296     -26.466 -42.652   7.125  1.00 41.37           C  
ATOM   2154  CE3 TRP A 296     -27.584 -41.164   5.508  1.00 41.97           C  
ATOM   2155  CZ2 TRP A 296     -25.313 -41.879   7.130  1.00 42.30           C  
ATOM   2156  CZ3 TRP A 296     -26.416 -40.389   5.522  1.00 43.76           C  
ATOM   2157  CH2 TRP A 296     -25.309 -40.742   6.314  1.00 44.59           C  
ATOM   2158  N   TYR A 297     -30.865 -40.470   5.775  1.00 33.65           N  
ATOM   2159  CA  TYR A 297     -30.578 -39.048   5.698  1.00 36.07           C  
ATOM   2160  C   TYR A 297     -31.412 -38.273   6.721  1.00 34.02           C  
ATOM   2161  O   TYR A 297     -30.886 -37.442   7.449  1.00 32.49           O  
ATOM   2162  CB  TYR A 297     -30.843 -38.548   4.274  1.00 42.43           C  
ATOM   2163  CG  TYR A 297     -30.358 -37.147   3.996  1.00 48.92           C  
ATOM   2164  CD1 TYR A 297     -29.014 -36.897   3.705  1.00 52.00           C  
ATOM   2165  CD2 TYR A 297     -31.246 -36.068   4.013  1.00 52.22           C  
ATOM   2166  CE1 TYR A 297     -28.568 -35.608   3.447  1.00 55.51           C  
ATOM   2167  CE2 TYR A 297     -30.812 -34.776   3.755  1.00 56.09           C  
ATOM   2168  CZ  TYR A 297     -29.474 -34.552   3.473  1.00 57.03           C  
ATOM   2169  OH  TYR A 297     -29.043 -33.271   3.221  1.00 58.88           O  
ATOM   2170  N   ARG A 298     -32.706 -38.568   6.784  1.00 34.70           N  
ATOM   2171  CA  ARG A 298     -33.604 -37.940   7.756  1.00 36.86           C  
ATOM   2172  C   ARG A 298     -33.129 -38.163   9.208  1.00 36.39           C  
ATOM   2173  O   ARG A 298     -33.067 -37.219   9.997  1.00 35.41           O  
ATOM   2174  CB  ARG A 298     -35.047 -38.434   7.546  1.00 38.47           C  
ATOM   2175  CG  ARG A 298     -36.083 -37.751   8.426  1.00 43.87           C  
ATOM   2176  CD  ARG A 298     -37.518 -38.061   8.000  1.00 47.99           C  
ATOM   2177  NE  ARG A 298     -38.471 -37.576   9.005  1.00 52.28           N  
ATOM   2178  CZ  ARG A 298     -39.771 -37.882   9.053  1.00 54.02           C  
ATOM   2179  NH1 ARG A 298     -40.338 -38.684   8.147  1.00 50.33           N  
ATOM   2180  NH2 ARG A 298     -40.516 -37.373  10.023  1.00 54.18           N  
ATOM   2181  N   LYS A 299     -32.776 -39.405   9.541  1.00 36.08           N  
ATOM   2182  CA  LYS A 299     -32.303 -39.753  10.890  1.00 37.82           C  
ATOM   2183  C   LYS A 299     -30.953 -39.111  11.238  1.00 37.03           C  
ATOM   2184  O   LYS A 299     -30.775 -38.590  12.338  1.00 36.53           O  
ATOM   2185  CB  LYS A 299     -32.193 -41.274  11.058  1.00 41.73           C  
ATOM   2186  CG  LYS A 299     -33.518 -42.021  11.127  1.00 45.31           C  
ATOM   2187  CD  LYS A 299     -33.267 -43.518  11.235  1.00 47.96           C  
ATOM   2188  CE  LYS A 299     -34.558 -44.298  11.426  1.00 49.72           C  
ATOM   2189  NZ  LYS A 299     -34.319 -45.766  11.273  1.00 50.02           N  
ATOM   2190  N   SER A 300     -30.004 -39.149  10.308  1.00 34.99           N  
ATOM   2191  CA  SER A 300     -28.674 -38.619  10.594  1.00 35.22           C  
ATOM   2192  C   SER A 300     -28.654 -37.081  10.734  1.00 32.94           C  
ATOM   2193  O   SER A 300     -27.880 -36.543  11.525  1.00 30.74           O  
ATOM   2194  CB  SER A 300     -27.664 -39.102   9.550  1.00 36.56           C  
ATOM   2195  OG  SER A 300     -27.667 -38.249   8.425  1.00 43.78           O  
ATOM   2196  N   GLY A 301     -29.515 -36.386   9.986  1.00 30.67           N  
ATOM   2197  CA  GLY A 301     -29.584 -34.922  10.040  1.00 29.65           C  
ATOM   2198  C   GLY A 301     -30.593 -34.378  11.041  1.00 29.71           C  
ATOM   2199  O   GLY A 301     -30.842 -33.170  11.089  1.00 27.05           O  
ATOM   2200  N   THR A 302     -31.181 -35.271  11.837  1.00 29.58           N  
ATOM   2201  CA  THR A 302     -32.080 -34.871  12.925  1.00 29.80           C  
ATOM   2202  C   THR A 302     -31.414 -35.185  14.256  1.00 29.89           C  
ATOM   2203  O   THR A 302     -31.041 -36.324  14.512  1.00 30.82           O  
ATOM   2204  CB  THR A 302     -33.459 -35.568  12.820  1.00 29.95           C  
ATOM   2205  OG1 THR A 302     -34.031 -35.297  11.535  1.00 31.41           O  
ATOM   2206  CG2 THR A 302     -34.414 -35.074  13.897  1.00 30.78           C  
ATOM   2207  N   TYR A 303     -31.249 -34.167  15.094  1.00 29.65           N  
ATOM   2208  CA  TYR A 303     -30.559 -34.319  16.378  1.00 30.30           C  
ATOM   2209  C   TYR A 303     -30.818 -33.120  17.277  1.00 30.08           C  
ATOM   2210  O   TYR A 303     -31.267 -32.059  16.819  1.00 27.77           O  
ATOM   2211  CB  TYR A 303     -29.042 -34.535  16.188  1.00 30.54           C  
ATOM   2212  CG  TYR A 303     -28.373 -33.522  15.281  1.00 30.14           C  
ATOM   2213  CD1 TYR A 303     -27.860 -32.320  15.792  1.00 29.73           C  
ATOM   2214  CD2 TYR A 303     -28.235 -33.769  13.917  1.00 30.31           C  
ATOM   2215  CE1 TYR A 303     -27.245 -31.397  14.965  1.00 29.15           C  
ATOM   2216  CE2 TYR A 303     -27.628 -32.847  13.081  1.00 30.65           C  
ATOM   2217  CZ  TYR A 303     -27.134 -31.665  13.610  1.00 31.32           C  
ATOM   2218  OH  TYR A 303     -26.529 -30.753  12.773  1.00 31.37           O  
ATOM   2219  N   ARG A 304     -30.542 -33.298  18.565  1.00 28.97           N  
ATOM   2220  CA  ARG A 304     -30.729 -32.235  19.521  1.00 30.07           C  
ATOM   2221  C   ARG A 304     -29.552 -32.148  20.466  1.00 29.46           C  
ATOM   2222  O   ARG A 304     -29.042 -33.170  20.928  1.00 29.46           O  
ATOM   2223  CB  ARG A 304     -32.033 -32.437  20.315  1.00 30.43           C  
ATOM   2224  CG  ARG A 304     -33.301 -32.430  19.475  1.00 31.19           C  
ATOM   2225  CD  ARG A 304     -33.689 -31.018  19.066  1.00 31.91           C  
ATOM   2226  NE  ARG A 304     -34.880 -30.988  18.219  1.00 32.82           N  
ATOM   2227  CZ  ARG A 304     -34.869 -31.016  16.887  1.00 33.15           C  
ATOM   2228  NH1 ARG A 304     -33.723 -31.082  16.212  1.00 32.08           N  
ATOM   2229  NH2 ARG A 304     -36.016 -30.974  16.224  1.00 33.84           N  
ATOM   2230  N   GLY A 305     -29.133 -30.916  20.743  1.00 29.96           N  
ATOM   2231  CA  GLY A 305     -28.110 -30.632  21.738  1.00 30.29           C  
ATOM   2232  C   GLY A 305     -26.734 -31.182  21.416  1.00 31.74           C  
ATOM   2233  O   GLY A 305     -26.003 -31.558  22.327  1.00 31.94           O  
ATOM   2234  N   LYS A 306     -26.367 -31.218  20.135  1.00 32.09           N  
ATOM   2235  CA  LYS A 306     -25.056 -31.752  19.734  1.00 32.38           C  
ATOM   2236  C   LYS A 306     -23.947 -30.694  19.785  1.00 33.41           C  
ATOM   2237  O   LYS A 306     -24.028 -29.642  19.127  1.00 31.92           O  
ATOM   2238  CB  LYS A 306     -25.118 -32.393  18.341  1.00 33.21           C  
ATOM   2239  CG  LYS A 306     -23.860 -33.171  17.962  1.00 36.31           C  
ATOM   2240  CD  LYS A 306     -23.704 -33.342  16.456  1.00 37.51           C  
ATOM   2241  CE  LYS A 306     -24.615 -34.432  15.919  1.00 41.41           C  
ATOM   2242  NZ  LYS A 306     -24.355 -34.685  14.474  1.00 44.63           N  
ATOM   2243  N   VAL A 307     -22.904 -30.994  20.556  1.00 33.14           N  
ATOM   2244  CA  VAL A 307     -21.754 -30.113  20.684  1.00 35.09           C  
ATOM   2245  C   VAL A 307     -20.895 -30.252  19.428  1.00 34.74           C  
ATOM   2246  O   VAL A 307     -20.521 -31.357  19.046  1.00 35.18           O  
ATOM   2247  CB  VAL A 307     -20.919 -30.439  21.945  1.00 35.49           C  
ATOM   2248  CG1 VAL A 307     -19.820 -29.398  22.160  1.00 35.65           C  
ATOM   2249  CG2 VAL A 307     -21.813 -30.507  23.175  1.00 37.09           C  
ATOM   2250  N   GLN A 308     -20.608 -29.128  18.783  1.00 34.54           N  
ATOM   2251  CA  GLN A 308     -19.793 -29.115  17.568  1.00 34.12           C  
ATOM   2252  C   GLN A 308     -18.751 -27.997  17.626  1.00 34.37           C  
ATOM   2253  O   GLN A 308     -19.022 -26.926  18.167  1.00 32.07           O  
ATOM   2254  CB  GLN A 308     -20.680 -28.925  16.328  1.00 34.06           C  
ATOM   2255  CG  GLN A 308     -21.774 -29.977  16.153  1.00 34.91           C  
ATOM   2256  CD  GLN A 308     -22.572 -29.820  14.868  1.00 36.21           C  
ATOM   2257  OE1 GLN A 308     -23.081 -28.738  14.557  1.00 36.94           O  
ATOM   2258  NE2 GLN A 308     -22.705 -30.912  14.119  1.00 36.00           N  
ATOM   2259  N   ASN A 309     -17.564 -28.253  17.075  1.00 36.03           N  
ATOM   2260  CA  ASN A 309     -16.595 -27.184  16.823  1.00 37.13           C  
ATOM   2261  C   ASN A 309     -17.000 -26.331  15.614  1.00 37.53           C  
ATOM   2262  O   ASN A 309     -18.082 -26.518  15.041  1.00 33.87           O  
ATOM   2263  CB  ASN A 309     -15.162 -27.732  16.684  1.00 39.02           C  
ATOM   2264  CG  ASN A 309     -14.958 -28.599  15.445  1.00 41.06           C  
ATOM   2265  OD1 ASN A 309     -15.667 -28.482  14.442  1.00 41.83           O  
ATOM   2266  ND2 ASN A 309     -13.956 -29.467  15.507  1.00 42.79           N  
ATOM   2267  N   LEU A 310     -16.130 -25.397  15.234  1.00 39.32           N  
ATOM   2268  CA  LEU A 310     -16.419 -24.458  14.158  1.00 38.78           C  
ATOM   2269  C   LEU A 310     -16.617 -25.134  12.806  1.00 38.50           C  
ATOM   2270  O   LEU A 310     -17.592 -24.852  12.105  1.00 36.71           O  
ATOM   2271  CB  LEU A 310     -15.319 -23.400  14.062  1.00 41.37           C  
ATOM   2272  CG  LEU A 310     -15.512 -22.382  12.937  1.00 41.43           C  
ATOM   2273  CD1 LEU A 310     -16.488 -21.276  13.333  1.00 41.49           C  
ATOM   2274  CD2 LEU A 310     -14.158 -21.826  12.531  1.00 41.85           C  
ATOM   2275  N   THR A 311     -15.697 -26.023  12.440  1.00 39.15           N  
ATOM   2276  CA  THR A 311     -15.795 -26.754  11.174  1.00 39.15           C  
ATOM   2277  C   THR A 311     -17.106 -27.536  11.085  1.00 38.98           C  
ATOM   2278  O   THR A 311     -17.816 -27.442  10.086  1.00 39.32           O  
ATOM   2279  CB  THR A 311     -14.598 -27.709  10.975  1.00 40.87           C  
ATOM   2280  OG1 THR A 311     -13.378 -26.973  11.104  1.00 39.13           O  
ATOM   2281  CG2 THR A 311     -14.643 -28.360   9.596  1.00 41.71           C  
ATOM   2282  N   GLN A 312     -17.432 -28.282  12.139  1.00 38.00           N  
ATOM   2283  CA  GLN A 312     -18.626 -29.130  12.152  1.00 38.23           C  
ATOM   2284  C   GLN A 312     -19.906 -28.330  11.953  1.00 38.12           C  
ATOM   2285  O   GLN A 312     -20.730 -28.653  11.089  1.00 38.23           O  
ATOM   2286  CB  GLN A 312     -18.701 -29.926  13.459  1.00 40.09           C  
ATOM   2287  CG  GLN A 312     -17.695 -31.063  13.532  1.00 42.70           C  
ATOM   2288  CD  GLN A 312     -17.373 -31.499  14.950  1.00 44.26           C  
ATOM   2289  OE1 GLN A 312     -17.385 -30.695  15.884  1.00 43.77           O  
ATOM   2290  NE2 GLN A 312     -17.052 -32.781  15.112  1.00 45.25           N  
ATOM   2291  N   PHE A 313     -20.061 -27.283  12.757  1.00 37.38           N  
ATOM   2292  CA  PHE A 313     -21.263 -26.472  12.744  1.00 35.09           C  
ATOM   2293  C   PHE A 313     -21.273 -25.502  11.566  1.00 36.41           C  
ATOM   2294  O   PHE A 313     -22.301 -25.336  10.913  1.00 36.64           O  
ATOM   2295  CB  PHE A 313     -21.394 -25.699  14.064  1.00 33.16           C  
ATOM   2296  CG  PHE A 313     -22.657 -24.878  14.165  1.00 32.98           C  
ATOM   2297  CD1 PHE A 313     -23.873 -25.490  14.445  1.00 30.49           C  
ATOM   2298  CD2 PHE A 313     -22.633 -23.498  13.954  1.00 31.25           C  
ATOM   2299  CE1 PHE A 313     -25.042 -24.746  14.532  1.00 33.17           C  
ATOM   2300  CE2 PHE A 313     -23.797 -22.750  14.034  1.00 32.77           C  
ATOM   2301  CZ  PHE A 313     -25.007 -23.376  14.329  1.00 31.98           C  
ATOM   2302  N   TYR A 314     -20.129 -24.869  11.299  1.00 36.09           N  
ATOM   2303  CA  TYR A 314     -20.091 -23.688  10.434  1.00 37.54           C  
ATOM   2304  C   TYR A 314     -19.526 -23.933   9.038  1.00 39.12           C  
ATOM   2305  O   TYR A 314     -19.903 -23.259   8.081  1.00 39.42           O  
ATOM   2306  CB  TYR A 314     -19.323 -22.547  11.111  1.00 36.35           C  
ATOM   2307  CG  TYR A 314     -19.933 -21.206  10.833  1.00 34.93           C  
ATOM   2308  CD1 TYR A 314     -20.788 -20.613  11.756  1.00 35.96           C  
ATOM   2309  CD2 TYR A 314     -19.680 -20.537   9.638  1.00 35.37           C  
ATOM   2310  CE1 TYR A 314     -21.372 -19.383  11.501  1.00 34.59           C  
ATOM   2311  CE2 TYR A 314     -20.261 -19.309   9.375  1.00 35.37           C  
ATOM   2312  CZ  TYR A 314     -21.106 -18.739  10.313  1.00 33.60           C  
ATOM   2313  OH  TYR A 314     -21.683 -17.518  10.061  1.00 32.71           O  
ATOM   2314  N   HIS A 315     -18.625 -24.899   8.920  1.00 41.54           N  
ATOM   2315  CA  HIS A 315     -18.069 -25.231   7.620  1.00 44.64           C  
ATOM   2316  C   HIS A 315     -18.320 -26.683   7.262  1.00 46.14           C  
ATOM   2317  O   HIS A 315     -17.381 -27.396   6.913  1.00 43.30           O  
ATOM   2318  CB  HIS A 315     -16.579 -24.863   7.581  1.00 44.51           C  
ATOM   2319  CG  HIS A 315     -16.293 -23.411   7.938  1.00 45.67           C  
ATOM   2320  ND1 HIS A 315     -16.609 -22.385   7.121  1.00 45.40           N  
ATOM   2321  CD2 HIS A 315     -15.698 -22.842   9.066  1.00 44.02           C  
ATOM   2322  CE1 HIS A 315     -16.237 -21.223   7.692  1.00 44.07           C  
ATOM   2323  NE2 HIS A 315     -15.680 -21.504   8.881  1.00 44.91           N  
ATOM   2324  N   PRO A 316     -19.604 -27.136   7.313  1.00 49.87           N  
ATOM   2325  CA  PRO A 316     -19.885 -28.578   7.186  1.00 53.11           C  
ATOM   2326  C   PRO A 316     -19.535 -29.160   5.810  1.00 55.81           C  
ATOM   2327  O   PRO A 316     -19.417 -30.379   5.668  1.00 56.50           O  
ATOM   2328  CB  PRO A 316     -21.398 -28.668   7.438  1.00 53.23           C  
ATOM   2329  CG  PRO A 316     -21.930 -27.348   6.999  1.00 53.19           C  
ATOM   2330  CD  PRO A 316     -20.852 -26.342   7.319  1.00 51.76           C  
ATOM   2331  N   LEU A 317     -19.364 -28.289   4.818  1.00 57.73           N  
ATOM   2332  CA  LEU A 317     -19.011 -28.709   3.464  1.00 60.80           C  
ATOM   2333  C   LEU A 317     -17.496 -28.897   3.260  1.00 61.59           C  
ATOM   2334  O   LEU A 317     -17.074 -29.386   2.210  1.00 62.66           O  
ATOM   2335  CB  LEU A 317     -19.598 -27.738   2.426  1.00 62.64           C  
ATOM   2336  CG  LEU A 317     -21.055 -27.891   1.942  1.00 64.81           C  
ATOM   2337  CD1 LEU A 317     -21.160 -28.938   0.841  1.00 65.36           C  
ATOM   2338  CD2 LEU A 317     -22.050 -28.198   3.060  1.00 64.82           C  
ATOM   2339  N   ASP A 318     -16.695 -28.518   4.261  1.00 60.62           N  
ATOM   2340  CA  ASP A 318     -15.236 -28.723   4.237  1.00 62.36           C  
ATOM   2341  C   ASP A 318     -14.838 -30.200   4.117  1.00 64.95           C  
ATOM   2342  O   ASP A 318     -13.844 -30.530   3.465  1.00 64.83           O  
ATOM   2343  CB  ASP A 318     -14.571 -28.104   5.474  1.00 61.18           C  
ATOM   2344  CG  ASP A 318     -14.331 -26.603   5.331  1.00 58.35           C  
ATOM   2345  OD1 ASP A 318     -14.683 -26.022   4.282  1.00 60.28           O  
ATOM   2346  OD2 ASP A 318     -13.782 -26.003   6.275  1.00 56.34           O  
ATOM   2347  N   MET A 319     -15.624 -31.075   4.746  1.00 66.75           N  
ATOM   2348  CA  MET A 319     -15.413 -32.529   4.690  1.00 67.26           C  
ATOM   2349  C   MET A 319     -15.536 -33.097   3.270  1.00 65.23           C  
ATOM   2350  O   MET A 319     -14.937 -34.127   2.959  1.00 61.59           O  
ATOM   2351  CB  MET A 319     -16.382 -33.252   5.638  1.00 69.46           C  
ATOM   2352  CG  MET A 319     -17.853 -33.097   5.263  1.00 73.84           C  
ATOM   2353  SD  MET A 319     -19.034 -33.795   6.435  1.00 80.24           S  
ATOM   2354  CE  MET A 319     -18.778 -32.752   7.875  1.00 78.63           C  
ATOM   2355  N   PHE A 320     -16.309 -32.420   2.418  1.00 64.84           N  
ATOM   2356  CA  PHE A 320     -16.532 -32.870   1.041  1.00 66.67           C  
ATOM   2357  C   PHE A 320     -15.341 -32.634   0.101  1.00 67.05           C  
ATOM   2358  O   PHE A 320     -15.376 -33.042  -1.063  1.00 63.74           O  
ATOM   2359  CB  PHE A 320     -17.830 -32.280   0.467  1.00 67.87           C  
ATOM   2360  CG  PHE A 320     -19.082 -32.831   1.106  1.00 69.50           C  
ATOM   2361  CD1 PHE A 320     -19.398 -34.188   1.008  1.00 69.47           C  
ATOM   2362  CD2 PHE A 320     -19.947 -31.996   1.809  1.00 70.48           C  
ATOM   2363  CE1 PHE A 320     -20.549 -34.696   1.599  1.00 68.91           C  
ATOM   2364  CE2 PHE A 320     -21.101 -32.499   2.400  1.00 70.96           C  
ATOM   2365  CZ  PHE A 320     -21.402 -33.850   2.294  1.00 68.43           C  
ATOM   2366  N   GLY A 321     -14.303 -31.970   0.617  1.00 68.62           N  
ATOM   2367  CA  GLY A 321     -13.016 -31.804  -0.070  1.00 69.35           C  
ATOM   2368  C   GLY A 321     -13.086 -31.275  -1.490  1.00 71.35           C  
ATOM   2369  O   GLY A 321     -13.649 -30.206  -1.737  1.00 72.17           O  
ATOM   2370  N   GLU A 322     -12.519 -32.045  -2.419  1.00 73.67           N  
ATOM   2371  CA  GLU A 322     -12.427 -31.665  -3.832  1.00 73.51           C  
ATOM   2372  C   GLU A 322     -13.754 -31.799  -4.590  1.00 73.07           C  
ATOM   2373  O   GLU A 322     -13.872 -31.319  -5.722  1.00 73.17           O  
ATOM   2374  CB  GLU A 322     -11.329 -32.484  -4.534  1.00 77.04           C  
ATOM   2375  CG  GLU A 322     -11.795 -33.849  -5.064  1.00 80.07           C  
ATOM   2376  CD  GLU A 322     -10.652 -34.844  -5.233  1.00 80.51           C  
ATOM   2377  OE1 GLU A 322      -9.521 -34.564  -4.775  1.00 81.05           O  
ATOM   2378  OE2 GLU A 322     -10.895 -35.919  -5.823  1.00 79.91           O  
ATOM   2379  N   TRP A 323     -14.738 -32.448  -3.964  1.00 70.63           N  
ATOM   2380  CA  TRP A 323     -16.032 -32.729  -4.601  1.00 71.59           C  
ATOM   2381  C   TRP A 323     -16.903 -31.526  -4.857  1.00 70.82           C  
ATOM   2382  O   TRP A 323     -17.665 -31.514  -5.824  1.00 69.68           O  
ATOM   2383  CB  TRP A 323     -16.825 -33.759  -3.801  1.00 71.34           C  
ATOM   2384  CG  TRP A 323     -16.255 -35.159  -3.812  1.00 71.68           C  
ATOM   2385  CD1 TRP A 323     -15.400 -35.733  -4.754  1.00 71.48           C  
ATOM   2386  CD2 TRP A 323     -16.530 -36.232  -2.846  1.00 70.27           C  
ATOM   2387  NE1 TRP A 323     -15.119 -37.036  -4.430  1.00 70.96           N  
ATOM   2388  CE2 TRP A 323     -15.765 -37.400  -3.302  1.00 70.80           C  
ATOM   2389  CE3 TRP A 323     -17.296 -36.336  -1.688  1.00 69.54           C  
ATOM   2390  CZ2 TRP A 323     -15.786 -38.604  -2.615  1.00 69.94           C  
ATOM   2391  CZ3 TRP A 323     -17.306 -37.556  -1.002  1.00 69.69           C  
ATOM   2392  CH2 TRP A 323     -16.567 -38.661  -1.456  1.00 69.35           C  
ATOM   2393  N   ASN A 324     -16.828 -30.516  -3.993  1.00 71.65           N  
ATOM   2394  CA  ASN A 324     -17.621 -29.299  -4.190  1.00 72.63           C  
ATOM   2395  C   ASN A 324     -17.029 -28.372  -5.257  1.00 72.87           C  
ATOM   2396  O   ASN A 324     -15.818 -28.121  -5.270  1.00 70.87           O  
ATOM   2397  CB  ASN A 324     -17.887 -28.563  -2.863  1.00 72.69           C  
ATOM   2398  CG  ASN A 324     -16.658 -28.464  -1.977  1.00 70.25           C  
ATOM   2399  OD1 ASN A 324     -15.631 -27.905  -2.369  1.00 72.72           O  
ATOM   2400  ND2 ASN A 324     -16.769 -28.980  -0.760  1.00 67.67           N  
ATOM   2401  N   ARG A 325     -17.897 -27.888  -6.151  1.00 74.14           N  
ATOM   2402  CA  ARG A 325     -17.505 -27.066  -7.309  1.00 76.15           C  
ATOM   2403  C   ARG A 325     -16.451 -27.758  -8.185  1.00 77.86           C  
ATOM   2404  O   ARG A 325     -15.439 -27.161  -8.566  1.00 77.15           O  
ATOM   2405  CB  ARG A 325     -17.045 -25.668  -6.865  1.00 75.91           C  
ATOM   2406  CG  ARG A 325     -18.197 -24.719  -6.582  1.00 75.66           C  
ATOM   2407  CD  ARG A 325     -17.865 -23.719  -5.486  1.00 72.49           C  
ATOM   2408  NE  ARG A 325     -19.095 -23.207  -4.884  1.00 73.17           N  
ATOM   2409  CZ  ARG A 325     -19.166 -22.198  -4.019  1.00 71.04           C  
ATOM   2410  NH1 ARG A 325     -18.068 -21.559  -3.632  1.00 67.56           N  
ATOM   2411  NH2 ARG A 325     -20.351 -21.826  -3.545  1.00 68.16           N  
ATOM   2412  N   ALA A 326     -16.710 -29.022  -8.505  1.00 79.86           N  
ATOM   2413  CA  ALA A 326     -15.749 -29.844  -9.231  1.00 86.98           C  
ATOM   2414  C   ALA A 326     -16.155 -30.089 -10.685  1.00 91.48           C  
ATOM   2415  O   ALA A 326     -17.272 -29.758 -11.099  1.00 90.13           O  
ATOM   2416  CB  ALA A 326     -15.546 -31.171  -8.508  1.00 86.40           C  
ATOM   2417  N   TYR A 327     -15.209 -30.641 -11.449  1.00 94.91           N  
ATOM   2418  CA  TYR A 327     -15.456 -31.252 -12.764  1.00 96.86           C  
ATOM   2419  C   TYR A 327     -15.748 -30.284 -13.920  1.00 98.11           C  
ATOM   2420  O   TYR A 327     -15.704 -30.688 -15.085  1.00 98.54           O  
ATOM   2421  CB  TYR A 327     -16.566 -32.311 -12.667  1.00 98.76           C  
ATOM   2422  CG  TYR A 327     -16.158 -33.677 -13.168  1.00100.68           C  
ATOM   2423  CD1 TYR A 327     -16.092 -33.954 -14.539  1.00100.33           C  
ATOM   2424  CD2 TYR A 327     -15.835 -34.698 -12.268  1.00100.07           C  
ATOM   2425  CE1 TYR A 327     -15.714 -35.208 -14.996  1.00 98.41           C  
ATOM   2426  CE2 TYR A 327     -15.459 -35.955 -12.715  1.00 99.30           C  
ATOM   2427  CZ  TYR A 327     -15.400 -36.204 -14.078  1.00 98.92           C  
ATOM   2428  OH  TYR A 327     -15.026 -37.452 -14.521  1.00 98.21           O  
ATOM   2429  N   GLY A 328     -16.042 -29.022 -13.604  1.00 96.46           N  
ATOM   2430  CA  GLY A 328     -16.423 -28.040 -14.620  1.00 90.20           C  
ATOM   2431  C   GLY A 328     -15.266 -27.195 -15.123  1.00 87.85           C  
ATOM   2432  O   GLY A 328     -14.767 -26.338 -14.387  1.00 85.04           O  
ATOM   2433  N   PRO A 329     -14.826 -27.428 -16.381  1.00 85.57           N  
ATOM   2434  CA  PRO A 329     -13.781 -26.581 -16.971  1.00 83.50           C  
ATOM   2435  C   PRO A 329     -14.315 -25.197 -17.366  1.00 79.17           C  
ATOM   2436  O   PRO A 329     -13.559 -24.221 -17.361  1.00 76.84           O  
ATOM   2437  CB  PRO A 329     -13.338 -27.372 -18.208  1.00 81.43           C  
ATOM   2438  CG  PRO A 329     -14.527 -28.191 -18.581  1.00 82.20           C  
ATOM   2439  CD  PRO A 329     -15.256 -28.500 -17.302  1.00 83.50           C  
ATOM   2440  N   ALA A 330     -15.609 -25.129 -17.688  1.00 74.96           N  
ATOM   2441  CA  ALA A 330     -16.273 -23.880 -18.066  1.00 70.07           C  
ATOM   2442  C   ALA A 330     -16.425 -22.921 -16.878  1.00 68.60           C  
ATOM   2443  O   ALA A 330     -16.514 -21.702 -17.062  1.00 69.17           O  
ATOM   2444  CB  ALA A 330     -17.628 -24.174 -18.696  1.00 67.20           C  
ATOM   2445  N   GLY A 331     -16.444 -23.477 -15.666  1.00 62.24           N  
ATOM   2446  CA  GLY A 331     -16.617 -22.693 -14.451  1.00 53.30           C  
ATOM   2447  C   GLY A 331     -18.053 -22.743 -13.968  1.00 50.41           C  
ATOM   2448  O   GLY A 331     -18.878 -23.498 -14.492  1.00 46.03           O  
ATOM   2449  N   PHE A 332     -18.344 -21.929 -12.958  1.00 47.62           N  
ATOM   2450  CA  PHE A 332     -19.650 -21.897 -12.318  1.00 45.57           C  
ATOM   2451  C   PHE A 332     -20.092 -20.447 -12.193  1.00 40.50           C  
ATOM   2452  O   PHE A 332     -19.269 -19.546 -12.128  1.00 39.42           O  
ATOM   2453  CB  PHE A 332     -19.585 -22.545 -10.918  1.00 48.21           C  
ATOM   2454  CG  PHE A 332     -19.570 -24.057 -10.933  1.00 49.52           C  
ATOM   2455  CD1 PHE A 332     -20.717 -24.783 -10.618  1.00 49.07           C  
ATOM   2456  CD2 PHE A 332     -18.405 -24.761 -11.252  1.00 50.32           C  
ATOM   2457  CE1 PHE A 332     -20.708 -26.174 -10.625  1.00 49.65           C  
ATOM   2458  CE2 PHE A 332     -18.394 -26.150 -11.271  1.00 49.44           C  
ATOM   2459  CZ  PHE A 332     -19.546 -26.857 -10.954  1.00 48.72           C  
ATOM   2460  N   LEU A 333     -21.396 -20.220 -12.162  1.00 38.49           N  
ATOM   2461  CA  LEU A 333     -21.908 -18.889 -11.873  1.00 35.72           C  
ATOM   2462  C   LEU A 333     -22.622 -18.937 -10.526  1.00 33.86           C  
ATOM   2463  O   LEU A 333     -23.636 -19.623 -10.380  1.00 29.21           O  
ATOM   2464  CB  LEU A 333     -22.845 -18.426 -12.991  1.00 36.18           C  
ATOM   2465  CG  LEU A 333     -23.224 -16.949 -13.120  1.00 38.72           C  
ATOM   2466  CD1 LEU A 333     -23.486 -16.603 -14.579  1.00 38.16           C  
ATOM   2467  CD2 LEU A 333     -24.448 -16.621 -12.277  1.00 37.63           C  
ATOM   2468  N   GLN A 334     -22.071 -18.218  -9.550  1.00 32.48           N  
ATOM   2469  CA  GLN A 334     -22.679 -18.085  -8.223  1.00 34.07           C  
ATOM   2470  C   GLN A 334     -23.771 -17.000  -8.248  1.00 33.68           C  
ATOM   2471  O   GLN A 334     -23.539 -15.874  -8.688  1.00 33.44           O  
ATOM   2472  CB  GLN A 334     -21.586 -17.811  -7.164  1.00 36.28           C  
ATOM   2473  CG  GLN A 334     -22.044 -17.233  -5.827  1.00 41.90           C  
ATOM   2474  CD  GLN A 334     -22.757 -18.230  -4.919  1.00 43.72           C  
ATOM   2475  OE1 GLN A 334     -23.537 -17.842  -4.044  1.00 49.30           O  
ATOM   2476  NE2 GLN A 334     -22.493 -19.512  -5.120  1.00 43.71           N  
ATOM   2477  N   TYR A 335     -24.969 -17.363  -7.800  1.00 30.81           N  
ATOM   2478  CA  TYR A 335     -26.124 -16.474  -7.855  1.00 28.42           C  
ATOM   2479  C   TYR A 335     -26.801 -16.415  -6.490  1.00 27.77           C  
ATOM   2480  O   TYR A 335     -27.329 -17.429  -6.022  1.00 28.46           O  
ATOM   2481  CB  TYR A 335     -27.110 -16.973  -8.924  1.00 27.72           C  
ATOM   2482  CG  TYR A 335     -28.152 -15.955  -9.324  1.00 28.17           C  
ATOM   2483  CD1 TYR A 335     -27.855 -14.951 -10.253  1.00 27.57           C  
ATOM   2484  CD2 TYR A 335     -29.436 -15.986  -8.772  1.00 27.34           C  
ATOM   2485  CE1 TYR A 335     -28.805 -14.004 -10.610  1.00 27.98           C  
ATOM   2486  CE2 TYR A 335     -30.393 -15.040  -9.125  1.00 28.06           C  
ATOM   2487  CZ  TYR A 335     -30.072 -14.055 -10.038  1.00 27.92           C  
ATOM   2488  OH  TYR A 335     -31.013 -13.129 -10.389  1.00 28.91           O  
ATOM   2489  N   GLN A 336     -26.783 -15.238  -5.852  1.00 25.34           N  
ATOM   2490  CA  GLN A 336     -27.361 -15.076  -4.525  1.00 24.43           C  
ATOM   2491  C   GLN A 336     -28.385 -13.934  -4.507  1.00 24.48           C  
