CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 29-DEC-06 2OEG  ***

elNémo ID: 21031700182711855

Job options:

ID        	=	 21031700182711855
JOBID     	=	 TRANSFERASE 29-DEC-06 2OEG
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             29-DEC-06   2OEG              
TITLE     OPEN AND CLOSED STRUCTURES OF THE UDP-GLUCOSE                         
TITLE    2 PYROPHOSPHORYLASE FROM LEISHMANIA MAJOR                              
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: UTP-GLUCOSE-1-PHOSPHATE URIDYLYLTRANSFERASE 2,             
COMPND   3 PUTATIVE;                                                            
COMPND   4 CHAIN: A;                                                            
COMPND   5 SYNONYM: UDP-GLUCOSE PYROPHOSPHORYLASE;                              
COMPND   6 EC: 2.7.7.9;                                                         
COMPND   7 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEISHMANIA MAJOR;                               
SOURCE   3 ORGANISM_TAXID: 5664;                                                
SOURCE   4 GENE: UGP;                                                           
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 562                                         
KEYWDS    ROSSMANN-FOLD, BETA-HELIX, PYROPHOSPHORYLASE, TRANSFERASE             
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    T.STEINER                                                             
REVDAT   3   24-FEB-09 2OEG    1       VERSN                                    
REVDAT   2   01-MAY-07 2OEG    1       JRNL                                     
REVDAT   1   13-FEB-07 2OEG    0                                                
JRNL        AUTH   T.STEINER,A.C.LAMERZ,P.HESS,C.BREITHAUPT,S.KRAPP,            
JRNL        AUTH 2 G.BOURENKOV,R.HUBER,R.GERARDY-SCHAHN,U.JACOB                 
JRNL        TITL   OPEN AND CLOSED STRUCTURES OF THE UDP-GLUCOSE                
JRNL        TITL 2 PYROPHOSPHORYLASE FROM LEISHMANIA MAJOR.                     
JRNL        REF    J.BIOL.CHEM.                  V. 282 13003 2007              
JRNL        REFN                   ISSN 0021-9258                               
JRNL        PMID   17303565                                                     
JRNL        DOI    10.1074/JBC.M609984200                                       
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.30 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES, PANNU,             
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.30                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 19.96                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 2056852.710                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 97.3                           
REMARK   3   NUMBER OF REFLECTIONS             : 21001                          
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 SET) : 0.210                           
REMARK   3   FREE R VALUE                     : 0.255                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1065                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.008                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.30                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.44                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 99.00                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 3435                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2500                       
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 5.40                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 197                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.021                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3721                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 36                                      
REMARK   3   SOLVENT ATOMS            : 225                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 22.20                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 28.00                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.27000                                             
REMARK   3    B22 (A**2) : 4.49000                                              
REMARK   3    B33 (A**2) : -2.22000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : 0.27                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.20                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : 5.00                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : 0.34                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.25                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.008                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.50                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 24.40                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.92                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : RESTRAINED                                
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.31                                                 
REMARK   3   BSOL        : 28.14                                                
REMARK   3                                                                      
REMARK   3  NCS MODEL : NULL                                                    
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS.                         RMS   SIGMA/WEIGHT          
REMARK   3   GROUP  1  POSITIONAL            (A) : NULL  ; NULL                 
REMARK   3   GROUP  1  B-FACTOR           (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  PARAMETER FILE  1  : PROTEIN_REP.PARAM                              
REMARK   3  PARAMETER FILE  2  : WATER_REP.PARAM                                
REMARK   3  PARAMETER FILE  3  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  4  : UPG_XPLOR.PAR                                  
REMARK   3  PARAMETER FILE  5  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  4   : UPG_XPLOR.TOP                                  
REMARK   3  TOPOLOGY FILE  5   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2OEG COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 03-JAN-07.                  
REMARK 100 THE RCSB ID CODE IS RCSB041032.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 04-FEB-05                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : EMBL/DESY, HAMBURG                 
REMARK 200  BEAMLINE                       : BW7A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.97920, 0.97960, 0.950            
REMARK 200  MONOCHROMATOR                  : GRAPHITE                           
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 21001                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.300                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 20.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.500                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 96.0                               
REMARK 200  DATA REDUNDANCY                : NULL                               
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : NULL                               
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.30                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.40                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: MAD                                            
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MAD                          
REMARK 200 SOFTWARE USED: CNS                                                   
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 43.37                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.17                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 27% PEG MONOMETHYL ETHER 2000, PH        
REMARK 280  6.5, VAPOR DIFFUSION, SITTING DROP, TEMPERATURE 293K                
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       68.58450            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       68.58450            
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  1.000000  0.000000  0.000000       40.12350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       44.96450            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       40.12350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       44.96450            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       68.58450            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       40.12350            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       44.96450            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       68.58450            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       40.12350            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       44.96450            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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 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     MSE A     1                                                      
REMARK 465     GLU A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     ASP A     4                                                      
REMARK 465     MSE A     5                                                      
REMARK 465     LYS A     6                                                      
REMARK 465     GLN A   489                                                      
REMARK 465     GLN A   490                                                      
REMARK 465     SER A   491                                                      
REMARK 465     THR A   492                                                      
REMARK 465     ASN A   493                                                      
REMARK 465     LYS A   494                                                      
REMARK 465     MSE A   495                                                      
REMARK 465     ARG A   496                                                      
REMARK 465     PRO A   497                                                      
REMARK 465     LEU A   498                                                      
REMARK 465     GLU A   499                                                      
REMARK 465     HIS A   500                                                      
REMARK 465     HIS A   501                                                      
REMARK 465     HIS A   502                                                      
REMARK 465     HIS A   503                                                      
REMARK 465     HIS A   504                                                      
REMARK 465     HIS A   505                                                      
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   NH1  ARG A   400     O    HOH A  5315              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    THR A  65      -32.54   -141.90                                   
REMARK 500    ASN A  82       30.60   -154.23                                   
REMARK 500    ASN A 181       87.00   -154.88                                   
REMARK 500    LYS A 269      168.93     85.55                                   
REMARK 500    ASP A 274      105.25    -48.11                                   
REMARK 500    SER A 469      -80.69     88.49                                   
REMARK 500    ALA A 479      152.98    -49.47                                   
REMARK 500    ASP A 483       62.03      9.87                                   
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 UPG A 5206                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2OEF   RELATED DB: PDB                                   
DBREF  2OEG A    1   494  UNP    Q4QDU3   Q4QDU3_LEIMA     1    494             
SEQADV 2OEG MSE A    1  UNP  Q4QDU3    MET     1 MODIFIED RESIDUE               
SEQADV 2OEG MSE A    5  UNP  Q4QDU3    MET     5 MODIFIED RESIDUE               
SEQADV 2OEG MSE A   19  UNP  Q4QDU3    MET    19 MODIFIED RESIDUE               
SEQADV 2OEG MSE A   38  UNP  Q4QDU3    MET    38 MODIFIED RESIDUE               
SEQADV 2OEG MSE A   53  UNP  Q4QDU3    MET    53 MODIFIED RESIDUE               
SEQADV 2OEG MSE A   89  UNP  Q4QDU3    MET    89 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  128  UNP  Q4QDU3    MET   128 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  130  UNP  Q4QDU3    MET   130 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  161  UNP  Q4QDU3    MET   161 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  215  UNP  Q4QDU3    MET   215 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  235  UNP  Q4QDU3    MET   235 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  244  UNP  Q4QDU3    MET   244 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  293  UNP  Q4QDU3    MET   293 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  321  UNP  Q4QDU3    MET   321 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  356  UNP  Q4QDU3    MET   356 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  362  UNP  Q4QDU3    MET   362 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  423  UNP  Q4QDU3    MET   423 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  424  UNP  Q4QDU3    MET   424 MODIFIED RESIDUE               
SEQADV 2OEG MSE A  495  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG ARG A  496  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG PRO A  497  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG LEU A  498  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG GLU A  499  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG HIS A  500  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG HIS A  501  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG HIS A  502  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG HIS A  503  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG HIS A  504  UNP  Q4QDU3              CLONING ARTIFACT               
SEQADV 2OEG HIS A  505  UNP  Q4QDU3              CLONING ARTIFACT               
SEQRES   1 A  505  MSE GLU ASN ASP MSE LYS SER LEU SER ALA ALA ALA GLN          
SEQRES   2 A  505  ALA CYS VAL LYS LYS MSE ARG ASP ALA LYS VAL ASN GLU          
SEQRES   3 A  505  ALA CYS ILE ARG THR PHE ILE ALA GLN HIS VAL MSE VAL          
SEQRES   4 A  505  SER LYS GLY GLU THR GLY SER ILE PRO ASP SER ALA ILE          
SEQRES   5 A  505  MSE PRO VAL ASP SER LEU ASP ALA LEU ASP SER LEU THR          
SEQRES   6 A  505  ILE GLU CYS ASP ASN ALA VAL LEU GLN SER THR VAL VAL          
SEQRES   7 A  505  LEU LYS LEU ASN GLY GLY LEU GLY THR GLY MSE GLY LEU          
SEQRES   8 A  505  CYS ASP ALA LYS THR LEU LEU GLU VAL LYS ASP GLY LYS          
SEQRES   9 A  505  THR PHE LEU ASP PHE THR ALA LEU GLN VAL GLN TYR LEU          
SEQRES  10 A  505  ARG GLN HIS CYS SER GLU HIS LEU ARG PHE MSE LEU MSE          
SEQRES  11 A  505  ASP SER PHE ASN THR SER ALA SER THR LYS SER PHE LEU          
SEQRES  12 A  505  LYS ALA ARG TYR PRO TRP LEU TYR GLN VAL PHE ASP SER          
SEQRES  13 A  505  GLU VAL GLU LEU MSE GLN ASN GLN VAL PRO LYS ILE LEU          
SEQRES  14 A  505  GLN ASP THR LEU GLU PRO ALA ALA TRP ALA GLU ASN PRO          
SEQRES  15 A  505  ALA TYR GLU TRP ALA PRO PRO GLY HIS GLY ASP ILE TYR          
SEQRES  16 A  505  THR ALA LEU TYR GLY SER GLY LYS LEU GLN GLU LEU VAL          
SEQRES  17 A  505  GLU GLN GLY TYR ARG TYR MSE PHE VAL SER ASN GLY ASP          
SEQRES  18 A  505  ASN LEU GLY ALA THR ILE ASP LYS ARG VAL LEU ALA TYR          
SEQRES  19 A  505  MSE GLU LYS GLU LYS ILE ASP PHE LEU MSE GLU VAL CYS          
SEQRES  20 A  505  ARG ARG THR GLU SER ASP LYS LYS GLY GLY HIS LEU ALA          
SEQRES  21 A  505  ARG GLN THR VAL TYR VAL LYS GLY LYS ASP GLY GLN PRO          
SEQRES  22 A  505  ASP ALA GLU LYS ARG VAL LEU LEU LEU ARG GLU SER ALA          
SEQRES  23 A  505  GLN CYS PRO LYS ALA ASP MSE GLU SER PHE GLN ASP ILE          
SEQRES  24 A  505  ASN LYS TYR SER PHE PHE ASN THR ASN ASN LEU TRP ILE          
SEQRES  25 A  505  ARG LEU PRO VAL LEU LEU GLU THR MSE GLN GLU HIS GLY          
SEQRES  26 A  505  GLY THR LEU PRO LEU PRO VAL ILE ARG ASN GLU LYS THR          
SEQRES  27 A  505  VAL ASP SER SER ASN SER ALA SER PRO LYS VAL TYR GLN          
SEQRES  28 A  505  LEU GLU THR ALA MSE GLY ALA ALA ILE ALA MSE PHE GLU          
SEQRES  29 A  505  SER ALA SER ALA ILE VAL VAL PRO ARG SER ARG PHE ALA          
SEQRES  30 A  505  PRO VAL LYS THR CYS ALA ASP LEU LEU ALA LEU ARG SER          
SEQRES  31 A  505  ASP ALA TYR VAL VAL THR ASP ASP PHE ARG LEU VAL LEU          
SEQRES  32 A  505  ASP ASP ARG CYS HIS GLY HIS PRO PRO VAL VAL ASP LEU          
SEQRES  33 A  505  ASP SER ALA HIS TYR LYS MSE MSE ASN GLY PHE GLU LYS          
SEQRES  34 A  505  LEU VAL GLN HIS GLY VAL PRO SER LEU VAL GLU CYS LYS          
SEQRES  35 A  505  ARG VAL THR VAL LYS GLY LEU VAL GLN PHE GLY ALA GLY          
SEQRES  36 A  505  ASN VAL LEU THR GLY THR VAL THR ILE GLU ASN THR ASP          
SEQRES  37 A  505  SER ALA SER ALA PHE VAL ILE PRO ASP GLY ALA LYS LEU          
SEQRES  38 A  505  ASN ASP THR THR ALA SER PRO GLN GLN SER THR ASN LYS          
SEQRES  39 A  505  MSE ARG PRO LEU GLU HIS HIS HIS HIS HIS HIS                  
MODRES 2OEG MSE A   19  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A   38  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A   53  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A   89  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  128  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  130  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  161  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  215  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  235  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  244  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  293  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  321  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  356  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  362  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  423  MET  SELENOMETHIONINE                                   
MODRES 2OEG MSE A  424  MET  SELENOMETHIONINE                                   
HET    MSE  A  19       8                                                       
HET    MSE  A  38       8                                                       
HET    MSE  A  53       8                                                       
HET    MSE  A  89       8                                                       
HET    MSE  A 128       8                                                       
HET    MSE  A 130       8                                                       
HET    MSE  A 161       8                                                       
HET    MSE  A 215       8                                                       
HET    MSE  A 235       8                                                       
HET    MSE  A 244       8                                                       
HET    MSE  A 293       8                                                       
HET    MSE  A 321       8                                                       
HET    MSE  A 356       8                                                       
HET    MSE  A 362       8                                                       
HET    MSE  A 423       8                                                       
HET    MSE  A 424       8                                                       
HET    UPG  A5206      36                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     UPG URIDINE-5'-DIPHOSPHATE-GLUCOSE                                   
HETSYN     UPG URIDINE-5'-MONOPHOSPHATE GLUCOPYRANOSYL-MONOPHOSPHATE            
HETSYN   2 UPG  ESTER                                                           
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   2  UPG    C15 H24 N2 O17 P2                                            
FORMUL   3  HOH   *225(H2 O)                                                    
HELIX    1   1 SER A    9  ALA A   22  1                                  14    
HELIX    2   2 ASN A   25  LYS A   41  1                                  17    
HELIX    3   3 PRO A   48  ILE A   52  5                                   5    
HELIX    4   4 ALA A   60  LEU A   64  5                                   5    
HELIX    5   5 ASP A   69  SER A   75  1                                   7    
HELIX    6   6 GLY A   86  GLY A   90  5                                   5    
HELIX    7   7 ALA A   94  LEU A   97  5                                   4    
HELIX    8   8 PHE A  106  CYS A  121  1                                  16    
HELIX    9   9 SER A  132  TYR A  147  1                                  16    
HELIX   10  10 TYR A  147  GLN A  152  1                                   6    
HELIX   11  11 ASN A  181  TYR A  184  5                                   4    
HELIX   12  12 GLY A  192  SER A  201  1                                  10    
HELIX   13  13 GLY A  202  GLN A  210  1                                   9    
HELIX   14  14 ASP A  228  LYS A  239  1                                  12    
HELIX   15  15 ALA A  286  CYS A  288  5                                   3    
HELIX   16  16 PRO A  289  ALA A  291  5                                   3    
HELIX   17  17 ASP A  292  ASP A  298  1                                   7    
HELIX   18  18 LEU A  314  HIS A  324  1                                  11    
HELIX   19  19 ALA A  355  MSE A  362  5                                   8    
HELIX   20  20 PRO A  372  PHE A  376  5                                   5    
HELIX   21  21 THR A  381  SER A  390  1                                  10    
HELIX   22  22 ASP A  405  HIS A  408  5                                   4    
HELIX   23  23 ASP A  417  LYS A  422  1                                   6    
HELIX   24  24 MSE A  423  VAL A  431  1                                   9    
SHEET    1   A 7 GLU A 159  MSE A 161  0                                        
SHEET    2   A 7 ARG A 126  ASP A 131  1  N  ASP A 131   O  LEU A 160           
SHEET    3   A 7 THR A  76  ASN A  82  1  N  VAL A  78   O  ARG A 126           
SHEET    4   A 7 TYR A 214  SER A 218  1  O  TYR A 214   N  VAL A  77           
SHEET    5   A 7 PHE A 304  ARG A 313 -1  O  LEU A 310   N  VAL A 217           
SHEET    6   A 7 PHE A 242  ARG A 248 -1  N  CYS A 247   O  PHE A 305           
SHEET    7   A 7 SER A 367  VAL A 370  1  O  ILE A 369   N  VAL A 246           
SHEET    1   B 2 GLU A  99  LYS A 101  0                                        
SHEET    2   B 2 LYS A 104  THR A 105 -1  O  LYS A 104   N  VAL A 100           
SHEET    1   C 2 VAL A 165  PRO A 166  0                                        
SHEET    2   C 2 TRP A 186  ALA A 187 -1  O  ALA A 187   N  VAL A 165           
SHEET    1   D 3 ILE A 168  LEU A 169  0                                        
SHEET    2   D 3 LYS A 348  GLU A 353 -1  O  TYR A 350   N  ILE A 168           
SHEET    3   D 3 ILE A 333  THR A 338 -1  N  LYS A 337   O  VAL A 349           
SHEET    1   E 2 GLY A 257  VAL A 266  0                                        
SHEET    2   E 2 ALA A 275  GLU A 284 -1  O  LYS A 277   N  VAL A 264           
SHEET    1   F 2 TYR A 393  VAL A 395  0                                        
SHEET    2   F 2 LEU A 401  LEU A 403 -1  O  VAL A 402   N  VAL A 394           
SHEET    1   G 4 VAL A 413  LEU A 416  0                                        
SHEET    2   G 4 CYS A 441  LYS A 447  1  O  VAL A 446   N  ASP A 415           
SHEET    3   G 4 VAL A 457  GLU A 465  1  O  VAL A 462   N  ARG A 443           
SHEET    4   G 4 LYS A 480  ASN A 482  1  O  LEU A 481   N  THR A 459           
SHEET    1   H 4 VAL A 413  LEU A 416  0                                        
SHEET    2   H 4 CYS A 441  LYS A 447  1  O  VAL A 446   N  ASP A 415           
SHEET    3   H 4 VAL A 457  GLU A 465  1  O  VAL A 462   N  ARG A 443           
SHEET    4   H 4 THR A 485  ALA A 486  1  O  ALA A 486   N  GLU A 465           
SHEET    1   I 2 VAL A 450  GLN A 451  0                                        
SHEET    2   I 2 PHE A 473  VAL A 474  1  O  PHE A 473   N  GLN A 451           
LINK         C   LYS A  18                 N   MSE A  19     1555   1555  1.33  
LINK         C   MSE A  19                 N   ARG A  20     1555   1555  1.33  
LINK         C   VAL A  37                 N   MSE A  38     1555   1555  1.33  
LINK         C   MSE A  38                 N   VAL A  39     1555   1555  1.33  
LINK         C   ILE A  52                 N   MSE A  53     1555   1555  1.33  
LINK         C   MSE A  53                 N   PRO A  54     1555   1555  1.34  
LINK         C   GLY A  88                 N   MSE A  89     1555   1555  1.33  
LINK         C   MSE A  89                 N   GLY A  90     1555   1555  1.33  
LINK         C   PHE A 127                 N   MSE A 128     1555   1555  1.33  
LINK         C   MSE A 128                 N   LEU A 129     1555   1555  1.33  
LINK         C   LEU A 129                 N   MSE A 130     1555   1555  1.33  
LINK         C   MSE A 130                 N   ASP A 131     1555   1555  1.33  
LINK         C   LEU A 160                 N   MSE A 161     1555   1555  1.32  
LINK         C   MSE A 161                 N   GLN A 162     1555   1555  1.33  
LINK         C   TYR A 214                 N   MSE A 215     1555   1555  1.32  
LINK         C   MSE A 215                 N   PHE A 216     1555   1555  1.32  
LINK         C   TYR A 234                 N   MSE A 235     1555   1555  1.33  
LINK         C   MSE A 235                 N   GLU A 236     1555   1555  1.33  
LINK         C   LEU A 243                 N   MSE A 244     1555   1555  1.33  
LINK         C   MSE A 244                 N   GLU A 245     1555   1555  1.33  
LINK         C   ASP A 292                 N   MSE A 293     1555   1555  1.33  
LINK         C   MSE A 293                 N   GLU A 294     1555   1555  1.33  
LINK         C   THR A 320                 N   MSE A 321     1555   1555  1.33  
LINK         C   MSE A 321                 N   GLN A 322     1555   1555  1.33  
LINK         C   ALA A 355                 N   MSE A 356     1555   1555  1.32  
LINK         C   MSE A 356                 N   GLY A 357     1555   1555  1.33  
LINK         C   ALA A 361                 N   MSE A 362     1555   1555  1.33  
LINK         C   MSE A 362                 N   PHE A 363     1555   1555  1.32  
LINK         C   LYS A 422                 N   MSE A 423     1555   1555  1.33  
LINK         C   MSE A 423                 N   MSE A 424     1555   1555  1.33  
LINK         C   MSE A 424                 N   ASN A 425     1555   1555  1.33  
SITE     1 AC1 29 LEU A  81  ASN A  82  GLY A  83  GLY A  84                    
SITE     2 AC1 29 MSE A 130  GLN A 162  PRO A 188  GLY A 190                    
SITE     3 AC1 29 HIS A 191  ASN A 219  GLY A 220  GLY A 256                    
SITE     4 AC1 29 GLY A 257  GLU A 284  PHE A 305  ASN A 306                    
SITE     5 AC1 29 ASN A 308  PHE A 376  LYS A 380  HOH A5214                    
SITE     6 AC1 29 HOH A5215  HOH A5216  HOH A5219  HOH A5220                    
SITE     7 AC1 29 HOH A5223  HOH A5229  HOH A5236  HOH A5279                    
SITE     8 AC1 29 HOH A5336                                                     
CRYST1   80.247   89.929  137.169  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012462  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.011120  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007290        0.00000                         
ATOM      1  N   SER A   7      24.979  19.508  69.674  1.00 36.62           N  
ATOM      2  CA  SER A   7      26.357  18.962  69.515  1.00 36.81           C  
ATOM      3  C   SER A   7      26.711  18.693  68.063  1.00 35.50           C  
ATOM      4  O   SER A   7      26.083  17.856  67.410  1.00 34.51           O  
ATOM      5  CB  SER A   7      26.508  17.664  70.291  1.00 38.73           C  
ATOM      6  OG  SER A   7      27.801  17.134  70.074  1.00 41.05           O  
ATOM      7  N   LEU A   8      27.741  19.377  67.571  1.00 35.36           N  
ATOM      8  CA  LEU A   8      28.174  19.246  66.181  1.00 34.44           C  
ATOM      9  C   LEU A   8      28.990  18.013  65.851  1.00 34.19           C  
ATOM     10  O   LEU A   8      29.780  17.533  66.662  1.00 34.30           O  
ATOM     11  CB  LEU A   8      28.981  20.481  65.774  1.00 33.11           C  
ATOM     12  CG  LEU A   8      28.265  21.777  65.357  1.00 34.77           C  
ATOM     13  CD1 LEU A   8      26.808  21.748  65.733  1.00 33.47           C  
ATOM     14  CD2 LEU A   8      28.973  22.940  66.020  1.00 33.97           C  
ATOM     15  N   SER A   9      28.778  17.508  64.643  1.00 33.04           N  
ATOM     16  CA  SER A   9      29.522  16.367  64.159  1.00 32.60           C  
ATOM     17  C   SER A   9      30.941  16.876  64.006  1.00 31.48           C  
ATOM     18  O   SER A   9      31.176  18.091  63.982  1.00 32.44           O  
ATOM     19  CB  SER A   9      29.033  15.945  62.786  1.00 33.59           C  
ATOM     20  OG  SER A   9      29.348  16.969  61.852  1.00 37.02           O  
ATOM     21  N   ALA A  10      31.878  15.945  63.890  1.00 28.70           N  
ATOM     22  CA  ALA A  10      33.280  16.278  63.730  1.00 27.19           C  
ATOM     23  C   ALA A  10      33.495  17.236  62.561  1.00 24.20           C  
ATOM     24  O   ALA A  10      34.243  18.204  62.671  1.00 23.53           O  
ATOM     25  CB  ALA A  10      34.079  15.000  63.504  1.00 28.47           C  
ATOM     26  N   ALA A  11      32.843  16.935  61.443  1.00 23.69           N  
ATOM     27  CA  ALA A  11      32.951  17.730  60.226  1.00 22.48           C  
ATOM     28  C   ALA A  11      32.541  19.186  60.463  1.00 22.75           C  
ATOM     29  O   ALA A  11      33.278  20.116  60.135  1.00 24.43           O  
ATOM     30  CB  ALA A  11      32.093  17.117  59.150  1.00 20.57           C  
ATOM     31  N   ALA A  12      31.366  19.375  61.047  1.00 22.12           N  
ATOM     32  CA  ALA A  12      30.859  20.709  61.323  1.00 21.96           C  
ATOM     33  C   ALA A  12      31.827  21.436  62.244  1.00 21.97           C  
ATOM     34  O   ALA A  12      32.158  22.595  62.023  1.00 19.10           O  
ATOM     35  CB  ALA A  12      29.482  20.612  61.962  1.00 21.45           C  
ATOM     36  N   GLN A  13      32.293  20.722  63.262  1.00 22.94           N  
ATOM     37  CA  GLN A  13      33.225  21.258  64.246  1.00 23.72           C  
ATOM     38  C   GLN A  13      34.554  21.663  63.578  1.00 23.16           C  
ATOM     39  O   GLN A  13      35.245  22.584  64.038  1.00 21.75           O  
ATOM     40  CB  GLN A  13      33.449  20.199  65.339  1.00 26.78           C  
ATOM     41  CG  GLN A  13      33.697  20.768  66.731  1.00 33.61           C  
ATOM     42  CD  GLN A  13      33.260  19.838  67.877  1.00 36.19           C  
ATOM     43  OE1 GLN A  13      33.368  20.209  69.049  1.00 38.03           O  
ATOM     44  NE2 GLN A  13      32.764  18.641  67.545  1.00 36.42           N  
ATOM     45  N   ALA A  14      34.900  20.980  62.488  1.00 20.13           N  
ATOM     46  CA  ALA A  14      36.126  21.278  61.746  1.00 19.62           C  
ATOM     47  C   ALA A  14      35.962  22.587  60.958  1.00 18.35           C  
ATOM     48  O   ALA A  14      36.914  23.358  60.792  1.00 17.44           O  
ATOM     49  CB  ALA A  14      36.452  20.128  60.789  1.00 19.65           C  
ATOM     50  N   CYS A  15      34.751  22.820  60.466  1.00 17.73           N  
ATOM     51  CA  CYS A  15      34.435  24.042  59.733  1.00 17.99           C  
ATOM     52  C   CYS A  15      34.503  25.217  60.698  1.00 17.76           C  
ATOM     53  O   CYS A  15      35.086  26.257  60.395  1.00 19.34           O  
ATOM     54  CB  CYS A  15      33.032  23.948  59.137  1.00 18.04           C  
ATOM     55  SG  CYS A  15      32.863  22.750  57.795  1.00 19.47           S  
ATOM     56  N   VAL A  16      33.892  25.050  61.864  1.00 17.81           N  
ATOM     57  CA  VAL A  16      33.909  26.087  62.885  1.00 19.03           C  
ATOM     58  C   VAL A  16      35.356  26.429  63.227  1.00 20.24           C  
ATOM     59  O   VAL A  16      35.742  27.595  63.266  1.00 21.14           O  
ATOM     60  CB  VAL A  16      33.203  25.603  64.166  1.00 19.27           C  
ATOM     61  CG1 VAL A  16      33.592  26.482  65.350  1.00 16.54           C  
ATOM     62  CG2 VAL A  16      31.699  25.610  63.947  1.00 19.24           C  
ATOM     63  N   LYS A  17      36.159  25.398  63.464  1.00 22.04           N  
ATOM     64  CA  LYS A  17      37.558  25.603  63.812  1.00 21.92           C  
ATOM     65  C   LYS A  17      38.295  26.324  62.689  1.00 21.56           C  
ATOM     66  O   LYS A  17      39.076  27.252  62.938  1.00 22.47           O  
ATOM     67  CB  LYS A  17      38.240  24.267  64.095  1.00 24.59           C  
ATOM     68  CG  LYS A  17      39.695  24.436  64.507  1.00 30.57           C  
ATOM     69  CD  LYS A  17      40.392  23.104  64.708  1.00 32.33           C  
ATOM     70  CE  LYS A  17      41.811  23.318  65.222  1.00 36.11           C  
ATOM     71  NZ  LYS A  17      42.619  24.215  64.343  1.00 36.99           N  
ATOM     72  N   LYS A  18      38.052  25.904  61.451  1.00 19.33           N  
ATOM     73  CA  LYS A  18      38.707  26.549  60.323  1.00 17.24           C  
ATOM     74  C   LYS A  18      38.295  28.024  60.239  1.00 18.21           C  
ATOM     75  O   LYS A  18      39.125  28.892  59.984  1.00 16.22           O  
ATOM     76  CB  LYS A  18      38.347  25.846  59.009  1.00 17.79           C  
ATOM     77  CG  LYS A  18      39.226  26.302  57.838  1.00 17.68           C  
ATOM     78  CD  LYS A  18      38.958  25.568  56.522  1.00 16.01           C  
ATOM     79  CE  LYS A  18      39.974  26.053  55.478  1.00 17.72           C  
ATOM     80  NZ  LYS A  18      39.783  25.494  54.115  1.00 18.21           N  
HETATM   81  N   MSE A  19      37.010  28.300  60.453  1.00 17.59           N  
HETATM   82  CA  MSE A  19      36.512  29.668  60.387  1.00 18.52           C  
HETATM   83  C   MSE A  19      37.020  30.526  61.538  1.00 18.69           C  
HETATM   84  O   MSE A  19      37.300  31.706  61.352  1.00 17.26           O  
HETATM   85  CB  MSE A  19      34.980  29.664  60.345  1.00 19.72           C  
HETATM   86  CG  MSE A  19      34.444  29.067  59.045  1.00 19.14           C  
HETATM   87 SE   MSE A  19      32.547  28.683  59.051  1.00 25.09          SE  
HETATM   88  CE  MSE A  19      31.865  30.334  58.375  1.00 12.67           C  
ATOM     89  N   ARG A  20      37.139  29.940  62.725  1.00 20.39           N  
ATOM     90  CA  ARG A  20      37.652  30.687  63.866  1.00 22.06           C  
ATOM     91  C   ARG A  20      39.101  31.044  63.573  1.00 22.36           C  
ATOM     92  O   ARG A  20      39.500  32.203  63.685  1.00 21.27           O  
ATOM     93  CB  ARG A  20      37.585  29.856  65.142  1.00 21.73           C  
ATOM     94  CG  ARG A  20      36.195  29.725  65.713  1.00 24.17           C  
ATOM     95  CD  ARG A  20      35.907  30.797  66.742  1.00 25.99           C  
ATOM     96  NE  ARG A  20      34.510  30.766  67.182  1.00 28.53           N  
ATOM     97  CZ  ARG A  20      33.904  29.711  67.719  1.00 27.42           C  
ATOM     98  NH1 ARG A  20      34.566  28.578  67.895  1.00 30.87           N  
ATOM     99  NH2 ARG A  20      32.629  29.780  68.073  1.00 27.01           N  
ATOM    100  N   ASP A  21      39.887  30.048  63.178  1.00 24.06           N  
ATOM    101  CA  ASP A  21      41.296  30.288  62.874  1.00 25.71           C  
ATOM    102  C   ASP A  21      41.459  31.405  61.850  1.00 25.45           C  
ATOM    103  O   ASP A  21      42.364  32.224  61.952  1.00 23.72           O  
ATOM    104  CB  ASP A  21      41.964  29.026  62.325  1.00 29.31           C  
ATOM    105  CG  ASP A  21      42.044  27.905  63.345  1.00 32.80           C  
ATOM    106  OD1 ASP A  21      42.139  28.195  64.558  1.00 33.18           O  
ATOM    107  OD2 ASP A  21      42.040  26.724  62.923  1.00 35.98           O  
ATOM    108  N   ALA A  22      40.572  31.441  60.863  1.00 24.10           N  
ATOM    109  CA  ALA A  22      40.660  32.455  59.832  1.00 23.26           C  
ATOM    110  C   ALA A  22      39.993  33.759  60.249  1.00 24.15           C  
ATOM    111  O   ALA A  22      39.814  34.664  59.428  1.00 24.85           O  
ATOM    112  CB  ALA A  22      40.056  31.938  58.548  1.00 24.12           C  
ATOM    113  N   LYS A  23      39.639  33.853  61.525  1.00 23.45           N  
ATOM    114  CA  LYS A  23      39.012  35.056  62.073  1.00 25.20           C  
ATOM    115  C   LYS A  23      37.673  35.404  61.441  1.00 23.98           C  
ATOM    116  O   LYS A  23      37.327  36.580  61.315  1.00 22.84           O  
ATOM    117  CB  LYS A  23      39.935  36.280  61.922  1.00 26.95           C  
ATOM    118  CG  LYS A  23      41.362  36.085  62.407  1.00 30.58           C  
ATOM    119  CD  LYS A  23      41.428  35.875  63.913  1.00 33.56           C  
ATOM    120  CE  LYS A  23      42.878  35.913  64.401  1.00 36.63           C  
ATOM    121  NZ  LYS A  23      43.565  37.203  64.053  1.00 36.26           N  
ATOM    122  N   VAL A  24      36.915  34.398  61.033  1.00 23.44           N  
ATOM    123  CA  VAL A  24      35.628  34.682  60.433  1.00 21.75           C  
ATOM    124  C   VAL A  24      34.694  35.175  61.524  1.00 23.46           C  
ATOM    125  O   VAL A  24      34.725  34.698  62.661  1.00 22.98           O  
ATOM    126  CB  VAL A  24      35.034  33.449  59.757  1.00 19.81           C  
ATOM    127  CG1 VAL A  24      33.615  33.725  59.336  1.00 15.35           C  
ATOM    128  CG2 VAL A  24      35.863  33.105  58.538  1.00 21.59           C  
ATOM    129  N   ASN A  25      33.890  36.163  61.164  1.00 23.46           N  
ATOM    130  CA  ASN A  25      32.934  36.779  62.060  1.00 24.77           C  
ATOM    131  C   ASN A  25      32.029  35.704  62.678  1.00 22.75           C  
ATOM    132  O   ASN A  25      31.584  34.788  61.983  1.00 21.17           O  
ATOM    133  CB  ASN A  25      32.127  37.803  61.248  1.00 27.56           C  
ATOM    134  CG  ASN A  25      31.134  38.538  62.076  1.00 30.60           C  
ATOM    135  OD1 ASN A  25      30.089  38.001  62.425  1.00 34.30           O  
ATOM    136  ND2 ASN A  25      31.450  39.783  62.410  1.00 33.64           N  
ATOM    137  N   GLU A  26      31.765  35.816  63.980  1.00 21.07           N  
ATOM    138  CA  GLU A  26      30.931  34.835  64.682  1.00 20.83           C  
ATOM    139  C   GLU A  26      29.543  34.649  64.103  1.00 18.94           C  
ATOM    140  O   GLU A  26      29.036  33.536  64.069  1.00 19.64           O  
ATOM    141  CB  GLU A  26      30.791  35.192  66.166  1.00 20.84           C  
ATOM    142  CG  GLU A  26      31.958  34.728  67.027  1.00 21.51           C  
ATOM    143  CD  GLU A  26      32.286  33.259  66.812  1.00 24.44           C  
ATOM    144  OE1 GLU A  26      31.372  32.399  66.922  1.00 25.63           O  
ATOM    145  OE2 GLU A  26      33.466  32.967  66.532  1.00 24.41           O  
ATOM    146  N   ALA A  27      28.920  35.746  63.680  1.00 17.65           N  
ATOM    147  CA  ALA A  27      27.578  35.698  63.098  1.00 16.27           C  
ATOM    148  C   ALA A  27      27.576  34.861  61.835  1.00 13.75           C  
ATOM    149  O   ALA A  27      26.645  34.111  61.581  1.00 13.82           O  
ATOM    150  CB  ALA A  27      27.086  37.113  62.777  1.00 15.15           C  
ATOM    151  N   CYS A  28      28.621  35.005  61.037  1.00 14.40           N  
ATOM    152  CA  CYS A  28      28.727  34.254  59.797  1.00 16.73           C  
ATOM    153  C   CYS A  28      28.904  32.770  60.099  1.00 16.84           C  
ATOM    154  O   CYS A  28      28.342  31.918  59.406  1.00 16.84           O  
ATOM    155  CB  CYS A  28      29.900  34.765  58.959  1.00 18.11           C  
ATOM    156  SG  CYS A  28      30.248  33.724  57.526  1.00 18.28           S  
ATOM    157  N   ILE A  29      29.663  32.470  61.144  1.00 16.62           N  
ATOM    158  CA  ILE A  29      29.894  31.077  61.531  1.00 18.05           C  
ATOM    159  C   ILE A  29      28.595  30.447  62.018  1.00 18.61           C  
ATOM    160  O   ILE A  29      28.236  29.338  61.595  1.00 15.56           O  
ATOM    161  CB  ILE A  29      30.956  30.965  62.658  1.00 18.26           C  
ATOM    162  CG1 ILE A  29      32.309  31.481  62.150  1.00 19.54           C  
ATOM    163  CG2 ILE A  29      31.065  29.511  63.135  1.00 19.66           C  
ATOM    164  CD1 ILE A  29      33.422  31.537  63.222  1.00 18.39           C  
ATOM    165  N   ARG A  30      27.885  31.152  62.903  1.00 18.18           N  
ATOM    166  CA  ARG A  30      26.625  30.627  63.411  1.00 17.93           C  
ATOM    167  C   ARG A  30      25.671  30.382  62.252  1.00 18.13           C  
ATOM    168  O   ARG A  30      24.983  29.375  62.216  1.00 20.11           O  
ATOM    169  CB  ARG A  30      25.974  31.603  64.410  1.00 20.92           C  
ATOM    170  CG  ARG A  30      26.646  31.666  65.794  1.00 23.40           C  
ATOM    171  CD  ARG A  30      25.740  32.357  66.838  1.00 24.56           C  
ATOM    172  NE  ARG A  30      25.415  33.730  66.462  1.00 24.17           N  
ATOM    173  CZ  ARG A  30      26.197  34.777  66.709  1.00 25.86           C  
ATOM    174  NH1 ARG A  30      27.354  34.619  67.347  1.00 24.09           N  
ATOM    175  NH2 ARG A  30      25.836  35.980  66.290  1.00 27.33           N  
ATOM    176  N   THR A  31      25.631  31.306  61.297  1.00 17.42           N  
ATOM    177  CA  THR A  31      24.734  31.170  60.148  1.00 18.05           C  
ATOM    178  C   THR A  31      25.140  30.003  59.250  1.00 17.04           C  
ATOM    179  O   THR A  31      24.298  29.191  58.850  1.00 16.97           O  
ATOM    180  CB  THR A  31      24.711  32.471  59.324  1.00 18.29           C  
ATOM    181  OG1 THR A  31      24.201  33.528  60.143  1.00 20.38           O  
ATOM    182  CG2 THR A  31      23.848  32.326  58.087  1.00 16.58           C  
ATOM    183  N   PHE A  32      26.427  29.917  58.940  1.00 16.42           N  
ATOM    184  CA  PHE A  32      26.922  28.835  58.095  1.00 16.81           C  
ATOM    185  C   PHE A  32      26.700  27.467  58.754  1.00 16.73           C  
ATOM    186  O   PHE A  32      26.276  26.521  58.107  1.00 17.60           O  
ATOM    187  CB  PHE A  32      28.408  29.019  57.812  1.00 14.80           C  
ATOM    188  CG  PHE A  32      29.043  27.845  57.099  1.00 12.88           C  
ATOM    189  CD1 PHE A  32      29.003  27.750  55.708  1.00 12.55           C  
ATOM    190  CD2 PHE A  32      29.674  26.827  57.829  1.00 12.49           C  
ATOM    191  CE1 PHE A  32      29.580  26.652  55.043  1.00 11.31           C  
ATOM    192  CE2 PHE A  32      30.255  25.732  57.188  1.00  8.77           C  
ATOM    193  CZ  PHE A  32      30.203  25.648  55.779  1.00 10.27           C  
ATOM    194  N   ILE A  33      26.982  27.373  60.043  1.00 16.71           N  
ATOM    195  CA  ILE A  33      26.824  26.113  60.755  1.00 17.88           C  
ATOM    196  C   ILE A  33      25.390  25.583  60.744  1.00 18.45           C  
ATOM    197  O   ILE A  33      25.167  24.390  60.552  1.00 16.70           O  
ATOM    198  CB  ILE A  33      27.313  26.266  62.194  1.00 17.21           C  
ATOM    199  CG1 ILE A  33      28.842  26.385  62.197  1.00 18.98           C  
ATOM    200  CG2 ILE A  33      26.803  25.126  63.048  1.00 23.48           C  
ATOM    201  CD1 ILE A  33      29.583  25.213  61.556  1.00 21.15           C  
ATOM    202  N   ALA A  34      24.420  26.468  60.956  1.00 17.92           N  
ATOM    203  CA  ALA A  34      23.016  26.062  60.951  1.00 18.54           C  
ATOM    204  C   ALA A  34      22.667  25.511  59.575  1.00 17.62           C  
ATOM    205  O   ALA A  34      21.812  24.629  59.437  1.00 19.41           O  
ATOM    206  CB  ALA A  34      22.107  27.255  61.304  1.00 17.32           C  
ATOM    207  N   GLN A  35      23.332  26.029  58.550  1.00 17.74           N  
ATOM    208  CA  GLN A  35      23.101  25.549  57.191  1.00 16.53           C  
ATOM    209  C   GLN A  35      23.744  24.160  57.038  1.00 16.92           C  
ATOM    210  O   GLN A  35      23.180  23.271  56.405  1.00 18.40           O  
ATOM    211  CB  GLN A  35      23.717  26.517  56.180  1.00 15.85           C  
ATOM    212  CG  GLN A  35      23.025  27.874  56.078  1.00 15.65           C  
ATOM    213  CD  GLN A  35      23.787  28.845  55.179  1.00 17.68           C  
ATOM    214  OE1 GLN A  35      23.323  29.952  54.899  1.00 20.89           O  
ATOM    215  NE2 GLN A  35      24.968  28.434  54.731  1.00 16.83           N  
ATOM    216  N   HIS A  36      24.933  24.004  57.611  1.00 16.68           N  
ATOM    217  CA  HIS A  36      25.684  22.751  57.583  1.00 19.43           C  
ATOM    218  C   HIS A  36      24.878  21.659  58.299  1.00 20.51           C  
ATOM    219  O   HIS A  36      24.873  20.504  57.878  1.00 21.88           O  
ATOM    220  CB  HIS A  36      27.036  22.956  58.274  1.00 17.18           C  
ATOM    221  CG  HIS A  36      28.036  21.878  58.003  1.00 17.75           C  
