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***  HYDROLASE 09-DEC-03 1V73  ***

elNémo ID: 220423181448104789

Job options:

ID        	=	 220423181448104789
JOBID     	=	 HYDROLASE 09-DEC-03 1V73
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    HYDROLASE                               09-DEC-03   1V73              
TITLE     CRYSTAL STRUCTURE OF COLD-ACTIVE PROTEIN-TYROSINE                     
TITLE    2 PHOSPHATASE OF A PSYCHROPHILE SHEWANELLA SP.                         
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PSYCHROPHILIC PHOSPHATASE I;                               
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: PROTEIN-TYROSINE-PHOSPHATASE;                               
COMPND   5 EC: 3.1.3.48;                                                        
COMPND   6 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: SHEWANELLA SP.;                                 
SOURCE   3 ORGANISM_TAXID: 50422;                                               
SOURCE   4 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   5 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   6 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   7 EXPRESSION_SYSTEM_PLASMID: PET22B                                    
KEYWDS    COLD-ACTIVE ENZYME, PSYCHROPHILE, PROTEIN-TYROSINE                    
KEYWDS   2 PHOSPHATASE, SHEWANELLA SP, HYDROLASE                                
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    H.TSURUTA,B.MIKAMI,Y.AIZONO                                           
REVDAT   2   24-FEB-09 1V73    1       VERSN                                    
REVDAT   1   01-MAR-05 1V73    0                                                
JRNL        AUTH   H.TSURUTA,B.MIKAMI,Y.AIZONO                                  
JRNL        TITL   CRYSTAL STRUCTURE OF COLD-ACTIVE PROTEIN-TYROSINE            
JRNL        TITL 2 PHOSPHATASE FROM A PSYCHROPHILE, SHEWANELLA SP               
JRNL        REF    J.BIOCHEM.(TOKYO)             V. 137    69 2005              
JRNL        REFN                   ISSN 0021-924X                               
JRNL        PMID   15713885                                                     
JRNL        DOI    10.1093/JB/MVI010                                            
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.82 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 : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.82                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.93                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 576049.930                     
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 84.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 27393                          
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) : 0.177                           
REMARK   3   FREE R VALUE                     : 0.226                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 10.000                          
REMARK   3   FREE R VALUE TEST SET COUNT      : 2740                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.004                           
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) : 1.82                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.93                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 57.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 2762                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1960                       
REMARK   3   BIN FREE R VALUE                    : 0.2640                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 9.00                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 272                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.016                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2651                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 2                                       
REMARK   3   SOLVENT ATOMS            : 451                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 4.90                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 13.40                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 3.96000                                              
REMARK   3    B22 (A**2) : -3.15000                                             
REMARK   3    B33 (A**2) : -0.81000                                             
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) : 0.18                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.10                            
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) : 0.24                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.14                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.30                            
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.10                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.67                            
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) : 1.200 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.750 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.900 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.640 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.35                                                 
REMARK   3   BSOL        : 39.84                                                
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  : CARBOHYDRATE.PARAM                             
REMARK   3  PARAMETER FILE  4  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  5  : ACYL.PARAM                                     
REMARK   3  PARAMETER FILE  6  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  3   : CARBOHYDRATE.TOP                               
REMARK   3  TOPOLOGY FILE  4   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  5   : ACYL.TOP                                       
REMARK   3  TOPOLOGY FILE  6   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1V73 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 11-DEC-03.                  
REMARK 100 THE RCSB ID CODE IS RCSB006288.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 28-DEC-01                          
REMARK 200  TEMPERATURE           (KELVIN) : 103                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : SIEMENS                            
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : AREA DETECTOR                      
REMARK 200  DETECTOR MANUFACTURER          : SIEMENS HI-STAR                    
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : SADIE                              