ATOM   2492  O   GLN A 336     -28.098 -12.825  -4.941  1.00 22.65           O  
ATOM   2493  CB  GLN A 336     -26.280 -14.854  -3.453  1.00 24.94           C  
ATOM   2494  CG  GLN A 336     -26.847 -14.567  -2.062  1.00 23.98           C  
ATOM   2495  CD  GLN A 336     -25.814 -14.600  -0.946  1.00 23.49           C  
ATOM   2496  OE1 GLN A 336     -24.610 -14.720  -1.184  1.00 24.29           O  
ATOM   2497  NE2 GLN A 336     -26.289 -14.518   0.288  1.00 21.54           N  
ATOM   2498  N   PHE A 337     -29.575 -14.222  -3.991  1.00 22.14           N  
ATOM   2499  CA  PHE A 337     -30.618 -13.221  -3.872  1.00 22.11           C  
ATOM   2500  C   PHE A 337     -31.386 -13.407  -2.574  1.00 21.38           C  
ATOM   2501  O   PHE A 337     -31.275 -14.446  -1.920  1.00 21.33           O  
ATOM   2502  CB  PHE A 337     -31.582 -13.281  -5.070  1.00 21.37           C  
ATOM   2503  CG  PHE A 337     -32.322 -14.589  -5.189  1.00 22.82           C  
ATOM   2504  CD1 PHE A 337     -33.591 -14.747  -4.612  1.00 23.01           C  
ATOM   2505  CD2 PHE A 337     -31.752 -15.666  -5.861  1.00 22.30           C  
ATOM   2506  CE1 PHE A 337     -34.271 -15.954  -4.716  1.00 23.23           C  
ATOM   2507  CE2 PHE A 337     -32.427 -16.873  -5.963  1.00 23.19           C  
ATOM   2508  CZ  PHE A 337     -33.689 -17.013  -5.396  1.00 23.47           C  
ATOM   2509  N   VAL A 338     -32.145 -12.380  -2.211  1.00 21.68           N  
ATOM   2510  CA  VAL A 338     -33.049 -12.430  -1.066  1.00 21.77           C  
ATOM   2511  C   VAL A 338     -34.420 -11.894  -1.496  1.00 22.77           C  
ATOM   2512  O   VAL A 338     -34.498 -10.937  -2.274  1.00 22.84           O  
ATOM   2513  CB  VAL A 338     -32.473 -11.640   0.142  1.00 21.91           C  
ATOM   2514  CG1 VAL A 338     -32.106 -10.211  -0.257  1.00 20.74           C  
ATOM   2515  CG2 VAL A 338     -33.437 -11.629   1.327  1.00 20.62           C  
ATOM   2516  N   ILE A 339     -35.495 -12.511  -0.994  1.00 22.80           N  
ATOM   2517  CA  ILE A 339     -36.859 -12.064  -1.254  1.00 22.74           C  
ATOM   2518  C   ILE A 339     -37.542 -11.698   0.081  1.00 23.90           C  
ATOM   2519  O   ILE A 339     -37.457 -12.459   1.044  1.00 23.75           O  
ATOM   2520  CB  ILE A 339     -37.678 -13.171  -1.980  1.00 23.63           C  
ATOM   2521  CG1 ILE A 339     -36.992 -13.649  -3.282  1.00 23.71           C  
ATOM   2522  CG2 ILE A 339     -39.121 -12.741  -2.233  1.00 23.87           C  
ATOM   2523  CD1 ILE A 339     -36.930 -12.632  -4.413  1.00 23.72           C  
ATOM   2524  N   PRO A 340     -38.222 -10.536   0.141  1.00 23.57           N  
ATOM   2525  CA  PRO A 340     -38.847 -10.084   1.387  1.00 24.63           C  
ATOM   2526  C   PRO A 340     -39.711 -11.184   2.009  1.00 25.30           C  
ATOM   2527  O   PRO A 340     -40.411 -11.899   1.289  1.00 25.39           O  
ATOM   2528  CB  PRO A 340     -39.750  -8.919   0.950  1.00 24.93           C  
ATOM   2529  CG  PRO A 340     -39.260  -8.491  -0.383  1.00 25.50           C  
ATOM   2530  CD  PRO A 340     -38.412  -9.586  -0.975  1.00 24.12           C  
ATOM   2531  N   THR A 341     -39.662 -11.283   3.335  1.00 25.84           N  
ATOM   2532  CA  THR A 341     -40.336 -12.339   4.103  1.00 26.40           C  
ATOM   2533  C   THR A 341     -41.759 -12.600   3.640  1.00 27.20           C  
ATOM   2534  O   THR A 341     -42.132 -13.754   3.387  1.00 26.16           O  
ATOM   2535  CB  THR A 341     -40.328 -12.005   5.608  1.00 26.83           C  
ATOM   2536  OG1 THR A 341     -39.000 -11.648   5.991  1.00 28.01           O  
ATOM   2537  CG2 THR A 341     -40.779 -13.203   6.463  1.00 27.38           C  
ATOM   2538  N   GLU A 342     -42.533 -11.520   3.496  1.00 28.34           N  
ATOM   2539  CA  GLU A 342     -43.972 -11.594   3.191  1.00 28.31           C  
ATOM   2540  C   GLU A 342     -44.270 -12.201   1.822  1.00 28.42           C  
ATOM   2541  O   GLU A 342     -45.343 -12.753   1.608  1.00 29.11           O  
ATOM   2542  CB  GLU A 342     -44.641 -10.210   3.325  1.00 28.08           C  
ATOM   2543  CG  GLU A 342     -44.155  -9.156   2.336  1.00 29.65           C  
ATOM   2544  CD  GLU A 342     -42.969  -8.345   2.851  1.00 30.64           C  
ATOM   2545  OE1 GLU A 342     -42.244  -8.828   3.749  1.00 30.95           O  
ATOM   2546  OE2 GLU A 342     -42.767  -7.214   2.358  1.00 30.00           O  
ATOM   2547  N   ALA A 343     -43.308 -12.122   0.907  1.00 27.30           N  
ATOM   2548  CA  ALA A 343     -43.503 -12.615  -0.454  1.00 26.58           C  
ATOM   2549  C   ALA A 343     -43.200 -14.107  -0.571  1.00 27.60           C  
ATOM   2550  O   ALA A 343     -42.361 -14.542  -1.378  1.00 25.49           O  
ATOM   2551  CB  ALA A 343     -42.663 -11.808  -1.434  1.00 24.64           C  
ATOM   2552  N   VAL A 344     -43.920 -14.901   0.212  1.00 29.54           N  
ATOM   2553  CA  VAL A 344     -43.622 -16.324   0.320  1.00 31.21           C  
ATOM   2554  C   VAL A 344     -44.014 -17.123  -0.931  1.00 30.49           C  
ATOM   2555  O   VAL A 344     -43.238 -17.972  -1.381  1.00 31.55           O  
ATOM   2556  CB  VAL A 344     -44.145 -16.937   1.663  1.00 32.17           C  
ATOM   2557  CG1 VAL A 344     -45.664 -16.938   1.734  1.00 33.20           C  
ATOM   2558  CG2 VAL A 344     -43.583 -18.337   1.872  1.00 33.75           C  
ATOM   2559  N   ASP A 345     -45.185 -16.844  -1.503  1.00 30.69           N  
ATOM   2560  CA  ASP A 345     -45.607 -17.502  -2.747  1.00 31.56           C  
ATOM   2561  C   ASP A 345     -44.691 -17.144  -3.900  1.00 29.95           C  
ATOM   2562  O   ASP A 345     -44.364 -17.989  -4.739  1.00 28.49           O  
ATOM   2563  CB  ASP A 345     -47.037 -17.105  -3.120  1.00 34.69           C  
ATOM   2564  CG  ASP A 345     -48.047 -17.529  -2.077  1.00 37.16           C  
ATOM   2565  OD1 ASP A 345     -47.890 -18.632  -1.514  1.00 37.78           O  
ATOM   2566  OD2 ASP A 345     -48.990 -16.750  -1.818  1.00 40.34           O  
ATOM   2567  N   GLU A 346     -44.296 -15.877  -3.939  1.00 28.29           N  
ATOM   2568  CA  GLU A 346     -43.352 -15.386  -4.930  1.00 28.98           C  
ATOM   2569  C   GLU A 346     -42.013 -16.128  -4.786  1.00 27.32           C  
ATOM   2570  O   GLU A 346     -41.410 -16.556  -5.779  1.00 27.37           O  
ATOM   2571  CB  GLU A 346     -43.162 -13.868  -4.759  1.00 29.07           C  
ATOM   2572  CG  GLU A 346     -44.393 -13.013  -5.071  1.00 31.16           C  
ATOM   2573  CD  GLU A 346     -45.448 -12.984  -3.965  1.00 31.78           C  
ATOM   2574  OE1 GLU A 346     -45.250 -13.584  -2.891  1.00 31.14           O  
ATOM   2575  OE2 GLU A 346     -46.501 -12.347  -4.172  1.00 34.48           O  
ATOM   2576  N   PHE A 347     -41.555 -16.279  -3.545  1.00 27.62           N  
ATOM   2577  CA  PHE A 347     -40.317 -17.003  -3.265  1.00 28.63           C  
ATOM   2578  C   PHE A 347     -40.402 -18.451  -3.775  1.00 28.00           C  
ATOM   2579  O   PHE A 347     -39.472 -18.949  -4.400  1.00 24.66           O  
ATOM   2580  CB  PHE A 347     -39.986 -16.971  -1.764  1.00 28.46           C  
ATOM   2581  CG  PHE A 347     -38.817 -17.844  -1.383  1.00 30.01           C  
ATOM   2582  CD1 PHE A 347     -37.551 -17.602  -1.904  1.00 29.73           C  
ATOM   2583  CD2 PHE A 347     -38.978 -18.901  -0.486  1.00 30.21           C  
ATOM   2584  CE1 PHE A 347     -36.479 -18.405  -1.554  1.00 29.86           C  
ATOM   2585  CE2 PHE A 347     -37.903 -19.702  -0.129  1.00 29.89           C  
ATOM   2586  CZ  PHE A 347     -36.652 -19.457  -0.670  1.00 30.34           C  
ATOM   2587  N   LYS A 348     -41.534 -19.104  -3.513  1.00 28.09           N  
ATOM   2588  CA  LYS A 348     -41.760 -20.481  -3.973  1.00 29.87           C  
ATOM   2589  C   LYS A 348     -41.771 -20.564  -5.488  1.00 28.98           C  
ATOM   2590  O   LYS A 348     -41.206 -21.498  -6.068  1.00 28.91           O  
ATOM   2591  CB  LYS A 348     -43.066 -21.033  -3.381  1.00 31.14           C  
ATOM   2592  CG  LYS A 348     -42.931 -21.327  -1.894  1.00 33.18           C  
ATOM   2593  CD  LYS A 348     -44.238 -21.157  -1.136  1.00 36.27           C  
ATOM   2594  CE  LYS A 348     -45.162 -22.335  -1.328  1.00 36.44           C  
ATOM   2595  NZ  LYS A 348     -45.954 -22.486  -0.077  1.00 41.22           N  
ATOM   2596  N   LYS A 349     -42.379 -19.564  -6.123  1.00 28.41           N  
ATOM   2597  CA  LYS A 349     -42.393 -19.475  -7.584  1.00 29.99           C  
ATOM   2598  C   LYS A 349     -40.964 -19.432  -8.150  1.00 28.91           C  
ATOM   2599  O   LYS A 349     -40.641 -20.164  -9.084  1.00 27.60           O  
ATOM   2600  CB  LYS A 349     -43.230 -18.271  -8.042  1.00 31.63           C  
ATOM   2601  CG  LYS A 349     -43.356 -18.072  -9.549  1.00 35.30           C  
ATOM   2602  CD  LYS A 349     -43.948 -19.294 -10.250  1.00 38.17           C  
ATOM   2603  CE  LYS A 349     -43.969 -19.132 -11.768  1.00 40.80           C  
ATOM   2604  NZ  LYS A 349     -44.999 -18.139 -12.207  1.00 41.33           N  
ATOM   2605  N   ILE A 350     -40.102 -18.601  -7.569  1.00 28.95           N  
ATOM   2606  CA  ILE A 350     -38.731 -18.502  -8.063  1.00 28.93           C  
ATOM   2607  C   ILE A 350     -37.946 -19.823  -7.901  1.00 27.16           C  
ATOM   2608  O   ILE A 350     -37.183 -20.196  -8.782  1.00 26.72           O  
ATOM   2609  CB  ILE A 350     -37.982 -17.275  -7.489  1.00 31.21           C  
ATOM   2610  CG1 ILE A 350     -36.594 -17.148  -8.114  1.00 32.30           C  
ATOM   2611  CG2 ILE A 350     -37.846 -17.345  -5.977  1.00 31.99           C  
ATOM   2612  CD1 ILE A 350     -36.077 -15.726  -8.124  1.00 37.59           C  
ATOM   2613  N   ILE A 351     -38.153 -20.535  -6.795  1.00 26.34           N  
ATOM   2614  CA  ILE A 351     -37.508 -21.844  -6.617  1.00 25.15           C  
ATOM   2615  C   ILE A 351     -37.990 -22.831  -7.691  1.00 24.90           C  
ATOM   2616  O   ILE A 351     -37.176 -23.548  -8.285  1.00 26.98           O  
ATOM   2617  CB  ILE A 351     -37.683 -22.412  -5.185  1.00 23.82           C  
ATOM   2618  CG1 ILE A 351     -37.155 -21.434  -4.117  1.00 23.83           C  
ATOM   2619  CG2 ILE A 351     -37.024 -23.792  -5.032  1.00 22.44           C  
ATOM   2620  CD1 ILE A 351     -35.668 -21.114  -4.214  1.00 23.55           C  
ATOM   2621  N   GLY A 352     -39.299 -22.840  -7.955  1.00 24.44           N  
ATOM   2622  CA  GLY A 352     -39.889 -23.618  -9.060  1.00 25.71           C  
ATOM   2623  C   GLY A 352     -39.266 -23.304 -10.423  1.00 27.27           C  
ATOM   2624  O   GLY A 352     -38.920 -24.218 -11.194  1.00 27.96           O  
ATOM   2625  N   VAL A 353     -39.100 -22.016 -10.710  1.00 26.66           N  
ATOM   2626  CA  VAL A 353     -38.486 -21.579 -11.967  1.00 28.08           C  
ATOM   2627  C   VAL A 353     -37.071 -22.156 -12.130  1.00 27.22           C  
ATOM   2628  O   VAL A 353     -36.747 -22.712 -13.168  1.00 28.77           O  
ATOM   2629  CB  VAL A 353     -38.488 -20.040 -12.078  1.00 29.08           C  
ATOM   2630  CG1 VAL A 353     -37.601 -19.574 -13.224  1.00 28.59           C  
ATOM   2631  CG2 VAL A 353     -39.923 -19.525 -12.244  1.00 28.67           C  
ATOM   2632  N   ILE A 354     -36.257 -22.051 -11.081  1.00 27.71           N  
ATOM   2633  CA  ILE A 354     -34.898 -22.595 -11.060  1.00 27.39           C  
ATOM   2634  C   ILE A 354     -34.874 -24.100 -11.350  1.00 27.68           C  
ATOM   2635  O   ILE A 354     -34.073 -24.585 -12.159  1.00 28.34           O  
ATOM   2636  CB  ILE A 354     -34.187 -22.273  -9.712  1.00 26.87           C  
ATOM   2637  CG1 ILE A 354     -33.887 -20.762  -9.639  1.00 25.86           C  
ATOM   2638  CG2 ILE A 354     -32.911 -23.106  -9.558  1.00 25.84           C  
ATOM   2639  CD1 ILE A 354     -33.515 -20.249  -8.262  1.00 25.85           C  
ATOM   2640  N   GLN A 355     -35.766 -24.824 -10.691  1.00 27.38           N  
ATOM   2641  CA  GLN A 355     -35.860 -26.264 -10.830  1.00 27.88           C  
ATOM   2642  C   GLN A 355     -36.278 -26.677 -12.241  1.00 28.07           C  
ATOM   2643  O   GLN A 355     -35.801 -27.688 -12.741  1.00 28.99           O  
ATOM   2644  CB  GLN A 355     -36.839 -26.836  -9.791  1.00 28.16           C  
ATOM   2645  CG  GLN A 355     -36.800 -28.360  -9.654  1.00 30.10           C  
ATOM   2646  CD  GLN A 355     -37.523 -29.083 -10.785  1.00 31.72           C  
ATOM   2647  OE1 GLN A 355     -38.469 -28.556 -11.375  1.00 32.06           O  
ATOM   2648  NE2 GLN A 355     -37.068 -30.288 -11.099  1.00 30.90           N  
ATOM   2649  N   ALA A 356     -37.165 -25.908 -12.867  1.00 27.60           N  
ATOM   2650  CA  ALA A 356     -37.669 -26.238 -14.201  1.00 29.02           C  
ATOM   2651  C   ALA A 356     -36.765 -25.712 -15.316  1.00 30.82           C  
ATOM   2652  O   ALA A 356     -37.038 -25.950 -16.492  1.00 32.97           O  
ATOM   2653  CB  ALA A 356     -39.097 -25.714 -14.387  1.00 28.55           C  
ATOM   2654  N   SER A 357     -35.697 -25.008 -14.947  1.00 30.25           N  
ATOM   2655  CA  SER A 357     -34.878 -24.275 -15.923  1.00 31.55           C  
ATOM   2656  C   SER A 357     -33.970 -25.161 -16.770  1.00 33.29           C  
ATOM   2657  O   SER A 357     -33.587 -24.778 -17.880  1.00 34.99           O  
ATOM   2658  CB  SER A 357     -34.015 -23.236 -15.212  1.00 28.93           C  
ATOM   2659  OG  SER A 357     -32.976 -23.847 -14.456  1.00 28.27           O  
ATOM   2660  N   GLY A 358     -33.599 -26.321 -16.240  1.00 33.03           N  
ATOM   2661  CA  GLY A 358     -32.621 -27.183 -16.910  1.00 33.87           C  
ATOM   2662  C   GLY A 358     -31.182 -26.842 -16.544  1.00 35.50           C  
ATOM   2663  O   GLY A 358     -30.241 -27.393 -17.119  1.00 36.25           O  
ATOM   2664  N   HIS A 359     -31.016 -25.917 -15.600  1.00 33.88           N  
ATOM   2665  CA  HIS A 359     -29.725 -25.623 -14.998  1.00 33.61           C  
ATOM   2666  C   HIS A 359     -29.703 -26.215 -13.614  1.00 34.39           C  
ATOM   2667  O   HIS A 359     -30.633 -26.004 -12.823  1.00 32.08           O  
ATOM   2668  CB  HIS A 359     -29.473 -24.118 -14.978  1.00 33.23           C  
ATOM   2669  CG  HIS A 359     -29.383 -23.511 -16.357  1.00 32.94           C  
ATOM   2670  ND1 HIS A 359     -28.267 -23.593 -17.112  1.00 32.25           N  
ATOM   2671  CD2 HIS A 359     -30.328 -22.837 -17.120  1.00 31.85           C  
ATOM   2672  CE1 HIS A 359     -28.489 -22.992 -18.292  1.00 32.08           C  
ATOM   2673  NE2 HIS A 359     -29.752 -22.531 -18.293  1.00 33.21           N  
ATOM   2674  N   TYR A 360     -28.651 -26.973 -13.314  1.00 33.58           N  
ATOM   2675  CA  TYR A 360     -28.625 -27.792 -12.098  1.00 36.24           C  
ATOM   2676  C   TYR A 360     -27.639 -27.304 -11.054  1.00 34.42           C  
ATOM   2677  O   TYR A 360     -26.425 -27.271 -11.292  1.00 33.49           O  
ATOM   2678  CB  TYR A 360     -28.351 -29.264 -12.437  1.00 39.12           C  
ATOM   2679  CG  TYR A 360     -29.214 -29.772 -13.567  1.00 41.30           C  
ATOM   2680  CD1 TYR A 360     -30.608 -29.788 -13.451  1.00 41.83           C  
ATOM   2681  CD2 TYR A 360     -28.640 -30.221 -14.757  1.00 41.66           C  
ATOM   2682  CE1 TYR A 360     -31.404 -30.246 -14.489  1.00 43.60           C  
ATOM   2683  CE2 TYR A 360     -29.427 -30.680 -15.801  1.00 43.06           C  
ATOM   2684  CZ  TYR A 360     -30.804 -30.694 -15.661  1.00 43.44           C  
ATOM   2685  OH  TYR A 360     -31.587 -31.143 -16.696  1.00 44.63           O  
ATOM   2686  N   SER A 361     -28.168 -26.914  -9.899  1.00 30.81           N  
ATOM   2687  CA  SER A 361     -27.315 -26.503  -8.790  1.00 31.34           C  
ATOM   2688  C   SER A 361     -27.342 -27.501  -7.641  1.00 31.74           C  
ATOM   2689  O   SER A 361     -28.409 -27.825  -7.108  1.00 28.53           O  
ATOM   2690  CB  SER A 361     -27.694 -25.110  -8.280  1.00 30.71           C  
ATOM   2691  OG  SER A 361     -26.829 -24.726  -7.219  1.00 29.78           O  
ATOM   2692  N   PHE A 362     -26.156 -27.975  -7.263  1.00 34.50           N  
ATOM   2693  CA  PHE A 362     -25.999 -28.896  -6.133  1.00 38.37           C  
ATOM   2694  C   PHE A 362     -25.699 -28.202  -4.795  1.00 36.77           C  
ATOM   2695  O   PHE A 362     -25.994 -28.742  -3.735  1.00 39.47           O  
ATOM   2696  CB  PHE A 362     -24.916 -29.941  -6.442  1.00 41.02           C  
ATOM   2697  CG  PHE A 362     -25.363 -31.012  -7.401  1.00 45.77           C  
ATOM   2698  CD1 PHE A 362     -26.161 -32.075  -6.963  1.00 47.33           C  
ATOM   2699  CD2 PHE A 362     -24.990 -30.967  -8.744  1.00 47.06           C  
ATOM   2700  CE1 PHE A 362     -26.574 -33.068  -7.850  1.00 49.49           C  
ATOM   2701  CE2 PHE A 362     -25.403 -31.957  -9.633  1.00 49.30           C  
ATOM   2702  CZ  PHE A 362     -26.196 -33.007  -9.188  1.00 48.34           C  
ATOM   2703  N   LEU A 363     -25.111 -27.014  -4.850  1.00 34.95           N  
ATOM   2704  CA  LEU A 363     -24.671 -26.316  -3.648  1.00 36.45           C  
ATOM   2705  C   LEU A 363     -25.616 -25.167  -3.325  1.00 34.50           C  
ATOM   2706  O   LEU A 363     -25.482 -24.074  -3.869  1.00 36.04           O  
ATOM   2707  CB  LEU A 363     -23.235 -25.805  -3.814  1.00 38.10           C  
ATOM   2708  CG  LEU A 363     -22.097 -26.815  -4.002  1.00 41.57           C  
ATOM   2709  CD1 LEU A 363     -20.764 -26.100  -3.827  1.00 43.41           C  
ATOM   2710  CD2 LEU A 363     -22.178 -27.997  -3.044  1.00 41.23           C  
ATOM   2711  N   ASN A 364     -26.579 -25.424  -2.446  1.00 32.83           N  
ATOM   2712  CA  ASN A 364     -27.668 -24.479  -2.222  1.00 32.27           C  
ATOM   2713  C   ASN A 364     -27.815 -24.020  -0.760  1.00 32.86           C  
ATOM   2714  O   ASN A 364     -28.103 -24.817   0.142  1.00 32.47           O  
ATOM   2715  CB  ASN A 364     -28.981 -25.054  -2.746  1.00 32.63           C  
ATOM   2716  CG  ASN A 364     -28.861 -25.596  -4.162  1.00 32.67           C  
ATOM   2717  OD1 ASN A 364     -29.050 -26.785  -4.392  1.00 33.09           O  
ATOM   2718  ND2 ASN A 364     -28.529 -24.730  -5.113  1.00 31.97           N  
ATOM   2719  N   VAL A 365     -27.607 -22.729  -0.547  1.00 29.96           N  
ATOM   2720  CA  VAL A 365     -27.719 -22.130   0.771  1.00 29.41           C  
ATOM   2721  C   VAL A 365     -29.109 -21.523   0.922  1.00 28.80           C  
ATOM   2722  O   VAL A 365     -29.638 -20.887  -0.003  1.00 29.60           O  
ATOM   2723  CB  VAL A 365     -26.627 -21.071   0.997  1.00 30.80           C  
ATOM   2724  CG1 VAL A 365     -26.982 -20.138   2.156  1.00 31.78           C  
ATOM   2725  CG2 VAL A 365     -25.289 -21.751   1.241  1.00 31.06           C  
ATOM   2726  N   PHE A 366     -29.709 -21.768   2.077  1.00 26.67           N  
ATOM   2727  CA  PHE A 366     -31.008 -21.219   2.415  1.00 24.75           C  
ATOM   2728  C   PHE A 366     -30.872 -20.619   3.813  1.00 25.34           C  
ATOM   2729  O   PHE A 366     -30.373 -21.271   4.740  1.00 24.89           O  
ATOM   2730  CB  PHE A 366     -32.059 -22.338   2.367  1.00 25.69           C  
ATOM   2731  CG  PHE A 366     -33.458 -21.911   2.730  1.00 26.62           C  
ATOM   2732  CD1 PHE A 366     -34.479 -21.959   1.780  1.00 29.91           C  
ATOM   2733  CD2 PHE A 366     -33.774 -21.523   4.020  1.00 27.05           C  
ATOM   2734  CE1 PHE A 366     -35.782 -21.592   2.114  1.00 30.89           C  
ATOM   2735  CE2 PHE A 366     -35.061 -21.144   4.359  1.00 27.67           C  
ATOM   2736  CZ  PHE A 366     -36.066 -21.177   3.408  1.00 29.63           C  
ATOM   2737  N   LYS A 367     -31.298 -19.369   3.966  1.00 24.70           N  
ATOM   2738  CA  LYS A 367     -31.327 -18.747   5.279  1.00 23.83           C  
ATOM   2739  C   LYS A 367     -32.422 -17.680   5.354  1.00 23.45           C  
ATOM   2740  O   LYS A 367     -32.696 -16.993   4.375  1.00 22.82           O  
ATOM   2741  CB  LYS A 367     -29.942 -18.213   5.677  1.00 25.34           C  
ATOM   2742  CG  LYS A 367     -29.965 -16.899   6.434  1.00 26.85           C  
ATOM   2743  CD  LYS A 367     -28.917 -16.812   7.512  1.00 27.18           C  
ATOM   2744  CE  LYS A 367     -29.514 -16.117   8.729  1.00 26.46           C  
ATOM   2745  NZ  LYS A 367     -30.123 -17.123   9.634  1.00 24.01           N  
ATOM   2746  N   LEU A 368     -33.084 -17.584   6.507  1.00 22.67           N  
ATOM   2747  CA  LEU A 368     -34.016 -16.479   6.742  1.00 21.64           C  
ATOM   2748  C   LEU A 368     -33.292 -15.290   7.387  1.00 20.29           C  
ATOM   2749  O   LEU A 368     -32.854 -15.364   8.535  1.00 20.97           O  
ATOM   2750  CB  LEU A 368     -35.215 -16.929   7.595  1.00 21.41           C  
ATOM   2751  CG  LEU A 368     -36.286 -15.876   7.930  1.00 21.41           C  
ATOM   2752  CD1 LEU A 368     -36.890 -15.273   6.665  1.00 22.00           C  
ATOM   2753  CD2 LEU A 368     -37.389 -16.484   8.801  1.00 21.82           C  
ATOM   2754  N   PHE A 369     -33.135 -14.202   6.630  1.00 21.53           N  
ATOM   2755  CA  PHE A 369     -32.509 -12.978   7.147  1.00 21.49           C  
ATOM   2756  C   PHE A 369     -33.403 -12.270   8.176  1.00 22.80           C  
ATOM   2757  O   PHE A 369     -34.635 -12.349   8.087  1.00 22.53           O  
ATOM   2758  CB  PHE A 369     -32.259 -11.998   6.006  1.00 22.32           C  
ATOM   2759  CG  PHE A 369     -30.993 -12.248   5.225  1.00 21.98           C  
ATOM   2760  CD1 PHE A 369     -29.954 -13.007   5.746  1.00 21.90           C  
ATOM   2761  CD2 PHE A 369     -30.830 -11.669   3.966  1.00 22.62           C  
ATOM   2762  CE1 PHE A 369     -28.787 -13.213   5.023  1.00 22.59           C  
ATOM   2763  CE2 PHE A 369     -29.668 -11.866   3.241  1.00 22.36           C  
ATOM   2764  CZ  PHE A 369     -28.637 -12.626   3.773  1.00 22.32           C  
ATOM   2765  N   GLY A 370     -32.788 -11.572   9.132  1.00 22.92           N  
ATOM   2766  CA  GLY A 370     -33.539 -10.694  10.033  1.00 23.96           C  
ATOM   2767  C   GLY A 370     -33.557  -9.231   9.575  1.00 24.16           C  
ATOM   2768  O   GLY A 370     -33.297  -8.949   8.410  1.00 23.42           O  
ATOM   2769  N   PRO A 371     -33.869  -8.292  10.500  1.00 24.55           N  
ATOM   2770  CA  PRO A 371     -33.894  -6.839  10.251  1.00 24.46           C  
ATOM   2771  C   PRO A 371     -32.661  -6.286   9.498  1.00 24.42           C  
ATOM   2772  O   PRO A 371     -31.536  -6.723   9.745  1.00 25.39           O  
ATOM   2773  CB  PRO A 371     -33.991  -6.249  11.673  1.00 25.10           C  
ATOM   2774  CG  PRO A 371     -34.777  -7.291  12.432  1.00 24.53           C  
ATOM   2775  CD  PRO A 371     -34.288  -8.618  11.884  1.00 24.08           C  
ATOM   2776  N   ARG A 372     -32.894  -5.338   8.586  1.00 23.59           N  
ATOM   2777  CA  ARG A 372     -31.828  -4.716   7.795  1.00 25.10           C  
ATOM   2778  C   ARG A 372     -31.141  -3.599   8.585  1.00 25.19           C  
ATOM   2779  O   ARG A 372     -31.582  -3.245   9.676  1.00 23.33           O  
ATOM   2780  CB  ARG A 372     -32.378  -4.194   6.453  1.00 24.92           C  
ATOM   2781  CG  ARG A 372     -33.436  -3.077   6.567  1.00 25.13           C  
ATOM   2782  CD  ARG A 372     -33.548  -2.302   5.250  1.00 25.64           C  
ATOM   2783  NE  ARG A 372     -32.275  -1.648   4.940  1.00 25.96           N  
ATOM   2784  CZ  ARG A 372     -31.753  -1.472   3.728  1.00 26.57           C  
ATOM   2785  NH1 ARG A 372     -32.380  -1.879   2.628  1.00 25.37           N  
ATOM   2786  NH2 ARG A 372     -30.577  -0.867   3.626  1.00 27.62           N  
ATOM   2787  N   ASN A 373     -30.039  -3.061   8.059  1.00 24.51           N  
ATOM   2788  CA  ASN A 373     -29.433  -1.900   8.702  1.00 23.49           C  
ATOM   2789  C   ASN A 373     -29.608  -0.619   7.884  1.00 23.53           C  
ATOM   2790  O   ASN A 373     -30.262  -0.605   6.835  1.00 22.12           O  
ATOM   2791  CB  ASN A 373     -27.967  -2.150   9.101  1.00 23.59           C  
ATOM   2792  CG  ASN A 373     -27.035  -2.280   7.895  1.00 22.27           C  
ATOM   2793  OD1 ASN A 373     -27.296  -1.730   6.824  1.00 23.84           O  
ATOM   2794  ND2 ASN A 373     -25.959  -3.024   8.065  1.00 24.02           N  
ATOM   2795  N   GLN A 374     -29.045   0.472   8.379  1.00 24.56           N  
ATOM   2796  CA  GLN A 374     -29.317   1.760   7.755  1.00 26.62           C  
ATOM   2797  C   GLN A 374     -28.385   2.063   6.564  1.00 25.06           C  
ATOM   2798  O   GLN A 374     -28.432   3.155   5.993  1.00 24.97           O  
ATOM   2799  CB  GLN A 374     -29.304   2.881   8.807  1.00 28.76           C  
ATOM   2800  CG  GLN A 374     -27.913   3.199   9.317  1.00 33.23           C  
ATOM   2801  CD  GLN A 374     -27.925   3.946  10.633  1.00 37.47           C  
ATOM   2802  OE1 GLN A 374     -28.062   3.345  11.702  1.00 37.32           O  
ATOM   2803  NE2 GLN A 374     -27.737   5.266  10.563  1.00 37.75           N  
ATOM   2804  N   ALA A 375     -27.556   1.101   6.164  1.00 23.92           N  
ATOM   2805  CA  ALA A 375     -26.665   1.329   5.006  1.00 22.43           C  
ATOM   2806  C   ALA A 375     -27.440   1.240   3.687  1.00 21.80           C  
ATOM   2807  O   ALA A 375     -28.026   0.194   3.384  1.00 22.08           O  
ATOM   2808  CB  ALA A 375     -25.506   0.342   5.014  1.00 22.39           C  
ATOM   2809  N   PRO A 376     -27.434   2.321   2.876  1.00 20.82           N  
ATOM   2810  CA  PRO A 376     -28.313   2.308   1.698  1.00 21.07           C  
ATOM   2811  C   PRO A 376     -28.022   1.242   0.647  1.00 21.02           C  
ATOM   2812  O   PRO A 376     -28.952   0.823  -0.025  1.00 21.07           O  
ATOM   2813  CB  PRO A 376     -28.175   3.717   1.117  1.00 21.30           C  
ATOM   2814  CG  PRO A 376     -26.972   4.311   1.759  1.00 20.64           C  
ATOM   2815  CD  PRO A 376     -26.775   3.623   3.068  1.00 21.02           C  
ATOM   2816  N   LEU A 377     -26.755   0.835   0.495  1.00 21.14           N  
ATOM   2817  CA  LEU A 377     -26.382  -0.249  -0.418  1.00 22.32           C  
ATOM   2818  C   LEU A 377     -26.198  -1.628   0.257  1.00 21.48           C  
ATOM   2819  O   LEU A 377     -25.757  -2.557  -0.398  1.00 22.26           O  
ATOM   2820  CB  LEU A 377     -25.108   0.090  -1.228  1.00 23.26           C  
ATOM   2821  CG  LEU A 377     -25.116   0.879  -2.544  1.00 25.34           C  
ATOM   2822  CD1 LEU A 377     -23.902   0.498  -3.402  1.00 27.23           C  
ATOM   2823  CD2 LEU A 377     -26.398   0.706  -3.343  1.00 24.20           C  
ATOM   2824  N   SER A 378     -26.499  -1.749   1.551  1.00 21.15           N  
ATOM   2825  CA  SER A 378     -26.486  -3.052   2.262  1.00 21.54           C  
ATOM   2826  C   SER A 378     -27.353  -4.063   1.498  1.00 20.21           C  
ATOM   2827  O   SER A 378     -28.451  -3.734   1.077  1.00 20.70           O  
ATOM   2828  CB  SER A 378     -27.038  -2.876   3.685  1.00 21.87           C  
ATOM   2829  OG  SER A 378     -26.920  -4.060   4.471  1.00 24.04           O  
ATOM   2830  N   PHE A 379     -26.850  -5.275   1.291  1.00 18.79           N  
ATOM   2831  CA  PHE A 379     -27.621  -6.315   0.630  1.00 18.41           C  