ATOM    222  ND1 HIS A  36      27.945  20.616  58.551  1.00 17.25           N  
ATOM    223  CD2 HIS A  36      29.174  21.888  57.270  1.00 17.74           C  
ATOM    224  CE1 HIS A  36      28.986  19.898  58.173  1.00 15.59           C  
ATOM    225  NE2 HIS A  36      29.747  20.645  57.395  1.00 15.66           N  
ATOM    226  N   VAL A  37      24.193  22.029  59.380  1.00 22.89           N  
ATOM    227  CA  VAL A  37      23.378  21.076  60.117  1.00 23.26           C  
ATOM    228  C   VAL A  37      22.260  20.578  59.202  1.00 25.87           C  
ATOM    229  O   VAL A  37      21.957  19.382  59.172  1.00 26.05           O  
ATOM    230  CB  VAL A  37      22.751  21.719  61.367  1.00 24.44           C  
ATOM    231  CG1 VAL A  37      21.795  20.732  62.037  1.00 22.55           C  
ATOM    232  CG2 VAL A  37      23.846  22.138  62.345  1.00 24.32           C  
HETATM  233  N   MSE A  38      21.654  21.501  58.457  1.00 26.72           N  
HETATM  234  CA  MSE A  38      20.584  21.154  57.532  1.00 29.05           C  
HETATM  235  C   MSE A  38      21.109  20.169  56.495  1.00 27.96           C  
HETATM  236  O   MSE A  38      20.579  19.074  56.347  1.00 28.27           O  
HETATM  237  CB  MSE A  38      20.050  22.400  56.816  1.00 32.24           C  
HETATM  238  CG  MSE A  38      19.347  23.426  57.716  1.00 39.81           C  
HETATM  239 SE   MSE A  38      17.692  22.790  58.531  1.00 50.98          SE  
HETATM  240  CE  MSE A  38      18.360  22.161  60.235  1.00 47.14           C  
ATOM    241  N   VAL A  39      22.157  20.565  55.784  1.00 26.36           N  
ATOM    242  CA  VAL A  39      22.739  19.718  54.761  1.00 25.80           C  
ATOM    243  C   VAL A  39      23.043  18.304  55.269  1.00 24.80           C  
ATOM    244  O   VAL A  39      22.654  17.326  54.644  1.00 24.54           O  
ATOM    245  CB  VAL A  39      24.016  20.368  54.180  1.00 25.93           C  
ATOM    246  CG1 VAL A  39      24.773  19.370  53.286  1.00 24.87           C  
ATOM    247  CG2 VAL A  39      23.622  21.589  53.355  1.00 25.49           C  
ATOM    248  N   SER A  40      23.729  18.204  56.399  1.00 26.26           N  
ATOM    249  CA  SER A  40      24.060  16.905  56.986  1.00 29.32           C  
ATOM    250  C   SER A  40      22.820  16.034  57.222  1.00 31.57           C  
ATOM    251  O   SER A  40      22.919  14.803  57.276  1.00 33.39           O  
ATOM    252  CB  SER A  40      24.797  17.102  58.306  1.00 28.70           C  
ATOM    253  OG  SER A  40      24.043  17.904  59.194  1.00 29.92           O  
ATOM    254  N   LYS A  41      21.660  16.670  57.360  1.00 32.20           N  
ATOM    255  CA  LYS A  41      20.417  15.940  57.580  1.00 33.68           C  
ATOM    256  C   LYS A  41      19.656  15.596  56.307  1.00 33.30           C  
ATOM    257  O   LYS A  41      18.566  15.042  56.376  1.00 32.99           O  
ATOM    258  CB  LYS A  41      19.497  16.706  58.530  1.00 33.05           C  
ATOM    259  CG  LYS A  41      19.872  16.493  59.985  1.00 36.22           C  
ATOM    260  CD  LYS A  41      18.799  16.999  60.944  1.00 39.26           C  
ATOM    261  CE  LYS A  41      18.865  18.509  61.128  1.00 42.04           C  
ATOM    262  NZ  LYS A  41      18.013  18.972  62.263  1.00 42.68           N  
ATOM    263  N   GLY A  42      20.226  15.917  55.149  1.00 32.75           N  
ATOM    264  CA  GLY A  42      19.551  15.600  53.899  1.00 32.75           C  
ATOM    265  C   GLY A  42      19.019  16.779  53.098  1.00 31.99           C  
ATOM    266  O   GLY A  42      18.652  16.618  51.937  1.00 30.24           O  
ATOM    267  N   GLU A  43      18.964  17.958  53.709  1.00 32.12           N  
ATOM    268  CA  GLU A  43      18.480  19.151  53.009  1.00 33.21           C  
ATOM    269  C   GLU A  43      19.323  19.401  51.762  1.00 34.01           C  
ATOM    270  O   GLU A  43      20.538  19.588  51.870  1.00 34.19           O  
ATOM    271  CB  GLU A  43      18.580  20.372  53.919  1.00 34.02           C  
ATOM    272  CG  GLU A  43      18.102  21.668  53.285  1.00 35.37           C  
ATOM    273  CD  GLU A  43      16.644  21.605  52.884  1.00 36.80           C  
ATOM    274  OE1 GLU A  43      16.354  21.428  51.679  1.00 34.77           O  
ATOM    275  OE2 GLU A  43      15.783  21.715  53.785  1.00 38.04           O  
ATOM    276  N   THR A  44      18.684  19.412  50.590  1.00 34.34           N  
ATOM    277  CA  THR A  44      19.383  19.648  49.319  1.00 34.55           C  
ATOM    278  C   THR A  44      19.177  21.086  48.865  1.00 34.65           C  
ATOM    279  O   THR A  44      19.927  21.602  48.029  1.00 36.54           O  
ATOM    280  CB  THR A  44      18.858  18.737  48.191  1.00 35.15           C  
ATOM    281  OG1 THR A  44      17.479  19.040  47.947  1.00 33.88           O  
ATOM    282  CG2 THR A  44      18.983  17.260  48.580  1.00 35.93           C  
ATOM    283  N   GLY A  45      18.148  21.718  49.417  1.00 33.26           N  
ATOM    284  CA  GLY A  45      17.840  23.092  49.077  1.00 33.14           C  
ATOM    285  C   GLY A  45      16.666  23.181  48.125  1.00 32.96           C  
ATOM    286  O   GLY A  45      16.043  24.240  47.995  1.00 32.85           O  
ATOM    287  N   SER A  46      16.354  22.059  47.477  1.00 31.34           N  
ATOM    288  CA  SER A  46      15.269  21.995  46.505  1.00 30.55           C  
ATOM    289  C   SER A  46      13.886  22.240  47.096  1.00 28.44           C  
ATOM    290  O   SER A  46      13.582  21.846  48.222  1.00 28.60           O  
ATOM    291  CB  SER A  46      15.289  20.636  45.779  1.00 31.72           C  
ATOM    292  OG  SER A  46      14.270  19.767  46.254  1.00 32.39           O  
ATOM    293  N   ILE A  47      13.058  22.921  46.319  1.00 26.73           N  
ATOM    294  CA  ILE A  47      11.684  23.232  46.701  1.00 25.92           C  
ATOM    295  C   ILE A  47      10.833  22.624  45.576  1.00 26.08           C  
ATOM    296  O   ILE A  47      10.744  23.181  44.476  1.00 23.97           O  
ATOM    297  CB  ILE A  47      11.468  24.774  46.782  1.00 26.02           C  
ATOM    298  CG1 ILE A  47      12.334  25.363  47.913  1.00 25.44           C  
ATOM    299  CG2 ILE A  47       9.978  25.087  46.979  1.00 24.49           C  
ATOM    300  CD1 ILE A  47      12.374  26.897  47.952  1.00 25.39           C  
ATOM    301  N   PRO A  48      10.230  21.451  45.830  1.00 25.76           N  
ATOM    302  CA  PRO A  48       9.413  20.807  44.799  1.00 26.27           C  
ATOM    303  C   PRO A  48       8.120  21.524  44.469  1.00 26.49           C  
ATOM    304  O   PRO A  48       7.530  22.188  45.312  1.00 26.47           O  
ATOM    305  CB  PRO A  48       9.175  19.410  45.368  1.00 26.66           C  
ATOM    306  CG  PRO A  48       9.126  19.675  46.883  1.00 25.62           C  
ATOM    307  CD  PRO A  48      10.293  20.630  47.058  1.00 25.05           C  
ATOM    308  N   ASP A  49       7.697  21.375  43.222  1.00 28.70           N  
ATOM    309  CA  ASP A  49       6.468  21.971  42.722  1.00 31.50           C  
ATOM    310  C   ASP A  49       5.248  21.618  43.575  1.00 30.78           C  
ATOM    311  O   ASP A  49       4.345  22.440  43.745  1.00 29.86           O  
ATOM    312  CB  ASP A  49       6.235  21.498  41.284  1.00 34.66           C  
ATOM    313  CG  ASP A  49       6.145  22.639  40.302  1.00 38.83           C  
ATOM    314  OD1 ASP A  49       5.009  23.105  40.063  1.00 42.26           O  
ATOM    315  OD2 ASP A  49       7.204  23.074  39.783  1.00 40.35           O  
ATOM    316  N   SER A  50       5.229  20.402  44.115  1.00 30.96           N  
ATOM    317  CA  SER A  50       4.102  19.941  44.924  1.00 31.51           C  
ATOM    318  C   SER A  50       4.004  20.695  46.245  1.00 30.69           C  
ATOM    319  O   SER A  50       2.950  20.707  46.888  1.00 31.99           O  
ATOM    320  CB  SER A  50       4.233  18.435  45.211  1.00 32.14           C  
ATOM    321  OG  SER A  50       5.239  18.173  46.178  1.00 30.30           O  
ATOM    322  N   ALA A  51       5.101  21.333  46.637  1.00 28.79           N  
ATOM    323  CA  ALA A  51       5.139  22.057  47.898  1.00 27.11           C  
ATOM    324  C   ALA A  51       4.792  23.540  47.818  1.00 26.73           C  
ATOM    325  O   ALA A  51       4.754  24.217  48.847  1.00 27.28           O  
ATOM    326  CB  ALA A  51       6.510  21.880  48.540  1.00 26.19           C  
ATOM    327  N   ILE A  52       4.539  24.051  46.617  1.00 26.08           N  
ATOM    328  CA  ILE A  52       4.218  25.468  46.465  1.00 26.09           C  
ATOM    329  C   ILE A  52       3.027  25.736  45.541  1.00 28.02           C  
ATOM    330  O   ILE A  52       2.571  24.848  44.834  1.00 27.59           O  
ATOM    331  CB  ILE A  52       5.445  26.263  45.940  1.00 24.24           C  
ATOM    332  CG1 ILE A  52       5.879  25.722  44.572  1.00 22.06           C  
ATOM    333  CG2 ILE A  52       6.585  26.173  46.949  1.00 21.41           C  
ATOM    334  CD1 ILE A  52       6.963  26.560  43.903  1.00 19.61           C  
HETATM  335  N   MSE A  53       2.534  26.972  45.554  1.00 30.66           N  
HETATM  336  CA  MSE A  53       1.392  27.354  44.732  1.00 34.27           C  
HETATM  337  C   MSE A  53       1.604  28.756  44.142  1.00 33.27           C  
HETATM  338  O   MSE A  53       2.358  29.556  44.685  1.00 31.92           O  
HETATM  339  CB  MSE A  53       0.117  27.314  45.581  1.00 40.32           C  
HETATM  340  CG  MSE A  53      -1.109  26.733  44.861  1.00 49.48           C  
HETATM  341 SE   MSE A  53      -1.094  24.794  44.546  1.00 61.17          SE  
HETATM  342  CE  MSE A  53      -0.038  24.700  42.931  1.00 56.43           C  
ATOM    343  N   PRO A  54       0.941  29.069  43.017  1.00 32.80           N  
ATOM    344  CA  PRO A  54       1.111  30.393  42.406  1.00 32.08           C  
ATOM    345  C   PRO A  54       0.484  31.524  43.212  1.00 31.26           C  
ATOM    346  O   PRO A  54      -0.399  31.300  44.044  1.00 30.42           O  
ATOM    347  CB  PRO A  54       0.439  30.248  41.035  1.00 32.79           C  
ATOM    348  CG  PRO A  54       0.356  28.746  40.819  1.00 35.20           C  
ATOM    349  CD  PRO A  54       0.070  28.219  42.190  1.00 32.69           C  
ATOM    350  N   VAL A  55       0.958  32.739  42.953  1.00 30.59           N  
ATOM    351  CA  VAL A  55       0.457  33.943  43.609  1.00 29.47           C  
ATOM    352  C   VAL A  55      -0.439  34.600  42.581  1.00 30.15           C  
ATOM    353  O   VAL A  55       0.026  34.928  41.486  1.00 30.14           O  
ATOM    354  CB  VAL A  55       1.603  34.896  43.948  1.00 28.19           C  
ATOM    355  CG1 VAL A  55       1.050  36.237  44.397  1.00 25.57           C  
ATOM    356  CG2 VAL A  55       2.483  34.270  45.026  1.00 27.03           C  
ATOM    357  N   ASP A  56      -1.711  34.795  42.918  1.00 30.97           N  
ATOM    358  CA  ASP A  56      -2.652  35.381  41.958  1.00 32.32           C  
ATOM    359  C   ASP A  56      -3.070  36.809  42.209  1.00 32.62           C  
ATOM    360  O   ASP A  56      -3.800  37.393  41.401  1.00 36.14           O  
ATOM    361  CB  ASP A  56      -3.933  34.548  41.873  1.00 33.48           C  
ATOM    362  CG  ASP A  56      -3.677  33.133  41.430  1.00 35.68           C  
ATOM    363  OD1 ASP A  56      -2.889  32.948  40.480  1.00 36.92           O  
ATOM    364  OD2 ASP A  56      -4.273  32.207  42.027  1.00 37.61           O  
ATOM    365  N   SER A  57      -2.629  37.394  43.309  1.00 30.19           N  
ATOM    366  CA  SER A  57      -3.068  38.740  43.571  1.00 27.68           C  
ATOM    367  C   SER A  57      -2.086  39.554  44.391  1.00 26.25           C  
ATOM    368  O   SER A  57      -1.801  39.213  45.542  1.00 25.36           O  
ATOM    369  CB  SER A  57      -4.427  38.671  44.275  1.00 28.75           C  
ATOM    370  OG  SER A  57      -4.954  39.956  44.520  1.00 31.58           O  
ATOM    371  N   LEU A  58      -1.575  40.628  43.790  1.00 21.43           N  
ATOM    372  CA  LEU A  58      -0.656  41.530  44.466  1.00 19.86           C  
ATOM    373  C   LEU A  58      -1.038  42.965  44.132  1.00 19.96           C  
ATOM    374  O   LEU A  58      -1.589  43.230  43.062  1.00 18.80           O  
ATOM    375  CB  LEU A  58       0.787  41.288  44.009  1.00 18.18           C  
ATOM    376  CG  LEU A  58       1.391  39.918  44.339  1.00 18.36           C  
ATOM    377  CD1 LEU A  58       2.791  39.813  43.758  1.00 15.03           C  
ATOM    378  CD2 LEU A  58       1.406  39.722  45.840  1.00 12.29           C  
ATOM    379  N   ASP A  59      -0.760  43.894  45.041  1.00 20.05           N  
ATOM    380  CA  ASP A  59      -1.045  45.297  44.750  1.00 20.20           C  
ATOM    381  C   ASP A  59      -0.030  45.685  43.688  1.00 18.99           C  
ATOM    382  O   ASP A  59       0.987  45.013  43.526  1.00 19.12           O  
ATOM    383  CB  ASP A  59      -0.861  46.195  45.983  1.00 21.79           C  
ATOM    384  CG  ASP A  59      -2.003  46.074  46.977  1.00 23.38           C  
ATOM    385  OD1 ASP A  59      -3.131  45.779  46.535  1.00 28.14           O  
ATOM    386  OD2 ASP A  59      -1.786  46.287  48.194  1.00 22.88           O  
ATOM    387  N   ALA A  60      -0.301  46.766  42.971  1.00 19.08           N  
ATOM    388  CA  ALA A  60       0.598  47.218  41.926  1.00 19.52           C  
ATOM    389  C   ALA A  60       1.127  48.608  42.232  1.00 20.32           C  
ATOM    390  O   ALA A  60       0.388  49.492  42.676  1.00 20.92           O  
ATOM    391  CB  ALA A  60      -0.126  47.206  40.571  1.00 19.30           C  
ATOM    392  N   LEU A  61       2.418  48.802  42.004  1.00 20.72           N  
ATOM    393  CA  LEU A  61       3.021  50.095  42.269  1.00 22.10           C  
ATOM    394  C   LEU A  61       2.342  51.186  41.429  1.00 23.98           C  
ATOM    395  O   LEU A  61       2.274  52.338  41.852  1.00 23.24           O  
ATOM    396  CB  LEU A  61       4.523  50.025  41.988  1.00 20.20           C  
ATOM    397  CG  LEU A  61       5.473  51.172  42.360  1.00 21.42           C  
ATOM    398  CD1 LEU A  61       5.774  51.973  41.131  1.00 23.29           C  
ATOM    399  CD2 LEU A  61       4.905  52.050  43.445  1.00 20.00           C  
ATOM    400  N   ASP A  62       1.819  50.813  40.259  1.00 25.90           N  
ATOM    401  CA  ASP A  62       1.142  51.753  39.349  1.00 29.14           C  
ATOM    402  C   ASP A  62      -0.114  52.390  39.935  1.00 27.71           C  
ATOM    403  O   ASP A  62      -0.550  53.446  39.479  1.00 28.01           O  
ATOM    404  CB  ASP A  62       0.751  51.049  38.041  1.00 33.84           C  
ATOM    405  CG  ASP A  62       1.935  50.798  37.140  1.00 38.11           C  
ATOM    406  OD1 ASP A  62       1.835  49.923  36.253  1.00 41.30           O  
ATOM    407  OD2 ASP A  62       2.965  51.481  37.310  1.00 41.86           O  
ATOM    408  N   SER A  63      -0.696  51.736  40.932  1.00 26.55           N  
ATOM    409  CA  SER A  63      -1.904  52.231  41.580  1.00 26.95           C  
ATOM    410  C   SER A  63      -1.585  53.202  42.713  1.00 26.96           C  
ATOM    411  O   SER A  63      -2.479  53.869  43.243  1.00 28.03           O  
ATOM    412  CB  SER A  63      -2.698  51.055  42.156  1.00 27.80           C  
ATOM    413  OG  SER A  63      -3.097  50.154  41.149  1.00 27.88           O  
ATOM    414  N   LEU A  64      -0.318  53.273  43.103  1.00 25.11           N  
ATOM    415  CA  LEU A  64       0.070  54.152  44.196  1.00 23.39           C  
ATOM    416  C   LEU A  64       0.316  55.570  43.716  1.00 22.72           C  
ATOM    417  O   LEU A  64       0.678  55.792  42.562  1.00 23.06           O  
ATOM    418  CB  LEU A  64       1.320  53.599  44.887  1.00 23.64           C  
ATOM    419  CG  LEU A  64       1.233  52.144  45.369  1.00 23.44           C  
ATOM    420  CD1 LEU A  64       2.462  51.798  46.195  1.00 20.72           C  
ATOM    421  CD2 LEU A  64      -0.032  51.949  46.193  1.00 23.05           C  
ATOM    422  N   THR A  65       0.122  56.540  44.601  1.00 23.08           N  
ATOM    423  CA  THR A  65       0.328  57.940  44.224  1.00 23.45           C  
ATOM    424  C   THR A  65       0.961  58.774  45.328  1.00 23.26           C  
ATOM    425  O   THR A  65       1.727  59.701  45.055  1.00 22.12           O  
ATOM    426  CB  THR A  65      -1.002  58.609  43.810  1.00 22.69           C  
ATOM    427  OG1 THR A  65      -1.934  58.536  44.900  1.00 24.40           O  
ATOM    428  CG2 THR A  65      -1.591  57.909  42.585  1.00 21.16           C  
ATOM    429  N   ILE A  66       0.651  58.436  46.573  1.00 24.12           N  
ATOM    430  CA  ILE A  66       1.179  59.176  47.712  1.00 26.12           C  
ATOM    431  C   ILE A  66       2.658  58.918  47.983  1.00 27.95           C  
ATOM    432  O   ILE A  66       3.108  57.767  48.022  1.00 27.31           O  
ATOM    433  CB  ILE A  66       0.369  58.867  48.999  1.00 25.80           C  
ATOM    434  CG1 ILE A  66      -1.122  59.123  48.749  1.00 25.43           C  
ATOM    435  CG2 ILE A  66       0.825  59.773  50.136  1.00 26.90           C  
ATOM    436  CD1 ILE A  66      -2.014  58.710  49.892  1.00 25.33           C  
ATOM    437  N   GLU A  67       3.408  60.004  48.159  1.00 29.78           N  
ATOM    438  CA  GLU A  67       4.837  59.921  48.448  1.00 32.66           C  
ATOM    439  C   GLU A  67       5.046  60.030  49.950  1.00 33.36           C  
ATOM    440  O   GLU A  67       4.250  60.665  50.650  1.00 34.63           O  
ATOM    441  CB  GLU A  67       5.607  61.052  47.765  1.00 33.66           C  
ATOM    442  CG  GLU A  67       5.515  61.088  46.252  1.00 37.15           C  
ATOM    443  CD  GLU A  67       6.325  62.236  45.670  1.00 40.28           C  
ATOM    444  OE1 GLU A  67       6.265  63.355  46.236  1.00 40.68           O  
ATOM    445  OE2 GLU A  67       7.017  62.023  44.648  1.00 41.22           O  
ATOM    446  N   CYS A  68       6.121  59.415  50.438  1.00 32.06           N  
ATOM    447  CA  CYS A  68       6.453  59.443  51.861  1.00 31.58           C  
ATOM    448  C   CYS A  68       6.866  60.849  52.303  1.00 32.72           C  
ATOM    449  O   CYS A  68       7.212  61.687  51.471  1.00 31.73           O  
ATOM    450  CB  CYS A  68       7.605  58.471  52.146  1.00 28.34           C  
ATOM    451  SG  CYS A  68       9.188  58.920  51.394  1.00 21.61           S  
ATOM    452  N   ASP A  69       6.843  61.102  53.610  1.00 35.61           N  
ATOM    453  CA  ASP A  69       7.251  62.411  54.128  1.00 38.16           C  
ATOM    454  C   ASP A  69       8.775  62.503  54.184  1.00 38.52           C  
ATOM    455  O   ASP A  69       9.478  61.492  54.070  1.00 38.80           O  
ATOM    456  CB  ASP A  69       6.645  62.678  55.515  1.00 41.03           C  
ATOM    457  CG  ASP A  69       6.972  61.595  56.526  1.00 43.83           C  
ATOM    458  OD1 ASP A  69       8.170  61.294  56.720  1.00 46.48           O  
ATOM    459  OD2 ASP A  69       6.026  61.054  57.140  1.00 45.88           O  
ATOM    460  N   ASN A  70       9.286  63.714  54.353  1.00 37.74           N  
ATOM    461  CA  ASN A  70      10.724  63.929  54.375  1.00 37.18           C  
ATOM    462  C   ASN A  70      11.455  63.051  55.385  1.00 36.01           C  
ATOM    463  O   ASN A  70      12.520  62.500  55.098  1.00 35.11           O  
ATOM    464  CB  ASN A  70      11.030  65.393  54.666  1.00 37.81           C  
ATOM    465  CG  ASN A  70      12.496  65.701  54.530  1.00 40.56           C  
ATOM    466  OD1 ASN A  70      13.147  66.151  55.479  1.00 41.54           O  
ATOM    467  ND2 ASN A  70      13.038  65.449  53.343  1.00 42.06           N  
ATOM    468  N   ALA A  71      10.881  62.936  56.573  1.00 34.18           N  
ATOM    469  CA  ALA A  71      11.476  62.131  57.627  1.00 32.81           C  
ATOM    470  C   ALA A  71      11.783  60.713  57.120  1.00 31.52           C  
ATOM    471  O   ALA A  71      12.936  60.268  57.126  1.00 30.04           O  
ATOM    472  CB  ALA A  71      10.534  62.079  58.818  1.00 30.57           C  
ATOM    473  N   VAL A  72      10.744  60.018  56.671  1.00 30.42           N  
ATOM    474  CA  VAL A  72      10.892  58.661  56.167  1.00 28.05           C  
ATOM    475  C   VAL A  72      11.950  58.565  55.082  1.00 28.64           C  
ATOM    476  O   VAL A  72      12.815  57.681  55.123  1.00 27.44           O  
ATOM    477  CB  VAL A  72       9.560  58.135  55.619  1.00 26.03           C  
ATOM    478  CG1 VAL A  72       9.761  56.794  54.928  1.00 23.68           C  
ATOM    479  CG2 VAL A  72       8.568  57.994  56.769  1.00 25.10           C  
ATOM    480  N   LEU A  73      11.905  59.483  54.124  1.00 27.81           N  
ATOM    481  CA  LEU A  73      12.873  59.442  53.042  1.00 29.03           C  
ATOM    482  C   LEU A  73      14.294  59.591  53.579  1.00 29.57           C  
ATOM    483  O   LEU A  73      15.215  58.896  53.133  1.00 29.23           O  
ATOM    484  CB  LEU A  73      12.586  60.547  52.022  1.00 30.60           C  
ATOM    485  CG  LEU A  73      13.364  60.560  50.691  1.00 32.13           C  
ATOM    486  CD1 LEU A  73      14.813  60.901  50.927  1.00 32.92           C  
ATOM    487  CD2 LEU A  73      13.248  59.207  49.992  1.00 33.16           C  
ATOM    488  N   GLN A  74      14.468  60.486  54.544  1.00 27.74           N  
ATOM    489  CA  GLN A  74      15.785  60.728  55.099  1.00 27.59           C  
ATOM    490  C   GLN A  74      16.338  59.511  55.832  1.00 24.88           C  
ATOM    491  O   GLN A  74      17.549  59.357  55.958  1.00 24.21           O  
ATOM    492  CB  GLN A  74      15.728  61.914  56.054  1.00 31.78           C  
ATOM    493  CG  GLN A  74      16.921  62.814  55.940  1.00 36.31           C  
ATOM    494  CD  GLN A  74      17.035  63.422  54.560  1.00 39.44           C  
ATOM    495  OE1 GLN A  74      16.099  64.054  54.057  1.00 40.96           O  
ATOM    496  NE2 GLN A  74      18.188  63.239  53.940  1.00 40.41           N  
ATOM    497  N   SER A  75      15.446  58.642  56.290  1.00 21.13           N  
ATOM    498  CA  SER A  75      15.834  57.460  57.043  1.00 20.20           C  
ATOM    499  C   SER A  75      16.082  56.251  56.153  1.00 19.79           C  
ATOM    500  O   SER A  75      16.169  55.131  56.660  1.00 19.25           O  
ATOM    501  CB  SER A  75      14.727  57.106  58.035  1.00 21.24           C  
ATOM    502  OG  SER A  75      13.536  56.744  57.348  1.00 20.30           O  
ATOM    503  N   THR A  76      16.197  56.482  54.842  1.00 18.11           N  
ATOM    504  CA  THR A  76      16.393  55.401  53.886  1.00 16.51           C  
ATOM    505  C   THR A  76      17.804  55.291  53.334  1.00 16.67           C  
ATOM    506  O   THR A  76      18.361  56.252  52.802  1.00 19.84           O  
ATOM    507  CB  THR A  76      15.392  55.533  52.699  1.00 17.00           C  
ATOM    508  OG1 THR A  76      14.057  55.601  53.216  1.00 15.73           O  
ATOM    509  CG2 THR A  76      15.478  54.321  51.756  1.00 15.64           C  
ATOM    510  N   VAL A  77      18.376  54.102  53.472  1.00 15.07           N  
ATOM    511  CA  VAL A  77      19.713  53.797  52.967  1.00 13.34           C  
ATOM    512  C   VAL A  77      19.610  53.064  51.620  1.00 11.48           C  
ATOM    513  O   VAL A  77      18.710  52.241  51.434  1.00  8.79           O  
ATOM    514  CB  VAL A  77      20.468  52.850  53.915  1.00 14.59           C  
ATOM    515  CG1 VAL A  77      21.851  52.536  53.343  1.00 17.15           C  
ATOM    516  CG2 VAL A  77      20.591  53.468  55.281  1.00 17.70           C  
ATOM    517  N   VAL A  78      20.534  53.355  50.704  1.00  9.39           N  
ATOM    518  CA  VAL A  78      20.567  52.706  49.404  1.00 11.40           C  
ATOM    519  C   VAL A  78      21.786  51.777  49.317  1.00 12.56           C  
ATOM    520  O   VAL A  78      22.914  52.180  49.603  1.00 11.29           O  
ATOM    521  CB  VAL A  78      20.689  53.719  48.241  1.00 12.60           C  
ATOM    522  CG1 VAL A  78      20.885  52.955  46.942  1.00 13.96           C  
ATOM    523  CG2 VAL A  78      19.442  54.599  48.152  1.00 12.43           C  
ATOM    524  N   LEU A  79      21.563  50.527  48.944  1.00 12.10           N  
ATOM    525  CA  LEU A  79      22.686  49.618  48.814  1.00 11.99           C  
ATOM    526  C   LEU A  79      22.602  48.864  47.493  1.00 11.33           C  
ATOM    527  O   LEU A  79      21.526  48.411  47.076  1.00 10.21           O  
ATOM    528  CB  LEU A  79      22.737  48.639  49.994  1.00 11.17           C  
ATOM    529  CG  LEU A  79      23.992  47.745  50.103  1.00 12.77           C  
ATOM    530  CD1 LEU A  79      24.236  47.374  51.564  1.00 11.95           C  
ATOM    531  CD2 LEU A  79      23.839  46.494  49.266  1.00 12.25           C  
ATOM    532  N   LYS A  80      23.750  48.773  46.835  1.00 12.34           N  
ATOM    533  CA  LYS A  80      23.906  48.066  45.576  1.00 13.24           C  
ATOM    534  C   LYS A  80      24.792  46.839  45.816  1.00 13.83           C  
ATOM    535  O   LYS A  80      25.888  46.974  46.351  1.00 14.24           O  
ATOM    536  CB  LYS A  80      24.580  48.970  44.550  1.00 11.86           C  
ATOM    537  CG  LYS A  80      23.639  49.857  43.743  1.00 16.93           C  
ATOM    538  CD  LYS A  80      22.817  49.006  42.777  1.00 19.27           C  
ATOM    539  CE  LYS A  80      22.003  49.841  41.800  1.00 20.87           C  
ATOM    540  NZ  LYS A  80      21.075  48.965  41.017  1.00 18.92           N  
ATOM    541  N   LEU A  81      24.316  45.651  45.438  1.00 13.13           N  
ATOM    542  CA  LEU A  81      25.101  44.423  45.558  1.00 10.42           C  
ATOM    543  C   LEU A  81      26.213  44.497  44.543  1.00 11.77           C  
ATOM    544  O   LEU A  81      25.971  44.904  43.393  1.00 10.22           O  
ATOM    545  CB  LEU A  81      24.227  43.181  45.329  1.00  8.69           C  
ATOM    546  CG  LEU A  81      22.975  43.019  46.194  1.00  5.01           C  
ATOM    547  CD1 LEU A  81      22.148  41.824  45.746  1.00  7.43           C  
ATOM    548  CD2 LEU A  81      23.341  42.874  47.662  1.00  4.24           C  
ATOM    549  N   ASN A  82      27.426  44.111  44.917  1.00 12.18           N  
ATOM    550  CA  ASN A  82      28.545  44.211  43.983  1.00 13.25           C  
ATOM    551  C   ASN A  82      29.649  43.202  44.299  1.00 14.73           C  
ATOM    552  O   ASN A  82      30.808  43.475  44.039  1.00 14.36           O  
ATOM    553  CB  ASN A  82      29.107  45.646  44.071  1.00 14.09           C  
ATOM    554  CG  ASN A  82      30.104  45.976  42.970  1.00 16.45           C  
ATOM    555  OD1 ASN A  82      29.815  45.809  41.788  1.00 18.25           O  
ATOM    556  ND2 ASN A  82      31.279  46.475  43.357  1.00 14.70           N  
ATOM    557  N   GLY A  83      29.311  42.039  44.853  1.00 16.49           N  
ATOM    558  CA  GLY A  83      30.368  41.096  45.184  1.00 20.33           C  
ATOM    559  C   GLY A  83      30.387  39.760  44.453  1.00 23.17           C  
ATOM    560  O   GLY A  83      31.114  38.832  44.828  1.00 22.86           O  
ATOM    561  N   GLY A  84      29.596  39.646  43.400  1.00 25.53           N  
ATOM    562  CA  GLY A  84      29.559  38.387  42.690  1.00 29.27           C  
ATOM    563  C   GLY A  84      30.571  38.266  41.569  1.00 31.13           C  
ATOM    564  O   GLY A  84      31.257  39.222  41.211  1.00 30.70           O  
ATOM    565  N   LEU A  85      30.662  37.061  41.026  1.00 33.83           N  
ATOM    566  CA  LEU A  85      31.552  36.767  39.920  1.00 37.37           C  
ATOM    567  C   LEU A  85      30.668  36.661  38.703  1.00 39.19           C  
ATOM    568  O   LEU A  85      29.503  36.293  38.810  1.00 41.58           O  
ATOM    569  CB  LEU A  85      32.243  35.432  40.145  1.00 39.61           C  
ATOM    570  CG  LEU A  85      33.406  35.449  41.126  1.00 40.23           C  
ATOM    571  CD1 LEU A  85      33.676  34.039  41.626  1.00 41.97           C  
ATOM    572  CD2 LEU A  85      34.627  36.042  40.428  1.00 41.48           C  
ATOM    573  N   GLY A  86      31.205  37.000  37.545  1.00 40.51           N  
ATOM    574  CA  GLY A  86      30.416  36.886  36.337  1.00 41.16           C  
ATOM    575  C   GLY A  86      30.938  35.678  35.586  1.00 41.60           C  
ATOM    576  O   GLY A  86      30.988  35.677  34.361  1.00 40.77           O  
ATOM    577  N   THR A  87      31.338  34.655  36.338  1.00 41.32           N  
ATOM    578  CA  THR A  87      31.886  33.430  35.768  1.00 42.64           C  
ATOM    579  C   THR A  87      31.197  33.001  34.474  1.00 41.35           C  
ATOM    580  O   THR A  87      31.865  32.707  33.482  1.00 40.69           O  
ATOM    581  CB  THR A  87      31.806  32.272  36.780  1.00 44.27           C  
ATOM    582  OG1 THR A  87      30.444  32.085  37.180  1.00 47.84           O  
ATOM    583  CG2 THR A  87      32.663  32.571  38.008  1.00 44.04           C  
ATOM    584  N   GLY A  88      29.864  32.976  34.495  1.00 41.33           N  
ATOM    585  CA  GLY A  88      29.085  32.587  33.328  1.00 39.88           C  
ATOM    586  C   GLY A  88      29.334  33.422  32.082  1.00 39.48           C  
ATOM    587  O   GLY A  88      29.132  32.938  30.967  1.00 40.73           O  
HETATM  588  N   MSE A  89      29.756  34.673  32.268  1.00 37.30           N  
HETATM  589  CA  MSE A  89      30.052  35.581  31.161  1.00 36.70           C  
HETATM  590  C   MSE A  89      31.567  35.694  30.950  1.00 37.92           C  
HETATM  591  O   MSE A  89      32.043  36.588  30.247  1.00 37.17           O  
HETATM  592  CB  MSE A  89      29.482  36.975  31.441  1.00 35.43           C  
HETATM  593  CG  MSE A  89      27.968  37.064  31.416  1.00 34.42           C  
HETATM  594 SE   MSE A  89      27.300  38.800  31.981  1.00 32.70          SE  
HETATM  595  CE  MSE A  89      27.573  39.843  30.410  1.00 30.82           C  
ATOM    596  N   GLY A  90      32.320  34.788  31.569  1.00 39.52           N  
ATOM    597  CA  GLY A  90      33.769  34.801  31.429  1.00 41.22           C  
ATOM    598  C   GLY A  90      34.446  36.035  31.997  1.00 43.23           C  
ATOM    599  O   GLY A  90      35.518  36.430  31.530  1.00 42.53           O  
ATOM    600  N   LEU A  91      33.822  36.648  33.002  1.00 44.26           N  
ATOM    601  CA  LEU A  91      34.382  37.836  33.630  1.00 46.20           C  
ATOM    602  C   LEU A  91      35.349  37.400  34.710  1.00 47.99           C  
ATOM    603  O   LEU A  91      35.267  36.271  35.202  1.00 49.74           O  
ATOM    604  CB  LEU A  91      33.283  38.684  34.273  1.00 45.36           C  
ATOM    605  CG  LEU A  91      32.159  39.229  33.397  1.00 45.43           C  
ATOM    606  CD1 LEU A  91      31.157  39.957  34.275  1.00 44.05           C  
ATOM    607  CD2 LEU A  91      32.724  40.158  32.339  1.00 45.07           C  
ATOM    608  N   CYS A  92      36.255  38.296  35.086  1.00 49.02           N  
ATOM    609  CA  CYS A  92      37.223  37.997  36.130  1.00 50.75           C  
ATOM    610  C   CYS A  92      37.230  39.078  37.203  1.00 48.73           C  
ATOM    611  O   CYS A  92      37.908  38.944  38.220  1.00 49.94           O  
ATOM    612  CB  CYS A  92      38.622  37.854  35.532  1.00 53.79           C  
ATOM    613  SG  CYS A  92      39.872  37.367  36.740  1.00 62.41           S  
ATOM    614  N   ASP A  93      36.477  40.151  36.973  1.00 45.92           N  
ATOM    615  CA  ASP A  93      36.399  41.248  37.937  1.00 41.68           C  
ATOM    616  C   ASP A  93      34.960  41.732  38.045  1.00 37.54           C  
ATOM    617  O   ASP A  93      34.056  41.110  37.494  1.00 36.54           O  
ATOM    618  CB  ASP A  93      37.321  42.401  37.520  1.00 43.40           C  
ATOM    619  CG  ASP A  93      37.783  43.252  38.710  1.00 44.50           C  
ATOM    620  OD1 ASP A  93      38.698  44.084  38.519  1.00 45.39           O  
ATOM    621  OD2 ASP A  93      37.241  43.101  39.829  1.00 42.89           O  
ATOM    622  N   ALA A  94      34.754  42.838  38.754  1.00 33.48           N  
ATOM    623  CA  ALA A  94      33.412  43.376  38.965  1.00 29.11           C  
ATOM    624  C   ALA A  94      32.653  43.610  37.668  1.00 26.39           C  
ATOM    625  O   ALA A  94      33.132  44.296  36.764  1.00 24.77           O  
ATOM    626  CB  ALA A  94      33.482  44.671  39.777  1.00 26.71           C  
ATOM    627  N   LYS A  95      31.457  43.038  37.586  1.00 23.86           N  
ATOM    628  CA  LYS A  95      30.645  43.189  36.394  1.00 22.30           C  
ATOM    629  C   LYS A  95      30.280  44.652  36.165  1.00 21.70           C  
ATOM    630  O   LYS A  95      30.173  45.110  35.027  1.00 20.69           O  
ATOM    631  CB  LYS A  95      29.363  42.356  36.508  1.00 20.49           C  
ATOM    632  CG  LYS A  95      28.459  42.488  35.275  1.00 16.98           C  
ATOM    633  CD  LYS A  95      27.166  41.704  35.412  1.00 16.51           C  
ATOM    634  CE  LYS A  95      27.401  40.216  35.473  1.00 20.07           C  
ATOM    635  NZ  LYS A  95      26.111  39.482  35.593  1.00 23.88           N  
ATOM    636  N   THR A  96      30.118  45.383  37.259  1.00 21.48           N  
ATOM    637  CA  THR A  96      29.743  46.781  37.207  1.00 21.25           C  
ATOM    638  C   THR A  96      30.758  47.688  36.532  1.00 22.92           C  
ATOM    639  O   THR A  96      30.448  48.844  36.239  1.00 22.80           O  
ATOM    640  CB  THR A  96      29.482  47.309  38.609  1.00 21.15           C  
ATOM    641  OG1 THR A  96      30.639  47.079  39.420  1.00 20.89           O  
ATOM    642  CG2 THR A  96      28.265  46.605  39.221  1.00 18.81           C  
ATOM    643  N   LEU A  97      31.958  47.172  36.278  1.00 23.10           N  
ATOM    644  CA  LEU A  97      32.998  47.968  35.627  1.00 24.51           C  
ATOM    645  C   LEU A  97      32.925  47.873  34.099  1.00 24.98           C  
ATOM    646  O   LEU A  97      33.726  48.483  33.385  1.00 25.33           O  
ATOM    647  CB  LEU A  97      34.378  47.528  36.115  1.00 26.43           C  
ATOM    648  CG  LEU A  97      34.625  47.739  37.613  1.00 27.24           C  
ATOM    649  CD1 LEU A  97      35.810  46.888  38.064  1.00 28.59           C  
ATOM    650  CD2 LEU A  97      34.859  49.212  37.886  1.00 24.30           C  
ATOM    651  N   LEU A  98      31.966  47.097  33.606  1.00 23.41           N  
ATOM    652  CA  LEU A  98      31.771  46.942  32.173  1.00 22.64           C  
ATOM    653  C   LEU A  98      31.006  48.147  31.646  1.00 21.98           C  
ATOM    654  O   LEU A  98      30.227  48.752  32.370  1.00 23.17           O  
ATOM    655  CB  LEU A  98      30.957  45.670  31.874  1.00 21.20           C  
ATOM    656  CG  LEU A  98      31.564  44.312  32.237  1.00 20.08           C  
ATOM    657  CD1 LEU A  98      30.566  43.206  31.895  1.00 21.09           C  
ATOM    658  CD2 LEU A  98      32.863  44.112  31.477  1.00 16.65           C  
ATOM    659  N   GLU A  99      31.222  48.492  30.385  1.00 24.10           N  
ATOM    660  CA  GLU A  99      30.515  49.618  29.786  1.00 27.16           C  
ATOM    661  C   GLU A  99      29.063  49.247  29.469  1.00 26.29           C  
ATOM    662  O   GLU A  99      28.772  48.115  29.086  1.00 24.33           O  
ATOM    663  CB  GLU A  99      31.226  50.075  28.506  1.00 28.80           C  
ATOM    664  CG  GLU A  99      32.328  51.100  28.741  1.00 35.55           C  
ATOM    665  CD  GLU A  99      32.967  51.576  27.444  1.00 38.68           C  
ATOM    666  OE1 GLU A  99      32.216  51.925  26.504  1.00 39.77           O  
ATOM    667  OE2 GLU A  99      34.219  51.605  27.368  1.00 41.28           O  
ATOM    668  N   VAL A 100      28.161  50.211  29.639  1.00 27.54           N  
ATOM    669  CA  VAL A 100      26.731  50.021  29.380  1.00 28.87           C  
ATOM    670  C   VAL A 100      26.314  50.897  28.196  1.00 28.31           C  
ATOM    671  O   VAL A 100      25.526  50.482  27.344  1.00 30.17           O  
ATOM    672  CB  VAL A 100      25.901  50.381  30.648  1.00 28.95           C  
ATOM    673  CG1 VAL A 100      24.416  50.523  30.303  1.00 30.37           C  
ATOM    674  CG2 VAL A 100      26.089  49.295  31.695  1.00 29.11           C  
ATOM    675  N   LYS A 101      26.847  52.114  28.173  1.00 27.76           N  
ATOM    676  CA  LYS A 101      26.623  53.084  27.100  1.00 28.70           C  
ATOM    677  C   LYS A 101      28.014  53.658  26.835  1.00 29.03           C  
ATOM    678  O   LYS A 101      28.896  53.555  27.691  1.00 30.47           O  
ATOM    679  CB  LYS A 101      25.658  54.208  27.523  1.00 26.38           C  
ATOM    680  CG  LYS A 101      24.194  53.784  27.688  1.00 24.49           C  
ATOM    681  CD  LYS A 101      23.618  53.125  26.416  1.00 24.88           C  
ATOM    682  CE  LYS A 101      22.134  52.798  26.576  1.00 24.20           C  
ATOM    683  NZ  LYS A 101      21.587  51.972  25.462  1.00 24.32           N  
ATOM    684  N   ASP A 102      28.217  54.253  25.665  1.00 29.00           N  
ATOM    685  CA  ASP A 102      29.520  54.806  25.321  1.00 28.69           C  
ATOM    686  C   ASP A 102      30.183  55.574  26.469  1.00 27.43           C  
ATOM    687  O   ASP A 102      29.683  56.597  26.922  1.00 27.29           O  
ATOM    688  CB  ASP A 102      29.407  55.693  24.068  1.00 29.53           C  
ATOM    689  CG  ASP A 102      30.753  56.314  23.649  1.00 31.81           C  
ATOM    690  OD1 ASP A 102      31.817  55.682  23.852  1.00 30.29           O  
ATOM    691  OD2 ASP A 102      30.740  57.436  23.098  1.00 32.90           O  
ATOM    692  N   GLY A 103      31.310  55.043  26.943  1.00 27.54           N  
ATOM    693  CA  GLY A 103      32.060  55.675  28.015  1.00 25.79           C  
ATOM    694  C   GLY A 103      31.480  55.629  29.419  1.00 25.67           C  
ATOM    695  O   GLY A 103      32.016  56.282  30.317  1.00 25.55           O  
ATOM    696  N   LYS A 104      30.397  54.879  29.623  1.00 24.40           N  
ATOM    697  CA  LYS A 104      29.790  54.795  30.949  1.00 23.94           C  
ATOM    698  C   LYS A 104      29.593  53.349  31.390  1.00 22.21           C  
ATOM    699  O   LYS A 104      29.046  52.526  30.656  1.00 22.56           O  
ATOM    700  CB  LYS A 104      28.447  55.537  30.968  1.00 24.33           C  
ATOM    701  CG  LYS A 104      28.550  57.033  30.676  1.00 27.76           C  
ATOM    702  CD  LYS A 104      29.206  57.780  31.827  1.00 29.40           C  
ATOM    703  CE  LYS A 104      29.361  59.265  31.531  1.00 32.35           C  
ATOM    704  NZ  LYS A 104      30.407  59.537  30.507  1.00 34.53           N  
ATOM    705  N   THR A 105      30.040  53.052  32.601  1.00 21.69           N  
ATOM    706  CA  THR A 105      29.931  51.713  33.168  1.00 18.80           C  
ATOM    707  C   THR A 105      28.719  51.658  34.085  1.00 18.58           C  
ATOM    708  O   THR A 105      28.077  52.685  34.342  1.00 16.23           O  
ATOM    709  CB  THR A 105      31.160  51.393  34.021  1.00 19.73           C  
ATOM    710  OG1 THR A 105      31.083  52.138  35.248  1.00 19.63           O  
ATOM    711  CG2 THR A 105      32.447  51.780  33.272  1.00 17.96           C  
ATOM    712  N   PHE A 106      28.397  50.464  34.576  1.00 17.55           N  
ATOM    713  CA  PHE A 106      27.287  50.318  35.508  1.00 18.08           C  
ATOM    714  C   PHE A 106      27.573  51.201  36.717  1.00 19.35           C  
ATOM    715  O   PHE A 106      26.679  51.849  37.260  1.00 19.63           O  
ATOM    716  CB  PHE A 106      27.167  48.878  36.011  1.00 16.55           C  
ATOM    717  CG  PHE A 106      26.754  47.893  34.973  1.00 17.07           C  
ATOM    718  CD1 PHE A 106      27.688  47.320  34.137  1.00 15.67           C  
ATOM    719  CD2 PHE A 106      25.424  47.497  34.868  1.00 17.72           C  
ATOM    720  CE1 PHE A 106      27.312  46.358  33.212  1.00 18.12           C  
ATOM    721  CE2 PHE A 106      25.035  46.537  33.947  1.00 17.69           C  
ATOM    722  CZ  PHE A 106      25.984  45.967  33.116  1.00 17.84           C  
ATOM    723  N   LEU A 107      28.836  51.203  37.127  1.00 21.39           N  
ATOM    724  CA  LEU A 107      29.287  51.974  38.281  1.00 22.60           C  
ATOM    725  C   LEU A 107      29.095  53.457  38.037  1.00 21.99           C  
ATOM    726  O   LEU A 107      28.776  54.202  38.960  1.00 22.35           O  
ATOM    727  CB  LEU A 107      30.765  51.681  38.560  1.00 22.01           C  
ATOM    728  CG  LEU A 107      31.183  51.383  39.995  1.00 24.88           C  
ATOM    729  CD1 LEU A 107      30.207  50.395  40.638  1.00 26.55           C  
ATOM    730  CD2 LEU A 107      32.594  50.804  40.002  1.00 23.30           C  
ATOM    731  N   ASP A 108      29.303  53.877  36.790  1.00 22.01           N  
ATOM    732  CA  ASP A 108      29.149  55.273  36.399  1.00 20.53           C  
ATOM    733  C   ASP A 108      27.707  55.728  36.627  1.00 19.79           C  
ATOM    734  O   ASP A 108      27.458  56.747  37.280  1.00 19.75           O  
ATOM    735  CB  ASP A 108      29.505  55.461  34.912  1.00 22.84           C  
ATOM    736  CG  ASP A 108      31.004  55.686  34.674  1.00 23.84           C  
ATOM    737  OD1 ASP A 108      31.592  56.541  35.358  1.00 25.96           O  
ATOM    738  OD2 ASP A 108      31.592  55.024  33.792  1.00 26.00           O  
ATOM    739  N   PHE A 109      26.762  54.964  36.084  1.00 18.36           N  
ATOM    740  CA  PHE A 109      25.350  55.281  36.217  1.00 17.12           C  
ATOM    741  C   PHE A 109      24.859  55.162  37.656  1.00 17.18           C  
ATOM    742  O   PHE A 109      23.986  55.910  38.081  1.00 18.82           O  
ATOM    743  CB  PHE A 109      24.521  54.390  35.292  1.00 18.70           C  
ATOM    744  CG  PHE A 109      24.582  54.807  33.840  1.00 21.66           C  
ATOM    745  CD1 PHE A 109      25.287  54.047  32.905  1.00 22.05           C  
ATOM    746  CD2 PHE A 109      23.953  55.983  33.413  1.00 21.84           C  
ATOM    747  CE1 PHE A 109      25.371  54.447  31.560  1.00 22.30           C  
ATOM    748  CE2 PHE A 109      24.032  56.397  32.073  1.00 23.67           C  
ATOM    749  CZ  PHE A 109      24.743  55.625  31.146  1.00 21.54           C  
ATOM    750  N   THR A 110      25.419  54.230  38.413  1.00 14.83           N  
ATOM    751  CA  THR A 110      25.013  54.094  39.800  1.00 15.83           C  
ATOM    752  C   THR A 110      25.321  55.384  40.551  1.00 14.02           C  
ATOM    753  O   THR A 110      24.459  55.935  41.224  1.00 15.07           O  
ATOM    754  CB  THR A 110      25.747  52.928  40.498  1.00 16.51           C  
ATOM    755  OG1 THR A 110      25.514  51.718  39.773  1.00 17.39           O  
ATOM    756  CG2 THR A 110      25.235  52.752  41.916  1.00 16.87           C  
ATOM    757  N   ALA A 111      26.555  55.853  40.426  1.00 14.93           N  
ATOM    758  CA  ALA A 111      27.009  57.077  41.092  1.00 17.45           C  
ATOM    759  C   ALA A 111      26.209  58.296  40.646  1.00 17.10           C  
ATOM    760  O   ALA A 111      25.859  59.154  41.454  1.00 19.10           O  
ATOM    761  CB  ALA A 111      28.497  57.306  40.804  1.00 16.45           C  
ATOM    762  N   LEU A 112      25.928  58.372  39.353  1.00 18.71           N  
ATOM    763  CA  LEU A 112      25.157  59.483  38.818  1.00 19.89           C  
ATOM    764  C   LEU A 112      23.779  59.445  39.460  1.00 21.06           C  
ATOM    765  O   LEU A 112      23.179  60.489  39.749  1.00 20.63           O  
ATOM    766  CB  LEU A 112      25.062  59.363  37.293  1.00 21.46           C  
ATOM    767  CG  LEU A 112      26.385  59.696  36.594  1.00 21.04           C  
ATOM    768  CD1 LEU A 112      26.341  59.364  35.108  1.00 20.28           C  
ATOM    769  CD2 LEU A 112      26.656  61.199  36.797  1.00 23.12           C  
ATOM    770  N   GLN A 113      23.285  58.234  39.704  1.00 20.93           N  
ATOM    771  CA  GLN A 113      21.983  58.069  40.340  1.00 21.38           C  
ATOM    772  C   GLN A 113      22.042  58.608  41.758  1.00 21.76           C  
ATOM    773  O   GLN A 113      21.183  59.371  42.181  1.00 23.82           O  
ATOM    774  CB  GLN A 113      21.581  56.597  40.361  1.00 21.73           C  
ATOM    775  CG  GLN A 113      21.032  56.093  39.029  1.00 22.84           C  
ATOM    776  CD  GLN A 113      20.973  54.574  38.932  1.00 22.49           C  
ATOM    777  OE1 GLN A 113      20.897  53.872  39.941  1.00 22.57           O  
ATOM    778  NE2 GLN A 113      20.989  54.066  37.707  1.00 22.31           N  
ATOM    779  N   VAL A 114      23.067  58.215  42.497  1.00 22.98           N  
ATOM    780  CA  VAL A 114      23.212  58.686  43.865  1.00 21.49           C  
ATOM    781  C   VAL A 114      23.298  60.213  43.854  1.00 21.89           C  
ATOM    782  O   VAL A 114      22.551  60.888  44.554  1.00 21.58           O  
ATOM    783  CB  VAL A 114      24.476  58.097  44.516  1.00 19.11           C  
ATOM    784  CG1 VAL A 114      24.636  58.639  45.916  1.00 17.94           C  
ATOM    785  CG2 VAL A 114      24.379  56.568  44.531  1.00 18.59           C  
ATOM    786  N   GLN A 115      24.201  60.746  43.038  1.00 23.32           N  