REMARK 200  DATA SCALING SOFTWARE          : SAINT                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 29747                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.820                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.930                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 1.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 91.4                               
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) : 1.82                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.93                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 76.3                               
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: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: PHASES                                                
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 47.50                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.36                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 30% PEG4000, 0.1M TRIS-HCL, 0.2M         
REMARK 280  AMMONIUM ACETATE, PH 8.5, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       28.25150            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.51200            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       38.38550            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       40.51200            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       28.25150            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       38.38550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 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     MET A     1                                                      
REMARK 465     GLY A     2                                                      
REMARK 465     ASN A     3                                                      
REMARK 465     THR A     4                                                      
REMARK 465     ALA A     5                                                      
REMARK 465     GLU A   337                                                      
REMARK 465     ASN A   338                                                      
REMARK 465     SER A   339                                                      
REMARK 465     LEU A   340                                                      
REMARK 465     ASN A   341                                                      
REMARK 465     GLN A   342                                                      
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    LEU A  39       11.40     56.63                                   
REMARK 500    THR A 112       44.83    -75.00                                   
REMARK 500    ASP A 117      153.78     68.76                                   
REMARK 500    ARG A 118      -59.52     76.15                                   
REMARK 500    ARG A 175      146.11   -173.92                                   
REMARK 500    ASN A 201     -127.75     58.35                                   
REMARK 500    PHE A 250     -163.38   -124.64                                   
REMARK 500    HIS A 286      -50.57     64.67                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 548        DISTANCE = 10.36 ANGSTROMS                       
REMARK 525    HOH A 567        DISTANCE =  6.61 ANGSTROMS                       
REMARK 525    HOH A 594        DISTANCE =  7.35 ANGSTROMS                       
REMARK 525    HOH A 595        DISTANCE =  6.34 ANGSTROMS                       
REMARK 525    HOH A 607        DISTANCE =  5.25 ANGSTROMS                       
REMARK 525    HOH A 698        DISTANCE =  5.95 ANGSTROMS                       
REMARK 525    HOH A 699        DISTANCE =  6.31 ANGSTROMS                       
REMARK 525    HOH A 793        DISTANCE =  8.75 ANGSTROMS                       
REMARK 525    HOH A 822        DISTANCE =  5.31 ANGSTROMS                       
REMARK 525    HOH A 823        DISTANCE =  5.33 ANGSTROMS                       
REMARK 525    HOH A 824        DISTANCE =  5.16 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620  (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;              
REMARK 620  SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                            
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2001  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ASP A  78   OD1                                                    
REMARK 620 2 HIS A  80   NE2 113.4                                              
REMARK 620 3 HOH A 772   O    85.8  95.2                                        
REMARK 620 4 HOH A 774   O    83.8 162.6  88.8                                  
REMARK 620 5 ASP A 114   OD1  86.3  97.7 166.8  79.8                            
REMARK 620 6  CA A2002  CA    88.8 136.0 125.1  36.4  44.0                      
REMARK 620 7 ACY A1001   O   153.6  92.9  89.0  70.2  93.4  73.2                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              CA A2002  CA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH A 774   O                                                      
REMARK 620 2 ASP A 114   OD1  76.0                                              
REMARK 620 3 HIS A 207   NE2 104.6  80.6                                        
REMARK 620 4 HIS A 286   ND1  85.8 159.3  94.7                                  
REMARK 620 5 ASN A 149   ND2 158.4  94.7  92.8 105.7                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2001                 
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CA A 2002                 
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ACY A 1001                
DBREF  1V73 A    3   342  UNP    Q9S427   Q9S427_9GAMM    22    361             
SEQADV 1V73 MET A    1  UNP  Q9S427              CLONING ARTIFACT               
SEQADV 1V73 GLY A    2  UNP  Q9S427              CLONING ARTIFACT               
SEQRES   1 A  342  MET GLY ASN THR ALA THR GLU PHE ASP GLY PRO TYR VAL          
SEQRES   2 A  342  ILE THR PRO ILE SER GLY GLN SER THR ALA TYR TRP ILE          
SEQRES   3 A  342  CYS ASP ASN ARG LEU LYS THR THR SER ILE GLU LYS LEU          
SEQRES   4 A  342  GLN VAL ASN ARG PRO GLU HIS CYS GLY ASP LEU PRO GLU          
SEQRES   5 A  342  THR LYS LEU SER SER GLU ILE LYS GLN ILE MET PRO ASP          
SEQRES   6 A  342  THR TYR LEU GLY ILE LYS LYS VAL VAL ALA LEU SER ASP          
SEQRES   7 A  342  VAL HIS GLY GLN TYR ASP VAL LEU LEU THR LEU LEU LYS          
SEQRES   8 A  342  LYS GLN LYS ILE ILE ASP SER ASP GLY ASN TRP ALA PHE          
SEQRES   9 A  342  GLY GLU GLY HIS MET VAL MET THR GLY ASP ILE PHE ASP          
SEQRES  10 A  342  ARG GLY HIS GLN VAL ASN GLU VAL LEU TRP PHE MET TYR          
SEQRES  11 A  342  GLN LEU ASP GLN GLN ALA ARG ASP ALA GLY GLY MET VAL          
SEQRES  12 A  342  HIS LEU LEU MET GLY ASN HIS GLU GLN MET VAL LEU GLY          