ATOM   2832  C   PHE A 379     -28.763  -6.898   1.501  1.00 18.33           C  
ATOM   2833  O   PHE A 379     -29.884  -7.001   1.014  1.00 17.09           O  
ATOM   2834  CB  PHE A 379     -26.690  -7.409   0.072  1.00 19.06           C  
ATOM   2835  CG  PHE A 379     -27.379  -8.722  -0.235  1.00 19.83           C  
ATOM   2836  CD1 PHE A 379     -28.209  -8.857  -1.352  1.00 19.19           C  
ATOM   2837  CD2 PHE A 379     -27.159  -9.839   0.577  1.00 19.32           C  
ATOM   2838  CE1 PHE A 379     -28.826 -10.067  -1.633  1.00 20.07           C  
ATOM   2839  CE2 PHE A 379     -27.759 -11.056   0.289  1.00 19.28           C  
ATOM   2840  CZ  PHE A 379     -28.608 -11.168  -0.811  1.00 19.27           C  
ATOM   2841  N   PRO A 380     -28.486  -7.266   2.771  1.00 18.23           N  
ATOM   2842  CA  PRO A 380     -29.540  -8.020   3.465  1.00 19.38           C  
ATOM   2843  C   PRO A 380     -30.782  -7.197   3.789  1.00 19.70           C  
ATOM   2844  O   PRO A 380     -30.687  -6.031   4.188  1.00 18.99           O  
ATOM   2845  CB  PRO A 380     -28.869  -8.455   4.767  1.00 18.99           C  
ATOM   2846  CG  PRO A 380     -27.406  -8.479   4.451  1.00 19.77           C  
ATOM   2847  CD  PRO A 380     -27.209  -7.315   3.517  1.00 18.88           C  
ATOM   2848  N   ILE A 381     -31.932  -7.818   3.571  1.00 21.34           N  
ATOM   2849  CA  ILE A 381     -33.221  -7.298   4.018  1.00 20.76           C  
ATOM   2850  C   ILE A 381     -33.917  -8.514   4.630  1.00 21.19           C  
ATOM   2851  O   ILE A 381     -33.584  -9.643   4.271  1.00 20.89           O  
ATOM   2852  CB  ILE A 381     -34.043  -6.698   2.856  1.00 20.27           C  
ATOM   2853  CG1 ILE A 381     -34.336  -7.757   1.782  1.00 21.09           C  
ATOM   2854  CG2 ILE A 381     -33.307  -5.503   2.249  1.00 20.52           C  
ATOM   2855  CD1 ILE A 381     -35.413  -7.365   0.784  1.00 20.87           C  
ATOM   2856  N   PRO A 382     -34.846  -8.301   5.581  1.00 20.93           N  
ATOM   2857  CA  PRO A 382     -35.543  -9.482   6.133  1.00 21.39           C  
ATOM   2858  C   PRO A 382     -36.248 -10.328   5.057  1.00 21.28           C  
ATOM   2859  O   PRO A 382     -36.987  -9.805   4.229  1.00 23.48           O  
ATOM   2860  CB  PRO A 382     -36.547  -8.875   7.135  1.00 20.34           C  
ATOM   2861  CG  PRO A 382     -36.596  -7.399   6.825  1.00 21.07           C  
ATOM   2862  CD  PRO A 382     -35.225  -7.057   6.279  1.00 20.45           C  
ATOM   2863  N   GLY A 383     -35.999 -11.628   5.050  1.00 20.94           N  
ATOM   2864  CA  GLY A 383     -36.634 -12.477   4.063  1.00 21.14           C  
ATOM   2865  C   GLY A 383     -35.750 -13.625   3.628  1.00 21.72           C  
ATOM   2866  O   GLY A 383     -34.739 -13.913   4.253  1.00 22.05           O  
ATOM   2867  N   TRP A 384     -36.145 -14.251   2.529  1.00 21.96           N  
ATOM   2868  CA  TRP A 384     -35.658 -15.559   2.142  1.00 23.15           C  
ATOM   2869  C   TRP A 384     -34.440 -15.417   1.288  1.00 22.33           C  
ATOM   2870  O   TRP A 384     -34.538 -14.987   0.149  1.00 23.15           O  
ATOM   2871  CB  TRP A 384     -36.765 -16.282   1.384  1.00 23.99           C  
ATOM   2872  CG  TRP A 384     -38.067 -16.290   2.156  1.00 24.59           C  
ATOM   2873  CD1 TRP A 384     -39.205 -15.517   1.933  1.00 24.97           C  
ATOM   2874  CD2 TRP A 384     -38.369 -17.085   3.338  1.00 25.20           C  
ATOM   2875  NE1 TRP A 384     -40.178 -15.790   2.866  1.00 25.64           N  
ATOM   2876  CE2 TRP A 384     -39.737 -16.726   3.741  1.00 25.91           C  
ATOM   2877  CE3 TRP A 384     -37.670 -18.033   4.082  1.00 26.04           C  
ATOM   2878  CZ2 TRP A 384     -40.354 -17.312   4.831  1.00 26.05           C  
ATOM   2879  CZ3 TRP A 384     -38.306 -18.614   5.185  1.00 26.51           C  
ATOM   2880  CH2 TRP A 384     -39.611 -18.257   5.550  1.00 26.12           C  
ATOM   2881  N   ASN A 385     -33.291 -15.769   1.845  1.00 22.50           N  
ATOM   2882  CA  ASN A 385     -32.002 -15.622   1.161  1.00 23.57           C  
ATOM   2883  C   ASN A 385     -31.543 -16.971   0.605  1.00 24.47           C  
ATOM   2884  O   ASN A 385     -31.559 -17.978   1.316  1.00 25.64           O  
ATOM   2885  CB  ASN A 385     -30.947 -15.050   2.114  1.00 22.10           C  
ATOM   2886  CG  ASN A 385     -29.541 -15.103   1.540  1.00 22.94           C  
ATOM   2887  OD1 ASN A 385     -29.130 -14.227   0.773  1.00 23.22           O  
ATOM   2888  ND2 ASN A 385     -28.787 -16.133   1.920  1.00 23.09           N  
ATOM   2889  N   ILE A 386     -31.106 -16.954  -0.650  1.00 25.25           N  
ATOM   2890  CA  ILE A 386     -30.790 -18.139  -1.426  1.00 26.16           C  
ATOM   2891  C   ILE A 386     -29.447 -17.955  -2.137  1.00 25.90           C  
ATOM   2892  O   ILE A 386     -29.227 -16.921  -2.770  1.00 26.81           O  
ATOM   2893  CB  ILE A 386     -31.887 -18.366  -2.498  1.00 27.80           C  
ATOM   2894  CG1 ILE A 386     -33.206 -18.808  -1.859  1.00 29.04           C  
ATOM   2895  CG2 ILE A 386     -31.467 -19.387  -3.543  1.00 29.29           C  
ATOM   2896  CD1 ILE A 386     -33.060 -19.945  -0.868  1.00 29.23           C  
ATOM   2897  N   CYS A 387     -28.561 -18.946  -2.040  1.00 25.80           N  
ATOM   2898  CA  CYS A 387     -27.384 -19.020  -2.929  1.00 27.63           C  
ATOM   2899  C   CYS A 387     -27.442 -20.278  -3.743  1.00 27.28           C  
ATOM   2900  O   CYS A 387     -27.676 -21.359  -3.198  1.00 26.37           O  
ATOM   2901  CB  CYS A 387     -26.077 -19.072  -2.160  1.00 30.59           C  
ATOM   2902  SG  CYS A 387     -25.918 -17.784  -0.946  1.00 36.62           S  
ATOM   2903  N   VAL A 388     -27.228 -20.134  -5.046  1.00 27.38           N  
ATOM   2904  CA  VAL A 388     -27.174 -21.275  -5.941  1.00 27.94           C  
ATOM   2905  C   VAL A 388     -25.911 -21.194  -6.786  1.00 28.26           C  
ATOM   2906  O   VAL A 388     -25.348 -20.122  -6.969  1.00 27.44           O  
ATOM   2907  CB  VAL A 388     -28.436 -21.404  -6.831  1.00 28.64           C  
ATOM   2908  CG1 VAL A 388     -29.659 -21.733  -5.984  1.00 29.52           C  
ATOM   2909  CG2 VAL A 388     -28.673 -20.130  -7.634  1.00 29.02           C  
ATOM   2910  N   ASP A 389     -25.481 -22.343  -7.291  1.00 30.02           N  
ATOM   2911  CA  ASP A 389     -24.278 -22.450  -8.108  1.00 33.10           C  
ATOM   2912  C   ASP A 389     -24.595 -23.146  -9.411  1.00 33.14           C  
ATOM   2913  O   ASP A 389     -24.803 -24.365  -9.424  1.00 33.67           O  
ATOM   2914  CB  ASP A 389     -23.211 -23.253  -7.370  1.00 37.11           C  
ATOM   2915  CG  ASP A 389     -22.013 -22.437  -7.044  1.00 42.77           C  
ATOM   2916  OD1 ASP A 389     -21.167 -22.229  -7.950  1.00 45.84           O  
ATOM   2917  OD2 ASP A 389     -21.915 -22.001  -5.882  1.00 47.64           O  
ATOM   2918  N   PHE A 390     -24.640 -22.387 -10.503  1.00 30.26           N  
ATOM   2919  CA  PHE A 390     -24.975 -22.982 -11.801  1.00 29.92           C  
ATOM   2920  C   PHE A 390     -23.712 -23.213 -12.623  1.00 29.87           C  
ATOM   2921  O   PHE A 390     -22.964 -22.272 -12.866  1.00 31.12           O  
ATOM   2922  CB  PHE A 390     -25.872 -22.079 -12.636  1.00 28.13           C  
ATOM   2923  CG  PHE A 390     -27.184 -21.722 -12.002  1.00 27.24           C  
ATOM   2924  CD1 PHE A 390     -28.147 -22.692 -11.735  1.00 27.32           C  
ATOM   2925  CD2 PHE A 390     -27.481 -20.394 -11.746  1.00 26.62           C  
ATOM   2926  CE1 PHE A 390     -29.373 -22.336 -11.181  1.00 27.72           C  
ATOM   2927  CE2 PHE A 390     -28.705 -20.028 -11.202  1.00 27.28           C  
ATOM   2928  CZ  PHE A 390     -29.653 -21.001 -10.920  1.00 26.19           C  
ATOM   2929  N   PRO A 391     -23.499 -24.455 -13.087  1.00 30.43           N  
ATOM   2930  CA  PRO A 391     -22.466 -24.739 -14.098  1.00 31.65           C  
ATOM   2931  C   PRO A 391     -22.682 -23.876 -15.350  1.00 31.83           C  
ATOM   2932  O   PRO A 391     -23.821 -23.727 -15.801  1.00 30.97           O  
ATOM   2933  CB  PRO A 391     -22.699 -26.219 -14.435  1.00 31.23           C  
ATOM   2934  CG  PRO A 391     -23.415 -26.782 -13.252  1.00 32.60           C  
ATOM   2935  CD  PRO A 391     -24.247 -25.661 -12.696  1.00 30.99           C  
ATOM   2936  N   ILE A 392     -21.611 -23.288 -15.880  1.00 32.03           N  
ATOM   2937  CA  ILE A 392     -21.714 -22.454 -17.072  1.00 33.00           C  
ATOM   2938  C   ILE A 392     -21.946 -23.342 -18.290  1.00 34.76           C  
ATOM   2939  O   ILE A 392     -21.168 -24.256 -18.565  1.00 35.16           O  
ATOM   2940  CB  ILE A 392     -20.473 -21.548 -17.281  1.00 33.91           C  
ATOM   2941  CG1 ILE A 392     -20.397 -20.477 -16.183  1.00 34.81           C  
ATOM   2942  CG2 ILE A 392     -20.508 -20.881 -18.651  1.00 32.50           C  
ATOM   2943  CD1 ILE A 392     -19.121 -19.653 -16.217  1.00 35.50           C  
ATOM   2944  N   LYS A 393     -23.040 -23.068 -18.995  1.00 34.95           N  
ATOM   2945  CA  LYS A 393     -23.425 -23.800 -20.194  1.00 33.13           C  
ATOM   2946  C   LYS A 393     -24.394 -22.937 -21.004  1.00 33.02           C  
ATOM   2947  O   LYS A 393     -24.864 -21.906 -20.515  1.00 31.34           O  
ATOM   2948  CB  LYS A 393     -24.050 -25.143 -19.818  1.00 33.58           C  
ATOM   2949  CG  LYS A 393     -25.446 -25.067 -19.217  1.00 33.30           C  
ATOM   2950  CD  LYS A 393     -25.829 -26.405 -18.610  1.00 32.28           C  
ATOM   2951  CE  LYS A 393     -27.334 -26.570 -18.561  1.00 32.24           C  
ATOM   2952  NZ  LYS A 393     -27.699 -27.801 -17.810  1.00 30.63           N  
ATOM   2953  N   ASP A 394     -24.699 -23.351 -22.231  1.00 31.75           N  
ATOM   2954  CA  ASP A 394     -25.538 -22.535 -23.108  1.00 31.89           C  
ATOM   2955  C   ASP A 394     -26.866 -22.166 -22.473  1.00 31.34           C  
ATOM   2956  O   ASP A 394     -27.525 -23.004 -21.844  1.00 29.53           O  
ATOM   2957  CB  ASP A 394     -25.805 -23.245 -24.431  1.00 33.91           C  
ATOM   2958  CG  ASP A 394     -24.573 -23.335 -25.300  1.00 36.03           C  
ATOM   2959  OD1 ASP A 394     -23.657 -22.494 -25.151  1.00 36.20           O  
ATOM   2960  OD2 ASP A 394     -24.535 -24.246 -26.144  1.00 39.72           O  
ATOM   2961  N   GLY A 395     -27.253 -20.910 -22.654  1.00 29.76           N  
ATOM   2962  CA  GLY A 395     -28.537 -20.437 -22.176  1.00 29.97           C  
ATOM   2963  C   GLY A 395     -28.507 -19.851 -20.771  1.00 29.81           C  
ATOM   2964  O   GLY A 395     -29.473 -19.208 -20.365  1.00 27.77           O  
ATOM   2965  N   LEU A 396     -27.419 -20.075 -20.026  1.00 28.02           N  
ATOM   2966  CA  LEU A 396     -27.348 -19.609 -18.624  1.00 27.70           C  
ATOM   2967  C   LEU A 396     -27.431 -18.095 -18.474  1.00 27.12           C  
ATOM   2968  O   LEU A 396     -28.171 -17.607 -17.628  1.00 27.73           O  
ATOM   2969  CB  LEU A 396     -26.108 -20.143 -17.881  1.00 26.55           C  
ATOM   2970  CG  LEU A 396     -26.005 -19.747 -16.399  1.00 27.18           C  
ATOM   2971  CD1 LEU A 396     -27.180 -20.312 -15.586  1.00 25.98           C  
ATOM   2972  CD2 LEU A 396     -24.673 -20.163 -15.786  1.00 26.43           C  
ATOM   2973  N   GLY A 397     -26.677 -17.356 -19.285  1.00 26.91           N  
ATOM   2974  CA  GLY A 397     -26.679 -15.893 -19.207  1.00 27.82           C  
ATOM   2975  C   GLY A 397     -28.079 -15.326 -19.362  1.00 27.67           C  
ATOM   2976  O   GLY A 397     -28.506 -14.479 -18.595  1.00 28.34           O  
ATOM   2977  N   LYS A 398     -28.805 -15.805 -20.361  1.00 28.62           N  
ATOM   2978  CA  LYS A 398     -30.146 -15.305 -20.604  1.00 28.88           C  
ATOM   2979  C   LYS A 398     -31.141 -15.789 -19.549  1.00 28.46           C  
ATOM   2980  O   LYS A 398     -32.079 -15.074 -19.209  1.00 29.50           O  
ATOM   2981  CB  LYS A 398     -30.595 -15.621 -22.029  1.00 31.40           C  
ATOM   2982  CG  LYS A 398     -29.942 -14.704 -23.051  1.00 33.29           C  
ATOM   2983  CD  LYS A 398     -30.661 -14.771 -24.383  1.00 35.99           C  
ATOM   2984  CE  LYS A 398     -30.215 -13.664 -25.322  1.00 37.50           C  
ATOM   2985  NZ  LYS A 398     -28.757 -13.714 -25.616  1.00 39.56           N  
ATOM   2986  N   PHE A 399     -30.914 -16.969 -18.987  1.00 27.76           N  
ATOM   2987  CA  PHE A 399     -31.765 -17.429 -17.887  1.00 27.11           C  
ATOM   2988  C   PHE A 399     -31.563 -16.631 -16.589  1.00 27.43           C  
ATOM   2989  O   PHE A 399     -32.545 -16.267 -15.927  1.00 25.92           O  
ATOM   2990  CB  PHE A 399     -31.583 -18.915 -17.613  1.00 28.13           C  
ATOM   2991  CG  PHE A 399     -32.287 -19.376 -16.376  1.00 28.67           C  
ATOM   2992  CD1 PHE A 399     -33.681 -19.433 -16.335  1.00 29.22           C  
ATOM   2993  CD2 PHE A 399     -31.564 -19.728 -15.244  1.00 28.44           C  
ATOM   2994  CE1 PHE A 399     -34.334 -19.845 -15.189  1.00 28.53           C  
ATOM   2995  CE2 PHE A 399     -32.216 -20.144 -14.091  1.00 28.85           C  
ATOM   2996  CZ  PHE A 399     -33.598 -20.201 -14.065  1.00 28.44           C  
ATOM   2997  N   VAL A 400     -30.318 -16.344 -16.224  1.00 25.84           N  
ATOM   2998  CA  VAL A 400     -30.102 -15.527 -15.024  1.00 28.21           C  
ATOM   2999  C   VAL A 400     -30.600 -14.083 -15.202  1.00 27.42           C  
ATOM   3000  O   VAL A 400     -30.940 -13.430 -14.226  1.00 26.96           O  
ATOM   3001  CB  VAL A 400     -28.663 -15.597 -14.463  1.00 29.49           C  
ATOM   3002  CG1 VAL A 400     -28.329 -17.021 -14.038  1.00 30.20           C  
ATOM   3003  CG2 VAL A 400     -27.646 -15.070 -15.468  1.00 30.99           C  
ATOM   3004  N   SER A 401     -30.680 -13.596 -16.442  1.00 27.91           N  
ATOM   3005  CA  SER A 401     -31.330 -12.305 -16.682  1.00 28.93           C  
ATOM   3006  C   SER A 401     -32.823 -12.382 -16.394  1.00 29.36           C  
ATOM   3007  O   SER A 401     -33.412 -11.411 -15.915  1.00 30.26           O  
ATOM   3008  CB  SER A 401     -31.084 -11.805 -18.104  1.00 31.19           C  
ATOM   3009  OG  SER A 401     -29.727 -11.429 -18.246  1.00 33.79           O  
ATOM   3010  N   GLU A 402     -33.433 -13.530 -16.681  1.00 28.47           N  
ATOM   3011  CA  GLU A 402     -34.845 -13.727 -16.352  1.00 30.25           C  
ATOM   3012  C   GLU A 402     -35.042 -13.834 -14.855  1.00 28.89           C  
ATOM   3013  O   GLU A 402     -35.990 -13.244 -14.318  1.00 30.73           O  
ATOM   3014  CB  GLU A 402     -35.459 -14.928 -17.087  1.00 30.94           C  
ATOM   3015  CG  GLU A 402     -35.606 -14.711 -18.591  1.00 32.14           C  
ATOM   3016  CD  GLU A 402     -36.413 -13.468 -18.927  1.00 34.56           C  
ATOM   3017  OE1 GLU A 402     -37.539 -13.313 -18.393  1.00 36.17           O  
ATOM   3018  OE2 GLU A 402     -35.914 -12.636 -19.709  1.00 32.43           O  
ATOM   3019  N   LEU A 403     -34.150 -14.563 -14.183  1.00 26.03           N  
ATOM   3020  CA  LEU A 403     -34.173 -14.615 -12.731  1.00 26.98           C  
ATOM   3021  C   LEU A 403     -34.079 -13.219 -12.123  1.00 26.32           C  
ATOM   3022  O   LEU A 403     -34.833 -12.916 -11.195  1.00 27.37           O  
ATOM   3023  CB  LEU A 403     -33.062 -15.514 -12.160  1.00 27.97           C  
ATOM   3024  CG  LEU A 403     -33.204 -17.038 -12.132  1.00 30.16           C  
ATOM   3025  CD1 LEU A 403     -32.021 -17.652 -11.383  1.00 29.23           C  
ATOM   3026  CD2 LEU A 403     -34.530 -17.475 -11.513  1.00 29.77           C  
ATOM   3027  N   ASP A 404     -33.164 -12.381 -12.640  1.00 24.56           N  
ATOM   3028  CA  ASP A 404     -33.014 -10.992 -12.184  1.00 24.51           C  
ATOM   3029  C   ASP A 404     -34.369 -10.296 -12.159  1.00 25.28           C  
ATOM   3030  O   ASP A 404     -34.717  -9.646 -11.184  1.00 25.05           O  
ATOM   3031  CB  ASP A 404     -32.103 -10.170 -13.107  1.00 25.32           C  
ATOM   3032  CG  ASP A 404     -30.620 -10.492 -12.960  1.00 25.47           C  
ATOM   3033  OD1 ASP A 404     -30.225 -11.332 -12.126  1.00 25.39           O  
ATOM   3034  OD2 ASP A 404     -29.823  -9.870 -13.704  1.00 26.44           O  
ATOM   3035  N   ARG A 405     -35.119 -10.448 -13.252  1.00 26.00           N  
ATOM   3036  CA  ARG A 405     -36.392  -9.780 -13.448  1.00 27.44           C  
ATOM   3037  C   ARG A 405     -37.414 -10.250 -12.420  1.00 26.04           C  
ATOM   3038  O   ARG A 405     -38.154  -9.448 -11.879  1.00 25.94           O  
ATOM   3039  CB  ARG A 405     -36.896 -10.017 -14.887  1.00 28.43           C  
ATOM   3040  CG  ARG A 405     -38.307  -9.528 -15.167  1.00 33.10           C  
ATOM   3041  CD  ARG A 405     -38.773  -9.872 -16.587  1.00 38.08           C  
ATOM   3042  NE  ARG A 405     -38.779 -11.319 -16.840  1.00 42.45           N  
ATOM   3043  CZ  ARG A 405     -39.775 -12.158 -16.539  1.00 43.06           C  
ATOM   3044  NH1 ARG A 405     -40.895 -11.721 -15.972  1.00 42.97           N  
ATOM   3045  NH2 ARG A 405     -39.650 -13.455 -16.817  1.00 43.88           N  
ATOM   3046  N   ARG A 406     -37.438 -11.549 -12.145  1.00 27.04           N  
ATOM   3047  CA  ARG A 406     -38.341 -12.079 -11.120  1.00 28.76           C  
ATOM   3048  C   ARG A 406     -37.934 -11.630  -9.722  1.00 26.60           C  
ATOM   3049  O   ARG A 406     -38.797 -11.233  -8.936  1.00 24.70           O  
ATOM   3050  CB  ARG A 406     -38.435 -13.600 -11.204  1.00 31.93           C  
ATOM   3051  CG  ARG A 406     -39.179 -14.061 -12.442  1.00 36.73           C  
ATOM   3052  CD  ARG A 406     -39.117 -15.568 -12.579  1.00 42.73           C  
ATOM   3053  NE  ARG A 406     -40.203 -16.112 -13.397  1.00 47.46           N  
ATOM   3054  CZ  ARG A 406     -41.461 -15.673 -13.407  1.00 49.46           C  
ATOM   3055  NH1 ARG A 406     -41.855 -14.665 -12.631  1.00 49.44           N  
ATOM   3056  NH2 ARG A 406     -42.334 -16.264 -14.196  1.00 50.67           N  
ATOM   3057  N   VAL A 407     -36.630 -11.666  -9.436  1.00 24.63           N  
ATOM   3058  CA  VAL A 407     -36.076 -11.175  -8.159  1.00 25.16           C  
ATOM   3059  C   VAL A 407     -36.486  -9.707  -7.942  1.00 24.33           C  
ATOM   3060  O   VAL A 407     -37.005  -9.348  -6.885  1.00 25.87           O  
ATOM   3061  CB  VAL A 407     -34.530 -11.329  -8.080  1.00 24.57           C  
ATOM   3062  CG1 VAL A 407     -33.958 -10.578  -6.885  1.00 24.96           C  
ATOM   3063  CG2 VAL A 407     -34.121 -12.797  -7.985  1.00 26.20           C  
ATOM   3064  N   LEU A 408     -36.283  -8.881  -8.962  1.00 24.46           N  
ATOM   3065  CA  LEU A 408     -36.640  -7.459  -8.900  1.00 24.92           C  
ATOM   3066  C   LEU A 408     -38.144  -7.269  -8.702  1.00 26.31           C  
ATOM   3067  O   LEU A 408     -38.581  -6.605  -7.754  1.00 25.72           O  
ATOM   3068  CB  LEU A 408     -36.173  -6.742 -10.176  1.00 25.12           C  
ATOM   3069  CG  LEU A 408     -36.692  -5.332 -10.474  1.00 25.69           C  
ATOM   3070  CD1 LEU A 408     -36.327  -4.397  -9.328  1.00 23.85           C  
ATOM   3071  CD2 LEU A 408     -36.118  -4.838 -11.801  1.00 25.42           C  
ATOM   3072  N   GLU A 409     -38.931  -7.866  -9.591  1.00 27.35           N  
ATOM   3073  CA  GLU A 409     -40.387  -7.793  -9.501  1.00 30.46           C  
ATOM   3074  C   GLU A 409     -40.915  -8.213  -8.120  1.00 29.04           C  
ATOM   3075  O   GLU A 409     -41.899  -7.651  -7.627  1.00 27.25           O  
ATOM   3076  CB  GLU A 409     -41.010  -8.627 -10.629  1.00 33.97           C  
ATOM   3077  CG  GLU A 409     -42.406  -9.160 -10.377  1.00 39.38           C  
ATOM   3078  CD  GLU A 409     -42.993  -9.839 -11.597  1.00 43.17           C  
ATOM   3079  OE1 GLU A 409     -42.316 -10.713 -12.189  1.00 45.83           O  
ATOM   3080  OE2 GLU A 409     -44.132  -9.488 -11.963  1.00 47.33           O  
ATOM   3081  N   PHE A 410     -40.251  -9.181  -7.493  1.00 26.91           N  
ATOM   3082  CA  PHE A 410     -40.684  -9.660  -6.185  1.00 27.72           C  
ATOM   3083  C   PHE A 410     -40.067  -8.898  -4.994  1.00 26.52           C  
ATOM   3084  O   PHE A 410     -40.035  -9.412  -3.874  1.00 24.86           O  
ATOM   3085  CB  PHE A 410     -40.459 -11.176  -6.059  1.00 29.39           C  
ATOM   3086  CG  PHE A 410     -41.263 -12.001  -7.038  1.00 32.28           C  
ATOM   3087  CD1 PHE A 410     -42.443 -11.509  -7.592  1.00 32.11           C  
ATOM   3088  CD2 PHE A 410     -40.853 -13.295  -7.378  1.00 33.76           C  
ATOM   3089  CE1 PHE A 410     -43.185 -12.276  -8.481  1.00 34.82           C  
ATOM   3090  CE2 PHE A 410     -41.597 -14.072  -8.261  1.00 35.61           C  
ATOM   3091  CZ  PHE A 410     -42.763 -13.560  -8.817  1.00 35.70           C  
ATOM   3092  N   GLY A 411     -39.590  -7.673  -5.246  1.00 24.63           N  
ATOM   3093  CA  GLY A 411     -39.011  -6.825  -4.200  1.00 23.71           C  
ATOM   3094  C   GLY A 411     -37.654  -7.206  -3.633  1.00 22.93           C  
ATOM   3095  O   GLY A 411     -37.227  -6.640  -2.616  1.00 23.21           O  
ATOM   3096  N   GLY A 412     -36.966  -8.155  -4.270  1.00 22.47           N  
ATOM   3097  CA  GLY A 412     -35.674  -8.611  -3.774  1.00 21.63           C  
ATOM   3098  C   GLY A 412     -34.487  -7.973  -4.473  1.00 23.24           C  
ATOM   3099  O   GLY A 412     -34.642  -7.058  -5.296  1.00 24.46           O  
ATOM   3100  N   ARG A 413     -33.294  -8.476  -4.173  1.00 22.42           N  
ATOM   3101  CA  ARG A 413     -32.069  -7.946  -4.786  1.00 21.64           C  
ATOM   3102  C   ARG A 413     -31.002  -9.017  -4.918  1.00 21.35           C  
ATOM   3103  O   ARG A 413     -31.081 -10.066  -4.274  1.00 20.62           O  
ATOM   3104  CB  ARG A 413     -31.505  -6.778  -3.955  1.00 20.27           C  
ATOM   3105  CG  ARG A 413     -31.220  -7.132  -2.497  1.00 19.56           C  
ATOM   3106  CD  ARG A 413     -32.379  -6.727  -1.580  1.00 19.95           C  
ATOM   3107  NE  ARG A 413     -32.581  -5.287  -1.711  1.00 19.93           N  
ATOM   3108  CZ  ARG A 413     -31.861  -4.368  -1.076  1.00 19.22           C  
ATOM   3109  NH1 ARG A 413     -30.943  -4.732  -0.195  1.00 18.89           N  
ATOM   3110  NH2 ARG A 413     -32.084  -3.075  -1.309  1.00 19.53           N  
ATOM   3111  N   LEU A 414     -29.988  -8.720  -5.731  1.00 22.69           N  
ATOM   3112  CA  LEU A 414     -28.753  -9.516  -5.798  1.00 23.01           C  
ATOM   3113  C   LEU A 414     -27.683  -8.898  -4.916  1.00 22.84           C  
ATOM   3114  O   LEU A 414     -27.774  -7.735  -4.541  1.00 22.47           O  
ATOM   3115  CB  LEU A 414     -28.203  -9.534  -7.231  1.00 24.95           C  
ATOM   3116  CG  LEU A 414     -29.115 -10.016  -8.345  1.00 26.65           C  
ATOM   3117  CD1 LEU A 414     -28.485  -9.739  -9.700  1.00 26.92           C  
ATOM   3118  CD2 LEU A 414     -29.362 -11.498  -8.127  1.00 27.21           C  
ATOM   3119  N   TYR A 415     -26.628  -9.664  -4.658  1.00 22.97           N  
ATOM   3120  CA  TYR A 415     -25.528  -9.263  -3.788  1.00 23.32           C  
ATOM   3121  C   TYR A 415     -24.310  -8.894  -4.639  1.00 24.23           C  
ATOM   3122  O   TYR A 415     -23.882  -9.697  -5.476  1.00 23.14           O  
ATOM   3123  CB  TYR A 415     -25.197 -10.465  -2.902  1.00 23.87           C  
ATOM   3124  CG  TYR A 415     -24.209 -10.282  -1.764  1.00 24.03           C  
ATOM   3125  CD1 TYR A 415     -23.819  -9.014  -1.306  1.00 23.33           C  
ATOM   3126  CD2 TYR A 415     -23.698 -11.404  -1.112  1.00 24.80           C  
ATOM   3127  CE1 TYR A 415     -22.930  -8.881  -0.249  1.00 23.63           C  
ATOM   3128  CE2 TYR A 415     -22.806 -11.286  -0.060  1.00 24.27           C  
ATOM   3129  CZ  TYR A 415     -22.424 -10.032   0.376  1.00 24.52           C  
ATOM   3130  OH  TYR A 415     -21.553  -9.945   1.445  1.00 22.93           O  
ATOM   3131  N   THR A 416     -23.722  -7.721  -4.408  1.00 24.66           N  
ATOM   3132  CA  THR A 416     -22.532  -7.315  -5.202  1.00 26.39           C  
ATOM   3133  C   THR A 416     -21.333  -8.271  -5.072  1.00 27.12           C  
ATOM   3134  O   THR A 416     -20.585  -8.460  -6.036  1.00 28.62           O  
ATOM   3135  CB  THR A 416     -22.046  -5.892  -4.872  1.00 26.42           C  
ATOM   3136  OG1 THR A 416     -21.685  -5.813  -3.483  1.00 28.20           O  
ATOM   3137  CG2 THR A 416     -23.126  -4.870  -5.181  1.00 27.14           C  
ATOM   3138  N   ALA A 417     -21.152  -8.858  -3.887  1.00 26.18           N  
ATOM   3139  CA  ALA A 417     -20.043  -9.779  -3.611  1.00 26.91           C  
ATOM   3140  C   ALA A 417     -20.092 -11.053  -4.460  1.00 27.85           C  
ATOM   3141  O   ALA A 417     -19.083 -11.759  -4.580  1.00 29.36           O  
ATOM   3142  CB  ALA A 417     -20.011 -10.150  -2.132  1.00 25.81           C  
ATOM   3143  N   LYS A 418     -21.267 -11.350  -5.014  1.00 27.54           N  
ATOM   3144  CA  LYS A 418     -21.458 -12.512  -5.867  1.00 29.38           C  
ATOM   3145  C   LYS A 418     -21.641 -12.143  -7.346  1.00 29.83           C  
ATOM   3146  O   LYS A 418     -21.353 -12.956  -8.213  1.00 31.68           O  
ATOM   3147  CB  LYS A 418     -22.634 -13.391  -5.381  1.00 28.89           C  
ATOM   3148  CG  LYS A 418     -22.681 -13.685  -3.875  1.00 29.56           C  
ATOM   3149  CD  LYS A 418     -21.420 -14.366  -3.343  1.00 29.53           C  
ATOM   3150  CE  LYS A 418     -21.598 -14.894  -1.922  1.00 28.02           C  
ATOM   3151  NZ  LYS A 418     -22.501 -16.086  -1.917  1.00 28.29           N  
ATOM   3152  N   ASP A 419     -22.091 -10.923  -7.629  1.00 27.98           N  
ATOM   3153  CA  ASP A 419     -22.472 -10.543  -8.998  1.00 29.06           C  
ATOM   3154  C   ASP A 419     -21.332 -10.177  -9.939  1.00 29.66           C  
ATOM   3155  O   ASP A 419     -20.448  -9.402  -9.586  1.00 29.29           O  
ATOM   3156  CB  ASP A 419     -23.453  -9.375  -8.991  1.00 28.26           C  
ATOM   3157  CG  ASP A 419     -23.831  -8.943 -10.402  1.00 28.51           C  
ATOM   3158  OD1 ASP A 419     -24.421  -9.776 -11.128  1.00 26.58           O  
ATOM   3159  OD2 ASP A 419     -23.510  -7.793 -10.788  1.00 28.09           O  
ATOM   3160  N   SER A 420     -21.406 -10.678 -11.167  1.00 30.93           N  
ATOM   3161  CA  SER A 420     -20.464 -10.274 -12.206  1.00 32.61           C  
ATOM   3162  C   SER A 420     -21.169  -9.865 -13.498  1.00 32.97           C  
ATOM   3163  O   SER A 420     -20.518  -9.416 -14.440  1.00 33.08           O  
ATOM   3164  CB  SER A 420     -19.456 -11.394 -12.487  1.00 35.78           C  
ATOM   3165  OG  SER A 420     -20.130 -12.607 -12.785  1.00 40.27           O  
ATOM   3166  N   ARG A 421     -22.496  -9.988 -13.552  1.00 31.56           N  
ATOM   3167  CA  ARG A 421     -23.172  -9.774 -14.832  1.00 30.76           C  
ATOM   3168  C   ARG A 421     -24.561  -9.114 -14.879  1.00 29.84           C  
ATOM   3169  O   ARG A 421     -25.102  -8.959 -15.969  1.00 29.51           O  
ATOM   3170  CB  ARG A 421     -23.127 -11.042 -15.712  1.00 32.46           C  