ATOM    787  CA  GLN A 115      24.397  62.188  42.916  1.00 25.33           C  
ATOM    788  C   GLN A 115      23.095  62.924  42.649  1.00 25.10           C  
ATOM    789  O   GLN A 115      22.780  63.899  43.313  1.00 25.50           O  
ATOM    790  CB  GLN A 115      25.384  62.464  41.793  1.00 27.25           C  
ATOM    791  CG  GLN A 115      25.698  63.921  41.566  1.00 28.92           C  
ATOM    792  CD  GLN A 115      26.799  64.094  40.531  1.00 31.03           C  
ATOM    793  OE1 GLN A 115      26.619  63.782  39.350  1.00 30.37           O  
ATOM    794  NE2 GLN A 115      27.953  64.583  40.975  1.00 31.60           N  
ATOM    795  N   TYR A 116      22.331  62.440  41.680  1.00 26.71           N  
ATOM    796  CA  TYR A 116      21.057  63.053  41.339  1.00 27.58           C  
ATOM    797  C   TYR A 116      20.145  63.142  42.555  1.00 28.70           C  
ATOM    798  O   TYR A 116      19.519  64.186  42.808  1.00 28.51           O  
ATOM    799  CB  TYR A 116      20.343  62.245  40.255  1.00 27.48           C  
ATOM    800  CG  TYR A 116      19.039  62.866  39.822  1.00 28.44           C  
ATOM    801  CD1 TYR A 116      18.993  63.771  38.760  1.00 29.33           C  
ATOM    802  CD2 TYR A 116      17.855  62.583  40.496  1.00 29.08           C  
ATOM    803  CE1 TYR A 116      17.802  64.376  38.381  1.00 29.12           C  
ATOM    804  CE2 TYR A 116      16.653  63.190  40.126  1.00 31.21           C  
ATOM    805  CZ  TYR A 116      16.638  64.085  39.066  1.00 29.86           C  
ATOM    806  OH  TYR A 116      15.454  64.684  38.692  1.00 33.00           O  
ATOM    807  N   LEU A 117      20.042  62.041  43.296  1.00 28.23           N  
ATOM    808  CA  LEU A 117      19.188  62.041  44.478  1.00 28.76           C  
ATOM    809  C   LEU A 117      19.726  62.964  45.577  1.00 27.74           C  
ATOM    810  O   LEU A 117      18.945  63.561  46.315  1.00 24.75           O  
ATOM    811  CB  LEU A 117      18.995  60.621  45.028  1.00 27.68           C  
ATOM    812  CG  LEU A 117      18.057  59.731  44.204  1.00 28.41           C  
ATOM    813  CD1 LEU A 117      17.783  58.463  44.970  1.00 28.43           C  
ATOM    814  CD2 LEU A 117      16.750  60.441  43.926  1.00 28.22           C  
ATOM    815  N   ARG A 118      21.046  63.092  45.677  1.00 28.40           N  
ATOM    816  CA  ARG A 118      21.610  63.965  46.691  1.00 32.18           C  
ATOM    817  C   ARG A 118      21.412  65.441  46.310  1.00 33.55           C  
ATOM    818  O   ARG A 118      21.446  66.320  47.169  1.00 34.90           O  
ATOM    819  CB  ARG A 118      23.099  63.669  46.911  1.00 30.66           C  
ATOM    820  CG  ARG A 118      23.363  62.481  47.820  1.00 32.41           C  
ATOM    821  CD  ARG A 118      24.818  62.373  48.227  1.00 32.79           C  
ATOM    822  NE  ARG A 118      25.106  61.051  48.773  1.00 35.98           N  
ATOM    823  CZ  ARG A 118      26.272  60.688  49.298  1.00 36.05           C  
ATOM    824  NH1 ARG A 118      27.269  61.556  49.349  1.00 37.45           N  
ATOM    825  NH2 ARG A 118      26.436  59.459  49.776  1.00 36.52           N  
ATOM    826  N   GLN A 119      21.202  65.717  45.030  1.00 34.81           N  
ATOM    827  CA  GLN A 119      21.000  67.093  44.618  1.00 37.27           C  
ATOM    828  C   GLN A 119      19.530  67.432  44.667  1.00 37.22           C  
ATOM    829  O   GLN A 119      19.156  68.587  44.849  1.00 36.41           O  
ATOM    830  CB  GLN A 119      21.585  67.323  43.215  1.00 38.83           C  
ATOM    831  CG  GLN A 119      23.106  67.278  43.217  1.00 41.50           C  
ATOM    832  CD  GLN A 119      23.729  67.187  41.828  1.00 42.58           C  
ATOM    833  OE1 GLN A 119      23.100  66.758  40.866  1.00 43.18           O  
ATOM    834  NE2 GLN A 119      24.993  67.565  41.736  1.00 43.14           N  
ATOM    835  N   HIS A 120      18.686  66.414  44.568  1.00 38.95           N  
ATOM    836  CA  HIS A 120      17.248  66.653  44.585  1.00 41.15           C  
ATOM    837  C   HIS A 120      16.502  66.153  45.814  1.00 42.36           C  
ATOM    838  O   HIS A 120      15.916  66.955  46.538  1.00 45.53           O  
ATOM    839  CB  HIS A 120      16.631  66.065  43.331  1.00 43.31           C  
ATOM    840  CG  HIS A 120      17.159  66.689  42.076  1.00 45.51           C  
ATOM    841  ND1 HIS A 120      16.736  67.921  41.627  1.00 46.83           N  
ATOM    842  CD2 HIS A 120      18.132  66.292  41.222  1.00 46.32           C  
ATOM    843  CE1 HIS A 120      17.423  68.258  40.547  1.00 47.39           C  
ATOM    844  NE2 HIS A 120      18.277  67.286  40.280  1.00 46.59           N  
ATOM    845  N   CYS A 121      16.514  64.850  46.073  1.00 42.85           N  
ATOM    846  CA  CYS A 121      15.775  64.323  47.224  1.00 43.40           C  
ATOM    847  C   CYS A 121      16.368  64.601  48.606  1.00 42.28           C  
ATOM    848  O   CYS A 121      15.796  65.362  49.382  1.00 42.93           O  
ATOM    849  CB  CYS A 121      15.550  62.822  47.049  1.00 44.65           C  
ATOM    850  SG  CYS A 121      14.515  62.453  45.630  1.00 52.07           S  
ATOM    851  N   SER A 122      17.494  63.971  48.924  1.00 40.56           N  
ATOM    852  CA  SER A 122      18.129  64.159  50.225  1.00 38.70           C  
ATOM    853  C   SER A 122      19.627  64.276  50.049  1.00 37.77           C  
ATOM    854  O   SER A 122      20.290  63.304  49.669  1.00 35.39           O  
ATOM    855  CB  SER A 122      17.813  62.973  51.134  1.00 40.80           C  
ATOM    856  OG  SER A 122      18.111  61.749  50.493  1.00 39.31           O  
ATOM    857  N   GLU A 123      20.163  65.457  50.342  1.00 36.92           N  
ATOM    858  CA  GLU A 123      21.588  65.701  50.161  1.00 38.00           C  
ATOM    859  C   GLU A 123      22.532  64.752  50.893  1.00 36.45           C  
ATOM    860  O   GLU A 123      23.669  64.570  50.465  1.00 34.88           O  
ATOM    861  CB  GLU A 123      21.931  67.159  50.521  1.00 41.73           C  
ATOM    862  CG  GLU A 123      21.695  67.552  51.973  1.00 45.35           C  
ATOM    863  CD  GLU A 123      22.152  68.979  52.281  1.00 48.13           C  
ATOM    864  OE1 GLU A 123      23.347  69.292  52.073  1.00 49.68           O  
ATOM    865  OE2 GLU A 123      21.315  69.787  52.735  1.00 48.45           O  
ATOM    866  N   HIS A 124      22.070  64.141  51.981  1.00 35.26           N  
ATOM    867  CA  HIS A 124      22.916  63.224  52.740  1.00 35.00           C  
ATOM    868  C   HIS A 124      22.522  61.764  52.562  1.00 31.96           C  
ATOM    869  O   HIS A 124      22.734  60.945  53.453  1.00 32.53           O  
ATOM    870  CB  HIS A 124      22.861  63.581  54.223  1.00 38.19           C  
ATOM    871  CG  HIS A 124      23.159  65.019  54.499  1.00 41.60           C  
ATOM    872  ND1 HIS A 124      24.400  65.575  54.279  1.00 42.70           N  
ATOM    873  CD2 HIS A 124      22.365  66.025  54.936  1.00 42.11           C  
ATOM    874  CE1 HIS A 124      24.358  66.864  54.567  1.00 44.33           C  
ATOM    875  NE2 HIS A 124      23.134  67.163  54.968  1.00 44.42           N  
ATOM    876  N   LEU A 125      21.942  61.438  51.416  1.00 30.01           N  
ATOM    877  CA  LEU A 125      21.526  60.066  51.145  1.00 28.18           C  
ATOM    878  C   LEU A 125      22.675  59.096  51.390  1.00 25.41           C  
ATOM    879  O   LEU A 125      23.772  59.283  50.863  1.00 23.84           O  
ATOM    880  CB  LEU A 125      21.066  59.922  49.695  1.00 30.34           C  
ATOM    881  CG  LEU A 125      20.755  58.474  49.313  1.00 32.44           C  
ATOM    882  CD1 LEU A 125      19.461  58.065  49.977  1.00 32.35           C  
ATOM    883  CD2 LEU A 125      20.646  58.336  47.815  1.00 32.29           C  
ATOM    884  N   ARG A 126      22.418  58.069  52.196  1.00 22.70           N  
ATOM    885  CA  ARG A 126      23.431  57.066  52.493  1.00 20.91           C  
ATOM    886  C   ARG A 126      23.424  55.997  51.403  1.00 19.61           C  
ATOM    887  O   ARG A 126      22.426  55.301  51.188  1.00 17.62           O  
ATOM    888  CB  ARG A 126      23.178  56.420  53.854  1.00 20.70           C  
ATOM    889  CG  ARG A 126      24.141  55.267  54.206  1.00 22.95           C  
ATOM    890  CD  ARG A 126      25.618  55.693  54.265  1.00 23.55           C  
ATOM    891  NE  ARG A 126      25.882  56.726  55.266  1.00 26.54           N  
ATOM    892  CZ  ARG A 126      26.064  56.507  56.568  1.00 29.50           C  
ATOM    893  NH1 ARG A 126      26.021  55.273  57.062  1.00 27.48           N  
ATOM    894  NH2 ARG A 126      26.284  57.533  57.387  1.00 31.24           N  
ATOM    895  N   PHE A 127      24.546  55.896  50.705  1.00 17.79           N  
ATOM    896  CA  PHE A 127      24.718  54.926  49.635  1.00 16.85           C  
ATOM    897  C   PHE A 127      25.774  53.898  50.018  1.00 15.56           C  
ATOM    898  O   PHE A 127      26.832  54.252  50.530  1.00 14.62           O  
ATOM    899  CB  PHE A 127      25.154  55.628  48.344  1.00 17.90           C  
ATOM    900  CG  PHE A 127      25.548  54.679  47.244  1.00 19.79           C  
ATOM    901  CD1 PHE A 127      24.590  53.888  46.610  1.00 18.74           C  
ATOM    902  CD2 PHE A 127      26.882  54.552  46.863  1.00 19.38           C  
ATOM    903  CE1 PHE A 127      24.957  52.982  45.614  1.00 19.45           C  
ATOM    904  CE2 PHE A 127      27.256  53.650  45.870  1.00 20.99           C  
ATOM    905  CZ  PHE A 127      26.291  52.862  45.246  1.00 19.16           C  
HETATM  906  N   MSE A 128      25.489  52.631  49.736  1.00 14.74           N  
HETATM  907  CA  MSE A 128      26.418  51.556  50.039  1.00 14.62           C  
HETATM  908  C   MSE A 128      26.568  50.550  48.891  1.00 14.12           C  
HETATM  909  O   MSE A 128      25.719  50.470  47.995  1.00 13.36           O  
HETATM  910  CB  MSE A 128      25.973  50.809  51.298  1.00 14.41           C  
HETATM  911  CG  MSE A 128      25.845  51.666  52.551  1.00 17.33           C  
HETATM  912 SE   MSE A 128      25.438  50.605  54.162  1.00 25.12          SE  
HETATM  913  CE  MSE A 128      27.259  50.207  54.693  1.00 20.64           C  
ATOM    914  N   LEU A 129      27.675  49.812  48.935  1.00 12.49           N  
ATOM    915  CA  LEU A 129      28.001  48.760  47.978  1.00 12.39           C  
ATOM    916  C   LEU A 129      28.543  47.555  48.754  1.00 12.19           C  
ATOM    917  O   LEU A 129      29.464  47.689  49.578  1.00 11.34           O  
ATOM    918  CB  LEU A 129      29.089  49.204  46.996  1.00 10.73           C  
ATOM    919  CG  LEU A 129      28.725  50.209  45.905  1.00 12.62           C  
ATOM    920  CD1 LEU A 129      29.975  50.929  45.439  1.00  8.92           C  
ATOM    921  CD2 LEU A 129      28.034  49.483  44.746  1.00 10.07           C  
HETATM  922  N   MSE A 130      27.972  46.381  48.512  1.00 11.30           N  
HETATM  923  CA  MSE A 130      28.484  45.198  49.174  1.00 12.51           C  
HETATM  924  C   MSE A 130      29.502  44.642  48.198  1.00 13.04           C  
HETATM  925  O   MSE A 130      29.165  44.345  47.043  1.00 12.38           O  
HETATM  926  CB  MSE A 130      27.379  44.174  49.437  1.00 13.73           C  
HETATM  927  CG  MSE A 130      27.923  42.906  50.095  1.00 16.54           C  
HETATM  928 SE   MSE A 130      26.567  41.740  50.825  1.00 24.92          SE  
HETATM  929  CE  MSE A 130      26.315  40.577  49.274  1.00 16.66           C  
ATOM    930  N   ASP A 131      30.749  44.537  48.643  1.00 12.15           N  
ATOM    931  CA  ASP A 131      31.821  44.028  47.792  1.00 14.67           C  
ATOM    932  C   ASP A 131      32.378  42.718  48.334  1.00 16.96           C  
ATOM    933  O   ASP A 131      32.162  42.393  49.503  1.00 17.35           O  
ATOM    934  CB  ASP A 131      32.980  45.030  47.728  1.00 12.27           C  
ATOM    935  CG  ASP A 131      32.573  46.361  47.132  1.00 15.29           C  
ATOM    936  OD1 ASP A 131      31.595  46.345  46.361  1.00 14.94           O  
ATOM    937  OD2 ASP A 131      33.235  47.400  47.414  1.00 12.29           O  
ATOM    938  N   SER A 132      33.090  41.988  47.476  1.00 17.97           N  
ATOM    939  CA  SER A 132      33.747  40.734  47.849  1.00 23.90           C  
ATOM    940  C   SER A 132      35.207  41.153  47.781  1.00 26.84           C  
ATOM    941  O   SER A 132      35.483  42.245  47.273  1.00 26.48           O  
ATOM    942  CB  SER A 132      33.482  39.640  46.814  1.00 24.19           C  
ATOM    943  OG  SER A 132      34.089  39.971  45.573  1.00 21.55           O  
ATOM    944  N   PHE A 133      36.159  40.351  48.259  1.00 31.46           N  
ATOM    945  CA  PHE A 133      37.527  40.859  48.159  1.00 36.92           C  
ATOM    946  C   PHE A 133      37.939  40.880  46.706  1.00 37.54           C  
ATOM    947  O   PHE A 133      38.822  41.633  46.308  1.00 38.87           O  
ATOM    948  CB  PHE A 133      38.543  40.051  48.963  1.00 41.74           C  
ATOM    949  CG  PHE A 133      39.841  40.798  49.168  1.00 47.13           C  
ATOM    950  CD1 PHE A 133      39.879  41.937  49.986  1.00 49.24           C  
ATOM    951  CD2 PHE A 133      40.991  40.454  48.455  1.00 48.75           C  
ATOM    952  CE1 PHE A 133      41.039  42.726  50.085  1.00 50.16           C  
ATOM    953  CE2 PHE A 133      42.158  41.234  48.545  1.00 51.03           C  
ATOM    954  CZ  PHE A 133      42.179  42.377  49.362  1.00 50.81           C  
ATOM    955  N   ASN A 134      37.280  40.053  45.910  1.00 37.73           N  
ATOM    956  CA  ASN A 134      37.575  40.011  44.494  1.00 38.14           C  
ATOM    957  C   ASN A 134      37.197  41.321  43.779  1.00 36.26           C  
ATOM    958  O   ASN A 134      37.879  41.745  42.840  1.00 37.95           O  
ATOM    959  CB  ASN A 134      36.840  38.845  43.841  1.00 40.68           C  
ATOM    960  CG  ASN A 134      36.967  38.859  42.329  1.00 45.59           C  
ATOM    961  OD1 ASN A 134      38.074  38.966  41.788  1.00 47.67           O  
ATOM    962  ND2 ASN A 134      35.832  38.752  41.633  1.00 46.72           N  
ATOM    963  N   THR A 135      36.127  41.976  44.226  1.00 31.79           N  
ATOM    964  CA  THR A 135      35.670  43.202  43.567  1.00 27.26           C  
ATOM    965  C   THR A 135      35.974  44.506  44.304  1.00 25.95           C  
ATOM    966  O   THR A 135      35.791  45.589  43.754  1.00 26.06           O  
ATOM    967  CB  THR A 135      34.138  43.164  43.347  1.00 26.25           C  
ATOM    968  OG1 THR A 135      33.477  43.357  44.598  1.00 22.33           O  
ATOM    969  CG2 THR A 135      33.699  41.828  42.801  1.00 24.39           C  
ATOM    970  N   SER A 136      36.430  44.398  45.545  1.00 24.66           N  
ATOM    971  CA  SER A 136      36.699  45.567  46.380  1.00 23.47           C  
ATOM    972  C   SER A 136      37.685  46.593  45.835  1.00 23.88           C  
ATOM    973  O   SER A 136      37.339  47.763  45.633  1.00 23.69           O  
ATOM    974  CB  SER A 136      37.164  45.099  47.763  1.00 22.98           C  
ATOM    975  OG  SER A 136      37.294  46.180  48.658  1.00 23.79           O  
ATOM    976  N   ALA A 137      38.914  46.152  45.604  1.00 23.60           N  
ATOM    977  CA  ALA A 137      39.970  47.027  45.116  1.00 25.14           C  
ATOM    978  C   ALA A 137      39.637  47.743  43.800  1.00 25.41           C  
ATOM    979  O   ALA A 137      39.858  48.947  43.658  1.00 24.37           O  
ATOM    980  CB  ALA A 137      41.271  46.223  44.967  1.00 24.86           C  
ATOM    981  N   SER A 138      39.102  46.992  42.846  1.00 26.42           N  
ATOM    982  CA  SER A 138      38.757  47.529  41.537  1.00 27.58           C  
ATOM    983  C   SER A 138      37.708  48.617  41.657  1.00 26.96           C  
ATOM    984  O   SER A 138      37.785  49.659  40.990  1.00 26.74           O  
ATOM    985  CB  SER A 138      38.215  46.407  40.650  1.00 29.94           C  
ATOM    986  OG  SER A 138      38.851  45.181  40.955  1.00 34.37           O  
ATOM    987  N   THR A 139      36.722  48.358  42.511  1.00 25.36           N  
ATOM    988  CA  THR A 139      35.628  49.292  42.727  1.00 24.10           C  
ATOM    989  C   THR A 139      36.153  50.572  43.372  1.00 24.39           C  
ATOM    990  O   THR A 139      35.867  51.682  42.905  1.00 24.18           O  
ATOM    991  CB  THR A 139      34.535  48.670  43.642  1.00 23.47           C  
ATOM    992  OG1 THR A 139      34.029  47.469  43.043  1.00 21.18           O  
ATOM    993  CG2 THR A 139      33.389  49.645  43.847  1.00 20.96           C  
ATOM    994  N   LYS A 140      36.927  50.413  44.439  1.00 24.00           N  
ATOM    995  CA  LYS A 140      37.475  51.564  45.139  1.00 25.78           C  
ATOM    996  C   LYS A 140      38.287  52.451  44.203  1.00 25.76           C  
ATOM    997  O   LYS A 140      38.057  53.659  44.122  1.00 24.30           O  
ATOM    998  CB  LYS A 140      38.349  51.105  46.304  1.00 27.36           C  
ATOM    999  CG  LYS A 140      38.754  52.227  47.249  1.00 30.39           C  
ATOM   1000  CD  LYS A 140      39.351  51.659  48.528  1.00 33.03           C  
ATOM   1001  CE  LYS A 140      39.775  52.759  49.497  1.00 35.19           C  
ATOM   1002  NZ  LYS A 140      40.283  52.170  50.775  1.00 35.50           N  
ATOM   1003  N   SER A 141      39.228  51.849  43.483  1.00 25.39           N  
ATOM   1004  CA  SER A 141      40.068  52.611  42.567  1.00 27.16           C  
ATOM   1005  C   SER A 141      39.259  53.339  41.488  1.00 27.23           C  
ATOM   1006  O   SER A 141      39.606  54.445  41.082  1.00 26.78           O  
ATOM   1007  CB  SER A 141      41.084  51.682  41.917  1.00 27.68           C  
ATOM   1008  OG  SER A 141      40.416  50.580  41.342  1.00 34.22           O  
ATOM   1009  N   PHE A 142      38.181  52.719  41.022  1.00 28.20           N  
ATOM   1010  CA  PHE A 142      37.358  53.356  40.005  1.00 28.37           C  
ATOM   1011  C   PHE A 142      36.764  54.646  40.592  1.00 29.26           C  
ATOM   1012  O   PHE A 142      36.883  55.719  39.999  1.00 30.09           O  
ATOM   1013  CB  PHE A 142      36.234  52.414  39.537  1.00 24.61           C  
ATOM   1014  CG  PHE A 142      35.334  53.030  38.506  1.00 22.66           C  
ATOM   1015  CD1 PHE A 142      35.704  53.056  37.170  1.00 24.91           C  
ATOM   1016  CD2 PHE A 142      34.160  53.659  38.880  1.00 23.06           C  
ATOM   1017  CE1 PHE A 142      34.916  53.709  36.216  1.00 25.55           C  
ATOM   1018  CE2 PHE A 142      33.361  54.317  37.939  1.00 23.25           C  
ATOM   1019  CZ  PHE A 142      33.741  54.343  36.603  1.00 24.42           C  
ATOM   1020  N   LEU A 143      36.138  54.536  41.765  1.00 29.21           N  
ATOM   1021  CA  LEU A 143      35.533  55.693  42.419  1.00 29.58           C  
ATOM   1022  C   LEU A 143      36.573  56.775  42.724  1.00 31.10           C  
ATOM   1023  O   LEU A 143      36.294  57.970  42.575  1.00 30.42           O  
ATOM   1024  CB  LEU A 143      34.838  55.280  43.724  1.00 25.57           C  
ATOM   1025  CG  LEU A 143      33.708  54.250  43.609  1.00 26.04           C  
ATOM   1026  CD1 LEU A 143      33.166  53.904  44.986  1.00 24.45           C  
ATOM   1027  CD2 LEU A 143      32.604  54.800  42.741  1.00 22.17           C  
ATOM   1028  N   LYS A 144      37.763  56.353  43.152  1.00 32.14           N  
ATOM   1029  CA  LYS A 144      38.823  57.297  43.485  1.00 35.01           C  
ATOM   1030  C   LYS A 144      39.177  58.189  42.303  1.00 35.23           C  
ATOM   1031  O   LYS A 144      39.359  59.402  42.456  1.00 34.50           O  
ATOM   1032  CB  LYS A 144      40.084  56.564  43.954  1.00 35.66           C  
ATOM   1033  CG  LYS A 144      41.184  57.522  44.393  1.00 37.54           C  
ATOM   1034  CD  LYS A 144      42.369  56.792  44.996  1.00 40.57           C  
ATOM   1035  CE  LYS A 144      43.356  57.779  45.623  1.00 42.58           C  
ATOM   1036  NZ  LYS A 144      44.568  57.104  46.166  1.00 42.12           N  
ATOM   1037  N   ALA A 145      39.264  57.577  41.128  1.00 35.53           N  
ATOM   1038  CA  ALA A 145      39.606  58.293  39.910  1.00 36.00           C  
ATOM   1039  C   ALA A 145      38.424  59.027  39.270  1.00 36.32           C  
ATOM   1040  O   ALA A 145      38.617  60.057  38.614  1.00 36.19           O  
ATOM   1041  CB  ALA A 145      40.216  57.319  38.900  1.00 34.89           C  
ATOM   1042  N   ARG A 146      37.207  58.516  39.465  1.00 35.69           N  
ATOM   1043  CA  ARG A 146      36.025  59.122  38.844  1.00 35.33           C  
ATOM   1044  C   ARG A 146      35.042  59.858  39.754  1.00 34.27           C  
ATOM   1045  O   ARG A 146      34.479  60.869  39.350  1.00 34.18           O  
ATOM   1046  CB  ARG A 146      35.251  58.057  38.054  1.00 37.02           C  
ATOM   1047  CG  ARG A 146      36.074  57.288  37.013  1.00 39.69           C  
ATOM   1048  CD  ARG A 146      36.681  58.222  35.965  1.00 41.68           C  
ATOM   1049  NE  ARG A 146      37.371  57.491  34.901  1.00 45.01           N  
ATOM   1050  CZ  ARG A 146      36.767  56.887  33.877  1.00 45.42           C  
ATOM   1051  NH1 ARG A 146      35.446  56.920  33.758  1.00 45.27           N  
ATOM   1052  NH2 ARG A 146      37.490  56.248  32.965  1.00 44.86           N  
ATOM   1053  N   TYR A 147      34.811  59.351  40.964  1.00 34.28           N  
ATOM   1054  CA  TYR A 147      33.857  59.986  41.887  1.00 33.73           C  
ATOM   1055  C   TYR A 147      34.444  60.129  43.295  1.00 33.71           C  
ATOM   1056  O   TYR A 147      33.956  59.520  44.252  1.00 34.60           O  
ATOM   1057  CB  TYR A 147      32.545  59.169  41.933  1.00 31.72           C  
ATOM   1058  CG  TYR A 147      31.896  58.998  40.577  1.00 29.14           C  
ATOM   1059  CD1 TYR A 147      32.238  57.937  39.738  1.00 27.10           C  
ATOM   1060  CD2 TYR A 147      31.006  59.958  40.093  1.00 29.70           C  
ATOM   1061  CE1 TYR A 147      31.724  57.848  38.448  1.00 28.04           C  
ATOM   1062  CE2 TYR A 147      30.481  59.878  38.806  1.00 30.31           C  
ATOM   1063  CZ  TYR A 147      30.843  58.819  37.986  1.00 30.13           C  
ATOM   1064  OH  TYR A 147      30.316  58.749  36.710  1.00 31.52           O  
ATOM   1065  N   PRO A 148      35.484  60.965  43.440  1.00 34.02           N  
ATOM   1066  CA  PRO A 148      36.164  61.202  44.716  1.00 32.89           C  
ATOM   1067  C   PRO A 148      35.266  61.462  45.917  1.00 32.14           C  
ATOM   1068  O   PRO A 148      35.610  61.081  47.029  1.00 30.68           O  
ATOM   1069  CB  PRO A 148      37.080  62.381  44.401  1.00 35.15           C  
ATOM   1070  CG  PRO A 148      36.299  63.133  43.375  1.00 36.45           C  
ATOM   1071  CD  PRO A 148      35.856  62.006  42.467  1.00 34.24           C  
ATOM   1072  N   TRP A 149      34.114  62.093  45.712  1.00 31.99           N  
ATOM   1073  CA  TRP A 149      33.230  62.367  46.844  1.00 31.60           C  
ATOM   1074  C   TRP A 149      32.745  61.054  47.487  1.00 31.16           C  
ATOM   1075  O   TRP A 149      32.384  61.025  48.668  1.00 30.41           O  
ATOM   1076  CB  TRP A 149      32.040  63.234  46.401  1.00 33.75           C  
ATOM   1077  CG  TRP A 149      30.846  62.464  45.878  1.00 36.45           C  
ATOM   1078  CD1 TRP A 149      29.933  61.748  46.613  1.00 37.12           C  
ATOM   1079  CD2 TRP A 149      30.459  62.315  44.511  1.00 36.56           C  
ATOM   1080  NE1 TRP A 149      29.007  61.158  45.783  1.00 36.75           N  
ATOM   1081  CE2 TRP A 149      29.309  61.485  44.487  1.00 37.35           C  
ATOM   1082  CE3 TRP A 149      30.978  62.789  43.302  1.00 36.96           C  
ATOM   1083  CZ2 TRP A 149      28.663  61.134  43.301  1.00 37.39           C  
ATOM   1084  CZ3 TRP A 149      30.337  62.441  42.123  1.00 38.75           C  
ATOM   1085  CH2 TRP A 149      29.193  61.614  42.133  1.00 38.76           C  
ATOM   1086  N   LEU A 150      32.734  59.977  46.703  1.00 29.90           N  
ATOM   1087  CA  LEU A 150      32.322  58.658  47.193  1.00 30.30           C  
ATOM   1088  C   LEU A 150      33.523  57.933  47.766  1.00 30.54           C  
ATOM   1089  O   LEU A 150      33.425  57.235  48.771  1.00 28.84           O  
ATOM   1090  CB  LEU A 150      31.734  57.814  46.064  1.00 31.81           C  
ATOM   1091  CG  LEU A 150      30.256  58.039  45.755  1.00 33.71           C  
ATOM   1092  CD1 LEU A 150      29.810  57.097  44.640  1.00 31.79           C  
ATOM   1093  CD2 LEU A 150      29.441  57.803  47.033  1.00 32.21           C  
ATOM   1094  N   TYR A 151      34.665  58.103  47.108  1.00 32.12           N  
ATOM   1095  CA  TYR A 151      35.912  57.489  47.549  1.00 32.96           C  
ATOM   1096  C   TYR A 151      36.308  57.916  48.972  1.00 33.34           C  
ATOM   1097  O   TYR A 151      36.693  57.086  49.801  1.00 33.47           O  
ATOM   1098  CB  TYR A 151      37.036  57.868  46.582  1.00 34.09           C  
ATOM   1099  CG  TYR A 151      38.404  57.452  47.058  1.00 35.64           C  
ATOM   1100  CD1 TYR A 151      38.792  56.116  47.020  1.00 36.55           C  
ATOM   1101  CD2 TYR A 151      39.293  58.386  47.601  1.00 36.07           C  
ATOM   1102  CE1 TYR A 151      40.026  55.708  47.514  1.00 37.75           C  
ATOM   1103  CE2 TYR A 151      40.535  57.987  48.101  1.00 37.62           C  
ATOM   1104  CZ  TYR A 151      40.891  56.642  48.053  1.00 38.47           C  
ATOM   1105  OH  TYR A 151      42.103  56.214  48.544  1.00 40.79           O  
ATOM   1106  N   GLN A 152      36.216  59.216  49.246  1.00 34.55           N  
ATOM   1107  CA  GLN A 152      36.593  59.760  50.547  1.00 36.04           C  
ATOM   1108  C   GLN A 152      35.853  59.178  51.747  1.00 35.59           C  
ATOM   1109  O   GLN A 152      36.324  59.287  52.876  1.00 36.39           O  
ATOM   1110  CB  GLN A 152      36.461  61.289  50.543  1.00 37.86           C  
ATOM   1111  CG  GLN A 152      37.745  62.005  50.126  1.00 42.71           C  
ATOM   1112  CD  GLN A 152      37.621  62.734  48.792  1.00 46.43           C  
ATOM   1113  OE1 GLN A 152      36.893  63.730  48.675  1.00 48.28           O  
ATOM   1114  NE2 GLN A 152      38.333  62.240  47.776  1.00 46.58           N  
ATOM   1115  N   VAL A 153      34.704  58.560  51.510  1.00 34.56           N  
ATOM   1116  CA  VAL A 153      33.942  57.954  52.592  1.00 33.88           C  
ATOM   1117  C   VAL A 153      33.669  56.484  52.275  1.00 33.13           C  
ATOM   1118  O   VAL A 153      32.744  55.877  52.817  1.00 32.60           O  
ATOM   1119  CB  VAL A 153      32.607  58.684  52.799  1.00 35.03           C  
ATOM   1120  CG1 VAL A 153      32.870  60.134  53.210  1.00 36.41           C  
ATOM   1121  CG2 VAL A 153      31.786  58.638  51.514  1.00 34.68           C  
ATOM   1122  N   PHE A 154      34.490  55.922  51.393  1.00 31.97           N  
ATOM   1123  CA  PHE A 154      34.362  54.530  50.976  1.00 31.28           C  
ATOM   1124  C   PHE A 154      34.429  53.580  52.165  1.00 31.51           C  
ATOM   1125  O   PHE A 154      33.534  52.758  52.373  1.00 31.03           O  
ATOM   1126  CB  PHE A 154      35.475  54.166  49.985  1.00 29.42           C  
ATOM   1127  CG  PHE A 154      35.322  52.795  49.366  1.00 28.92           C  
ATOM   1128  CD1 PHE A 154      34.411  52.574  48.335  1.00 28.76           C  
ATOM   1129  CD2 PHE A 154      36.081  51.722  49.828  1.00 28.01           C  
ATOM   1130  CE1 PHE A 154      34.258  51.299  47.771  1.00 28.95           C  
ATOM   1131  CE2 PHE A 154      35.941  50.448  49.277  1.00 27.98           C  
ATOM   1132  CZ  PHE A 154      35.028  50.234  48.246  1.00 28.70           C  
ATOM   1133  N   ASP A 155      35.492  53.694  52.947  1.00 30.94           N  
ATOM   1134  CA  ASP A 155      35.667  52.812  54.087  1.00 32.69           C  
ATOM   1135  C   ASP A 155      34.699  53.114  55.206  1.00 31.87           C  
ATOM   1136  O   ASP A 155      34.137  52.205  55.812  1.00 31.41           O  
ATOM   1137  CB  ASP A 155      37.099  52.900  54.622  1.00 36.72           C  
ATOM   1138  CG  ASP A 155      38.122  52.347  53.648  1.00 40.11           C  
ATOM   1139  OD1 ASP A 155      38.434  53.031  52.653  1.00 43.34           O  
ATOM   1140  OD2 ASP A 155      38.609  51.218  53.876  1.00 44.07           O  
ATOM   1141  N   SER A 156      34.497  54.397  55.472  1.00 30.74           N  
ATOM   1142  CA  SER A 156      33.615  54.811  56.552  1.00 29.21           C  
ATOM   1143  C   SER A 156      32.141  54.506  56.388  1.00 27.87           C  
ATOM   1144  O   SER A 156      31.497  54.050  57.330  1.00 29.72           O  
ATOM   1145  CB  SER A 156      33.773  56.312  56.812  1.00 29.36           C  
ATOM   1146  OG  SER A 156      33.555  57.067  55.627  1.00 30.41           O  
ATOM   1147  N   GLU A 157      31.586  54.741  55.207  1.00 24.84           N  
ATOM   1148  CA  GLU A 157      30.157  54.524  55.078  1.00 24.16           C  
ATOM   1149  C   GLU A 157      29.637  53.772  53.873  1.00 21.15           C  
ATOM   1150  O   GLU A 157      28.505  53.321  53.887  1.00 22.62           O  
ATOM   1151  CB  GLU A 157      29.441  55.875  55.151  1.00 26.56           C  
ATOM   1152  CG  GLU A 157      29.976  56.912  54.176  1.00 27.71           C  
ATOM   1153  CD  GLU A 157      29.147  58.196  54.155  1.00 30.65           C  
ATOM   1154  OE1 GLU A 157      28.181  58.292  53.357  1.00 29.88           O  
ATOM   1155  OE2 GLU A 157      29.464  59.112  54.948  1.00 30.10           O  
ATOM   1156  N   VAL A 158      30.445  53.618  52.835  1.00 16.66           N  
ATOM   1157  CA  VAL A 158      29.952  52.958  51.650  1.00 15.44           C  
ATOM   1158  C   VAL A 158      30.098  51.445  51.554  1.00 15.14           C  
ATOM   1159  O   VAL A 158      29.121  50.732  51.295  1.00 15.20           O  
ATOM   1160  CB  VAL A 158      30.580  53.566  50.397  1.00 15.43           C  
ATOM   1161  CG1 VAL A 158      30.174  52.751  49.177  1.00 10.27           C  
ATOM   1162  CG2 VAL A 158      30.149  55.037  50.246  1.00 14.21           C  
ATOM   1163  N   GLU A 159      31.303  50.947  51.784  1.00 15.10           N  
ATOM   1164  CA  GLU A 159      31.530  49.532  51.636  1.00 16.16           C  
ATOM   1165  C   GLU A 159      31.127  48.595  52.745  1.00 16.70           C  
ATOM   1166  O   GLU A 159      31.445  48.803  53.906  1.00 16.41           O  
ATOM   1167  CB  GLU A 159      32.994  49.263  51.288  1.00 18.89           C  
ATOM   1168  CG  GLU A 159      33.292  47.762  51.072  1.00 22.26           C  
ATOM   1169  CD  GLU A 159      34.730  47.487  50.651  1.00 25.07           C  
ATOM   1170  OE1 GLU A 159      35.643  47.608  51.507  1.00 23.19           O  
ATOM   1171  OE2 GLU A 159      34.941  47.161  49.456  1.00 25.21           O  
ATOM   1172  N   LEU A 160      30.412  47.554  52.334  1.00 15.89           N  
ATOM   1173  CA  LEU A 160      30.017  46.475  53.213  1.00 15.15           C  
ATOM   1174  C   LEU A 160      30.776  45.297  52.588  1.00 16.14           C  
ATOM   1175  O   LEU A 160      30.610  44.999  51.404  1.00 16.98           O  
ATOM   1176  CB  LEU A 160      28.517  46.206  53.157  1.00 12.82           C  
ATOM   1177  CG  LEU A 160      28.146  44.970  53.983  1.00 13.16           C  
ATOM   1178  CD1 LEU A 160      28.235  45.330  55.462  1.00 12.66           C  
ATOM   1179  CD2 LEU A 160      26.741  44.470  53.627  1.00 11.13           C  
HETATM 1180  N   MSE A 161      31.660  44.666  53.345  1.00 18.58           N  
HETATM 1181  CA  MSE A 161      32.412  43.548  52.802  1.00 18.51           C  
HETATM 1182  C   MSE A 161      31.658  42.263  53.091  1.00 17.30           C  
HETATM 1183  O   MSE A 161      31.330  42.000  54.235  1.00 17.51           O  
HETATM 1184  CB  MSE A 161      33.795  43.490  53.443  1.00 22.90           C  
HETATM 1185  CG  MSE A 161      34.885  44.164  52.615  1.00 32.22           C  
HETATM 1186 SE   MSE A 161      35.259  43.135  51.020  1.00 38.48          SE  
HETATM 1187  CE  MSE A 161      36.093  41.607  51.833  1.00 39.12           C  
ATOM   1188  N   GLN A 162      31.372  41.461  52.072  1.00 15.38           N  
ATOM   1189  CA  GLN A 162      30.666  40.210  52.329  1.00 17.81           C  
ATOM   1190  C   GLN A 162      31.599  39.221  53.003  1.00 16.22           C  
ATOM   1191  O   GLN A 162      32.809  39.427  53.042  1.00 16.14           O  
ATOM   1192  CB  GLN A 162      30.107  39.596  51.038  1.00 18.70           C  
ATOM   1193  CG  GLN A 162      31.144  39.193  50.017  1.00 20.77           C  
ATOM   1194  CD  GLN A 162      30.516  38.590  48.766  1.00 24.57           C  
ATOM   1195  OE1 GLN A 162      29.382  38.933  48.390  1.00 22.67           O  
ATOM   1196  NE2 GLN A 162      31.258  37.695  48.102  1.00 25.79           N  
ATOM   1197  N   ASN A 163      31.026  38.165  53.566  1.00 17.00           N  
ATOM   1198  CA  ASN A 163      31.819  37.139  54.237  1.00 16.79           C  
ATOM   1199  C   ASN A 163      32.316  36.112  53.225  1.00 16.03           C  
ATOM   1200  O   ASN A 163      31.965  36.157  52.044  1.00 13.41           O  
ATOM   1201  CB  ASN A 163      30.989  36.404  55.289  1.00 17.59           C  
ATOM   1202  CG  ASN A 163      30.663  37.268  56.504  1.00 19.28           C  
ATOM   1203  OD1 ASN A 163      31.544  37.667  57.277  1.00 20.59           O  
ATOM   1204  ND2 ASN A 163      29.392  37.551  56.678  1.00 17.25           N  
ATOM   1205  N   GLN A 164      33.111  35.181  53.733  1.00 15.34           N  
ATOM   1206  CA  GLN A 164      33.687  34.100  52.961  1.00 16.26           C  
ATOM   1207  C   GLN A 164      33.448  32.857  53.792  1.00 14.72           C  
ATOM   1208  O   GLN A 164      33.698  32.883  54.996  1.00 12.25           O  
ATOM   1209  CB  GLN A 164      35.186  34.295  52.830  1.00 20.43           C  
ATOM   1210  CG  GLN A 164      35.677  34.561  51.447  1.00 26.65           C  
ATOM   1211  CD  GLN A 164      37.187  34.639  51.409  1.00 29.94           C  
ATOM   1212  OE1 GLN A 164      37.793  34.664  50.342  1.00 30.75           O  
ATOM   1213  NE2 GLN A 164      37.801  34.683  52.585  1.00 29.35           N  
ATOM   1214  N   VAL A 165      32.958  31.787  53.164  1.00 13.36           N  
ATOM   1215  CA  VAL A 165      32.686  30.536  53.857  1.00 12.48           C  
ATOM   1216  C   VAL A 165      33.438  29.406  53.185  1.00 13.62           C  
ATOM   1217  O   VAL A 165      33.738  29.463  51.988  1.00 12.53           O  
ATOM   1218  CB  VAL A 165      31.190  30.211  53.879  1.00 12.27           C  
ATOM   1219  CG1 VAL A 165      30.450  31.225  54.757  1.00 12.76           C  
ATOM   1220  CG2 VAL A 165      30.643  30.221  52.475  1.00 11.99           C  
ATOM   1221  N   PRO A 166      33.755  28.357  53.953  1.00 14.53           N  
ATOM   1222  CA  PRO A 166      34.495  27.225  53.403  1.00 14.16           C  
ATOM   1223  C   PRO A 166      33.710  26.248  52.544  1.00 13.92           C  
ATOM   1224  O   PRO A 166      32.613  25.835  52.906  1.00 14.35           O  
ATOM   1225  CB  PRO A 166      35.081  26.560  54.653  1.00 14.62           C  
ATOM   1226  CG  PRO A 166      34.020  26.803  55.697  1.00 15.43           C  
ATOM   1227  CD  PRO A 166      33.595  28.239  55.419  1.00 14.56           C  
ATOM   1228  N   LYS A 167      34.277  25.899  51.392  1.00 13.51           N  
ATOM   1229  CA  LYS A 167      33.667  24.903  50.509  1.00 14.92           C  
ATOM   1230  C   LYS A 167      33.823  23.588  51.292  1.00 14.43           C  
ATOM   1231  O   LYS A 167      34.832  23.389  51.966  1.00 13.09           O  
ATOM   1232  CB  LYS A 167      34.434  24.834  49.184  1.00 16.11           C  
ATOM   1233  CG  LYS A 167      34.486  26.162  48.423  1.00 13.38           C  
ATOM   1234  CD  LYS A 167      35.284  25.997  47.124  1.00 14.77           C  
ATOM   1235  CE  LYS A 167      35.271  27.298  46.318  1.00 14.33           C  
ATOM   1236  NZ  LYS A 167      36.301  27.357  45.262  1.00 13.70           N  
ATOM   1237  N   ILE A 168      32.830  22.712  51.235  1.00 12.91           N  
ATOM   1238  CA  ILE A 168      32.894  21.475  51.997  1.00 16.04           C  
ATOM   1239  C   ILE A 168      32.808  20.230  51.119  1.00 16.19           C  
ATOM   1240  O   ILE A 168      32.037  20.181  50.164  1.00 17.22           O  
ATOM   1241  CB  ILE A 168      31.764  21.431  53.083  1.00 16.40           C  
ATOM   1242  CG1 ILE A 168      30.387  21.503  52.430  1.00 14.40           C  
ATOM   1243  CG2 ILE A 168      31.916  22.605  54.051  1.00 18.72           C  
ATOM   1244  CD1 ILE A 168      29.230  21.385  53.414  1.00 13.77           C  
ATOM   1245  N   LEU A 169      33.619  19.233  51.447  1.00 16.75           N  
ATOM   1246  CA  LEU A 169      33.656  17.983  50.689  1.00 17.70           C  
ATOM   1247  C   LEU A 169      32.263  17.374  50.659  1.00 17.09           C  
ATOM   1248  O   LEU A 169      31.592  17.282  51.687  1.00 16.81           O  
ATOM   1249  CB  LEU A 169      34.661  17.013  51.327  1.00 15.45           C  
ATOM   1250  CG  LEU A 169      36.094  17.568  51.372  1.00 18.66           C  
ATOM   1251  CD1 LEU A 169      37.019  16.630  52.149  1.00 17.27           C  
ATOM   1252  CD2 LEU A 169      36.608  17.764  49.949  1.00 17.85           C  
ATOM   1253  N   GLN A 170      31.834  16.977  49.469  1.00 19.53           N  
ATOM   1254  CA  GLN A 170      30.516  16.385  49.272  1.00 23.31           C  
ATOM   1255  C   GLN A 170      30.201  15.162  50.126  1.00 25.80           C  
ATOM   1256  O   GLN A 170      29.061  14.970  50.543  1.00 26.47           O  
ATOM   1257  CB  GLN A 170      30.318  16.030  47.799  1.00 22.67           C  
ATOM   1258  CG  GLN A 170      29.974  17.233  46.913  1.00 25.94           C  
ATOM   1259  CD  GLN A 170      29.417  16.814  45.564  1.00 27.33           C  
ATOM   1260  OE1 GLN A 170      28.863  15.719  45.428  1.00 28.98           O  
ATOM   1261  NE2 GLN A 170      29.542  17.687  44.565  1.00 27.43           N  
ATOM   1262  N   ASP A 171      31.205  14.340  50.401  1.00 29.36           N  
ATOM   1263  CA  ASP A 171      30.976  13.133  51.188  1.00 32.23           C  
ATOM   1264  C   ASP A 171      30.780  13.361  52.668  1.00 31.80           C  
ATOM   1265  O   ASP A 171      29.683  13.187  53.198  1.00 33.00           O  
ATOM   1266  CB  ASP A 171      32.131  12.151  51.008  1.00 35.28           C  
ATOM   1267  CG  ASP A 171      32.239  11.648  49.590  1.00 39.44           C  
ATOM   1268  OD1 ASP A 171      31.165  11.424  48.975  1.00 40.65           O  
ATOM   1269  OD2 ASP A 171      33.385  11.469  49.101  1.00 39.20           O  
ATOM   1270  N   THR A 172      31.865  13.759  53.319  1.00 29.82           N  
ATOM   1271  CA  THR A 172      31.914  13.975  54.753  1.00 25.83           C  
ATOM   1272  C   THR A 172      31.485  15.355  55.243  1.00 25.03           C  
ATOM   1273  O   THR A 172      31.276  15.551  56.445  1.00 25.83           O  
ATOM   1274  CB  THR A 172      33.333  13.736  55.224  1.00 25.94           C  
ATOM   1275  OG1 THR A 172      34.156  14.795  54.732  1.00 24.45           O  
ATOM   1276  CG2 THR A 172      33.868  12.414  54.647  1.00 24.78           C  
ATOM   1277  N   LEU A 173      31.368  16.316  54.333  1.00 21.82           N  
ATOM   1278  CA  LEU A 173      30.997  17.680  54.712  1.00 21.51           C  
ATOM   1279  C   LEU A 173      32.106  18.354  55.500  1.00 21.35           C  
ATOM   1280  O   LEU A 173      31.842  19.293  56.259  1.00 21.58           O  
ATOM   1281  CB  LEU A 173      29.710  17.694  55.544  1.00 19.78           C  
ATOM   1282  CG  LEU A 173      28.541  17.007  54.858  1.00 19.48           C  
ATOM   1283  CD1 LEU A 173      27.264  17.224  55.674  1.00 20.90           C  
ATOM   1284  CD2 LEU A 173      28.394  17.551  53.427  1.00 18.47           C  
ATOM   1285  N   GLU A 174      33.335  17.858  55.337  1.00 20.34           N  
ATOM   1286  CA  GLU A 174      34.497  18.433  56.014  1.00 20.19           C  
ATOM   1287  C   GLU A 174      34.965  19.589  55.150  1.00 17.88           C  
ATOM   1288  O   GLU A 174      34.723  19.600  53.940  1.00 17.05           O  
ATOM   1289  CB  GLU A 174      35.642  17.422  56.101  1.00 21.97           C  
ATOM   1290  CG  GLU A 174      35.342  16.164  56.882  1.00 28.43           C  
ATOM   1291  CD  GLU A 174      36.401  15.076  56.669  1.00 31.84           C  
ATOM   1292  OE1 GLU A 174      36.696  14.732  55.496  1.00 34.09           O  
ATOM   1293  OE2 GLU A 174      36.930  14.558  57.680  1.00 33.56           O  
ATOM   1294  N   PRO A 175      35.643  20.577  55.741  1.00 16.95           N  
ATOM   1295  CA  PRO A 175      36.084  21.671  54.874  1.00 18.24           C  
ATOM   1296  C   PRO A 175      37.120  21.138  53.910  1.00 19.21           C  
ATOM   1297  O   PRO A 175      37.969  20.341  54.300  1.00 21.05           O  
ATOM   1298  CB  PRO A 175      36.655  22.703  55.860  1.00 16.43           C  
ATOM   1299  CG  PRO A 175      37.012  21.898  57.060  1.00 15.90           C  
ATOM   1300  CD  PRO A 175      35.893  20.889  57.151  1.00 16.94           C  
ATOM   1301  N   ALA A 176      37.041  21.539  52.647  1.00 20.10           N  
ATOM   1302  CA  ALA A 176      37.999  21.064  51.654  1.00 20.80           C  
ATOM   1303  C   ALA A 176      39.323  21.828  51.696  1.00 22.27           C  
ATOM   1304  O   ALA A 176      39.363  23.021  52.018  1.00 22.24           O  
ATOM   1305  CB  ALA A 176      37.385  21.151  50.264  1.00 20.52           C  
ATOM   1306  N   ALA A 177      40.404  21.125  51.372  1.00 21.59           N  
ATOM   1307  CA  ALA A 177      41.733  21.723  51.330  1.00 22.36           C  
ATOM   1308  C   ALA A 177      42.235  21.686  49.876  1.00 22.42           C  
ATOM   1309  O   ALA A 177      41.915  20.768  49.118  1.00 24.35           O  
ATOM   1310  CB  ALA A 177      42.701  20.954  52.261  1.00 18.72           C  
ATOM   1311  N   TRP A 178      42.990  22.699  49.484  1.00 21.21           N  
ATOM   1312  CA  TRP A 178      43.531  22.754  48.133  1.00 24.84           C  
ATOM   1313  C   TRP A 178      44.943  23.313  48.256  1.00 25.17           C  
ATOM   1314  O   TRP A 178      45.139  24.535  48.206  1.00 25.76           O  
ATOM   1315  CB  TRP A 178      42.684  23.671  47.236  1.00 24.98           C  
ATOM   1316  CG  TRP A 178      43.018  23.567  45.770  1.00 25.38           C  
ATOM   1317  CD1 TRP A 178      43.281  24.596  44.918  1.00 27.56           C  
ATOM   1318  CD2 TRP A 178      43.135  22.367  44.995  1.00 25.73           C  
ATOM   1319  NE1 TRP A 178      43.558  24.115  43.663  1.00 27.69           N  
ATOM   1320  CE2 TRP A 178      43.474  22.750  43.681  1.00 25.27           C  
ATOM   1321  CE3 TRP A 178      42.978  21.003  45.282  1.00 25.54           C  
ATOM   1322  CZ2 TRP A 178      43.672  21.817  42.651  1.00 27.20           C  
ATOM   1323  CZ3 TRP A 178      43.172  20.070  44.252  1.00 25.12           C  
ATOM   1324  CH2 TRP A 178      43.514  20.485  42.957  1.00 25.99           C  
ATOM   1325  N   ALA A 179      45.908  22.407  48.434  1.00 23.85           N  
ATOM   1326  CA  ALA A 179      47.319  22.760  48.591  1.00 25.40           C  
ATOM   1327  C   ALA A 179      47.827  23.736  47.537  1.00 25.09           C  
ATOM   1328  O   ALA A 179      48.497  24.709  47.854  1.00 27.08           O  
ATOM   1329  CB  ALA A 179      48.177  21.487  48.577  1.00 23.21           C  
ATOM   1330  N   GLU A 180      47.504  23.470  46.283  1.00 27.00           N  
ATOM   1331  CA  GLU A 180      47.936  24.317  45.177  1.00 28.85           C  
ATOM   1332  C   GLU A 180      47.564  25.798  45.325  1.00 27.33           C  
ATOM   1333  O   GLU A 180      48.359  26.688  45.005  1.00 26.49           O  
ATOM   1334  CB  GLU A 180      47.349  23.772  43.878  1.00 32.52           C  
ATOM   1335  CG  GLU A 180      47.937  24.373  42.627  1.00 38.79           C  
ATOM   1336  CD  GLU A 180      47.244  23.874  41.366  1.00 42.46           C  
ATOM   1337  OE1 GLU A 180      46.996  22.646  41.262  1.00 44.02           O  
ATOM   1338  OE2 GLU A 180      46.960  24.713  40.478  1.00 43.12           O  
ATOM   1339  N   ASN A 181      46.355  26.063  45.807  1.00 26.05           N  
ATOM   1340  CA  ASN A 181      45.883  27.435  45.972  1.00 23.20           C  
ATOM   1341  C   ASN A 181      44.824  27.404  47.067  1.00 21.60           C  
ATOM   1342  O   ASN A 181      43.634  27.255  46.796  1.00 20.10           O  
ATOM   1343  CB  ASN A 181      45.264  27.928  44.656  1.00 25.12           C  
ATOM   1344  CG  ASN A 181      44.984  29.434  44.649  1.00 27.73           C  
ATOM   1345  OD1 ASN A 181      44.843  30.072  45.695  1.00 30.67           O  
ATOM   1346  ND2 ASN A 181      44.883  29.999  43.456  1.00 28.54           N  
ATOM   1347  N   PRO A 182      45.252  27.521  48.327  1.00 20.65           N  
ATOM   1348  CA  PRO A 182      44.313  27.499  49.447  1.00 19.29           C  
ATOM   1349  C   PRO A 182      43.194  28.549  49.383  1.00 19.45           C  
ATOM   1350  O   PRO A 182      42.138  28.369  49.982  1.00 18.57           O  
ATOM   1351  CB  PRO A 182      45.235  27.662  50.657  1.00 21.37           C  
ATOM   1352  CG  PRO A 182      46.488  26.885  50.207  1.00 20.77           C  