SEQRES  13 A  342  GLY ASP LEU ARG TYR VAL HIS GLN ARG TYR ASP ILE ALA          
SEQRES  14 A  342  THR THR LEU ILE ASN ARG PRO TYR ASN LYS LEU TYR GLY          
SEQRES  15 A  342  ALA ASP THR GLU ILE GLY GLN TRP LEU ARG SER LYS ASN          
SEQRES  16 A  342  THR ILE ILE LYS ILE ASN ASP VAL LEU TYR MET HIS GLY          
SEQRES  17 A  342  GLY ILE SER SER GLU TRP ILE SER ARG GLU LEU THR LEU          
SEQRES  18 A  342  ASP LYS ALA ASN ALA LEU TYR ARG ALA ASN VAL ASP ALA          
SEQRES  19 A  342  SER LYS LYS SER LEU LYS ALA ASP ASP LEU LEU ASN PHE          
SEQRES  20 A  342  LEU PHE PHE GLY ASN GLY PRO THR TRP TYR ARG GLY TYR          
SEQRES  21 A  342  PHE SER GLU THR PHE THR GLU ALA GLU LEU ASP THR ILE          
SEQRES  22 A  342  LEU GLN HIS PHE ASN VAL ASN HIS ILE VAL VAL GLY HIS          
SEQRES  23 A  342  THR SER GLN GLU ARG VAL LEU GLY LEU PHE HIS ASN LYS          
SEQRES  24 A  342  VAL ILE ALA VAL ASP SER SER ILE LYS VAL GLY LYS SER          
SEQRES  25 A  342  GLY GLU LEU LEU LEU LEU GLU ASN ASN ARG LEU ILE ARG          
SEQRES  26 A  342  GLY LEU TYR ASP GLY THR ARG GLU THR LEU GLN GLU ASN          
SEQRES  27 A  342  SER LEU ASN GLN                                              
HET     CA  A2001       1                                                       
HET     CA  A2002       1                                                       
HET    ACY  A1001       4                                                       
HETNAM      CA CALCIUM ION                                                      
HETNAM     ACY ACETIC ACID                                                      
FORMUL   2   CA    2(CA 2+)                                                     
FORMUL   4  ACY    C2 H4 O2                                                     
FORMUL   5  HOH   *447(H2 O)                                                    
HELIX    1   1 SER A   57  GLN A   61  5                                   5    
HELIX    2   2 GLN A   82  GLN A   93  1                                  12    
HELIX    3   3 GLN A  121  ALA A  139  1                                  19    
HELIX    4   4 GLY A  148  GLY A  157  1                                  10    
HELIX    5   5 HIS A  163  ARG A  165  5                                   3    
HELIX    6   6 TYR A  166  ILE A  173  1                                   8    
HELIX    7   7 PRO A  176  GLY A  182  5                                   7    
HELIX    8   8 THR A  185  ARG A  192  1                                   8    
HELIX    9   9 SER A  212  ARG A  217  1                                   6    
HELIX   10  10 THR A  220  VAL A  232  1                                  13    
HELIX   11  11 SER A  235  ASP A  242  1                                   8    
HELIX   12  12 ASP A  242  PHE A  250  1                                   9    
HELIX   13  13 ARG A  258  SER A  262  5                                   5    
HELIX   14  14 THR A  266  ASN A  278  1                                  13    
HELIX   15  15 SER A  306  GLY A  310  5                                   5    
SHEET    1   A 3 PHE A   8  ILE A  14  0                                        
SHEET    2   A 3 THR A  22  CYS A  27 -1  O  ILE A  26   N  ASP A   9           
SHEET    3   A 3 ARG A  30  SER A  35 -1  O  ARG A  30   N  CYS A  27           
SHEET    1   B 2 GLN A  40  VAL A  41  0                                        
SHEET    2   B 2 THR A  53  LYS A  54 -1  O  THR A  53   N  VAL A  41           
SHEET    1   C 6 THR A  66  TYR A  67  0                                        
SHEET    2   C 6 ILE A 197  ILE A 200  1  O  LYS A 199   N  TYR A  67           
SHEET    3   C 6 VAL A 203  MET A 206 -1  O  TYR A 205   N  ILE A 198           
SHEET    4   C 6 HIS A 281  VAL A 284  1  O  VAL A 283   N  LEU A 204           
SHEET    5   C 6 VAL A 300  ALA A 302  1  O  ILE A 301   N  ILE A 282           
SHEET    6   C 6 LEU A 293  LEU A 295 -1  N  LEU A 293   O  ALA A 302           
SHEET    1   D 6 MET A 142  LEU A 145  0                                        
SHEET    2   D 6 HIS A 108  MET A 111  1  N  MET A 109   O  HIS A 144           
SHEET    3   D 6 LYS A  72  LEU A  76  1  N  VAL A  74   O  VAL A 110           
SHEET    4   D 6 LEU A 315  GLU A 319 -1  O  LEU A 318   N  VAL A  73           
SHEET    5   D 6 ARG A 322  GLY A 326 -1  O  GLY A 326   N  LEU A 315           
SHEET    6   D 6 ARG A 332  THR A 334 -1  O  GLU A 333   N  ARG A 325           
SSBOND   1 CYS A   27    CYS A   47                          1555   1555  2.03  
LINK        CA    CA A2001                 OD1 ASP A  78     1555   1555  1.98  
LINK        CA    CA A2001                 NE2 HIS A  80     1555   1555  2.10  
LINK        CA    CA A2001                 O   HOH A 772     1555   1555  2.17  
LINK        CA    CA A2001                 O   HOH A 774     1555   1555  2.08  
LINK        CA    CA A2001                 OD1 ASP A 114     1555   1555  2.20  
LINK        CA    CA A2001                CA    CA A2002     1555   1555  3.37  
LINK        CA    CA A2001                 O   ACY A1001     1555   1555  2.68  
LINK        CA    CA A2002                 O   HOH A 774     1555   1555  2.09  
LINK        CA    CA A2002                 OD1 ASP A 114     1555   1555  2.35  
LINK        CA    CA A2002                 NE2 HIS A 207     1555   1555  2.04  
LINK        CA    CA A2002                 ND1 HIS A 286     1555   1555  2.19  
LINK        CA    CA A2002                 ND2 ASN A 149     1555   1555  2.02  
CISPEP   1 GLY A   10    PRO A   11          0         0.26                     
SITE     1 AC1  7 ASP A  78  HIS A  80  ASP A 114  HOH A 772                    
SITE     2 AC1  7 HOH A 774  ACY A1001   CA A2002                               
SITE     1 AC2  7 ASP A 114  ASN A 149  HIS A 207  HIS A 286                    
SITE     2 AC2  7 HOH A 774  ACY A1001   CA A2001                               
SITE     1 AC3 11 HIS A  80  ASP A 114  ARG A 118  ASN A 149                    
SITE     2 AC3 11 HIS A 150  ARG A 258  HIS A 286  HOH A 758                    
SITE     3 AC3 11 HOH A 774   CA A2001   CA A2002                               
CRYST1   56.503   76.771   81.024  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017698  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013026  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012342        0.00000                         
ATOM      1  N   THR A   6      40.951  22.381 -15.840  1.00 33.97           N  
ATOM      2  CA  THR A   6      40.186  23.568 -15.353  1.00 33.55           C  
ATOM      3  C   THR A   6      40.459  23.789 -13.858  1.00 31.33           C  
ATOM      4  O   THR A   6      40.048  22.995 -13.010  1.00 32.97           O  
ATOM      5  CB  THR A   6      38.662  23.379 -15.619  1.00 34.26           C  