ATOM   3171  CG  ARG A 421     -23.460 -12.359 -15.037  1.00 34.30           C  
ATOM   3172  CD  ARG A 421     -24.942 -12.655 -15.165  1.00 37.17           C  
ATOM   3173  NE  ARG A 421     -25.687 -12.264 -13.973  1.00 38.03           N  
ATOM   3174  CZ  ARG A 421     -26.925 -11.764 -13.964  1.00 36.59           C  
ATOM   3175  NH1 ARG A 421     -27.592 -11.544 -15.097  1.00 35.70           N  
ATOM   3176  NH2 ARG A 421     -27.491 -11.465 -12.802  1.00 33.32           N  
ATOM   3177  N   THR A 422     -25.146  -8.721 -13.745  1.00 27.74           N  
ATOM   3178  CA  THR A 422     -26.409  -7.977 -13.834  1.00 26.95           C  
ATOM   3179  C   THR A 422     -26.168  -6.591 -14.467  1.00 26.98           C  
ATOM   3180  O   THR A 422     -25.031  -6.160 -14.643  1.00 27.35           O  
ATOM   3181  CB  THR A 422     -27.186  -7.873 -12.496  1.00 26.57           C  
ATOM   3182  OG1 THR A 422     -28.558  -7.549 -12.774  1.00 28.70           O  
ATOM   3183  CG2 THR A 422     -26.601  -6.818 -11.552  1.00 25.24           C  
ATOM   3184  N   THR A 423     -27.245  -5.926 -14.844  1.00 27.74           N  
ATOM   3185  CA  THR A 423     -27.152  -4.612 -15.465  1.00 27.54           C  
ATOM   3186  C   THR A 423     -27.333  -3.521 -14.430  1.00 26.39           C  
ATOM   3187  O   THR A 423     -27.939  -3.748 -13.373  1.00 25.69           O  
ATOM   3188  CB  THR A 423     -28.235  -4.424 -16.540  1.00 27.50           C  
ATOM   3189  OG1 THR A 423     -29.535  -4.548 -15.940  1.00 27.58           O  
ATOM   3190  CG2 THR A 423     -28.078  -5.460 -17.632  1.00 29.31           C  
ATOM   3191  N   ALA A 424     -26.826  -2.335 -14.758  1.00 25.33           N  
ATOM   3192  CA  ALA A 424     -27.044  -1.124 -13.981  1.00 25.96           C  
ATOM   3193  C   ALA A 424     -28.534  -0.849 -13.756  1.00 27.12           C  
ATOM   3194  O   ALA A 424     -28.943  -0.535 -12.643  1.00 26.88           O  
ATOM   3195  CB  ALA A 424     -26.367   0.062 -14.660  1.00 26.62           C  
ATOM   3196  N   GLU A 425     -29.344  -0.982 -14.805  1.00 28.10           N  
ATOM   3197  CA  GLU A 425     -30.786  -0.727 -14.702  1.00 28.57           C  
ATOM   3198  C   GLU A 425     -31.445  -1.633 -13.648  1.00 27.45           C  
ATOM   3199  O   GLU A 425     -32.189  -1.161 -12.782  1.00 28.02           O  
ATOM   3200  CB  GLU A 425     -31.460  -0.884 -16.077  1.00 30.01           C  
ATOM   3201  CG  GLU A 425     -32.956  -0.598 -16.084  1.00 32.04           C  
ATOM   3202  CD  GLU A 425     -33.606  -0.793 -17.448  1.00 33.38           C  
ATOM   3203  OE1 GLU A 425     -32.972  -1.338 -18.372  1.00 35.94           O  
ATOM   3204  OE2 GLU A 425     -34.775  -0.417 -17.599  1.00 36.18           O  
ATOM   3205  N   THR A 426     -31.150  -2.925 -13.711  1.00 25.35           N  
ATOM   3206  CA  THR A 426     -31.673  -3.892 -12.744  1.00 24.83           C  
ATOM   3207  C   THR A 426     -31.160  -3.609 -11.336  1.00 24.00           C  
ATOM   3208  O   THR A 426     -31.939  -3.598 -10.375  1.00 23.62           O  
ATOM   3209  CB  THR A 426     -31.293  -5.326 -13.144  1.00 24.33           C  
ATOM   3210  OG1 THR A 426     -31.918  -5.637 -14.386  1.00 25.63           O  
ATOM   3211  CG2 THR A 426     -31.764  -6.336 -12.106  1.00 24.75           C  
ATOM   3212  N   PHE A 427     -29.853  -3.393 -11.217  1.00 22.11           N  
ATOM   3213  CA  PHE A 427     -29.248  -3.116  -9.932  1.00 22.88           C  
ATOM   3214  C   PHE A 427     -29.845  -1.874  -9.284  1.00 23.04           C  
ATOM   3215  O   PHE A 427     -30.124  -1.884  -8.082  1.00 22.11           O  
ATOM   3216  CB  PHE A 427     -27.725  -2.949 -10.022  1.00 22.93           C  
ATOM   3217  CG  PHE A 427     -27.062  -2.779  -8.679  1.00 23.17           C  
ATOM   3218  CD1 PHE A 427     -26.623  -3.893  -7.961  1.00 22.95           C  
ATOM   3219  CD2 PHE A 427     -26.886  -1.515  -8.125  1.00 22.39           C  
ATOM   3220  CE1 PHE A 427     -26.022  -3.740  -6.720  1.00 23.37           C  
ATOM   3221  CE2 PHE A 427     -26.287  -1.357  -6.880  1.00 23.75           C  
ATOM   3222  CZ  PHE A 427     -25.853  -2.475  -6.172  1.00 23.00           C  
ATOM   3223  N   HIS A 428     -30.005  -0.801 -10.063  1.00 22.83           N  
ATOM   3224  CA  HIS A 428     -30.571   0.427  -9.504  1.00 22.41           C  
ATOM   3225  C   HIS A 428     -31.992   0.245  -9.048  1.00 22.88           C  
ATOM   3226  O   HIS A 428     -32.377   0.812  -8.036  1.00 23.50           O  
ATOM   3227  CB  HIS A 428     -30.455   1.600 -10.467  1.00 22.17           C  
ATOM   3228  CG  HIS A 428     -29.055   2.140 -10.592  1.00 22.59           C  
ATOM   3229  ND1 HIS A 428     -28.769   3.449 -10.471  1.00 22.81           N  
ATOM   3230  CD2 HIS A 428     -27.840   1.493 -10.844  1.00 22.26           C  
ATOM   3231  CE1 HIS A 428     -27.444   3.638 -10.644  1.00 22.96           C  
ATOM   3232  NE2 HIS A 428     -26.879   2.441 -10.875  1.00 22.64           N  
ATOM   3233  N   ALA A 429     -32.778  -0.548  -9.770  1.00 22.26           N  
ATOM   3234  CA  ALA A 429     -34.176  -0.809  -9.363  1.00 22.68           C  
ATOM   3235  C   ALA A 429     -34.269  -1.677  -8.106  1.00 23.25           C  
ATOM   3236  O   ALA A 429     -35.195  -1.528  -7.287  1.00 24.04           O  
ATOM   3237  CB  ALA A 429     -34.950  -1.433 -10.509  1.00 22.41           C  
ATOM   3238  N   MET A 430     -33.304  -2.583  -7.954  1.00 22.41           N  
ATOM   3239  CA  MET A 430     -33.211  -3.460  -6.790  1.00 23.49           C  
ATOM   3240  C   MET A 430     -32.779  -2.714  -5.523  1.00 23.94           C  
ATOM   3241  O   MET A 430     -33.046  -3.172  -4.422  1.00 26.14           O  
ATOM   3242  CB  MET A 430     -32.218  -4.604  -7.066  1.00 22.93           C  
ATOM   3243  CG  MET A 430     -32.709  -5.689  -8.020  1.00 21.95           C  
ATOM   3244  SD  MET A 430     -31.318  -6.795  -8.330  1.00 23.53           S  
ATOM   3245  CE  MET A 430     -32.119  -8.108  -9.256  1.00 24.16           C  
ATOM   3246  N   TYR A 431     -32.089  -1.589  -5.692  1.00 23.65           N  
ATOM   3247  CA  TYR A 431     -31.603  -0.777  -4.584  1.00 23.07           C  
ATOM   3248  C   TYR A 431     -32.200   0.644  -4.658  1.00 24.34           C  
ATOM   3249  O   TYR A 431     -31.530   1.559  -5.141  1.00 23.37           O  
ATOM   3250  CB  TYR A 431     -30.053  -0.731  -4.616  1.00 22.73           C  
ATOM   3251  CG  TYR A 431     -29.392  -2.016  -4.142  1.00 21.95           C  
ATOM   3252  CD1 TYR A 431     -28.847  -2.112  -2.867  1.00 21.94           C  
ATOM   3253  CD2 TYR A 431     -29.343  -3.143  -4.958  1.00 21.70           C  
ATOM   3254  CE1 TYR A 431     -28.258  -3.294  -2.425  1.00 21.52           C  
ATOM   3255  CE2 TYR A 431     -28.762  -4.326  -4.529  1.00 20.88           C  
ATOM   3256  CZ  TYR A 431     -28.222  -4.392  -3.262  1.00 20.40           C  
ATOM   3257  OH  TYR A 431     -27.648  -5.555  -2.825  1.00 20.62           O  
ATOM   3258  N   PRO A 432     -33.456   0.845  -4.163  1.00 24.88           N  
ATOM   3259  CA  PRO A 432     -34.095   2.176  -4.332  1.00 25.08           C  
ATOM   3260  C   PRO A 432     -33.397   3.325  -3.604  1.00 25.77           C  
ATOM   3261  O   PRO A 432     -33.699   4.489  -3.872  1.00 26.64           O  
ATOM   3262  CB  PRO A 432     -35.524   1.998  -3.784  1.00 25.79           C  
ATOM   3263  CG  PRO A 432     -35.608   0.611  -3.226  1.00 25.61           C  
ATOM   3264  CD  PRO A 432     -34.315  -0.130  -3.470  1.00 24.49           C  
ATOM   3265  N   ARG A 433     -32.479   3.009  -2.696  1.00 25.33           N  
ATOM   3266  CA  ARG A 433     -31.668   4.039  -2.045  1.00 25.82           C  
ATOM   3267  C   ARG A 433     -30.340   4.286  -2.779  1.00 25.08           C  
ATOM   3268  O   ARG A 433     -29.454   4.937  -2.250  1.00 24.67           O  
ATOM   3269  CB  ARG A 433     -31.415   3.684  -0.583  1.00 24.59           C  
ATOM   3270  CG  ARG A 433     -32.685   3.611   0.273  1.00 24.69           C  
ATOM   3271  CD  ARG A 433     -32.339   3.111   1.652  1.00 25.70           C  
ATOM   3272  NE  ARG A 433     -31.597   4.103   2.428  1.00 25.87           N  
ATOM   3273  CZ  ARG A 433     -31.188   3.928   3.685  1.00 26.57           C  
ATOM   3274  NH1 ARG A 433     -31.446   2.791   4.329  1.00 27.13           N  
ATOM   3275  NH2 ARG A 433     -30.522   4.896   4.307  1.00 25.56           N  
ATOM   3276  N   VAL A 434     -30.206   3.779  -3.999  1.00 26.50           N  
ATOM   3277  CA  VAL A 434     -28.941   3.949  -4.752  1.00 25.78           C  
ATOM   3278  C   VAL A 434     -28.628   5.434  -5.039  1.00 27.24           C  
ATOM   3279  O   VAL A 434     -27.472   5.863  -4.923  1.00 28.77           O  
ATOM   3280  CB  VAL A 434     -28.905   3.102  -6.051  1.00 25.54           C  
ATOM   3281  CG1 VAL A 434     -29.880   3.630  -7.111  1.00 23.54           C  
ATOM   3282  CG2 VAL A 434     -27.473   2.991  -6.595  1.00 24.25           C  
ATOM   3283  N   ASP A 435     -29.643   6.217  -5.405  1.00 26.94           N  
ATOM   3284  CA  ASP A 435     -29.417   7.651  -5.700  1.00 28.70           C  
ATOM   3285  C   ASP A 435     -28.930   8.396  -4.459  1.00 27.32           C  
ATOM   3286  O   ASP A 435     -28.008   9.203  -4.540  1.00 27.85           O  
ATOM   3287  CB  ASP A 435     -30.671   8.316  -6.271  1.00 30.02           C  
ATOM   3288  CG  ASP A 435     -31.014   7.825  -7.665  1.00 31.24           C  
ATOM   3289  OD1 ASP A 435     -30.136   7.292  -8.369  1.00 32.93           O  
ATOM   3290  OD2 ASP A 435     -32.177   7.990  -8.074  1.00 33.30           O  
ATOM   3291  N   GLU A 436     -29.550   8.101  -3.314  1.00 26.93           N  
ATOM   3292  CA  GLU A 436     -29.091   8.587  -2.015  1.00 26.51           C  
ATOM   3293  C   GLU A 436     -27.615   8.245  -1.754  1.00 26.41           C  
ATOM   3294  O   GLU A 436     -26.831   9.094  -1.328  1.00 26.58           O  
ATOM   3295  CB  GLU A 436     -29.975   8.015  -0.902  1.00 25.68           C  
ATOM   3296  CG  GLU A 436     -29.359   8.083   0.488  1.00 25.37           C  
ATOM   3297  CD  GLU A 436     -30.090   7.220   1.502  1.00 25.78           C  
ATOM   3298  OE1 GLU A 436     -31.108   6.587   1.135  1.00 24.67           O  
ATOM   3299  OE2 GLU A 436     -29.640   7.170   2.668  1.00 25.79           O  
ATOM   3300  N   TRP A 437     -27.242   6.998  -2.016  1.00 26.76           N  
ATOM   3301  CA  TRP A 437     -25.851   6.566  -1.886  1.00 25.74           C  
ATOM   3302  C   TRP A 437     -24.934   7.266  -2.873  1.00 26.16           C  
ATOM   3303  O   TRP A 437     -23.853   7.724  -2.502  1.00 25.94           O  
ATOM   3304  CB  TRP A 437     -25.769   5.049  -2.043  1.00 25.18           C  
ATOM   3305  CG  TRP A 437     -24.381   4.516  -1.851  1.00 25.23           C  
ATOM   3306  CD1 TRP A 437     -23.790   4.078  -0.669  1.00 24.21           C  
ATOM   3307  CD2 TRP A 437     -23.354   4.350  -2.881  1.00 24.22           C  
ATOM   3308  NE1 TRP A 437     -22.494   3.669  -0.898  1.00 25.87           N  
ATOM   3309  CE2 TRP A 437     -22.174   3.804  -2.201  1.00 24.88           C  
ATOM   3310  CE3 TRP A 437     -23.295   4.591  -4.248  1.00 25.09           C  
ATOM   3311  CZ2 TRP A 437     -20.998   3.522  -2.883  1.00 24.44           C  
ATOM   3312  CZ3 TRP A 437     -22.105   4.302  -4.923  1.00 24.62           C  
ATOM   3313  CH2 TRP A 437     -20.990   3.779  -4.254  1.00 24.68           C  
ATOM   3314  N   ILE A 438     -25.346   7.341  -4.137  1.00 26.91           N  
ATOM   3315  CA  ILE A 438     -24.564   8.028  -5.180  1.00 27.28           C  
ATOM   3316  C   ILE A 438     -24.240   9.488  -4.808  1.00 28.54           C  
ATOM   3317  O   ILE A 438     -23.109   9.943  -5.011  1.00 27.98           O  
ATOM   3318  CB  ILE A 438     -25.253   7.930  -6.564  1.00 28.10           C  
ATOM   3319  CG1 ILE A 438     -25.089   6.518  -7.142  1.00 27.27           C  
ATOM   3320  CG2 ILE A 438     -24.699   8.959  -7.555  1.00 29.05           C  
ATOM   3321  CD1 ILE A 438     -25.991   6.237  -8.336  1.00 25.38           C  
ATOM   3322  N   SER A 439     -25.217  10.208  -4.250  1.00 28.11           N  
ATOM   3323  CA  SER A 439     -24.996  11.595  -3.817  1.00 29.28           C  
ATOM   3324  C   SER A 439     -23.938  11.725  -2.735  1.00 29.85           C  
ATOM   3325  O   SER A 439     -23.173  12.694  -2.740  1.00 29.74           O  
ATOM   3326  CB  SER A 439     -26.286  12.237  -3.315  1.00 28.83           C  
ATOM   3327  OG  SER A 439     -27.259  12.239  -4.332  1.00 29.86           O  
ATOM   3328  N   VAL A 440     -23.911  10.782  -1.789  1.00 29.66           N  
ATOM   3329  CA  VAL A 440     -22.844  10.750  -0.790  1.00 30.15           C  
ATOM   3330  C   VAL A 440     -21.487  10.537  -1.478  1.00 31.13           C  
ATOM   3331  O   VAL A 440     -20.519  11.237  -1.180  1.00 29.78           O  
ATOM   3332  CB  VAL A 440     -23.068   9.669   0.292  1.00 30.00           C  
ATOM   3333  CG1 VAL A 440     -21.908   9.666   1.275  1.00 29.04           C  
ATOM   3334  CG2 VAL A 440     -24.382   9.903   1.030  1.00 29.30           C  
ATOM   3335  N   ARG A 441     -21.435   9.588  -2.411  1.00 32.56           N  
ATOM   3336  CA  ARG A 441     -20.194   9.262  -3.121  1.00 34.42           C  
ATOM   3337  C   ARG A 441     -19.631  10.430  -3.937  1.00 35.98           C  
ATOM   3338  O   ARG A 441     -18.415  10.620  -3.983  1.00 38.85           O  
ATOM   3339  CB  ARG A 441     -20.369   8.031  -4.011  1.00 34.98           C  
ATOM   3340  CG  ARG A 441     -19.368   7.971  -5.153  1.00 34.87           C  
ATOM   3341  CD  ARG A 441     -19.060   6.572  -5.628  1.00 34.30           C  
ATOM   3342  NE  ARG A 441     -18.354   6.636  -6.900  1.00 38.34           N  
ATOM   3343  CZ  ARG A 441     -17.040   6.837  -7.043  1.00 39.00           C  
ATOM   3344  NH1 ARG A 441     -16.241   6.984  -5.986  1.00 35.06           N  
ATOM   3345  NH2 ARG A 441     -16.528   6.888  -8.265  1.00 38.37           N  
ATOM   3346  N   ARG A 442     -20.507  11.200  -4.579  1.00 37.78           N  
ATOM   3347  CA  ARG A 442     -20.067  12.333  -5.402  1.00 40.26           C  
ATOM   3348  C   ARG A 442     -19.638  13.505  -4.541  1.00 40.37           C  
ATOM   3349  O   ARG A 442     -18.824  14.321  -4.957  1.00 42.10           O  
ATOM   3350  CB  ARG A 442     -21.153  12.771  -6.375  1.00 40.84           C  
ATOM   3351  CG  ARG A 442     -21.256  11.889  -7.602  1.00 42.41           C  
ATOM   3352  CD  ARG A 442     -22.503  12.240  -8.376  1.00 43.69           C  
ATOM   3353  NE  ARG A 442     -22.807  11.248  -9.398  1.00 45.93           N  
ATOM   3354  CZ  ARG A 442     -23.914  11.256 -10.133  1.00 47.20           C  
ATOM   3355  NH1 ARG A 442     -24.828  12.206  -9.953  1.00 48.40           N  
ATOM   3356  NH2 ARG A 442     -24.113  10.312 -11.046  1.00 48.58           N  
ATOM   3357  N   LYS A 443     -20.207  13.580  -3.343  1.00 41.38           N  
ATOM   3358  CA  LYS A 443     -19.822  14.574  -2.349  1.00 41.19           C  
ATOM   3359  C   LYS A 443     -18.428  14.269  -1.787  1.00 40.08           C  
ATOM   3360  O   LYS A 443     -17.664  15.184  -1.495  1.00 38.88           O  
ATOM   3361  CB  LYS A 443     -20.872  14.618  -1.236  1.00 40.72           C  
ATOM   3362  CG  LYS A 443     -20.757  15.775  -0.263  1.00 43.64           C  
ATOM   3363  CD  LYS A 443     -22.087  16.022   0.443  1.00 44.90           C  
ATOM   3364  CE  LYS A 443     -22.407  14.919   1.439  1.00 44.45           C  
ATOM   3365  NZ  LYS A 443     -23.814  14.991   1.916  1.00 47.82           N  
ATOM   3366  N   VAL A 444     -18.090  12.985  -1.668  1.00 38.78           N  
ATOM   3367  CA  VAL A 444     -16.825  12.576  -1.048  1.00 37.17           C  
ATOM   3368  C   VAL A 444     -15.744  12.244  -2.083  1.00 36.58           C  
ATOM   3369  O   VAL A 444     -14.557  12.182  -1.752  1.00 38.28           O  
ATOM   3370  CB  VAL A 444     -17.036  11.414  -0.031  1.00 38.05           C  
ATOM   3371  CG1 VAL A 444     -17.008  10.053  -0.720  1.00 35.83           C  
ATOM   3372  CG2 VAL A 444     -15.993  11.462   1.075  1.00 38.56           C  
ATOM   3373  N   ASP A 445     -16.151  12.038  -3.334  1.00 35.41           N  
ATOM   3374  CA  ASP A 445     -15.202  11.750  -4.411  1.00 34.38           C  
ATOM   3375  C   ASP A 445     -15.667  12.376  -5.737  1.00 33.11           C  
ATOM   3376  O   ASP A 445     -15.979  11.654  -6.697  1.00 30.40           O  
ATOM   3377  CB  ASP A 445     -14.981  10.234  -4.537  1.00 35.09           C  
ATOM   3378  CG  ASP A 445     -13.940   9.873  -5.579  1.00 37.47           C  
ATOM   3379  OD1 ASP A 445     -13.195  10.779  -6.027  1.00 35.83           O  
ATOM   3380  OD2 ASP A 445     -13.869   8.678  -5.965  1.00 37.25           O  
ATOM   3381  N   PRO A 446     -15.721  13.727  -5.791  1.00 34.06           N  
ATOM   3382  CA  PRO A 446     -16.220  14.434  -6.983  1.00 35.44           C  
ATOM   3383  C   PRO A 446     -15.458  14.093  -8.263  1.00 35.17           C  
ATOM   3384  O   PRO A 446     -16.052  14.081  -9.346  1.00 35.86           O  
ATOM   3385  CB  PRO A 446     -16.061  15.924  -6.624  1.00 35.79           C  
ATOM   3386  CG  PRO A 446     -15.203  15.971  -5.402  1.00 34.28           C  
ATOM   3387  CD  PRO A 446     -15.363  14.661  -4.703  1.00 34.67           C  
ATOM   3388  N   LEU A 447     -14.174  13.781  -8.126  1.00 35.34           N  
ATOM   3389  CA  LEU A 447     -13.314  13.454  -9.268  1.00 36.91           C  
ATOM   3390  C   LEU A 447     -13.260  11.975  -9.649  1.00 36.96           C  
ATOM   3391  O   LEU A 447     -12.540  11.608 -10.574  1.00 35.65           O  
ATOM   3392  CB  LEU A 447     -11.884  13.929  -9.003  1.00 38.64           C  
ATOM   3393  CG  LEU A 447     -11.569  15.409  -9.161  1.00 42.94           C  
ATOM   3394  CD1 LEU A 447     -10.190  15.677  -8.566  1.00 43.37           C  
ATOM   3395  CD2 LEU A 447     -11.635  15.812 -10.631  1.00 41.53           C  
ATOM   3396  N   ARG A 448     -14.007  11.119  -8.948  1.00 37.34           N  
ATOM   3397  CA  ARG A 448     -13.972   9.679  -9.246  1.00 36.60           C  
ATOM   3398  C   ARG A 448     -12.541   9.120  -9.118  1.00 34.67           C  
ATOM   3399  O   ARG A 448     -12.061   8.360  -9.960  1.00 33.63           O  
ATOM   3400  CB  ARG A 448     -14.568   9.373 -10.635  1.00 36.67           C  
ATOM   3401  CG  ARG A 448     -16.048   9.708 -10.804  1.00 39.93           C  
ATOM   3402  CD  ARG A 448     -16.307  11.145 -11.257  1.00 42.56           C  
ATOM   3403  NE  ARG A 448     -15.678  11.451 -12.546  1.00 44.87           N  
ATOM   3404  CZ  ARG A 448     -15.577  12.672 -13.076  1.00 46.15           C  
ATOM   3405  NH1 ARG A 448     -16.063  13.729 -12.439  1.00 45.04           N  
ATOM   3406  NH2 ARG A 448     -14.975  12.840 -14.248  1.00 47.34           N  
ATOM   3407  N   VAL A 449     -11.868   9.519  -8.045  1.00 33.85           N  
ATOM   3408  CA  VAL A 449     -10.580   8.960  -7.672  1.00 34.08           C  
ATOM   3409  C   VAL A 449     -10.726   7.453  -7.416  1.00 34.40           C  
ATOM   3410  O   VAL A 449      -9.832   6.658  -7.747  1.00 31.66           O  
ATOM   3411  CB  VAL A 449     -10.011   9.705  -6.445  1.00 34.15           C  
ATOM   3412  CG1 VAL A 449      -8.728   9.058  -5.935  1.00 34.81           C  
ATOM   3413  CG2 VAL A 449      -9.771  11.176  -6.789  1.00 34.86           C  
ATOM   3414  N   PHE A 450     -11.868   7.059  -6.852  1.00 32.75           N  
ATOM   3415  CA  PHE A 450     -12.140   5.641  -6.621  1.00 32.41           C  
ATOM   3416  C   PHE A 450     -13.117   5.093  -7.638  1.00 32.54           C  
ATOM   3417  O   PHE A 450     -14.206   5.633  -7.840  1.00 32.49           O  
ATOM   3418  CB  PHE A 450     -12.577   5.383  -5.175  1.00 31.82           C  
ATOM   3419  CG  PHE A 450     -11.549   5.814  -4.168  1.00 30.88           C  
ATOM   3420  CD1 PHE A 450     -10.438   5.030  -3.918  1.00 31.18           C  
ATOM   3421  CD2 PHE A 450     -11.669   7.030  -3.518  1.00 30.24           C  
ATOM   3422  CE1 PHE A 450      -9.476   5.435  -3.012  1.00 31.01           C  
ATOM   3423  CE2 PHE A 450     -10.709   7.447  -2.613  1.00 31.10           C  
ATOM   3424  CZ  PHE A 450      -9.615   6.648  -2.355  1.00 31.08           C  
ATOM   3425  N   ALA A 451     -12.688   4.027  -8.302  1.00 32.35           N  
ATOM   3426  CA  ALA A 451     -13.415   3.473  -9.419  1.00 31.88           C  
ATOM   3427  C   ALA A 451     -13.024   2.026  -9.578  1.00 31.42           C  
ATOM   3428  O   ALA A 451     -11.907   1.636  -9.239  1.00 33.26           O  
ATOM   3429  CB  ALA A 451     -13.096   4.250 -10.689  1.00 33.28           C  
ATOM   3430  N   SER A 452     -13.947   1.231 -10.105  1.00 30.13           N  
ATOM   3431  CA  SER A 452     -13.711  -0.185 -10.332  1.00 29.12           C  
ATOM   3432  C   SER A 452     -14.495  -0.648 -11.552  1.00 29.19           C  
ATOM   3433  O   SER A 452     -15.356   0.074 -12.059  1.00 32.08           O  
ATOM   3434  CB  SER A 452     -14.172  -0.976  -9.110  1.00 28.52           C  
ATOM   3435  OG  SER A 452     -15.577  -0.854  -8.972  1.00 27.91           O  
ATOM   3436  N   ASP A 453     -14.216  -1.858 -12.016  1.00 27.75           N  
ATOM   3437  CA  ASP A 453     -15.018  -2.449 -13.080  1.00 28.08           C  
ATOM   3438  C   ASP A 453     -16.510  -2.543 -12.705  1.00 27.37           C  
ATOM   3439  O   ASP A 453     -17.382  -2.270 -13.534  1.00 24.02           O  
ATOM   3440  CB  ASP A 453     -14.454  -3.813 -13.467  1.00 28.98           C  
ATOM   3441  CG  ASP A 453     -13.098  -3.699 -14.139  1.00 30.20           C  
ATOM   3442  OD1 ASP A 453     -12.595  -2.564 -14.289  1.00 32.12           O  
ATOM   3443  OD2 ASP A 453     -12.540  -4.732 -14.530  1.00 32.66           O  
ATOM   3444  N   MET A 454     -16.795  -2.907 -11.458  1.00 26.12           N  
ATOM   3445  CA  MET A 454     -18.191  -2.941 -11.011  1.00 27.66           C  
ATOM   3446  C   MET A 454     -18.833  -1.560 -11.044  1.00 26.94           C  
ATOM   3447  O   MET A 454     -19.967  -1.412 -11.519  1.00 29.35           O  
ATOM   3448  CB  MET A 454     -18.341  -3.557  -9.616  1.00 27.85           C  
ATOM   3449  CG  MET A 454     -19.804  -3.596  -9.171  1.00 29.74           C  
ATOM   3450  SD  MET A 454     -20.035  -4.464  -7.621  1.00 31.34           S  
ATOM   3451  CE  MET A 454     -19.732  -6.163  -8.148  1.00 32.58           C  
ATOM   3452  N   ALA A 455     -18.121  -0.555 -10.534  1.00 26.60           N  
ATOM   3453  CA  ALA A 455     -18.625   0.821 -10.551  1.00 26.76           C  
ATOM   3454  C   ALA A 455     -19.054   1.245 -11.952  1.00 26.96           C  
ATOM   3455  O   ALA A 455     -20.114   1.852 -12.123  1.00 25.63           O  
ATOM   3456  CB  ALA A 455     -17.601   1.795  -9.987  1.00 26.17           C  
ATOM   3457  N   ARG A 456     -18.241   0.906 -12.950  1.00 26.22           N  
ATOM   3458  CA  ARG A 456     -18.542   1.258 -14.345  1.00 29.31           C  
ATOM   3459  C   ARG A 456     -19.714   0.455 -14.926  1.00 28.91           C  
ATOM   3460  O   ARG A 456     -20.598   1.016 -15.560  1.00 30.28           O  
ATOM   3461  CB  ARG A 456     -17.272   1.176 -15.231  1.00 30.44           C  
ATOM   3462  CG  ARG A 456     -16.248   2.273 -14.917  1.00 31.23           C  
ATOM   3463  CD  ARG A 456     -14.995   2.228 -15.793  1.00 32.41           C  
ATOM   3464  NE  ARG A 456     -14.113   1.129 -15.405  1.00 34.93           N  
ATOM   3465  CZ  ARG A 456     -13.090   1.240 -14.559  1.00 34.37           C  
ATOM   3466  NH1 ARG A 456     -12.770   2.410 -14.017  1.00 34.27           N  
ATOM   3467  NH2 ARG A 456     -12.367   0.174 -14.273  1.00 36.28           N  
ATOM   3468  N   ARG A 457     -19.738  -0.851 -14.678  1.00 28.49           N  
ATOM   3469  CA  ARG A 457     -20.819  -1.719 -15.153  1.00 27.61           C  
ATOM   3470  C   ARG A 457     -22.195  -1.380 -14.523  1.00 26.50           C  
ATOM   3471  O   ARG A 457     -23.222  -1.353 -15.221  1.00 25.26           O  
ATOM   3472  CB  ARG A 457     -20.439  -3.183 -14.883  1.00 27.83           C  
ATOM   3473  CG  ARG A 457     -21.452  -4.223 -15.326  1.00 28.73           C  
ATOM   3474  CD  ARG A 457     -20.879  -5.631 -15.176  1.00 30.02           C  
ATOM   3475  NE  ARG A 457     -20.455  -5.902 -13.800  1.00 30.95           N  
ATOM   3476  CZ  ARG A 457     -21.259  -6.371 -12.850  1.00 30.88           C  
ATOM   3477  NH1 ARG A 457     -22.534  -6.630 -13.124  1.00 30.33           N  
ATOM   3478  NH2 ARG A 457     -20.789  -6.581 -11.623  1.00 31.87           N  
ATOM   3479  N   LEU A 458     -22.208  -1.123 -13.216  1.00 25.54           N  
ATOM   3480  CA  LEU A 458     -23.464  -0.841 -12.466  1.00 24.51           C  
ATOM   3481  C   LEU A 458     -23.778   0.665 -12.348  1.00 26.07           C  
ATOM   3482  O   LEU A 458     -24.729   1.087 -11.647  1.00 25.11           O  
ATOM   3483  CB  LEU A 458     -23.413  -1.518 -11.088  1.00 24.01           C  
ATOM   3484  CG  LEU A 458     -23.274  -3.053 -11.072  1.00 23.85           C  
ATOM   3485  CD1 LEU A 458     -23.223  -3.595  -9.645  1.00 23.84           C  
ATOM   3486  CD2 LEU A 458     -24.378  -3.748 -11.853  1.00 23.74           C  
ATOM   3487  N   GLU A 459     -22.989   1.469 -13.059  1.00 27.02           N  
ATOM   3488  CA  GLU A 459     -23.125   2.928 -13.080  1.00 27.67           C  
ATOM   3489  C   GLU A 459     -23.251   3.498 -11.674  1.00 28.08           C  
ATOM   3490  O   GLU A 459     -24.188   4.219 -11.349  1.00 28.22           O  
ATOM   3491  CB  GLU A 459     -24.253   3.378 -14.026  1.00 28.36           C  
ATOM   3492  CG  GLU A 459     -24.034   2.879 -15.449  1.00 29.01           C  
ATOM   3493  CD  GLU A 459     -25.203   3.107 -16.391  1.00 30.60           C  
ATOM   3494  OE1 GLU A 459     -25.964   4.084 -16.219  1.00 30.81           O  
ATOM   3495  OE2 GLU A 459     -25.350   2.297 -17.329  1.00 31.72           O  
ATOM   3496  N   LEU A 460     -22.292   3.115 -10.839  1.00 29.77           N  
ATOM   3497  CA  LEU A 460     -22.141   3.646  -9.496  1.00 31.47           C  
ATOM   3498  C   LEU A 460     -21.025   4.677  -9.484  1.00 36.26           C  
ATOM   3499  O   LEU A 460     -20.854   5.400  -8.505  1.00 36.74           O  
ATOM   3500  CB  LEU A 460     -21.797   2.522  -8.529  1.00 29.06           C  
ATOM   3501  CG  LEU A 460     -22.841   1.417  -8.402  1.00 28.74           C  
ATOM   3502  CD1 LEU A 460     -22.317   0.396  -7.421  1.00 29.39           C  
ATOM   3503  CD2 LEU A 460     -24.182   1.985  -7.947  1.00 27.99           C  
ATOM   3504  N   LEU A 461     -20.263   4.716 -10.579  1.00 40.23           N  
ATOM   3505  CA  LEU A 461     -19.096   5.592 -10.708  1.00 44.59           C  
ATOM   3506  C   LEU A 461     -19.469   7.056 -10.513  1.00 45.60           C  
ATOM   3507  O   LEU A 461     -18.754   7.777  -9.824  1.00 47.32           O  
ATOM   3508  CB  LEU A 461     -18.430   5.386 -12.071  1.00 44.71           C  
ATOM   3509  CG  LEU A 461     -17.081   6.052 -12.360  1.00 48.06           C  