ATOM   1353  CD  PRO A 182      46.650  27.435  48.803  1.00 20.79           C  
ATOM   1354  N   ALA A 183      43.403  29.643  48.662  1.00 19.44           N  
ATOM   1355  CA  ALA A 183      42.344  30.648  48.565  1.00 20.08           C  
ATOM   1356  C   ALA A 183      41.098  30.023  47.915  1.00 19.16           C  
ATOM   1357  O   ALA A 183      39.989  30.545  48.064  1.00 18.89           O  
ATOM   1358  CB  ALA A 183      42.821  31.846  47.751  1.00 18.99           C  
ATOM   1359  N   TYR A 184      41.285  28.912  47.194  1.00 18.32           N  
ATOM   1360  CA  TYR A 184      40.167  28.213  46.548  1.00 18.32           C  
ATOM   1361  C   TYR A 184      39.341  27.386  47.540  1.00 17.45           C  
ATOM   1362  O   TYR A 184      38.365  26.757  47.157  1.00 16.75           O  
ATOM   1363  CB  TYR A 184      40.663  27.306  45.414  1.00 19.49           C  
ATOM   1364  CG  TYR A 184      41.055  28.050  44.147  1.00 23.35           C  
ATOM   1365  CD1 TYR A 184      41.557  27.364  43.035  1.00 25.28           C  
ATOM   1366  CD2 TYR A 184      40.944  29.443  44.065  1.00 26.50           C  
ATOM   1367  CE1 TYR A 184      41.942  28.047  41.872  1.00 26.98           C  
ATOM   1368  CE2 TYR A 184      41.327  30.136  42.915  1.00 27.80           C  
ATOM   1369  CZ  TYR A 184      41.826  29.431  41.822  1.00 28.86           C  
ATOM   1370  OH  TYR A 184      42.220  30.116  40.693  1.00 30.81           O  
ATOM   1371  N   GLU A 185      39.732  27.410  48.813  1.00 17.54           N  
ATOM   1372  CA  GLU A 185      39.013  26.692  49.873  1.00 17.34           C  
ATOM   1373  C   GLU A 185      37.871  27.549  50.424  1.00 16.91           C  
ATOM   1374  O   GLU A 185      37.108  27.097  51.271  1.00 17.38           O  
ATOM   1375  CB  GLU A 185      39.965  26.335  51.017  1.00 14.81           C  
ATOM   1376  CG  GLU A 185      41.072  25.368  50.607  1.00 17.09           C  
ATOM   1377  CD  GLU A 185      42.232  25.358  51.590  1.00 18.19           C  
ATOM   1378  OE1 GLU A 185      42.083  25.947  52.681  1.00 16.55           O  
ATOM   1379  OE2 GLU A 185      43.289  24.762  51.269  1.00 19.78           O  
ATOM   1380  N   TRP A 186      37.751  28.779  49.932  1.00 16.79           N  
ATOM   1381  CA  TRP A 186      36.694  29.688  50.384  1.00 17.37           C  
ATOM   1382  C   TRP A 186      35.828  30.200  49.240  1.00 18.37           C  
ATOM   1383  O   TRP A 186      36.323  30.457  48.141  1.00 19.55           O  
ATOM   1384  CB  TRP A 186      37.303  30.889  51.108  1.00 16.43           C  
ATOM   1385  CG  TRP A 186      38.175  30.501  52.246  1.00 15.95           C  
ATOM   1386  CD1 TRP A 186      39.506  30.161  52.196  1.00 15.51           C  
ATOM   1387  CD2 TRP A 186      37.778  30.365  53.613  1.00 14.06           C  
ATOM   1388  NE1 TRP A 186      39.951  29.817  53.449  1.00 16.75           N  
ATOM   1389  CE2 TRP A 186      38.907  29.923  54.335  1.00 14.56           C  
ATOM   1390  CE3 TRP A 186      36.570  30.552  54.293  1.00 12.10           C  
ATOM   1391  CZ2 TRP A 186      38.868  29.694  55.705  1.00 17.20           C  
ATOM   1392  CZ3 TRP A 186      36.530  30.324  55.656  1.00 12.52           C  
ATOM   1393  CH2 TRP A 186      37.665  29.888  56.346  1.00 16.94           C  
ATOM   1394  N   ALA A 187      34.535  30.356  49.494  1.00 19.84           N  
ATOM   1395  CA  ALA A 187      33.630  30.864  48.464  1.00 19.60           C  
ATOM   1396  C   ALA A 187      32.641  31.878  49.020  1.00 20.25           C  
ATOM   1397  O   ALA A 187      32.333  31.883  50.210  1.00 17.60           O  
ATOM   1398  CB  ALA A 187      32.871  29.722  47.829  1.00 19.55           C  
ATOM   1399  N   PRO A 188      32.142  32.775  48.158  1.00 22.94           N  
ATOM   1400  CA  PRO A 188      31.177  33.759  48.648  1.00 22.40           C  
ATOM   1401  C   PRO A 188      29.947  32.961  49.078  1.00 21.03           C  
ATOM   1402  O   PRO A 188      29.715  31.855  48.584  1.00 20.25           O  
ATOM   1403  CB  PRO A 188      30.937  34.641  47.421  1.00 24.33           C  
ATOM   1404  CG  PRO A 188      31.126  33.695  46.281  1.00 23.77           C  
ATOM   1405  CD  PRO A 188      32.366  32.935  46.710  1.00 24.23           C  
ATOM   1406  N   PRO A 189      29.159  33.493  50.025  1.00 20.28           N  
ATOM   1407  CA  PRO A 189      27.964  32.772  50.492  1.00 18.54           C  
ATOM   1408  C   PRO A 189      26.627  33.172  49.859  1.00 16.58           C  
ATOM   1409  O   PRO A 189      25.569  32.838  50.384  1.00 17.51           O  
ATOM   1410  CB  PRO A 189      27.993  33.034  51.993  1.00 18.95           C  
ATOM   1411  CG  PRO A 189      28.469  34.457  52.043  1.00 20.60           C  
ATOM   1412  CD  PRO A 189      29.535  34.569  50.962  1.00 17.96           C  
ATOM   1413  N   GLY A 190      26.672  33.857  48.722  1.00 15.54           N  
ATOM   1414  CA  GLY A 190      25.436  34.295  48.083  1.00 13.84           C  
ATOM   1415  C   GLY A 190      25.053  35.678  48.583  1.00 12.23           C  
ATOM   1416  O   GLY A 190      25.561  36.116  49.633  1.00 12.62           O  
ATOM   1417  N   HIS A 191      24.205  36.402  47.840  1.00 12.85           N  
ATOM   1418  CA  HIS A 191      23.867  37.772  48.302  1.00 12.81           C  
ATOM   1419  C   HIS A 191      23.044  37.734  49.591  1.00 13.71           C  
ATOM   1420  O   HIS A 191      22.924  38.725  50.295  1.00 13.17           O  
ATOM   1421  CB  HIS A 191      23.176  38.640  47.235  1.00 13.94           C  
ATOM   1422  CG  HIS A 191      22.188  37.862  46.355  1.00 11.24           C  
ATOM   1423  ND1 HIS A 191      20.982  37.386  46.814  1.00 13.40           N  
ATOM   1424  CD2 HIS A 191      22.283  37.473  45.066  1.00  8.24           C  
ATOM   1425  CE1 HIS A 191      20.368  36.736  45.843  1.00 14.11           C  
ATOM   1426  NE2 HIS A 191      21.137  36.776  44.769  1.00 10.86           N  
ATOM   1427  N   GLY A 192      22.461  36.583  49.905  1.00 13.13           N  
ATOM   1428  CA  GLY A 192      21.679  36.432  51.121  1.00 12.46           C  
ATOM   1429  C   GLY A 192      22.573  36.714  52.324  1.00 13.94           C  
ATOM   1430  O   GLY A 192      22.108  36.873  53.449  1.00 12.83           O  
ATOM   1431  N   ASP A 193      23.880  36.766  52.074  1.00 14.37           N  
ATOM   1432  CA  ASP A 193      24.880  37.053  53.104  1.00 13.00           C  
ATOM   1433  C   ASP A 193      24.840  38.510  53.578  1.00 12.21           C  
ATOM   1434  O   ASP A 193      25.457  38.856  54.583  1.00 12.88           O  
ATOM   1435  CB  ASP A 193      26.273  36.757  52.557  1.00 14.17           C  
ATOM   1436  CG  ASP A 193      27.360  37.050  53.557  1.00 17.24           C  
ATOM   1437  OD1 ASP A 193      28.244  37.892  53.265  1.00 17.86           O  
ATOM   1438  OD2 ASP A 193      27.328  36.437  54.643  1.00 17.37           O  
ATOM   1439  N   ILE A 194      24.141  39.372  52.844  1.00 11.35           N  
ATOM   1440  CA  ILE A 194      24.050  40.780  53.225  1.00  9.81           C  
ATOM   1441  C   ILE A 194      23.537  40.956  54.665  1.00 10.86           C  
ATOM   1442  O   ILE A 194      24.086  41.738  55.435  1.00 11.03           O  
ATOM   1443  CB  ILE A 194      23.107  41.567  52.252  1.00 11.51           C  
ATOM   1444  CG1 ILE A 194      22.981  43.028  52.704  1.00 10.31           C  
ATOM   1445  CG2 ILE A 194      21.722  40.933  52.210  1.00  7.33           C  
ATOM   1446  CD1 ILE A 194      22.292  43.931  51.694  1.00 12.23           C  
ATOM   1447  N   TYR A 195      22.494  40.220  55.039  1.00 12.17           N  
ATOM   1448  CA  TYR A 195      21.935  40.360  56.382  1.00 12.72           C  
ATOM   1449  C   TYR A 195      22.968  39.985  57.436  1.00 13.44           C  
ATOM   1450  O   TYR A 195      23.159  40.686  58.432  1.00 13.89           O  
ATOM   1451  CB  TYR A 195      20.682  39.488  56.537  1.00 13.08           C  
ATOM   1452  CG  TYR A 195      19.640  39.704  55.458  1.00 13.44           C  
ATOM   1453  CD1 TYR A 195      19.413  38.737  54.488  1.00 13.59           C  
ATOM   1454  CD2 TYR A 195      18.914  40.893  55.383  1.00 13.09           C  
ATOM   1455  CE1 TYR A 195      18.498  38.941  53.476  1.00 13.79           C  
ATOM   1456  CE2 TYR A 195      17.991  41.107  54.357  1.00 12.75           C  
ATOM   1457  CZ  TYR A 195      17.789  40.132  53.413  1.00 12.08           C  
ATOM   1458  OH  TYR A 195      16.886  40.331  52.390  1.00 11.61           O  
ATOM   1459  N   THR A 196      23.632  38.867  57.195  1.00 14.37           N  
ATOM   1460  CA  THR A 196      24.658  38.359  58.083  1.00 13.83           C  
ATOM   1461  C   THR A 196      25.815  39.346  58.223  1.00 13.05           C  
ATOM   1462  O   THR A 196      26.262  39.614  59.332  1.00 15.30           O  
ATOM   1463  CB  THR A 196      25.223  37.036  57.530  1.00 16.36           C  
ATOM   1464  OG1 THR A 196      24.143  36.150  57.236  1.00 15.22           O  
ATOM   1465  CG2 THR A 196      26.178  36.395  58.525  1.00 14.20           C  
ATOM   1466  N   ALA A 197      26.315  39.863  57.099  1.00 12.65           N  
ATOM   1467  CA  ALA A 197      27.449  40.802  57.130  1.00 13.38           C  
ATOM   1468  C   ALA A 197      27.061  42.120  57.780  1.00 11.66           C  
ATOM   1469  O   ALA A 197      27.866  42.721  58.494  1.00 11.02           O  
ATOM   1470  CB  ALA A 197      27.985  41.066  55.717  1.00 11.97           C  
ATOM   1471  N   LEU A 198      25.835  42.570  57.506  1.00 11.64           N  
ATOM   1472  CA  LEU A 198      25.334  43.816  58.080  1.00  8.88           C  
ATOM   1473  C   LEU A 198      25.280  43.660  59.579  1.00  9.07           C  
ATOM   1474  O   LEU A 198      25.669  44.552  60.315  1.00  9.80           O  
ATOM   1475  CB  LEU A 198      23.924  44.131  57.579  1.00  8.69           C  
ATOM   1476  CG  LEU A 198      23.753  44.840  56.230  1.00 11.34           C  
ATOM   1477  CD1 LEU A 198      22.279  45.002  55.923  1.00  7.54           C  
ATOM   1478  CD2 LEU A 198      24.431  46.196  56.275  1.00  7.63           C  
ATOM   1479  N   TYR A 199      24.797  42.506  60.025  1.00 11.08           N  
ATOM   1480  CA  TYR A 199      24.646  42.232  61.446  1.00 10.86           C  
ATOM   1481  C   TYR A 199      25.970  42.024  62.176  1.00 12.29           C  
ATOM   1482  O   TYR A 199      26.249  42.679  63.192  1.00  9.03           O  
ATOM   1483  CB  TYR A 199      23.780  40.992  61.639  1.00  9.65           C  
ATOM   1484  CG  TYR A 199      23.463  40.685  63.090  1.00 10.94           C  
ATOM   1485  CD1 TYR A 199      22.339  41.222  63.697  1.00 11.05           C  
ATOM   1486  CD2 TYR A 199      24.297  39.861  63.856  1.00  9.80           C  
ATOM   1487  CE1 TYR A 199      22.038  40.953  65.026  1.00 10.97           C  
ATOM   1488  CE2 TYR A 199      24.003  39.582  65.193  1.00 10.07           C  
ATOM   1489  CZ  TYR A 199      22.865  40.134  65.766  1.00 11.30           C  
ATOM   1490  OH  TYR A 199      22.527  39.861  67.068  1.00 10.54           O  
ATOM   1491  N   GLY A 200      26.776  41.110  61.636  1.00 12.74           N  
ATOM   1492  CA  GLY A 200      28.044  40.765  62.242  1.00 14.99           C  
ATOM   1493  C   GLY A 200      29.080  41.855  62.354  1.00 16.26           C  
ATOM   1494  O   GLY A 200      29.839  41.895  63.325  1.00 18.39           O  
ATOM   1495  N   SER A 201      29.116  42.742  61.369  1.00 16.20           N  
ATOM   1496  CA  SER A 201      30.092  43.817  61.373  1.00 17.93           C  
ATOM   1497  C   SER A 201      29.681  44.923  62.322  1.00 18.15           C  
ATOM   1498  O   SER A 201      30.483  45.807  62.623  1.00 20.83           O  
ATOM   1499  CB  SER A 201      30.249  44.394  59.958  1.00 17.70           C  
ATOM   1500  OG  SER A 201      29.003  44.840  59.446  1.00 21.45           O  
ATOM   1501  N   GLY A 202      28.434  44.874  62.779  1.00 18.95           N  
ATOM   1502  CA  GLY A 202      27.914  45.900  63.672  1.00 18.70           C  
ATOM   1503  C   GLY A 202      27.341  47.080  62.893  1.00 18.45           C  
ATOM   1504  O   GLY A 202      26.895  48.070  63.462  1.00 17.89           O  
ATOM   1505  N   LYS A 203      27.345  46.977  61.573  1.00 18.64           N  
ATOM   1506  CA  LYS A 203      26.844  48.066  60.750  1.00 20.32           C  
ATOM   1507  C   LYS A 203      25.320  48.195  60.853  1.00 19.71           C  
ATOM   1508  O   LYS A 203      24.783  49.306  60.910  1.00 18.79           O  
ATOM   1509  CB  LYS A 203      27.296  47.864  59.290  1.00 23.55           C  
ATOM   1510  CG  LYS A 203      26.802  48.932  58.318  1.00 27.17           C  
ATOM   1511  CD  LYS A 203      27.360  50.328  58.607  1.00 30.43           C  
ATOM   1512  CE  LYS A 203      28.829  50.432  58.231  1.00 33.71           C  
ATOM   1513  NZ  LYS A 203      29.267  51.851  58.112  1.00 34.71           N  
ATOM   1514  N   LEU A 204      24.621  47.062  60.896  1.00 18.29           N  
ATOM   1515  CA  LEU A 204      23.172  47.096  61.007  1.00 15.66           C  
ATOM   1516  C   LEU A 204      22.779  47.859  62.265  1.00 15.60           C  
ATOM   1517  O   LEU A 204      21.912  48.733  62.227  1.00 15.59           O  
ATOM   1518  CB  LEU A 204      22.588  45.673  61.043  1.00 13.87           C  
ATOM   1519  CG  LEU A 204      21.062  45.628  61.219  1.00 13.19           C  
ATOM   1520  CD1 LEU A 204      20.405  46.458  60.120  1.00  8.89           C  
ATOM   1521  CD2 LEU A 204      20.544  44.179  61.168  1.00 10.74           C  
ATOM   1522  N   GLN A 205      23.416  47.535  63.387  1.00 16.96           N  
ATOM   1523  CA  GLN A 205      23.110  48.217  64.638  1.00 17.57           C  
ATOM   1524  C   GLN A 205      23.431  49.712  64.560  1.00 18.06           C  
ATOM   1525  O   GLN A 205      22.677  50.551  65.060  1.00 17.20           O  
ATOM   1526  CB  GLN A 205      23.896  47.612  65.801  1.00 20.37           C  
ATOM   1527  CG  GLN A 205      23.602  48.374  67.098  1.00 24.60           C  
ATOM   1528  CD  GLN A 205      23.993  47.629  68.357  1.00 28.12           C  
ATOM   1529  OE1 GLN A 205      25.171  47.619  68.747  1.00 28.49           O  
ATOM   1530  NE2 GLN A 205      23.002  46.990  69.006  1.00 24.08           N  
ATOM   1531  N   GLU A 206      24.558  50.026  63.933  1.00 17.68           N  
ATOM   1532  CA  GLU A 206      25.022  51.398  63.774  1.00 19.87           C  
ATOM   1533  C   GLU A 206      24.026  52.254  62.973  1.00 18.82           C  
ATOM   1534  O   GLU A 206      23.714  53.382  63.356  1.00 17.25           O  
ATOM   1535  CB  GLU A 206      26.372  51.379  63.065  1.00 22.99           C  
ATOM   1536  CG  GLU A 206      27.224  52.605  63.274  1.00 30.71           C  
ATOM   1537  CD  GLU A 206      28.462  52.582  62.401  1.00 35.14           C  
ATOM   1538  OE1 GLU A 206      28.417  53.177  61.299  1.00 36.86           O  
ATOM   1539  OE2 GLU A 206      29.466  51.949  62.809  1.00 37.00           O  
ATOM   1540  N   LEU A 207      23.530  51.708  61.866  1.00 16.86           N  
ATOM   1541  CA  LEU A 207      22.580  52.426  61.028  1.00 16.85           C  
ATOM   1542  C   LEU A 207      21.321  52.703  61.818  1.00 14.76           C  
ATOM   1543  O   LEU A 207      20.806  53.818  61.810  1.00 15.97           O  
ATOM   1544  CB  LEU A 207      22.243  51.616  59.776  1.00 15.76           C  
ATOM   1545  CG  LEU A 207      23.351  51.476  58.737  1.00 17.01           C  
ATOM   1546  CD1 LEU A 207      22.948  50.422  57.700  1.00 14.75           C  
ATOM   1547  CD2 LEU A 207      23.613  52.824  58.070  1.00 14.67           C  
ATOM   1548  N   VAL A 208      20.828  51.692  62.517  1.00 13.24           N  
ATOM   1549  CA  VAL A 208      19.646  51.892  63.320  1.00 12.97           C  
ATOM   1550  C   VAL A 208      19.877  52.921  64.450  1.00 14.15           C  
ATOM   1551  O   VAL A 208      18.958  53.661  64.803  1.00 14.43           O  
ATOM   1552  CB  VAL A 208      19.146  50.581  63.921  1.00 11.91           C  
ATOM   1553  CG1 VAL A 208      18.003  50.879  64.864  1.00  8.02           C  
ATOM   1554  CG2 VAL A 208      18.675  49.639  62.798  1.00  9.48           C  
ATOM   1555  N   GLU A 209      21.081  52.964  65.021  1.00 14.39           N  
ATOM   1556  CA  GLU A 209      21.370  53.936  66.081  1.00 15.82           C  
ATOM   1557  C   GLU A 209      21.361  55.356  65.492  1.00 17.90           C  
ATOM   1558  O   GLU A 209      20.908  56.309  66.130  1.00 18.37           O  
ATOM   1559  CB  GLU A 209      22.740  53.675  66.716  1.00 11.80           C  
ATOM   1560  CG  GLU A 209      22.858  52.342  67.455  1.00 15.45           C  
ATOM   1561  CD  GLU A 209      24.269  52.060  67.923  1.00 12.83           C  
ATOM   1562  OE1 GLU A 209      25.212  52.505  67.259  1.00 16.51           O  
ATOM   1563  OE2 GLU A 209      24.445  51.384  68.946  1.00 18.11           O  
ATOM   1564  N   GLN A 210      21.848  55.487  64.266  1.00 17.29           N  
ATOM   1565  CA  GLN A 210      21.904  56.788  63.620  1.00 20.11           C  
ATOM   1566  C   GLN A 210      20.567  57.247  63.060  1.00 19.72           C  
ATOM   1567  O   GLN A 210      20.492  58.309  62.457  1.00 19.66           O  
ATOM   1568  CB  GLN A 210      22.966  56.779  62.514  1.00 20.87           C  
ATOM   1569  CG  GLN A 210      24.386  56.654  63.046  1.00 25.10           C  
ATOM   1570  CD  GLN A 210      25.413  56.409  61.949  1.00 28.74           C  
ATOM   1571  OE1 GLN A 210      25.092  56.429  60.756  1.00 30.41           O  
ATOM   1572  NE2 GLN A 210      26.660  56.179  62.349  1.00 30.10           N  
ATOM   1573  N   GLY A 211      19.516  56.448  63.250  1.00 20.73           N  
ATOM   1574  CA  GLY A 211      18.198  56.838  62.765  1.00 19.01           C  
ATOM   1575  C   GLY A 211      17.738  56.333  61.400  1.00 19.98           C  
ATOM   1576  O   GLY A 211      16.720  56.801  60.875  1.00 20.15           O  
ATOM   1577  N   TYR A 212      18.472  55.405  60.796  1.00 18.21           N  
ATOM   1578  CA  TYR A 212      18.044  54.877  59.507  1.00 17.97           C  
ATOM   1579  C   TYR A 212      16.965  53.860  59.803  1.00 18.34           C  
ATOM   1580  O   TYR A 212      17.077  53.102  60.772  1.00 18.75           O  
ATOM   1581  CB  TYR A 212      19.219  54.233  58.755  1.00 18.20           C  
ATOM   1582  CG  TYR A 212      20.241  55.263  58.336  1.00 18.67           C  
ATOM   1583  CD1 TYR A 212      21.376  55.499  59.098  1.00 19.55           C  
ATOM   1584  CD2 TYR A 212      20.014  56.080  57.236  1.00 21.11           C  
ATOM   1585  CE1 TYR A 212      22.269  56.532  58.772  1.00 20.44           C  
ATOM   1586  CE2 TYR A 212      20.896  57.122  56.902  1.00 22.83           C  
ATOM   1587  CZ  TYR A 212      22.015  57.338  57.675  1.00 22.10           C  
ATOM   1588  OH  TYR A 212      22.877  58.351  57.341  1.00 23.55           O  
ATOM   1589  N   ARG A 213      15.915  53.841  58.988  1.00 17.84           N  
ATOM   1590  CA  ARG A 213      14.813  52.917  59.219  1.00 18.83           C  
ATOM   1591  C   ARG A 213      14.533  51.970  58.056  1.00 19.61           C  
ATOM   1592  O   ARG A 213      13.986  50.875  58.253  1.00 19.01           O  
ATOM   1593  CB  ARG A 213      13.559  53.717  59.581  1.00 20.39           C  
ATOM   1594  CG  ARG A 213      13.705  54.495  60.907  1.00 22.90           C  
ATOM   1595  CD  ARG A 213      13.878  53.526  62.085  1.00 24.42           C  
ATOM   1596  NE  ARG A 213      14.163  54.183  63.365  1.00 24.16           N  
ATOM   1597  CZ  ARG A 213      15.379  54.356  63.892  1.00 25.56           C  
ATOM   1598  NH1 ARG A 213      16.479  53.924  63.266  1.00 22.24           N  
ATOM   1599  NH2 ARG A 213      15.493  54.964  65.069  1.00 25.32           N  
ATOM   1600  N   TYR A 214      14.923  52.376  56.851  1.00 18.21           N  
ATOM   1601  CA  TYR A 214      14.696  51.548  55.668  1.00 16.81           C  
ATOM   1602  C   TYR A 214      15.933  51.394  54.812  1.00 15.90           C  
ATOM   1603  O   TYR A 214      16.825  52.244  54.800  1.00 16.62           O  
ATOM   1604  CB  TYR A 214      13.609  52.153  54.773  1.00 16.63           C  
ATOM   1605  CG  TYR A 214      12.194  52.088  55.309  1.00 18.06           C  
ATOM   1606  CD1 TYR A 214      11.624  53.177  55.971  1.00 19.05           C  
ATOM   1607  CD2 TYR A 214      11.405  50.961  55.103  1.00 18.15           C  
ATOM   1608  CE1 TYR A 214      10.299  53.149  56.407  1.00 17.32           C  
ATOM   1609  CE2 TYR A 214      10.085  50.922  55.537  1.00 19.60           C  
ATOM   1610  CZ  TYR A 214       9.537  52.024  56.188  1.00 19.80           C  
ATOM   1611  OH  TYR A 214       8.228  51.983  56.631  1.00 21.06           O  
HETATM 1612  N   MSE A 215      15.982  50.299  54.079  1.00 14.99           N  
HETATM 1613  CA  MSE A 215      17.079  50.081  53.170  1.00 13.12           C  
HETATM 1614  C   MSE A 215      16.514  49.580  51.846  1.00 12.58           C  
HETATM 1615  O   MSE A 215      15.681  48.677  51.809  1.00 13.17           O  
HETATM 1616  CB  MSE A 215      18.076  49.065  53.724  1.00 12.60           C  
HETATM 1617  CG  MSE A 215      19.224  48.791  52.748  1.00 13.81           C  
HETATM 1618 SE   MSE A 215      20.522  47.495  53.414  1.00 19.77          SE  
HETATM 1619  CE  MSE A 215      21.607  48.692  54.515  1.00 15.83           C  
ATOM   1620  N   PHE A 216      16.957  50.187  50.758  1.00 12.54           N  
ATOM   1621  CA  PHE A 216      16.517  49.771  49.443  1.00 12.58           C  
ATOM   1622  C   PHE A 216      17.703  49.100  48.789  1.00 13.31           C  
ATOM   1623  O   PHE A 216      18.702  49.760  48.506  1.00 12.46           O  
ATOM   1624  CB  PHE A 216      16.107  50.960  48.592  1.00 11.19           C  
ATOM   1625  CG  PHE A 216      15.792  50.585  47.180  1.00 12.71           C  
ATOM   1626  CD1 PHE A 216      14.772  49.670  46.911  1.00 13.68           C  
ATOM   1627  CD2 PHE A 216      16.528  51.105  46.121  1.00 12.29           C  
ATOM   1628  CE1 PHE A 216      14.489  49.273  45.601  1.00 12.73           C  
ATOM   1629  CE2 PHE A 216      16.256  50.715  44.806  1.00 12.35           C  
ATOM   1630  CZ  PHE A 216      15.234  49.796  44.549  1.00 11.27           C  
ATOM   1631  N   VAL A 217      17.596  47.793  48.553  1.00 13.94           N  
ATOM   1632  CA  VAL A 217      18.679  47.042  47.936  1.00 13.30           C  
ATOM   1633  C   VAL A 217      18.291  46.572  46.541  1.00 14.28           C  
ATOM   1634  O   VAL A 217      17.129  46.266  46.288  1.00 15.27           O  
ATOM   1635  CB  VAL A 217      19.037  45.788  48.776  1.00 14.96           C  
ATOM   1636  CG1 VAL A 217      20.232  45.069  48.158  1.00 13.55           C  
ATOM   1637  CG2 VAL A 217      19.321  46.188  50.202  1.00 13.67           C  
ATOM   1638  N   SER A 218      19.265  46.501  45.639  1.00 13.99           N  
ATOM   1639  CA  SER A 218      19.010  46.019  44.271  1.00 15.63           C  
ATOM   1640  C   SER A 218      20.330  45.499  43.686  1.00 14.59           C  
ATOM   1641  O   SER A 218      21.405  45.841  44.176  1.00 15.55           O  
ATOM   1642  CB  SER A 218      18.423  47.139  43.384  1.00 13.27           C  
ATOM   1643  OG  SER A 218      19.353  48.183  43.155  1.00 15.09           O  
ATOM   1644  N   ASN A 219      20.251  44.665  42.657  1.00 15.16           N  
ATOM   1645  CA  ASN A 219      21.455  44.103  42.043  1.00 13.83           C  
ATOM   1646  C   ASN A 219      22.310  45.150  41.381  1.00 14.65           C  
ATOM   1647  O   ASN A 219      21.797  46.142  40.859  1.00 16.36           O  
ATOM   1648  CB  ASN A 219      21.104  43.078  40.983  1.00 13.87           C  
ATOM   1649  CG  ASN A 219      20.299  41.946  41.523  1.00 13.73           C  
ATOM   1650  OD1 ASN A 219      20.465  41.536  42.682  1.00 12.86           O  
ATOM   1651  ND2 ASN A 219      19.424  41.410  40.686  1.00 10.39           N  
ATOM   1652  N   GLY A 220      23.616  44.911  41.380  1.00 14.83           N  
ATOM   1653  CA  GLY A 220      24.530  45.843  40.745  1.00 14.69           C  
ATOM   1654  C   GLY A 220      24.336  45.924  39.230  1.00 14.48           C  
ATOM   1655  O   GLY A 220      24.702  46.929  38.629  1.00 13.17           O  
ATOM   1656  N   ASP A 221      23.749  44.889  38.618  1.00 13.62           N  
ATOM   1657  CA  ASP A 221      23.540  44.873  37.159  1.00 15.34           C  
ATOM   1658  C   ASP A 221      22.251  45.547  36.695  1.00 15.37           C  
ATOM   1659  O   ASP A 221      22.098  45.879  35.520  1.00 17.40           O  
ATOM   1660  CB  ASP A 221      23.557  43.436  36.640  1.00 14.75           C  
ATOM   1661  CG  ASP A 221      22.468  42.580  37.262  1.00 16.36           C  
ATOM   1662  OD1 ASP A 221      21.314  42.615  36.783  1.00 16.66           O  
ATOM   1663  OD2 ASP A 221      22.767  41.881  38.245  1.00 14.88           O  
ATOM   1664  N   ASN A 222      21.330  45.761  37.624  1.00 15.03           N  
ATOM   1665  CA  ASN A 222      20.052  46.369  37.304  1.00 14.22           C  
ATOM   1666  C   ASN A 222      20.047  47.885  37.521  1.00 13.41           C  
ATOM   1667  O   ASN A 222      19.941  48.364  38.650  1.00 15.19           O  
ATOM   1668  CB  ASN A 222      18.956  45.697  38.142  1.00 14.84           C  
ATOM   1669  CG  ASN A 222      17.590  46.224  37.817  1.00 14.07           C  
ATOM   1670  OD1 ASN A 222      17.350  46.669  36.693  1.00 18.16           O  
ATOM   1671  ND2 ASN A 222      16.679  46.168  38.781  1.00 11.33           N  
ATOM   1672  N   LEU A 223      20.141  48.639  36.432  1.00 11.81           N  
ATOM   1673  CA  LEU A 223      20.173  50.096  36.516  1.00 11.98           C  
ATOM   1674  C   LEU A 223      18.807  50.775  36.371  1.00 12.45           C  
ATOM   1675  O   LEU A 223      18.726  51.990  36.233  1.00 11.20           O  
ATOM   1676  CB  LEU A 223      21.146  50.645  35.473  1.00 13.24           C  
ATOM   1677  CG  LEU A 223      22.615  50.231  35.613  1.00 12.01           C  
ATOM   1678  CD1 LEU A 223      23.339  50.452  34.295  1.00 14.05           C  
ATOM   1679  CD2 LEU A 223      23.268  51.030  36.743  1.00 12.10           C  
ATOM   1680  N   GLY A 224      17.738  49.987  36.398  1.00 12.95           N  
ATOM   1681  CA  GLY A 224      16.408  50.554  36.309  1.00 13.66           C  
ATOM   1682  C   GLY A 224      15.846  50.776  37.698  1.00 15.90           C  
ATOM   1683  O   GLY A 224      14.774  51.358  37.873  1.00 17.08           O  
ATOM   1684  N   ALA A 225      16.592  50.331  38.702  1.00 16.90           N  
ATOM   1685  CA  ALA A 225      16.145  50.438  40.079  1.00 17.06           C  
ATOM   1686  C   ALA A 225      16.716  51.549  40.958  1.00 17.88           C  
ATOM   1687  O   ALA A 225      17.916  51.580  41.233  1.00 17.68           O  
ATOM   1688  CB  ALA A 225      16.356  49.097  40.776  1.00 17.40           C  
ATOM   1689  N   THR A 226      15.833  52.449  41.385  1.00 17.70           N  
ATOM   1690  CA  THR A 226      16.165  53.516  42.317  1.00 21.08           C  
ATOM   1691  C   THR A 226      14.972  53.634  43.265  1.00 21.07           C  
ATOM   1692  O   THR A 226      13.932  52.992  43.080  1.00 21.84           O  
ATOM   1693  CB  THR A 226      16.394  54.906  41.656  1.00 22.65           C  
ATOM   1694  OG1 THR A 226      15.196  55.333  40.998  1.00 26.86           O  
ATOM   1695  CG2 THR A 226      17.550  54.857  40.685  1.00 22.07           C  
ATOM   1696  N   ILE A 227      15.130  54.463  44.280  1.00 21.45           N  
ATOM   1697  CA  ILE A 227      14.097  54.678  45.272  1.00 21.49           C  
ATOM   1698  C   ILE A 227      12.831  55.327  44.751  1.00 21.73           C  
ATOM   1699  O   ILE A 227      12.873  56.312  44.033  1.00 20.67           O  
ATOM   1700  CB  ILE A 227      14.621  55.559  46.415  1.00 21.45           C  
ATOM   1701  CG1 ILE A 227      15.527  54.741  47.332  1.00 22.46           C  
ATOM   1702  CG2 ILE A 227      13.459  56.122  47.217  1.00 22.28           C  
ATOM   1703  CD1 ILE A 227      16.116  55.567  48.458  1.00 23.52           C  
ATOM   1704  N   ASP A 228      11.694  54.770  45.129  1.00 23.06           N  
ATOM   1705  CA  ASP A 228      10.435  55.362  44.743  1.00 23.05           C  
ATOM   1706  C   ASP A 228       9.727  55.680  46.057  1.00 22.89           C  
ATOM   1707  O   ASP A 228       9.369  54.774  46.816  1.00 22.65           O  
ATOM   1708  CB  ASP A 228       9.615  54.402  43.878  1.00 24.90           C  
ATOM   1709  CG  ASP A 228       8.340  55.053  43.335  1.00 25.53           C  
ATOM   1710  OD1 ASP A 228       7.925  54.722  42.199  1.00 25.28           O  
ATOM   1711  OD2 ASP A 228       7.749  55.891  44.058  1.00 27.43           O  
ATOM   1712  N   LYS A 229       9.548  56.972  46.320  1.00 21.38           N  
ATOM   1713  CA  LYS A 229       8.925  57.440  47.552  1.00 21.97           C  
ATOM   1714  C   LYS A 229       7.518  56.906  47.787  1.00 19.64           C  
ATOM   1715  O   LYS A 229       7.017  56.952  48.904  1.00 21.45           O  
ATOM   1716  CB  LYS A 229       8.923  58.973  47.592  1.00 22.54           C  
ATOM   1717  CG  LYS A 229      10.314  59.597  47.397  1.00 28.28           C  
ATOM   1718  CD  LYS A 229      10.275  61.116  47.601  1.00 31.72           C  
ATOM   1719  CE  LYS A 229      11.150  61.861  46.595  1.00 34.67           C  
ATOM   1720  NZ  LYS A 229      10.676  61.695  45.178  1.00 37.52           N  
ATOM   1721  N   ARG A 230       6.876  56.393  46.748  1.00 18.28           N  
ATOM   1722  CA  ARG A 230       5.536  55.843  46.927  1.00 18.96           C  
ATOM   1723  C   ARG A 230       5.619  54.509  47.661  1.00 17.29           C  
ATOM   1724  O   ARG A 230       4.738  54.189  48.453  1.00 20.06           O  
ATOM   1725  CB  ARG A 230       4.831  55.650  45.577  1.00 16.74           C  
ATOM   1726  CG  ARG A 230       4.536  56.954  44.861  1.00 19.71           C  
ATOM   1727  CD  ARG A 230       3.943  56.680  43.484  1.00 23.02           C  
ATOM   1728  NE  ARG A 230       4.907  56.039  42.590  1.00 20.44           N  
ATOM   1729  CZ  ARG A 230       4.586  55.433  41.453  1.00 22.36           C  
ATOM   1730  NH1 ARG A 230       3.319  55.379  41.067  1.00 20.50           N  
ATOM   1731  NH2 ARG A 230       5.535  54.883  40.695  1.00 22.54           N  
ATOM   1732  N   VAL A 231       6.670  53.733  47.389  1.00 15.95           N  
ATOM   1733  CA  VAL A 231       6.873  52.437  48.047  1.00 15.54           C  
ATOM   1734  C   VAL A 231       7.016  52.623  49.554  1.00 15.36           C  
ATOM   1735  O   VAL A 231       6.459  51.857  50.348  1.00 15.77           O  
ATOM   1736  CB  VAL A 231       8.154  51.734  47.535  1.00 15.27           C  
ATOM   1737  CG1 VAL A 231       8.368  50.443  48.298  1.00 16.21           C  
ATOM   1738  CG2 VAL A 231       8.045  51.464  46.046  1.00 13.49           C  
ATOM   1739  N   LEU A 232       7.775  53.648  49.936  1.00 14.42           N  
ATOM   1740  CA  LEU A 232       7.999  53.969  51.339  1.00 16.89           C  
ATOM   1741  C   LEU A 232       6.706  54.355  52.059  1.00 18.73           C  
ATOM   1742  O   LEU A 232       6.468  53.914  53.187  1.00 18.75           O  
ATOM   1743  CB  LEU A 232       9.022  55.102  51.446  1.00 16.58           C  
ATOM   1744  CG  LEU A 232      10.455  54.690  51.074  1.00 15.56           C  
ATOM   1745  CD1 LEU A 232      11.304  55.924  50.854  1.00 14.72           C  
ATOM   1746  CD2 LEU A 232      11.049  53.810  52.184  1.00 12.35           C  
ATOM   1747  N   ALA A 233       5.876  55.177  51.411  1.00 20.22           N  
ATOM   1748  CA  ALA A 233       4.601  55.606  51.998  1.00 20.02           C  
ATOM   1749  C   ALA A 233       3.689  54.405  52.182  1.00 19.83           C  
ATOM   1750  O   ALA A 233       3.008  54.274  53.199  1.00 20.15           O  
ATOM   1751  CB  ALA A 233       3.920  56.632  51.094  1.00 21.67           C  
ATOM   1752  N   TYR A 234       3.676  53.538  51.173  1.00 20.49           N  
ATOM   1753  CA  TYR A 234       2.875  52.312  51.184  1.00 20.31           C  
ATOM   1754  C   TYR A 234       3.365  51.436  52.339  1.00 20.13           C  
ATOM   1755  O   TYR A 234       2.571  50.928  53.129  1.00 20.05           O  
ATOM   1756  CB  TYR A 234       3.038  51.587  49.836  1.00 20.16           C  
ATOM   1757  CG  TYR A 234       2.384  50.224  49.700  1.00 20.84           C  
ATOM   1758  CD1 TYR A 234       1.002  50.096  49.517  1.00 22.07           C  
ATOM   1759  CD2 TYR A 234       3.160  49.054  49.692  1.00 21.68           C  
ATOM   1760  CE1 TYR A 234       0.411  48.842  49.321  1.00 19.31           C  
ATOM   1761  CE2 TYR A 234       2.574  47.791  49.496  1.00 20.47           C  
ATOM   1762  CZ  TYR A 234       1.201  47.696  49.310  1.00 21.60           C  
ATOM   1763  OH  TYR A 234       0.618  46.462  49.107  1.00 21.45           O  
HETATM 1764  N   MSE A 235       4.676  51.274  52.456  1.00 21.25           N  
HETATM 1765  CA  MSE A 235       5.209  50.457  53.536  1.00 23.82           C  
HETATM 1766  C   MSE A 235       4.870  51.020  54.911  1.00 24.87           C  
HETATM 1767  O   MSE A 235       4.519  50.277  55.837  1.00 22.90           O  
HETATM 1768  CB  MSE A 235       6.720  50.300  53.376  1.00 23.23           C  
HETATM 1769  CG  MSE A 235       7.087  49.295  52.305  1.00 23.36           C  
HETATM 1770 SE   MSE A 235       8.956  49.115  52.074  1.00 23.39          SE  
HETATM 1771  CE  MSE A 235       9.339  47.844  53.479  1.00 20.54           C  
ATOM   1772  N   GLU A 236       4.992  52.334  55.044  1.00 25.45           N  
ATOM   1773  CA  GLU A 236       4.677  53.019  56.307  1.00 28.91           C  
ATOM   1774  C   GLU A 236       3.234  52.767  56.726  1.00 28.97           C  
ATOM   1775  O   GLU A 236       2.941  52.459  57.875  1.00 29.51           O  
ATOM   1776  CB  GLU A 236       4.857  54.532  56.131  1.00 29.87           C  
ATOM   1777  CG  GLU A 236       6.287  55.010  56.195  1.00 32.47           C  
ATOM   1778  CD  GLU A 236       6.813  54.953  57.608  1.00 35.71           C  
ATOM   1779  OE1 GLU A 236       6.927  53.834  58.160  1.00 35.06           O  
ATOM   1780  OE2 GLU A 236       7.101  56.035  58.161  1.00 37.44           O  
ATOM   1781  N   LYS A 237       2.343  52.925  55.765  1.00 28.84           N  
ATOM   1782  CA  LYS A 237       0.925  52.761  55.977  1.00 30.71           C  
ATOM   1783  C   LYS A 237       0.453  51.339  56.179  1.00 30.02           C  
ATOM   1784  O   LYS A 237      -0.294  51.059  57.107  1.00 31.86           O  
ATOM   1785  CB  LYS A 237       0.209  53.346  54.787  1.00 33.24           C  
ATOM   1786  CG  LYS A 237      -1.187  52.842  54.594  1.00 36.97           C  
ATOM   1787  CD  LYS A 237      -1.672  53.317  53.253  1.00 38.23           C  
ATOM   1788  CE  LYS A 237      -3.106  52.952  53.003  1.00 40.73           C  
ATOM   1789  NZ  LYS A 237      -3.484  53.558  51.703  1.00 44.60           N  
ATOM   1790  N   GLU A 238       0.855  50.455  55.280  1.00 29.64           N  
ATOM   1791  CA  GLU A 238       0.462  49.058  55.360  1.00 30.40           C  
ATOM   1792  C   GLU A 238       1.287  48.359  56.412  1.00 30.14           C  
ATOM   1793  O   GLU A 238       1.102  47.171  56.663  1.00 30.66           O  
ATOM   1794  CB  GLU A 238       0.647  48.369  54.006  1.00 29.20           C  
ATOM   1795  CG  GLU A 238      -0.279  48.913  52.931  1.00 33.17           C  
ATOM   1796  CD  GLU A 238      -1.744  48.866  53.352  1.00 36.91           C  
ATOM   1797  OE1 GLU A 238      -2.271  47.753  53.586  1.00 38.63           O  
ATOM   1798  OE2 GLU A 238      -2.367  49.947  53.460  1.00 39.51           O  
ATOM   1799  N   LYS A 239       2.202  49.104  57.030  1.00 29.84           N  
ATOM   1800  CA  LYS A 239       3.061  48.545  58.073  1.00 30.62           C  
ATOM   1801  C   LYS A 239       3.760  47.260  57.606  1.00 27.71           C  
ATOM   1802  O   LYS A 239       3.684  46.219  58.266  1.00 25.91           O  
ATOM   1803  CB  LYS A 239       2.227  48.259  59.331  1.00 33.69           C  
ATOM   1804  CG  LYS A 239       1.742  49.516  60.045  1.00 38.07           C  
ATOM   1805  CD  LYS A 239       0.673  49.190  61.079  1.00 42.47           C  
ATOM   1806  CE  LYS A 239       0.299  50.426  61.884  1.00 44.87           C  
ATOM   1807  NZ  LYS A 239       0.095  51.617  61.005  1.00 47.20           N  
ATOM   1808  N   ILE A 240       4.439  47.344  56.466  1.00 24.64           N  
ATOM   1809  CA  ILE A 240       5.141  46.198  55.921  1.00 20.67           C  
ATOM   1810  C   ILE A 240       6.602  46.314  56.289  1.00 19.96           C  
ATOM   1811  O   ILE A 240       7.201  47.377  56.171  1.00 20.68           O  
ATOM   1812  CB  ILE A 240       4.952  46.131  54.397  1.00 20.43           C  
ATOM   1813  CG1 ILE A 240       3.466  45.925  54.088  1.00 19.03           C  
ATOM   1814  CG2 ILE A 240       5.762  44.968  53.795  1.00 20.08           C  
ATOM   1815  CD1 ILE A 240       3.138  46.000  52.594  1.00 19.78           C  
ATOM   1816  N   ASP A 241       7.181  45.222  56.761  1.00 19.09           N  
ATOM   1817  CA  ASP A 241       8.577  45.253  57.161  1.00 18.53           C  
ATOM   1818  C   ASP A 241       9.549  44.809  56.066  1.00 17.38           C  
ATOM   1819  O   ASP A 241      10.744  45.102  56.123  1.00 17.37           O  
ATOM   1820  CB  ASP A 241       8.763  44.411  58.423  1.00 18.93           C  
ATOM   1821  CG  ASP A 241       7.901  44.899  59.579  1.00 22.45           C  
ATOM   1822  OD1 ASP A 241       7.851  46.127  59.830  1.00 26.05           O  
ATOM   1823  OD2 ASP A 241       7.280  44.058  60.248  1.00 23.04           O  
ATOM   1824  N   PHE A 242       9.034  44.119  55.058  1.00 15.89           N  
ATOM   1825  CA  PHE A 242       9.870  43.642  53.969  1.00 15.52           C  
ATOM   1826  C   PHE A 242       9.034  43.651  52.709  1.00 16.13           C  
ATOM   1827  O   PHE A 242       7.910  43.145  52.698  1.00 18.47           O  
ATOM   1828  CB  PHE A 242      10.341  42.216  54.269  1.00 17.09           C  
ATOM   1829  CG  PHE A 242      11.163  41.608  53.176  1.00 16.45           C  
ATOM   1830  CD1 PHE A 242      12.547  41.622  53.241  1.00 18.11           C  
ATOM   1831  CD2 PHE A 242      10.554  41.014  52.090  1.00 13.51           C  
ATOM   1832  CE1 PHE A 242      13.311  41.049  52.240  1.00 15.55           C  
ATOM   1833  CE2 PHE A 242      11.310  40.441  51.087  1.00 15.03           C  
ATOM   1834  CZ  PHE A 242      12.688  40.459  51.163  1.00 14.25           C  
ATOM   1835  N   LEU A 243       9.578  44.213  51.638  1.00 15.76           N  
ATOM   1836  CA  LEU A 243       8.829  44.270  50.396  1.00 14.16           C  
ATOM   1837  C   LEU A 243       9.663  43.897  49.188  1.00 14.58           C  
ATOM   1838  O   LEU A 243      10.697  44.525  48.909  1.00 15.05           O  
ATOM   1839  CB  LEU A 243       8.249  45.675  50.178  1.00 14.53           C  
ATOM   1840  CG  LEU A 243       7.211  45.757  49.053  1.00 14.08           C  
ATOM   1841  CD1 LEU A 243       6.006  44.897  49.431  1.00 13.24           C  
ATOM   1842  CD2 LEU A 243       6.759  47.194  48.852  1.00 14.85           C  
HETATM 1843  N   MSE A 244       9.198  42.886  48.460  1.00 13.27           N  
HETATM 1844  CA  MSE A 244       9.876  42.448  47.256  1.00 14.17           C  
HETATM 1845  C   MSE A 244       9.197  43.002  46.017  1.00 13.37           C  
HETATM 1846  O   MSE A 244       7.980  42.880  45.856  1.00 12.65           O  
HETATM 1847  CB  MSE A 244       9.877  40.916  47.147  1.00 15.82           C  
HETATM 1848  CG  MSE A 244      10.384  40.395  45.793  1.00 16.91           C  
HETATM 1849 SE   MSE A 244      10.184  38.452  45.619  1.00 21.46          SE  
HETATM 1850  CE  MSE A 244      11.491  37.971  46.953  1.00 16.53           C  
ATOM   1851  N   GLU A 245       9.979  43.608  45.135  1.00 13.56           N  
ATOM   1852  CA  GLU A 245       9.414  44.101  43.888  1.00 13.65           C  
ATOM   1853  C   GLU A 245       9.488  42.958  42.864  1.00 15.12           C  
ATOM   1854  O   GLU A 245      10.568  42.426  42.597  1.00 15.53           O  
ATOM   1855  CB  GLU A 245      10.211  45.301  43.381  1.00 12.31           C  
ATOM   1856  CG  GLU A 245      10.035  46.551  44.221  1.00 12.26           C  
ATOM   1857  CD  GLU A 245      10.778  47.742  43.648  1.00 12.05           C  
ATOM   1858  OE1 GLU A 245      10.980  47.775  42.417  1.00 10.50           O  
ATOM   1859  OE2 GLU A 245      11.143  48.651  44.424  1.00 13.09           O  
ATOM   1860  N   VAL A 246       8.340  42.574  42.312  1.00 16.04           N  
ATOM   1861  CA  VAL A 246       8.284  41.523  41.301  1.00 15.72           C  
ATOM   1862  C   VAL A 246       7.741  42.083  39.983  1.00 16.15           C  
ATOM   1863  O   VAL A 246       6.945  43.030  39.976  1.00 14.34           O  
ATOM   1864  CB  VAL A 246       7.381  40.350  41.753  1.00 15.92           C  
ATOM   1865  CG1 VAL A 246       7.934  39.714  43.032  1.00 14.43           C  
ATOM   1866  CG2 VAL A 246       5.971  40.849  41.970  1.00 14.30           C  
ATOM   1867  N   CYS A 247       8.179  41.505  38.870  1.00 15.48           N  
ATOM   1868  CA  CYS A 247       7.723  41.928  37.547  1.00 18.30           C  
ATOM   1869  C   CYS A 247       6.952  40.790  36.877  1.00 19.51           C  
ATOM   1870  O   CYS A 247       7.193  39.628  37.188  1.00 19.53           O  
ATOM   1871  CB  CYS A 247       8.917  42.276  36.660  1.00 17.45           C  
ATOM   1872  SG  CYS A 247       9.513  43.979  36.747  1.00 25.40           S  
ATOM   1873  N   ARG A 248       6.031  41.127  35.976  1.00 20.44           N  
ATOM   1874  CA  ARG A 248       5.274  40.126  35.224  1.00 23.29           C  
ATOM   1875  C   ARG A 248       6.352  39.407  34.424  1.00 23.29           C  
ATOM   1876  O   ARG A 248       7.091  40.048  33.674  1.00 23.37           O  
ATOM   1877  CB  ARG A 248       4.315  40.786  34.228  1.00 27.84           C  
ATOM   1878  CG  ARG A 248       2.845  40.482  34.443  1.00 34.76           C  
ATOM   1879  CD  ARG A 248       2.603  39.031  34.816  1.00 37.26           C  
ATOM   1880  NE  ARG A 248       1.315  38.863  35.496  1.00 40.85           N  
ATOM   1881  CZ  ARG A 248       0.737  39.793  36.260  1.00 42.57           C  
ATOM   1882  NH1 ARG A 248       1.312  40.975  36.449  1.00 45.09           N  
ATOM   1883  NH2 ARG A 248      -0.412  39.544  36.859  1.00 41.36           N  
ATOM   1884  N   ARG A 249       6.444  38.090  34.563  1.00 21.96           N  
ATOM   1885  CA  ARG A 249       7.490  37.337  33.882  1.00 23.31           C  
ATOM   1886  C   ARG A 249       7.396  37.330  32.369  1.00 24.84           C  
ATOM   1887  O   ARG A 249       6.328  37.097  31.800  1.00 27.85           O  
ATOM   1888  CB  ARG A 249       7.499  35.910  34.403  1.00 22.17           C  
ATOM   1889  CG  ARG A 249       8.778  35.173  34.142  1.00 20.97           C  
ATOM   1890  CD  ARG A 249       8.721  33.834  34.850  1.00 21.14           C  
ATOM   1891  NE  ARG A 249       9.947  33.053  34.695  1.00 21.72           N  
ATOM   1892  CZ  ARG A 249      10.170  31.906  35.330  1.00 21.53           C  
ATOM   1893  NH1 ARG A 249       9.254  31.419  36.155  1.00 17.67           N  
ATOM   1894  NH2 ARG A 249      11.303  31.243  35.144  1.00 21.56           N  
ATOM   1895  N   THR A 250       8.525  37.591  31.721  1.00 24.34           N  
ATOM   1896  CA  THR A 250       8.600  37.584  30.269  1.00 26.08           C  
ATOM   1897  C   THR A 250       9.431  36.386  29.829  1.00 27.51           C  
ATOM   1898  O   THR A 250       9.953  35.638  30.666  1.00 28.55           O  
ATOM   1899  CB  THR A 250       9.282  38.838  29.722  1.00 27.58           C  
ATOM   1900  OG1 THR A 250      10.634  38.880  30.202  1.00 27.90           O  
ATOM   1901  CG2 THR A 250       8.508  40.103  30.138  1.00 26.19           C  
ATOM   1902  N   GLU A 251       9.555  36.215  28.516  1.00 28.21           N  
ATOM   1903  CA  GLU A 251      10.312  35.108  27.934  1.00 30.28           C  
ATOM   1904  C   GLU A 251      11.800  35.182  28.310  1.00 29.83           C  
ATOM   1905  O   GLU A 251      12.458  34.146  28.453  1.00 29.89           O  
ATOM   1906  CB  GLU A 251      10.169  35.127  26.400  1.00 32.13           C  
ATOM   1907  CG  GLU A 251      10.419  33.774  25.724  1.00 34.39           C  
ATOM   1908  CD  GLU A 251      10.442  33.863  24.192  1.00 37.28           C  
ATOM   1909  OE1 GLU A 251       9.604  34.610  23.632  1.00 35.24           O  
ATOM   1910  OE2 GLU A 251      11.287  33.178  23.552  1.00 35.78           O  
ATOM   1911  N   SER A 252      12.309  36.410  28.467  1.00 30.01           N  
ATOM   1912  CA  SER A 252      13.710  36.679  28.817  1.00 28.70           C  
ATOM   1913  C   SER A 252      14.082  36.379  30.274  1.00 28.36           C  
ATOM   1914  O   SER A 252      15.264  36.385  30.627  1.00 30.13           O  
ATOM   1915  CB  SER A 252      14.038  38.142  28.548  1.00 29.03           C  
ATOM   1916  OG  SER A 252      13.581  38.553  27.275  1.00 31.54           O  
ATOM   1917  N   ASP A 253      13.092  36.137  31.129  1.00 26.65           N  