ATOM      6  OG1 THR A   6      37.971  24.607 -15.358  1.00 37.44           O  
ATOM      7  CG2 THR A   6      38.084  22.275 -14.745  1.00 35.62           C  
ATOM      8  N   GLU A   7      41.163  24.874 -13.546  1.00 28.52           N  
ATOM      9  CA  GLU A   7      41.524  25.197 -12.165  1.00 25.56           C  
ATOM     10  C   GLU A   7      40.875  26.466 -11.609  1.00 21.85           C  
ATOM     11  O   GLU A   7      40.877  27.511 -12.259  1.00 19.71           O  
ATOM     12  CB  GLU A   7      43.045  25.344 -12.059  1.00 27.72           C  
ATOM     13  CG  GLU A   7      43.825  24.084 -12.381  1.00 30.11           C  
ATOM     14  CD  GLU A   7      43.967  23.162 -11.186  1.00 32.05           C  
ATOM     15  OE1 GLU A   7      42.934  22.789 -10.586  1.00 32.80           O  
ATOM     16  OE2 GLU A   7      45.119  22.808 -10.849  1.00 32.54           O  
ATOM     17  N   PHE A   8      40.330  26.361 -10.399  1.00 16.17           N  
ATOM     18  CA  PHE A   8      39.709  27.493  -9.715  1.00 13.80           C  
ATOM     19  C   PHE A   8      40.351  27.599  -8.339  1.00 11.07           C  
ATOM     20  O   PHE A   8      40.549  26.590  -7.665  1.00  7.55           O  
ATOM     21  CB  PHE A   8      38.201  27.290  -9.579  1.00 14.27           C  
ATOM     22  CG  PHE A   8      37.483  27.267 -10.893  1.00 17.38           C  
ATOM     23  CD1 PHE A   8      37.630  26.188 -11.759  1.00 18.56           C  
ATOM     24  CD2 PHE A   8      36.694  28.340 -11.286  1.00 17.89           C  
ATOM     25  CE1 PHE A   8      37.002  26.180 -13.001  1.00 20.37           C  
ATOM     26  CE2 PHE A   8      36.059  28.344 -12.527  1.00 20.51           C  
ATOM     27  CZ  PHE A   8      36.213  27.263 -13.387  1.00 20.02           C  
ATOM     28  N   ASP A   9      40.673  28.818  -7.922  1.00  9.09           N  
ATOM     29  CA  ASP A   9      41.337  29.009  -6.640  1.00  6.36           C  
ATOM     30  C   ASP A   9      41.156  30.421  -6.096  1.00  7.49           C  
ATOM     31  O   ASP A   9      41.127  31.395  -6.852  1.00  6.77           O  
ATOM     32  CB  ASP A   9      42.827  28.707  -6.806  1.00  6.54           C  
ATOM     33  CG  ASP A   9      43.619  28.933  -5.534  1.00  7.09           C  
ATOM     34  OD1 ASP A   9      44.779  29.399  -5.633  1.00  6.76           O  
ATOM     35  OD2 ASP A   9      43.089  28.638  -4.443  1.00  5.37           O  
ATOM     36  N   GLY A  10      41.044  30.523  -4.776  1.00  7.98           N  
ATOM     37  CA  GLY A  10      40.872  31.820  -4.151  1.00  7.64           C  
ATOM     38  C   GLY A  10      39.659  31.889  -3.243  1.00  5.74           C  
ATOM     39  O   GLY A  10      39.058  30.869  -2.910  1.00  7.11           O  
ATOM     40  N   PRO A  11      39.257  33.099  -2.846  1.00  6.49           N  
ATOM     41  CA  PRO A  11      39.923  34.339  -3.248  1.00  5.95           C  
ATOM     42  C   PRO A  11      41.111  34.709  -2.370  1.00  5.76           C  
ATOM     43  O   PRO A  11      41.294  34.159  -1.284  1.00  3.53           O  
ATOM     44  CB  PRO A  11      38.809  35.365  -3.125  1.00  5.86           C  
ATOM     45  CG  PRO A  11      38.112  34.905  -1.882  1.00  7.21           C  
ATOM     46  CD  PRO A  11      38.038  33.387  -2.068  1.00  5.96           C  
ATOM     47  N   TYR A  12      41.914  35.642  -2.872  1.00  5.09           N  
ATOM     48  CA  TYR A  12      43.057  36.176  -2.143  1.00  6.43           C  
ATOM     49  C   TYR A  12      42.627  37.611  -1.930  1.00  6.18           C  
ATOM     50  O   TYR A  12      42.577  38.403  -2.874  1.00  7.37           O  
ATOM     51  CB  TYR A  12      44.329  36.122  -2.982  1.00  6.21           C  
ATOM     52  CG  TYR A  12      44.793  34.715  -3.263  1.00  7.37           C  
ATOM     53  CD1 TYR A  12      44.271  33.983  -4.330  1.00  4.71           C  
ATOM     54  CD2 TYR A  12      45.732  34.102  -2.443  1.00  5.02           C  
ATOM     55  CE1 TYR A  12      44.682  32.667  -4.568  1.00  6.37           C  
ATOM     56  CE2 TYR A  12      46.145  32.797  -2.669  1.00  5.67           C  
ATOM     57  CZ  TYR A  12      45.620  32.084  -3.730  1.00  6.37           C  
ATOM     58  OH  TYR A  12      46.052  30.790  -3.949  1.00  7.69           O  
ATOM     59  N   VAL A  13      42.291  37.936  -0.690  1.00  5.52           N  
ATOM     60  CA  VAL A  13      41.801  39.260  -0.363  1.00  5.34           C  
ATOM     61  C   VAL A  13      42.846  40.205   0.192  1.00  6.34           C  
ATOM     62  O   VAL A  13      43.574  39.869   1.120  1.00  6.40           O  
ATOM     63  CB  VAL A  13      40.638  39.171   0.650  1.00  3.55           C  
ATOM     64  CG1 VAL A  13      40.195  40.569   1.070  1.00  4.32           C  
ATOM     65  CG2 VAL A  13      39.476  38.407   0.032  1.00  5.93           C  
ATOM     66  N   ILE A  14      42.905  41.393  -0.397  1.00  8.36           N  
ATOM     67  CA  ILE A  14      43.820  42.431   0.046  1.00 10.65           C  
ATOM     68  C   ILE A  14      42.974  43.372   0.898  1.00 12.60           C  
ATOM     69  O   ILE A  14      41.905  43.815   0.464  1.00 12.23           O  
ATOM     70  CB  ILE A  14      44.395  43.229  -1.141  1.00 12.04           C  
ATOM     71  CG1 ILE A  14      45.060  42.279  -2.139  1.00 12.76           C  
ATOM     72  CG2 ILE A  14      45.391  44.265  -0.638  1.00 12.90           C  
ATOM     73  CD1 ILE A  14      46.174  41.434  -1.554  1.00 12.44           C  
ATOM     74  N   THR A  15      43.437  43.665   2.110  1.00 12.69           N  
ATOM     75  CA  THR A  15      42.702  44.554   3.001  1.00 13.41           C  
ATOM     76  C   THR A  15      43.575  45.716   3.463  1.00 16.63           C  
ATOM     77  O   THR A  15      44.431  45.559   4.333  1.00 14.77           O  
ATOM     78  CB  THR A  15      42.168  43.797   4.234  1.00 12.52           C  
ATOM     79  OG1 THR A  15      41.224  42.805   3.810  1.00 11.03           O  
ATOM     80  CG2 THR A  15      41.477  44.756   5.195  1.00 12.47           C  
ATOM     81  N   PRO A  16      43.369  46.902   2.875  1.00 17.99           N  
ATOM     82  CA  PRO A  16      44.148  48.090   3.240  1.00 20.64           C  
ATOM     83  C   PRO A  16      43.692  48.642   4.587  1.00 21.46           C  
ATOM     84  O   PRO A  16      42.626  48.273   5.086  1.00 19.38           O  
ATOM     85  CB  PRO A  16      43.867  49.046   2.088  1.00 19.07           C  
ATOM     86  CG  PRO A  16      42.441  48.731   1.760  1.00 20.30           C  
ATOM     87  CD  PRO A  16      42.415  47.210   1.794  1.00 19.07           C  
ATOM     88  N   ILE A  17      44.501  49.525   5.165  1.00 23.86           N  
ATOM     89  CA  ILE A  17      44.200  50.127   6.461  1.00 26.12           C  