ATOM   3510  CD1 LEU A 461     -15.978   5.368 -11.572  1.00 48.26           C  
ATOM   3511  CD2 LEU A 461     -16.767   6.032 -13.854  1.00 46.83           C  
ATOM   3512  OXT LEU A 461     -20.489   7.545 -11.016  1.00 48.46           O  
TER    3513      LEU A 461                                                      
ATOM   3514  N   THR B   7     -16.855 -22.011  52.342  1.00 80.16           N  
ATOM   3515  CA  THR B   7     -16.160 -21.378  51.178  1.00 80.93           C  
ATOM   3516  C   THR B   7     -14.754 -21.960  50.921  1.00 81.42           C  
ATOM   3517  O   THR B   7     -14.329 -22.071  49.769  1.00 83.59           O  
ATOM   3518  CB  THR B   7     -16.136 -19.827  51.287  1.00 81.92           C  
ATOM   3519  OG1 THR B   7     -15.495 -19.263  50.134  1.00 81.92           O  
ATOM   3520  CG2 THR B   7     -15.422 -19.348  52.561  1.00 80.76           C  
ATOM   3521  N   THR B   8     -14.049 -22.338  51.988  1.00 79.67           N  
ATOM   3522  CA  THR B   8     -12.685 -22.877  51.873  1.00 77.13           C  
ATOM   3523  C   THR B   8     -12.632 -24.396  52.069  1.00 74.72           C  
ATOM   3524  O   THR B   8     -13.519 -24.981  52.690  1.00 75.92           O  
ATOM   3525  CB  THR B   8     -11.703 -22.198  52.860  1.00 78.59           C  
ATOM   3526  OG1 THR B   8     -12.033 -22.559  54.208  1.00 81.27           O  
ATOM   3527  CG2 THR B   8     -11.737 -20.676  52.714  1.00 76.85           C  
ATOM   3528  N   THR B   9     -11.588 -25.023  51.529  1.00 72.26           N  
ATOM   3529  CA  THR B   9     -11.369 -26.463  51.663  1.00 69.73           C  
ATOM   3530  C   THR B   9     -10.049 -26.725  52.385  1.00 70.45           C  
ATOM   3531  O   THR B   9      -9.003 -26.199  51.991  1.00 70.88           O  
ATOM   3532  CB  THR B   9     -11.362 -27.162  50.282  1.00 68.76           C  
ATOM   3533  OG1 THR B   9     -12.653 -27.038  49.675  1.00 69.06           O  
ATOM   3534  CG2 THR B   9     -11.014 -28.645  50.403  1.00 66.59           C  
ATOM   3535  N   ALA B  10     -10.103 -27.524  53.450  1.00 68.26           N  
ATOM   3536  CA  ALA B  10      -8.895 -27.961  54.144  1.00 65.70           C  
ATOM   3537  C   ALA B  10      -8.130 -28.916  53.229  1.00 64.02           C  
ATOM   3538  O   ALA B  10      -8.653 -29.961  52.844  1.00 63.76           O  
ATOM   3539  CB  ALA B  10      -9.244 -28.627  55.469  1.00 64.50           C  
ATOM   3540  N   THR B  11      -6.905 -28.542  52.859  1.00 62.40           N  
ATOM   3541  CA  THR B  11      -6.128 -29.318  51.886  1.00 60.98           C  
ATOM   3542  C   THR B  11      -4.685 -29.551  52.327  1.00 61.03           C  
ATOM   3543  O   THR B  11      -4.036 -28.652  52.876  1.00 59.40           O  
ATOM   3544  CB  THR B  11      -6.120 -28.654  50.488  1.00 59.30           C  
ATOM   3545  OG1 THR B  11      -7.390 -28.046  50.223  1.00 57.90           O  
ATOM   3546  CG2 THR B  11      -5.818 -29.678  49.399  1.00 58.79           C  
ATOM   3547  N   ARG B  12      -4.205 -30.770  52.073  1.00 61.78           N  
ATOM   3548  CA  ARG B  12      -2.812 -31.155  52.284  1.00 63.15           C  
ATOM   3549  C   ARG B  12      -1.969 -30.667  51.105  1.00 62.99           C  
ATOM   3550  O   ARG B  12      -2.123 -31.141  49.975  1.00 62.35           O  
ATOM   3551  CB  ARG B  12      -2.704 -32.676  52.428  1.00 64.67           C  
ATOM   3552  CG  ARG B  12      -1.340 -33.184  52.866  1.00 69.73           C  
ATOM   3553  CD  ARG B  12      -1.234 -34.688  52.653  1.00 72.87           C  
ATOM   3554  NE  ARG B  12       0.149 -35.167  52.679  1.00 74.54           N  
ATOM   3555  CZ  ARG B  12       1.013 -35.045  51.672  1.00 76.35           C  
ATOM   3556  NH1 ARG B  12       0.651 -34.441  50.545  1.00 78.56           N  
ATOM   3557  NH2 ARG B  12       2.249 -35.514  51.794  1.00 74.99           N  
ATOM   3558  N   LEU B  13      -1.080 -29.718  51.373  1.00 61.50           N  
ATOM   3559  CA  LEU B  13      -0.289 -29.095  50.315  1.00 60.36           C  
ATOM   3560  C   LEU B  13       1.197 -29.394  50.444  1.00 60.39           C  
ATOM   3561  O   LEU B  13       1.720 -29.503  51.557  1.00 59.26           O  
ATOM   3562  CB  LEU B  13      -0.502 -27.578  50.314  1.00 58.21           C  
ATOM   3563  CG  LEU B  13      -1.912 -27.052  50.046  1.00 58.78           C  
ATOM   3564  CD1 LEU B  13      -2.005 -25.582  50.430  1.00 57.52           C  
ATOM   3565  CD2 LEU B  13      -2.309 -27.268  48.592  1.00 59.08           C  
ATOM   3566  N   THR B  14       1.865 -29.529  49.299  1.00 58.40           N  
ATOM   3567  CA  THR B  14       3.333 -29.553  49.241  1.00 59.19           C  
ATOM   3568  C   THR B  14       3.835 -28.663  48.096  1.00 58.87           C  
ATOM   3569  O   THR B  14       3.049 -28.206  47.263  1.00 57.06           O  
ATOM   3570  CB  THR B  14       3.907 -30.980  49.051  1.00 58.64           C  
ATOM   3571  OG1 THR B  14       3.684 -31.423  47.705  1.00 57.23           O  
ATOM   3572  CG2 THR B  14       3.294 -31.976  50.036  1.00 57.51           C  
ATOM   3573  N   GLY B  15       5.143 -28.421  48.057  1.00 58.66           N  
ATOM   3574  CA  GLY B  15       5.771 -27.830  46.879  1.00 55.88           C  
ATOM   3575  C   GLY B  15       5.887 -28.875  45.781  1.00 57.99           C  
ATOM   3576  O   GLY B  15       5.412 -30.007  45.935  1.00 56.54           O  
ATOM   3577  N   TRP B  16       6.520 -28.497  44.671  1.00 57.00           N  
ATOM   3578  CA  TRP B  16       6.748 -29.410  43.548  1.00 55.01           C  
ATOM   3579  C   TRP B  16       7.646 -30.547  43.948  1.00 56.05           C  
ATOM   3580  O   TRP B  16       7.541 -31.651  43.408  1.00 57.31           O  
ATOM   3581  CB  TRP B  16       7.341 -28.662  42.354  1.00 52.37           C  
ATOM   3582  CG  TRP B  16       7.218 -29.411  41.045  1.00 49.88           C  
ATOM   3583  CD1 TRP B  16       8.230 -30.045  40.327  1.00 47.78           C  
ATOM   3584  CD2 TRP B  16       5.996 -29.631  40.252  1.00 48.16           C  
ATOM   3585  NE1 TRP B  16       7.734 -30.620  39.182  1.00 45.78           N  
ATOM   3586  CE2 TRP B  16       6.405 -30.411  39.076  1.00 47.26           C  
ATOM   3587  CE3 TRP B  16       4.658 -29.274  40.394  1.00 48.16           C  
ATOM   3588  CZ2 TRP B  16       5.494 -30.807  38.101  1.00 48.27           C  
ATOM   3589  CZ3 TRP B  16       3.750 -29.681  39.405  1.00 48.14           C  
ATOM   3590  CH2 TRP B  16       4.161 -30.427  38.286  1.00 47.37           C  
ATOM   3591  N   GLY B  17       8.532 -30.283  44.909  1.00 57.16           N  
ATOM   3592  CA  GLY B  17       9.439 -31.296  45.450  1.00 59.80           C  
ATOM   3593  C   GLY B  17       8.745 -32.437  46.180  1.00 60.51           C  
ATOM   3594  O   GLY B  17       9.380 -33.442  46.500  1.00 57.80           O  
ATOM   3595  N   ARG B  18       7.444 -32.280  46.444  1.00 63.18           N  
ATOM   3596  CA  ARG B  18       6.641 -33.308  47.114  1.00 66.58           C  
ATOM   3597  C   ARG B  18       7.266 -33.637  48.479  1.00 67.59           C  
ATOM   3598  O   ARG B  18       7.578 -34.790  48.789  1.00 70.93           O  
ATOM   3599  CB  ARG B  18       6.493 -34.545  46.205  1.00 69.32           C  
ATOM   3600  CG  ARG B  18       5.748 -35.743  46.784  1.00 73.65           C  
ATOM   3601  CD  ARG B  18       4.268 -35.472  46.998  1.00 75.50           C  
ATOM   3602  NE  ARG B  18       3.516 -36.714  47.177  1.00 77.95           N  
ATOM   3603  CZ  ARG B  18       2.348 -36.805  47.810  1.00 78.29           C  
ATOM   3604  NH1 ARG B  18       1.788 -35.726  48.344  1.00 76.21           N  
ATOM   3605  NH2 ARG B  18       1.740 -37.980  47.916  1.00 77.93           N  
ATOM   3606  N   THR B  19       7.463 -32.591  49.277  1.00 65.52           N  
ATOM   3607  CA  THR B  19       8.095 -32.705  50.586  1.00 64.80           C  
ATOM   3608  C   THR B  19       7.446 -31.728  51.570  1.00 63.18           C  
ATOM   3609  O   THR B  19       6.771 -30.783  51.156  1.00 62.07           O  
ATOM   3610  CB  THR B  19       9.628 -32.472  50.498  1.00 66.63           C  
ATOM   3611  OG1 THR B  19      10.275 -33.064  51.630  1.00 68.98           O  
ATOM   3612  CG2 THR B  19       9.977 -30.975  50.425  1.00 65.50           C  
ATOM   3613  N   ALA B  20       7.656 -31.974  52.864  1.00 62.05           N  
ATOM   3614  CA  ALA B  20       7.128 -31.143  53.959  1.00 60.51           C  
ATOM   3615  C   ALA B  20       5.632 -30.779  53.839  1.00 59.59           C  
ATOM   3616  O   ALA B  20       5.291 -29.595  53.714  1.00 58.58           O  
ATOM   3617  CB  ALA B  20       7.988 -29.892  54.147  1.00 58.87           C  
ATOM   3618  N   PRO B  21       4.735 -31.793  53.894  1.00 59.34           N  
ATOM   3619  CA  PRO B  21       3.293 -31.538  53.749  1.00 58.95           C  
ATOM   3620  C   PRO B  21       2.748 -30.590  54.811  1.00 59.70           C  
ATOM   3621  O   PRO B  21       3.296 -30.518  55.916  1.00 58.28           O  
ATOM   3622  CB  PRO B  21       2.662 -32.928  53.908  1.00 60.35           C  
ATOM   3623  CG  PRO B  21       3.696 -33.764  54.583  1.00 58.75           C  
ATOM   3624  CD  PRO B  21       5.016 -33.225  54.120  1.00 59.09           C  
ATOM   3625  N   SER B  22       1.675 -29.877  54.470  1.00 60.79           N  
ATOM   3626  CA  SER B  22       1.085 -28.872  55.354  1.00 62.23           C  
ATOM   3627  C   SER B  22      -0.396 -28.646  55.040  1.00 62.53           C  
ATOM   3628  O   SER B  22      -0.753 -28.317  53.905  1.00 63.40           O  
ATOM   3629  CB  SER B  22       1.857 -27.557  55.235  1.00 63.28           C  
ATOM   3630  OG  SER B  22       1.362 -26.584  56.132  1.00 65.18           O  
ATOM   3631  N   VAL B  23      -1.245 -28.817  56.055  1.00 62.78           N  
ATOM   3632  CA  VAL B  23      -2.703 -28.710  55.901  1.00 61.03           C  
ATOM   3633  C   VAL B  23      -3.175 -27.264  56.025  1.00 59.51           C  
ATOM   3634  O   VAL B  23      -2.987 -26.621  57.064  1.00 58.67           O  
ATOM   3635  CB  VAL B  23      -3.473 -29.586  56.921  1.00 61.14           C  
ATOM   3636  CG1 VAL B  23      -4.948 -29.685  56.539  1.00 61.09           C  
ATOM   3637  CG2 VAL B  23      -2.857 -30.975  57.018  1.00 60.98           C  
ATOM   3638  N   ALA B  24      -3.798 -26.764  54.961  1.00 56.81           N  
ATOM   3639  CA  ALA B  24      -4.259 -25.383  54.922  1.00 54.66           C  
ATOM   3640  C   ALA B  24      -5.693 -25.248  54.425  1.00 53.75           C  
ATOM   3641  O   ALA B  24      -6.205 -26.104  53.702  1.00 54.46           O  
ATOM   3642  CB  ALA B  24      -3.327 -24.545  54.063  1.00 55.17           C  
ATOM   3643  N   ASN B  25      -6.336 -24.160  54.824  1.00 52.19           N  
ATOM   3644  CA  ASN B  25      -7.607 -23.785  54.232  1.00 55.82           C  
ATOM   3645  C   ASN B  25      -7.358 -23.153  52.864  1.00 54.35           C  
ATOM   3646  O   ASN B  25      -6.663 -22.143  52.755  1.00 55.27           O  
ATOM   3647  CB  ASN B  25      -8.374 -22.833  55.151  1.00 55.52           C  
ATOM   3648  CG  ASN B  25      -8.649 -23.434  56.523  1.00 59.39           C  
ATOM   3649  OD1 ASN B  25      -8.794 -24.655  56.673  1.00 57.25           O  
ATOM   3650  ND2 ASN B  25      -8.727 -22.573  57.534  1.00 59.39           N  
ATOM   3651  N   VAL B  26      -7.915 -23.772  51.828  1.00 53.19           N  
ATOM   3652  CA  VAL B  26      -7.733 -23.317  50.449  1.00 53.90           C  
ATOM   3653  C   VAL B  26      -8.989 -22.640  49.889  1.00 53.71           C  
ATOM   3654  O   VAL B  26     -10.052 -23.262  49.765  1.00 53.15           O  
ATOM   3655  CB  VAL B  26      -7.275 -24.473  49.526  1.00 51.99           C  
ATOM   3656  CG1 VAL B  26      -7.262 -24.039  48.066  1.00 51.79           C  
ATOM   3657  CG2 VAL B  26      -5.898 -24.967  49.948  1.00 52.30           C  
ATOM   3658  N   LEU B  27      -8.853 -21.357  49.567  1.00 54.18           N  
ATOM   3659  CA  LEU B  27      -9.893 -20.617  48.868  1.00 52.13           C  
ATOM   3660  C   LEU B  27      -9.626 -20.681  47.370  1.00 52.82           C  
ATOM   3661  O   LEU B  27      -8.504 -20.418  46.919  1.00 51.04           O  
ATOM   3662  CB  LEU B  27      -9.931 -19.166  49.349  1.00 53.07           C  
ATOM   3663  CG  LEU B  27     -10.930 -18.211  48.694  1.00 54.03           C  
ATOM   3664  CD1 LEU B  27     -12.361 -18.713  48.838  1.00 55.81           C  
ATOM   3665  CD2 LEU B  27     -10.783 -16.817  49.283  1.00 53.46           C  
ATOM   3666  N   ARG B  28     -10.652 -21.040  46.602  1.00 52.28           N  
ATOM   3667  CA  ARG B  28     -10.503 -21.178  45.153  1.00 54.52           C  
ATOM   3668  C   ARG B  28     -11.679 -20.560  44.400  1.00 54.58           C  
ATOM   3669  O   ARG B  28     -12.669 -21.233  44.105  1.00 55.51           O  
ATOM   3670  CB  ARG B  28     -10.311 -22.644  44.762  1.00 55.56           C  
ATOM   3671  CG  ARG B  28      -9.818 -22.812  43.341  1.00 59.50           C  
ATOM   3672  CD  ARG B  28     -10.053 -24.211  42.806  1.00 61.27           C  
ATOM   3673  NE  ARG B  28     -10.007 -24.212  41.345  1.00 66.35           N  
ATOM   3674  CZ  ARG B  28      -8.890 -24.248  40.621  1.00 68.07           C  
ATOM   3675  NH1 ARG B  28      -7.702 -24.291  41.212  1.00 67.38           N  
ATOM   3676  NH2 ARG B  28      -8.961 -24.240  39.296  1.00 71.44           N  
ATOM   3677  N   THR B  29     -11.550 -19.279  44.078  1.00 52.58           N  
ATOM   3678  CA  THR B  29     -12.646 -18.527  43.482  1.00 53.53           C  
ATOM   3679  C   THR B  29     -12.181 -17.634  42.319  1.00 52.82           C  
ATOM   3680  O   THR B  29     -11.103 -17.042  42.387  1.00 53.34           O  
ATOM   3681  CB  THR B  29     -13.367 -17.681  44.556  1.00 54.16           C  
ATOM   3682  OG1 THR B  29     -14.410 -16.909  43.950  1.00 56.76           O  
ATOM   3683  CG2 THR B  29     -12.385 -16.745  45.276  1.00 53.01           C  
ATOM   3684  N   PRO B  30     -12.982 -17.552  41.236  1.00 51.67           N  
ATOM   3685  CA  PRO B  30     -12.700 -16.532  40.217  1.00 49.52           C  
ATOM   3686  C   PRO B  30     -13.213 -15.154  40.637  1.00 49.94           C  
ATOM   3687  O   PRO B  30     -13.072 -14.179  39.898  1.00 50.41           O  
ATOM   3688  CB  PRO B  30     -13.444 -17.045  38.980  1.00 49.77           C  
ATOM   3689  CG  PRO B  30     -14.507 -17.948  39.508  1.00 49.90           C  
ATOM   3690  CD  PRO B  30     -13.980 -18.540  40.783  1.00 51.47           C  
ATOM   3691  N   ASP B  31     -13.785 -15.080  41.833  1.00 51.88           N  
ATOM   3692  CA  ASP B  31     -14.391 -13.857  42.340  1.00 54.78           C  
ATOM   3693  C   ASP B  31     -13.374 -13.041  43.138  1.00 55.53           C  
ATOM   3694  O   ASP B  31     -13.028 -13.396  44.269  1.00 55.73           O  
ATOM   3695  CB  ASP B  31     -15.603 -14.221  43.207  1.00 58.34           C  
ATOM   3696  CG  ASP B  31     -16.566 -13.071  43.397  1.00 58.84           C  
ATOM   3697  OD1 ASP B  31     -16.145 -11.897  43.327  1.00 59.40           O  
ATOM   3698  OD2 ASP B  31     -17.760 -13.353  43.637  1.00 63.38           O  
ATOM   3699  N   ALA B  32     -12.903 -11.946  42.543  1.00 55.62           N  
ATOM   3700  CA  ALA B  32     -11.897 -11.084  43.168  1.00 56.86           C  
ATOM   3701  C   ALA B  32     -12.431 -10.419  44.432  1.00 58.84           C  
ATOM   3702  O   ALA B  32     -11.670 -10.122  45.355  1.00 58.58           O  
ATOM   3703  CB  ALA B  32     -11.398 -10.039  42.182  1.00 54.91           C  
ATOM   3704  N   GLU B  33     -13.745 -10.202  44.457  1.00 60.39           N  
ATOM   3705  CA  GLU B  33     -14.450  -9.645  45.607  1.00 61.70           C  
ATOM   3706  C   GLU B  33     -14.320 -10.566  46.823  1.00 59.02           C  
ATOM   3707  O   GLU B  33     -14.127 -10.099  47.948  1.00 55.49           O  
ATOM   3708  CB  GLU B  33     -15.928  -9.428  45.252  1.00 65.03           C  
ATOM   3709  CG  GLU B  33     -16.650  -8.415  46.126  1.00 72.19           C  
ATOM   3710  CD  GLU B  33     -16.014  -7.038  46.078  1.00 75.62           C  
ATOM   3711  OE1 GLU B  33     -15.744  -6.473  47.161  1.00 77.39           O  
ATOM   3712  OE2 GLU B  33     -15.777  -6.526  44.961  1.00 75.82           O  
ATOM   3713  N   MET B  34     -14.412 -11.871  46.573  1.00 58.18           N  
ATOM   3714  CA  MET B  34     -14.250 -12.901  47.593  1.00 59.09           C  
ATOM   3715  C   MET B  34     -12.842 -12.884  48.200  1.00 58.68           C  
ATOM   3716  O   MET B  34     -12.677 -12.993  49.420  1.00 57.40           O  
ATOM   3717  CB  MET B  34     -14.543 -14.276  46.984  1.00 61.21           C  
ATOM   3718  CG  MET B  34     -15.412 -15.185  47.837  1.00 66.72           C  
ATOM   3719  SD  MET B  34     -17.162 -14.739  47.750  1.00 74.99           S  
ATOM   3720  CE  MET B  34     -17.328 -13.573  49.103  1.00 66.76           C  
ATOM   3721  N   ILE B  35     -11.835 -12.736  47.343  1.00 56.83           N  
ATOM   3722  CA  ILE B  35     -10.438 -12.711  47.776  1.00 54.84           C  
ATOM   3723  C   ILE B  35     -10.191 -11.532  48.720  1.00 53.49           C  
ATOM   3724  O   ILE B  35      -9.488 -11.676  49.716  1.00 54.87           O  
ATOM   3725  CB  ILE B  35      -9.465 -12.717  46.568  1.00 54.80           C  
ATOM   3726  CG1 ILE B  35      -9.617 -14.022  45.771  1.00 53.29           C  
ATOM   3727  CG2 ILE B  35      -8.019 -12.542  47.017  1.00 53.78           C  
ATOM   3728  CD1 ILE B  35      -9.003 -13.991  44.386  1.00 53.86           C  
ATOM   3729  N   VAL B  36     -10.797 -10.386  48.419  1.00 54.33           N  
ATOM   3730  CA  VAL B  36     -10.728  -9.210  49.293  1.00 55.99           C  
ATOM   3731  C   VAL B  36     -11.356  -9.484  50.667  1.00 58.50           C  
ATOM   3732  O   VAL B  36     -10.815  -9.058  51.691  1.00 59.76           O  
ATOM   3733  CB  VAL B  36     -11.380  -7.966  48.642  1.00 55.49           C  
ATOM   3734  CG1 VAL B  36     -11.343  -6.765  49.582  1.00 55.09           C  
ATOM   3735  CG2 VAL B  36     -10.685  -7.623  47.334  1.00 55.57           C  
ATOM   3736  N   LYS B  37     -12.480 -10.203  50.687  1.00 59.65           N  
ATOM   3737  CA  LYS B  37     -13.179 -10.506  51.948  1.00 61.17           C  
ATOM   3738  C   LYS B  37     -12.408 -11.495  52.816  1.00 58.53           C  
ATOM   3739  O   LYS B  37     -12.367 -11.345  54.035  1.00 59.27           O  
ATOM   3740  CB  LYS B  37     -14.615 -11.015  51.712  1.00 63.21           C  
ATOM   3741  CG  LYS B  37     -15.522 -10.096  50.897  1.00 67.96           C  
ATOM   3742  CD  LYS B  37     -15.446  -8.643  51.348  1.00 70.47           C  
ATOM   3743  CE  LYS B  37     -15.836  -7.700  50.221  1.00 74.43           C  
ATOM   3744  NZ  LYS B  37     -15.186  -6.366  50.370  1.00 76.52           N  
ATOM   3745  N   ALA B  38     -11.803 -12.500  52.183  1.00 57.37           N  
ATOM   3746  CA  ALA B  38     -11.028 -13.516  52.895  1.00 56.48           C  
ATOM   3747  C   ALA B  38      -9.820 -12.921  53.614  1.00 56.53           C  
ATOM   3748  O   ALA B  38      -9.494 -13.338  54.721  1.00 57.78           O  
ATOM   3749  CB  ALA B  38     -10.598 -14.619  51.948  1.00 55.72           C  
ATOM   3750  N   VAL B  39      -9.168 -11.943  52.986  1.00 56.97           N  
ATOM   3751  CA  VAL B  39      -8.070 -11.207  53.620  1.00 55.44           C  
ATOM   3752  C   VAL B  39      -8.571 -10.433  54.849  1.00 57.12           C  
ATOM   3753  O   VAL B  39      -7.991 -10.541  55.933  1.00 54.32           O  
ATOM   3754  CB  VAL B  39      -7.349 -10.271  52.617  1.00 55.10           C  
ATOM   3755  CG1 VAL B  39      -6.361  -9.348  53.324  1.00 54.25           C  
ATOM   3756  CG2 VAL B  39      -6.636 -11.088  51.549  1.00 52.97           C  
ATOM   3757  N   ALA B  40      -9.655  -9.675  54.681  1.00 57.45           N  
ATOM   3758  CA  ALA B  40     -10.269  -8.939  55.791  1.00 58.47           C  
ATOM   3759  C   ALA B  40     -10.670  -9.884  56.930  1.00 58.38           C  
ATOM   3760  O   ALA B  40     -10.499  -9.552  58.105  1.00 60.31           O  
ATOM   3761  CB  ALA B  40     -11.467  -8.136  55.304  1.00 57.21           C  
ATOM   3762  N   ARG B  41     -11.182 -11.059  56.563  1.00 58.38           N  
ATOM   3763  CA  ARG B  41     -11.518 -12.129  57.507  1.00 61.30           C  
ATOM   3764  C   ARG B  41     -10.301 -12.578  58.325  1.00 61.98           C  
ATOM   3765  O   ARG B  41     -10.402 -12.783  59.538  1.00 61.67           O  
ATOM   3766  CB  ARG B  41     -12.129 -13.318  56.754  1.00 64.51           C  
ATOM   3767  CG  ARG B  41     -12.655 -14.441  57.635  1.00 68.01           C  
ATOM   3768  CD  ARG B  41     -13.494 -15.422  56.833  1.00 71.45           C  
ATOM   3769  NE  ARG B  41     -14.091 -16.444  57.691  1.00 76.60           N  
ATOM   3770  CZ  ARG B  41     -14.963 -17.368  57.290  1.00 78.50           C  
ATOM   3771  NH1 ARG B  41     -15.367 -17.421  56.024  1.00 79.61           N  
ATOM   3772  NH2 ARG B  41     -15.435 -18.246  58.164  1.00 79.72           N  
ATOM   3773  N   VAL B  42      -9.159 -12.725  57.652  1.00 61.44           N  
ATOM   3774  CA  VAL B  42      -7.888 -13.052  58.304  1.00 58.83           C  
ATOM   3775  C   VAL B  42      -7.384 -11.860  59.123  1.00 58.96           C  
ATOM   3776  O   VAL B  42      -6.803 -12.040  60.193  1.00 60.17           O  
ATOM   3777  CB  VAL B  42      -6.826 -13.516  57.275  1.00 58.17           C  
ATOM   3778  CG1 VAL B  42      -5.450 -13.653  57.914  1.00 57.07           C  
ATOM   3779  CG2 VAL B  42      -7.240 -14.836  56.639  1.00 56.06           C  
ATOM   3780  N   ALA B  43      -7.633 -10.649  58.627  1.00 60.55           N  
ATOM   3781  CA  ALA B  43      -7.267  -9.416  59.336  1.00 64.66           C  
ATOM   3782  C   ALA B  43      -8.166  -9.114  60.547  1.00 70.99           C  
ATOM   3783  O   ALA B  43      -7.838  -8.251  61.369  1.00 72.02           O  
ATOM   3784  CB  ALA B  43      -7.249  -8.234  58.379  1.00 63.28           C  
ATOM   3785  N   GLU B  44      -9.299  -9.811  60.638  1.00 76.32           N  
ATOM   3786  CA  GLU B  44     -10.164  -9.764  61.822  1.00 78.86           C  
ATOM   3787  C   GLU B  44      -9.871 -10.956  62.742  1.00 79.63           C  
ATOM   3788  O   GLU B  44     -10.029 -10.866  63.963  1.00 75.96           O  
ATOM   3789  CB  GLU B  44     -11.643  -9.742  61.420  1.00 80.18           C  
ATOM   3790  CG  GLU B  44     -12.592  -9.441  62.575  1.00 83.61           C  
ATOM   3791  CD  GLU B  44     -14.046  -9.336  62.148  1.00 85.39           C  
ATOM   3792  OE1 GLU B  44     -14.481 -10.117  61.272  1.00 85.76           O  
ATOM   3793  OE2 GLU B  44     -14.758  -8.471  62.704  1.00 84.81           O  
ATOM   3794  N   SER B  45      -9.436 -12.063  62.141  1.00 81.88           N  
ATOM   3795  CA  SER B  45      -8.979 -13.246  62.874  1.00 84.51           C  
ATOM   3796  C   SER B  45      -7.886 -12.894  63.891  1.00 85.98           C  
ATOM   3797  O   SER B  45      -7.740 -13.566  64.914  1.00 87.75           O  
ATOM   3798  CB  SER B  45      -8.468 -14.305  61.891  1.00 84.03           C  
ATOM   3799  OG  SER B  45      -8.474 -15.598  62.468  1.00 85.26           O  
ATOM   3800  N   GLY B  46      -7.126 -11.838  63.600  1.00 86.87           N  
ATOM   3801  CA  GLY B  46      -6.102 -11.326  64.508  1.00 85.68           C  
ATOM   3802  C   GLY B  46      -4.682 -11.510  64.003  1.00 87.60           C  
ATOM   3803  O   GLY B  46      -3.724 -11.344  64.764  1.00 87.90           O  
ATOM   3804  N   GLY B  47      -4.544 -11.849  62.721  1.00 84.38           N  
ATOM   3805  CA  GLY B  47      -3.235 -12.084  62.114  1.00 79.69           C  
ATOM   3806  C   GLY B  47      -2.979 -13.557  61.867  1.00 76.79           C  
ATOM   3807  O   GLY B  47      -3.479 -14.119  60.891  1.00 74.41           O  
ATOM   3808  N   GLY B  48      -2.197 -14.178  62.754  1.00 75.97           N  
ATOM   3809  CA  GLY B  48      -1.906 -15.614  62.687  1.00 69.20           C  
ATOM   3810  C   GLY B  48      -3.204 -16.398  62.652  1.00 69.70           C  
ATOM   3811  O   GLY B  48      -4.132 -16.083  63.402  1.00 71.79           O  
ATOM   3812  N   ARG B  49      -3.288 -17.427  61.810  1.00 66.48           N  
ATOM   3813  CA  ARG B  49      -2.150 -18.001  61.088  1.00 64.55           C  
ATOM   3814  C   ARG B  49      -1.959 -17.473  59.654  1.00 60.29           C  
ATOM   3815  O   ARG B  49      -1.420 -18.176  58.795  1.00 59.63           O  
ATOM   3816  CB  ARG B  49      -2.293 -19.525  61.066  1.00 68.15           C  
ATOM   3817  CG  ARG B  49      -2.552 -20.151  62.430  1.00 70.42           C  
ATOM   3818  CD  ARG B  49      -1.258 -20.621  63.064  1.00 74.59           C  
ATOM   3819  NE  ARG B  49      -0.720 -21.785  62.361  1.00 77.83           N  
ATOM   3820  CZ  ARG B  49       0.574 -22.072  62.253  1.00 77.63           C  
ATOM   3821  NH1 ARG B  49       1.491 -21.280  62.796  1.00 82.08           N  
ATOM   3822  NH2 ARG B  49       0.956 -23.157  61.594  1.00 78.40           N  
ATOM   3823  N   GLY B  50      -2.409 -16.243  59.409  1.00 56.16           N  
ATOM   3824  CA  GLY B  50      -2.170 -15.538  58.147  1.00 51.96           C  
ATOM   3825  C   GLY B  50      -2.724 -16.158  56.873  1.00 48.22           C  
ATOM   3826  O   GLY B  50      -3.449 -17.152  56.903  1.00 45.55           O  
ATOM   3827  N   ALA B  51      -2.364 -15.556  55.744  1.00 47.68           N  
ATOM   3828  CA  ALA B  51      -2.754 -16.059  54.425  1.00 45.54           C  
ATOM   3829  C   ALA B  51      -1.573 -16.012  53.467  1.00 42.61           C  
ATOM   3830  O   ALA B  51      -0.684 -15.185  53.620  1.00 43.69           O  
ATOM   3831  CB  ALA B  51      -3.906 -15.237  53.870  1.00 45.05           C  
ATOM   3832  N   ILE B  52      -1.563 -16.899  52.479  1.00 42.46           N  
ATOM   3833  CA  ILE B  52      -0.582 -16.817  51.392  1.00 41.61           C  
ATOM   3834  C   ILE B  52      -1.220 -17.165  50.044  1.00 41.00           C  
ATOM   3835  O   ILE B  52      -2.035 -18.083  49.960  1.00 41.40           O  
ATOM   3836  CB  ILE B  52       0.657 -17.716  51.650  1.00 40.88           C  
ATOM   3837  CG1 ILE B  52       1.834 -17.315  50.748  1.00 39.71           C  
ATOM   3838  CG2 ILE B  52       0.330 -19.193  51.467  1.00 40.50           C  
ATOM   3839  CD1 ILE B  52       2.571 -16.074  51.204  1.00 39.66           C  
ATOM   3840  N   ALA B  53      -0.836 -16.443  48.992  1.00 39.56           N  
ATOM   3841  CA  ALA B  53      -1.287 -16.788  47.647  1.00 38.12           C  
ATOM   3842  C   ALA B  53      -0.567 -18.033  47.152  1.00 37.48           C  
ATOM   3843  O   ALA B  53       0.571 -18.301  47.546  1.00 39.58           O  
ATOM   3844  CB  ALA B  53      -1.081 -15.622  46.685  1.00 35.83           C  
ATOM   3845  N   ARG B  54      -1.244 -18.796  46.301  1.00 35.71           N  
ATOM   3846  CA  ARG B  54      -0.643 -19.929  45.607  1.00 36.25           C  
ATOM   3847  C   ARG B  54      -0.927 -19.833  44.099  1.00 35.96           C  
ATOM   3848  O   ARG B  54      -2.029 -19.462  43.686  1.00 36.32           O  