ATOM   1918  CA  ASP A 253      13.382  35.850  32.537  1.00 26.39           C  
ATOM   1919  C   ASP A 253      13.553  34.351  32.768  1.00 26.55           C  
ATOM   1920  O   ASP A 253      12.602  33.646  33.095  1.00 25.56           O  
ATOM   1921  CB  ASP A 253      12.277  36.395  33.440  1.00 23.03           C  
ATOM   1922  CG  ASP A 253      11.979  37.845  33.168  1.00 21.02           C  
ATOM   1923  OD1 ASP A 253      12.940  38.626  32.987  1.00 20.60           O  
ATOM   1924  OD2 ASP A 253      10.786  38.208  33.134  1.00 19.58           O  
ATOM   1925  N   LYS A 254      14.792  33.896  32.608  1.00 28.59           N  
ATOM   1926  CA  LYS A 254      15.157  32.497  32.754  1.00 29.57           C  
ATOM   1927  C   LYS A 254      16.153  32.263  33.882  1.00 28.01           C  
ATOM   1928  O   LYS A 254      16.202  31.175  34.450  1.00 27.09           O  
ATOM   1929  CB  LYS A 254      15.749  32.005  31.436  1.00 33.31           C  
ATOM   1930  CG  LYS A 254      14.883  32.354  30.239  1.00 37.72           C  
ATOM   1931  CD  LYS A 254      15.338  31.635  28.981  1.00 42.57           C  
ATOM   1932  CE  LYS A 254      14.244  31.656  27.920  1.00 43.96           C  
ATOM   1933  NZ  LYS A 254      14.577  30.761  26.776  1.00 46.24           N  
ATOM   1934  N   LYS A 255      16.961  33.276  34.188  1.00 27.23           N  
ATOM   1935  CA  LYS A 255      17.951  33.178  35.260  1.00 26.58           C  
ATOM   1936  C   LYS A 255      17.578  34.135  36.384  1.00 24.30           C  
ATOM   1937  O   LYS A 255      17.670  35.348  36.235  1.00 24.43           O  
ATOM   1938  CB  LYS A 255      19.357  33.521  34.758  1.00 29.12           C  
ATOM   1939  CG  LYS A 255      20.103  32.385  34.072  1.00 34.04           C  
ATOM   1940  CD  LYS A 255      21.612  32.695  34.059  1.00 36.49           C  
ATOM   1941  CE  LYS A 255      22.429  31.562  33.446  1.00 38.12           C  
ATOM   1942  NZ  LYS A 255      22.193  31.429  31.972  1.00 39.99           N  
ATOM   1943  N   GLY A 256      17.169  33.570  37.512  1.00 21.86           N  
ATOM   1944  CA  GLY A 256      16.751  34.363  38.649  1.00 19.70           C  
ATOM   1945  C   GLY A 256      15.793  33.520  39.473  1.00 20.14           C  
ATOM   1946  O   GLY A 256      15.933  32.288  39.527  1.00 21.54           O  
ATOM   1947  N   GLY A 257      14.825  34.163  40.118  1.00 18.22           N  
ATOM   1948  CA  GLY A 257      13.868  33.426  40.928  1.00 15.29           C  
ATOM   1949  C   GLY A 257      12.457  33.951  40.761  1.00 16.44           C  
ATOM   1950  O   GLY A 257      12.243  35.073  40.289  1.00 14.46           O  
ATOM   1951  N   HIS A 258      11.478  33.144  41.141  1.00 15.44           N  
ATOM   1952  CA  HIS A 258      10.104  33.583  41.026  1.00 14.57           C  
ATOM   1953  C   HIS A 258       9.435  33.511  42.379  1.00 14.95           C  
ATOM   1954  O   HIS A 258       9.893  32.803  43.280  1.00 14.72           O  
ATOM   1955  CB  HIS A 258       9.347  32.718  40.009  1.00 14.55           C  
ATOM   1956  CG  HIS A 258       9.118  31.305  40.460  1.00 15.77           C  
ATOM   1957  ND1 HIS A 258       8.130  30.961  41.357  1.00 13.25           N  
ATOM   1958  CD2 HIS A 258       9.744  30.151  40.127  1.00 13.77           C  
ATOM   1959  CE1 HIS A 258       8.154  29.654  41.555  1.00 14.47           C  
ATOM   1960  NE2 HIS A 258       9.124  29.140  40.821  1.00 16.00           N  
ATOM   1961  N   LEU A 259       8.342  34.251  42.509  1.00 14.40           N  
ATOM   1962  CA  LEU A 259       7.569  34.294  43.743  1.00 13.89           C  
ATOM   1963  C   LEU A 259       6.653  33.075  43.807  1.00 14.93           C  
ATOM   1964  O   LEU A 259       6.374  32.443  42.787  1.00 14.57           O  
ATOM   1965  CB  LEU A 259       6.715  35.571  43.760  1.00 13.41           C  
ATOM   1966  CG  LEU A 259       5.950  35.911  45.039  1.00 15.12           C  
ATOM   1967  CD1 LEU A 259       6.946  36.141  46.177  1.00 14.15           C  
ATOM   1968  CD2 LEU A 259       5.095  37.158  44.823  1.00 13.66           C  
ATOM   1969  N   ALA A 260       6.183  32.750  45.005  1.00 14.80           N  
ATOM   1970  CA  ALA A 260       5.275  31.631  45.190  1.00 15.98           C  
ATOM   1971  C   ALA A 260       4.688  31.744  46.580  1.00 16.79           C  
ATOM   1972  O   ALA A 260       5.155  32.544  47.398  1.00 16.35           O  
ATOM   1973  CB  ALA A 260       6.010  30.301  45.043  1.00 16.28           C  
ATOM   1974  N   ARG A 261       3.689  30.921  46.855  1.00 16.99           N  
ATOM   1975  CA  ARG A 261       3.046  30.936  48.159  1.00 21.88           C  
ATOM   1976  C   ARG A 261       2.804  29.530  48.695  1.00 23.05           C  
ATOM   1977  O   ARG A 261       2.866  28.545  47.962  1.00 22.01           O  
ATOM   1978  CB  ARG A 261       1.690  31.647  48.062  1.00 21.14           C  
ATOM   1979  CG  ARG A 261       0.688  30.948  47.116  1.00 24.53           C  
ATOM   1980  CD  ARG A 261      -0.741  31.521  47.243  1.00 23.87           C  
ATOM   1981  NE  ARG A 261      -1.338  31.153  48.522  1.00 26.39           N  
ATOM   1982  CZ  ARG A 261      -2.373  31.775  49.079  1.00 28.48           C  
ATOM   1983  NH1 ARG A 261      -2.935  32.811  48.467  1.00 26.72           N  
ATOM   1984  NH2 ARG A 261      -2.843  31.362  50.256  1.00 28.53           N  
ATOM   1985  N   GLN A 262       2.526  29.464  49.987  1.00 25.46           N  
ATOM   1986  CA  GLN A 262       2.175  28.234  50.665  1.00 30.08           C  
ATOM   1987  C   GLN A 262       1.042  28.733  51.572  1.00 32.21           C  
ATOM   1988  O   GLN A 262       0.831  29.943  51.707  1.00 31.30           O  
ATOM   1989  CB  GLN A 262       3.351  27.669  51.480  1.00 29.94           C  
ATOM   1990  CG  GLN A 262       4.524  27.276  50.619  1.00 32.60           C  
ATOM   1991  CD  GLN A 262       5.662  26.598  51.378  1.00 33.94           C  
ATOM   1992  OE1 GLN A 262       6.016  26.956  52.498  1.00 34.72           O  
ATOM   1993  NE2 GLN A 262       6.258  25.627  50.734  1.00 33.99           N  
ATOM   1994  N   THR A 263       0.274  27.827  52.150  1.00 35.74           N  
ATOM   1995  CA  THR A 263      -0.813  28.261  53.009  1.00 39.53           C  
ATOM   1996  C   THR A 263      -0.577  27.739  54.396  1.00 42.82           C  
ATOM   1997  O   THR A 263      -0.338  26.546  54.585  1.00 43.12           O  
ATOM   1998  CB  THR A 263      -2.177  27.749  52.519  1.00 39.10           C  
ATOM   1999  OG1 THR A 263      -2.465  28.326  51.242  1.00 37.50           O  
ATOM   2000  CG2 THR A 263      -3.284  28.141  53.507  1.00 38.36           C  
ATOM   2001  N   VAL A 264      -0.639  28.653  55.356  1.00 46.53           N  
ATOM   2002  CA  VAL A 264      -0.442  28.329  56.758  1.00 50.67           C  
ATOM   2003  C   VAL A 264      -1.765  28.523  57.484  1.00 54.63           C  
ATOM   2004  O   VAL A 264      -2.495  29.475  57.201  1.00 54.12           O  
ATOM   2005  CB  VAL A 264       0.618  29.246  57.370  1.00 49.95           C  
ATOM   2006  CG1 VAL A 264       0.671  29.056  58.869  1.00 50.38           C  
ATOM   2007  CG2 VAL A 264       1.974  28.943  56.745  1.00 51.13           C  
ATOM   2008  N   TYR A 265      -2.074  27.616  58.411  1.00 59.19           N  
ATOM   2009  CA  TYR A 265      -3.323  27.688  59.168  1.00 63.26           C  
ATOM   2010  C   TYR A 265      -3.157  28.224  60.575  1.00 64.75           C  
ATOM   2011  O   TYR A 265      -2.528  27.594  61.427  1.00 65.68           O  
ATOM   2012  CB  TYR A 265      -3.987  26.314  59.219  1.00 64.79           C  
ATOM   2013  CG  TYR A 265      -4.375  25.835  57.849  1.00 67.59           C  
ATOM   2014  CD1 TYR A 265      -3.425  25.284  56.987  1.00 68.65           C  
ATOM   2015  CD2 TYR A 265      -5.680  25.996  57.383  1.00 69.12           C  
ATOM   2016  CE1 TYR A 265      -3.764  24.910  55.690  1.00 69.95           C  
ATOM   2017  CE2 TYR A 265      -6.032  25.626  56.090  1.00 70.20           C  
ATOM   2018  CZ  TYR A 265      -5.069  25.085  55.249  1.00 70.52           C  
ATOM   2019  OH  TYR A 265      -5.409  24.729  53.966  1.00 72.14           O  
ATOM   2020  N   VAL A 266      -3.725  29.400  60.805  1.00 66.23           N  
ATOM   2021  CA  VAL A 266      -3.660  30.034  62.108  1.00 68.27           C  
ATOM   2022  C   VAL A 266      -5.016  29.929  62.777  1.00 69.84           C  
ATOM   2023  O   VAL A 266      -5.847  30.829  62.650  1.00 70.83           O  
ATOM   2024  CB  VAL A 266      -3.282  31.521  61.998  1.00 68.09           C  
ATOM   2025  CG1 VAL A 266      -1.771  31.691  62.112  1.00 68.49           C  
ATOM   2026  CG2 VAL A 266      -3.784  32.076  60.675  1.00 68.42           C  
ATOM   2027  N   LYS A 267      -5.249  28.821  63.475  1.00 71.24           N  
ATOM   2028  CA  LYS A 267      -6.517  28.636  64.165  1.00 72.42           C  
ATOM   2029  C   LYS A 267      -6.550  29.552  65.381  1.00 72.73           C  
ATOM   2030  O   LYS A 267      -6.457  29.103  66.531  1.00 73.06           O  
ATOM   2031  CB  LYS A 267      -6.711  27.179  64.586  1.00 72.87           C  
ATOM   2032  CG  LYS A 267      -7.932  26.534  63.935  1.00 74.07           C  
ATOM   2033  CD  LYS A 267      -9.158  27.434  64.083  1.00 74.31           C  
ATOM   2034  CE  LYS A 267      -9.487  27.675  65.557  1.00 75.59           C  
ATOM   2035  NZ  LYS A 267      -9.737  29.114  65.877  1.00 75.78           N  
ATOM   2036  N   GLY A 268      -6.678  30.847  65.103  1.00 72.67           N  
ATOM   2037  CA  GLY A 268      -6.713  31.845  66.151  1.00 73.00           C  
ATOM   2038  C   GLY A 268      -8.118  32.137  66.631  1.00 73.62           C  
ATOM   2039  O   GLY A 268      -9.052  32.282  65.833  1.00 73.49           O  
ATOM   2040  N   LYS A 269      -8.252  32.205  67.953  1.00 73.33           N  
ATOM   2041  CA  LYS A 269      -9.509  32.498  68.633  1.00 72.44           C  
ATOM   2042  C   LYS A 269     -10.484  31.364  68.930  1.00 71.41           C  
ATOM   2043  O   LYS A 269     -10.364  30.231  68.449  1.00 70.51           O  
ATOM   2044  CB  LYS A 269     -10.274  33.613  67.911  1.00 73.23           C  
ATOM   2045  CG  LYS A 269      -9.811  35.014  68.258  1.00 73.68           C  
ATOM   2046  CD  LYS A 269     -10.716  36.041  67.605  1.00 74.04           C  
ATOM   2047  CE  LYS A 269     -12.170  35.828  68.011  1.00 74.28           C  
ATOM   2048  NZ  LYS A 269     -13.093  36.724  67.256  1.00 74.87           N  
ATOM   2049  N   ASP A 270     -11.460  31.736  69.749  1.00 70.03           N  
ATOM   2050  CA  ASP A 270     -12.525  30.880  70.231  1.00 68.04           C  
ATOM   2051  C   ASP A 270     -13.806  31.251  69.488  1.00 66.43           C  
ATOM   2052  O   ASP A 270     -14.262  32.398  69.541  1.00 65.54           O  
ATOM   2053  CB  ASP A 270     -12.677  31.124  71.728  1.00 69.35           C  
ATOM   2054  CG  ASP A 270     -11.955  32.389  72.178  1.00 69.72           C  
ATOM   2055  OD1 ASP A 270     -12.296  33.480  71.668  1.00 71.13           O  
ATOM   2056  OD2 ASP A 270     -11.040  32.297  73.024  1.00 69.52           O  
ATOM   2057  N   GLY A 271     -14.386  30.275  68.800  1.00 64.54           N  
ATOM   2058  CA  GLY A 271     -15.585  30.532  68.026  1.00 62.16           C  
ATOM   2059  C   GLY A 271     -15.215  30.682  66.558  1.00 60.72           C  
ATOM   2060  O   GLY A 271     -15.744  29.970  65.698  1.00 60.45           O  
ATOM   2061  N   GLN A 272     -14.297  31.606  66.275  1.00 58.61           N  
ATOM   2062  CA  GLN A 272     -13.845  31.843  64.912  1.00 56.66           C  
ATOM   2063  C   GLN A 272     -13.186  30.565  64.414  1.00 56.79           C  
ATOM   2064  O   GLN A 272     -12.542  29.845  65.176  1.00 57.13           O  
ATOM   2065  CB  GLN A 272     -12.841  32.993  64.870  1.00 54.29           C  
ATOM   2066  CG  GLN A 272     -13.435  34.354  65.109  1.00 51.92           C  
ATOM   2067  CD  GLN A 272     -14.442  34.737  64.052  1.00 50.76           C  
ATOM   2068  OE1 GLN A 272     -14.143  34.750  62.861  1.00 49.58           O  
ATOM   2069  NE2 GLN A 272     -15.643  35.057  64.487  1.00 48.52           N  
ATOM   2070  N   PRO A 273     -13.349  30.254  63.127  1.00 57.08           N  
ATOM   2071  CA  PRO A 273     -12.751  29.039  62.575  1.00 58.06           C  
ATOM   2072  C   PRO A 273     -11.371  29.192  61.922  1.00 59.25           C  
ATOM   2073  O   PRO A 273     -10.697  30.218  62.053  1.00 58.42           O  
ATOM   2074  CB  PRO A 273     -13.803  28.587  61.582  1.00 57.41           C  
ATOM   2075  CG  PRO A 273     -14.246  29.901  60.996  1.00 57.36           C  
ATOM   2076  CD  PRO A 273     -14.367  30.803  62.214  1.00 56.48           C  
ATOM   2077  N   ASP A 274     -10.977  28.133  61.221  1.00 61.23           N  
ATOM   2078  CA  ASP A 274      -9.708  28.058  60.508  1.00 62.68           C  
ATOM   2079  C   ASP A 274      -9.413  29.275  59.647  1.00 62.37           C  
ATOM   2080  O   ASP A 274      -9.996  29.442  58.575  1.00 63.27           O  
ATOM   2081  CB  ASP A 274      -9.691  26.820  59.612  1.00 64.44           C  
ATOM   2082  CG  ASP A 274      -9.343  25.563  60.366  1.00 67.18           C  
ATOM   2083  OD1 ASP A 274      -9.949  25.316  61.434  1.00 68.91           O  
ATOM   2084  OD2 ASP A 274      -8.463  24.817  59.884  1.00 68.74           O  
ATOM   2085  N   ALA A 275      -8.500  30.118  60.111  1.00 61.58           N  
ATOM   2086  CA  ALA A 275      -8.116  31.300  59.355  1.00 60.23           C  
ATOM   2087  C   ALA A 275      -6.920  30.916  58.491  1.00 59.06           C  
ATOM   2088  O   ALA A 275      -5.882  30.494  59.011  1.00 59.35           O  
ATOM   2089  CB  ALA A 275      -7.742  32.436  60.305  1.00 61.27           C  
ATOM   2090  N   GLU A 276      -7.073  31.039  57.175  1.00 56.82           N  
ATOM   2091  CA  GLU A 276      -5.988  30.706  56.260  1.00 54.80           C  
ATOM   2092  C   GLU A 276      -5.066  31.897  56.108  1.00 52.13           C  
ATOM   2093  O   GLU A 276      -5.523  33.041  56.008  1.00 52.04           O  
ATOM   2094  CB  GLU A 276      -6.527  30.303  54.895  1.00 55.98           C  
ATOM   2095  CG  GLU A 276      -7.292  29.011  54.913  1.00 58.65           C  
ATOM   2096  CD  GLU A 276      -7.736  28.597  53.533  1.00 60.76           C  
ATOM   2097  OE1 GLU A 276      -8.423  29.403  52.868  1.00 61.73           O  
ATOM   2098  OE2 GLU A 276      -7.397  27.467  53.114  1.00 61.82           O  
ATOM   2099  N   LYS A 277      -3.767  31.621  56.092  1.00 47.92           N  
ATOM   2100  CA  LYS A 277      -2.772  32.671  55.975  1.00 43.83           C  
ATOM   2101  C   LYS A 277      -1.755  32.328  54.894  1.00 40.47           C  
ATOM   2102  O   LYS A 277      -1.032  31.331  54.983  1.00 37.45           O  
ATOM   2103  CB  LYS A 277      -2.060  32.874  57.319  1.00 45.06           C  
ATOM   2104  CG  LYS A 277      -1.147  34.092  57.369  1.00 46.91           C  
ATOM   2105  CD  LYS A 277      -0.218  34.078  58.585  1.00 48.15           C  
ATOM   2106  CE  LYS A 277      -0.996  33.941  59.896  1.00 50.55           C  
ATOM   2107  NZ  LYS A 277      -2.106  34.937  60.033  1.00 50.81           N  
ATOM   2108  N   ARG A 278      -1.724  33.174  53.871  1.00 37.31           N  
ATOM   2109  CA  ARG A 278      -0.813  33.019  52.752  1.00 35.46           C  
ATOM   2110  C   ARG A 278       0.576  33.500  53.145  1.00 33.63           C  
ATOM   2111  O   ARG A 278       0.728  34.616  53.646  1.00 34.71           O  
ATOM   2112  CB  ARG A 278      -1.308  33.842  51.551  1.00 34.98           C  
ATOM   2113  CG  ARG A 278      -0.315  33.917  50.398  1.00 32.79           C  
ATOM   2114  CD  ARG A 278       0.086  35.354  50.110  1.00 33.96           C  
ATOM   2115  NE  ARG A 278      -0.512  35.823  48.871  1.00 33.36           N  
ATOM   2116  CZ  ARG A 278      -0.564  37.093  48.474  1.00 32.96           C  
ATOM   2117  NH1 ARG A 278      -0.052  38.067  49.221  1.00 32.76           N  
ATOM   2118  NH2 ARG A 278      -1.137  37.385  47.311  1.00 29.66           N  
ATOM   2119  N   VAL A 279       1.579  32.649  52.939  1.00 30.20           N  
ATOM   2120  CA  VAL A 279       2.964  33.012  53.219  1.00 26.51           C  
ATOM   2121  C   VAL A 279       3.674  32.972  51.868  1.00 24.32           C  
ATOM   2122  O   VAL A 279       3.416  32.085  51.051  1.00 24.14           O  
ATOM   2123  CB  VAL A 279       3.652  32.024  54.195  1.00 26.32           C  
ATOM   2124  CG1 VAL A 279       2.949  32.058  55.546  1.00 25.08           C  
ATOM   2125  CG2 VAL A 279       3.653  30.619  53.607  1.00 26.16           C  
ATOM   2126  N   LEU A 280       4.552  33.938  51.624  1.00 20.93           N  
ATOM   2127  CA  LEU A 280       5.252  34.003  50.349  1.00 19.08           C  
ATOM   2128  C   LEU A 280       6.642  33.461  50.520  1.00 17.66           C  
ATOM   2129  O   LEU A 280       7.133  33.371  51.639  1.00 18.32           O  
ATOM   2130  CB  LEU A 280       5.325  35.445  49.856  1.00 18.00           C  
ATOM   2131  CG  LEU A 280       3.978  36.195  49.791  1.00 20.17           C  
ATOM   2132  CD1 LEU A 280       4.204  37.696  49.643  1.00 15.95           C  
ATOM   2133  CD2 LEU A 280       3.152  35.652  48.639  1.00 17.57           C  
ATOM   2134  N   LEU A 281       7.267  33.096  49.407  1.00 16.57           N  
ATOM   2135  CA  LEU A 281       8.625  32.565  49.422  1.00 16.94           C  
ATOM   2136  C   LEU A 281       9.245  32.718  48.041  1.00 15.00           C  
ATOM   2137  O   LEU A 281       8.550  32.938  47.056  1.00 16.13           O  
ATOM   2138  CB  LEU A 281       8.644  31.085  49.858  1.00 17.16           C  
ATOM   2139  CG  LEU A 281       7.931  30.027  48.993  1.00 21.51           C  
ATOM   2140  CD1 LEU A 281       8.506  28.645  49.286  1.00 23.45           C  
ATOM   2141  CD2 LEU A 281       6.432  30.026  49.272  1.00 19.92           C  
ATOM   2142  N   LEU A 282      10.564  32.617  47.982  1.00 14.72           N  
ATOM   2143  CA  LEU A 282      11.295  32.754  46.735  1.00 13.95           C  
ATOM   2144  C   LEU A 282      11.841  31.393  46.314  1.00 14.18           C  
ATOM   2145  O   LEU A 282      12.241  30.602  47.155  1.00  9.74           O  
ATOM   2146  CB  LEU A 282      12.482  33.699  46.942  1.00 13.13           C  
ATOM   2147  CG  LEU A 282      13.179  34.402  45.773  1.00 16.07           C  
ATOM   2148  CD1 LEU A 282      14.669  34.576  46.086  1.00 15.12           C  
ATOM   2149  CD2 LEU A 282      13.010  33.633  44.516  1.00 17.21           C  
ATOM   2150  N   ARG A 283      11.834  31.111  45.016  1.00 15.89           N  
ATOM   2151  CA  ARG A 283      12.425  29.873  44.529  1.00 16.55           C  
ATOM   2152  C   ARG A 283      13.352  30.229  43.375  1.00 16.38           C  
ATOM   2153  O   ARG A 283      12.907  30.598  42.283  1.00 16.95           O  
ATOM   2154  CB  ARG A 283      11.379  28.849  44.062  1.00 16.58           C  
ATOM   2155  CG  ARG A 283      12.038  27.523  43.586  1.00 15.40           C  
ATOM   2156  CD  ARG A 283      11.036  26.391  43.283  1.00 13.86           C  
ATOM   2157  NE  ARG A 283      10.286  26.593  42.041  1.00 17.18           N  
ATOM   2158  CZ  ARG A 283       9.639  25.630  41.379  1.00 15.81           C  
ATOM   2159  NH1 ARG A 283       9.645  24.386  41.824  1.00 16.01           N  
ATOM   2160  NH2 ARG A 283       8.965  25.914  40.274  1.00 13.39           N  
ATOM   2161  N   GLU A 284      14.649  30.153  43.654  1.00 15.90           N  
ATOM   2162  CA  GLU A 284      15.683  30.423  42.676  1.00 14.11           C  
ATOM   2163  C   GLU A 284      15.702  29.247  41.722  1.00 16.48           C  
ATOM   2164  O   GLU A 284      15.233  28.153  42.053  1.00 15.66           O  
ATOM   2165  CB  GLU A 284      17.055  30.487  43.360  1.00 17.74           C  
ATOM   2166  CG  GLU A 284      17.270  31.659  44.264  1.00 17.99           C  
ATOM   2167  CD  GLU A 284      17.092  32.948  43.503  1.00 21.75           C  
ATOM   2168  OE1 GLU A 284      15.942  33.394  43.422  1.00 22.54           O  
ATOM   2169  OE2 GLU A 284      18.084  33.494  42.965  1.00 20.10           O  
ATOM   2170  N   SER A 285      16.270  29.464  40.549  1.00 17.42           N  
ATOM   2171  CA  SER A 285      16.393  28.402  39.571  1.00 21.52           C  
ATOM   2172  C   SER A 285      17.084  27.198  40.231  1.00 22.34           C  
ATOM   2173  O   SER A 285      16.636  26.056  40.095  1.00 20.98           O  
ATOM   2174  CB  SER A 285      17.224  28.899  38.387  1.00 23.52           C  
ATOM   2175  OG  SER A 285      17.556  27.836  37.520  1.00 29.19           O  
ATOM   2176  N   ALA A 286      18.159  27.471  40.966  1.00 22.93           N  
ATOM   2177  CA  ALA A 286      18.924  26.422  41.646  1.00 24.96           C  
ATOM   2178  C   ALA A 286      18.125  25.640  42.701  1.00 26.45           C  
ATOM   2179  O   ALA A 286      18.556  24.569  43.150  1.00 27.85           O  
ATOM   2180  CB  ALA A 286      20.189  27.026  42.286  1.00 24.67           C  
ATOM   2181  N   GLN A 287      16.967  26.164  43.098  1.00 25.68           N  
ATOM   2182  CA  GLN A 287      16.146  25.485  44.094  1.00 24.26           C  
ATOM   2183  C   GLN A 287      15.097  24.578  43.482  1.00 25.42           C  
ATOM   2184  O   GLN A 287      14.375  23.879  44.196  1.00 26.74           O  
ATOM   2185  CB  GLN A 287      15.464  26.494  45.020  1.00 22.27           C  
ATOM   2186  CG  GLN A 287      16.353  26.943  46.153  1.00 19.61           C  
ATOM   2187  CD  GLN A 287      15.782  28.109  46.911  1.00 19.13           C  
ATOM   2188  OE1 GLN A 287      15.530  29.165  46.341  1.00 20.00           O  
ATOM   2189  NE2 GLN A 287      15.576  27.928  48.202  1.00 19.71           N  
ATOM   2190  N   CYS A 288      14.997  24.594  42.160  1.00 26.23           N  
ATOM   2191  CA  CYS A 288      14.038  23.725  41.494  1.00 26.75           C  
ATOM   2192  C   CYS A 288      14.695  22.381  41.235  1.00 25.29           C  
ATOM   2193  O   CYS A 288      15.789  22.325  40.673  1.00 24.98           O  
ATOM   2194  CB  CYS A 288      13.598  24.309  40.161  1.00 26.05           C  
ATOM   2195  SG  CYS A 288      12.420  23.213  39.319  1.00 31.23           S  
ATOM   2196  N   PRO A 289      14.052  21.279  41.655  1.00 25.71           N  
ATOM   2197  CA  PRO A 289      14.677  19.974  41.399  1.00 25.67           C  
ATOM   2198  C   PRO A 289      15.081  19.901  39.932  1.00 26.95           C  
ATOM   2199  O   PRO A 289      14.262  20.133  39.040  1.00 25.40           O  
ATOM   2200  CB  PRO A 289      13.585  18.967  41.790  1.00 25.74           C  
ATOM   2201  CG  PRO A 289      12.315  19.793  41.923  1.00 25.35           C  
ATOM   2202  CD  PRO A 289      12.784  21.136  42.385  1.00 24.04           C  
ATOM   2203  N   LYS A 290      16.360  19.618  39.698  1.00 29.14           N  
ATOM   2204  CA  LYS A 290      16.917  19.562  38.349  1.00 31.37           C  
ATOM   2205  C   LYS A 290      16.035  18.905  37.305  1.00 32.29           C  
ATOM   2206  O   LYS A 290      15.957  19.387  36.179  1.00 33.05           O  
ATOM   2207  CB  LYS A 290      18.284  18.861  38.366  1.00 34.61           C  
ATOM   2208  CG  LYS A 290      18.320  17.579  39.197  1.00 37.26           C  
ATOM   2209  CD  LYS A 290      19.452  16.617  38.783  1.00 40.78           C  
ATOM   2210  CE  LYS A 290      20.864  17.154  39.034  1.00 41.28           C  
ATOM   2211  NZ  LYS A 290      21.319  18.130  38.003  1.00 43.32           N  
ATOM   2212  N   ALA A 291      15.361  17.818  37.677  1.00 33.02           N  
ATOM   2213  CA  ALA A 291      14.507  17.088  36.742  1.00 34.12           C  
ATOM   2214  C   ALA A 291      13.060  17.577  36.627  1.00 35.54           C  
ATOM   2215  O   ALA A 291      12.215  16.875  36.071  1.00 34.99           O  
ATOM   2216  CB  ALA A 291      14.524  15.602  37.093  1.00 32.62           C  
ATOM   2217  N   ASP A 292      12.785  18.772  37.144  1.00 37.55           N  
ATOM   2218  CA  ASP A 292      11.447  19.367  37.112  1.00 38.80           C  
ATOM   2219  C   ASP A 292      11.550  20.801  36.651  1.00 38.97           C  
ATOM   2220  O   ASP A 292      10.633  21.592  36.854  1.00 36.59           O  
ATOM   2221  CB  ASP A 292      10.836  19.382  38.508  1.00 42.71           C  
ATOM   2222  CG  ASP A 292      10.061  18.140  38.816  1.00 44.67           C  
ATOM   2223  OD1 ASP A 292      10.297  17.558  39.894  1.00 48.90           O  
ATOM   2224  OD2 ASP A 292       9.207  17.756  37.991  1.00 47.84           O  
HETATM 2225  N   MSE A 293      12.683  21.127  36.046  1.00 40.08           N  
HETATM 2226  CA  MSE A 293      12.958  22.470  35.570  1.00 42.26           C  
HETATM 2227  C   MSE A 293      11.926  23.110  34.645  1.00 42.92           C  
HETATM 2228  O   MSE A 293      11.745  24.332  34.670  1.00 40.45           O  
HETATM 2229  CB  MSE A 293      14.337  22.489  34.916  1.00 44.00           C  
HETATM 2230  CG  MSE A 293      15.466  22.628  35.918  1.00 47.18           C  
HETATM 2231 SE   MSE A 293      15.394  24.364  36.793  1.00 54.58          SE  
HETATM 2232  CE  MSE A 293      15.687  25.480  35.247  1.00 49.64           C  
ATOM   2233  N   GLU A 294      11.245  22.306  33.832  1.00 44.00           N  
ATOM   2234  CA  GLU A 294      10.251  22.867  32.919  1.00 45.73           C  
ATOM   2235  C   GLU A 294       9.161  23.625  33.673  1.00 44.00           C  
ATOM   2236  O   GLU A 294       8.650  24.631  33.187  1.00 43.77           O  
ATOM   2237  CB  GLU A 294       9.628  21.773  32.042  1.00 48.94           C  
ATOM   2238  CG  GLU A 294       8.823  20.722  32.794  1.00 55.39           C  
ATOM   2239  CD  GLU A 294       8.339  19.582  31.888  1.00 59.84           C  
ATOM   2240  OE1 GLU A 294       8.700  19.559  30.685  1.00 61.90           O  
ATOM   2241  OE2 GLU A 294       7.598  18.703  32.388  1.00 60.81           O  
ATOM   2242  N   SER A 295       8.804  23.148  34.860  1.00 41.55           N  
ATOM   2243  CA  SER A 295       7.792  23.836  35.654  1.00 39.84           C  
ATOM   2244  C   SER A 295       8.312  25.214  36.117  1.00 37.74           C  
ATOM   2245  O   SER A 295       7.545  26.177  36.179  1.00 37.18           O  
ATOM   2246  CB  SER A 295       7.397  22.988  36.865  1.00 40.42           C  
ATOM   2247  OG  SER A 295       8.499  22.785  37.728  1.00 42.36           O  
ATOM   2248  N   PHE A 296       9.602  25.302  36.451  1.00 34.08           N  
ATOM   2249  CA  PHE A 296      10.200  26.573  36.866  1.00 30.66           C  
ATOM   2250  C   PHE A 296      10.229  27.480  35.639  1.00 31.41           C  
ATOM   2251  O   PHE A 296      10.098  28.699  35.749  1.00 31.27           O  
ATOM   2252  CB  PHE A 296      11.644  26.365  37.363  1.00 26.36           C  
ATOM   2253  CG  PHE A 296      12.415  27.656  37.599  1.00 22.02           C  
ATOM   2254  CD1 PHE A 296      12.429  28.269  38.855  1.00 19.45           C  
ATOM   2255  CD2 PHE A 296      13.089  28.279  36.550  1.00 17.77           C  
ATOM   2256  CE1 PHE A 296      13.098  29.483  39.063  1.00 17.65           C  
ATOM   2257  CE2 PHE A 296      13.756  29.486  36.738  1.00 17.58           C  
ATOM   2258  CZ  PHE A 296      13.763  30.099  38.003  1.00 18.46           C  
ATOM   2259  N   GLN A 297      10.404  26.869  34.470  1.00 31.46           N  
ATOM   2260  CA  GLN A 297      10.500  27.607  33.200  1.00 32.75           C  
ATOM   2261  C   GLN A 297       9.181  28.104  32.607  1.00 30.90           C  
ATOM   2262  O   GLN A 297       9.170  28.959  31.713  1.00 30.13           O  
ATOM   2263  CB  GLN A 297      11.201  26.738  32.148  1.00 34.93           C  
ATOM   2264  CG  GLN A 297      12.710  26.585  32.330  1.00 41.12           C  
ATOM   2265  CD  GLN A 297      13.302  25.516  31.409  1.00 44.95           C  
ATOM   2266  OE1 GLN A 297      12.893  25.368  30.245  1.00 47.32           O  
ATOM   2267  NE2 GLN A 297      14.276  24.774  31.924  1.00 46.25           N  
ATOM   2268  N   ASP A 298       8.078  27.546  33.087  1.00 28.88           N  
ATOM   2269  CA  ASP A 298       6.761  27.914  32.602  1.00 27.64           C  
ATOM   2270  C   ASP A 298       6.412  29.284  33.164  1.00 25.61           C  
ATOM   2271  O   ASP A 298       6.093  29.418  34.353  1.00 24.99           O  
ATOM   2272  CB  ASP A 298       5.751  26.849  33.047  1.00 29.68           C  
ATOM   2273  CG  ASP A 298       4.317  27.243  32.767  1.00 32.41           C  
ATOM   2274  OD1 ASP A 298       4.099  28.221  32.023  1.00 36.03           O  
ATOM   2275  OD2 ASP A 298       3.405  26.566  33.288  1.00 34.32           O  
ATOM   2276  N   ILE A 299       6.486  30.302  32.315  1.00 24.48           N  
ATOM   2277  CA  ILE A 299       6.199  31.658  32.757  1.00 25.31           C  
ATOM   2278  C   ILE A 299       4.722  31.966  32.977  1.00 26.74           C  
ATOM   2279  O   ILE A 299       4.363  33.090  33.331  1.00 27.04           O  
ATOM   2280  CB  ILE A 299       6.793  32.715  31.799  1.00 24.24           C  
ATOM   2281  CG1 ILE A 299       6.021  32.762  30.487  1.00 24.80           C  
ATOM   2282  CG2 ILE A 299       8.248  32.394  31.509  1.00 22.03           C  
ATOM   2283  CD1 ILE A 299       6.527  33.889  29.563  1.00 24.91           C  
ATOM   2284  N   ASN A 300       3.861  30.977  32.774  1.00 27.64           N  
ATOM   2285  CA  ASN A 300       2.439  31.187  32.996  1.00 28.88           C  
ATOM   2286  C   ASN A 300       2.104  30.696  34.392  1.00 29.57           C  
ATOM   2287  O   ASN A 300       1.379  31.361  35.137  1.00 29.34           O  
ATOM   2288  CB  ASN A 300       1.623  30.433  31.949  1.00 30.66           C  
ATOM   2289  CG  ASN A 300       1.906  30.924  30.550  1.00 32.83           C  
ATOM   2290  OD1 ASN A 300       2.292  30.153  29.667  1.00 36.72           O  
ATOM   2291  ND2 ASN A 300       1.730  32.219  30.341  1.00 33.08           N  
ATOM   2292  N   LYS A 301       2.648  29.537  34.752  1.00 28.94           N  
ATOM   2293  CA  LYS A 301       2.403  28.977  36.073  1.00 29.32           C  
ATOM   2294  C   LYS A 301       2.951  29.916  37.155  1.00 28.00           C  
ATOM   2295  O   LYS A 301       2.289  30.165  38.157  1.00 28.34           O  
ATOM   2296  CB  LYS A 301       3.062  27.605  36.188  1.00 32.76           C  
ATOM   2297  CG  LYS A 301       2.712  26.830  37.457  1.00 36.72           C  
ATOM   2298  CD  LYS A 301       3.115  25.354  37.310  1.00 40.52           C  
ATOM   2299  CE  LYS A 301       2.600  24.481  38.455  1.00 41.86           C  
ATOM   2300  NZ  LYS A 301       2.980  23.051  38.233  1.00 41.43           N  
ATOM   2301  N   TYR A 302       4.159  30.433  36.951  1.00 25.39           N  
ATOM   2302  CA  TYR A 302       4.766  31.357  37.912  1.00 23.95           C  
ATOM   2303  C   TYR A 302       5.146  32.609  37.159  1.00 21.29           C  
ATOM   2304  O   TYR A 302       6.272  32.739  36.671  1.00 18.69           O  
ATOM   2305  CB  TYR A 302       6.014  30.739  38.559  1.00 25.80           C  
ATOM   2306  CG  TYR A 302       5.734  29.443  39.284  1.00 27.48           C  
ATOM   2307  CD1 TYR A 302       6.161  28.227  38.759  1.00 28.58           C  
ATOM   2308  CD2 TYR A 302       5.024  29.431  40.485  1.00 29.84           C  
ATOM   2309  CE1 TYR A 302       5.896  27.032  39.405  1.00 29.35           C  
ATOM   2310  CE2 TYR A 302       4.747  28.233  41.142  1.00 30.69           C  
ATOM   2311  CZ  TYR A 302       5.190  27.039  40.591  1.00 30.76           C  
ATOM   2312  OH  TYR A 302       4.934  25.844  41.221  1.00 34.98           O  
ATOM   2313  N   SER A 303       4.197  33.534  37.073  1.00 20.53           N  
ATOM   2314  CA  SER A 303       4.404  34.762  36.323  1.00 19.44           C  
ATOM   2315  C   SER A 303       4.990  35.931  37.077  1.00 19.57           C  
ATOM   2316  O   SER A 303       5.155  37.003  36.503  1.00 20.45           O  
ATOM   2317  CB  SER A 303       3.088  35.189  35.677  1.00 22.00           C  
ATOM   2318  OG  SER A 303       2.035  35.131  36.617  1.00 23.09           O  
ATOM   2319  N   PHE A 304       5.293  35.744  38.356  1.00 18.64           N  
ATOM   2320  CA  PHE A 304       5.885  36.828  39.135  1.00 18.12           C  
ATOM   2321  C   PHE A 304       7.355  36.540  39.410  1.00 17.48           C  
ATOM   2322  O   PHE A 304       7.712  35.688  40.236  1.00 16.10           O  
ATOM   2323  CB  PHE A 304       5.093  37.045  40.422  1.00 16.86           C  
ATOM   2324  CG  PHE A 304       3.766  37.739  40.194  1.00 19.55           C  
ATOM   2325  CD1 PHE A 304       2.563  37.129  40.560  1.00 18.63           C  
ATOM   2326  CD2 PHE A 304       3.727  39.005  39.616  1.00 18.67           C  
ATOM   2327  CE1 PHE A 304       1.328  37.774  40.355  1.00 20.52           C  
ATOM   2328  CE2 PHE A 304       2.510  39.658  39.405  1.00 21.89           C  
ATOM   2329  CZ  PHE A 304       1.302  39.037  39.779  1.00 21.04           C  
ATOM   2330  N   PHE A 305       8.195  37.276  38.690  1.00 15.33           N  
ATOM   2331  CA  PHE A 305       9.639  37.129  38.735  1.00 14.42           C  
ATOM   2332  C   PHE A 305      10.247  38.174  39.649  1.00 14.27           C  
ATOM   2333  O   PHE A 305       9.934  39.357  39.548  1.00 15.87           O  
ATOM   2334  CB  PHE A 305      10.200  37.303  37.313  1.00 14.74           C  
ATOM   2335  CG  PHE A 305      11.549  36.649  37.083  1.00 15.64           C  
ATOM   2336  CD1 PHE A 305      11.665  35.259  37.019  1.00 14.86           C  
ATOM   2337  CD2 PHE A 305      12.701  37.425  36.921  1.00 14.33           C  
ATOM   2338  CE1 PHE A 305      12.908  34.647  36.799  1.00 15.70           C  
ATOM   2339  CE2 PHE A 305      13.947  36.829  36.699  1.00 14.62           C  
ATOM   2340  CZ  PHE A 305      14.057  35.439  36.639  1.00 14.96           C  
ATOM   2341  N   ASN A 306      11.125  37.729  40.533  1.00 12.37           N  
ATOM   2342  CA  ASN A 306      11.806  38.617  41.461  1.00 13.69           C  
ATOM   2343  C   ASN A 306      12.813  39.514  40.740  1.00 12.80           C  
ATOM   2344  O   ASN A 306      13.641  39.036  39.955  1.00  9.92           O  
ATOM   2345  CB  ASN A 306      12.521  37.787  42.537  1.00 13.76           C  
ATOM   2346  CG  ASN A 306      13.333  38.636  43.486  1.00 16.81           C  
ATOM   2347  OD1 ASN A 306      12.921  39.742  43.857  1.00 19.19           O  
ATOM   2348  ND2 ASN A 306      14.485  38.117  43.908  1.00 12.04           N  
ATOM   2349  N   THR A 307      12.735  40.815  41.005  1.00 11.52           N  
ATOM   2350  CA  THR A 307      13.660  41.771  40.393  1.00 11.52           C  
ATOM   2351  C   THR A 307      14.860  41.967  41.312  1.00 10.10           C  
ATOM   2352  O   THR A 307      15.873  42.507  40.899  1.00 10.83           O  
ATOM   2353  CB  THR A 307      13.016  43.167  40.226  1.00 13.02           C  
ATOM   2354  OG1 THR A 307      12.837  43.757  41.524  1.00 11.55           O  
ATOM   2355  CG2 THR A 307      11.682  43.059  39.518  1.00 12.71           C  
ATOM   2356  N   ASN A 308      14.714  41.511  42.552  1.00 10.39           N  
ATOM   2357  CA  ASN A 308      15.708  41.644  43.616  1.00 13.59           C  
ATOM   2358  C   ASN A 308      15.774  43.111  44.064  1.00 13.85           C  
ATOM   2359  O   ASN A 308      16.768  43.539  44.669  1.00 14.43           O  
ATOM   2360  CB  ASN A 308      17.112  41.112  43.202  1.00 17.34           C  
ATOM   2361  CG  ASN A 308      17.663  40.066  44.175  1.00 19.92           C  
ATOM   2362  OD1 ASN A 308      17.628  40.266  45.375  1.00 22.76           O  
ATOM   2363  ND2 ASN A 308      18.178  38.963  43.653  1.00 29.81           N  
ATOM   2364  N   ASN A 309      14.752  43.875  43.731  1.00 12.19           N  
ATOM   2365  CA  ASN A 309      14.610  45.228  44.221  1.00 13.05           C  
ATOM   2366  C   ASN A 309      13.875  45.043  45.529  1.00 12.32           C  
ATOM   2367  O   ASN A 309      12.667  44.886  45.563  1.00 14.50           O  
ATOM   2368  CB  ASN A 309      13.764  46.115  43.302  1.00 12.54           C  
ATOM   2369  CG  ASN A 309      14.332  46.306  41.924  1.00 14.32           C  
ATOM   2370  OD1 ASN A 309      15.516  46.050  41.698  1.00 15.71           O  
ATOM   2371  ND2 ASN A 309      13.511  46.745  40.990  1.00 14.55           N  
ATOM   2372  N   LEU A 310      14.619  45.053  46.628  1.00 12.37           N  
ATOM   2373  CA  LEU A 310      14.055  44.789  47.949  1.00 12.34           C  
ATOM   2374  C   LEU A 310      14.155  45.958  48.905  1.00 10.93           C  
ATOM   2375  O   LEU A 310      15.125  46.712  48.885  1.00  9.27           O  
ATOM   2376  CB  LEU A 310      14.758  43.586  48.603  1.00 11.59           C  
ATOM   2377  CG  LEU A 310      14.414  42.138  48.250  1.00 14.37           C  
ATOM   2378  CD1 LEU A 310      13.886  42.012  46.844  1.00 10.11           C  
ATOM   2379  CD2 LEU A 310      15.661  41.302  48.460  1.00 12.21           C  
ATOM   2380  N   TRP A 311      13.131  46.064  49.743  1.00 12.44           N  
ATOM   2381  CA  TRP A 311      13.014  47.091  50.762  1.00 14.75           C  
ATOM   2382  C   TRP A 311      12.893  46.369  52.093  1.00 14.94           C  
ATOM   2383  O   TRP A 311      12.095  45.429  52.244  1.00 15.35           O  
ATOM   2384  CB  TRP A 311      11.756  47.925  50.549  1.00 11.94           C  
ATOM   2385  CG  TRP A 311      11.684  48.583  49.226  1.00 14.74           C  
ATOM   2386  CD1 TRP A 311      11.337  48.007  48.037  1.00 13.38           C  
ATOM   2387  CD2 TRP A 311      11.894  49.971  48.958  1.00 12.94           C  
ATOM   2388  NE1 TRP A 311      11.312  48.958  47.041  1.00 15.43           N  
ATOM   2389  CE2 TRP A 311      11.656  50.172  47.579  1.00 16.06           C  
ATOM   2390  CE3 TRP A 311      12.270  51.063  49.748  1.00 15.00           C  
ATOM   2391  CZ2 TRP A 311      11.761  51.432  46.972  1.00 15.04           C  
ATOM   2392  CZ3 TRP A 311      12.378  52.316  49.148  1.00 15.57           C  
ATOM   2393  CH2 TRP A 311      12.126  52.486  47.768  1.00 13.66           C  
ATOM   2394  N   ILE A 312      13.685  46.815  53.054  1.00 16.04           N  
ATOM   2395  CA  ILE A 312      13.686  46.217  54.375  1.00 15.83           C  
ATOM   2396  C   ILE A 312      13.710  47.269  55.466  1.00 15.30           C  
ATOM   2397  O   ILE A 312      14.470  48.242  55.383  1.00 15.21           O  
ATOM   2398  CB  ILE A 312      14.924  45.314  54.597  1.00 17.90           C  
ATOM   2399  CG1 ILE A 312      15.115  44.366  53.402  1.00 21.45           C  
ATOM   2400  CG2 ILE A 312      14.730  44.484  55.883  1.00 18.93           C  
ATOM   2401  CD1 ILE A 312      16.074  44.874  52.347  1.00 21.42           C  
ATOM   2402  N   ARG A 313      12.873  47.061  56.481  1.00 14.62           N  
ATOM   2403  CA  ARG A 313      12.809  47.949  57.628  1.00 14.26           C  
ATOM   2404  C   ARG A 313      13.885  47.437  58.577  1.00 13.45           C  
ATOM   2405  O   ARG A 313      13.775  46.349  59.165  1.00 12.75           O  
ATOM   2406  CB  ARG A 313      11.423  47.902  58.282  1.00 15.93           C  
ATOM   2407  CG  ARG A 313      11.387  48.600  59.624  1.00 22.90           C  
ATOM   2408  CD  ARG A 313      10.027  49.198  59.974  1.00 26.97           C  
ATOM   2409  NE  ARG A 313       8.998  48.947  58.967  1.00 32.12           N  
ATOM   2410  CZ  ARG A 313       7.945  49.738  58.777  1.00 34.91           C  
ATOM   2411  NH1 ARG A 313       7.794  50.829  59.527  1.00 35.76           N  
ATOM   2412  NH2 ARG A 313       7.046  49.448  57.842  1.00 34.39           N  
ATOM   2413  N   LEU A 314      14.945  48.228  58.677  1.00 13.14           N  
ATOM   2414  CA  LEU A 314      16.119  47.930  59.476  1.00 11.64           C  
ATOM   2415  C   LEU A 314      15.934  47.577  60.956  1.00 12.94           C  
ATOM   2416  O   LEU A 314      16.533  46.623  61.442  1.00 12.86           O  
ATOM   2417  CB  LEU A 314      17.097  49.092  59.322  1.00 12.06           C  
ATOM   2418  CG  LEU A 314      17.454  49.304  57.849  1.00 15.50           C  
ATOM   2419  CD1 LEU A 314      18.345  50.540  57.660  1.00 12.98           C  
ATOM   2420  CD2 LEU A 314      18.141  48.044  57.346  1.00 12.33           C  
ATOM   2421  N   PRO A 315      15.126  48.346  61.699  1.00 11.70           N  
ATOM   2422  CA  PRO A 315      14.964  47.987  63.114  1.00 13.33           C  
ATOM   2423  C   PRO A 315      14.378  46.588  63.298  1.00 12.64           C  
ATOM   2424  O   PRO A 315      14.753  45.855  64.217  1.00 10.93           O  
ATOM   2425  CB  PRO A 315      14.023  49.070  63.654  1.00 11.37           C  
ATOM   2426  CG  PRO A 315      14.313  50.230  62.762  1.00 15.28           C  
ATOM   2427  CD  PRO A 315      14.491  49.636  61.397  1.00 10.32           C  
ATOM   2428  N   VAL A 316      13.442  46.241  62.424  1.00 12.33           N  
ATOM   2429  CA  VAL A 316      12.772  44.957  62.487  1.00 12.00           C  
ATOM   2430  C   VAL A 316      13.719  43.830  62.108  1.00 13.90           C  
ATOM   2431  O   VAL A 316      13.713  42.773  62.721  1.00 13.40           O  
ATOM   2432  CB  VAL A 316      11.536  44.950  61.565  1.00 12.29           C  
ATOM   2433  CG1 VAL A 316      10.819  43.608  61.650  1.00 10.59           C  
ATOM   2434  CG2 VAL A 316      10.586  46.086  61.967  1.00 12.96           C  
ATOM   2435  N   LEU A 317      14.537  44.065  61.094  1.00 13.42           N  
ATOM   2436  CA  LEU A 317      15.486  43.059  60.672  1.00 13.43           C  
ATOM   2437  C   LEU A 317      16.425  42.796  61.830  1.00 13.37           C  
ATOM   2438  O   LEU A 317      16.685  41.643  62.197  1.00 17.30           O  
ATOM   2439  CB  LEU A 317      16.289  43.567  59.475  1.00 11.33           C  
ATOM   2440  CG  LEU A 317      17.507  42.744  59.091  1.00 10.30           C  
ATOM   2441  CD1 LEU A 317      17.071  41.411  58.458  1.00  9.21           C  
ATOM   2442  CD2 LEU A 317      18.344  43.564  58.126  1.00  9.37           C  
ATOM   2443  N   LEU A 318      16.921  43.875  62.416  1.00 12.00           N  
ATOM   2444  CA  LEU A 318      17.859  43.779  63.516  1.00 13.19           C  
ATOM   2445  C   LEU A 318      17.257  43.016  64.692  1.00 14.79           C  
ATOM   2446  O   LEU A 318      17.904  42.128  65.263  1.00 13.55           O  
ATOM   2447  CB  LEU A 318      18.308  45.188  63.940  1.00 12.02           C  
ATOM   2448  CG  LEU A 318      19.269  45.335  65.132  1.00 13.92           C  
ATOM   2449  CD1 LEU A 318      20.560  44.525  64.922  1.00  9.85           C  
ATOM   2450  CD2 LEU A 318      19.589  46.817  65.322  1.00 11.77           C  
ATOM   2451  N   GLU A 319      16.021  43.343  65.058  1.00 15.90           N  
ATOM   2452  CA  GLU A 319      15.407  42.644  66.182  1.00 19.26           C  
ATOM   2453  C   GLU A 319      15.099  41.176  65.886  1.00 17.50           C  
ATOM   2454  O   GLU A 319      15.335  40.332  66.740  1.00 12.69           O  
ATOM   2455  CB  GLU A 319      14.137  43.378  66.684  1.00 20.65           C  
ATOM   2456  CG  GLU A 319      12.969  43.439  65.716  1.00 30.02           C  
ATOM   2457  CD  GLU A 319      11.805  44.303  66.230  1.00 35.49           C  
ATOM   2458  OE1 GLU A 319      11.996  45.066  67.210  1.00 37.23           O  
ATOM   2459  OE2 GLU A 319      10.704  44.222  65.634  1.00 36.40           O  
ATOM   2460  N   THR A 320      14.586  40.848  64.697  1.00 16.93           N  
ATOM   2461  CA  THR A 320      14.306  39.430  64.483  1.00 18.08           C  
ATOM   2462  C   THR A 320      15.592  38.610  64.423  1.00 17.19           C  
ATOM   2463  O   THR A 320      15.588  37.449  64.805  1.00 15.42           O  
ATOM   2464  CB  THR A 320      13.389  39.107  63.250  1.00 18.21           C  
ATOM   2465  OG1 THR A 320      14.156  38.487  62.218  1.00 20.38           O  
ATOM   2466  CG2 THR A 320      12.688  40.325  62.748  1.00 10.23           C  
HETATM 2467  N   MSE A 321      16.694  39.210  63.976  1.00 17.46           N  
HETATM 2468  CA  MSE A 321      17.963  38.478  63.937  1.00 18.60           C  
HETATM 2469  C   MSE A 321      18.460  38.280  65.368  1.00 18.57           C  
HETATM 2470  O   MSE A 321      18.998  37.222  65.719  1.00 16.94           O  
HETATM 2471  CB  MSE A 321      19.013  39.234  63.106  1.00 17.96           C  
HETATM 2472  CG  MSE A 321      18.785  39.096  61.595  1.00 16.66           C  
HETATM 2473 SE   MSE A 321      20.107  39.967  60.504  1.00 19.08          SE  
HETATM 2474  CE  MSE A 321      21.499  38.594  60.531  1.00 16.24           C  
ATOM   2475  N   GLN A 322      18.266  39.303  66.194  1.00 17.33           N  
ATOM   2476  CA  GLN A 322      18.680  39.233  67.589  1.00 18.31           C  
ATOM   2477  C   GLN A 322      17.930  38.122  68.298  1.00 18.93           C  
ATOM   2478  O   GLN A 322      18.534  37.341  69.023  1.00 20.48           O  
ATOM   2479  CB  GLN A 322      18.418  40.573  68.307  1.00 14.58           C  
ATOM   2480  CG  GLN A 322      19.483  41.578  67.996  1.00 13.41           C  
ATOM   2481  CD  GLN A 322      19.150  43.015  68.367  1.00  8.82           C  
ATOM   2482  OE1 GLN A 322      20.043  43.849  68.365  1.00 14.00           O  
ATOM   2483  NE2 GLN A 322      17.891  43.312  68.678  1.00  9.21           N  