ATOM     90  C   ILE A  17      42.844  50.827   6.498  1.00 27.43           C  
ATOM     91  O   ILE A  17      42.059  50.622   7.425  1.00 28.18           O  
ATOM     92  CB  ILE A  17      45.297  51.139   6.871  1.00 27.19           C  
ATOM     93  CG1 ILE A  17      45.222  52.403   6.005  1.00 27.45           C  
ATOM     94  CG2 ILE A  17      46.666  50.490   6.740  1.00 26.95           C  
ATOM     95  CD1 ILE A  17      45.352  52.172   4.504  1.00 26.63           C  
ATOM     96  N   SER A  18      42.570  51.652   5.493  1.00 29.03           N  
ATOM     97  CA  SER A  18      41.304  52.373   5.423  1.00 30.17           C  
ATOM     98  C   SER A  18      40.485  51.945   4.216  1.00 30.06           C  
ATOM     99  O   SER A  18      39.296  51.646   4.334  1.00 31.34           O  
ATOM    100  CB  SER A  18      41.548  53.883   5.351  1.00 30.32           C  
ATOM    101  OG  SER A  18      42.002  54.394   6.594  1.00 31.71           O  
ATOM    102  N   GLY A  19      41.131  51.919   3.057  1.00 29.69           N  
ATOM    103  CA  GLY A  19      40.444  51.547   1.835  1.00 29.08           C  
ATOM    104  C   GLY A  19      39.548  50.319   1.890  1.00 28.66           C  
ATOM    105  O   GLY A  19      39.516  49.568   2.871  1.00 29.79           O  
ATOM    106  N   GLN A  20      38.804  50.137   0.806  1.00 26.59           N  
ATOM    107  CA  GLN A  20      37.895  49.014   0.625  1.00 24.58           C  
ATOM    108  C   GLN A  20      38.776  47.823   0.228  1.00 21.12           C  
ATOM    109  O   GLN A  20      39.812  48.013  -0.406  1.00 20.15           O  
ATOM    110  CB  GLN A  20      36.919  49.371  -0.501  1.00 26.89           C  
ATOM    111  CG  GLN A  20      35.998  48.274  -0.968  1.00 29.41           C  
ATOM    112  CD  GLN A  20      35.180  48.702  -2.183  1.00 31.58           C  
ATOM    113  OE1 GLN A  20      35.735  49.018  -3.237  1.00 32.52           O  
ATOM    114  NE2 GLN A  20      33.858  48.720  -2.037  1.00 31.97           N  
ATOM    115  N   SER A  21      38.386  46.606   0.599  1.00 18.43           N  
ATOM    116  CA  SER A  21      39.191  45.434   0.250  1.00 14.86           C  
ATOM    117  C   SER A  21      38.997  45.017  -1.206  1.00 13.69           C  
ATOM    118  O   SER A  21      37.998  45.366  -1.841  1.00 12.68           O  
ATOM    119  CB  SER A  21      38.863  44.253   1.172  1.00 14.28           C  
ATOM    120  OG  SER A  21      39.336  44.478   2.492  1.00 10.89           O  
ATOM    121  N   THR A  22      39.971  44.276  -1.727  1.00 12.46           N  
ATOM    122  CA  THR A  22      39.944  43.788  -3.100  1.00 13.10           C  
ATOM    123  C   THR A  22      40.177  42.280  -3.104  1.00 11.58           C  
ATOM    124  O   THR A  22      40.998  41.769  -2.344  1.00 10.51           O  
ATOM    125  CB  THR A  22      41.042  44.468  -3.941  1.00 14.08           C  
ATOM    126  OG1 THR A  22      40.790  45.879  -3.990  1.00 14.75           O  
ATOM    127  CG2 THR A  22      41.071  43.904  -5.362  1.00 11.87           C  
ATOM    128  N   ALA A  23      39.458  41.566  -3.963  1.00 10.64           N  
ATOM    129  CA  ALA A  23      39.611  40.118  -4.033  1.00  8.42           C  
ATOM    130  C   ALA A  23      40.109  39.655  -5.394  1.00  8.18           C  
ATOM    131  O   ALA A  23      39.645  40.128  -6.432  1.00  7.69           O  
ATOM    132  CB  ALA A  23      38.290  39.438  -3.709  1.00  7.98           C  
ATOM    133  N   TYR A  24      41.075  38.743  -5.379  1.00  8.43           N  
ATOM    134  CA  TYR A  24      41.621  38.175  -6.604  1.00  8.19           C  
ATOM    135  C   TYR A  24      41.135  36.741  -6.663  1.00  8.54           C  
ATOM    136  O   TYR A  24      41.225  36.013  -5.673  1.00  7.00           O  
ATOM    137  CB  TYR A  24      43.149  38.178  -6.592  1.00  7.68           C  
ATOM    138  CG  TYR A  24      43.761  39.552  -6.656  1.00  9.82           C  
ATOM    139  CD1 TYR A  24      44.278  40.157  -5.515  1.00 10.65           C  
ATOM    140  CD2 TYR A  24      43.813  40.254  -7.857  1.00  9.72           C  
ATOM    141  CE1 TYR A  24      44.833  41.426  -5.566  1.00 11.91           C  
ATOM    142  CE2 TYR A  24      44.367  41.527  -7.921  1.00 10.18           C  
ATOM    143  CZ  TYR A  24      44.874  42.107  -6.770  1.00 10.44           C  
ATOM    144  OH  TYR A  24      45.402  43.374  -6.817  1.00 10.51           O  
ATOM    145  N   TRP A  25      40.624  36.339  -7.821  1.00  8.49           N  
ATOM    146  CA  TRP A  25      40.111  34.987  -8.005  1.00 10.64           C  
ATOM    147  C   TRP A  25      40.769  34.314  -9.198  1.00 11.65           C  
ATOM    148  O   TRP A  25      40.918  34.925 -10.257  1.00 12.33           O  
ATOM    149  CB  TRP A  25      38.605  35.011  -8.255  1.00  8.78           C  
ATOM    150  CG  TRP A  25      37.832  35.873  -7.316  1.00  8.59           C  
ATOM    151  CD1 TRP A  25      37.751  37.236  -7.327  1.00  6.92           C  
ATOM    152  CD2 TRP A  25      37.018  35.427  -6.227  1.00  6.99           C  
ATOM    153  NE1 TRP A  25      36.932  37.667  -6.310  1.00  7.77           N  
ATOM    154  CE2 TRP A  25      36.470  36.576  -5.619  1.00  7.57           C  
ATOM    155  CE3 TRP A  25      36.700  34.164  -5.705  1.00  8.48           C  
ATOM    156  CZ2 TRP A  25      35.618  36.504  -4.513  1.00  8.08           C  
ATOM    157  CZ3 TRP A  25      35.850  34.092  -4.602  1.00  5.41           C  
ATOM    158  CH2 TRP A  25      35.321  35.258  -4.020  1.00  6.31           C  
ATOM    159  N   ILE A  26      41.166  33.060  -9.029  1.00 11.43           N  
ATOM    160  CA  ILE A  26      41.763  32.323 -10.130  1.00 12.85           C  
ATOM    161  C   ILE A  26      40.612  31.500 -10.687  1.00 14.60           C  
ATOM    162  O   ILE A  26      40.095  30.604 -10.023  1.00 15.03           O  
ATOM    163  CB  ILE A  26      42.895  31.395  -9.659  1.00 13.57           C  
ATOM    164  CG1 ILE A  26      43.970  32.207  -8.931  1.00 10.97           C  
ATOM    165  CG2 ILE A  26      43.496  30.674 -10.854  1.00 13.99           C  
ATOM    166  CD1 ILE A  26      44.591  33.314  -9.765  1.00 12.72           C  
ATOM    167  N   CYS A  27      40.195  31.817 -11.904  1.00 16.23           N  
ATOM    168  CA  CYS A  27      39.072  31.116 -12.495  1.00 18.26           C  
ATOM    169  C   CYS A  27      39.388  30.608 -13.888  1.00 19.43           C  
ATOM    170  O   CYS A  27      39.525  31.385 -14.832  1.00 18.91           O  
ATOM    171  CB  CYS A  27      37.870  32.056 -12.510  1.00 18.03           C  
ATOM    172  SG  CYS A  27      37.756  32.950 -10.925  1.00 21.85           S  
ATOM    173  N   ASP A  28      39.510  29.292 -14.003  1.00 20.34           N  