ATOM   3849  CB  ARG B  54      -1.191 -21.236  46.174  1.00 35.14           C  
ATOM   3850  CG  ARG B  54      -0.636 -22.506  45.550  1.00 36.49           C  
ATOM   3851  CD  ARG B  54      -1.350 -23.721  46.128  1.00 37.22           C  
ATOM   3852  NE  ARG B  54      -0.747 -24.985  45.709  1.00 38.01           N  
ATOM   3853  CZ  ARG B  54       0.255 -25.590  46.341  1.00 38.32           C  
ATOM   3854  NH1 ARG B  54       0.794 -25.044  47.425  1.00 39.71           N  
ATOM   3855  NH2 ARG B  54       0.733 -26.736  45.878  1.00 39.26           N  
ATOM   3856  N   GLY B  55       0.072 -20.161  43.286  1.00 36.08           N  
ATOM   3857  CA  GLY B  55      -0.085 -20.173  41.835  1.00 34.31           C  
ATOM   3858  C   GLY B  55      -0.291 -21.593  41.365  1.00 36.40           C  
ATOM   3859  O   GLY B  55      -1.205 -22.271  41.828  1.00 36.56           O  
ATOM   3860  N   LEU B  56       0.570 -22.059  40.462  1.00 34.75           N  
ATOM   3861  CA  LEU B  56       0.460 -23.416  39.941  1.00 34.97           C  
ATOM   3862  C   LEU B  56       1.303 -24.433  40.716  1.00 36.10           C  
ATOM   3863  O   LEU B  56       1.450 -25.581  40.284  1.00 37.37           O  
ATOM   3864  CB  LEU B  56       0.803 -23.452  38.445  1.00 35.19           C  
ATOM   3865  CG  LEU B  56      -0.358 -23.206  37.476  1.00 36.10           C  
ATOM   3866  CD1 LEU B  56       0.142 -22.700  36.132  1.00 35.51           C  
ATOM   3867  CD2 LEU B  56      -1.211 -24.462  37.298  1.00 37.21           C  
ATOM   3868  N   GLY B  57       1.862 -24.003  41.849  1.00 36.73           N  
ATOM   3869  CA  GLY B  57       2.606 -24.891  42.754  1.00 36.20           C  
ATOM   3870  C   GLY B  57       3.900 -25.466  42.194  1.00 35.90           C  
ATOM   3871  O   GLY B  57       4.293 -26.572  42.557  1.00 34.66           O  
ATOM   3872  N   ARG B  58       4.576 -24.710  41.331  1.00 34.57           N  
ATOM   3873  CA  ARG B  58       5.827 -25.181  40.721  1.00 35.10           C  
ATOM   3874  C   ARG B  58       7.104 -24.924  41.530  1.00 33.91           C  
ATOM   3875  O   ARG B  58       8.140 -25.515  41.236  1.00 35.43           O  
ATOM   3876  CB  ARG B  58       5.984 -24.651  39.292  1.00 34.77           C  
ATOM   3877  CG  ARG B  58       5.567 -25.639  38.212  1.00 36.88           C  
ATOM   3878  CD  ARG B  58       4.100 -26.038  38.309  1.00 38.53           C  
ATOM   3879  NE  ARG B  58       3.733 -27.007  37.273  1.00 41.33           N  
ATOM   3880  CZ  ARG B  58       2.512 -27.511  37.105  1.00 41.68           C  
ATOM   3881  NH1 ARG B  58       1.515 -27.157  37.907  1.00 42.11           N  
ATOM   3882  NH2 ARG B  58       2.289 -28.376  36.130  1.00 43.96           N  
ATOM   3883  N   SER B  59       7.046 -24.046  42.530  1.00 34.54           N  
ATOM   3884  CA  SER B  59       8.159 -23.932  43.473  1.00 34.85           C  
ATOM   3885  C   SER B  59       8.295 -25.253  44.221  1.00 36.10           C  
ATOM   3886  O   SER B  59       7.288 -25.850  44.608  1.00 35.59           O  
ATOM   3887  CB  SER B  59       7.935 -22.799  44.465  1.00 33.98           C  
ATOM   3888  OG  SER B  59       7.822 -21.562  43.798  1.00 34.87           O  
ATOM   3889  N   TYR B  60       9.532 -25.701  44.415  1.00 37.01           N  
ATOM   3890  CA  TYR B  60       9.826 -27.010  45.017  1.00 40.19           C  
ATOM   3891  C   TYR B  60       9.631 -27.043  46.536  1.00 41.55           C  
ATOM   3892  O   TYR B  60       9.366 -28.102  47.107  1.00 43.55           O  
ATOM   3893  CB  TYR B  60      11.263 -27.432  44.699  1.00 40.89           C  
ATOM   3894  CG  TYR B  60      11.516 -27.831  43.265  1.00 43.49           C  
ATOM   3895  CD1 TYR B  60      11.824 -29.153  42.938  1.00 44.91           C  
ATOM   3896  CD2 TYR B  60      11.460 -26.890  42.229  1.00 45.50           C  
ATOM   3897  CE1 TYR B  60      12.068 -29.526  41.626  1.00 45.71           C  
ATOM   3898  CE2 TYR B  60      11.705 -27.251  40.909  1.00 45.07           C  
ATOM   3899  CZ  TYR B  60      12.007 -28.570  40.614  1.00 47.58           C  
ATOM   3900  OH  TYR B  60      12.248 -28.944  39.308  1.00 46.39           O  
ATOM   3901  N   GLY B  61       9.786 -25.890  47.180  1.00 41.85           N  
ATOM   3902  CA  GLY B  61       9.744 -25.802  48.639  1.00 43.45           C  
ATOM   3903  C   GLY B  61       8.398 -25.388  49.200  1.00 42.69           C  
ATOM   3904  O   GLY B  61       7.356 -25.736  48.654  1.00 42.16           O  
ATOM   3905  N   ASP B  62       8.438 -24.609  50.275  1.00 44.02           N  
ATOM   3906  CA  ASP B  62       7.272 -24.350  51.122  1.00 42.54           C  
ATOM   3907  C   ASP B  62       6.803 -22.893  51.125  1.00 41.46           C  
ATOM   3908  O   ASP B  62       6.226 -22.427  52.116  1.00 42.32           O  
ATOM   3909  CB  ASP B  62       7.589 -24.803  52.562  1.00 44.70           C  
ATOM   3910  CG  ASP B  62       8.852 -24.133  53.137  1.00 47.18           C  
ATOM   3911  OD1 ASP B  62       9.604 -23.472  52.380  1.00 46.24           O  
ATOM   3912  OD2 ASP B  62       9.094 -24.266  54.357  1.00 47.53           O  
ATOM   3913  N   ASN B  63       7.050 -22.164  50.038  1.00 40.55           N  
ATOM   3914  CA  ASN B  63       6.645 -20.752  49.983  1.00 38.67           C  
ATOM   3915  C   ASN B  63       5.177 -20.534  49.610  1.00 37.74           C  
ATOM   3916  O   ASN B  63       4.607 -19.488  49.923  1.00 36.67           O  
ATOM   3917  CB  ASN B  63       7.580 -19.912  49.094  1.00 38.00           C  
ATOM   3918  CG  ASN B  63       7.751 -20.484  47.701  1.00 38.21           C  
ATOM   3919  OD1 ASN B  63       7.390 -21.630  47.436  1.00 38.57           O  
ATOM   3920  ND2 ASN B  63       8.322 -19.682  46.800  1.00 35.99           N  
ATOM   3921  N   ALA B  64       4.576 -21.532  48.964  1.00 38.39           N  
ATOM   3922  CA  ALA B  64       3.185 -21.451  48.506  1.00 42.68           C  
ATOM   3923  C   ALA B  64       2.231 -22.298  49.353  1.00 45.10           C  
ATOM   3924  O   ALA B  64       1.206 -22.770  48.851  1.00 46.21           O  
ATOM   3925  CB  ALA B  64       3.084 -21.845  47.032  1.00 41.42           C  
ATOM   3926  N   GLN B  65       2.577 -22.492  50.628  1.00 46.04           N  
ATOM   3927  CA  GLN B  65       1.705 -23.186  51.583  1.00 47.50           C  
ATOM   3928  C   GLN B  65       1.750 -22.540  52.972  1.00 47.10           C  
ATOM   3929  O   GLN B  65       2.729 -21.877  53.330  1.00 46.72           O  
ATOM   3930  CB  GLN B  65       2.026 -24.684  51.645  1.00 46.97           C  
ATOM   3931  CG  GLN B  65       3.391 -25.028  52.212  1.00 47.90           C  
ATOM   3932  CD  GLN B  65       3.880 -26.388  51.752  1.00 49.84           C  
ATOM   3933  OE1 GLN B  65       4.141 -26.598  50.570  1.00 52.94           O  
ATOM   3934  NE2 GLN B  65       4.017 -27.316  52.688  1.00 51.45           N  
ATOM   3935  N   ASN B  66       0.680 -22.733  53.742  1.00 45.36           N  
ATOM   3936  CA  ASN B  66       0.523 -22.068  55.031  1.00 45.20           C  
ATOM   3937  C   ASN B  66      -0.264 -22.959  56.001  1.00 45.18           C  
ATOM   3938  O   ASN B  66      -1.475 -22.789  56.166  1.00 43.94           O  
ATOM   3939  CB  ASN B  66      -0.166 -20.710  54.825  1.00 44.05           C  
ATOM   3940  CG  ASN B  66      -0.211 -19.864  56.087  1.00 44.35           C  
ATOM   3941  OD1 ASN B  66       0.483 -20.137  57.064  1.00 44.06           O  
ATOM   3942  ND2 ASN B  66      -1.032 -18.816  56.063  1.00 44.25           N  
ATOM   3943  N   GLY B  67       0.436 -23.906  56.628  1.00 46.23           N  
ATOM   3944  CA  GLY B  67      -0.165 -24.866  57.567  1.00 48.08           C  
ATOM   3945  C   GLY B  67      -1.019 -24.229  58.642  1.00 48.30           C  
ATOM   3946  O   GLY B  67      -0.583 -23.299  59.322  1.00 49.35           O  
ATOM   3947  N   GLY B  68      -2.248 -24.720  58.778  1.00 50.14           N  
ATOM   3948  CA  GLY B  68      -3.196 -24.183  59.757  1.00 50.96           C  
ATOM   3949  C   GLY B  68      -3.672 -22.779  59.430  1.00 51.03           C  
ATOM   3950  O   GLY B  68      -4.269 -22.106  60.271  1.00 51.15           O  
ATOM   3951  N   GLY B  69      -3.410 -22.335  58.202  1.00 51.50           N  
ATOM   3952  CA  GLY B  69      -3.789 -20.995  57.776  1.00 49.57           C  
ATOM   3953  C   GLY B  69      -4.485 -20.987  56.433  1.00 49.32           C  
ATOM   3954  O   GLY B  69      -4.851 -22.042  55.904  1.00 48.36           O  
ATOM   3955  N   LEU B  70      -4.659 -19.788  55.882  1.00 49.45           N  
ATOM   3956  CA  LEU B  70      -5.302 -19.624  54.583  1.00 48.74           C  
ATOM   3957  C   LEU B  70      -4.300 -19.621  53.426  1.00 49.06           C  
ATOM   3958  O   LEU B  70      -3.245 -18.975  53.498  1.00 46.28           O  
ATOM   3959  CB  LEU B  70      -6.150 -18.349  54.550  1.00 48.59           C  
ATOM   3960  CG  LEU B  70      -6.971 -18.079  53.277  1.00 46.14           C  
ATOM   3961  CD1 LEU B  70      -8.081 -19.104  53.089  1.00 44.66           C  
ATOM   3962  CD2 LEU B  70      -7.532 -16.666  53.294  1.00 44.64           C  
ATOM   3963  N   VAL B  71      -4.659 -20.359  52.376  1.00 48.84           N  
ATOM   3964  CA  VAL B  71      -3.956 -20.377  51.099  1.00 47.57           C  
ATOM   3965  C   VAL B  71      -4.968 -20.044  50.003  1.00 47.88           C  
ATOM   3966  O   VAL B  71      -5.927 -20.792  49.789  1.00 48.40           O  
ATOM   3967  CB  VAL B  71      -3.331 -21.761  50.820  1.00 47.86           C  
ATOM   3968  CG1 VAL B  71      -2.886 -21.883  49.367  1.00 47.77           C  
ATOM   3969  CG2 VAL B  71      -2.162 -22.019  51.755  1.00 47.95           C  
ATOM   3970  N   ILE B  72      -4.764 -18.912  49.331  1.00 43.62           N  
ATOM   3971  CA  ILE B  72      -5.656 -18.484  48.255  1.00 43.17           C  
ATOM   3972  C   ILE B  72      -5.082 -18.885  46.893  1.00 43.94           C  
ATOM   3973  O   ILE B  72      -4.124 -18.273  46.409  1.00 42.55           O  
ATOM   3974  CB  ILE B  72      -5.938 -16.964  48.321  1.00 43.63           C  
ATOM   3975  CG1 ILE B  72      -6.605 -16.608  49.653  1.00 43.47           C  
ATOM   3976  CG2 ILE B  72      -6.798 -16.509  47.143  1.00 43.09           C  
ATOM   3977  CD1 ILE B  72      -6.790 -15.122  49.881  1.00 44.23           C  
ATOM   3978  N   ASP B  73      -5.669 -19.928  46.301  1.00 42.59           N  
ATOM   3979  CA  ASP B  73      -5.335 -20.389  44.954  1.00 44.69           C  
ATOM   3980  C   ASP B  73      -5.783 -19.342  43.928  1.00 44.04           C  
ATOM   3981  O   ASP B  73      -6.978 -19.065  43.790  1.00 44.48           O  
ATOM   3982  CB  ASP B  73      -5.994 -21.750  44.684  1.00 44.93           C  
ATOM   3983  CG  ASP B  73      -5.697 -22.301  43.289  1.00 47.77           C  
ATOM   3984  OD1 ASP B  73      -5.155 -21.580  42.423  1.00 47.76           O  
ATOM   3985  OD2 ASP B  73      -6.020 -23.482  43.052  1.00 49.66           O  
ATOM   3986  N   MET B  74      -4.810 -18.769  43.221  1.00 42.89           N  
ATOM   3987  CA  MET B  74      -5.057 -17.650  42.314  1.00 40.93           C  
ATOM   3988  C   MET B  74      -5.330 -18.063  40.873  1.00 38.86           C  
ATOM   3989  O   MET B  74      -5.609 -17.207  40.034  1.00 40.57           O  
ATOM   3990  CB  MET B  74      -3.879 -16.663  42.343  1.00 42.60           C  
ATOM   3991  CG  MET B  74      -3.709 -15.919  43.656  1.00 42.56           C  
ATOM   3992  SD  MET B  74      -5.140 -14.916  44.079  1.00 44.05           S  
ATOM   3993  CE  MET B  74      -4.989 -13.590  42.882  1.00 43.41           C  
ATOM   3994  N   THR B  75      -5.251 -19.357  40.582  1.00 38.30           N  
ATOM   3995  CA  THR B  75      -5.389 -19.849  39.202  1.00 40.22           C  
ATOM   3996  C   THR B  75      -6.758 -19.582  38.527  1.00 43.13           C  
ATOM   3997  O   THR B  75      -6.813 -19.454  37.300  1.00 43.54           O  
ATOM   3998  CB  THR B  75      -5.021 -21.340  39.063  1.00 40.86           C  
ATOM   3999  OG1 THR B  75      -5.885 -22.123  39.895  1.00 41.44           O  
ATOM   4000  CG2 THR B  75      -3.563 -21.586  39.454  1.00 38.91           C  
ATOM   4001  N   PRO B  76      -7.864 -19.518  39.310  1.00 43.25           N  
ATOM   4002  CA  PRO B  76      -9.140 -19.141  38.685  1.00 42.47           C  
ATOM   4003  C   PRO B  76      -9.167 -17.695  38.189  1.00 41.44           C  
ATOM   4004  O   PRO B  76      -9.977 -17.359  37.328  1.00 39.91           O  
ATOM   4005  CB  PRO B  76     -10.149 -19.304  39.828  1.00 42.73           C  
ATOM   4006  CG  PRO B  76      -9.538 -20.343  40.704  1.00 43.86           C  
ATOM   4007  CD  PRO B  76      -8.075 -20.016  40.684  1.00 44.04           C  
ATOM   4008  N   LEU B  77      -8.300 -16.848  38.735  1.00 39.99           N  
ATOM   4009  CA  LEU B  77      -8.250 -15.453  38.318  1.00 39.95           C  
ATOM   4010  C   LEU B  77      -7.291 -15.350  37.131  1.00 38.75           C  
ATOM   4011  O   LEU B  77      -6.151 -14.921  37.280  1.00 38.66           O  
ATOM   4012  CB  LEU B  77      -7.818 -14.560  39.487  1.00 41.31           C  
ATOM   4013  CG  LEU B  77      -8.158 -13.071  39.433  1.00 44.36           C  
ATOM   4014  CD1 LEU B  77      -9.587 -12.821  39.893  1.00 43.79           C  
ATOM   4015  CD2 LEU B  77      -7.181 -12.266  40.276  1.00 45.27           C  
ATOM   4016  N   ASN B  78      -7.770 -15.757  35.957  1.00 35.65           N  
ATOM   4017  CA  ASN B  78      -6.911 -15.944  34.790  1.00 35.05           C  
ATOM   4018  C   ASN B  78      -7.367 -15.155  33.561  1.00 33.53           C  
ATOM   4019  O   ASN B  78      -7.202 -15.613  32.436  1.00 32.09           O  
ATOM   4020  CB  ASN B  78      -6.840 -17.433  34.440  1.00 34.09           C  
ATOM   4021  CG  ASN B  78      -8.181 -17.983  33.974  1.00 36.32           C  
ATOM   4022  OD1 ASN B  78      -9.232 -17.366  34.192  1.00 34.82           O  
ATOM   4023  ND2 ASN B  78      -8.151 -19.135  33.313  1.00 34.46           N  
ATOM   4024  N   THR B  79      -7.941 -13.975  33.775  1.00 32.95           N  
ATOM   4025  CA  THR B  79      -8.397 -13.153  32.661  1.00 33.41           C  
ATOM   4026  C   THR B  79      -7.257 -12.363  32.033  1.00 31.94           C  
ATOM   4027  O   THR B  79      -6.517 -11.665  32.730  1.00 31.41           O  
ATOM   4028  CB  THR B  79      -9.519 -12.181  33.087  1.00 34.43           C  
ATOM   4029  OG1 THR B  79     -10.662 -12.938  33.488  1.00 36.21           O  
ATOM   4030  CG2 THR B  79      -9.913 -11.250  31.937  1.00 35.54           C  
ATOM   4031  N   ILE B  80      -7.136 -12.480  30.714  1.00 31.98           N  
ATOM   4032  CA  ILE B  80      -6.298 -11.580  29.921  1.00 32.05           C  
ATOM   4033  C   ILE B  80      -7.144 -10.364  29.512  1.00 30.39           C  
ATOM   4034  O   ILE B  80      -8.020 -10.461  28.648  1.00 29.85           O  
ATOM   4035  CB  ILE B  80      -5.686 -12.303  28.688  1.00 33.21           C  
ATOM   4036  CG1 ILE B  80      -4.729 -13.409  29.152  1.00 34.22           C  
ATOM   4037  CG2 ILE B  80      -4.973 -11.310  27.779  1.00 33.93           C  
ATOM   4038  CD1 ILE B  80      -4.287 -14.374  28.070  1.00 33.68           C  
ATOM   4039  N   HIS B  81      -6.885  -9.223  30.146  1.00 28.50           N  
ATOM   4040  CA  HIS B  81      -7.674  -8.016  29.911  1.00 28.89           C  
ATOM   4041  C   HIS B  81      -7.399  -7.365  28.582  1.00 28.38           C  
ATOM   4042  O   HIS B  81      -8.329  -7.010  27.849  1.00 27.82           O  
ATOM   4043  CB  HIS B  81      -7.475  -7.020  31.058  1.00 28.90           C  
ATOM   4044  CG  HIS B  81      -7.933  -7.547  32.393  1.00 29.91           C  
ATOM   4045  ND1 HIS B  81      -9.231  -7.535  32.775  1.00 32.44           N  
ATOM   4046  CD2 HIS B  81      -7.224  -8.141  33.430  1.00 30.26           C  
ATOM   4047  CE1 HIS B  81      -9.344  -8.086  33.998  1.00 31.25           C  
ATOM   4048  NE2 HIS B  81      -8.115  -8.460  34.399  1.00 32.18           N  
ATOM   4049  N   SER B  82      -6.120  -7.193  28.258  1.00 26.62           N  
ATOM   4050  CA  SER B  82      -5.745  -6.534  27.013  1.00 25.83           C  
ATOM   4051  C   SER B  82      -4.319  -6.852  26.637  1.00 24.52           C  
ATOM   4052  O   SER B  82      -3.475  -7.123  27.504  1.00 25.34           O  
ATOM   4053  CB  SER B  82      -5.928  -5.005  27.083  1.00 25.51           C  
ATOM   4054  OG  SER B  82      -4.874  -4.387  27.812  1.00 25.68           O  
ATOM   4055  N   ILE B  83      -4.079  -6.828  25.332  1.00 24.09           N  
ATOM   4056  CA  ILE B  83      -2.746  -6.937  24.758  1.00 24.30           C  
ATOM   4057  C   ILE B  83      -2.660  -5.890  23.658  1.00 24.47           C  
ATOM   4058  O   ILE B  83      -3.586  -5.755  22.868  1.00 24.79           O  
ATOM   4059  CB  ILE B  83      -2.477  -8.344  24.175  1.00 23.73           C  
ATOM   4060  CG1 ILE B  83      -2.563  -9.412  25.272  1.00 22.39           C  
ATOM   4061  CG2 ILE B  83      -1.113  -8.394  23.489  1.00 22.73           C  
ATOM   4062  CD1 ILE B  83      -2.084 -10.792  24.855  1.00 23.36           C  
ATOM   4063  N   ASP B  84      -1.546  -5.167  23.594  1.00 26.38           N  
ATOM   4064  CA  ASP B  84      -1.387  -4.079  22.623  1.00 27.23           C  
ATOM   4065  C   ASP B  84      -0.032  -4.157  21.912  1.00 28.76           C  
ATOM   4066  O   ASP B  84       0.999  -3.971  22.539  1.00 28.20           O  
ATOM   4067  CB  ASP B  84      -1.530  -2.744  23.365  1.00 28.43           C  
ATOM   4068  CG  ASP B  84      -1.579  -1.541  22.442  1.00 29.18           C  
ATOM   4069  OD1 ASP B  84      -0.669  -1.340  21.599  1.00 30.84           O  
ATOM   4070  OD2 ASP B  84      -2.533  -0.764  22.590  1.00 29.40           O  
ATOM   4071  N   ALA B  85      -0.055  -4.412  20.604  1.00 28.65           N  
ATOM   4072  CA  ALA B  85       1.159  -4.533  19.799  1.00 31.62           C  
ATOM   4073  C   ALA B  85       1.949  -3.221  19.687  1.00 30.92           C  
ATOM   4074  O   ALA B  85       3.151  -3.250  19.440  1.00 31.83           O  
ATOM   4075  CB  ALA B  85       0.827  -5.074  18.409  1.00 31.63           C  
ATOM   4076  N   ASP B  86       1.276  -2.085  19.870  1.00 30.04           N  
ATOM   4077  CA  ASP B  86       1.938  -0.787  19.750  1.00 30.49           C  
ATOM   4078  C   ASP B  86       2.638  -0.378  21.034  1.00 29.36           C  
ATOM   4079  O   ASP B  86       3.771   0.068  20.989  1.00 28.66           O  
ATOM   4080  CB  ASP B  86       0.971   0.299  19.274  1.00 31.05           C  
ATOM   4081  CG  ASP B  86       0.370  -0.017  17.923  1.00 33.30           C  
ATOM   4082  OD1 ASP B  86       1.129  -0.318  16.978  1.00 36.25           O  
ATOM   4083  OD2 ASP B  86      -0.862   0.037  17.799  1.00 32.85           O  
ATOM   4084  N   THR B  87       1.979  -0.540  22.177  1.00 28.64           N  
ATOM   4085  CA  THR B  87       2.624  -0.228  23.450  1.00 27.95           C  
ATOM   4086  C   THR B  87       3.455  -1.426  23.933  1.00 29.23           C  
ATOM   4087  O   THR B  87       4.281  -1.279  24.833  1.00 28.68           O  
ATOM   4088  CB  THR B  87       1.615   0.149  24.541  1.00 28.35           C  
ATOM   4089  OG1 THR B  87       0.817  -0.993  24.834  1.00 25.98           O  
ATOM   4090  CG2 THR B  87       0.695   1.316  24.092  1.00 27.92           C  
ATOM   4091  N   LYS B  88       3.232  -2.601  23.326  1.00 27.96           N  
ATOM   4092  CA  LYS B  88       3.887  -3.856  23.730  1.00 28.62           C  
ATOM   4093  C   LYS B  88       3.474  -4.299  25.141  1.00 28.11           C  
ATOM   4094  O   LYS B  88       4.119  -5.149  25.760  1.00 27.91           O  
ATOM   4095  CB  LYS B  88       5.414  -3.744  23.581  1.00 30.01           C  
ATOM   4096  CG  LYS B  88       5.845  -3.328  22.177  1.00 32.10           C  
ATOM   4097  CD  LYS B  88       7.357  -3.246  22.017  1.00 35.37           C  
ATOM   4098  CE  LYS B  88       7.927  -2.002  22.688  1.00 38.75           C  
ATOM   4099  NZ  LYS B  88       9.418  -2.029  22.749  1.00 40.69           N  
ATOM   4100  N   LEU B  89       2.364  -3.741  25.624  1.00 25.86           N  
ATOM   4101  CA  LEU B  89       1.876  -4.013  26.978  1.00 25.78           C  
ATOM   4102  C   LEU B  89       0.764  -5.071  27.046  1.00 26.08           C  
ATOM   4103  O   LEU B  89      -0.171  -5.074  26.234  1.00 24.29           O  
ATOM   4104  CB  LEU B  89       1.373  -2.705  27.613  1.00 25.89           C  
ATOM   4105  CG  LEU B  89       2.228  -1.850  28.552  1.00 27.74           C  
ATOM   4106  CD1 LEU B  89       3.729  -1.937  28.277  1.00 27.31           C  
ATOM   4107  CD2 LEU B  89       1.732  -0.407  28.578  1.00 27.13           C  
ATOM   4108  N   VAL B  90       0.877  -5.958  28.032  1.00 25.66           N  
ATOM   4109  CA  VAL B  90      -0.190  -6.877  28.382  1.00 26.20           C  
ATOM   4110  C   VAL B  90      -0.710  -6.550  29.786  1.00 26.99           C  
ATOM   4111  O   VAL B  90       0.060  -6.250  30.695  1.00 27.39           O  
ATOM   4112  CB  VAL B  90       0.248  -8.360  28.301  1.00 26.37           C  
ATOM   4113  CG1 VAL B  90       0.708  -8.724  26.892  1.00 26.07           C  
ATOM   4114  CG2 VAL B  90       1.334  -8.674  29.323  1.00 25.62           C  
ATOM   4115  N   ASP B  91      -2.028  -6.601  29.941  1.00 27.29           N  
ATOM   4116  CA  ASP B  91      -2.691  -6.340  31.216  1.00 28.16           C  
ATOM   4117  C   ASP B  91      -3.410  -7.654  31.513  1.00 29.04           C  
ATOM   4118  O   ASP B  91      -4.310  -8.054  30.772  1.00 28.14           O  
ATOM   4119  CB  ASP B  91      -3.640  -5.141  31.052  1.00 27.44           C  
ATOM   4120  CG  ASP B  91      -4.448  -4.811  32.309  1.00 29.19           C  
ATOM   4121  OD1 ASP B  91      -4.295  -5.464  33.361  1.00 26.62           O  
ATOM   4122  OD2 ASP B  91      -5.270  -3.875  32.212  1.00 29.64           O  
ATOM   4123  N   ILE B  92      -2.949  -8.364  32.542  1.00 28.79           N  
ATOM   4124  CA  ILE B  92      -3.491  -9.683  32.868  1.00 30.32           C  
ATOM   4125  C   ILE B  92      -3.625  -9.876  34.373  1.00 31.45           C  
ATOM   4126  O   ILE B  92      -2.884  -9.264  35.143  1.00 32.58           O  
ATOM   4127  CB  ILE B  92      -2.616 -10.848  32.303  1.00 31.83           C  
ATOM   4128  CG1 ILE B  92      -1.323 -11.061  33.123  1.00 30.56           C  
ATOM   4129  CG2 ILE B  92      -2.358 -10.694  30.805  1.00 31.46           C  
ATOM   4130  CD1 ILE B  92      -0.235 -10.024  32.920  1.00 30.90           C  
ATOM   4131  N   ASP B  93      -4.566 -10.732  34.778  1.00 32.90           N  
ATOM   4132  CA  ASP B  93      -4.702 -11.163  36.167  1.00 33.87           C  
ATOM   4133  C   ASP B  93      -3.523 -12.036  36.575  1.00 34.34           C  
ATOM   4134  O   ASP B  93      -2.989 -12.791  35.750  1.00 30.56           O  
ATOM   4135  CB  ASP B  93      -5.965 -12.008  36.346  1.00 36.29           C  
ATOM   4136  CG  ASP B  93      -7.237 -11.222  36.187  1.00 36.56           C  
ATOM   4137  OD1 ASP B  93      -7.220  -9.970  36.258  1.00 39.12           O  
ATOM   4138  OD2 ASP B  93      -8.271 -11.886  36.003  1.00 39.00           O  
ATOM   4139  N   ALA B  94      -3.155 -11.966  37.859  1.00 34.56           N  
ATOM   4140  CA  ALA B  94      -1.986 -12.687  38.375  1.00 33.44           C  
ATOM   4141  C   ALA B  94      -2.072 -14.193  38.181  1.00 33.27           C  
ATOM   4142  O   ALA B  94      -1.048 -14.891  38.191  1.00 33.46           O  
ATOM   4143  CB  ALA B  94      -1.752 -12.350  39.840  1.00 34.47           C  
ATOM   4144  N   GLY B  95      -3.289 -14.696  37.993  1.00 32.06           N  
ATOM   4145  CA  GLY B  95      -3.500 -16.126  37.831  1.00 31.84           C  
ATOM   4146  C   GLY B  95      -3.261 -16.634  36.420  1.00 31.45           C  
ATOM   4147  O   GLY B  95      -3.218 -17.838  36.198  1.00 32.60           O  
ATOM   4148  N   VAL B  96      -3.113 -15.724  35.460  1.00 30.37           N  
ATOM   4149  CA  VAL B  96      -2.781 -16.119  34.085  1.00 28.88           C  
ATOM   4150  C   VAL B  96      -1.437 -16.840  34.132  1.00 28.53           C  
ATOM   4151  O   VAL B  96      -0.539 -16.440  34.879  1.00 26.75           O  
ATOM   4152  CB  VAL B  96      -2.699 -14.893  33.139  1.00 29.22           C  
ATOM   4153  CG1 VAL B  96      -2.106 -15.263  31.780  1.00 26.69           C  
ATOM   4154  CG2 VAL B  96      -4.073 -14.251  32.964  1.00 27.98           C  
ATOM   4155  N   ASN B  97      -1.311 -17.917  33.362  1.00 29.18           N  
ATOM   4156  CA  ASN B  97      -0.040 -18.621  33.281  1.00 28.26           C  
ATOM   4157  C   ASN B  97       0.749 -18.263  32.016  1.00 29.29           C  
ATOM   4158  O   ASN B  97       0.186 -17.717  31.053  1.00 28.20           O  
ATOM   4159  CB  ASN B  97      -0.214 -20.145  33.486  1.00 28.68           C  
ATOM   4160  CG  ASN B  97      -0.791 -20.852  32.269  1.00 29.61           C  
ATOM   4161  OD1 ASN B  97      -0.133 -20.970  31.240  1.00 30.01           O  
ATOM   4162  ND2 ASN B  97      -2.016 -21.356  32.395  1.00 29.09           N  
ATOM   4163  N   LEU B  98       2.050 -18.574  32.032  1.00 27.34           N  
ATOM   4164  CA  LEU B  98       2.972 -18.122  30.989  1.00 27.10           C  
ATOM   4165  C   LEU B  98       2.752 -18.805  29.651  1.00 26.90           C  
ATOM   4166  O   LEU B  98       3.007 -18.209  28.611  1.00 25.62           O  
ATOM   4167  CB  LEU B  98       4.439 -18.270  31.436  1.00 26.96           C  
ATOM   4168  CG  LEU B  98       4.902 -17.402  32.619  1.00 26.93           C  
ATOM   4169  CD1 LEU B  98       6.418 -17.460  32.773  1.00 27.37           C  
ATOM   4170  CD2 LEU B  98       4.443 -15.958  32.480  1.00 27.88           C  
ATOM   4171  N   ASP B  99       2.299 -20.056  29.679  1.00 27.46           N  
ATOM   4172  CA  ASP B  99       1.908 -20.751  28.452  1.00 29.71           C  
ATOM   4173  C   ASP B  99       0.692 -20.081  27.804  1.00 27.85           C  
ATOM   4174  O   ASP B  99       0.700 -19.786  26.612  1.00 25.62           O  
ATOM   4175  CB  ASP B  99       1.621 -22.236  28.721  1.00 32.99           C  
ATOM   4176  CG  ASP B  99       1.546 -23.053  27.441  1.00 36.37           C  
ATOM   4177  OD1 ASP B  99       2.572 -23.163  26.740  1.00 39.88           O  
ATOM   4178  OD2 ASP B  99       0.462 -23.578  27.123  1.00 38.88           O  
ATOM   4179  N   GLN B 100      -0.347 -19.850  28.608  1.00 28.84           N  
ATOM   4180  CA  GLN B 100      -1.549 -19.125  28.178  1.00 29.60           C  
ATOM   4181  C   GLN B 100      -1.179 -17.746  27.621  1.00 29.26           C  
ATOM   4182  O   GLN B 100      -1.677 -17.349  26.563  1.00 30.09           O  
ATOM   4183  CB  GLN B 100      -2.521 -18.998  29.359  1.00 30.40           C  
ATOM   4184  CG  GLN B 100      -3.820 -18.241  29.100  1.00 31.98           C  
ATOM   4185  CD  GLN B 100      -4.496 -17.830  30.397  1.00 32.55           C  
ATOM   4186  OE1 GLN B 100      -4.020 -18.171  31.485  1.00 33.20           O  
ATOM   4187  NE2 GLN B 100      -5.602 -17.101  30.296  1.00 32.29           N  