ATOM   2484  N   GLU A 323      16.622  38.045  68.079  1.00 21.51           N  
ATOM   2485  CA  GLU A 323      15.814  37.023  68.743  1.00 26.11           C  
ATOM   2486  C   GLU A 323      16.076  35.641  68.215  1.00 25.34           C  
ATOM   2487  O   GLU A 323      15.666  34.658  68.821  1.00 27.29           O  
ATOM   2488  CB  GLU A 323      14.308  37.302  68.615  1.00 28.39           C  
ATOM   2489  CG  GLU A 323      13.723  37.366  67.189  1.00 37.10           C  
ATOM   2490  CD  GLU A 323      13.515  36.001  66.482  1.00 41.18           C  
ATOM   2491  OE1 GLU A 323      12.643  35.906  65.588  1.00 44.39           O  
ATOM   2492  OE2 GLU A 323      14.213  35.014  66.779  1.00 47.03           O  
ATOM   2493  N   HIS A 324      16.751  35.559  67.081  1.00 26.82           N  
ATOM   2494  CA  HIS A 324      17.016  34.277  66.487  1.00 27.46           C  
ATOM   2495  C   HIS A 324      18.487  33.894  66.543  1.00 26.88           C  
ATOM   2496  O   HIS A 324      19.041  33.409  65.562  1.00 27.43           O  
ATOM   2497  CB  HIS A 324      16.531  34.288  65.045  1.00 30.11           C  
ATOM   2498  CG  HIS A 324      16.145  32.936  64.549  1.00 36.83           C  
ATOM   2499  ND1 HIS A 324      17.056  31.911  64.414  1.00 38.79           N  
ATOM   2500  CD2 HIS A 324      14.932  32.409  64.265  1.00 37.76           C  
ATOM   2501  CE1 HIS A 324      16.420  30.803  64.074  1.00 39.63           C  
ATOM   2502  NE2 HIS A 324      15.130  31.078  63.979  1.00 41.18           N  
ATOM   2503  N   GLY A 325      19.121  34.141  67.681  1.00 25.43           N  
ATOM   2504  CA  GLY A 325      20.516  33.781  67.836  1.00 22.25           C  
ATOM   2505  C   GLY A 325      21.511  34.603  67.054  1.00 20.23           C  
ATOM   2506  O   GLY A 325      22.664  34.211  66.905  1.00 20.11           O  
ATOM   2507  N   GLY A 326      21.076  35.741  66.537  1.00 20.00           N  
ATOM   2508  CA  GLY A 326      21.982  36.587  65.777  1.00 17.76           C  
ATOM   2509  C   GLY A 326      22.231  36.078  64.370  1.00 17.60           C  
ATOM   2510  O   GLY A 326      23.362  36.073  63.890  1.00 19.41           O  
ATOM   2511  N   THR A 327      21.164  35.649  63.706  1.00 17.18           N  
ATOM   2512  CA  THR A 327      21.241  35.132  62.341  1.00 16.26           C  
ATOM   2513  C   THR A 327      19.869  35.259  61.708  1.00 14.87           C  
ATOM   2514  O   THR A 327      18.885  35.505  62.380  1.00 14.58           O  
ATOM   2515  CB  THR A 327      21.607  33.611  62.284  1.00 18.08           C  
ATOM   2516  OG1 THR A 327      20.502  32.838  62.770  1.00 19.96           O  
ATOM   2517  CG2 THR A 327      22.825  33.301  63.129  1.00 17.46           C  
ATOM   2518  N   LEU A 328      19.810  35.093  60.403  1.00 15.37           N  
ATOM   2519  CA  LEU A 328      18.546  35.120  59.695  1.00 17.11           C  
ATOM   2520  C   LEU A 328      18.566  33.744  59.055  1.00 17.19           C  
ATOM   2521  O   LEU A 328      19.345  33.479  58.154  1.00 20.25           O  
ATOM   2522  CB  LEU A 328      18.523  36.217  58.632  1.00 17.57           C  
ATOM   2523  CG  LEU A 328      17.121  36.489  58.067  1.00 17.34           C  
ATOM   2524  CD1 LEU A 328      16.230  37.017  59.193  1.00 17.54           C  
ATOM   2525  CD2 LEU A 328      17.196  37.512  56.929  1.00 17.68           C  
ATOM   2526  N   PRO A 329      17.723  32.835  59.542  1.00 19.01           N  
ATOM   2527  CA  PRO A 329      17.671  31.478  59.007  1.00 18.60           C  
ATOM   2528  C   PRO A 329      17.086  31.337  57.615  1.00 19.13           C  
ATOM   2529  O   PRO A 329      16.023  30.746  57.452  1.00 21.83           O  
ATOM   2530  CB  PRO A 329      16.843  30.748  60.043  1.00 20.74           C  
ATOM   2531  CG  PRO A 329      15.834  31.821  60.433  1.00 21.11           C  
ATOM   2532  CD  PRO A 329      16.750  33.009  60.636  1.00 18.64           C  
ATOM   2533  N   LEU A 330      17.782  31.864  56.610  1.00 17.82           N  
ATOM   2534  CA  LEU A 330      17.327  31.777  55.227  1.00 15.03           C  
ATOM   2535  C   LEU A 330      17.500  30.352  54.741  1.00 17.19           C  
ATOM   2536  O   LEU A 330      18.441  29.665  55.152  1.00 14.56           O  
ATOM   2537  CB  LEU A 330      18.146  32.710  54.335  1.00 12.38           C  
ATOM   2538  CG  LEU A 330      18.061  34.211  54.651  1.00 14.20           C  
ATOM   2539  CD1 LEU A 330      18.841  34.992  53.602  1.00 11.10           C  
ATOM   2540  CD2 LEU A 330      16.615  34.668  54.674  1.00  8.81           C  
ATOM   2541  N   PRO A 331      16.596  29.887  53.853  1.00 18.56           N  
ATOM   2542  CA  PRO A 331      16.696  28.520  53.328  1.00 20.41           C  
ATOM   2543  C   PRO A 331      17.988  28.329  52.534  1.00 21.99           C  
ATOM   2544  O   PRO A 331      18.278  29.081  51.589  1.00 21.78           O  
ATOM   2545  CB  PRO A 331      15.437  28.375  52.458  1.00 19.50           C  
ATOM   2546  CG  PRO A 331      15.091  29.785  52.088  1.00 18.66           C  
ATOM   2547  CD  PRO A 331      15.386  30.560  53.346  1.00 17.02           C  
ATOM   2548  N   VAL A 332      18.758  27.313  52.929  1.00 22.14           N  
ATOM   2549  CA  VAL A 332      20.037  27.013  52.294  1.00 21.16           C  
ATOM   2550  C   VAL A 332      19.929  26.547  50.849  1.00 22.39           C  
ATOM   2551  O   VAL A 332      18.991  25.829  50.475  1.00 24.34           O  
ATOM   2552  CB  VAL A 332      20.798  25.919  53.062  1.00 22.29           C  
ATOM   2553  CG1 VAL A 332      20.138  24.566  52.816  1.00 22.63           C  
ATOM   2554  CG2 VAL A 332      22.263  25.892  52.630  1.00 20.89           C  
ATOM   2555  N   ILE A 333      20.897  26.971  50.042  1.00 20.85           N  
ATOM   2556  CA  ILE A 333      20.983  26.568  48.654  1.00 20.23           C  
ATOM   2557  C   ILE A 333      22.313  25.802  48.555  1.00 21.81           C  
ATOM   2558  O   ILE A 333      23.388  26.343  48.827  1.00 19.57           O  
ATOM   2559  CB  ILE A 333      20.982  27.774  47.714  1.00 20.59           C  
ATOM   2560  CG1 ILE A 333      19.627  28.497  47.797  1.00 21.41           C  
ATOM   2561  CG2 ILE A 333      21.249  27.306  46.278  1.00 21.10           C  
ATOM   2562  CD1 ILE A 333      19.505  29.758  46.911  1.00 16.23           C  
ATOM   2563  N   ARG A 334      22.222  24.529  48.193  1.00 23.20           N  
ATOM   2564  CA  ARG A 334      23.390  23.660  48.099  1.00 24.51           C  
ATOM   2565  C   ARG A 334      23.963  23.627  46.701  1.00 25.26           C  
ATOM   2566  O   ARG A 334      23.527  22.841  45.857  1.00 26.94           O  
ATOM   2567  CB  ARG A 334      23.008  22.240  48.514  1.00 27.38           C  
ATOM   2568  CG  ARG A 334      24.134  21.426  49.127  1.00 28.50           C  
ATOM   2569  CD  ARG A 334      23.685  19.988  49.324  1.00 28.37           C  
ATOM   2570  NE  ARG A 334      23.473  19.310  48.044  1.00 31.11           N  
ATOM   2571  CZ  ARG A 334      23.147  18.024  47.928  1.00 32.43           C  
ATOM   2572  NH1 ARG A 334      22.987  17.283  49.017  1.00 30.99           N  
ATOM   2573  NH2 ARG A 334      23.005  17.471  46.727  1.00 32.88           N  
ATOM   2574  N   ASN A 335      24.953  24.477  46.463  1.00 25.42           N  
ATOM   2575  CA  ASN A 335      25.599  24.559  45.165  1.00 24.99           C  
ATOM   2576  C   ASN A 335      26.736  23.518  45.048  1.00 24.20           C  
ATOM   2577  O   ASN A 335      27.579  23.401  45.925  1.00 23.39           O  
ATOM   2578  CB  ASN A 335      26.116  25.986  44.980  1.00 26.48           C  
ATOM   2579  CG  ASN A 335      26.731  26.217  43.621  1.00 29.20           C  
ATOM   2580  OD1 ASN A 335      26.493  25.464  42.679  1.00 30.56           O  
ATOM   2581  ND2 ASN A 335      27.519  27.279  43.505  1.00 30.98           N  
ATOM   2582  N   GLU A 336      26.736  22.751  43.966  1.00 24.92           N  
ATOM   2583  CA  GLU A 336      27.753  21.727  43.743  1.00 25.74           C  
ATOM   2584  C   GLU A 336      28.797  22.226  42.763  1.00 24.75           C  
ATOM   2585  O   GLU A 336      28.459  22.742  41.705  1.00 24.69           O  
ATOM   2586  CB  GLU A 336      27.121  20.458  43.164  1.00 26.98           C  
ATOM   2587  CG  GLU A 336      25.778  20.109  43.758  1.00 30.49           C  
ATOM   2588  CD  GLU A 336      25.208  18.825  43.193  1.00 33.67           C  
ATOM   2589  OE1 GLU A 336      25.600  18.431  42.071  1.00 35.77           O  
ATOM   2590  OE2 GLU A 336      24.353  18.218  43.866  1.00 34.81           O  
ATOM   2591  N   LYS A 337      30.065  22.066  43.122  1.00 25.22           N  
ATOM   2592  CA  LYS A 337      31.180  22.470  42.268  1.00 25.40           C  
ATOM   2593  C   LYS A 337      32.409  21.680  42.677  1.00 23.60           C  
ATOM   2594  O   LYS A 337      32.293  20.719  43.436  1.00 23.18           O  
ATOM   2595  CB  LYS A 337      31.433  23.980  42.397  1.00 28.58           C  
ATOM   2596  CG  LYS A 337      30.386  24.784  41.649  1.00 31.61           C  
ATOM   2597  CD  LYS A 337      30.674  26.253  41.563  1.00 36.80           C  
ATOM   2598  CE  LYS A 337      29.632  26.918  40.663  1.00 39.69           C  
ATOM   2599  NZ  LYS A 337      29.603  28.407  40.777  1.00 44.19           N  
ATOM   2600  N   THR A 338      33.574  22.042  42.152  1.00 22.98           N  
ATOM   2601  CA  THR A 338      34.812  21.361  42.547  1.00 22.13           C  
ATOM   2602  C   THR A 338      35.668  22.461  43.173  1.00 22.65           C  
ATOM   2603  O   THR A 338      35.563  23.613  42.756  1.00 21.02           O  
ATOM   2604  CB  THR A 338      35.546  20.712  41.335  1.00 22.36           C  
ATOM   2605  OG1 THR A 338      35.833  21.707  40.344  1.00 20.71           O  
ATOM   2606  CG2 THR A 338      34.696  19.604  40.723  1.00 18.49           C  
ATOM   2607  N   VAL A 339      36.490  22.120  44.169  1.00 24.20           N  
ATOM   2608  CA  VAL A 339      37.306  23.124  44.864  1.00 27.38           C  
ATOM   2609  C   VAL A 339      37.963  24.102  43.902  1.00 29.42           C  
ATOM   2610  O   VAL A 339      38.026  25.307  44.163  1.00 29.20           O  
ATOM   2611  CB  VAL A 339      38.428  22.504  45.723  1.00 28.51           C  
ATOM   2612  CG1 VAL A 339      38.578  23.308  47.007  1.00 25.18           C  
ATOM   2613  CG2 VAL A 339      38.140  21.056  46.009  1.00 30.08           C  
ATOM   2614  N   ASP A 340      38.481  23.570  42.803  1.00 30.97           N  
ATOM   2615  CA  ASP A 340      39.090  24.393  41.778  1.00 33.78           C  
ATOM   2616  C   ASP A 340      38.070  24.322  40.648  1.00 35.02           C  
ATOM   2617  O   ASP A 340      38.062  23.356  39.876  1.00 35.04           O  
ATOM   2618  CB  ASP A 340      40.423  23.795  41.326  1.00 34.61           C  
ATOM   2619  CG  ASP A 340      41.142  24.671  40.316  1.00 36.46           C  
ATOM   2620  OD1 ASP A 340      40.463  25.416  39.574  1.00 35.28           O  
ATOM   2621  OD2 ASP A 340      42.389  24.599  40.259  1.00 37.61           O  
ATOM   2622  N   SER A 341      37.198  25.329  40.573  1.00 35.74           N  
ATOM   2623  CA  SER A 341      36.146  25.365  39.555  1.00 37.58           C  
ATOM   2624  C   SER A 341      36.645  24.941  38.177  1.00 38.23           C  
ATOM   2625  O   SER A 341      35.972  24.182  37.482  1.00 39.17           O  
ATOM   2626  CB  SER A 341      35.519  26.763  39.484  1.00 36.82           C  
ATOM   2627  OG  SER A 341      36.497  27.750  39.216  1.00 38.91           O  
ATOM   2628  N   SER A 342      37.831  25.413  37.803  1.00 39.20           N  
ATOM   2629  CA  SER A 342      38.443  25.104  36.504  1.00 40.42           C  
ATOM   2630  C   SER A 342      38.771  23.621  36.326  1.00 40.86           C  
ATOM   2631  O   SER A 342      38.431  23.006  35.311  1.00 43.13           O  
ATOM   2632  CB  SER A 342      39.741  25.902  36.334  1.00 39.94           C  
ATOM   2633  OG  SER A 342      39.601  27.230  36.807  1.00 41.09           O  
ATOM   2634  N   ASN A 343      39.449  23.061  37.318  1.00 40.10           N  
ATOM   2635  CA  ASN A 343      39.868  21.669  37.287  1.00 39.06           C  
ATOM   2636  C   ASN A 343      38.784  20.701  37.769  1.00 39.92           C  
ATOM   2637  O   ASN A 343      38.362  20.747  38.927  1.00 38.91           O  
ATOM   2638  CB  ASN A 343      41.118  21.523  38.146  1.00 38.74           C  
ATOM   2639  CG  ASN A 343      41.619  20.112  38.206  1.00 38.82           C  
ATOM   2640  OD1 ASN A 343      41.040  19.208  37.603  1.00 37.83           O  
ATOM   2641  ND2 ASN A 343      42.711  19.905  38.936  1.00 38.07           N  
ATOM   2642  N   SER A 344      38.346  19.812  36.882  1.00 39.75           N  
ATOM   2643  CA  SER A 344      37.317  18.840  37.229  1.00 39.30           C  
ATOM   2644  C   SER A 344      37.889  17.570  37.823  1.00 38.70           C  
ATOM   2645  O   SER A 344      37.172  16.595  38.044  1.00 39.16           O  
ATOM   2646  CB  SER A 344      36.462  18.506  36.010  1.00 40.72           C  
ATOM   2647  OG  SER A 344      35.568  19.574  35.744  1.00 42.35           O  
ATOM   2648  N   ALA A 345      39.191  17.579  38.073  1.00 37.74           N  
ATOM   2649  CA  ALA A 345      39.847  16.439  38.687  1.00 36.31           C  
ATOM   2650  C   ALA A 345      39.935  16.756  40.175  1.00 34.71           C  
ATOM   2651  O   ALA A 345      40.212  15.875  40.996  1.00 34.16           O  
ATOM   2652  CB  ALA A 345      41.250  16.244  38.105  1.00 36.48           C  
ATOM   2653  N   SER A 346      39.716  18.027  40.516  1.00 32.89           N  
ATOM   2654  CA  SER A 346      39.766  18.451  41.915  1.00 30.12           C  
ATOM   2655  C   SER A 346      38.526  17.900  42.607  1.00 28.20           C  
ATOM   2656  O   SER A 346      37.520  17.607  41.965  1.00 29.06           O  
ATOM   2657  CB  SER A 346      39.830  19.979  42.029  1.00 29.91           C  
ATOM   2658  OG  SER A 346      38.736  20.601  41.378  1.00 29.90           O  
ATOM   2659  N   PRO A 347      38.593  17.727  43.929  1.00 26.80           N  
ATOM   2660  CA  PRO A 347      37.483  17.194  44.727  1.00 24.67           C  
ATOM   2661  C   PRO A 347      36.152  17.941  44.577  1.00 25.70           C  
ATOM   2662  O   PRO A 347      36.123  19.174  44.420  1.00 23.95           O  
ATOM   2663  CB  PRO A 347      38.016  17.272  46.155  1.00 24.31           C  
ATOM   2664  CG  PRO A 347      39.516  17.169  45.972  1.00 25.12           C  
ATOM   2665  CD  PRO A 347      39.757  18.043  44.779  1.00 25.35           C  
ATOM   2666  N   LYS A 348      35.057  17.182  44.649  1.00 23.60           N  
ATOM   2667  CA  LYS A 348      33.717  17.732  44.554  1.00 23.40           C  
ATOM   2668  C   LYS A 348      33.369  18.371  45.887  1.00 21.54           C  
ATOM   2669  O   LYS A 348      33.728  17.859  46.942  1.00 21.35           O  
ATOM   2670  CB  LYS A 348      32.711  16.632  44.216  1.00 26.48           C  
ATOM   2671  CG  LYS A 348      32.979  16.000  42.866  1.00 30.93           C  
ATOM   2672  CD  LYS A 348      31.903  15.013  42.469  1.00 33.58           C  
ATOM   2673  CE  LYS A 348      32.119  14.585  41.033  1.00 36.01           C  
ATOM   2674  NZ  LYS A 348      32.335  15.808  40.201  1.00 35.67           N  
ATOM   2675  N   VAL A 349      32.670  19.495  45.834  1.00 18.30           N  
ATOM   2676  CA  VAL A 349      32.319  20.205  47.047  1.00 16.31           C  
ATOM   2677  C   VAL A 349      30.920  20.809  46.981  1.00 15.20           C  
ATOM   2678  O   VAL A 349      30.307  20.904  45.925  1.00 13.82           O  
ATOM   2679  CB  VAL A 349      33.293  21.362  47.295  1.00 15.31           C  
ATOM   2680  CG1 VAL A 349      34.716  20.842  47.343  1.00 12.50           C  
ATOM   2681  CG2 VAL A 349      33.147  22.419  46.184  1.00 14.60           C  
ATOM   2682  N   TYR A 350      30.432  21.206  48.140  1.00 15.72           N  
ATOM   2683  CA  TYR A 350      29.154  21.870  48.244  1.00 17.27           C  
ATOM   2684  C   TYR A 350      29.550  23.278  48.677  1.00 17.64           C  
ATOM   2685  O   TYR A 350      30.494  23.446  49.454  1.00 16.54           O  
ATOM   2686  CB  TYR A 350      28.277  21.231  49.328  1.00 18.23           C  
ATOM   2687  CG  TYR A 350      27.684  19.881  48.957  1.00 20.66           C  
ATOM   2688  CD1 TYR A 350      27.641  18.841  49.888  1.00 22.71           C  
ATOM   2689  CD2 TYR A 350      27.132  19.655  47.693  1.00 19.80           C  
ATOM   2690  CE1 TYR A 350      27.064  17.607  49.576  1.00 23.38           C  
ATOM   2691  CE2 TYR A 350      26.550  18.428  47.372  1.00 24.09           C  
ATOM   2692  CZ  TYR A 350      26.520  17.405  48.326  1.00 24.18           C  
ATOM   2693  OH  TYR A 350      25.940  16.186  48.031  1.00 26.00           O  
ATOM   2694  N   GLN A 351      28.869  24.283  48.142  1.00 17.44           N  
ATOM   2695  CA  GLN A 351      29.122  25.666  48.528  1.00 17.79           C  
ATOM   2696  C   GLN A 351      27.755  26.139  48.960  1.00 18.43           C  
ATOM   2697  O   GLN A 351      26.860  26.297  48.128  1.00 20.33           O  
ATOM   2698  CB  GLN A 351      29.636  26.485  47.335  1.00 17.88           C  
ATOM   2699  CG  GLN A 351      30.956  25.954  46.830  1.00 19.14           C  
ATOM   2700  CD  GLN A 351      31.568  26.746  45.692  1.00 19.96           C  
ATOM   2701  OE1 GLN A 351      31.212  27.903  45.431  1.00 21.69           O  
ATOM   2702  NE2 GLN A 351      32.520  26.128  45.022  1.00 19.02           N  
ATOM   2703  N   LEU A 352      27.588  26.323  50.265  1.00 16.99           N  
ATOM   2704  CA  LEU A 352      26.313  26.765  50.821  1.00 17.44           C  
ATOM   2705  C   LEU A 352      26.093  28.262  50.612  1.00 17.92           C  
ATOM   2706  O   LEU A 352      26.966  29.080  50.912  1.00 17.27           O  
ATOM   2707  CB  LEU A 352      26.255  26.415  52.303  1.00 14.33           C  
ATOM   2708  CG  LEU A 352      26.760  24.994  52.552  1.00 15.76           C  
ATOM   2709  CD1 LEU A 352      26.565  24.616  54.015  1.00 13.57           C  
ATOM   2710  CD2 LEU A 352      26.003  24.033  51.636  1.00 15.37           C  
ATOM   2711  N   GLU A 353      24.919  28.605  50.091  1.00 17.94           N  
ATOM   2712  CA  GLU A 353      24.585  29.988  49.806  1.00 17.39           C  
ATOM   2713  C   GLU A 353      23.140  30.251  50.123  1.00 16.08           C  
ATOM   2714  O   GLU A 353      22.358  29.331  50.356  1.00 14.84           O  
ATOM   2715  CB  GLU A 353      24.795  30.294  48.323  1.00 19.34           C  
ATOM   2716  CG  GLU A 353      25.904  29.492  47.671  1.00 24.56           C  
ATOM   2717  CD  GLU A 353      25.888  29.599  46.159  1.00 25.15           C  
ATOM   2718  OE1 GLU A 353      24.779  29.584  45.581  1.00 27.03           O  
ATOM   2719  OE2 GLU A 353      26.980  29.680  45.553  1.00 25.42           O  
ATOM   2720  N   THR A 354      22.787  31.529  50.118  1.00 15.14           N  
ATOM   2721  CA  THR A 354      21.412  31.934  50.346  1.00 13.90           C  
ATOM   2722  C   THR A 354      21.151  33.127  49.437  1.00 13.96           C  
ATOM   2723  O   THR A 354      22.070  33.834  49.044  1.00 14.68           O  
ATOM   2724  CB  THR A 354      21.161  32.330  51.817  1.00 13.30           C  
ATOM   2725  OG1 THR A 354      22.036  33.404  52.198  1.00 15.60           O  
ATOM   2726  CG2 THR A 354      21.388  31.129  52.728  1.00 11.90           C  
ATOM   2727  N   ALA A 355      19.896  33.332  49.085  1.00 12.60           N  
ATOM   2728  CA  ALA A 355      19.527  34.439  48.239  1.00 13.07           C  
ATOM   2729  C   ALA A 355      18.799  35.485  49.108  1.00 14.46           C  
ATOM   2730  O   ALA A 355      17.932  35.158  49.921  1.00 15.77           O  
ATOM   2731  CB  ALA A 355      18.615  33.958  47.121  1.00 12.36           C  
HETATM 2732  N   MSE A 356      19.182  36.737  48.927  1.00 13.89           N  
HETATM 2733  CA  MSE A 356      18.618  37.890  49.624  1.00 14.34           C  
HETATM 2734  C   MSE A 356      17.089  37.928  49.657  1.00 14.17           C  
HETATM 2735  O   MSE A 356      16.493  38.257  50.685  1.00 14.73           O  
HETATM 2736  CB  MSE A 356      19.139  39.147  48.947  1.00 16.30           C  
HETATM 2737  CG  MSE A 356      18.625  40.390  49.529  1.00 21.87           C  
HETATM 2738 SE   MSE A 356      19.588  41.739  48.599  1.00 19.82          SE  
HETATM 2739  CE  MSE A 356      18.434  41.994  47.054  1.00 13.88           C  
ATOM   2740  N   GLY A 357      16.454  37.574  48.545  1.00 12.54           N  
ATOM   2741  CA  GLY A 357      15.003  37.605  48.500  1.00 13.22           C  
ATOM   2742  C   GLY A 357      14.281  36.569  49.350  1.00 15.08           C  
ATOM   2743  O   GLY A 357      13.104  36.736  49.665  1.00 14.23           O  
ATOM   2744  N   ALA A 358      14.985  35.504  49.727  1.00 14.16           N  
ATOM   2745  CA  ALA A 358      14.396  34.454  50.538  1.00 15.55           C  
ATOM   2746  C   ALA A 358      13.898  35.011  51.869  1.00 15.83           C  
ATOM   2747  O   ALA A 358      13.089  34.375  52.544  1.00 18.21           O  
ATOM   2748  CB  ALA A 358      15.428  33.324  50.783  1.00 11.11           C  
ATOM   2749  N   ALA A 359      14.376  36.193  52.249  1.00 15.30           N  
ATOM   2750  CA  ALA A 359      13.962  36.814  53.511  1.00 14.70           C  
ATOM   2751  C   ALA A 359      12.465  37.114  53.542  1.00 13.86           C  
ATOM   2752  O   ALA A 359      11.895  37.289  54.603  1.00 13.88           O  
ATOM   2753  CB  ALA A 359      14.764  38.107  53.756  1.00 13.90           C  
ATOM   2754  N   ILE A 360      11.830  37.151  52.375  1.00 15.66           N  
ATOM   2755  CA  ILE A 360      10.393  37.425  52.290  1.00 15.22           C  
ATOM   2756  C   ILE A 360       9.571  36.450  53.123  1.00 15.36           C  
ATOM   2757  O   ILE A 360       8.409  36.718  53.447  1.00 14.55           O  
ATOM   2758  CB  ILE A 360       9.885  37.367  50.820  1.00 14.07           C  
ATOM   2759  CG1 ILE A 360       8.486  37.988  50.723  1.00 13.64           C  
ATOM   2760  CG2 ILE A 360       9.845  35.912  50.327  1.00 13.03           C  
ATOM   2761  CD1 ILE A 360       7.980  38.118  49.284  1.00 10.39           C  
ATOM   2762  N   ALA A 361      10.174  35.318  53.471  1.00 16.06           N  
ATOM   2763  CA  ALA A 361       9.487  34.307  54.266  1.00 19.23           C  
ATOM   2764  C   ALA A 361       9.759  34.543  55.737  1.00 19.96           C  
ATOM   2765  O   ALA A 361       9.163  33.889  56.565  1.00 20.18           O  
ATOM   2766  CB  ALA A 361       9.981  32.886  53.889  1.00 17.59           C  
HETATM 2767  N   MSE A 362      10.645  35.473  56.072  1.00 21.60           N  
HETATM 2768  CA  MSE A 362      10.973  35.661  57.477  1.00 23.84           C  
HETATM 2769  C   MSE A 362      10.263  36.700  58.314  1.00 22.82           C  
HETATM 2770  O   MSE A 362      10.565  36.843  59.482  1.00 20.89           O  
HETATM 2771  CB  MSE A 362      12.444  35.931  57.642  1.00 26.17           C  
HETATM 2772  CG  MSE A 362      13.031  35.072  58.723  1.00 34.10           C  
HETATM 2773 SE   MSE A 362      13.989  33.693  57.757  1.00 38.66          SE  
HETATM 2774  CE  MSE A 362      12.475  32.636  57.261  1.00 34.74           C  
ATOM   2775  N   PHE A 363       9.349  37.448  57.735  1.00 22.73           N  
ATOM   2776  CA  PHE A 363       8.657  38.458  58.510  1.00 22.34           C  
ATOM   2777  C   PHE A 363       7.163  38.277  58.343  1.00 23.00           C  
ATOM   2778  O   PHE A 363       6.675  38.097  57.234  1.00 22.49           O  
ATOM   2779  CB  PHE A 363       9.063  39.856  58.048  1.00 18.85           C  
ATOM   2780  CG  PHE A 363      10.535  40.100  58.079  1.00 18.76           C  
ATOM   2781  CD1 PHE A 363      11.309  39.914  56.933  1.00 15.97           C  
ATOM   2782  CD2 PHE A 363      11.154  40.524  59.253  1.00 18.57           C  
ATOM   2783  CE1 PHE A 363      12.667  40.151  56.952  1.00 15.21           C  
ATOM   2784  CE2 PHE A 363      12.519  40.759  59.283  1.00 17.42           C  
ATOM   2785  CZ  PHE A 363      13.278  40.571  58.120  1.00 15.95           C  
ATOM   2786  N   GLU A 364       6.447  38.316  59.455  1.00 25.32           N  
ATOM   2787  CA  GLU A 364       5.000  38.172  59.432  1.00 27.55           C  
ATOM   2788  C   GLU A 364       4.348  39.119  58.419  1.00 26.04           C  
ATOM   2789  O   GLU A 364       3.453  38.719  57.683  1.00 28.13           O  
ATOM   2790  CB  GLU A 364       4.433  38.438  60.838  1.00 30.70           C  
ATOM   2791  CG  GLU A 364       2.903  38.552  60.918  1.00 37.05           C  
ATOM   2792  CD  GLU A 364       2.175  37.215  60.749  1.00 42.58           C  
ATOM   2793  OE1 GLU A 364       0.924  37.235  60.645  1.00 43.71           O  
ATOM   2794  OE2 GLU A 364       2.842  36.147  60.726  1.00 45.82           O  
ATOM   2795  N   SER A 365       4.813  40.364  58.353  1.00 24.81           N  
ATOM   2796  CA  SER A 365       4.205  41.338  57.444  1.00 24.29           C  
ATOM   2797  C   SER A 365       4.916  41.525  56.110  1.00 22.96           C  
ATOM   2798  O   SER A 365       4.773  42.564  55.463  1.00 25.62           O  
ATOM   2799  CB  SER A 365       4.098  42.705  58.120  1.00 20.55           C  
ATOM   2800  OG  SER A 365       5.358  43.350  58.064  1.00 24.13           O  
ATOM   2801  N   ALA A 366       5.682  40.531  55.694  1.00 22.50           N  
ATOM   2802  CA  ALA A 366       6.387  40.631  54.427  1.00 20.84           C  
ATOM   2803  C   ALA A 366       5.367  40.607  53.286  1.00 21.27           C  
ATOM   2804  O   ALA A 366       4.250  40.095  53.433  1.00 19.85           O  
ATOM   2805  CB  ALA A 366       7.363  39.482  54.293  1.00 19.63           C  
ATOM   2806  N   SER A 367       5.736  41.190  52.153  1.00 20.38           N  
ATOM   2807  CA  SER A 367       4.838  41.181  51.008  1.00 19.95           C  
ATOM   2808  C   SER A 367       5.622  41.467  49.743  1.00 18.87           C  
ATOM   2809  O   SER A 367       6.837  41.687  49.790  1.00 16.39           O  
ATOM   2810  CB  SER A 367       3.721  42.220  51.186  1.00 21.43           C  
ATOM   2811  OG  SER A 367       2.604  41.922  50.354  1.00 24.04           O  
ATOM   2812  N   ALA A 368       4.918  41.432  48.616  1.00 18.90           N  
ATOM   2813  CA  ALA A 368       5.503  41.697  47.305  1.00 18.72           C  
ATOM   2814  C   ALA A 368       4.603  42.700  46.607  1.00 19.34           C  
ATOM   2815  O   ALA A 368       3.444  42.857  46.977  1.00 20.45           O  
ATOM   2816  CB  ALA A 368       5.576  40.420  46.480  1.00 16.71           C  
ATOM   2817  N   ILE A 369       5.132  43.381  45.602  1.00 19.52           N  
ATOM   2818  CA  ILE A 369       4.340  44.349  44.870  1.00 20.13           C  
ATOM   2819  C   ILE A 369       4.744  44.261  43.406  1.00 19.65           C  
ATOM   2820  O   ILE A 369       5.933  44.184  43.094  1.00 18.52           O  
ATOM   2821  CB  ILE A 369       4.598  45.772  45.415  1.00 22.81           C  
ATOM   2822  CG1 ILE A 369       3.613  46.762  44.807  1.00 24.02           C  
ATOM   2823  CG2 ILE A 369       6.015  46.197  45.106  1.00 20.33           C  
ATOM   2824  CD1 ILE A 369       3.747  48.172  45.360  1.00 25.05           C  
ATOM   2825  N   VAL A 370       3.763  44.239  42.507  1.00 18.92           N  
ATOM   2826  CA  VAL A 370       4.079  44.173  41.087  1.00 17.53           C  
ATOM   2827  C   VAL A 370       4.526  45.563  40.660  1.00 16.26           C  
ATOM   2828  O   VAL A 370       3.844  46.538  40.958  1.00 17.89           O  
ATOM   2829  CB  VAL A 370       2.848  43.765  40.227  1.00 18.35           C  
ATOM   2830  CG1 VAL A 370       3.292  43.481  38.807  1.00 18.51           C  
ATOM   2831  CG2 VAL A 370       2.162  42.531  40.802  1.00 18.63           C  
ATOM   2832  N   VAL A 371       5.674  45.658  39.989  1.00 15.39           N  
ATOM   2833  CA  VAL A 371       6.191  46.941  39.513  1.00 14.08           C  
ATOM   2834  C   VAL A 371       6.344  46.902  37.991  1.00 17.18           C  
ATOM   2835  O   VAL A 371       6.463  45.818  37.392  1.00 17.28           O  
ATOM   2836  CB  VAL A 371       7.576  47.285  40.140  1.00 13.21           C  
ATOM   2837  CG1 VAL A 371       7.476  47.267  41.665  1.00 14.84           C  
ATOM   2838  CG2 VAL A 371       8.639  46.306  39.681  1.00 11.22           C  
ATOM   2839  N   PRO A 372       6.312  48.076  37.334  1.00 17.45           N  
ATOM   2840  CA  PRO A 372       6.461  48.077  35.873  1.00 19.17           C  
ATOM   2841  C   PRO A 372       7.842  47.556  35.492  1.00 19.22           C  
ATOM   2842  O   PRO A 372       8.737  47.505  36.330  1.00 19.55           O  
ATOM   2843  CB  PRO A 372       6.257  49.547  35.494  1.00 19.59           C  
ATOM   2844  CG  PRO A 372       6.662  50.291  36.750  1.00 20.97           C  
ATOM   2845  CD  PRO A 372       6.086  49.436  37.851  1.00 19.48           C  
ATOM   2846  N   ARG A 373       8.007  47.163  34.235  1.00 18.44           N  
ATOM   2847  CA  ARG A 373       9.284  46.630  33.754  1.00 17.81           C  
ATOM   2848  C   ARG A 373      10.429  47.657  33.769  1.00 16.68           C  
ATOM   2849  O   ARG A 373      11.601  47.285  33.743  1.00 16.30           O  
ATOM   2850  CB  ARG A 373       9.103  46.083  32.333  1.00 20.50           C  
ATOM   2851  CG  ARG A 373      10.305  45.313  31.776  1.00 23.24           C  
ATOM   2852  CD  ARG A 373      10.333  43.899  32.302  1.00 23.14           C  
ATOM   2853  NE  ARG A 373      11.541  43.180  31.918  1.00 23.34           N  
ATOM   2854  CZ  ARG A 373      11.752  41.901  32.201  1.00 25.33           C  
ATOM   2855  NH1 ARG A 373      10.824  41.210  32.864  1.00 24.05           N  
ATOM   2856  NH2 ARG A 373      12.889  41.319  31.841  1.00 24.51           N  
ATOM   2857  N   SER A 374      10.092  48.942  33.809  1.00 15.86           N  
ATOM   2858  CA  SER A 374      11.102  50.003  33.821  1.00 16.73           C  
ATOM   2859  C   SER A 374      12.029  49.951  35.039  1.00 16.99           C  
ATOM   2860  O   SER A 374      13.118  50.524  35.014  1.00 17.70           O  
ATOM   2861  CB  SER A 374      10.426  51.388  33.758  1.00 17.98           C  
ATOM   2862  OG  SER A 374       9.540  51.580  34.847  1.00 19.55           O  
ATOM   2863  N   ARG A 375      11.599  49.272  36.099  1.00 16.18           N  
ATOM   2864  CA  ARG A 375      12.410  49.146  37.314  1.00 16.88           C  
ATOM   2865  C   ARG A 375      13.252  47.859  37.273  1.00 17.73           C  
ATOM   2866  O   ARG A 375      13.860  47.477  38.275  1.00 17.59           O  
ATOM   2867  CB  ARG A 375      11.508  49.146  38.570  1.00 13.77           C  
ATOM   2868  CG  ARG A 375      10.819  50.509  38.851  1.00 16.65           C  
ATOM   2869  CD  ARG A 375       9.972  50.521  40.140  1.00 15.55           C  
ATOM   2870  NE  ARG A 375      10.777  50.236  41.330  1.00 15.66           N  
ATOM   2871  CZ  ARG A 375      11.632  51.090  41.888  1.00 17.76           C  
ATOM   2872  NH1 ARG A 375      11.800  52.313  41.378  1.00 16.56           N  
ATOM   2873  NH2 ARG A 375      12.345  50.710  42.942  1.00 15.01           N  
ATOM   2874  N   PHE A 376      13.290  47.199  36.115  1.00 17.42           N  
ATOM   2875  CA  PHE A 376      14.056  45.960  35.976  1.00 16.42           C  
ATOM   2876  C   PHE A 376      14.713  45.791  34.594  1.00 17.08           C  
ATOM   2877  O   PHE A 376      14.060  45.400  33.629  1.00 16.71           O  
ATOM   2878  CB  PHE A 376      13.129  44.778  36.275  1.00 16.25           C  
ATOM   2879  CG  PHE A 376      13.826  43.446  36.360  1.00 16.75           C  
ATOM   2880  CD1 PHE A 376      14.933  43.271  37.174  1.00 14.84           C  
ATOM   2881  CD2 PHE A 376      13.359  42.359  35.632  1.00 16.72           C  
ATOM   2882  CE1 PHE A 376      15.570  42.041  37.263  1.00 12.26           C  
ATOM   2883  CE2 PHE A 376      13.994  41.117  35.715  1.00 17.92           C  
ATOM   2884  CZ  PHE A 376      15.106  40.962  36.535  1.00 15.83           C  
ATOM   2885  N   ALA A 377      16.004  46.109  34.507  1.00 16.58           N  
ATOM   2886  CA  ALA A 377      16.784  45.955  33.273  1.00 15.84           C  
ATOM   2887  C   ALA A 377      17.958  45.045  33.662  1.00 15.18           C  
ATOM   2888  O   ALA A 377      19.071  45.512  33.863  1.00 14.64           O  
ATOM   2889  CB  ALA A 377      17.306  47.315  32.809  1.00 17.37           C  
ATOM   2890  N   PRO A 378      17.719  43.729  33.769  1.00 15.63           N  
ATOM   2891  CA  PRO A 378      18.779  42.783  34.156  1.00 16.92           C  
ATOM   2892  C   PRO A 378      19.891  42.489  33.152  1.00 17.94           C  
ATOM   2893  O   PRO A 378      19.694  42.557  31.941  1.00 19.25           O  
ATOM   2894  CB  PRO A 378      17.993  41.513  34.506  1.00 16.54           C  
ATOM   2895  CG  PRO A 378      16.859  41.549  33.484  1.00 14.46           C  
ATOM   2896  CD  PRO A 378      16.431  43.028  33.569  1.00 17.09           C  
ATOM   2897  N   VAL A 379      21.066  42.157  33.675  1.00 18.25           N  
ATOM   2898  CA  VAL A 379      22.203  41.785  32.845  1.00 16.20           C  
ATOM   2899  C   VAL A 379      22.860  40.554  33.463  1.00 16.97           C  
ATOM   2900  O   VAL A 379      23.803  40.683  34.239  1.00 18.63           O  
ATOM   2901  CB  VAL A 379      23.253  42.907  32.752  1.00 16.29           C  
ATOM   2902  CG1 VAL A 379      24.475  42.402  31.978  1.00 16.12           C  
ATOM   2903  CG2 VAL A 379      22.668  44.130  32.050  1.00 15.68           C  
ATOM   2904  N   LYS A 380      22.342  39.372  33.131  1.00 17.01           N  
ATOM   2905  CA  LYS A 380      22.876  38.094  33.626  1.00 19.88           C  
ATOM   2906  C   LYS A 380      23.755  37.392  32.584  1.00 21.59           C  
ATOM   2907  O   LYS A 380      24.585  36.551  32.928  1.00 24.28           O  
ATOM   2908  CB  LYS A 380      21.743  37.124  33.994  1.00 19.26           C  
ATOM   2909  CG  LYS A 380      20.707  37.701  34.928  1.00 22.46           C  
ATOM   2910  CD  LYS A 380      21.376  38.229  36.170  1.00 22.95           C  
ATOM   2911  CE  LYS A 380      20.463  39.161  36.917  1.00 23.16           C  
ATOM   2912  NZ  LYS A 380      21.133  39.715  38.120  1.00 22.75           N  
ATOM   2913  N   THR A 381      23.555  37.723  31.311  1.00 22.14           N  
ATOM   2914  CA  THR A 381      24.307  37.092  30.229  1.00 21.97           C  
ATOM   2915  C   THR A 381      24.793  38.152  29.252  1.00 21.82           C  
ATOM   2916  O   THR A 381      24.443  39.316  29.381  1.00 22.16           O  
ATOM   2917  CB  THR A 381      23.407  36.124  29.443  1.00 20.94           C  
ATOM   2918  OG1 THR A 381      22.355  36.871  28.817  1.00 20.28           O  
ATOM   2919  CG2 THR A 381      22.792  35.083  30.368  1.00 18.40           C  
ATOM   2920  N   CYS A 382      25.604  37.754  28.279  1.00 21.41           N  
ATOM   2921  CA  CYS A 382      26.072  38.711  27.277  1.00 22.01           C  
ATOM   2922  C   CYS A 382      24.882  39.070  26.384  1.00 19.58           C  
ATOM   2923  O   CYS A 382      24.837  40.133  25.791  1.00 18.87           O  
ATOM   2924  CB  CYS A 382      27.207  38.110  26.444  1.00 20.78           C  
ATOM   2925  SG  CYS A 382      28.752  37.930  27.367  1.00 27.49           S  
ATOM   2926  N   ALA A 383      23.922  38.157  26.297  1.00 20.05           N  
ATOM   2927  CA  ALA A 383      22.713  38.370  25.503  1.00 20.42           C  
ATOM   2928  C   ALA A 383      21.939  39.565  26.086  1.00 20.14           C  
ATOM   2929  O   ALA A 383      21.415  40.398  25.346  1.00 20.16           O  
ATOM   2930  CB  ALA A 383      21.857  37.104  25.532  1.00 19.15           C  
ATOM   2931  N   ASP A 384      21.878  39.636  27.419  1.00 18.92           N  
ATOM   2932  CA  ASP A 384      21.210  40.729  28.107  1.00 18.99           C  
ATOM   2933  C   ASP A 384      22.046  41.994  27.923  1.00 18.34           C  
ATOM   2934  O   ASP A 384      21.513  43.097  27.779  1.00 18.18           O  
ATOM   2935  CB  ASP A 384      21.072  40.440  29.608  1.00 20.48           C  
ATOM   2936  CG  ASP A 384      20.104  39.305  29.908  1.00 24.79           C  
ATOM   2937  OD1 ASP A 384      19.218  39.023  29.071  1.00 28.42           O  
ATOM   2938  OD2 ASP A 384      20.212  38.703  30.998  1.00 25.09           O  
ATOM   2939  N   LEU A 385      23.363  41.835  27.924  1.00 17.40           N  
ATOM   2940  CA  LEU A 385      24.236  42.982  27.765  1.00 18.34           C  
ATOM   2941  C   LEU A 385      24.035  43.621  26.399  1.00 20.20           C  
ATOM   2942  O   LEU A 385      24.076  44.851  26.262  1.00 21.91           O  
ATOM   2943  CB  LEU A 385      25.692  42.570  27.951  1.00 17.54           C  
ATOM   2944  CG  LEU A 385      26.697  43.721  27.853  1.00 15.91           C  
ATOM   2945  CD1 LEU A 385      26.326  44.842  28.810  1.00 11.12           C  
ATOM   2946  CD2 LEU A 385      28.077  43.185  28.182  1.00 13.67           C  
ATOM   2947  N   LEU A 386      23.811  42.787  25.390  1.00 20.34           N  
ATOM   2948  CA  LEU A 386      23.576  43.283  24.038  1.00 22.10           C  
ATOM   2949  C   LEU A 386      22.335  44.182  24.055  1.00 22.49           C  
ATOM   2950  O   LEU A 386      22.337  45.290  23.525  1.00 23.37           O  
ATOM   2951  CB  LEU A 386      23.312  42.118  23.080  1.00 21.71           C  
ATOM   2952  CG  LEU A 386      23.686  42.331  21.608  1.00 22.29           C  
ATOM   2953  CD1 LEU A 386      22.905  41.351  20.765  1.00 21.57           C  
ATOM   2954  CD2 LEU A 386      23.400  43.760  21.170  1.00 23.09           C  
ATOM   2955  N   ALA A 387      21.268  43.679  24.667  1.00 22.43           N  
ATOM   2956  CA  ALA A 387      20.022  44.423  24.743  1.00 21.43           C  
ATOM   2957  C   ALA A 387      20.231  45.755  25.437  1.00 21.05           C  
ATOM   2958  O   ALA A 387      19.793  46.784  24.940  1.00 21.69           O  
ATOM   2959  CB  ALA A 387      18.961  43.605  25.478  1.00 20.46           C  
ATOM   2960  N   LEU A 388      20.908  45.732  26.582  1.00 21.83           N  
ATOM   2961  CA  LEU A 388      21.167  46.946  27.350  1.00 22.66           C  
ATOM   2962  C   LEU A 388      21.984  47.955  26.548  1.00 22.64           C  
ATOM   2963  O   LEU A 388      21.758  49.164  26.627  1.00 22.54           O  
ATOM   2964  CB  LEU A 388      21.928  46.608  28.639  1.00 24.71           C  
ATOM   2965  CG  LEU A 388      21.398  47.092  29.997  1.00 26.80           C  
ATOM   2966  CD1 LEU A 388      22.595  47.436  30.849  1.00 27.54           C  
ATOM   2967  CD2 LEU A 388      20.486  48.321  29.882  1.00 27.42           C  
ATOM   2968  N   ARG A 389      22.940  47.457  25.778  1.00 23.56           N  
ATOM   2969  CA  ARG A 389      23.774  48.343  24.980  1.00 26.16           C  
ATOM   2970  C   ARG A 389      23.069  48.932  23.760  1.00 25.39           C  
ATOM   2971  O   ARG A 389      23.341  50.072  23.388  1.00 23.90           O  
ATOM   2972  CB  ARG A 389      25.051  47.618  24.538  1.00 26.67           C  
ATOM   2973  CG  ARG A 389      26.011  47.337  25.690  1.00 27.20           C  
ATOM   2974  CD  ARG A 389      27.388  46.901  25.191  1.00 29.45           C  
ATOM   2975  NE  ARG A 389      28.329  46.701  26.292  1.00 28.64           N  
ATOM   2976  CZ  ARG A 389      29.587  46.294  26.147  1.00 29.97           C  
ATOM   2977  NH1 ARG A 389      30.075  46.035  24.940  1.00 30.49           N  
ATOM   2978  NH2 ARG A 389      30.359  46.148  27.215  1.00 32.00           N  
ATOM   2979  N   SER A 390      22.165  48.165  23.150  1.00 25.64           N  
ATOM   2980  CA  SER A 390      21.448  48.630  21.959  1.00 25.78           C  
ATOM   2981  C   SER A 390      20.525  49.790  22.292  1.00 27.69           C  
ATOM   2982  O   SER A 390      20.278  50.080  23.467  1.00 29.01           O  
ATOM   2983  CB  SER A 390      20.623  47.499  21.347  1.00 26.63           C  
ATOM   2984  OG  SER A 390      19.506  47.188  22.158  1.00 25.55           O  
ATOM   2985  N   ASP A 391      20.004  50.451  21.263  1.00 28.15           N  
ATOM   2986  CA  ASP A 391      19.129  51.587  21.490  1.00 29.38           C  
ATOM   2987  C   ASP A 391      17.820  51.166  22.138  1.00 29.89           C  
ATOM   2988  O   ASP A 391      16.996  52.010  22.479  1.00 31.24           O  
ATOM   2989  CB  ASP A 391      18.877  52.366  20.182  1.00 30.71           C  
ATOM   2990  CG  ASP A 391      18.207  51.529  19.095  1.00 30.01           C  
ATOM   2991  OD1 ASP A 391      17.840  50.360  19.343  1.00 30.74           O  
ATOM   2992  OD2 ASP A 391      18.043  52.060  17.974  1.00 31.76           O  
ATOM   2993  N   ALA A 392      17.628  49.862  22.322  1.00 29.92           N  
ATOM   2994  CA  ALA A 392      16.415  49.377  22.969  1.00 29.19           C  
ATOM   2995  C   ALA A 392      16.276  50.029  24.352  1.00 29.31           C  
ATOM   2996  O   ALA A 392      15.165  50.342  24.782  1.00 30.04           O  
ATOM   2997  CB  ALA A 392      16.447  47.858  23.097  1.00 30.38           C  
ATOM   2998  N   TYR A 393      17.396  50.236  25.046  1.00 27.71           N  
ATOM   2999  CA  TYR A 393      17.367  50.878  26.367  1.00 27.15           C  
ATOM   3000  C   TYR A 393      17.810  52.329  26.309  1.00 26.73           C  
ATOM   3001  O   TYR A 393      18.760  52.668  25.604  1.00 26.87           O  
ATOM   3002  CB  TYR A 393      18.242  50.130  27.378  1.00 23.55           C  
ATOM   3003  CG  TYR A 393      17.572  48.893  27.928  1.00 20.97           C  
ATOM   3004  CD1 TYR A 393      17.576  47.704  27.214  1.00 20.77           C  
ATOM   3005  CD2 TYR A 393      16.902  48.925  29.139  1.00 18.16           C  
ATOM   3006  CE1 TYR A 393      16.925  46.578  27.692  1.00 20.02           C  
ATOM   3007  CE2 TYR A 393      16.253  47.809  29.627  1.00 17.77           C  
ATOM   3008  CZ  TYR A 393      16.262  46.637  28.900  1.00 18.80           C  
ATOM   3009  OH  TYR A 393      15.577  45.529  29.356  1.00 19.41           O  
ATOM   3010  N   VAL A 394      17.133  53.180  27.073  1.00 26.14           N  
ATOM   3011  CA  VAL A 394      17.443  54.610  27.085  1.00 25.51           C  
ATOM   3012  C   VAL A 394      17.807  55.111  28.477  1.00 25.03           C  
ATOM   3013  O   VAL A 394      17.482  54.477  29.481  1.00 24.32           O  
ATOM   3014  CB  VAL A 394      16.231  55.438  26.556  1.00 24.26           C  
ATOM   3015  CG1 VAL A 394      15.924  55.044  25.105  1.00 25.47           C  
ATOM   3016  CG2 VAL A 394      15.004  55.180  27.430  1.00 21.69           C  
ATOM   3017  N   VAL A 395      18.480  56.256  28.523  1.00 25.40           N  
ATOM   3018  CA  VAL A 395      18.892  56.872  29.784  1.00 25.65           C  
ATOM   3019  C   VAL A 395      17.903  57.957  30.193  1.00 26.69           C  
ATOM   3020  O   VAL A 395      17.582  58.843  29.396  1.00 27.83           O  
ATOM   3021  CB  VAL A 395      20.270  57.537  29.661  1.00 25.37           C  
ATOM   3022  CG1 VAL A 395      20.690  58.073  31.010  1.00 26.71           C  
ATOM   3023  CG2 VAL A 395      21.291  56.550  29.135  1.00 24.25           C  
ATOM   3024  N   THR A 396      17.426  57.903  31.432  1.00 26.85           N  
ATOM   3025  CA  THR A 396      16.478  58.907  31.894  1.00 25.50           C  
ATOM   3026  C   THR A 396      17.250  60.042  32.538  1.00 24.82           C  
ATOM   3027  O   THR A 396      18.478  59.988  32.633  1.00 23.34           O  
ATOM   3028  CB  THR A 396      15.481  58.326  32.913  1.00 26.35           C  
ATOM   3029  OG1 THR A 396      16.188  57.892  34.084  1.00 27.09           O  
ATOM   3030  CG2 THR A 396      14.722  57.149  32.296  1.00 24.04           C  
ATOM   3031  N   ASP A 397      16.530  61.078  32.952  1.00 24.54           N  
ATOM   3032  CA  ASP A 397      17.149  62.229  33.594  1.00 26.92           C  
ATOM   3033  C   ASP A 397      17.756  61.883  34.964  1.00 25.65           C  
ATOM   3034  O   ASP A 397      18.810  62.404  35.314  1.00 25.58           O  
ATOM   3035  CB  ASP A 397      16.126  63.354  33.729  1.00 30.82           C  
ATOM   3036  CG  ASP A 397      15.819  64.011  32.399  1.00 35.88           C  
ATOM   3037  OD1 ASP A 397      15.893  63.308  31.367  1.00 38.55           O  
ATOM   3038  OD2 ASP A 397      15.496  65.219  32.382  1.00 38.90           O  
ATOM   3039  N   ASP A 398      17.100  61.015  35.734  1.00 22.84           N  
ATOM   3040  CA  ASP A 398      17.641  60.617  37.028  1.00 24.70           C  
ATOM   3041  C   ASP A 398      18.621  59.450  36.862  1.00 25.00           C  
ATOM   3042  O   ASP A 398      18.950  58.741  37.815  1.00 26.49           O  
ATOM   3043  CB  ASP A 398      16.528  60.253  38.012  1.00 25.79           C  
ATOM   3044  CG  ASP A 398      15.521  59.286  37.430  1.00 27.95           C  
ATOM   3045  OD1 ASP A 398      14.744  58.725  38.228  1.00 28.25           O  
ATOM   3046  OD2 ASP A 398      15.498  59.095  36.190  1.00 32.26           O  
ATOM   3047  N   PHE A 399      19.069  59.277  35.619  1.00 23.71           N  
ATOM   3048  CA  PHE A 399      20.066  58.285  35.202  1.00 21.96           C  
ATOM   3049  C   PHE A 399      19.810  56.784  35.317  1.00 21.99           C  