ATOM    174  CA  ASP A  28      39.814  28.665 -15.277  1.00 21.70           C  
ATOM    175  C   ASP A  28      41.153  29.210 -15.763  1.00 20.67           C  
ATOM    176  O   ASP A  28      41.311  29.566 -16.930  1.00 19.36           O  
ATOM    177  CB  ASP A  28      38.714  28.979 -16.295  1.00 23.87           C  
ATOM    178  CG  ASP A  28      38.383  27.795 -17.183  1.00 27.14           C  
ATOM    179  OD1 ASP A  28      39.325  27.152 -17.694  1.00 28.20           O  
ATOM    180  OD2 ASP A  28      37.178  27.511 -17.375  1.00 29.35           O  
ATOM    181  N   ASN A  29      42.109  29.291 -14.843  1.00 19.81           N  
ATOM    182  CA  ASN A  29      43.449  29.776 -15.149  1.00 20.61           C  
ATOM    183  C   ASN A  29      43.482  31.220 -15.637  1.00 18.66           C  
ATOM    184  O   ASN A  29      44.392  31.625 -16.360  1.00 17.17           O  
ATOM    185  CB  ASN A  29      44.111  28.856 -16.176  1.00 23.00           C  
ATOM    186  CG  ASN A  29      44.148  27.412 -15.714  1.00 26.34           C  
ATOM    187  OD1 ASN A  29      44.571  27.120 -14.595  1.00 27.37           O  
ATOM    188  ND2 ASN A  29      43.705  26.499 -16.573  1.00 28.66           N  
ATOM    189  N   ARG A  30      42.478  31.992 -15.239  1.00 17.47           N  
ATOM    190  CA  ARG A  30      42.405  33.395 -15.608  1.00 16.88           C  
ATOM    191  C   ARG A  30      42.146  34.184 -14.338  1.00 14.76           C  
ATOM    192  O   ARG A  30      41.467  33.704 -13.428  1.00 15.34           O  
ATOM    193  CB  ARG A  30      41.278  33.629 -16.617  1.00 20.53           C  
ATOM    194  CG  ARG A  30      41.471  32.890 -17.927  1.00 23.28           C  
ATOM    195  CD  ARG A  30      40.257  32.032 -18.252  1.00 30.05           C  
ATOM    196  NE  ARG A  30      40.493  31.145 -19.390  1.00 31.68           N  
ATOM    197  CZ  ARG A  30      39.581  30.322 -19.900  1.00 33.72           C  
ATOM    198  NH1 ARG A  30      38.363  30.272 -19.374  1.00 34.52           N  
ATOM    199  NH2 ARG A  30      39.888  29.548 -20.936  1.00 34.66           N  
ATOM    200  N   LEU A  31      42.690  35.393 -14.275  1.00 12.65           N  
ATOM    201  CA  LEU A  31      42.517  36.226 -13.096  1.00 11.17           C  
ATOM    202  C   LEU A  31      41.289  37.124 -13.155  1.00 11.39           C  
ATOM    203  O   LEU A  31      41.006  37.756 -14.176  1.00 10.75           O  
ATOM    204  CB  LEU A  31      43.759  37.090 -12.877  1.00 10.09           C  
ATOM    205  CG  LEU A  31      43.683  38.037 -11.680  1.00  7.94           C  
ATOM    206  CD1 LEU A  31      43.539  37.227 -10.399  1.00  6.65           C  
ATOM    207  CD2 LEU A  31      44.923  38.911 -11.638  1.00  9.59           C  
ATOM    208  N   LYS A  32      40.552  37.147 -12.050  1.00 10.36           N  
ATOM    209  CA  LYS A  32      39.372  37.988 -11.906  1.00  9.48           C  
ATOM    210  C   LYS A  32      39.649  38.815 -10.661  1.00  8.05           C  
ATOM    211  O   LYS A  32      40.155  38.293  -9.668  1.00  8.23           O  
ATOM    212  CB  LYS A  32      38.110  37.149 -11.687  1.00 10.70           C  
ATOM    213  CG  LYS A  32      37.764  36.196 -12.826  1.00 15.31           C  
ATOM    214  CD  LYS A  32      37.510  36.925 -14.130  1.00 19.13           C  
ATOM    215  CE  LYS A  32      37.212  35.936 -15.258  1.00 21.23           C  
ATOM    216  NZ  LYS A  32      37.096  36.601 -16.589  1.00 21.63           N  
ATOM    217  N   THR A  33      39.328  40.101 -10.716  1.00  6.33           N  
ATOM    218  CA  THR A  33      39.558  40.990  -9.585  1.00  5.75           C  
ATOM    219  C   THR A  33      38.270  41.732  -9.261  1.00  6.75           C  
ATOM    220  O   THR A  33      37.637  42.305 -10.145  1.00  7.04           O  
ATOM    221  CB  THR A  33      40.671  42.001  -9.912  1.00  6.01           C  
ATOM    222  OG1 THR A  33      41.844  41.287 -10.328  1.00  6.68           O  
ATOM    223  CG2 THR A  33      41.006  42.849  -8.690  1.00  1.23           C  
ATOM    224  N   THR A  34      37.872  41.703  -7.994  1.00  7.62           N  
ATOM    225  CA  THR A  34      36.649  42.373  -7.577  1.00  7.03           C  
ATOM    226  C   THR A  34      36.872  43.305  -6.398  1.00  8.99           C  
ATOM    227  O   THR A  34      37.774  43.096  -5.587  1.00  8.69           O  
ATOM    228  CB  THR A  34      35.574  41.356  -7.174  1.00  8.02           C  
ATOM    229  OG1 THR A  34      36.069  40.532  -6.110  1.00  7.02           O  
ATOM    230  CG2 THR A  34      35.208  40.484  -8.356  1.00  6.09           C  
ATOM    231  N   SER A  35      36.044  44.340  -6.314  1.00  7.35           N  
ATOM    232  CA  SER A  35      36.125  45.299  -5.220  1.00  9.54           C  
ATOM    233  C   SER A  35      35.094  44.850  -4.200  1.00 10.42           C  
ATOM    234  O   SER A  35      33.922  44.692  -4.533  1.00  8.01           O  
ATOM    235  CB  SER A  35      35.790  46.705  -5.717  1.00 10.27           C  
ATOM    236  OG  SER A  35      36.700  47.120  -6.716  1.00  9.45           O  
ATOM    237  N   ILE A  36      35.529  44.641  -2.962  1.00 11.70           N  
ATOM    238  CA  ILE A  36      34.629  44.179  -1.913  1.00 13.29           C  
ATOM    239  C   ILE A  36      33.711  45.279  -1.400  1.00 14.65           C  
ATOM    240  O   ILE A  36      34.168  46.331  -0.970  1.00 12.91           O  
ATOM    241  CB  ILE A  36      35.420  43.596  -0.722  1.00 13.43           C  
ATOM    242  CG1 ILE A  36      36.393  42.525  -1.218  1.00 12.76           C  
ATOM    243  CG2 ILE A  36      34.463  42.994   0.296  1.00 11.43           C  
ATOM    244  CD1 ILE A  36      35.744  41.440  -2.026  1.00 15.39           C  
ATOM    245  N   GLU A  37      32.409  45.024  -1.440  1.00 16.84           N  
ATOM    246  CA  GLU A  37      31.439  46.001  -0.973  1.00 21.36           C  
ATOM    247  C   GLU A  37      30.661  45.483   0.228  1.00 22.67           C  
ATOM    248  O   GLU A  37      30.122  44.369   0.208  1.00 22.19           O  
ATOM    249  CB  GLU A  37      30.492  46.367  -2.116  1.00 23.70           C  
ATOM    250  CG  GLU A  37      31.217  47.033  -3.274  1.00 26.73           C  
ATOM    251  CD  GLU A  37      30.379  47.129  -4.525  1.00 29.33           C  
ATOM    252  OE1 GLU A  37      30.913  47.599  -5.555  1.00 29.96           O  
ATOM    253  OE2 GLU A  37      29.192  46.733  -4.482  1.00 31.09           O  
ATOM    254  N   LYS A  38      30.625  46.298   1.278  1.00 22.17           N  
ATOM    255  CA  LYS A  38      29.923  45.954   2.504  1.00 22.64           C  
ATOM    256  C   LYS A  38      30.517  44.710   3.168  1.00 21.80           C  
ATOM    257  O   LYS A  38      29.794  43.865   3.703  1.00 21.29           O  