ATOM   4188  N   LEU B 101      -0.282 -17.037  28.316  1.00 27.38           N  
ATOM   4189  CA  LEU B 101       0.135 -15.708  27.887  1.00 26.32           C  
ATOM   4190  C   LEU B 101       0.923 -15.742  26.565  1.00 26.28           C  
ATOM   4191  O   LEU B 101       0.631 -14.969  25.647  1.00 25.36           O  
ATOM   4192  CB  LEU B 101       0.929 -14.977  28.984  1.00 24.79           C  
ATOM   4193  CG  LEU B 101       1.435 -13.556  28.664  1.00 25.36           C  
ATOM   4194  CD1 LEU B 101       0.339 -12.649  28.115  1.00 25.38           C  
ATOM   4195  CD2 LEU B 101       2.077 -12.899  29.883  1.00 24.72           C  
ATOM   4196  N   MET B 102       1.906 -16.632  26.481  1.00 25.89           N  
ATOM   4197  CA  MET B 102       2.686 -16.810  25.248  1.00 27.46           C  
ATOM   4198  C   MET B 102       1.795 -17.016  24.022  1.00 25.79           C  
ATOM   4199  O   MET B 102       1.922 -16.310  23.036  1.00 25.05           O  
ATOM   4200  CB  MET B 102       3.656 -17.986  25.375  1.00 29.50           C  
ATOM   4201  CG  MET B 102       4.262 -18.378  24.038  1.00 33.31           C  
ATOM   4202  SD  MET B 102       5.291 -19.835  24.142  1.00 41.89           S  
ATOM   4203  CE  MET B 102       4.057 -21.135  24.085  1.00 40.67           C  
ATOM   4204  N   LYS B 103       0.889 -17.984  24.103  1.00 26.84           N  
ATOM   4205  CA  LYS B 103      -0.030 -18.279  23.005  1.00 27.46           C  
ATOM   4206  C   LYS B 103      -0.916 -17.092  22.638  1.00 26.18           C  
ATOM   4207  O   LYS B 103      -1.119 -16.820  21.470  1.00 26.76           O  
ATOM   4208  CB  LYS B 103      -0.847 -19.541  23.313  1.00 29.24           C  
ATOM   4209  CG  LYS B 103       0.069 -20.761  23.421  1.00 33.46           C  
ATOM   4210  CD  LYS B 103      -0.654 -22.066  23.698  1.00 34.96           C  
ATOM   4211  CE  LYS B 103       0.332 -23.224  23.640  1.00 36.38           C  
ATOM   4212  NZ  LYS B 103      -0.069 -24.324  24.571  1.00 39.90           N  
ATOM   4213  N   ALA B 104      -1.409 -16.369  23.636  1.00 26.14           N  
ATOM   4214  CA  ALA B 104      -2.270 -15.216  23.384  1.00 25.91           C  
ATOM   4215  C   ALA B 104      -1.517 -14.043  22.773  1.00 25.65           C  
ATOM   4216  O   ALA B 104      -2.068 -13.319  21.949  1.00 24.26           O  
ATOM   4217  CB  ALA B 104      -2.980 -14.783  24.664  1.00 26.92           C  
ATOM   4218  N   ALA B 105      -0.253 -13.879  23.162  1.00 25.64           N  
ATOM   4219  CA  ALA B 105       0.535 -12.711  22.766  1.00 26.06           C  
ATOM   4220  C   ALA B 105       1.217 -12.845  21.398  1.00 25.06           C  
ATOM   4221  O   ALA B 105       1.463 -11.844  20.728  1.00 25.05           O  
ATOM   4222  CB  ALA B 105       1.551 -12.373  23.850  1.00 25.15           C  
ATOM   4223  N   LEU B 106       1.509 -14.075  20.984  1.00 25.73           N  
ATOM   4224  CA  LEU B 106       2.178 -14.330  19.700  1.00 25.96           C  
ATOM   4225  C   LEU B 106       1.565 -13.645  18.457  1.00 26.71           C  
ATOM   4226  O   LEU B 106       2.302 -13.079  17.661  1.00 28.12           O  
ATOM   4227  CB  LEU B 106       2.379 -15.836  19.452  1.00 26.38           C  
ATOM   4228  CG  LEU B 106       3.688 -16.366  20.024  1.00 27.21           C  
ATOM   4229  CD1 LEU B 106       3.719 -17.896  20.020  1.00 28.70           C  
ATOM   4230  CD2 LEU B 106       4.880 -15.776  19.284  1.00 24.66           C  
ATOM   4231  N   PRO B 107       0.226 -13.699  18.282  1.00 27.65           N  
ATOM   4232  CA  PRO B 107      -0.383 -13.047  17.107  1.00 28.61           C  
ATOM   4233  C   PRO B 107      -0.251 -11.518  17.083  1.00 28.65           C  
ATOM   4234  O   PRO B 107      -0.640 -10.891  16.097  1.00 29.11           O  
ATOM   4235  CB  PRO B 107      -1.864 -13.442  17.221  1.00 28.81           C  
ATOM   4236  CG  PRO B 107      -1.831 -14.723  17.978  1.00 29.11           C  
ATOM   4237  CD  PRO B 107      -0.769 -14.500  19.015  1.00 27.52           C  
ATOM   4238  N   PHE B 108       0.281 -10.936  18.162  1.00 27.74           N  
ATOM   4239  CA  PHE B 108       0.577  -9.501  18.231  1.00 27.37           C  
ATOM   4240  C   PHE B 108       2.053  -9.211  17.944  1.00 27.61           C  
ATOM   4241  O   PHE B 108       2.498  -8.063  18.028  1.00 28.81           O  
ATOM   4242  CB  PHE B 108       0.221  -8.943  19.608  1.00 27.15           C  
ATOM   4243  CG  PHE B 108      -1.241  -9.069  19.966  1.00 26.80           C  
ATOM   4244  CD1 PHE B 108      -2.119  -8.014  19.747  1.00 26.51           C  
ATOM   4245  CD2 PHE B 108      -1.734 -10.238  20.529  1.00 27.38           C  
ATOM   4246  CE1 PHE B 108      -3.459  -8.129  20.081  1.00 27.49           C  
ATOM   4247  CE2 PHE B 108      -3.074 -10.357  20.867  1.00 27.37           C  
ATOM   4248  CZ  PHE B 108      -3.936  -9.306  20.641  1.00 26.85           C  
ATOM   4249  N   GLY B 109       2.824 -10.243  17.626  1.00 27.48           N  
ATOM   4250  CA  GLY B 109       4.272 -10.060  17.429  1.00 27.21           C  
ATOM   4251  C   GLY B 109       4.993  -9.767  18.739  1.00 27.07           C  
ATOM   4252  O   GLY B 109       5.980  -9.015  18.762  1.00 27.16           O  
ATOM   4253  N   LEU B 110       4.503 -10.370  19.823  1.00 25.18           N  
ATOM   4254  CA  LEU B 110       5.044 -10.172  21.171  1.00 24.56           C  
ATOM   4255  C   LEU B 110       5.490 -11.480  21.817  1.00 24.50           C  
ATOM   4256  O   LEU B 110       4.893 -12.534  21.583  1.00 24.66           O  
ATOM   4257  CB  LEU B 110       3.995  -9.504  22.069  1.00 23.79           C  
ATOM   4258  CG  LEU B 110       3.465  -8.123  21.659  1.00 23.63           C  
ATOM   4259  CD1 LEU B 110       2.375  -7.662  22.622  1.00 23.89           C  
ATOM   4260  CD2 LEU B 110       4.590  -7.105  21.612  1.00 23.40           C  
ATOM   4261  N   TRP B 111       6.509 -11.386  22.669  1.00 24.51           N  
ATOM   4262  CA  TRP B 111       7.177 -12.539  23.268  1.00 25.50           C  
ATOM   4263  C   TRP B 111       7.317 -12.323  24.760  1.00 26.19           C  
ATOM   4264  O   TRP B 111       7.692 -11.225  25.196  1.00 25.88           O  
ATOM   4265  CB  TRP B 111       8.542 -12.747  22.584  1.00 25.63           C  
ATOM   4266  CG  TRP B 111       9.185 -14.063  22.926  1.00 25.41           C  
ATOM   4267  CD1 TRP B 111      10.216 -14.291  23.822  1.00 25.99           C  
ATOM   4268  CD2 TRP B 111       8.827 -15.395  22.406  1.00 26.05           C  
ATOM   4269  NE1 TRP B 111      10.510 -15.630  23.900  1.00 26.78           N  
ATOM   4270  CE2 TRP B 111       9.715 -16.347  23.076  1.00 26.52           C  
ATOM   4271  CE3 TRP B 111       7.893 -15.872  21.491  1.00 25.86           C  
ATOM   4272  CZ2 TRP B 111       9.660 -17.712  22.823  1.00 26.55           C  
ATOM   4273  CZ3 TRP B 111       7.838 -17.249  21.253  1.00 26.56           C  
ATOM   4274  CH2 TRP B 111       8.710 -18.145  21.898  1.00 27.39           C  
ATOM   4275  N   VAL B 112       6.953 -13.335  25.562  1.00 25.23           N  
ATOM   4276  CA  VAL B 112       7.136 -13.286  27.014  1.00 25.17           C  
ATOM   4277  C   VAL B 112       8.630 -13.062  27.295  1.00 26.51           C  
ATOM   4278  O   VAL B 112       9.459 -13.896  26.918  1.00 25.56           O  
ATOM   4279  CB  VAL B 112       6.629 -14.572  27.720  1.00 25.60           C  
ATOM   4280  CG1 VAL B 112       6.863 -14.496  29.223  1.00 24.97           C  
ATOM   4281  CG2 VAL B 112       5.150 -14.805  27.442  1.00 24.23           C  
ATOM   4282  N   PRO B 113       8.971 -11.923  27.939  1.00 26.45           N  
ATOM   4283  CA  PRO B 113      10.369 -11.477  28.015  1.00 25.51           C  
ATOM   4284  C   PRO B 113      11.277 -12.352  28.874  1.00 25.86           C  
ATOM   4285  O   PRO B 113      12.484 -12.366  28.646  1.00 25.40           O  
ATOM   4286  CB  PRO B 113      10.262 -10.061  28.610  1.00 25.44           C  
ATOM   4287  CG  PRO B 113       8.969 -10.068  29.365  1.00 24.68           C  
ATOM   4288  CD  PRO B 113       8.047 -10.945  28.558  1.00 24.31           C  
ATOM   4289  N   VAL B 114      10.707 -13.085  29.830  1.00 24.39           N  
ATOM   4290  CA  VAL B 114      11.468 -14.046  30.620  1.00 24.77           C  
ATOM   4291  C   VAL B 114      10.657 -15.329  30.753  1.00 26.69           C  
ATOM   4292  O   VAL B 114       9.562 -15.333  31.337  1.00 27.74           O  
ATOM   4293  CB  VAL B 114      11.842 -13.495  32.028  1.00 22.88           C  
ATOM   4294  CG1 VAL B 114      12.409 -14.596  32.917  1.00 21.95           C  
ATOM   4295  CG2 VAL B 114      12.825 -12.340  31.934  1.00 22.47           C  
ATOM   4296  N   LEU B 115      11.186 -16.414  30.201  1.00 28.47           N  
ATOM   4297  CA  LEU B 115      10.559 -17.722  30.324  1.00 30.79           C  
ATOM   4298  C   LEU B 115      11.452 -18.687  31.103  1.00 32.31           C  
ATOM   4299  O   LEU B 115      12.641 -18.808  30.800  1.00 33.15           O  
ATOM   4300  CB  LEU B 115      10.230 -18.284  28.936  1.00 31.68           C  
ATOM   4301  CG  LEU B 115       9.016 -17.651  28.254  1.00 31.46           C  
ATOM   4302  CD1 LEU B 115       9.047 -17.849  26.746  1.00 30.15           C  
ATOM   4303  CD2 LEU B 115       7.722 -18.205  28.847  1.00 31.15           C  
ATOM   4304  N   PRO B 116      10.889 -19.372  32.116  1.00 32.01           N  
ATOM   4305  CA  PRO B 116      11.671 -20.339  32.875  1.00 31.50           C  
ATOM   4306  C   PRO B 116      11.676 -21.695  32.150  1.00 34.42           C  
ATOM   4307  O   PRO B 116      11.119 -21.801  31.054  1.00 35.18           O  
ATOM   4308  CB  PRO B 116      10.908 -20.424  34.196  1.00 30.97           C  
ATOM   4309  CG  PRO B 116       9.481 -20.165  33.818  1.00 31.14           C  
ATOM   4310  CD  PRO B 116       9.472 -19.379  32.527  1.00 30.21           C  
ATOM   4311  N   GLY B 117      12.289 -22.715  32.750  1.00 35.75           N  
ATOM   4312  CA  GLY B 117      12.361 -24.053  32.132  1.00 37.23           C  
ATOM   4313  C   GLY B 117      11.039 -24.809  32.004  1.00 39.89           C  
ATOM   4314  O   GLY B 117      11.014 -25.933  31.508  1.00 43.04           O  
ATOM   4315  N   THR B 118       9.950 -24.204  32.475  1.00 39.58           N  
ATOM   4316  CA  THR B 118       8.597 -24.746  32.332  1.00 39.63           C  
ATOM   4317  C   THR B 118       7.644 -23.570  32.148  1.00 39.54           C  
ATOM   4318  O   THR B 118       7.854 -22.516  32.738  1.00 38.68           O  
ATOM   4319  CB  THR B 118       8.161 -25.590  33.556  1.00 41.02           C  
ATOM   4320  OG1 THR B 118       6.848 -26.115  33.331  1.00 43.99           O  
ATOM   4321  CG2 THR B 118       8.124 -24.756  34.843  1.00 40.88           C  
ATOM   4322  N   ARG B 119       6.607 -23.735  31.332  1.00 39.50           N  
ATOM   4323  CA  ARG B 119       5.669 -22.635  31.088  1.00 39.16           C  
ATOM   4324  C   ARG B 119       4.454 -22.699  32.005  1.00 39.09           C  
ATOM   4325  O   ARG B 119       3.613 -21.786  32.003  1.00 37.46           O  
ATOM   4326  CB  ARG B 119       5.232 -22.592  29.621  1.00 42.34           C  
ATOM   4327  CG  ARG B 119       6.348 -22.254  28.634  1.00 44.51           C  
ATOM   4328  CD  ARG B 119       5.816 -22.049  27.220  1.00 46.00           C  
ATOM   4329  NE  ARG B 119       5.050 -23.201  26.740  1.00 47.98           N  
ATOM   4330  CZ  ARG B 119       5.536 -24.177  25.972  1.00 49.89           C  
ATOM   4331  NH1 ARG B 119       6.801 -24.153  25.567  1.00 49.88           N  
ATOM   4332  NH2 ARG B 119       4.749 -25.176  25.598  1.00 48.54           N  
ATOM   4333  N   GLN B 120       4.352 -23.772  32.789  1.00 36.62           N  
ATOM   4334  CA  GLN B 120       3.256 -23.889  33.749  1.00 37.78           C  
ATOM   4335  C   GLN B 120       3.564 -23.126  35.049  1.00 36.01           C  
ATOM   4336  O   GLN B 120       3.741 -23.718  36.121  1.00 37.32           O  
ATOM   4337  CB  GLN B 120       2.884 -25.361  33.997  1.00 40.17           C  
ATOM   4338  CG  GLN B 120       2.283 -26.054  32.776  1.00 42.71           C  
ATOM   4339  CD  GLN B 120       0.912 -25.510  32.400  1.00 47.25           C  
ATOM   4340  OE1 GLN B 120       0.017 -25.399  33.245  1.00 50.30           O  
ATOM   4341  NE2 GLN B 120       0.737 -25.174  31.124  1.00 48.24           N  
ATOM   4342  N   VAL B 121       3.617 -21.800  34.920  1.00 34.06           N  
ATOM   4343  CA  VAL B 121       3.917 -20.871  36.010  1.00 32.95           C  
ATOM   4344  C   VAL B 121       2.963 -19.677  35.878  1.00 33.07           C  
ATOM   4345  O   VAL B 121       2.736 -19.201  34.767  1.00 32.93           O  
ATOM   4346  CB  VAL B 121       5.390 -20.402  35.921  1.00 32.74           C  
ATOM   4347  CG1 VAL B 121       5.648 -19.186  36.792  1.00 34.50           C  
ATOM   4348  CG2 VAL B 121       6.349 -21.534  36.289  1.00 32.63           C  
ATOM   4349  N   THR B 122       2.401 -19.201  36.994  1.00 33.66           N  
ATOM   4350  CA  THR B 122       1.505 -18.038  36.962  1.00 31.99           C  
ATOM   4351  C   THR B 122       2.321 -16.745  36.919  1.00 31.85           C  
ATOM   4352  O   THR B 122       3.493 -16.736  37.299  1.00 32.56           O  
ATOM   4353  CB  THR B 122       0.517 -17.996  38.158  1.00 33.44           C  
ATOM   4354  OG1 THR B 122       1.230 -17.764  39.378  1.00 33.72           O  
ATOM   4355  CG2 THR B 122      -0.296 -19.300  38.274  1.00 31.74           C  
ATOM   4356  N   VAL B 123       1.706 -15.667  36.438  1.00 29.02           N  
ATOM   4357  CA  VAL B 123       2.318 -14.336  36.464  1.00 28.01           C  
ATOM   4358  C   VAL B 123       2.626 -13.937  37.920  1.00 28.26           C  
ATOM   4359  O   VAL B 123       3.678 -13.368  38.211  1.00 27.32           O  
ATOM   4360  CB  VAL B 123       1.398 -13.280  35.809  1.00 26.40           C  
ATOM   4361  CG1 VAL B 123       1.938 -11.875  36.026  1.00 25.51           C  
ATOM   4362  CG2 VAL B 123       1.199 -13.573  34.323  1.00 26.71           C  
ATOM   4363  N   GLY B 124       1.696 -14.246  38.822  1.00 27.78           N  
ATOM   4364  CA  GLY B 124       1.889 -14.046  40.264  1.00 28.68           C  
ATOM   4365  C   GLY B 124       3.117 -14.750  40.827  1.00 28.51           C  
ATOM   4366  O   GLY B 124       3.909 -14.135  41.526  1.00 29.77           O  
ATOM   4367  N   GLY B 125       3.274 -16.034  40.511  1.00 28.76           N  
ATOM   4368  CA  GLY B 125       4.468 -16.800  40.882  1.00 28.58           C  
ATOM   4369  C   GLY B 125       5.751 -16.319  40.218  1.00 29.61           C  
ATOM   4370  O   GLY B 125       6.816 -16.334  40.827  1.00 29.06           O  
ATOM   4371  N   ALA B 126       5.637 -15.909  38.955  1.00 28.11           N  
ATOM   4372  CA  ALA B 126       6.737 -15.353  38.193  1.00 27.14           C  
ATOM   4373  C   ALA B 126       7.310 -14.090  38.848  1.00 27.75           C  
ATOM   4374  O   ALA B 126       8.531 -13.910  38.913  1.00 27.11           O  
ATOM   4375  CB  ALA B 126       6.256 -15.038  36.788  1.00 27.96           C  
ATOM   4376  N   ILE B 127       6.414 -13.221  39.322  1.00 27.95           N  
ATOM   4377  CA  ILE B 127       6.788 -11.980  39.995  1.00 27.43           C  
ATOM   4378  C   ILE B 127       7.311 -12.242  41.406  1.00 27.70           C  
ATOM   4379  O   ILE B 127       8.379 -11.746  41.776  1.00 25.85           O  
ATOM   4380  CB  ILE B 127       5.610 -10.971  40.038  1.00 27.71           C  
ATOM   4381  CG1 ILE B 127       5.226 -10.551  38.614  1.00 28.04           C  
ATOM   4382  CG2 ILE B 127       5.985  -9.742  40.856  1.00 27.66           C  
ATOM   4383  CD1 ILE B 127       3.973  -9.699  38.511  1.00 27.92           C  
ATOM   4384  N   ALA B 128       6.567 -13.039  42.176  1.00 27.68           N  
ATOM   4385  CA  ALA B 128       6.907 -13.311  43.573  1.00 28.33           C  
ATOM   4386  C   ALA B 128       8.228 -14.059  43.771  1.00 28.98           C  
ATOM   4387  O   ALA B 128       8.825 -13.977  44.842  1.00 29.42           O  
ATOM   4388  CB  ALA B 128       5.772 -14.052  44.264  1.00 27.56           C  
ATOM   4389  N   CYS B 129       8.654 -14.810  42.756  1.00 27.50           N  
ATOM   4390  CA  CYS B 129       9.947 -15.485  42.792  1.00 28.33           C  
ATOM   4391  C   CYS B 129      10.955 -14.779  41.895  1.00 27.44           C  
ATOM   4392  O   CYS B 129      12.096 -15.212  41.802  1.00 28.18           O  
ATOM   4393  CB  CYS B 129       9.826 -16.964  42.411  1.00 28.76           C  
ATOM   4394  SG  CYS B 129       9.179 -17.995  43.757  1.00 30.81           S  
ATOM   4395  N   ASP B 130      10.524 -13.681  41.268  1.00 26.47           N  
ATOM   4396  CA  ASP B 130      11.356 -12.912  40.341  1.00 25.56           C  
ATOM   4397  C   ASP B 130      12.130 -13.890  39.459  1.00 25.25           C  
ATOM   4398  O   ASP B 130      13.358 -13.931  39.498  1.00 27.33           O  
ATOM   4399  CB  ASP B 130      12.310 -11.998  41.112  1.00 24.38           C  
ATOM   4400  CG  ASP B 130      12.991 -10.963  40.221  1.00 23.61           C  
ATOM   4401  OD1 ASP B 130      12.540 -10.733  39.072  1.00 23.05           O  
ATOM   4402  OD2 ASP B 130      13.971 -10.366  40.691  1.00 22.88           O  
ATOM   4403  N   ILE B 131      11.401 -14.685  38.683  1.00 24.34           N  
ATOM   4404  CA  ILE B 131      11.993 -15.841  37.997  1.00 24.43           C  
ATOM   4405  C   ILE B 131      12.970 -15.400  36.905  1.00 23.85           C  
ATOM   4406  O   ILE B 131      12.870 -14.290  36.376  1.00 23.62           O  
ATOM   4407  CB  ILE B 131      10.923 -16.815  37.439  1.00 23.64           C  
ATOM   4408  CG1 ILE B 131      10.026 -16.118  36.407  1.00 23.33           C  
ATOM   4409  CG2 ILE B 131      10.077 -17.394  38.577  1.00 23.78           C  
ATOM   4410  CD1 ILE B 131       9.205 -17.078  35.563  1.00 22.89           C  
ATOM   4411  N   HIS B 132      13.927 -16.272  36.606  1.00 25.06           N  
ATOM   4412  CA  HIS B 132      14.941 -16.019  35.603  1.00 25.23           C  
ATOM   4413  C   HIS B 132      14.850 -17.078  34.553  1.00 25.68           C  
ATOM   4414  O   HIS B 132      14.120 -18.061  34.708  1.00 25.21           O  
ATOM   4415  CB  HIS B 132      16.330 -16.027  36.225  1.00 25.84           C  
ATOM   4416  CG  HIS B 132      16.632 -17.270  37.038  1.00 26.90           C  
ATOM   4417  ND1 HIS B 132      17.178 -18.388  36.495  1.00 28.52           N  
ATOM   4418  CD2 HIS B 132      16.460 -17.534  38.382  1.00 24.86           C  
ATOM   4419  CE1 HIS B 132      17.324 -19.319  37.453  1.00 26.14           C  
ATOM   4420  NE2 HIS B 132      16.888 -18.795  38.606  1.00 28.26           N  
ATOM   4421  N   GLY B 133      15.584 -16.891  33.465  1.00 24.20           N  
ATOM   4422  CA  GLY B 133      15.546 -17.850  32.382  1.00 25.17           C  
ATOM   4423  C   GLY B 133      16.843 -17.852  31.614  1.00 25.84           C  
ATOM   4424  O   GLY B 133      17.819 -17.229  32.025  1.00 23.70           O  
ATOM   4425  N   LYS B 134      16.807 -18.534  30.476  1.00 26.52           N  
ATOM   4426  CA  LYS B 134      17.955 -18.759  29.609  1.00 26.89           C  
ATOM   4427  C   LYS B 134      18.504 -17.434  29.050  1.00 25.40           C  
ATOM   4428  O   LYS B 134      19.660 -17.345  28.635  1.00 24.55           O  
ATOM   4429  CB  LYS B 134      17.504 -19.713  28.495  1.00 29.36           C  
ATOM   4430  CG  LYS B 134      18.605 -20.457  27.766  1.00 30.36           C  
ATOM   4431  CD  LYS B 134      18.014 -21.432  26.754  1.00 32.28           C  
ATOM   4432  CE  LYS B 134      19.087 -21.996  25.813  1.00 32.93           C  
ATOM   4433  NZ  LYS B 134      18.468 -22.946  24.839  1.00 34.91           N  
ATOM   4434  N   ASN B 135      17.674 -16.396  29.073  1.00 24.18           N  
ATOM   4435  CA  ASN B 135      18.063 -15.076  28.589  1.00 24.00           C  
ATOM   4436  C   ASN B 135      18.408 -14.060  29.690  1.00 24.94           C  
ATOM   4437  O   ASN B 135      18.469 -12.847  29.425  1.00 25.30           O  
ATOM   4438  CB  ASN B 135      16.981 -14.500  27.667  1.00 23.28           C  
ATOM   4439  CG  ASN B 135      15.691 -14.215  28.407  1.00 23.79           C  
ATOM   4440  OD1 ASN B 135      15.519 -14.653  29.540  1.00 23.00           O  
ATOM   4441  ND2 ASN B 135      14.789 -13.497  27.772  1.00 22.07           N  
ATOM   4442  N   HIS B 136      18.652 -14.537  30.911  1.00 24.14           N  
ATOM   4443  CA  HIS B 136      18.935 -13.609  32.017  1.00 24.85           C  
ATOM   4444  C   HIS B 136      20.045 -12.623  31.746  1.00 26.44           C  
ATOM   4445  O   HIS B 136      19.943 -11.450  32.112  1.00 25.70           O  
ATOM   4446  CB  HIS B 136      19.226 -14.323  33.329  1.00 23.70           C  
ATOM   4447  CG  HIS B 136      19.404 -13.365  34.481  1.00 24.86           C  
ATOM   4448  ND1 HIS B 136      20.604 -12.837  34.808  1.00 24.79           N  
ATOM   4449  CD2 HIS B 136      18.467 -12.782  35.336  1.00 23.87           C  
ATOM   4450  CE1 HIS B 136      20.442 -11.982  35.836  1.00 25.95           C  
ATOM   4451  NE2 HIS B 136      19.130 -11.948  36.152  1.00 23.55           N  
ATOM   4452  N   HIS B 137      21.122 -13.085  31.118  1.00 26.87           N  
ATOM   4453  CA  HIS B 137      22.289 -12.231  30.892  1.00 28.45           C  
ATOM   4454  C   HIS B 137      22.025 -11.094  29.944  1.00 28.98           C  
ATOM   4455  O   HIS B 137      22.765 -10.113  29.933  1.00 30.52           O  
ATOM   4456  CB  HIS B 137      23.463 -13.061  30.386  1.00 27.69           C  
ATOM   4457  CG  HIS B 137      23.254 -13.622  29.009  1.00 28.33           C  
ATOM   4458  ND1 HIS B 137      22.411 -14.636  28.765  1.00 29.23           N  
ATOM   4459  CD2 HIS B 137      23.825 -13.280  27.785  1.00 29.13           C  
ATOM   4460  CE1 HIS B 137      22.419 -14.925  27.451  1.00 28.83           C  
ATOM   4461  NE2 HIS B 137      23.294 -14.096  26.852  1.00 30.23           N  
ATOM   4462  N   SER B 138      20.991 -11.223  29.115  1.00 29.22           N  
ATOM   4463  CA  SER B 138      20.610 -10.136  28.212  1.00 29.60           C  
ATOM   4464  C   SER B 138      19.299  -9.447  28.606  1.00 28.61           C  
ATOM   4465  O   SER B 138      19.042  -8.340  28.172  1.00 29.79           O  
ATOM   4466  CB  SER B 138      20.521 -10.632  26.763  1.00 29.82           C  
ATOM   4467  OG  SER B 138      19.449 -11.550  26.596  1.00 30.39           O  
ATOM   4468  N   ALA B 139      18.476 -10.087  29.430  1.00 28.72           N  
ATOM   4469  CA  ALA B 139      17.142  -9.553  29.693  1.00 28.83           C  
ATOM   4470  C   ALA B 139      16.803  -9.313  31.169  1.00 28.94           C  
ATOM   4471  O   ALA B 139      15.752  -8.745  31.467  1.00 29.43           O  
ATOM   4472  CB  ALA B 139      16.086 -10.444  29.040  1.00 28.69           C  
ATOM   4473  N   GLY B 140      17.679  -9.748  32.079  1.00 28.08           N  
ATOM   4474  CA  GLY B 140      17.400  -9.715  33.515  1.00 26.67           C  
ATOM   4475  C   GLY B 140      16.316 -10.716  33.893  1.00 26.27           C  
ATOM   4476  O   GLY B 140      16.027 -11.651  33.139  1.00 26.59           O  
ATOM   4477  N   SER B 141      15.708 -10.527  35.057  1.00 24.67           N  
ATOM   4478  CA  SER B 141      14.668 -11.451  35.509  1.00 24.44           C  
ATOM   4479  C   SER B 141      13.274 -10.884  35.248  1.00 23.66           C  
ATOM   4480  O   SER B 141      13.134  -9.802  34.688  1.00 23.75           O  
ATOM   4481  CB  SER B 141      14.887 -11.874  36.975  1.00 23.74           C  
ATOM   4482  OG  SER B 141      14.853 -10.774  37.869  1.00 23.87           O  
ATOM   4483  N   PHE B 142      12.245 -11.630  35.636  1.00 23.87           N  
ATOM   4484  CA  PHE B 142      10.872 -11.278  35.330  1.00 24.07           C  
ATOM   4485  C   PHE B 142      10.478  -9.897  35.870  1.00 25.14           C  
ATOM   4486  O   PHE B 142       9.786  -9.138  35.189  1.00 25.75           O  
ATOM   4487  CB  PHE B 142       9.929 -12.353  35.873  1.00 24.03           C  
ATOM   4488  CG  PHE B 142       8.598 -12.376  35.195  1.00 24.37           C  
ATOM   4489  CD1 PHE B 142       8.410 -13.128  34.039  1.00 24.09           C  
ATOM   4490  CD2 PHE B 142       7.518 -11.642  35.714  1.00 23.57           C  
ATOM   4491  CE1 PHE B 142       7.176 -13.164  33.402  1.00 24.49           C  
ATOM   4492  CE2 PHE B 142       6.291 -11.662  35.075  1.00 23.62           C  
ATOM   4493  CZ  PHE B 142       6.112 -12.421  33.922  1.00 24.34           C  
ATOM   4494  N   GLY B 143      10.940  -9.580  37.081  1.00 24.97           N  
ATOM   4495  CA  GLY B 143      10.667  -8.301  37.726  1.00 24.90           C  
ATOM   4496  C   GLY B 143      11.044  -7.087  36.902  1.00 25.51           C  
ATOM   4497  O   GLY B 143      10.358  -6.073  36.983  1.00 26.47           O  
ATOM   4498  N   ASN B 144      12.120  -7.198  36.105  1.00 24.45           N  
ATOM   4499  CA  ASN B 144      12.595  -6.119  35.221  1.00 25.10           C  
ATOM   4500  C   ASN B 144      11.582  -5.645  34.182  1.00 24.05           C  
ATOM   4501  O   ASN B 144      11.753  -4.570  33.603  1.00 23.94           O  
ATOM   4502  CB  ASN B 144      13.875  -6.531  34.442  1.00 26.14           C  
ATOM   4503  CG  ASN B 144      15.090  -6.793  35.333  1.00 26.70           C  
ATOM   4504  OD1 ASN B 144      16.186  -6.314  35.042  1.00 29.15           O  
ATOM   4505  ND2 ASN B 144      14.925  -7.593  36.370  1.00 25.28           N  
ATOM   4506  N   HIS B 145      10.555  -6.453  33.922  1.00 22.25           N  
ATOM   4507  CA  HIS B 145       9.644  -6.221  32.802  1.00 22.22           C  
ATOM   4508  C   HIS B 145       8.253  -5.845  33.262  1.00 23.24           C  
ATOM   4509  O   HIS B 145       7.361  -5.598  32.454  1.00 22.83           O  
ATOM   4510  CB  HIS B 145       9.623  -7.466  31.916  1.00 22.39           C  
ATOM   4511  CG  HIS B 145      11.004  -7.854  31.418  1.00 21.67           C  
ATOM   4512  ND1 HIS B 145      11.613  -7.204  30.399  1.00 22.93           N  
ATOM   4513  CD2 HIS B 145      11.914  -8.791  31.884  1.00 22.36           C  
ATOM   4514  CE1 HIS B 145      12.850  -7.714  30.208  1.00 21.34           C  
ATOM   4515  NE2 HIS B 145      13.039  -8.688  31.108  1.00 22.20           N  
ATOM   4516  N   VAL B 146       8.058  -5.815  34.570  1.00 23.54           N  
ATOM   4517  CA  VAL B 146       6.745  -5.499  35.128  1.00 25.85           C  
ATOM   4518  C   VAL B 146       6.632  -3.988  35.179  1.00 27.44           C  
ATOM   4519  O   VAL B 146       7.517  -3.320  35.723  1.00 29.14           O  
ATOM   4520  CB  VAL B 146       6.559  -6.117  36.521  1.00 25.49           C  
ATOM   4521  CG1 VAL B 146       5.207  -5.720  37.113  1.00 25.57           C  
ATOM   4522  CG2 VAL B 146       6.691  -7.635  36.454  1.00 24.27           C  
ATOM   4523  N   ARG B 147       5.572  -3.451  34.576  1.00 29.02           N  
ATOM   4524  CA  ARG B 147       5.397  -1.999  34.487  1.00 30.69           C  
ATOM   4525  C   ARG B 147       4.444  -1.478  35.558  1.00 31.00           C  
ATOM   4526  O   ARG B 147       4.513  -0.316  35.955  1.00 32.23           O  