ATOM   3050  O   PHE A 399      20.725  55.998  35.574  1.00 19.36           O  
ATOM   3051  CB  PHE A 399      21.405  58.629  35.843  1.00 21.71           C  
ATOM   3052  CG  PHE A 399      21.831  60.044  35.588  1.00 22.54           C  
ATOM   3053  CD1 PHE A 399      21.512  61.058  36.482  1.00 23.47           C  
ATOM   3054  CD2 PHE A 399      22.501  60.375  34.415  1.00 24.50           C  
ATOM   3055  CE1 PHE A 399      21.856  62.390  36.213  1.00 25.88           C  
ATOM   3056  CE2 PHE A 399      22.850  61.701  34.133  1.00 26.70           C  
ATOM   3057  CZ  PHE A 399      22.525  62.710  35.035  1.00 25.52           C  
ATOM   3058  N   ARG A 400      18.564  56.385  35.107  1.00 23.47           N  
ATOM   3059  CA  ARG A 400      18.227  54.983  35.119  1.00 24.07           C  
ATOM   3060  C   ARG A 400      18.175  54.522  33.667  1.00 25.03           C  
ATOM   3061  O   ARG A 400      17.926  55.317  32.754  1.00 25.27           O  
ATOM   3062  CB  ARG A 400      16.874  54.758  35.777  1.00 24.33           C  
ATOM   3063  CG  ARG A 400      16.799  55.275  37.179  1.00 24.96           C  
ATOM   3064  CD  ARG A 400      15.705  54.583  37.944  1.00 26.54           C  
ATOM   3065  NE  ARG A 400      14.495  54.441  37.155  1.00 25.79           N  
ATOM   3066  CZ  ARG A 400      13.848  55.458  36.612  1.00 27.89           C  
ATOM   3067  NH1 ARG A 400      14.313  56.684  36.789  1.00 26.46           N  
ATOM   3068  NH2 ARG A 400      12.754  55.244  35.886  1.00 24.80           N  
ATOM   3069  N   LEU A 401      18.433  53.239  33.459  1.00 24.44           N  
ATOM   3070  CA  LEU A 401      18.383  52.670  32.124  1.00 24.80           C  
ATOM   3071  C   LEU A 401      17.048  51.971  31.967  1.00 24.67           C  
ATOM   3072  O   LEU A 401      16.793  50.950  32.610  1.00 24.92           O  
ATOM   3073  CB  LEU A 401      19.525  51.674  31.916  1.00 24.23           C  
ATOM   3074  CG  LEU A 401      20.855  52.295  31.498  1.00 27.27           C  
ATOM   3075  CD1 LEU A 401      20.704  52.899  30.113  1.00 30.07           C  
ATOM   3076  CD2 LEU A 401      21.289  53.363  32.494  1.00 25.60           C  
ATOM   3077  N   VAL A 402      16.179  52.530  31.130  1.00 24.01           N  
ATOM   3078  CA  VAL A 402      14.879  51.914  30.922  1.00 24.11           C  
ATOM   3079  C   VAL A 402      14.621  51.599  29.462  1.00 23.93           C  
ATOM   3080  O   VAL A 402      15.170  52.221  28.557  1.00 20.91           O  
ATOM   3081  CB  VAL A 402      13.707  52.803  31.436  1.00 23.40           C  
ATOM   3082  CG1 VAL A 402      13.970  53.241  32.854  1.00 21.44           C  
ATOM   3083  CG2 VAL A 402      13.490  54.009  30.506  1.00 22.30           C  
ATOM   3084  N   LEU A 403      13.766  50.612  29.261  1.00 26.01           N  
ATOM   3085  CA  LEU A 403      13.382  50.166  27.942  1.00 27.38           C  
ATOM   3086  C   LEU A 403      12.763  51.361  27.224  1.00 28.71           C  
ATOM   3087  O   LEU A 403      12.159  52.231  27.851  1.00 28.06           O  
ATOM   3088  CB  LEU A 403      12.354  49.047  28.102  1.00 28.43           C  
ATOM   3089  CG  LEU A 403      12.315  47.783  27.252  1.00 30.99           C  
ATOM   3090  CD1 LEU A 403      13.702  47.214  27.041  1.00 29.74           C  
ATOM   3091  CD2 LEU A 403      11.429  46.777  27.972  1.00 29.43           C  
ATOM   3092  N   ASP A 404      12.928  51.410  25.909  1.00 30.84           N  
ATOM   3093  CA  ASP A 404      12.350  52.483  25.107  1.00 32.74           C  
ATOM   3094  C   ASP A 404      10.826  52.354  25.189  1.00 33.57           C  
ATOM   3095  O   ASP A 404      10.307  51.252  25.374  1.00 32.93           O  
ATOM   3096  CB  ASP A 404      12.817  52.356  23.652  1.00 33.41           C  
ATOM   3097  CG  ASP A 404      12.331  53.492  22.779  1.00 33.52           C  
ATOM   3098  OD1 ASP A 404      11.103  53.570  22.535  1.00 34.55           O  
ATOM   3099  OD2 ASP A 404      13.178  54.308  22.346  1.00 34.93           O  
ATOM   3100  N   ASP A 405      10.111  53.469  25.065  1.00 34.76           N  
ATOM   3101  CA  ASP A 405       8.647  53.443  25.135  1.00 37.65           C  
ATOM   3102  C   ASP A 405       8.029  52.571  24.045  1.00 37.65           C  
ATOM   3103  O   ASP A 405       6.982  51.952  24.249  1.00 38.10           O  
ATOM   3104  CB  ASP A 405       8.078  54.862  25.036  1.00 39.07           C  
ATOM   3105  CG  ASP A 405       8.432  55.719  26.239  1.00 40.80           C  
ATOM   3106  OD1 ASP A 405       8.222  55.260  27.383  1.00 40.47           O  
ATOM   3107  OD2 ASP A 405       8.912  56.855  26.039  1.00 43.71           O  
ATOM   3108  N   ARG A 406       8.688  52.508  22.896  1.00 38.33           N  
ATOM   3109  CA  ARG A 406       8.194  51.708  21.785  1.00 39.24           C  
ATOM   3110  C   ARG A 406       8.142  50.209  22.094  1.00 39.99           C  
ATOM   3111  O   ARG A 406       7.395  49.463  21.452  1.00 40.52           O  
ATOM   3112  CB  ARG A 406       9.068  51.939  20.553  1.00 40.01           C  
ATOM   3113  CG  ARG A 406       9.271  53.403  20.223  1.00 39.54           C  
ATOM   3114  CD  ARG A 406      10.003  53.574  18.909  1.00 40.23           C  
ATOM   3115  NE  ARG A 406      11.315  54.188  19.075  1.00 38.66           N  
ATOM   3116  CZ  ARG A 406      12.053  54.638  18.066  1.00 38.80           C  
ATOM   3117  NH1 ARG A 406      11.609  54.546  16.818  1.00 38.12           N  
ATOM   3118  NH2 ARG A 406      13.240  55.178  18.300  1.00 40.72           N  
ATOM   3119  N   CYS A 407       8.917  49.768  23.081  1.00 38.36           N  
ATOM   3120  CA  CYS A 407       8.955  48.352  23.433  1.00 36.93           C  
ATOM   3121  C   CYS A 407       7.749  47.826  24.209  1.00 36.42           C  
ATOM   3122  O   CYS A 407       7.498  46.611  24.233  1.00 34.87           O  
ATOM   3123  CB  CYS A 407      10.235  48.050  24.223  1.00 37.83           C  
ATOM   3124  SG  CYS A 407      11.768  48.337  23.302  1.00 35.93           S  
ATOM   3125  N   HIS A 408       7.010  48.734  24.845  1.00 36.81           N  
ATOM   3126  CA  HIS A 408       5.839  48.366  25.646  1.00 36.85           C  
ATOM   3127  C   HIS A 408       6.159  47.403  26.780  1.00 35.28           C  
ATOM   3128  O   HIS A 408       5.424  46.445  27.007  1.00 33.10           O  
ATOM   3129  CB  HIS A 408       4.758  47.756  24.757  1.00 40.26           C  
ATOM   3130  CG  HIS A 408       3.953  48.773  24.016  1.00 43.62           C  
ATOM   3131  ND1 HIS A 408       4.527  49.856  23.387  1.00 43.75           N  
ATOM   3132  CD2 HIS A 408       2.619  48.876  23.807  1.00 44.21           C  
ATOM   3133  CE1 HIS A 408       3.580  50.584  22.821  1.00 45.13           C  
ATOM   3134  NE2 HIS A 408       2.414  50.011  23.060  1.00 44.90           N  
ATOM   3135  N   GLY A 409       7.254  47.666  27.493  1.00 35.22           N  
ATOM   3136  CA  GLY A 409       7.652  46.805  28.600  1.00 34.78           C  
ATOM   3137  C   GLY A 409       8.151  45.447  28.132  1.00 35.13           C  
ATOM   3138  O   GLY A 409       8.352  44.528  28.934  1.00 34.39           O  
ATOM   3139  N   HIS A 410       8.353  45.322  26.823  1.00 35.10           N  
ATOM   3140  CA  HIS A 410       8.820  44.075  26.230  1.00 35.68           C  
ATOM   3141  C   HIS A 410      10.246  44.184  25.716  1.00 33.80           C  
ATOM   3142  O   HIS A 410      10.493  44.750  24.650  1.00 34.67           O  
ATOM   3143  CB  HIS A 410       7.887  43.666  25.088  1.00 38.26           C  
ATOM   3144  CG  HIS A 410       6.549  43.188  25.553  1.00 40.93           C  
ATOM   3145  ND1 HIS A 410       5.398  43.361  24.816  1.00 41.70           N  
ATOM   3146  CD2 HIS A 410       6.180  42.542  26.685  1.00 42.02           C  
ATOM   3147  CE1 HIS A 410       4.377  42.843  25.475  1.00 42.73           C  
ATOM   3148  NE2 HIS A 410       4.824  42.341  26.612  1.00 42.32           N  
ATOM   3149  N   PRO A 411      11.210  43.651  26.474  1.00 32.80           N  
ATOM   3150  CA  PRO A 411      12.598  43.728  26.018  1.00 32.57           C  
ATOM   3151  C   PRO A 411      12.829  42.738  24.873  1.00 32.00           C  
ATOM   3152  O   PRO A 411      12.172  41.702  24.795  1.00 30.89           O  
ATOM   3153  CB  PRO A 411      13.385  43.379  27.274  1.00 32.73           C  
ATOM   3154  CG  PRO A 411      12.470  42.393  27.970  1.00 32.66           C  
ATOM   3155  CD  PRO A 411      11.118  43.029  27.810  1.00 32.08           C  
ATOM   3156  N   PRO A 412      13.746  43.066  23.950  1.00 31.50           N  
ATOM   3157  CA  PRO A 412      14.049  42.189  22.816  1.00 30.89           C  
ATOM   3158  C   PRO A 412      14.466  40.802  23.282  1.00 30.29           C  
ATOM   3159  O   PRO A 412      15.255  40.669  24.209  1.00 32.22           O  
ATOM   3160  CB  PRO A 412      15.183  42.927  22.121  1.00 31.10           C  
ATOM   3161  CG  PRO A 412      14.825  44.359  22.366  1.00 31.00           C  
ATOM   3162  CD  PRO A 412      14.439  44.360  23.814  1.00 30.48           C  
ATOM   3163  N   VAL A 413      13.934  39.760  22.661  1.00 30.43           N  
ATOM   3164  CA  VAL A 413      14.321  38.416  23.065  1.00 29.95           C  
ATOM   3165  C   VAL A 413      15.586  38.042  22.303  1.00 31.84           C  
ATOM   3166  O   VAL A 413      15.541  37.653  21.136  1.00 32.16           O  
ATOM   3167  CB  VAL A 413      13.200  37.399  22.796  1.00 30.32           C  
ATOM   3168  CG1 VAL A 413      13.685  35.988  23.134  1.00 29.96           C  
ATOM   3169  CG2 VAL A 413      11.966  37.756  23.647  1.00 26.75           C  
ATOM   3170  N   VAL A 414      16.721  38.185  22.978  1.00 32.59           N  
ATOM   3171  CA  VAL A 414      18.017  37.901  22.380  1.00 32.75           C  
ATOM   3172  C   VAL A 414      18.511  36.498  22.668  1.00 33.58           C  
ATOM   3173  O   VAL A 414      18.409  36.016  23.799  1.00 35.78           O  
ATOM   3174  CB  VAL A 414      19.064  38.887  22.889  1.00 31.88           C  
ATOM   3175  CG1 VAL A 414      20.386  38.630  22.201  1.00 30.81           C  
ATOM   3176  CG2 VAL A 414      18.579  40.325  22.656  1.00 30.86           C  
ATOM   3177  N   ASP A 415      19.048  35.842  21.643  1.00 32.61           N  
ATOM   3178  CA  ASP A 415      19.571  34.488  21.804  1.00 32.58           C  
ATOM   3179  C   ASP A 415      20.852  34.338  20.999  1.00 30.62           C  
ATOM   3180  O   ASP A 415      20.832  34.281  19.770  1.00 29.45           O  
ATOM   3181  CB  ASP A 415      18.527  33.442  21.382  1.00 34.53           C  
ATOM   3182  CG  ASP A 415      19.091  32.020  21.341  1.00 38.10           C  
ATOM   3183  OD1 ASP A 415      20.048  31.708  22.091  1.00 40.49           O  
ATOM   3184  OD2 ASP A 415      18.564  31.197  20.562  1.00 39.97           O  
ATOM   3185  N   LEU A 416      21.970  34.282  21.714  1.00 29.60           N  
ATOM   3186  CA  LEU A 416      23.272  34.175  21.081  1.00 29.44           C  
ATOM   3187  C   LEU A 416      23.866  32.795  21.252  1.00 29.14           C  
ATOM   3188  O   LEU A 416      23.772  32.193  22.321  1.00 29.74           O  
ATOM   3189  CB  LEU A 416      24.217  35.222  21.671  1.00 28.95           C  
ATOM   3190  CG  LEU A 416      23.605  36.621  21.786  1.00 28.99           C  
ATOM   3191  CD1 LEU A 416      24.637  37.584  22.349  1.00 27.01           C  
ATOM   3192  CD2 LEU A 416      23.096  37.095  20.422  1.00 26.06           C  
ATOM   3193  N   ASP A 417      24.477  32.301  20.182  1.00 29.50           N  
ATOM   3194  CA  ASP A 417      25.111  30.986  20.184  1.00 28.55           C  
ATOM   3195  C   ASP A 417      26.063  30.887  21.384  1.00 28.36           C  
ATOM   3196  O   ASP A 417      27.043  31.622  21.475  1.00 27.17           O  
ATOM   3197  CB  ASP A 417      25.883  30.799  18.874  1.00 29.52           C  
ATOM   3198  CG  ASP A 417      26.380  29.381  18.681  1.00 29.36           C  
ATOM   3199  OD1 ASP A 417      27.092  28.868  19.570  1.00 29.98           O  
ATOM   3200  OD2 ASP A 417      26.061  28.785  17.630  1.00 30.34           O  
ATOM   3201  N   SER A 418      25.775  29.980  22.309  1.00 29.22           N  
ATOM   3202  CA  SER A 418      26.623  29.833  23.484  1.00 30.57           C  
ATOM   3203  C   SER A 418      28.085  29.502  23.149  1.00 30.93           C  
ATOM   3204  O   SER A 418      28.981  29.766  23.954  1.00 30.87           O  
ATOM   3205  CB  SER A 418      26.048  28.753  24.409  1.00 32.78           C  
ATOM   3206  OG  SER A 418      26.111  27.469  23.811  1.00 37.14           O  
ATOM   3207  N   ALA A 419      28.331  28.933  21.971  1.00 29.20           N  
ATOM   3208  CA  ALA A 419      29.691  28.562  21.591  1.00 29.64           C  
ATOM   3209  C   ALA A 419      30.567  29.745  21.199  1.00 28.36           C  
ATOM   3210  O   ALA A 419      31.792  29.661  21.270  1.00 28.67           O  
ATOM   3211  CB  ALA A 419      29.668  27.528  20.442  1.00 29.23           C  
ATOM   3212  N   HIS A 420      29.958  30.852  20.800  1.00 27.72           N  
ATOM   3213  CA  HIS A 420      30.751  32.010  20.389  1.00 26.80           C  
ATOM   3214  C   HIS A 420      30.517  33.275  21.195  1.00 27.54           C  
ATOM   3215  O   HIS A 420      31.369  34.160  21.214  1.00 27.38           O  
ATOM   3216  CB  HIS A 420      30.488  32.338  18.914  1.00 28.13           C  
ATOM   3217  CG  HIS A 420      30.835  31.228  17.976  1.00 29.88           C  
ATOM   3218  ND1 HIS A 420      29.994  30.161  17.744  1.00 32.06           N  
ATOM   3219  CD2 HIS A 420      31.957  30.987  17.259  1.00 30.07           C  
ATOM   3220  CE1 HIS A 420      30.585  29.308  16.926  1.00 31.98           C  
ATOM   3221  NE2 HIS A 420      31.779  29.785  16.618  1.00 31.11           N  
ATOM   3222  N   TYR A 421      29.379  33.374  21.869  1.00 27.02           N  
ATOM   3223  CA  TYR A 421      29.102  34.592  22.600  1.00 30.24           C  
ATOM   3224  C   TYR A 421      28.865  34.517  24.107  1.00 30.06           C  
ATOM   3225  O   TYR A 421      28.718  35.557  24.756  1.00 29.50           O  
ATOM   3226  CB  TYR A 421      27.929  35.298  21.924  1.00 32.08           C  
ATOM   3227  CG  TYR A 421      28.032  35.238  20.418  1.00 32.99           C  
ATOM   3228  CD1 TYR A 421      27.387  34.229  19.695  1.00 33.01           C  
ATOM   3229  CD2 TYR A 421      28.832  36.144  19.720  1.00 32.51           C  
ATOM   3230  CE1 TYR A 421      27.544  34.124  18.315  1.00 32.66           C  
ATOM   3231  CE2 TYR A 421      28.998  36.047  18.340  1.00 31.72           C  
ATOM   3232  CZ  TYR A 421      28.353  35.035  17.648  1.00 31.86           C  
ATOM   3233  OH  TYR A 421      28.531  34.912  16.294  1.00 32.68           O  
ATOM   3234  N   LYS A 422      28.839  33.315  24.675  1.00 30.45           N  
ATOM   3235  CA  LYS A 422      28.606  33.195  26.107  1.00 30.95           C  
ATOM   3236  C   LYS A 422      29.665  33.952  26.908  1.00 31.79           C  
ATOM   3237  O   LYS A 422      29.350  34.572  27.921  1.00 32.71           O  
ATOM   3238  CB  LYS A 422      28.582  31.728  26.525  1.00 30.72           C  
ATOM   3239  CG  LYS A 422      27.972  31.494  27.903  1.00 31.44           C  
ATOM   3240  CD  LYS A 422      28.084  30.027  28.301  1.00 34.36           C  
ATOM   3241  CE  LYS A 422      27.402  29.746  29.634  1.00 35.80           C  
ATOM   3242  NZ  LYS A 422      27.971  30.533  30.758  1.00 37.56           N  
HETATM 3243  N   MSE A 423      30.911  33.907  26.442  1.00 32.52           N  
HETATM 3244  CA  MSE A 423      32.035  34.586  27.094  1.00 34.20           C  
HETATM 3245  C   MSE A 423      32.144  36.033  26.617  1.00 32.95           C  
HETATM 3246  O   MSE A 423      31.888  36.329  25.453  1.00 33.25           O  
HETATM 3247  CB  MSE A 423      33.345  33.852  26.779  1.00 38.39           C  
HETATM 3248  CG  MSE A 423      33.361  32.374  27.178  1.00 43.07           C  
HETATM 3249 SE   MSE A 423      33.539  32.008  29.096  1.00 51.18          SE  
HETATM 3250  CE  MSE A 423      31.689  32.129  29.640  1.00 47.66           C  
HETATM 3251  N   MSE A 424      32.546  36.936  27.504  1.00 32.51           N  
HETATM 3252  CA  MSE A 424      32.660  38.341  27.136  1.00 33.79           C  
HETATM 3253  C   MSE A 424      33.588  38.589  25.953  1.00 33.42           C  
HETATM 3254  O   MSE A 424      33.349  39.511  25.161  1.00 31.75           O  
HETATM 3255  CB  MSE A 424      33.143  39.173  28.324  1.00 36.71           C  
HETATM 3256  CG  MSE A 424      33.001  40.686  28.117  1.00 38.39           C  
HETATM 3257 SE   MSE A 424      31.127  41.232  28.091  1.00 41.82          SE  
HETATM 3258  CE  MSE A 424      30.514  39.960  29.390  1.00 41.40           C  
ATOM   3259  N   ASN A 425      34.650  37.789  25.843  1.00 33.32           N  
ATOM   3260  CA  ASN A 425      35.605  37.930  24.740  1.00 34.12           C  
ATOM   3261  C   ASN A 425      34.919  37.599  23.416  1.00 32.88           C  
ATOM   3262  O   ASN A 425      35.186  38.229  22.391  1.00 33.39           O  
ATOM   3263  CB  ASN A 425      36.821  37.009  24.932  1.00 37.69           C  
ATOM   3264  CG  ASN A 425      37.700  37.423  26.112  1.00 41.73           C  
ATOM   3265  OD1 ASN A 425      37.654  38.571  26.578  1.00 44.48           O  
ATOM   3266  ND2 ASN A 425      38.524  36.489  26.587  1.00 42.10           N  
ATOM   3267  N   GLY A 426      34.037  36.606  23.437  1.00 29.86           N  
ATOM   3268  CA  GLY A 426      33.321  36.254  22.226  1.00 29.08           C  
ATOM   3269  C   GLY A 426      32.307  37.338  21.902  1.00 29.56           C  
ATOM   3270  O   GLY A 426      32.298  37.882  20.807  1.00 30.33           O  
ATOM   3271  N   PHE A 427      31.446  37.666  22.859  1.00 29.35           N  
ATOM   3272  CA  PHE A 427      30.454  38.714  22.644  1.00 28.24           C  
ATOM   3273  C   PHE A 427      31.087  40.035  22.201  1.00 28.55           C  
ATOM   3274  O   PHE A 427      30.543  40.740  21.351  1.00 27.54           O  
ATOM   3275  CB  PHE A 427      29.653  38.965  23.924  1.00 27.17           C  
ATOM   3276  CG  PHE A 427      28.861  40.245  23.898  1.00 26.46           C  
ATOM   3277  CD1 PHE A 427      27.740  40.370  23.086  1.00 27.83           C  
ATOM   3278  CD2 PHE A 427      29.263  41.342  24.651  1.00 27.20           C  
ATOM   3279  CE1 PHE A 427      27.029  41.575  23.023  1.00 27.54           C  
ATOM   3280  CE2 PHE A 427      28.560  42.551  24.595  1.00 27.70           C  
ATOM   3281  CZ  PHE A 427      27.442  42.664  23.778  1.00 27.62           C  
ATOM   3282  N   GLU A 428      32.231  40.380  22.775  1.00 29.40           N  
ATOM   3283  CA  GLU A 428      32.872  41.641  22.418  1.00 31.16           C  
ATOM   3284  C   GLU A 428      33.269  41.737  20.944  1.00 31.28           C  
ATOM   3285  O   GLU A 428      33.299  42.830  20.385  1.00 31.38           O  
ATOM   3286  CB  GLU A 428      34.099  41.887  23.293  1.00 33.10           C  
ATOM   3287  CG  GLU A 428      34.654  43.294  23.151  1.00 36.39           C  
ATOM   3288  CD  GLU A 428      34.420  44.146  24.394  1.00 38.87           C  
ATOM   3289  OE1 GLU A 428      33.261  44.215  24.874  1.00 38.19           O  
ATOM   3290  OE2 GLU A 428      35.401  44.755  24.885  1.00 38.30           O  
ATOM   3291  N   LYS A 429      33.581  40.608  20.312  1.00 30.99           N  
ATOM   3292  CA  LYS A 429      33.943  40.640  18.898  1.00 32.33           C  
ATOM   3293  C   LYS A 429      32.678  40.685  18.013  1.00 31.12           C  
ATOM   3294  O   LYS A 429      32.731  41.045  16.838  1.00 29.39           O  
ATOM   3295  CB  LYS A 429      34.823  39.429  18.538  1.00 36.16           C  
ATOM   3296  CG  LYS A 429      34.140  38.348  17.709  1.00 39.90           C  
ATOM   3297  CD  LYS A 429      33.403  37.349  18.574  1.00 41.80           C  
ATOM   3298  CE  LYS A 429      32.425  36.525  17.757  1.00 44.45           C  
ATOM   3299  NZ  LYS A 429      31.796  35.460  18.585  1.00 46.71           N  
ATOM   3300  N   LEU A 430      31.539  40.319  18.592  1.00 30.24           N  
ATOM   3301  CA  LEU A 430      30.276  40.348  17.866  1.00 29.30           C  
ATOM   3302  C   LEU A 430      29.828  41.782  17.611  1.00 28.48           C  
ATOM   3303  O   LEU A 430      29.233  42.071  16.571  1.00 29.48           O  
ATOM   3304  CB  LEU A 430      29.186  39.613  18.650  1.00 28.11           C  
ATOM   3305  CG  LEU A 430      27.738  39.799  18.172  1.00 25.99           C  
ATOM   3306  CD1 LEU A 430      27.558  39.311  16.726  1.00 24.91           C  
ATOM   3307  CD2 LEU A 430      26.822  39.023  19.121  1.00 24.69           C  
ATOM   3308  N   VAL A 431      30.108  42.678  18.555  1.00 27.79           N  
ATOM   3309  CA  VAL A 431      29.723  44.086  18.404  1.00 27.12           C  
ATOM   3310  C   VAL A 431      30.919  44.984  18.155  1.00 27.78           C  
ATOM   3311  O   VAL A 431      30.827  46.211  18.240  1.00 27.23           O  
ATOM   3312  CB  VAL A 431      28.969  44.615  19.643  1.00 26.83           C  
ATOM   3313  CG1 VAL A 431      27.604  43.961  19.727  1.00 24.35           C  
ATOM   3314  CG2 VAL A 431      29.794  44.364  20.910  1.00 25.57           C  
ATOM   3315  N   GLN A 432      32.037  44.353  17.828  1.00 30.92           N  
ATOM   3316  CA  GLN A 432      33.287  45.040  17.544  1.00 35.05           C  
ATOM   3317  C   GLN A 432      33.110  46.239  16.604  1.00 35.31           C  
ATOM   3318  O   GLN A 432      33.745  47.279  16.783  1.00 34.06           O  
ATOM   3319  CB  GLN A 432      34.273  44.048  16.914  1.00 37.89           C  
ATOM   3320  CG  GLN A 432      35.712  44.532  16.835  1.00 43.44           C  
ATOM   3321  CD  GLN A 432      36.607  43.575  16.055  1.00 48.08           C  
ATOM   3322  OE1 GLN A 432      36.558  42.353  16.246  1.00 49.43           O  
ATOM   3323  NE2 GLN A 432      37.436  44.129  15.173  1.00 49.92           N  
ATOM   3324  N   HIS A 433      32.245  46.087  15.607  1.00 36.40           N  
ATOM   3325  CA  HIS A 433      32.025  47.134  14.620  1.00 39.18           C  
ATOM   3326  C   HIS A 433      30.795  48.000  14.849  1.00 39.53           C  
ATOM   3327  O   HIS A 433      30.477  48.866  14.026  1.00 39.43           O  
ATOM   3328  CB  HIS A 433      31.966  46.498  13.234  1.00 42.13           C  
ATOM   3329  CG  HIS A 433      33.234  45.810  12.846  1.00 46.58           C  
ATOM   3330  ND1 HIS A 433      33.263  44.701  12.026  1.00 48.74           N  
ATOM   3331  CD2 HIS A 433      34.521  46.057  13.193  1.00 48.09           C  
ATOM   3332  CE1 HIS A 433      34.514  44.292  11.890  1.00 49.99           C  
ATOM   3333  NE2 HIS A 433      35.296  45.097  12.588  1.00 49.12           N  
ATOM   3334  N   GLY A 434      30.104  47.765  15.960  1.00 38.96           N  
ATOM   3335  CA  GLY A 434      28.926  48.550  16.265  1.00 37.26           C  
ATOM   3336  C   GLY A 434      27.824  47.712  16.862  1.00 36.71           C  
ATOM   3337  O   GLY A 434      27.767  46.502  16.632  1.00 36.74           O  
ATOM   3338  N   VAL A 435      26.960  48.355  17.646  1.00 36.05           N  
ATOM   3339  CA  VAL A 435      25.829  47.676  18.278  1.00 34.86           C  
ATOM   3340  C   VAL A 435      24.580  47.931  17.432  1.00 34.64           C  
ATOM   3341  O   VAL A 435      24.173  49.076  17.233  1.00 33.69           O  
ATOM   3342  CB  VAL A 435      25.565  48.194  19.718  1.00 34.19           C  
ATOM   3343  CG1 VAL A 435      24.333  47.507  20.292  1.00 32.58           C  
ATOM   3344  CG2 VAL A 435      26.778  47.928  20.610  1.00 33.02           C  
ATOM   3345  N   PRO A 436      23.955  46.856  16.930  1.00 34.04           N  
ATOM   3346  CA  PRO A 436      22.753  46.941  16.100  1.00 33.53           C  
ATOM   3347  C   PRO A 436      21.541  47.516  16.818  1.00 33.55           C  
ATOM   3348  O   PRO A 436      21.286  47.185  17.982  1.00 32.67           O  
ATOM   3349  CB  PRO A 436      22.531  45.492  15.683  1.00 34.66           C  
ATOM   3350  CG  PRO A 436      23.007  44.739  16.897  1.00 34.67           C  
ATOM   3351  CD  PRO A 436      24.300  45.448  17.202  1.00 33.47           C  
ATOM   3352  N   SER A 437      20.806  48.386  16.123  1.00 32.80           N  
ATOM   3353  CA  SER A 437      19.590  48.976  16.676  1.00 31.56           C  
ATOM   3354  C   SER A 437      18.638  47.805  16.909  1.00 31.23           C  
ATOM   3355  O   SER A 437      18.418  46.996  16.011  1.00 31.35           O  
ATOM   3356  CB  SER A 437      18.972  49.959  15.684  1.00 32.93           C  
ATOM   3357  OG  SER A 437      17.654  50.304  16.071  1.00 31.69           O  
ATOM   3358  N   LEU A 438      18.085  47.706  18.114  1.00 30.32           N  
ATOM   3359  CA  LEU A 438      17.186  46.606  18.451  1.00 28.89           C  
ATOM   3360  C   LEU A 438      15.848  47.103  18.944  1.00 29.73           C  
ATOM   3361  O   LEU A 438      14.935  46.309  19.174  1.00 30.96           O  
ATOM   3362  CB  LEU A 438      17.814  45.731  19.544  1.00 26.52           C  
ATOM   3363  CG  LEU A 438      18.477  44.384  19.228  1.00 26.38           C  
ATOM   3364  CD1 LEU A 438      19.258  44.423  17.925  1.00 25.18           C  
ATOM   3365  CD2 LEU A 438      19.377  44.005  20.402  1.00 25.96           C  
ATOM   3366  N   VAL A 439      15.737  48.412  19.122  1.00 29.47           N  
ATOM   3367  CA  VAL A 439      14.501  48.995  19.622  1.00 31.46           C  
ATOM   3368  C   VAL A 439      13.245  48.424  18.937  1.00 33.63           C  
ATOM   3369  O   VAL A 439      12.271  48.059  19.621  1.00 31.75           O  
ATOM   3370  CB  VAL A 439      14.531  50.543  19.482  1.00 29.97           C  
ATOM   3371  CG1 VAL A 439      14.614  50.933  18.007  1.00 28.38           C  
ATOM   3372  CG2 VAL A 439      13.299  51.161  20.161  1.00 28.75           C  
ATOM   3373  N   GLU A 440      13.278  48.324  17.604  1.00 34.91           N  
ATOM   3374  CA  GLU A 440      12.141  47.811  16.836  1.00 36.19           C  
ATOM   3375  C   GLU A 440      12.267  46.320  16.580  1.00 36.84           C  
ATOM   3376  O   GLU A 440      11.557  45.755  15.736  1.00 36.88           O  
ATOM   3377  CB  GLU A 440      12.023  48.552  15.499  1.00 38.09           C  
ATOM   3378  CG  GLU A 440      11.845  50.061  15.628  1.00 39.78           C  
ATOM   3379  CD  GLU A 440      10.435  50.468  16.024  1.00 42.55           C  
ATOM   3380  OE1 GLU A 440       9.686  49.617  16.555  1.00 43.14           O  
ATOM   3381  OE2 GLU A 440      10.081  51.652  15.816  1.00 42.81           O  
ATOM   3382  N   CYS A 441      13.169  45.678  17.313  1.00 36.02           N  
ATOM   3383  CA  CYS A 441      13.384  44.245  17.157  1.00 35.38           C  
ATOM   3384  C   CYS A 441      12.758  43.477  18.315  1.00 35.86           C  
ATOM   3385  O   CYS A 441      13.041  43.757  19.475  1.00 36.73           O  
ATOM   3386  CB  CYS A 441      14.878  43.941  17.085  1.00 33.47           C  
ATOM   3387  SG  CYS A 441      15.219  42.189  16.962  1.00 35.71           S  
ATOM   3388  N   LYS A 442      11.910  42.507  17.989  1.00 35.60           N  
ATOM   3389  CA  LYS A 442      11.233  41.701  18.992  1.00 36.63           C  
ATOM   3390  C   LYS A 442      11.997  40.435  19.348  1.00 36.53           C  
ATOM   3391  O   LYS A 442      11.873  39.905  20.457  1.00 35.64           O  
ATOM   3392  CB  LYS A 442       9.832  41.295  18.525  1.00 38.95           C  
ATOM   3393  CG  LYS A 442       9.373  39.985  19.169  1.00 42.36           C  
ATOM   3394  CD  LYS A 442       7.941  39.591  18.854  1.00 46.04           C  
ATOM   3395  CE  LYS A 442       7.670  38.183  19.383  1.00 47.53           C  
ATOM   3396  NZ  LYS A 442       6.228  37.931  19.654  1.00 52.10           N  
ATOM   3397  N   ARG A 443      12.773  39.934  18.402  1.00 36.00           N  
ATOM   3398  CA  ARG A 443      13.538  38.726  18.646  1.00 36.76           C  
ATOM   3399  C   ARG A 443      14.683  38.632  17.660  1.00 36.05           C  
ATOM   3400  O   ARG A 443      14.499  38.760  16.454  1.00 35.91           O  
ATOM   3401  CB  ARG A 443      12.632  37.496  18.527  1.00 37.64           C  
ATOM   3402  CG  ARG A 443      13.255  36.211  19.030  1.00 38.61           C  
ATOM   3403  CD  ARG A 443      12.344  35.040  18.732  1.00 41.37           C  
ATOM   3404  NE  ARG A 443      11.069  35.197  19.420  1.00 43.73           N  
ATOM   3405  CZ  ARG A 443      10.792  34.667  20.606  1.00 44.33           C  
ATOM   3406  NH1 ARG A 443      11.700  33.930  21.238  1.00 43.89           N  
ATOM   3407  NH2 ARG A 443       9.615  34.898  21.169  1.00 44.01           N  
ATOM   3408  N   VAL A 444      15.870  38.419  18.202  1.00 35.38           N  
ATOM   3409  CA  VAL A 444      17.070  38.292  17.404  1.00 35.07           C  
ATOM   3410  C   VAL A 444      17.865  37.095  17.897  1.00 35.08           C  
ATOM   3411  O   VAL A 444      18.187  36.976  19.085  1.00 35.84           O  
ATOM   3412  CB  VAL A 444      17.951  39.563  17.475  1.00 34.86           C  
ATOM   3413  CG1 VAL A 444      18.120  40.014  18.918  1.00 35.74           C  
ATOM   3414  CG2 VAL A 444      19.311  39.279  16.845  1.00 35.12           C  
ATOM   3415  N   THR A 445      18.164  36.196  16.973  1.00 34.30           N  
ATOM   3416  CA  THR A 445      18.923  35.009  17.296  1.00 34.09           C  
ATOM   3417  C   THR A 445      20.168  35.047  16.423  1.00 34.53           C  
ATOM   3418  O   THR A 445      20.140  35.570  15.312  1.00 34.86           O  
ATOM   3419  CB  THR A 445      18.098  33.734  16.998  1.00 34.82           C  
ATOM   3420  OG1 THR A 445      16.876  33.774  17.746  1.00 33.80           O  
ATOM   3421  CG2 THR A 445      18.877  32.474  17.386  1.00 34.91           C  
ATOM   3422  N   VAL A 446      21.273  34.536  16.943  1.00 34.62           N  
ATOM   3423  CA  VAL A 446      22.512  34.499  16.177  1.00 33.04           C  
ATOM   3424  C   VAL A 446      23.074  33.101  16.341  1.00 32.61           C  
ATOM   3425  O   VAL A 446      23.323  32.640  17.458  1.00 33.28           O  
ATOM   3426  CB  VAL A 446      23.531  35.542  16.674  1.00 32.43           C  
ATOM   3427  CG1 VAL A 446      24.780  35.518  15.802  1.00 31.59           C  
ATOM   3428  CG2 VAL A 446      22.901  36.922  16.649  1.00 32.75           C  
ATOM   3429  N   LYS A 447      23.223  32.415  15.219  1.00 31.57           N  
ATOM   3430  CA  LYS A 447      23.741  31.063  15.208  1.00 32.60           C  
ATOM   3431  C   LYS A 447      25.075  31.088  14.481  1.00 32.22           C  
ATOM   3432  O   LYS A 447      25.228  31.791  13.482  1.00 31.81           O  
ATOM   3433  CB  LYS A 447      22.760  30.145  14.488  1.00 35.18           C  
ATOM   3434  CG  LYS A 447      21.348  30.205  15.055  1.00 38.38           C  
ATOM   3435  CD  LYS A 447      20.431  29.191  14.379  1.00 41.17           C  
ATOM   3436  CE  LYS A 447      19.118  29.034  15.142  1.00 43.04           C  
ATOM   3437  NZ  LYS A 447      18.270  27.919  14.609  1.00 44.47           N  
ATOM   3438  N   GLY A 448      26.042  30.335  14.993  1.00 31.62           N  
ATOM   3439  CA  GLY A 448      27.354  30.305  14.371  1.00 31.91           C  
ATOM   3440  C   GLY A 448      28.085  31.622  14.558  1.00 31.78           C  
ATOM   3441  O   GLY A 448      27.548  32.565  15.142  1.00 28.88           O  
ATOM   3442  N   LEU A 449      29.314  31.684  14.051  1.00 32.80           N  
ATOM   3443  CA  LEU A 449      30.140  32.875  14.170  1.00 31.67           C  
ATOM   3444  C   LEU A 449      29.643  33.977  13.259  1.00 32.88           C  
ATOM   3445  O   LEU A 449      29.481  33.784  12.058  1.00 33.77           O  
ATOM   3446  CB  LEU A 449      31.596  32.546  13.840  1.00 31.15           C  
ATOM   3447  CG  LEU A 449      32.569  33.724  13.977  1.00 30.24           C  
ATOM   3448  CD1 LEU A 449      32.581  34.216  15.408  1.00 28.90           C  
ATOM   3449  CD2 LEU A 449      33.962  33.292  13.564  1.00 30.48           C  
ATOM   3450  N   VAL A 450      29.414  35.146  13.841  1.00 33.73           N  
ATOM   3451  CA  VAL A 450      28.916  36.291  13.097  1.00 33.16           C  
ATOM   3452  C   VAL A 450      29.500  37.572  13.664  1.00 33.41           C  
ATOM   3453  O   VAL A 450      29.980  37.604  14.793  1.00 34.19           O  
ATOM   3454  CB  VAL A 450      27.377  36.369  13.189  1.00 33.16           C  
ATOM   3455  CG1 VAL A 450      26.873  37.684  12.596  1.00 31.26           C  
ATOM   3456  CG2 VAL A 450      26.759  35.179  12.480  1.00 33.10           C  
ATOM   3457  N   GLN A 451      29.438  38.633  12.877  1.00 33.71           N  
ATOM   3458  CA  GLN A 451      29.960  39.912  13.304  1.00 35.21           C  
ATOM   3459  C   GLN A 451      29.089  41.039  12.761  1.00 34.72           C  
ATOM   3460  O   GLN A 451      28.930  41.173  11.545  1.00 35.13           O  
ATOM   3461  CB  GLN A 451      31.394  40.065  12.804  1.00 37.39           C  
ATOM   3462  CG  GLN A 451      32.179  41.150  13.506  1.00 41.08           C  
ATOM   3463  CD  GLN A 451      33.660  41.106  13.171  1.00 42.79           C  
ATOM   3464  OE1 GLN A 451      34.482  41.764  13.827  1.00 44.31           O  
ATOM   3465  NE2 GLN A 451      34.010  40.333  12.148  1.00 42.27           N  
ATOM   3466  N   PHE A 452      28.513  41.842  13.655  1.00 33.66           N  
ATOM   3467  CA  PHE A 452      27.682  42.952  13.207  1.00 33.38           C  
ATOM   3468  C   PHE A 452      28.553  43.988  12.516  1.00 33.78           C  
ATOM   3469  O   PHE A 452      29.744  44.124  12.818  1.00 32.24           O  
ATOM   3470  CB  PHE A 452      26.945  43.632  14.370  1.00 32.45           C  
ATOM   3471  CG  PHE A 452      25.817  42.814  14.947  1.00 32.35           C  
ATOM   3472  CD1 PHE A 452      25.937  42.221  16.205  1.00 32.04           C  
ATOM   3473  CD2 PHE A 452      24.645  42.620  14.232  1.00 31.33           C  
ATOM   3474  CE1 PHE A 452      24.908  41.443  16.738  1.00 30.42           C  
ATOM   3475  CE2 PHE A 452      23.603  41.841  14.759  1.00 32.15           C  
ATOM   3476  CZ  PHE A 452      23.739  41.251  16.015  1.00 31.28           C  
ATOM   3477  N   GLY A 453      27.940  44.689  11.566  1.00 34.52           N  
ATOM   3478  CA  GLY A 453      28.621  45.747  10.853  1.00 35.71           C  
ATOM   3479  C   GLY A 453      28.095  47.019  11.483  1.00 36.65           C  
ATOM   3480  O   GLY A 453      27.411  46.954  12.506  1.00 37.88           O  
ATOM   3481  N   ALA A 454      28.395  48.171  10.900  1.00 37.41           N  
ATOM   3482  CA  ALA A 454      27.915  49.427  11.463  1.00 38.07           C  
ATOM   3483  C   ALA A 454      26.480  49.674  11.007  1.00 38.98           C  
ATOM   3484  O   ALA A 454      26.003  49.035  10.064  1.00 39.94           O  
ATOM   3485  CB  ALA A 454      28.818  50.569  11.024  1.00 37.23           C  
ATOM   3486  N   GLY A 455      25.794  50.585  11.694  1.00 39.64           N  
ATOM   3487  CA  GLY A 455      24.419  50.925  11.352  1.00 39.39           C  
ATOM   3488  C   GLY A 455      23.422  49.790  11.157  1.00 39.67           C  
ATOM   3489  O   GLY A 455      22.360  49.996  10.567  1.00 40.66           O  
ATOM   3490  N   ASN A 456      23.746  48.591  11.630  1.00 39.16           N  
ATOM   3491  CA  ASN A 456      22.828  47.458  11.510  1.00 38.71           C  
ATOM   3492  C   ASN A 456      21.512  47.791  12.244  1.00 38.61           C  
ATOM   3493  O   ASN A 456      21.533  48.191  13.412  1.00 38.45           O  
ATOM   3494  CB  ASN A 456      23.466  46.201  12.117  1.00 39.78           C  
ATOM   3495  CG  ASN A 456      24.556  45.604  11.236  1.00 39.40           C  
ATOM   3496  OD1 ASN A 456      25.277  46.321  10.543  1.00 40.02           O  
ATOM   3497  ND2 ASN A 456      24.688  44.282  11.276  1.00 37.32           N  
ATOM   3498  N   VAL A 457      20.380  47.629  11.554  1.00 37.62           N  
ATOM   3499  CA  VAL A 457      19.061  47.918  12.117  1.00 36.27           C  
ATOM   3500  C   VAL A 457      18.137  46.712  11.999  1.00 37.12           C  
ATOM   3501  O   VAL A 457      17.733  46.339  10.896  1.00 38.52           O  
ATOM   3502  CB  VAL A 457      18.382  49.100  11.381  1.00 35.77           C  
ATOM   3503  CG1 VAL A 457      16.980  49.300  11.917  1.00 35.21           C  
ATOM   3504  CG2 VAL A 457      19.207  50.382  11.547  1.00 34.71           C  
ATOM   3505  N   LEU A 458      17.785  46.098  13.123  1.00 36.30           N  
ATOM   3506  CA  LEU A 458      16.901  44.945  13.060  1.00 36.02           C  
ATOM   3507  C   LEU A 458      15.470  45.332  13.423  1.00 37.80           C  
ATOM   3508  O   LEU A 458      15.239  46.245  14.220  1.00 37.10           O  
ATOM   3509  CB  LEU A 458      17.406  43.829  13.981  1.00 35.24           C  
ATOM   3510  CG  LEU A 458      18.905  43.478  13.912  1.00 34.24           C  
ATOM   3511  CD1 LEU A 458      19.098  42.027  14.330  1.00 32.14           C  
ATOM   3512  CD2 LEU A 458      19.450  43.687  12.516  1.00 35.00           C  
ATOM   3513  N   THR A 459      14.513  44.641  12.811  1.00 38.92           N  
ATOM   3514  CA  THR A 459      13.098  44.895  13.041  1.00 39.05           C  
ATOM   3515  C   THR A 459      12.334  43.578  12.985  1.00 39.56           C  
ATOM   3516  O   THR A 459      12.658  42.695  12.186  1.00 39.32           O  
ATOM   3517  CB  THR A 459      12.536  45.859  11.974  1.00 40.09           C  
ATOM   3518  OG1 THR A 459      13.033  47.186  12.212  1.00 40.33           O  
ATOM   3519  CG2 THR A 459      11.016  45.867  12.004  1.00 41.74           C  
ATOM   3520  N   GLY A 460      11.316  43.449  13.830  1.00 39.24           N  
ATOM   3521  CA  GLY A 460      10.536  42.227  13.853  1.00 38.85           C  
ATOM   3522  C   GLY A 460      11.412  41.070  14.284  1.00 39.56           C  
ATOM   3523  O   GLY A 460      12.402  41.274  14.980  1.00 40.97           O  
ATOM   3524  N   THR A 461      11.061  39.857  13.874  1.00 38.93           N  
ATOM   3525  CA  THR A 461      11.836  38.677  14.235  1.00 39.14           C  
ATOM   3526  C   THR A 461      12.978  38.441  13.247  1.00 40.62           C  
ATOM   3527  O   THR A 461      12.744  38.166  12.066  1.00 40.14           O  
ATOM   3528  CB  THR A 461      10.934  37.434  14.285  1.00 38.28           C  
ATOM   3529  OG1 THR A 461       9.940  37.617  15.300  1.00 37.61           O  
ATOM   3530  CG2 THR A 461      11.748  36.181  14.595  1.00 37.79           C  
ATOM   3531  N   VAL A 462      14.212  38.540  13.745  1.00 41.11           N  
ATOM   3532  CA  VAL A 462      15.412  38.358  12.925  1.00 39.97           C  
ATOM   3533  C   VAL A 462      16.380  37.273  13.401  1.00 41.54           C  
ATOM   3534  O   VAL A 462      16.801  37.265  14.554  1.00 43.16           O  
ATOM   3535  CB  VAL A 462      16.211  39.663  12.839  1.00 38.65           C  
ATOM   3536  CG1 VAL A 462      17.506  39.425  12.081  1.00 38.77           C  
ATOM   3537  CG2 VAL A 462      15.381  40.740  12.169  1.00 35.96           C  
ATOM   3538  N   THR A 463      16.732  36.354  12.510  1.00 41.37           N  
ATOM   3539  CA  THR A 463      17.686  35.304  12.842  1.00 41.73           C  
ATOM   3540  C   THR A 463      18.860  35.473  11.908  1.00 43.47           C  
ATOM   3541  O   THR A 463      18.687  35.804  10.740  1.00 44.70           O  
ATOM   3542  CB  THR A 463      17.126  33.883  12.626  1.00 41.13           C  
ATOM   3543  OG1 THR A 463      16.215  33.556  13.679  1.00 42.13           O  
ATOM   3544  CG2 THR A 463      18.248  32.866  12.627  1.00 40.01           C  
ATOM   3545  N   ILE A 464      20.059  35.261  12.427  1.00 45.12           N  
ATOM   3546  CA  ILE A 464      21.260  35.370  11.619  1.00 46.45           C  
ATOM   3547  C   ILE A 464      21.996  34.042  11.729  1.00 48.85           C  
ATOM   3548  O   ILE A 464      22.481  33.673  12.800  1.00 48.47           O  
ATOM   3549  CB  ILE A 464      22.151  36.535  12.097  1.00 43.99           C  
ATOM   3550  CG1 ILE A 464      21.394  37.852  11.926  1.00 43.79           C  
ATOM   3551  CG2 ILE A 464      23.445  36.576  11.301  1.00 43.36           C  
ATOM   3552  CD1 ILE A 464      22.162  39.069  12.359  1.00 42.76           C  
ATOM   3553  N   GLU A 465      22.035  33.305  10.621  1.00 51.81           N  
ATOM   3554  CA  GLU A 465      22.698  32.010  10.599  1.00 54.64           C  
ATOM   3555  C   GLU A 465      24.022  32.003   9.875  1.00 56.31           C  
ATOM   3556  O   GLU A 465      24.179  32.608   8.820  1.00 56.84           O  
ATOM   3557  CB  GLU A 465      21.808  30.942   9.969  1.00 55.74           C  
ATOM   3558  CG  GLU A 465      20.765  30.376  10.908  1.00 58.99           C  
ATOM   3559  CD  GLU A 465      20.352  28.961  10.538  1.00 60.09           C  
ATOM   3560  OE1 GLU A 465      19.914  28.747   9.386  1.00 60.60           O  
ATOM   3561  OE2 GLU A 465      20.469  28.063  11.406  1.00 60.26           O  
ATOM   3562  N   ASN A 466      24.968  31.298  10.475  1.00 59.39           N  
ATOM   3563  CA  ASN A 466      26.305  31.135   9.941  1.00 62.06           C  
ATOM   3564  C   ASN A 466      26.502  29.626   9.978  1.00 63.43           C  
ATOM   3565  O   ASN A 466      27.227  29.095  10.821  1.00 62.96           O  
ATOM   3566  CB  ASN A 466      27.333  31.823  10.845  1.00 63.67           C  
ATOM   3567  CG  ASN A 466      28.747  31.728  10.302  1.00 65.26           C  
ATOM   3568  OD1 ASN A 466      29.112  32.435   9.361  1.00 65.77           O  
ATOM   3569  ND2 ASN A 466      29.546  30.838  10.884  1.00 65.79           N  
ATOM   3570  N   THR A 467      25.815  28.942   9.070  1.00 65.47           N  
ATOM   3571  CA  THR A 467      25.884  27.487   8.971  1.00 67.69           C  
ATOM   3572  C   THR A 467      27.277  27.082   8.513  1.00 68.64           C  
ATOM   3573  O   THR A 467      27.753  25.990   8.824  1.00 67.88           O  
ATOM   3574  CB  THR A 467      24.872  26.968   7.947  1.00 68.72           C  
ATOM   3575  OG1 THR A 467      23.625  27.656   8.119  1.00 69.16           O  
ATOM   3576  CG2 THR A 467      24.652  25.473   8.134  1.00 69.35           C  
ATOM   3577  N   ASP A 468      27.912  27.988   7.769  1.00 70.35           N  
ATOM   3578  CA  ASP A 468      29.257  27.801   7.227  1.00 71.13           C  
ATOM   3579  C   ASP A 468      30.278  27.383   8.281  1.00 70.61           C  
ATOM   3580  O   ASP A 468      30.995  26.401   8.090  1.00 70.67           O  
ATOM   3581  CB  ASP A 468      29.712  29.090   6.534  1.00 73.26           C  
ATOM   3582  CG  ASP A 468      29.394  30.334   7.347  1.00 75.14           C  
ATOM   3583  OD1 ASP A 468      28.723  30.198   8.390  1.00 74.88           O  
ATOM   3584  OD2 ASP A 468      29.807  31.442   6.939  1.00 76.16           O  
ATOM   3585  N   SER A 469      30.350  28.145   9.373  1.00 69.54           N  
ATOM   3586  CA  SER A 469      31.251  27.870  10.497  1.00 68.46           C  
ATOM   3587  C   SER A 469      32.661  28.459  10.436  1.00 67.63           C  
ATOM   3588  O   SER A 469      32.947  29.485  11.055  1.00 67.67           O  
ATOM   3589  CB  SER A 469      31.358  26.355  10.736  1.00 68.87           C  
ATOM   3590  OG  SER A 469      30.120  25.804  11.156  1.00 68.59           O  
ATOM   3591  N   ALA A 470      33.538  27.790   9.697  1.00 65.86           N  
ATOM   3592  CA  ALA A 470      34.936  28.189   9.559  1.00 63.65           C  
ATOM   3593  C   ALA A 470      35.227  29.640   9.156  1.00 62.25           C  
ATOM   3594  O   ALA A 470      36.379  30.076   9.226  1.00 62.13           O  
ATOM   3595  CB  ALA A 470      35.632  27.240   8.585  1.00 63.52           C  
ATOM   3596  N   SER A 471      34.204  30.384   8.739  1.00 59.81           N  
ATOM   3597  CA  SER A 471      34.402  31.774   8.321  1.00 56.89           C  
ATOM   3598  C   SER A 471      33.368  32.712   8.917  1.00 54.71           C  
ATOM   3599  O   SER A 471      32.171  32.489   8.767  1.00 53.99           O  
ATOM   3600  CB  SER A 471      34.348  31.889   6.795  1.00 56.32           C  
ATOM   3601  OG  SER A 471      35.380  31.138   6.181  1.00 57.23           O  
ATOM   3602  N   ALA A 472      33.844  33.772   9.566  1.00 52.18           N  
ATOM   3603  CA  ALA A 472      32.977  34.762  10.196  1.00 50.64           C  
ATOM   3604  C   ALA A 472      32.113  35.513   9.190  1.00 49.72           C  
ATOM   3605  O   ALA A 472      32.618  36.298   8.387  1.00 50.54           O  
ATOM   3606  CB  ALA A 472      33.816  35.751  10.988  1.00 48.74           C  
ATOM   3607  N   PHE A 473      30.808  35.267   9.242  1.00 48.26           N  
ATOM   3608  CA  PHE A 473      29.859  35.931   8.355  1.00 48.40           C  
ATOM   3609  C   PHE A 473      29.697  37.389   8.794  1.00 47.79           C  
ATOM   3610  O   PHE A 473      28.907  37.681   9.690  1.00 48.04           O  
ATOM   3611  CB  PHE A 473      28.507  35.226   8.429  1.00 48.22           C  
ATOM   3612  CG  PHE A 473      27.416  35.926   7.678  1.00 50.89           C  
ATOM   3613  CD1 PHE A 473      26.122  35.951   8.181  1.00 51.38           C  
ATOM   3614  CD2 PHE A 473      27.675  36.555   6.465  1.00 52.08           C  