ATOM    258  CB  LYS A  38      28.438  45.751   2.205  1.00 24.80           C  
ATOM    259  CG  LYS A  38      27.791  46.977   1.565  1.00 28.00           C  
ATOM    260  CD  LYS A  38      26.305  46.771   1.323  1.00 29.27           C  
ATOM    261  CE  LYS A  38      25.671  48.023   0.737  1.00 31.07           C  
ATOM    262  NZ  LYS A  38      25.908  49.215   1.605  1.00 31.90           N  
ATOM    263  N   LEU A  39      31.842  44.614   3.121  1.00 20.08           N  
ATOM    264  CA  LEU A  39      32.576  43.504   3.717  1.00 19.66           C  
ATOM    265  C   LEU A  39      32.163  42.124   3.216  1.00 19.15           C  
ATOM    266  O   LEU A  39      32.565  41.105   3.780  1.00 17.97           O  
ATOM    267  CB  LEU A  39      32.449  43.558   5.242  1.00 20.19           C  
ATOM    268  CG  LEU A  39      32.976  44.841   5.893  1.00 22.23           C  
ATOM    269  CD1 LEU A  39      32.801  44.759   7.402  1.00 22.08           C  
ATOM    270  CD2 LEU A  39      34.448  45.038   5.537  1.00 21.83           C  
ATOM    271  N   GLN A  40      31.372  42.086   2.150  1.00 18.25           N  
ATOM    272  CA  GLN A  40      30.931  40.816   1.602  1.00 17.86           C  
ATOM    273  C   GLN A  40      31.782  40.394   0.412  1.00 17.73           C  
ATOM    274  O   GLN A  40      31.797  41.059  -0.621  1.00 17.43           O  
ATOM    275  CB  GLN A  40      29.463  40.899   1.182  1.00 20.20           C  
ATOM    276  CG  GLN A  40      28.928  39.590   0.646  1.00 22.00           C  
ATOM    277  CD  GLN A  40      29.162  38.440   1.605  1.00 23.18           C  
ATOM    278  OE1 GLN A  40      29.620  37.367   1.206  1.00 21.87           O  
ATOM    279  NE2 GLN A  40      28.845  38.657   2.879  1.00 21.39           N  
ATOM    280  N   VAL A  41      32.495  39.285   0.563  1.00 15.84           N  
ATOM    281  CA  VAL A  41      33.335  38.779  -0.510  1.00 14.89           C  
ATOM    282  C   VAL A  41      32.511  37.853  -1.398  1.00 15.32           C  
ATOM    283  O   VAL A  41      32.282  36.698  -1.052  1.00 15.37           O  
ATOM    284  CB  VAL A  41      34.543  38.007   0.048  1.00 13.28           C  
ATOM    285  CG1 VAL A  41      35.444  37.554  -1.097  1.00 13.58           C  
ATOM    286  CG2 VAL A  41      35.319  38.889   1.018  1.00 11.77           C  
ATOM    287  N   ASN A  42      32.067  38.374  -2.539  1.00 15.47           N  
ATOM    288  CA  ASN A  42      31.264  37.602  -3.484  1.00 16.74           C  
ATOM    289  C   ASN A  42      32.091  37.199  -4.701  1.00 14.87           C  
ATOM    290  O   ASN A  42      32.802  38.023  -5.280  1.00 13.94           O  
ATOM    291  CB  ASN A  42      30.056  38.421  -3.950  1.00 19.37           C  
ATOM    292  CG  ASN A  42      29.139  38.814  -2.809  1.00 22.33           C  
ATOM    293  OD1 ASN A  42      28.665  37.963  -2.054  1.00 24.78           O  
ATOM    294  ND2 ASN A  42      28.878  40.111  -2.680  1.00 24.55           N  
ATOM    295  N   ARG A  43      31.986  35.933  -5.095  1.00 15.44           N  
ATOM    296  CA  ARG A  43      32.735  35.443  -6.244  1.00 15.12           C  
ATOM    297  C   ARG A  43      32.163  36.006  -7.542  1.00 14.79           C  
ATOM    298  O   ARG A  43      30.960  36.240  -7.654  1.00 14.91           O  
ATOM    299  CB  ARG A  43      32.720  33.907  -6.290  1.00 16.16           C  
ATOM    300  CG  ARG A  43      31.507  33.291  -6.976  1.00 18.83           C  
ATOM    301  CD  ARG A  43      31.716  31.794  -7.230  1.00 17.75           C  
ATOM    302  NE  ARG A  43      31.610  31.007  -6.007  1.00 19.20           N  
ATOM    303  CZ  ARG A  43      30.463  30.733  -5.394  1.00 19.63           C  
ATOM    304  NH1 ARG A  43      29.319  31.178  -5.895  1.00 23.26           N  
ATOM    305  NH2 ARG A  43      30.459  30.028  -4.272  1.00 20.78           N  
ATOM    306  N   PRO A  44      33.030  36.248  -8.535  1.00 15.13           N  
ATOM    307  CA  PRO A  44      32.613  36.786  -9.831  1.00 15.98           C  
ATOM    308  C   PRO A  44      31.935  35.703 -10.657  1.00 17.12           C  
ATOM    309  O   PRO A  44      31.777  34.567 -10.206  1.00 16.95           O  
ATOM    310  CB  PRO A  44      33.931  37.218 -10.476  1.00 15.91           C  
ATOM    311  CG  PRO A  44      34.893  37.332  -9.324  1.00 15.74           C  
ATOM    312  CD  PRO A  44      34.496  36.182  -8.455  1.00 15.15           C  
ATOM    313  N   GLU A  45      31.534  36.067 -11.868  1.00 18.42           N  
ATOM    314  CA  GLU A  45      30.913  35.119 -12.778  1.00 20.89           C  
ATOM    315  C   GLU A  45      32.038  34.236 -13.322  1.00 19.10           C  
ATOM    316  O   GLU A  45      33.186  34.673 -13.414  1.00 19.88           O  
ATOM    317  CB  GLU A  45      30.241  35.862 -13.939  1.00 21.06           C  
ATOM    318  CG  GLU A  45      29.032  36.697 -13.548  1.00 26.95           C  
ATOM    319  CD  GLU A  45      27.829  35.841 -13.196  1.00 29.97           C  
ATOM    320  OE1 GLU A  45      26.771  36.405 -12.840  1.00 33.66           O  
ATOM    321  OE2 GLU A  45      27.940  34.599 -13.281  1.00 32.77           O  
ATOM    322  N   HIS A  46      31.708  32.998 -13.670  1.00 17.69           N  
ATOM    323  CA  HIS A  46      32.688  32.070 -14.227  1.00 18.97           C  
ATOM    324  C   HIS A  46      33.851  31.747 -13.295  1.00 19.13           C  
ATOM    325  O   HIS A  46      34.990  31.633 -13.747  1.00 18.51           O  
ATOM    326  CB  HIS A  46      33.242  32.629 -15.541  1.00 17.91           C  
ATOM    327  CG  HIS A  46      32.181  33.014 -16.524  1.00 17.95           C  
ATOM    328  ND1 HIS A  46      31.380  32.087 -17.154  1.00 17.34           N  
ATOM    329  CD2 HIS A  46      31.763  34.229 -16.952  1.00 16.60           C  
ATOM    330  CE1 HIS A  46      30.511  32.714 -17.927  1.00 16.42           C  
ATOM    331  NE2 HIS A  46      30.721  34.014 -17.822  1.00 16.48           N  
ATOM    332  N   CYS A  47      33.569  31.606 -12.002  1.00 20.17           N  
ATOM    333  CA  CYS A  47      34.607  31.279 -11.026  1.00 21.26           C  
ATOM    334  C   CYS A  47      34.262  30.065 -10.186  1.00 21.20           C  
ATOM    335  O   CYS A  47      34.526  30.033  -8.982  1.00 22.21           O  
ATOM    336  CB  CYS A  47      34.888  32.462 -10.102  1.00 20.53           C  
ATOM    337  SG  CYS A  47      35.894  33.747 -10.895  1.00 23.03           S  
ATOM    338  N   GLY A  48      33.669  29.069 -10.834  1.00 21.32           N  
ATOM    339  CA  GLY A  48      33.304  27.842 -10.154  1.00 19.96           C  
ATOM    340  C   GLY A  48      32.522  28.034  -8.873  1.00 18.51           C  
ATOM    341  O   GLY A  48      31.555  28.794  -8.827  1.00 19.72           O  