ATOM   4527  CB  ARG B 147       4.947  -1.590  33.082  1.00 31.65           C  
ATOM   4528  CG  ARG B 147       5.978  -1.910  31.994  1.00 32.38           C  
ATOM   4529  CD  ARG B 147       7.286  -1.152  32.192  1.00 33.33           C  
ATOM   4530  NE  ARG B 147       8.373  -1.675  31.353  1.00 33.54           N  
ATOM   4531  CZ  ARG B 147       9.417  -2.385  31.796  1.00 33.18           C  
ATOM   4532  NH1 ARG B 147       9.545  -2.684  33.088  1.00 29.10           N  
ATOM   4533  NH2 ARG B 147      10.349  -2.795  30.935  1.00 31.93           N  
ATOM   4534  N   SER B 148       3.564  -2.351  36.022  1.00 30.52           N  
ATOM   4535  CA  SER B 148       2.716  -2.051  37.169  1.00 31.32           C  
ATOM   4536  C   SER B 148       2.169  -3.349  37.716  1.00 31.94           C  
ATOM   4537  O   SER B 148       2.102  -4.360  37.007  1.00 31.63           O  
ATOM   4538  CB  SER B 148       1.556  -1.133  36.771  1.00 31.72           C  
ATOM   4539  OG  SER B 148       0.588  -1.855  36.027  1.00 31.53           O  
ATOM   4540  N   MET B 149       1.799  -3.331  38.992  1.00 32.37           N  
ATOM   4541  CA  MET B 149       0.982  -4.392  39.550  1.00 32.59           C  
ATOM   4542  C   MET B 149       0.037  -3.845  40.615  1.00 34.04           C  
ATOM   4543  O   MET B 149       0.333  -2.850  41.289  1.00 33.95           O  
ATOM   4544  CB  MET B 149       1.813  -5.577  40.075  1.00 31.25           C  
ATOM   4545  CG  MET B 149       3.008  -5.205  40.928  1.00 33.75           C  
ATOM   4546  SD  MET B 149       3.923  -6.659  41.509  1.00 36.35           S  
ATOM   4547  CE  MET B 149       5.496  -5.918  41.919  1.00 34.31           C  
ATOM   4548  N   ASP B 150      -1.111  -4.493  40.735  1.00 35.82           N  
ATOM   4549  CA  ASP B 150      -2.085  -4.148  41.755  1.00 37.35           C  
ATOM   4550  C   ASP B 150      -1.930  -5.158  42.875  1.00 37.12           C  
ATOM   4551  O   ASP B 150      -2.089  -6.351  42.655  1.00 35.89           O  
ATOM   4552  CB  ASP B 150      -3.498  -4.215  41.181  1.00 39.08           C  
ATOM   4553  CG  ASP B 150      -3.702  -3.268  40.015  1.00 42.74           C  
ATOM   4554  OD1 ASP B 150      -3.028  -2.213  39.947  1.00 43.89           O  
ATOM   4555  OD2 ASP B 150      -4.553  -3.585  39.162  1.00 46.41           O  
ATOM   4556  N   LEU B 151      -1.617  -4.667  44.071  1.00 38.64           N  
ATOM   4557  CA  LEU B 151      -1.347  -5.528  45.222  1.00 38.58           C  
ATOM   4558  C   LEU B 151      -2.405  -5.360  46.310  1.00 39.21           C  
ATOM   4559  O   LEU B 151      -2.573  -4.260  46.858  1.00 38.56           O  
ATOM   4560  CB  LEU B 151       0.033  -5.205  45.805  1.00 37.28           C  
ATOM   4561  CG  LEU B 151       0.437  -5.955  47.075  1.00 36.64           C  
ATOM   4562  CD1 LEU B 151       0.870  -7.368  46.728  1.00 36.33           C  
ATOM   4563  CD2 LEU B 151       1.549  -5.213  47.796  1.00 36.81           C  
ATOM   4564  N   LEU B 152      -3.102  -6.451  46.623  1.00 39.15           N  
ATOM   4565  CA  LEU B 152      -4.078  -6.462  47.718  1.00 40.88           C  
ATOM   4566  C   LEU B 152      -3.364  -6.442  49.068  1.00 42.00           C  
ATOM   4567  O   LEU B 152      -2.889  -7.473  49.553  1.00 41.82           O  
ATOM   4568  CB  LEU B 152      -5.012  -7.671  47.613  1.00 40.09           C  
ATOM   4569  CG  LEU B 152      -5.952  -8.011  48.783  1.00 41.80           C  
ATOM   4570  CD1 LEU B 152      -6.871  -6.853  49.162  1.00 40.12           C  
ATOM   4571  CD2 LEU B 152      -6.759  -9.253  48.452  1.00 39.37           C  
ATOM   4572  N   THR B 153      -3.301  -5.252  49.656  1.00 43.33           N  
ATOM   4573  CA  THR B 153      -2.601  -5.007  50.915  1.00 45.73           C  
ATOM   4574  C   THR B 153      -3.374  -5.529  52.146  1.00 47.39           C  
ATOM   4575  O   THR B 153      -4.573  -5.816  52.067  1.00 43.07           O  
ATOM   4576  CB  THR B 153      -2.228  -3.506  51.006  1.00 49.01           C  
ATOM   4577  OG1 THR B 153      -0.912  -3.319  50.471  1.00 52.03           O  
ATOM   4578  CG2 THR B 153      -2.248  -2.990  52.412  1.00 51.86           C  
ATOM   4579  N   ALA B 154      -2.663  -5.671  53.267  1.00 48.51           N  
ATOM   4580  CA  ALA B 154      -3.192  -6.254  54.509  1.00 46.82           C  
ATOM   4581  C   ALA B 154      -4.435  -5.562  55.080  1.00 47.84           C  
ATOM   4582  O   ALA B 154      -5.288  -6.218  55.675  1.00 45.27           O  
ATOM   4583  CB  ALA B 154      -2.096  -6.319  55.565  1.00 46.23           C  
ATOM   4584  N   ASP B 155      -4.527  -4.246  54.900  1.00 49.87           N  
ATOM   4585  CA  ASP B 155      -5.688  -3.481  55.359  1.00 54.12           C  
ATOM   4586  C   ASP B 155      -6.821  -3.434  54.325  1.00 55.32           C  
ATOM   4587  O   ASP B 155      -7.760  -2.651  54.458  1.00 56.51           O  
ATOM   4588  CB  ASP B 155      -5.272  -2.066  55.792  1.00 56.58           C  
ATOM   4589  CG  ASP B 155      -4.625  -1.262  54.670  1.00 58.65           C  
ATOM   4590  OD1 ASP B 155      -4.184  -0.126  54.942  1.00 60.89           O  
ATOM   4591  OD2 ASP B 155      -4.560  -1.747  53.521  1.00 57.32           O  
ATOM   4592  N   GLY B 156      -6.720  -4.272  53.297  1.00 55.58           N  
ATOM   4593  CA  GLY B 156      -7.777  -4.418  52.302  1.00 55.85           C  
ATOM   4594  C   GLY B 156      -7.715  -3.485  51.103  1.00 55.62           C  
ATOM   4595  O   GLY B 156      -8.506  -3.632  50.175  1.00 58.49           O  
ATOM   4596  N   GLU B 157      -6.794  -2.525  51.110  1.00 56.42           N  
ATOM   4597  CA  GLU B 157      -6.672  -1.601  49.979  1.00 59.13           C  
ATOM   4598  C   GLU B 157      -5.755  -2.143  48.877  1.00 60.71           C  
ATOM   4599  O   GLU B 157      -4.866  -2.964  49.135  1.00 61.43           O  
ATOM   4600  CB  GLU B 157      -6.237  -0.197  50.428  1.00 61.37           C  
ATOM   4601  CG  GLU B 157      -4.750  -0.022  50.712  1.00 61.74           C  
ATOM   4602  CD  GLU B 157      -4.243   1.366  50.348  1.00 63.87           C  
ATOM   4603  OE1 GLU B 157      -3.581   2.012  51.192  1.00 61.09           O  
ATOM   4604  OE2 GLU B 157      -4.501   1.813  49.210  1.00 64.51           O  
ATOM   4605  N   ILE B 158      -5.991  -1.680  47.650  1.00 57.71           N  
ATOM   4606  CA  ILE B 158      -5.208  -2.096  46.491  1.00 53.94           C  
ATOM   4607  C   ILE B 158      -4.202  -1.002  46.136  1.00 53.90           C  
ATOM   4608  O   ILE B 158      -4.572   0.075  45.666  1.00 54.33           O  
ATOM   4609  CB  ILE B 158      -6.105  -2.418  45.271  1.00 53.76           C  
ATOM   4610  CG1 ILE B 158      -7.297  -3.309  45.668  1.00 53.64           C  
ATOM   4611  CG2 ILE B 158      -5.287  -3.039  44.145  1.00 54.44           C  
ATOM   4612  CD1 ILE B 158      -6.958  -4.742  46.023  1.00 50.65           C  
ATOM   4613  N   ARG B 159      -2.929  -1.276  46.387  1.00 51.18           N  
ATOM   4614  CA  ARG B 159      -1.876  -0.344  46.027  1.00 51.77           C  
ATOM   4615  C   ARG B 159      -1.522  -0.564  44.560  1.00 50.52           C  
ATOM   4616  O   ARG B 159      -1.356  -1.704  44.115  1.00 51.43           O  
ATOM   4617  CB  ARG B 159      -0.644  -0.527  46.923  1.00 52.93           C  
ATOM   4618  CG  ARG B 159      -0.922  -0.544  48.425  1.00 53.48           C  
ATOM   4619  CD  ARG B 159      -0.923   0.854  49.023  1.00 52.43           C  
ATOM   4620  NE  ARG B 159       0.425   1.414  49.126  1.00 52.23           N  
ATOM   4621  CZ  ARG B 159       1.192   1.339  50.212  1.00 50.58           C  
ATOM   4622  NH1 ARG B 159       0.755   0.720  51.304  1.00 50.33           N  
ATOM   4623  NH2 ARG B 159       2.402   1.879  50.204  1.00 49.59           N  
ATOM   4624  N   HIS B 160      -1.449   0.524  43.801  1.00 48.04           N  
ATOM   4625  CA  HIS B 160      -0.989   0.450  42.428  1.00 45.03           C  
ATOM   4626  C   HIS B 160       0.483   0.687  42.449  1.00 44.47           C  
ATOM   4627  O   HIS B 160       0.941   1.812  42.661  1.00 46.55           O  
ATOM   4628  CB  HIS B 160      -1.700   1.464  41.542  1.00 44.61           C  
ATOM   4629  CG  HIS B 160      -1.452   1.257  40.067  1.00 45.22           C  
ATOM   4630  ND1 HIS B 160      -2.042   0.271  39.366  1.00 44.74           N  
ATOM   4631  CD2 HIS B 160      -0.635   1.946  39.168  1.00 44.14           C  
ATOM   4632  CE1 HIS B 160      -1.636   0.329  38.081  1.00 44.26           C  
ATOM   4633  NE2 HIS B 160      -0.773   1.354  37.963  1.00 44.04           N  
ATOM   4634  N   LEU B 161       1.243  -0.385  42.259  1.00 42.12           N  
ATOM   4635  CA  LEU B 161       2.699  -0.319  42.347  1.00 40.18           C  
ATOM   4636  C   LEU B 161       3.335  -0.192  40.973  1.00 38.48           C  
ATOM   4637  O   LEU B 161       2.966  -0.910  40.044  1.00 37.67           O  
ATOM   4638  CB  LEU B 161       3.251  -1.555  43.064  1.00 39.51           C  
ATOM   4639  CG  LEU B 161       2.584  -2.003  44.364  1.00 39.70           C  
ATOM   4640  CD1 LEU B 161       3.290  -3.232  44.909  1.00 38.32           C  
ATOM   4641  CD2 LEU B 161       2.586  -0.885  45.399  1.00 38.15           C  
ATOM   4642  N   THR B 162       4.279   0.738  40.855  1.00 38.33           N  
ATOM   4643  CA  THR B 162       5.088   0.900  39.653  1.00 36.74           C  
ATOM   4644  C   THR B 162       6.551   0.933  40.097  1.00 36.23           C  
ATOM   4645  O   THR B 162       6.836   1.348  41.227  1.00 35.28           O  
ATOM   4646  CB  THR B 162       4.729   2.184  38.855  1.00 38.85           C  
ATOM   4647  OG1 THR B 162       5.358   3.329  39.444  1.00 37.00           O  
ATOM   4648  CG2 THR B 162       3.208   2.406  38.793  1.00 36.27           C  
ATOM   4649  N   PRO B 163       7.476   0.463  39.230  1.00 34.99           N  
ATOM   4650  CA  PRO B 163       8.903   0.378  39.551  1.00 35.81           C  
ATOM   4651  C   PRO B 163       9.573   1.699  39.923  1.00 39.58           C  
ATOM   4652  O   PRO B 163      10.468   1.695  40.764  1.00 40.69           O  
ATOM   4653  CB  PRO B 163       9.532  -0.164  38.252  1.00 32.90           C  
ATOM   4654  CG  PRO B 163       8.518   0.098  37.182  1.00 32.95           C  
ATOM   4655  CD  PRO B 163       7.202  -0.084  37.889  1.00 34.51           C  
ATOM   4656  N   THR B 164       9.167   2.804  39.295  1.00 42.37           N  
ATOM   4657  CA  THR B 164       9.833   4.099  39.512  1.00 45.83           C  
ATOM   4658  C   THR B 164       8.938   5.174  40.131  1.00 47.95           C  
ATOM   4659  O   THR B 164       9.361   6.323  40.275  1.00 49.66           O  
ATOM   4660  CB  THR B 164      10.425   4.685  38.209  1.00 45.73           C  
ATOM   4661  OG1 THR B 164       9.361   5.059  37.326  1.00 46.12           O  
ATOM   4662  CG2 THR B 164      11.347   3.690  37.514  1.00 47.20           C  
ATOM   4663  N   GLY B 165       7.714   4.807  40.492  1.00 48.29           N  
ATOM   4664  CA  GLY B 165       6.767   5.766  41.060  1.00 51.27           C  
ATOM   4665  C   GLY B 165       6.975   6.002  42.544  1.00 52.65           C  
ATOM   4666  O   GLY B 165       8.042   5.697  43.086  1.00 51.82           O  
ATOM   4667  N   GLU B 166       5.947   6.541  43.199  1.00 53.79           N  
ATOM   4668  CA  GLU B 166       6.004   6.851  44.631  1.00 55.15           C  
ATOM   4669  C   GLU B 166       6.035   5.583  45.488  1.00 52.85           C  
ATOM   4670  O   GLU B 166       6.563   5.591  46.600  1.00 53.73           O  
ATOM   4671  CB  GLU B 166       4.829   7.750  45.043  1.00 57.65           C  
ATOM   4672  CG  GLU B 166       3.496   7.021  45.205  1.00 59.63           C  
ATOM   4673  CD  GLU B 166       2.330   7.960  45.422  1.00 61.72           C  
ATOM   4674  OE1 GLU B 166       2.307   9.033  44.784  1.00 62.52           O  
ATOM   4675  OE2 GLU B 166       1.428   7.618  46.223  1.00 63.53           O  
ATOM   4676  N   ASP B 167       5.463   4.502  44.962  1.00 48.82           N  
ATOM   4677  CA  ASP B 167       5.466   3.214  45.643  1.00 47.61           C  
ATOM   4678  C   ASP B 167       6.562   2.266  45.128  1.00 42.62           C  
ATOM   4679  O   ASP B 167       6.423   1.048  45.208  1.00 43.11           O  
ATOM   4680  CB  ASP B 167       4.079   2.559  45.568  1.00 50.27           C  
ATOM   4681  CG  ASP B 167       3.357   2.556  46.909  1.00 53.02           C  
ATOM   4682  OD1 ASP B 167       4.027   2.457  47.954  1.00 57.23           O  
ATOM   4683  OD2 ASP B 167       2.112   2.633  46.926  1.00 53.82           O  
ATOM   4684  N   ALA B 168       7.647   2.842  44.617  1.00 40.06           N  
ATOM   4685  CA  ALA B 168       8.802   2.095  44.101  1.00 39.67           C  
ATOM   4686  C   ALA B 168       9.350   1.066  45.091  1.00 40.69           C  
ATOM   4687  O   ALA B 168       9.682  -0.057  44.709  1.00 40.74           O  
ATOM   4688  CB  ALA B 168       9.908   3.058  43.689  1.00 39.30           C  
ATOM   4689  N   GLU B 169       9.443   1.462  46.359  1.00 41.04           N  
ATOM   4690  CA  GLU B 169       9.989   0.623  47.422  1.00 39.96           C  
ATOM   4691  C   GLU B 169       9.122  -0.616  47.703  1.00 38.28           C  
ATOM   4692  O   GLU B 169       9.643  -1.725  47.849  1.00 37.45           O  
ATOM   4693  CB  GLU B 169      10.206   1.478  48.681  1.00 43.37           C  
ATOM   4694  CG  GLU B 169      10.462   0.718  49.967  1.00 45.84           C  
ATOM   4695  CD  GLU B 169      10.598   1.651  51.161  1.00 48.49           C  
ATOM   4696  OE1 GLU B 169      11.684   2.244  51.334  1.00 50.00           O  
ATOM   4697  OE2 GLU B 169       9.621   1.789  51.925  1.00 48.65           O  
ATOM   4698  N   LEU B 170       7.805  -0.441  47.772  1.00 35.56           N  
ATOM   4699  CA  LEU B 170       6.921  -1.594  47.929  1.00 34.06           C  
ATOM   4700  C   LEU B 170       6.878  -2.479  46.659  1.00 31.94           C  
ATOM   4701  O   LEU B 170       6.758  -3.693  46.749  1.00 30.69           O  
ATOM   4702  CB  LEU B 170       5.511  -1.159  48.352  1.00 34.18           C  
ATOM   4703  CG  LEU B 170       4.498  -2.274  48.650  1.00 34.39           C  
ATOM   4704  CD1 LEU B 170       5.030  -3.282  49.667  1.00 34.67           C  
ATOM   4705  CD2 LEU B 170       3.165  -1.690  49.118  1.00 34.62           C  
ATOM   4706  N   PHE B 171       6.969  -1.857  45.492  1.00 32.90           N  
ATOM   4707  CA  PHE B 171       7.062  -2.585  44.226  1.00 34.00           C  
ATOM   4708  C   PHE B 171       8.230  -3.573  44.283  1.00 32.52           C  
ATOM   4709  O   PHE B 171       8.052  -4.782  44.098  1.00 31.18           O  
ATOM   4710  CB  PHE B 171       7.248  -1.609  43.056  1.00 34.44           C  
ATOM   4711  CG  PHE B 171       7.349  -2.280  41.706  1.00 35.51           C  
ATOM   4712  CD1 PHE B 171       6.213  -2.481  40.930  1.00 35.17           C  
ATOM   4713  CD2 PHE B 171       8.579  -2.716  41.214  1.00 34.94           C  
ATOM   4714  CE1 PHE B 171       6.301  -3.095  39.687  1.00 35.30           C  
ATOM   4715  CE2 PHE B 171       8.669  -3.336  39.974  1.00 35.42           C  
ATOM   4716  CZ  PHE B 171       7.529  -3.528  39.212  1.00 33.92           C  
ATOM   4717  N   TRP B 172       9.413  -3.047  44.573  1.00 31.97           N  
ATOM   4718  CA  TRP B 172      10.631  -3.850  44.578  1.00 31.89           C  
ATOM   4719  C   TRP B 172      10.766  -4.831  45.717  1.00 32.38           C  
ATOM   4720  O   TRP B 172      11.596  -5.736  45.649  1.00 32.43           O  
ATOM   4721  CB  TRP B 172      11.846  -2.956  44.425  1.00 31.13           C  
ATOM   4722  CG  TRP B 172      11.925  -2.409  43.027  1.00 31.35           C  
ATOM   4723  CD1 TRP B 172      11.697  -1.103  42.606  1.00 30.85           C  
ATOM   4724  CD2 TRP B 172      12.231  -3.158  41.800  1.00 31.44           C  
ATOM   4725  NE1 TRP B 172      11.848  -0.994  41.249  1.00 31.02           N  
ATOM   4726  CE2 TRP B 172      12.172  -2.189  40.704  1.00 31.66           C  
ATOM   4727  CE3 TRP B 172      12.551  -4.486  41.514  1.00 32.97           C  
ATOM   4728  CZ2 TRP B 172      12.426  -2.552  39.386  1.00 30.46           C  
ATOM   4729  CZ3 TRP B 172      12.794  -4.840  40.181  1.00 31.64           C  
ATOM   4730  CH2 TRP B 172      12.729  -3.896  39.146  1.00 31.42           C  
ATOM   4731  N   ALA B 173       9.938  -4.689  46.754  1.00 32.03           N  
ATOM   4732  CA  ALA B 173       9.870  -5.695  47.819  1.00 32.00           C  
ATOM   4733  C   ALA B 173       8.913  -6.827  47.446  1.00 31.56           C  
ATOM   4734  O   ALA B 173       9.029  -7.958  47.941  1.00 31.08           O  
ATOM   4735  CB  ALA B 173       9.460  -5.061  49.145  1.00 33.23           C  
ATOM   4736  N   THR B 174       7.969  -6.513  46.570  1.00 30.48           N  
ATOM   4737  CA  THR B 174       7.000  -7.492  46.097  1.00 31.29           C  
ATOM   4738  C   THR B 174       7.644  -8.416  45.046  1.00 29.74           C  
ATOM   4739  O   THR B 174       7.372  -9.617  45.016  1.00 29.83           O  
ATOM   4740  CB  THR B 174       5.730  -6.777  45.586  1.00 32.72           C  
ATOM   4741  OG1 THR B 174       5.213  -5.949  46.641  1.00 33.38           O  
ATOM   4742  CG2 THR B 174       4.652  -7.775  45.156  1.00 31.29           C  
ATOM   4743  N   VAL B 175       8.508  -7.844  44.210  1.00 28.96           N  
ATOM   4744  CA  VAL B 175       9.352  -8.613  43.284  1.00 29.02           C  
ATOM   4745  C   VAL B 175      10.257  -9.513  44.123  1.00 28.12           C  
ATOM   4746  O   VAL B 175      10.986  -9.034  44.990  1.00 28.68           O  
ATOM   4747  CB  VAL B 175      10.190  -7.678  42.372  1.00 29.09           C  
ATOM   4748  CG1 VAL B 175      11.251  -8.450  41.592  1.00 28.32           C  
ATOM   4749  CG2 VAL B 175       9.292  -6.921  41.402  1.00 28.38           C  
ATOM   4750  N   GLY B 176      10.172 -10.819  43.899  1.00 27.54           N  
ATOM   4751  CA  GLY B 176      10.954 -11.780  44.677  1.00 30.23           C  
ATOM   4752  C   GLY B 176      10.541 -11.868  46.144  1.00 31.90           C  
ATOM   4753  O   GLY B 176      11.184 -12.563  46.936  1.00 31.60           O  
ATOM   4754  N   GLY B 177       9.452 -11.182  46.500  1.00 32.05           N  
ATOM   4755  CA  GLY B 177       8.960 -11.157  47.876  1.00 32.14           C  
ATOM   4756  C   GLY B 177       8.193 -12.371  48.372  1.00 33.45           C  
ATOM   4757  O   GLY B 177       7.688 -12.371  49.511  1.00 33.79           O  
ATOM   4758  N   ASN B 178       8.084 -13.397  47.532  1.00 31.89           N  
ATOM   4759  CA  ASN B 178       7.429 -14.669  47.899  1.00 33.45           C  
ATOM   4760  C   ASN B 178       5.996 -14.581  48.458  1.00 36.05           C  
ATOM   4761  O   ASN B 178       5.594 -15.398  49.298  1.00 37.80           O  
ATOM   4762  CB  ASN B 178       8.333 -15.494  48.832  1.00 32.55           C  
ATOM   4763  CG  ASN B 178       9.544 -16.056  48.110  1.00 31.84           C  
ATOM   4764  OD1 ASN B 178       9.525 -17.189  47.655  1.00 33.07           O  
ATOM   4765  ND2 ASN B 178      10.587 -15.245  47.970  1.00 33.48           N  
ATOM   4766  N   GLY B 179       5.232 -13.605  47.972  1.00 35.80           N  
ATOM   4767  CA  GLY B 179       3.830 -13.425  48.372  1.00 38.84           C  
ATOM   4768  C   GLY B 179       3.611 -12.767  49.732  1.00 39.55           C  
ATOM   4769  O   GLY B 179       2.485 -12.726  50.231  1.00 42.11           O  
ATOM   4770  N   LEU B 180       4.675 -12.237  50.327  1.00 38.68           N  
ATOM   4771  CA  LEU B 180       4.627 -11.819  51.725  1.00 39.07           C  
ATOM   4772  C   LEU B 180       4.395 -10.335  51.914  1.00 40.68           C  
ATOM   4773  O   LEU B 180       4.477  -9.831  53.034  1.00 44.34           O  
ATOM   4774  CB  LEU B 180       5.888 -12.268  52.467  1.00 38.14           C  
ATOM   4775  CG  LEU B 180       6.118 -13.779  52.548  1.00 38.91           C  
ATOM   4776  CD1 LEU B 180       7.545 -14.080  52.983  1.00 38.96           C  
ATOM   4777  CD2 LEU B 180       5.108 -14.463  53.464  1.00 39.47           C  
ATOM   4778  N   THR B 181       4.118  -9.630  50.822  1.00 38.23           N  
ATOM   4779  CA  THR B 181       3.704  -8.235  50.910  1.00 37.86           C  
ATOM   4780  C   THR B 181       2.211  -8.116  50.626  1.00 36.60           C  
ATOM   4781  O   THR B 181       1.645  -7.028  50.712  1.00 37.17           O  
ATOM   4782  CB  THR B 181       4.452  -7.343  49.907  1.00 36.37           C  
ATOM   4783  OG1 THR B 181       4.153  -7.788  48.580  1.00 35.77           O  
ATOM   4784  CG2 THR B 181       5.952  -7.384  50.156  1.00 37.04           C  
ATOM   4785  N   GLY B 182       1.590  -9.240  50.276  1.00 37.79           N  
ATOM   4786  CA  GLY B 182       0.180  -9.274  49.908  1.00 38.40           C  
ATOM   4787  C   GLY B 182      -0.085 -10.111  48.673  1.00 39.50           C  
ATOM   4788  O   GLY B 182       0.774 -10.885  48.235  1.00 39.53           O  
ATOM   4789  N   ILE B 183      -1.281  -9.947  48.110  1.00 39.15           N  
ATOM   4790  CA  ILE B 183      -1.705 -10.697  46.929  1.00 38.71           C  
ATOM   4791  C   ILE B 183      -1.680  -9.812  45.678  1.00 37.89           C  
ATOM   4792  O   ILE B 183      -2.398  -8.810  45.601  1.00 36.92           O  
ATOM   4793  CB  ILE B 183      -3.105 -11.319  47.132  1.00 40.26           C  
ATOM   4794  CG1 ILE B 183      -3.066 -12.345  48.270  1.00 41.18           C  
ATOM   4795  CG2 ILE B 183      -3.598 -11.981  45.850  1.00 38.73           C  
ATOM   4796  CD1 ILE B 183      -4.428 -12.768  48.766  1.00 41.78           C  
ATOM   4797  N   ILE B 184      -0.816 -10.169  44.725  1.00 37.12           N  
ATOM   4798  CA  ILE B 184      -0.777  -9.510  43.419  1.00 34.95           C  
ATOM   4799  C   ILE B 184      -2.050  -9.946  42.714  1.00 34.28           C  
ATOM   4800  O   ILE B 184      -2.316 -11.142  42.589  1.00 33.91           O  
ATOM   4801  CB  ILE B 184       0.464  -9.928  42.594  1.00 34.57           C  
ATOM   4802  CG1 ILE B 184       1.748  -9.638  43.385  1.00 33.47           C  
ATOM   4803  CG2 ILE B 184       0.488  -9.199  41.256  1.00 33.98           C  
ATOM   4804  CD1 ILE B 184       2.887 -10.598  43.106  1.00 34.22           C  
ATOM   4805  N   MET B 185      -2.862  -8.976  42.305  1.00 34.06           N  
ATOM   4806  CA  MET B 185      -4.161  -9.285  41.705  1.00 35.75           C  
ATOM   4807  C   MET B 185      -4.074  -9.243  40.187  1.00 34.57           C  
ATOM   4808  O   MET B 185      -4.770  -9.973  39.488  1.00 34.79           O  
ATOM   4809  CB  MET B 185      -5.232  -8.292  42.183  1.00 37.20           C  
ATOM   4810  CG  MET B 185      -5.409  -8.208  43.695  1.00 39.33           C  
ATOM   4811  SD  MET B 185      -6.206  -9.658  44.419  1.00 42.46           S  
ATOM   4812  CE  MET B 185      -7.892  -9.462  43.835  1.00 40.81           C  
ATOM   4813  N   ARG B 186      -3.197  -8.384  39.688  1.00 35.50           N  
ATOM   4814  CA  ARG B 186      -3.198  -8.015  38.287  1.00 36.18           C  
ATOM   4815  C   ARG B 186      -1.882  -7.303  38.016  1.00 35.15           C  
ATOM   4816  O   ARG B 186      -1.295  -6.700  38.925  1.00 36.96           O  
ATOM   4817  CB  ARG B 186      -4.383  -7.072  38.034  1.00 35.89           C  
ATOM   4818  CG  ARG B 186      -4.729  -6.788  36.584  1.00 36.77           C  
ATOM   4819  CD  ARG B 186      -6.059  -6.059  36.506  1.00 35.91           C  
ATOM   4820  NE  ARG B 186      -6.250  -5.415  35.208  1.00 35.13           N  
ATOM   4821  CZ  ARG B 186      -7.409  -4.926  34.768  1.00 36.25           C  
ATOM   4822  NH1 ARG B 186      -8.512  -5.021  35.514  1.00 32.31           N  
ATOM   4823  NH2 ARG B 186      -7.469  -4.351  33.572  1.00 33.72           N  
ATOM   4824  N   ALA B 187      -1.421  -7.381  36.771  1.00 32.30           N  
ATOM   4825  CA  ALA B 187      -0.153  -6.784  36.386  1.00 29.65           C  
ATOM   4826  C   ALA B 187      -0.158  -6.311  34.938  1.00 29.27           C  
ATOM   4827  O   ALA B 187      -0.944  -6.791  34.121  1.00 27.06           O  
ATOM   4828  CB  ALA B 187       0.977  -7.774  36.619  1.00 29.35           C  
ATOM   4829  N   THR B 188       0.717  -5.356  34.631  1.00 28.93           N  
ATOM   4830  CA  THR B 188       1.016  -5.027  33.245  1.00 30.13           C  
ATOM   4831  C   THR B 188       2.480  -5.329  32.999  1.00 29.49           C  
ATOM   4832  O   THR B 188       3.335  -4.869  33.744  1.00 29.85           O  
ATOM   4833  CB  THR B 188       0.700  -3.564  32.862  1.00 31.71           C  
ATOM   4834  OG1 THR B 188       1.478  -2.678  33.669  1.00 37.91           O  
ATOM   4835  CG2 THR B 188      -0.775  -3.251  33.059  1.00 30.74           C  
ATOM   4836  N   ILE B 189       2.743  -6.117  31.957  1.00 28.10           N  
ATOM   4837  CA  ILE B 189       4.083  -6.564  31.600  1.00 27.48           C  
ATOM   4838  C   ILE B 189       4.454  -5.973  30.238  1.00 28.31           C  
ATOM   4839  O   ILE B 189       3.651  -5.991  29.293  1.00 27.66           O  
ATOM   4840  CB  ILE B 189       4.147  -8.115  31.525  1.00 27.55           C  
ATOM   4841  CG1 ILE B 189       3.480  -8.784  32.750  1.00 28.34           C  
ATOM   4842  CG2 ILE B 189       5.569  -8.627  31.288  1.00 27.72           C  
ATOM   4843  CD1 ILE B 189       4.192  -8.592  34.071  1.00 28.91           C  
ATOM   4844  N   GLU B 190       5.664  -5.443  30.130  1.00 27.93           N  
ATOM   4845  CA  GLU B 190       6.150  -5.044  28.838  1.00 27.32           C  
ATOM   4846  C   GLU B 190       6.785  -6.263  28.163  1.00 27.41           C  
ATOM   4847  O   GLU B 190       7.748  -6.845  28.679  1.00 25.10           O  
ATOM   4848  CB  GLU B 190       7.149  -3.889  28.929  1.00 28.30           C  
ATOM   4849  CG  GLU B 190       7.479  -3.330  27.560  1.00 29.41           C  
ATOM   4850  CD  GLU B 190       8.525  -2.227  27.576  1.00 31.27           C  
ATOM   4851  OE1 GLU B 190       8.796  -1.643  28.641  1.00 33.57           O  
ATOM   4852  OE2 GLU B 190       9.062  -1.930  26.499  1.00 32.30           O  
ATOM   4853  N   MET B 191       6.235  -6.608  27.000  1.00 26.78           N  
ATOM   4854  CA  MET B 191       6.655  -7.774  26.223  1.00 27.50           C  
ATOM   4855  C   MET B 191       7.823  -7.436  25.309  1.00 27.43           C  
ATOM   4856  O   MET B 191       8.112  -6.256  25.054  1.00 27.53           O  
ATOM   4857  CB  MET B 191       5.468  -8.302  25.395  1.00 25.79           C  
ATOM   4858  CG  MET B 191       4.229  -8.593  26.231  1.00 26.98           C  
ATOM   4859  SD  MET B 191       4.429  -9.988  27.354  1.00 28.49           S  
ATOM   4860  CE  MET B 191       4.137 -11.348  26.222  1.00 28.86           C  
ATOM   4861  N   THR B 192       8.501  -8.473  24.829  1.00 27.67           N  
ATOM   4862  CA  THR B 192       9.587  -8.308  23.862  1.00 27.74           C  
ATOM   4863  C   THR B 192       9.011  -8.472  22.448  1.00 28.01           C  
ATOM   4864  O   THR B 192       8.341  -9.467  22.166  1.00 27.67           O  
ATOM   4865  CB  THR B 192      10.714  -9.333  24.122  1.00 28.54           C  
ATOM   4866  O