ATOM   3615  CE1 PHE A 473      25.099  36.595   7.488  1.00 51.52           C  
ATOM   3616  CE2 PHE A 473      26.660  37.202   5.764  1.00 52.56           C  
ATOM   3617  CZ  PHE A 473      25.369  37.222   6.277  1.00 52.22           C  
ATOM   3618  N   VAL A 474      30.442  38.298   8.169  1.00 46.37           N  
ATOM   3619  CA  VAL A 474      30.369  39.710   8.531  1.00 46.04           C  
ATOM   3620  C   VAL A 474      29.230  40.428   7.831  1.00 46.23           C  
ATOM   3621  O   VAL A 474      29.202  40.549   6.609  1.00 46.05           O  
ATOM   3622  CB  VAL A 474      31.677  40.450   8.202  1.00 46.86           C  
ATOM   3623  CG1 VAL A 474      31.560  41.925   8.601  1.00 46.72           C  
ATOM   3624  CG2 VAL A 474      32.838  39.785   8.925  1.00 47.20           C  
ATOM   3625  N   ILE A 475      28.290  40.913   8.625  1.00 46.05           N  
ATOM   3626  CA  ILE A 475      27.145  41.619   8.087  1.00 45.40           C  
ATOM   3627  C   ILE A 475      27.581  42.998   7.615  1.00 44.86           C  
ATOM   3628  O   ILE A 475      28.307  43.698   8.311  1.00 44.43           O  
ATOM   3629  CB  ILE A 475      26.046  41.738   9.153  1.00 44.74           C  
ATOM   3630  CG1 ILE A 475      25.632  40.333   9.595  1.00 44.68           C  
ATOM   3631  CG2 ILE A 475      24.857  42.510   8.599  1.00 44.01           C  
ATOM   3632  CD1 ILE A 475      24.804  40.293  10.842  1.00 44.97           C  
ATOM   3633  N   PRO A 476      27.156  43.389   6.404  1.00 45.33           N  
ATOM   3634  CA  PRO A 476      27.463  44.675   5.766  1.00 45.45           C  
ATOM   3635  C   PRO A 476      27.057  45.869   6.620  1.00 45.62           C  
ATOM   3636  O   PRO A 476      26.205  45.746   7.497  1.00 44.37           O  
ATOM   3637  CB  PRO A 476      26.657  44.616   4.471  1.00 45.05           C  
ATOM   3638  CG  PRO A 476      26.642  43.152   4.153  1.00 45.30           C  
ATOM   3639  CD  PRO A 476      26.364  42.535   5.499  1.00 45.78           C  
ATOM   3640  N   ASP A 477      27.665  47.020   6.356  1.00 46.23           N  
ATOM   3641  CA  ASP A 477      27.331  48.226   7.091  1.00 47.90           C  
ATOM   3642  C   ASP A 477      25.983  48.750   6.624  1.00 48.49           C  
ATOM   3643  O   ASP A 477      25.550  48.448   5.516  1.00 49.38           O  
ATOM   3644  CB  ASP A 477      28.401  49.294   6.882  1.00 48.91           C  
ATOM   3645  CG  ASP A 477      29.702  48.951   7.576  1.00 51.33           C  
ATOM   3646  OD1 ASP A 477      30.618  49.804   7.585  1.00 53.22           O  
ATOM   3647  OD2 ASP A 477      29.809  47.824   8.114  1.00 51.53           O  
ATOM   3648  N   GLY A 478      25.319  49.519   7.482  1.00 48.74           N  
ATOM   3649  CA  GLY A 478      24.027  50.087   7.143  1.00 48.74           C  
ATOM   3650  C   GLY A 478      22.947  49.068   6.849  1.00 49.62           C  
ATOM   3651  O   GLY A 478      21.817  49.425   6.511  1.00 49.53           O  
ATOM   3652  N   ALA A 479      23.293  47.793   6.976  1.00 50.52           N  
ATOM   3653  CA  ALA A 479      22.343  46.715   6.717  1.00 51.20           C  
ATOM   3654  C   ALA A 479      21.018  46.939   7.448  1.00 51.44           C  
ATOM   3655  O   ALA A 479      20.972  47.603   8.486  1.00 52.38           O  
ATOM   3656  CB  ALA A 479      22.949  45.384   7.138  1.00 51.15           C  
ATOM   3657  N   LYS A 480      19.946  46.388   6.891  1.00 50.51           N  
ATOM   3658  CA  LYS A 480      18.622  46.498   7.486  1.00 50.29           C  
ATOM   3659  C   LYS A 480      17.965  45.137   7.374  1.00 50.21           C  
ATOM   3660  O   LYS A 480      17.749  44.625   6.273  1.00 51.06           O  
ATOM   3661  CB  LYS A 480      17.800  47.569   6.772  1.00 49.35           C  
ATOM   3662  CG  LYS A 480      18.419  48.942   6.908  1.00 49.75           C  
ATOM   3663  CD  LYS A 480      17.669  50.005   6.134  1.00 50.03           C  
ATOM   3664  CE  LYS A 480      18.461  51.299   6.162  1.00 49.58           C  
ATOM   3665  NZ  LYS A 480      18.812  51.656   7.565  1.00 49.00           N  
ATOM   3666  N   LEU A 481      17.668  44.541   8.522  1.00 50.19           N  
ATOM   3667  CA  LEU A 481      17.075  43.213   8.562  1.00 49.80           C  
ATOM   3668  C   LEU A 481      15.702  43.177   9.244  1.00 49.72           C  
ATOM   3669  O   LEU A 481      15.590  43.351  10.458  1.00 50.50           O  
ATOM   3670  CB  LEU A 481      18.047  42.259   9.271  1.00 50.22           C  
ATOM   3671  CG  LEU A 481      19.531  42.518   8.995  1.00 50.49           C  
ATOM   3672  CD1 LEU A 481      20.400  41.501   9.730  1.00 49.74           C  
ATOM   3673  CD2 LEU A 481      19.802  42.454   7.501  1.00 51.04           C  
ATOM   3674  N   ASN A 482      14.668  42.944   8.442  1.00 49.08           N  
ATOM   3675  CA  ASN A 482      13.303  42.864   8.915  1.00 48.72           C  
ATOM   3676  C   ASN A 482      12.854  41.418   8.766  1.00 48.47           C  
ATOM   3677  O   ASN A 482      13.262  40.745   7.830  1.00 49.04           O  
ATOM   3678  CB  ASN A 482      12.397  43.750   8.065  1.00 49.58           C  
ATOM   3679  CG  ASN A 482      12.855  45.198   8.015  1.00 50.94           C  
ATOM   3680  OD1 ASN A 482      14.005  45.501   7.692  1.00 51.60           O  
ATOM   3681  ND2 ASN A 482      11.941  46.105   8.333  1.00 52.22           N  
ATOM   3682  N   ASP A 483      12.015  40.957   9.689  1.00 47.94           N  
ATOM   3683  CA  ASP A 483      11.493  39.587   9.692  1.00 48.13           C  
ATOM   3684  C   ASP A 483      12.158  38.633   8.691  1.00 47.14           C  
ATOM   3685  O   ASP A 483      11.496  38.095   7.802  1.00 46.21           O  
ATOM   3686  CB  ASP A 483       9.982  39.603   9.434  1.00 49.42           C  
ATOM   3687  CG  ASP A 483       9.201  40.262  10.554  1.00 50.08           C  
ATOM   3688  OD1 ASP A 483       8.071  40.724  10.303  1.00 52.21           O  
ATOM   3689  OD2 ASP A 483       9.708  40.303  11.692  1.00 50.42           O  
ATOM   3690  N   THR A 484      13.457  38.405   8.854  1.00 46.48           N  
ATOM   3691  CA  THR A 484      14.187  37.535   7.951  1.00 46.50           C  
ATOM   3692  C   THR A 484      15.223  36.661   8.665  1.00 46.35           C  
ATOM   3693  O   THR A 484      15.410  36.763   9.878  1.00 46.47           O  
ATOM   3694  CB  THR A 484      14.879  38.383   6.836  1.00 46.54           C  
ATOM   3695  OG1 THR A 484      15.530  37.515   5.906  1.00 48.03           O  
ATOM   3696  CG2 THR A 484      15.914  39.327   7.435  1.00 46.24           C  
ATOM   3697  N   THR A 485      15.868  35.787   7.897  1.00 45.94           N  
ATOM   3698  CA  THR A 485      16.916  34.894   8.391  1.00 45.54           C  
ATOM   3699  C   THR A 485      18.084  35.159   7.444  1.00 45.66           C  
ATOM   3700  O   THR A 485      18.146  34.602   6.350  1.00 46.33           O  
ATOM   3701  CB  THR A 485      16.482  33.387   8.316  1.00 45.31           C  
ATOM   3702  OG1 THR A 485      15.637  33.067   9.430  1.00 45.03           O  
ATOM   3703  CG2 THR A 485      17.693  32.456   8.333  1.00 44.03           C  
ATOM   3704  N   ALA A 486      18.984  36.046   7.853  1.00 45.95           N  
ATOM   3705  CA  ALA A 486      20.135  36.394   7.029  1.00 45.77           C  
ATOM   3706  C   ALA A 486      21.290  35.435   7.266  1.00 46.01           C  
ATOM   3707  O   ALA A 486      21.611  35.086   8.406  1.00 46.38           O  
ATOM   3708  CB  ALA A 486      20.573  37.820   7.314  1.00 44.18           C  
ATOM   3709  N   SER A 487      21.907  35.003   6.176  1.00 45.19           N  
ATOM   3710  CA  SER A 487      23.031  34.086   6.249  1.00 44.59           C  
ATOM   3711  C   SER A 487      23.884  34.269   4.998  1.00 43.99           C  
ATOM   3712  O   SER A 487      23.491  34.980   4.072  1.00 43.09           O  
ATOM   3713  CB  SER A 487      22.527  32.639   6.373  1.00 44.57           C  
ATOM   3714  OG  SER A 487      21.603  32.309   5.353  1.00 45.23           O  
ATOM   3715  N   PRO A 488      25.076  33.653   4.964  1.00 43.54           N  
ATOM   3716  CA  PRO A 488      25.944  33.790   3.788  1.00 44.26           C  
ATOM   3717  C   PRO A 488      25.438  32.996   2.569  1.00 44.26           C  
ATOM   3718  O   PRO A 488      25.084  33.639   1.556  1.00 45.52           O  
ATOM   3719  CB  PRO A 488      27.294  33.298   4.308  1.00 43.73           C  
ATOM   3720  CG  PRO A 488      26.893  32.232   5.291  1.00 43.33           C  
ATOM   3721  CD  PRO A 488      25.728  32.860   6.023  1.00 43.00           C  
TER    3722      PRO A 488                                                      
HETATM 3723  N1  UPG A5206      26.253  39.111  44.579  1.00 18.88           N  
HETATM 3724  C2  UPG A5206      27.053  39.476  45.712  1.00 15.15           C  
HETATM 3725  N3  UPG A5206      27.549  38.413  46.433  1.00 15.91           N  
HETATM 3726  C4  UPG A5206      27.356  37.057  46.220  1.00 17.86           C  
HETATM 3727  C5  UPG A5206      26.600  36.731  44.982  1.00 18.01           C  
HETATM 3728  C6  UPG A5206      26.083  37.754  44.237  1.00 17.67           C  
HETATM 3729  O2  UPG A5206      27.234  40.644  46.017  1.00 19.13           O  
HETATM 3730  O4  UPG A5206      27.776  36.212  46.991  1.00 21.76           O  
HETATM 3731  C1C UPG A5206      25.686  40.215  43.748  1.00 17.65           C  
HETATM 3732  C2C UPG A5206      25.976  40.200  42.237  1.00 16.79           C  
HETATM 3733  O2C UPG A5206      27.185  40.827  41.848  1.00 16.39           O  
HETATM 3734  C3C UPG A5206      24.667  40.795  41.728  1.00 18.15           C  
HETATM 3735  C4C UPG A5206      23.594  40.234  42.653  1.00 20.01           C  
HETATM 3736  O4C UPG A5206      24.256  40.208  43.942  1.00 18.50           O  
HETATM 3737  O3C UPG A5206      24.722  42.248  41.789  1.00 16.73           O  
HETATM 3738  C5C UPG A5206      23.163  38.749  42.418  1.00 23.30           C  
HETATM 3739  O5C UPG A5206      22.756  38.497  41.157  1.00 25.98           O  
HETATM 3740  PA  UPG A5206      23.225  37.415  40.140  1.00 22.46           P  
HETATM 3741  O1A UPG A5206      23.596  38.144  38.929  1.00 21.73           O  
HETATM 3742  O2A UPG A5206      24.083  36.360  40.657  1.00 24.31           O  
HETATM 3743  O3A UPG A5206      21.815  36.792  40.015  1.00 20.01           O  
HETATM 3744  PB  UPG A5206      20.958  35.698  40.794  1.00 15.38           P  
HETATM 3745  O1B UPG A5206      21.451  35.466  42.132  1.00 16.92           O  
HETATM 3746  O2B UPG A5206      20.936  34.514  39.909  1.00 20.13           O  
HETATM 3747  O3B UPG A5206      19.474  36.282  40.985  1.00 15.90           O  
HETATM 3748  C1' UPG A5206      19.024  37.443  41.679  1.00 13.45           C  
HETATM 3749  C2' UPG A5206      17.913  36.964  42.608  1.00 13.78           C  
HETATM 3750  C3' UPG A5206      16.736  36.356  41.785  1.00 14.98           C  
HETATM 3751  C4' UPG A5206      16.237  37.447  40.815  1.00 14.19           C  
HETATM 3752  C5' UPG A5206      17.403  37.943  39.928  1.00 12.38           C  
HETATM 3753  C6' UPG A5206      16.951  39.174  39.164  1.00 11.34           C  
HETATM 3754  O2' UPG A5206      18.431  36.004  43.511  1.00 15.29           O  
HETATM 3755  O3' UPG A5206      15.671  35.907  42.640  1.00 15.39           O  
HETATM 3756  O4' UPG A5206      15.221  36.922  39.936  1.00 13.85           O  
HETATM 3757  O5' UPG A5206      18.522  38.432  40.758  1.00 13.93           O  
HETATM 3758  O6' UPG A5206      18.005  39.373  38.229  1.00 13.72           O  
HETATM 3759  O   HOH A5207      21.020  47.685  33.907  1.00 14.38           O  
HETATM 3760  O   HOH A5208      24.771  45.075  64.101  1.00 10.63           O  
HETATM 3761  O   HOH A5209      -2.346  34.752  45.975  1.00  8.27           O  
HETATM 3762  O   HOH A5210      18.113  31.379  50.043  1.00  6.09           O  
HETATM 3763  O   HOH A5211      19.601  49.904  45.505  1.00 14.57           O  
HETATM 3764  O   HOH A5212      17.640  44.259  41.227  1.00 11.62           O  
HETATM 3765  O   HOH A5213      26.577  35.034  28.454  1.00 22.78           O  
HETATM 3766  O   HOH A5214      19.051  42.090  37.801  1.00 13.00           O  
HETATM 3767  O   HOH A5215      19.327  32.531  40.582  1.00 20.33           O  
HETATM 3768  O   HOH A5216      26.588  43.055  39.716  1.00 19.30           O  
HETATM 3769  O   HOH A5217       0.481  43.080  47.586  1.00 20.40           O  
HETATM 3770  O   HOH A5218      11.878  32.015  51.039  1.00 24.26           O  
HETATM 3771  O   HOH A5219      17.089  37.022  45.864  1.00 10.77           O  
HETATM 3772  O   HOH A5220      20.815  33.166  43.981  1.00 18.05           O  
HETATM 3773  O   HOH A5221      17.718  55.166  66.814  1.00 17.67           O  
HETATM 3774  O   HOH A5222      20.765  30.725  56.395  1.00 17.52           O  
HETATM 3775  O   HOH A5223      17.154  38.082  35.977  1.00 10.00           O  
HETATM 3776  O   HOH A5224       5.471  43.909  35.726  1.00 20.98           O  
HETATM 3777  O   HOH A5225       1.924  55.153  48.146  1.00 19.77           O  
HETATM 3778  O   HOH A5226      18.331  55.929  21.778  1.00 28.41           O  
HETATM 3779  O   HOH A5227      42.521  28.860  53.106  1.00 20.65           O  
HETATM 3780  O   HOH A5228      33.340  41.707  60.698  1.00 38.79           O  
HETATM 3781  O   HOH A5229      25.014  40.519  38.303  1.00 24.61           O  
HETATM 3782  O   HOH A5230      26.903  53.024  55.768  1.00 25.81           O  
HETATM 3783  O   HOH A5231      22.870  35.687  59.381  1.00 22.07           O  
HETATM 3784  O   HOH A5232      18.777  58.191  66.188  1.00 22.35           O  
HETATM 3785  O   HOH A5233      15.190  16.361  39.915  1.00 22.69           O  
HETATM 3786  O   HOH A5234      24.442  32.536  53.381  1.00 30.57           O  
HETATM 3787  O   HOH A5235      35.149  38.867  53.981  1.00 41.30           O  
HETATM 3788  O   HOH A5236      27.935  40.046  39.213  1.00 20.23           O  
HETATM 3789  O   HOH A5237       8.380  50.024  26.783  1.00 23.21           O  
HETATM 3790  O   HOH A5238      32.170  45.640  55.983  1.00 19.09           O  
HETATM 3791  O   HOH A5239       1.362  54.036  60.031  1.00 34.94           O  
HETATM 3792  O   HOH A5240      12.398  53.228  37.216  1.00 27.74           O  
HETATM 3793  O   HOH A5241      25.773  34.322  32.808  1.00 31.70           O  
HETATM 3794  O   HOH A5242       2.502  62.612  48.231  1.00 35.89           O  
HETATM 3795  O   HOH A5243      17.228  35.829  32.973  1.00 22.71           O  
HETATM 3796  O   HOH A5244      29.206  29.161  49.694  1.00 19.91           O  
HETATM 3797  O   HOH A5245      19.539  30.046  41.128  1.00 18.60           O  
HETATM 3798  O   HOH A5246       3.035  48.222  38.906  1.00 24.52           O  
HETATM 3799  O   HOH A5247      28.885  38.631  59.407  1.00 21.19           O  
HETATM 3800  O   HOH A5248      41.651  24.599  60.948  1.00 38.98           O  
HETATM 3801  O   HOH A5249       0.896  37.115  52.126  1.00 25.89           O  
HETATM 3802  O   HOH A5250      20.324  30.329  61.239  1.00 20.47           O  
HETATM 3803  O   HOH A5251      13.912  45.525  31.035  1.00 28.33           O  
HETATM 3804  O   HOH A5252      19.673  58.250  53.684  1.00 34.13           O  
HETATM 3805  O   HOH A5253      27.067  56.880  51.103  1.00 23.86           O  
HETATM 3806  O   HOH A5254      31.451  14.368  60.571  1.00 30.63           O  
HETATM 3807  O   HOH A5255      39.206  49.818  38.745  1.00 30.93           O  
HETATM 3808  O   HOH A5256       5.918  35.961  53.753  1.00 26.35           O  
HETATM 3809  O   HOH A5257      30.336  26.761  51.181  1.00 33.61           O  
HETATM 3810  O   HOH A5258      17.158  59.083  51.666  1.00 26.57           O  
HETATM 3811  O   HOH A5259      29.163  43.906  40.207  1.00 23.02           O  
HETATM 3812  O   HOH A5260      18.200  54.587  44.811  1.00 11.45           O  
HETATM 3813  O   HOH A5261      39.459  22.752  60.707  1.00 21.53           O  
HETATM 3814  O   HOH A5262      20.294  24.186  61.453  1.00 21.15           O  
HETATM 3815  O   HOH A5263       4.062  35.261  32.505  1.00 29.06           O  
HETATM 3816  O   HOH A5264      37.376  24.663  53.082  1.00 23.16           O  
HETATM 3817  O   HOH A5265      -2.869  36.097  54.371  1.00 37.90           O  
HETATM 3818  O   HOH A5266       4.941  33.697  40.298  1.00 24.98           O  
HETATM 3819  O   HOH A5267      23.782  27.985  22.155  1.00 27.76           O  
HETATM 3820  O   HOH A5268      16.822  41.285  26.352  1.00 30.24           O  
HETATM 3821  O   HOH A5269      33.420  45.309  21.092  1.00 33.61           O  
HETATM 3822  O   HOH A5270      21.167  33.695  55.788  1.00 17.22           O  
HETATM 3823  O   HOH A5271      15.898  54.347  21.563  1.00 16.97           O  
HETATM 3824  O   HOH A5272      -0.951  56.169  47.287  1.00 28.40           O  
HETATM 3825  O   HOH A5273       0.881  43.029  35.331  1.00 25.61           O  
HETATM 3826  O   HOH A5274       5.004  64.445  48.339  1.00 27.73           O  
HETATM 3827  O   HOH A5275      21.481  29.886  58.845  1.00 20.66           O  
HETATM 3828  O   HOH A5276      15.759  47.365  66.378  1.00 13.53           O  
HETATM 3829  O   HOH A5277      15.486  48.573  15.822  1.00 27.32           O  
HETATM 3830  O   HOH A5278      15.271  41.151  30.435  1.00 26.26           O  
HETATM 3831  O   HOH A5279      26.707  36.613  40.771  1.00 25.82           O  
HETATM 3832  O   HOH A5280      26.541  19.178  60.497  1.00 23.98           O  
HETATM 3833  O   HOH A5281      22.306  50.645  13.662  1.00 34.92           O  
HETATM 3834  O   HOH A5282      22.417  65.254  38.897  1.00 31.51           O  
HETATM 3835  O   HOH A5283      22.049  34.160  24.515  1.00 39.33           O  
HETATM 3836  O   HOH A5284       6.759  18.203  42.652  1.00 33.63           O  
HETATM 3837  O   HOH A5285      33.278  47.073  28.888  1.00 27.89           O  
HETATM 3838  O   HOH A5286      13.539  30.455  49.328  1.00 24.21           O  
HETATM 3839  O   HOH A5287      24.549  28.005  27.368  1.00 33.73           O  
HETATM 3840  O   HOH A5288      26.180  51.352  23.904  1.00 31.88           O  
HETATM 3841  O   HOH A5289       2.907  44.581  34.882  1.00 36.85           O  
HETATM 3842  O   HOH A5290      26.184  53.848  23.643  1.00 28.16           O  
HETATM 3843  O   HOH A5291      27.674  14.393  43.435  1.00 33.23           O  
HETATM 3844  O   HOH A5292      26.126  32.872  30.174  1.00 30.40           O  
HETATM 3845  O   HOH A5293      14.742  49.155  33.258  1.00 20.21           O  
HETATM 3846  O   HOH A5294      27.082  42.561  65.989  1.00 27.72           O  
HETATM 3847  O   HOH A5295      19.899  51.520  39.629  1.00 19.43           O  
HETATM 3848  O   HOH A5296      15.377  24.838  53.598  1.00 41.17           O  
HETATM 3849  O   HOH A5297      31.605  51.069  55.271  1.00 22.92           O  
HETATM 3850  O   HOH A5298      30.304  45.260   8.372  1.00 32.92           O  
HETATM 3851  O   HOH A5299      11.318  55.842  25.424  1.00 34.57           O  
HETATM 3852  O   HOH A5300      31.642  29.408  25.038  1.00 31.39           O  
HETATM 3853  O   HOH A5301      19.125  36.243  31.545  1.00 19.54           O  
HETATM 3854  O   HOH A5302      12.878  33.302   9.316  1.00 28.64           O  
HETATM 3855  O   HOH A5303      -1.079  27.692  48.848  1.00 33.47           O  
HETATM 3856  O   HOH A5304      37.989  34.231  65.408  1.00 27.71           O  
HETATM 3857  O   HOH A5305      30.395  41.172  39.717  1.00 27.56           O  
HETATM 3858  O   HOH A5306      19.679  60.617  54.690  1.00 39.24           O  
HETATM 3859  O   HOH A5307      34.235  37.095  58.509  1.00 32.73           O  
HETATM 3860  O   HOH A5308      26.537  30.031  53.508  1.00 33.88           O  
HETATM 3861  O   HOH A5309       9.016  63.264  50.025  1.00 38.65           O  
HETATM 3862  O   HOH A5310      31.024  58.786  27.472  1.00 27.78           O  
HETATM 3863  O   HOH A5311       5.678  58.967  54.698  1.00 37.30           O  
HETATM 3864  O   HOH A5312      25.683  59.435  53.596  1.00 35.22           O  
HETATM 3865  O   HOH A5313      11.954  18.998  33.699  1.00 35.53           O  
HETATM 3866  O   HOH A5314      -2.644  29.391  44.454  1.00 44.34           O  
HETATM 3867  O   HOH A5315      12.910  58.054  35.812  1.00 29.40           O  
HETATM 3868  O   HOH A5316       7.770  30.289  28.972  1.00 43.01           O  
HETATM 3869  O   HOH A5317      11.488  21.832  29.853  1.00 44.46           O  
HETATM 3870  O   HOH A5318      27.833  33.922  38.805  1.00 40.30           O  
HETATM 3871  O   HOH A5319      24.041  44.082  66.064  1.00 28.46           O  
HETATM 3872  O   HOH A5320      19.367  52.258  43.737  1.00 19.67           O  
HETATM 3873  O   HOH A5321      15.919  31.137  48.346  1.00 18.29           O  
HETATM 3874  O   HOH A5322       9.795  51.691  29.531  1.00 42.83           O  
HETATM 3875  O   HOH A5323      25.013  48.795  14.044  1.00 35.76           O  
HETATM 3876  O   HOH A5324      30.696  29.182  12.944  1.00 45.29           O  
HETATM 3877  O   HOH A5325      33.671  58.394  34.833  1.00 35.54           O  
HETATM 3878  O   HOH A5326       7.543  37.523  26.845  1.00 32.34           O  
HETATM 3879  O   HOH A5327      19.557  31.242  38.162  1.00 30.86           O  
HETATM 3880  O   HOH A5328      34.125  16.670  38.229  1.00 33.23           O  
HETATM 3881  O   HOH A5329      14.393  60.741  59.682  1.00 29.68           O  
HETATM 3882  O   HOH A5330      19.722  57.068  25.855  1.00 46.39           O  
HETATM 3883  O   HOH A5331      21.811  50.858  18.913  1.00 28.46           O  
HETATM 3884  O   HOH A5332      11.193  39.825  26.539  1.00 39.81           O  
HETATM 3885  O   HOH A5333      30.077  32.197  39.748  1.00 38.31           O  
HETATM 3886  O   HOH A5334      10.441  41.644  22.480  1.00 31.75           O  
HETATM 3887  O   HOH A5335      34.046  58.260  30.567  1.00 42.65           O  
HETATM 3888  O   HOH A5336      24.660  36.556  36.681  1.00 47.90           O  
HETATM 3889  O   HOH A5337      25.388  32.154  25.050  1.00 38.24           O  
HETATM 3890  O   HOH A5338      26.205  54.932  66.228  1.00 38.35           O  
HETATM 3891  O   HOH A5339      31.159  48.143  19.802  1.00 37.81           O  
HETATM 3892  O   HOH A5340      46.144  21.240  44.947  1.00 41.21           O  
HETATM 3893  O   HOH A5341      34.697  15.452  47.611  1.00 30.06           O  
HETATM 3894  O   HOH A5342      17.691  59.666  59.723  1.00 15.53           O  
HETATM 3895  O   HOH A5343       6.567  58.944  42.331  1.00 46.80           O  
HETATM 3896  O   HOH A5344       0.756  25.788  48.627  1.00 36.27           O  
HETATM 3897  O   HOH A5345       1.114  40.156  51.222  1.00 31.06           O  
HETATM 3898  O   HOH A5346      26.805  36.780  34.994  1.00 48.17           O  
HETATM 3899  O   HOH A5347      23.593  33.054  40.674  1.00 40.69           O  
HETATM 3900  O   HOH A5348      42.027  54.756  39.384  1.00 37.53           O  
HETATM 3901  O   HOH A5349       7.021  49.081  31.453  1.00 31.20           O  
HETATM 3902  O   HOH A5350       3.435  37.224  53.312  1.00 33.54           O  
HETATM 3903  O   HOH A5351      36.851  30.159  44.895  1.00 31.11           O  
HETATM 3904  O   HOH A5352      35.231  38.719  49.967  1.00 31.40           O  
HETATM 3905  O   HOH A5353      27.040  14.074  52.709  1.00 34.25           O  
HETATM 3906  O   HOH A5354      14.195  21.951  30.753  1.00 41.46           O  
HETATM 3907  O   HOH A5355      28.004  16.703  59.643  1.00 30.01           O  
HETATM 3908  O   HOH A5356      43.139  26.938  55.470  1.00 52.24           O  
HETATM 3909  O   HOH A5357       7.288  34.801  59.017  1.00 44.56           O  
HETATM 3910  O   HOH A5358      45.377  28.701  40.853  1.00 30.63           O  
HETATM 3911  O   HOH A5359      35.647  50.402  34.402  1.00 40.30           O  
HETATM 3912  O   HOH A5360      24.172  63.337  38.699  1.00 32.68           O  
HETATM 3913  O   HOH A5361      -1.461  43.764  40.307  1.00 31.44           O  
HETATM 3914  O   HOH A5362      -2.139  40.875  40.721  1.00 31.48           O  
HETATM 3915  O   HOH A5363       8.600  25.700  30.261  1.00 47.17           O  
HETATM 3916  O   HOH A5364      29.785  60.400  49.274  1.00 32.66           O  
HETATM 3917  O   HOH A5365       7.913  42.366  33.009  1.00 29.24           O  
HETATM 3918  O   HOH A5366      -2.502  49.329  38.608  1.00 39.48           O  
HETATM 3919  O   HOH A5367      -5.449  31.749  50.810  1.00 31.12           O  
HETATM 3920  O   HOH A5368      13.088  48.317  31.382  1.00 29.41           O  
HETATM 3921  O   HOH A5369      39.396  33.099  48.821  1.00 26.83           O  
HETATM 3922  O   HOH A5370       8.886  19.631  41.347  1.00 37.62           O  
HETATM 3923  O   HOH A5371      21.940  52.884  23.081  1.00 32.99           O  
HETATM 3924  O   HOH A5372       2.391  25.273  54.992  1.00 39.27           O  
HETATM 3925  O   HOH A5373      17.943  23.628  39.406  1.00 41.35           O  
HETATM 3926  O   HOH A5374       9.106  35.600  17.747  1.00 32.44           O  
HETATM 3927  O   HOH A5375      22.338  51.648  16.623  1.00 31.03           O  
HETATM 3928  O   HOH A5376      13.529  22.794  50.788  1.00 37.96           O  
HETATM 3929  O   HOH A5377      35.803  36.182  28.421  1.00 33.55           O  
HETATM 3930  O   HOH A5378      35.256  33.364  34.631  1.00 36.10           O  
HETATM 3931  O   HOH A5379      15.516  16.702  47.846  1.00 44.85           O  
HETATM 3932  O   HOH A5380      24.754  34.875  26.059  1.00 11.29           O  
HETATM 3933  O   HOH A5381      19.859  27.093  58.556  1.00 27.66           O  
HETATM 3934  O   HOH A5382      22.992  33.838  45.814  1.00 29.58           O  
HETATM 3935  O   HOH A5383      21.853  36.175  56.145  1.00 27.92           O  
HETATM 3936  O   HOH A5384      11.518  55.144  28.294  1.00 31.45           O  
HETATM 3937  O   HOH A5385      27.349  37.687  38.740  1.00 33.85           O  
HETATM 3938  O   HOH A5386      32.882  23.242  39.432  1.00 38.61           O  
HETATM 3939  O   HOH A5387      14.051  25.310  51.178  1.00 29.17           O  
HETATM 3940  O   HOH A5388       4.087  26.989  55.106  1.00 28.07           O  
HETATM 3941  O   HOH A5389      20.265  56.463  43.836  1.00 24.38           O  
HETATM 3942  O   HOH A5390       2.361  33.077  40.547  1.00 40.91           O  
HETATM 3943  O   HOH A5391      31.720  28.661  27.544  1.00 35.03           O  
HETATM 3944  O   HOH A5392      29.908  38.943  65.013  1.00 39.10           O  
HETATM 3945  O   HOH A5393      25.597  34.343  55.408  1.00 21.52           O  
HETATM 3946  O   HOH A5394      34.595  26.379  43.172  1.00 30.58           O  
HETATM 3947  O   HOH A5395      14.395  19.321  34.049  1.00 36.84           O  
HETATM 3948  O   HOH A5396      19.962  54.430  23.657  1.00 33.48           O  
HETATM 3949  O   HOH A5397      22.997  19.980  45.334  1.00 32.67           O  
HETATM 3950  O   HOH A5398       9.758  49.247  30.315  1.00 33.44           O  
HETATM 3951  O   HOH A5399      22.178  17.529  51.375  1.00 41.77           O  
HETATM 3952  O   HOH A5400      24.497  48.998  39.707  1.00 39.36           O  
HETATM 3953  O   HOH A5401      24.154  55.698  23.764  1.00 31.45           O  
HETATM 3954  O   HOH A5402      12.545  55.257  40.805  1.00 30.79           O  
HETATM 3955  O   HOH A5403       4.765  52.942  38.418  1.00 31.25           O  
HETATM 3956  O   HOH A5404      -1.066  41.274  48.244  1.00 30.76           O  
HETATM 3957  O   HOH A5405      31.808  31.856  24.132  1.00 37.70           O  
HETATM 3958  O   HOH A5406      23.236  52.032  20.771  1.00 28.70           O  
HETATM 3959  O   HOH A5407      35.921  23.001  35.303  1.00 36.52           O  
HETATM 3960  O   HOH A5408      33.766  14.194  49.572  1.00 60.20           O  
HETATM 3961  O   HOH A5409      29.304  30.295  46.702  1.00 34.80           O  
HETATM 3962  O   HOH A5410      -1.997  38.172  52.049  1.00 37.03           O  
HETATM 3963  O   HOH A5411       8.136  40.251  23.203  1.00 39.30           O  
HETATM 3964  O   HOH A5412      39.714  43.827  46.534  1.00 39.54           O  
HETATM 3965  O   HOH A5413      27.316  33.195  36.446  1.00 38.28           O  
HETATM 3966  O   HOH A5414      44.533  26.002  41.496  1.00 39.88           O  
HETATM 3967  O   HOH A5415      14.223  35.795  12.169  1.00 48.65           O  
HETATM 3968  O   HOH A5416      36.734  37.602  46.681  1.00 41.38           O  
HETATM 3969  O   HOH A5417       2.614  25.323  41.931  1.00 43.18           O  
HETATM 3970  O   HOH A5418      24.268  30.320  26.396  1.00 39.45           O  
HETATM 3971  O   HOH A5419      -0.433  43.836  37.852  1.00 43.36           O  
HETATM 3972  O   HOH A5420      41.066  55.614  51.352  1.00 32.03           O  
HETATM 3973  O   HOH A5421      35.609  48.204  53.873  1.00 30.74           O  
HETATM 3974  O   HOH A5422       0.167  45.102  55.510  1.00 42.81           O  
HETATM 3975  O   HOH A5423      21.865  30.581  18.751  1.00 31.03           O  
HETATM 3976  O   HOH A5424      -1.276  47.291  36.941  1.00 35.24           O  
HETATM 3977  O   HOH A5425      19.047  44.046  29.502  1.00 48.42           O  
HETATM 3978  O   HOH A5426      24.002  31.509  29.568  1.00 36.70           O  
HETATM 3979  O   HOH A5427       5.407  35.364  56.313  1.00 36.77           O  
HETATM 3980  O   HOH A5428       6.964  41.419  60.237  1.00 19.50           O  
HETATM 3981  O   HOH A5429      11.094  55.436  33.352  1.00 40.14           O  
HETATM 3982  O   HOH A5430      19.807  23.687  46.412  1.00 35.33           O  
HETATM 3983  O   HOH A5431      10.286  54.070  39.651  1.00 37.35           O  
CONECT   74   81                                                                
CONECT   81   74   82                                                           
CONECT   82   81   83   85                                                      
CONECT   83   82   84   89                                                      
CONECT   84   83                                                                
CONECT   85   82   86                                                           
CONECT   86   85   87                                                           
CONECT   87   86   88                                                           
CONECT   88   87                                                                
CONECT   89   83                                                                
CONECT  228  233                                                                
CONECT  233  228  234                                                           
CONECT  234  233  235  237                                                      
CONECT  235  234  236  241                                                      
CONECT  236  235                                                                
CONECT  237  234  238                                                           
CONECT  238  237  239                                                           
CONECT  239  238  240                                                           
CONECT  240  239                                                                
CONECT  241  235                                                                
CONECT  329  335                                                                
CONECT  335  329  336                                                           
CONECT  336  335  337  339                                                      
CONECT  337  336  338  343                                                      
CONECT  338  337                                                                
CONECT  339  336  340                                                           
CONECT  340  339  341                                                           
CONECT  341  340  342                                                           
CONECT  342  341                                                                
CONECT  343  337                                                                
CONECT  586  588                                                                
CONECT  588  586  589                                                           
CONECT  589  588  590  592                                                      
CONECT  590  589  591  596                                                      
CONECT  591  590                                                                
CONECT  592  589  593                                                           
CONECT  593  592  594                                                           
CONECT  594  593  595                                                           
CONECT  595  594                                                                
CONECT  596  590                                                                
CONECT  897  906                                                                
CONECT  906  897  907                                                           
CONECT  907  906  908  910                                                      
CONECT  908  907  909  914                                                      
CONECT  909  908                                                                
CONECT  910  907  911                                                           
CONECT  911  910  912                                                           
CONECT  912  911  913                                                           
CONECT  913  912                                                                
CONECT  914  908                                                                
CONECT  916  922                                                                
CONECT  922  916  923                                                           
CONECT  923  922  924  926                                                      
CONECT  924  923  925  930                                                      
CONECT  925  924                                                                
CONECT  926  923  927                                                           
CONECT  927  926  928                                                           
CONECT  928  927  929                                                           
CONECT  929  928                                                                
CONECT  930  924                                                                
CONECT 1174 1180                                                                
CONECT 1180 1174 1181                                                           
CONECT 1181 1180 1182 1184                                                      
CONECT 1182 1181 1183 1188                                                      
CONECT 1183 1182                                                                
CONECT 1184 1181 1185                                                           
CONECT 1185 1184 1186                                                           
CONECT 1186 1185 1187                                                           
CONECT 1187 1186                                                                
CONECT 1188 1182                                                                
CONECT 1602 1612                                                                
CONECT 1612 1602 1613                                                           
CONECT 1613 1612 1614 1616                                                      
CONECT 1614 1613 1615 1620                                                      
CONECT 1615 1614                                                                
CONECT 1616 1613 1617                                                           
CONECT 1617 1616 1618                                                           
CONECT 1618 1617 1619                                                           
CONECT 1619 1618                                                                
CONECT 1620 1614                                                                
CONECT 1754 1764                                                                
CONECT 1764 1754 1765                                                           
CONECT 1765 1764 1766 1768                                                      
CONECT 1766 1765 1767 1772                                                      
CONECT 1767 1766                                                                
CONECT 1768 1765 1769                                                           
CONECT 1769 1768 1770                                                           
CONECT 1770 1769 1771                                                           
CONECT 1771 1770                                                                
CONECT 1772 1766                                                                
CONECT 1837 1843                                                                
CONECT 1843 1837 1844                                                           
CONECT 1844 1843 1845 1847                                                      
CONECT 1845 1844 1846 1851                                                      
CONECT 1846 1845                                                                
CONECT 1847 1844 1848                                                           
CONECT 1848 1847 1849                                                           
CONECT 1849 1848 1850                                                           
CONECT 1850 1849                                                                
CONECT 1851 1845                                                                
CONECT 2219 2225                                                                
CONECT 2225 2219 2226                                                           
CONECT 2226 2225 2227 2229                                                      
CONECT 2227 2226 2228 2233                                                      
CONECT 2228 2227                                                                
CONECT 2229 2226 2230                                                           
CONECT 2230 2229 2231                                                           
CONECT 2231 2230 2232                                                           
CONECT 2232 2231                                                                
CONECT 2233 2227                                                                
CONECT 2462 2467                                                                
CONECT 2467 2462 2468                                                           
CONECT 2468 2467 2469 2471                                                      
CONECT 2469 2468 2470 2475                                                      
CONECT 2470 2469                                                                
CONECT 2471 2468 2472                                                           
CONECT 2472 2471 2473                                                           
CONECT 2473 2472 2474                                                           
CONECT 2474 2473                                                                
CONECT 2475 2469                                                                
CONECT 2729 2732                                                                
CONECT 2732 2729 2733                                                           
CONECT 2733 2732 2734 2736                                                      
CONECT 2734 2733 2735 2740                                                      
CONECT 2735 2734                                                                
CONECT 2736 2733 2737                                                           
CONECT 2737 2736 2738                                                           
CONECT 2738 2737 2739                                                           
CONECT 2739 2738                                                                
CONECT 2740 2734                                                                
CONECT 2764 2767                                                                
CONECT 2767 2764 2768                                                           
CONECT 2768 2767 2769 2771                                                      
CONECT 2769 2768 2770 2775                                                      
CONECT 2770 2769                                                                
CONECT 2771 2768 2772                                                           
CONECT 2772 2771 2773                                                           
CONECT 2773 2772 2774                                                           
CONECT 2774 2773                                                                
CONECT 2775 2769                                                                
CONECT 3236 3243                                                                
CONECT 3243 3236 3244                                                           
CONECT 3244 3243 3245 3247                                                      
CONECT 3245 3244 3246 3251                                                      
CONECT 3246 3245                                                                
CONECT 3247 3244 3248                                                           
CONECT 3248 3247 3249                                                           
CONECT 3249 3248 3250                                                           
CONECT 3250 3249                                                                
CONECT 3251 3245 3252                                                           
CONECT 3252 3251 3253 3255                                                      
CONECT 3253 3252 3254 3259                                                      
CONECT 3254 3253                                                                
CONECT 3255 3252 3256                                                           
CONECT 3256 3255 3257                                                           
CONECT 3257 3256 3258                                                           
CONECT 3258 3257                                                                
CONECT 3259 3253                                                                
CONECT 3723 3724 3728 3731                                                      
CONECT 3724 3723 3725 3729                                                      
CONECT 3725 3724 3726                                                           
CONECT 3726 3725 3727 3730                                                      
CONECT 3727 3726 3728                                                           
CONECT 3728 3723 3727                                                           
CONECT 3729 3724                                                                
CONECT 3730 3726                                                                
CONECT 3731 3723 3732 3736                                                      
CONECT 3732 3731 3733 3734                                                      
CONECT 3733 3732                                                                
CONECT 3734 3732 3735 3737                                                      
CONECT 3735 3734 3736 3738                                                      
CONECT 3736 3731 3735                                                           
CONECT 3737 3734                                                                
CONECT 3738 3735 3739                                                           
CONECT 3739 3738 3740                                                           
CONECT 3740 3739 3741 3742 3743                                                 
CONECT 3741 3740                                                                
CONECT 3742 3740                                                                
CONECT 3743 3740 3744                                                           
CONECT 3744 3743 3745 3746 3747                                                 
CONECT 3745 3744                                                                
CONECT 3746 3744                                                                
CONECT 3747 3744 3748                                                           
CONECT 3748 3747 3749 3757                                                      
CONECT 3749 3748 3750 3754                                                      
CONECT 3750 3749 3751 3755                                                      
CONECT 3751 3750 3752 3756                                                      
CONECT 3752 3751 3753 3757                                                      
CONECT 3753 3752 3758                                                           
CONECT 3754 3749                                                                
CONECT 3755 3750                                                                
CONECT 3756 3751                                                                
CONECT 3757 3748 3752                                                           
CONECT 3758 3753                                                                
MASTER      306    0   17   24   28    0    8    6 3982    1  194   39          
END                                                                             



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