ATOM    342  N   ASP A  49      32.949  27.342  -7.824  1.00 16.66           N  
ATOM    343  CA  ASP A  49      32.274  27.423  -6.540  1.00 17.56           C  
ATOM    344  C   ASP A  49      33.190  27.914  -5.423  1.00 15.49           C  
ATOM    345  O   ASP A  49      33.057  27.483  -4.280  1.00 14.60           O  
ATOM    346  CB  ASP A  49      31.719  26.050  -6.163  1.00 20.43           C  
ATOM    347  CG  ASP A  49      30.664  26.130  -5.081  1.00 23.79           C  
ATOM    348  OD1 ASP A  49      30.516  25.152  -4.318  1.00 25.09           O  
ATOM    349  OD2 ASP A  49      29.974  27.171  -5.003  1.00 24.84           O  
ATOM    350  N   LEU A  50      34.109  28.820  -5.748  1.00 13.87           N  
ATOM    351  CA  LEU A  50      35.035  29.348  -4.750  1.00 10.89           C  
ATOM    352  C   LEU A  50      34.285  29.937  -3.561  1.00 10.92           C  
ATOM    353  O   LEU A  50      33.199  30.503  -3.715  1.00 10.02           O  
ATOM    354  CB  LEU A  50      35.957  30.388  -5.388  1.00 11.19           C  
ATOM    355  CG  LEU A  50      36.843  29.784  -6.484  1.00 10.19           C  
ATOM    356  CD1 LEU A  50      37.668  30.868  -7.152  1.00  9.45           C  
ATOM    357  CD2 LEU A  50      37.744  28.719  -5.876  1.00 11.68           C  
ATOM    358  N   PRO A  51      34.862  29.816  -2.352  1.00  9.43           N  
ATOM    359  CA  PRO A  51      34.251  30.323  -1.121  1.00  9.72           C  
ATOM    360  C   PRO A  51      34.008  31.818  -1.048  1.00  9.90           C  
ATOM    361  O   PRO A  51      34.838  32.630  -1.461  1.00  9.27           O  
ATOM    362  CB  PRO A  51      35.216  29.851  -0.037  1.00  7.86           C  
ATOM    363  CG  PRO A  51      36.530  29.931  -0.726  1.00  9.57           C  
ATOM    364  CD  PRO A  51      36.223  29.320  -2.083  1.00  7.64           C  
ATOM    365  N   GLU A  52      32.846  32.160  -0.509  1.00 11.15           N  
ATOM    366  CA  GLU A  52      32.444  33.540  -0.322  1.00 13.43           C  
ATOM    367  C   GLU A  52      32.261  33.689   1.174  1.00 15.20           C  
ATOM    368  O   GLU A  52      31.693  32.811   1.824  1.00 17.91           O  
ATOM    369  CB  GLU A  52      31.121  33.814  -1.028  1.00 13.44           C  
ATOM    370  CG  GLU A  52      31.153  33.566  -2.520  1.00 13.65           C  
ATOM    371  CD  GLU A  52      29.812  33.827  -3.161  1.00 16.29           C  
ATOM    372  OE1 GLU A  52      28.822  33.187  -2.741  1.00 17.19           O  
ATOM    373  OE2 GLU A  52      29.747  34.671  -4.079  1.00 15.85           O  
ATOM    374  N   THR A  53      32.754  34.783   1.732  1.00 15.59           N  
ATOM    375  CA  THR A  53      32.614  34.989   3.163  1.00 17.79           C  
ATOM    376  C   THR A  53      32.502  36.451   3.542  1.00 17.57           C  
ATOM    377  O   THR A  53      32.976  37.339   2.833  1.00 17.70           O  
ATOM    378  CB  THR A  53      33.784  34.328   3.948  1.00 19.95           C  
ATOM    379  OG1 THR A  53      34.289  35.235   4.934  1.00 22.52           O  
ATOM    380  CG2 THR A  53      34.895  33.924   3.016  1.00 17.95           C  
ATOM    381  N   LYS A  54      31.832  36.693   4.659  1.00 17.33           N  
ATOM    382  CA  LYS A  54      31.651  38.038   5.168  1.00 17.54           C  
ATOM    383  C   LYS A  54      32.884  38.383   5.992  1.00 16.98           C  
ATOM    384  O   LYS A  54      33.175  37.714   6.986  1.00 15.44           O  
ATOM    385  CB  LYS A  54      30.397  38.096   6.043  1.00 20.67           C  
ATOM    386  CG  LYS A  54      30.191  39.410   6.768  1.00 24.75           C  
ATOM    387  CD  LYS A  54      30.102  40.577   5.803  1.00 26.60           C  
ATOM    388  CE  LYS A  54      29.823  41.872   6.548  1.00 30.61           C  
ATOM    389  NZ  LYS A  54      28.520  41.828   7.274  1.00 32.53           N  
ATOM    390  N   LEU A  55      33.614  39.410   5.568  1.00 13.74           N  
ATOM    391  CA  LEU A  55      34.811  39.825   6.286  1.00 14.16           C  
ATOM    392  C   LEU A  55      34.467  40.239   7.709  1.00 13.93           C  
ATOM    393  O   LEU A  55      33.436  40.864   7.959  1.00 14.17           O  
ATOM    394  CB  LEU A  55      35.503  40.983   5.564  1.00 12.94           C  
ATOM    395  CG  LEU A  55      36.052  40.687   4.168  1.00 12.46           C  
ATOM    396  CD1 LEU A  55      36.850  41.891   3.679  1.00 14.00           C  
ATOM    397  CD2 LEU A  55      36.938  39.448   4.212  1.00 12.52           C  
ATOM    398  N   SER A  56      35.341  39.882   8.640  1.00 15.36           N  
ATOM    399  CA  SER A  56      35.135  40.200  10.041  1.00 16.98           C  
ATOM    400  C   SER A  56      36.298  40.997  10.599  1.00 19.56           C  
ATOM    401  O   SER A  56      37.451  40.769  10.243  1.00 21.27           O  
ATOM    402  CB  SER A  56      34.973  38.913  10.850  1.00 16.14           C  
ATOM    403  OG  SER A  56      35.115  39.165  12.235  1.00 15.62           O  
ATOM    404  N   SER A  57      35.993  41.932  11.483  1.00 23.11           N  
ATOM    405  CA  SER A  57      37.032  42.736  12.094  1.00 23.62           C  
ATOM    406  C   SER A  57      37.442  42.096  13.414  1.00 22.99           C  
ATOM    407  O   SER A  57      38.632  41.936  13.707  1.00 21.90           O  
ATOM    408  CB  SER A  57      36.513  44.151  12.355  1.00 26.57           C  
ATOM    409  OG  SER A  57      35.430  44.128  13.271  1.00 30.27           O  
ATOM    410  N   GLU A  58      36.446  41.700  14.197  1.00 20.85           N  
ATOM    411  CA  GLU A  58      36.708  41.132  15.506  1.00 19.51           C  
ATOM    412  C   GLU A  58      37.547  39.856  15.592  1.00 16.80           C  
ATOM    413  O   GLU A  58      38.319  39.704  16.537  1.00 17.53           O  
ATOM    414  CB  GLU A  58      35.390  40.955  16.267  1.00 22.34           C  
ATOM    415  CG  GLU A  58      34.500  39.827  15.803  1.00 25.26           C  
ATOM    416  CD  GLU A  58      33.205  39.767  16.601  1.00 29.00           C  
ATOM    417  OE1 GLU A  58      32.552  38.701  16.617  1.00 29.70           O  
ATOM    418  OE2 GLU A  58      32.835  40.792  17.212  1.00 30.91           O  
ATOM    419  N   ILE A  59      37.438  38.945  14.629  1.00 12.78           N  
ATOM    420  CA  ILE A  59      38.231  37.724  14.733  1.00 10.31           C  
ATOM    421  C   ILE A  59      39.725  37.928  14.496  1.00  9.52           C  
ATOM    422  O   ILE A  59      40.524  37.028  14.757  1.00  8.58           O  
ATOM    423  CB  ILE A  59      37.711  36.599  13.801  1.00 10.59           C  
ATOM    424  CG1 ILE A  59      37.822  37.017  12.337  1.00 10.20           C  
ATOM    425  CG2 ILE A  59      36.272  36.260  14.168  1.00 10.14           C  
ATOM    426  CD1 ILE A  59      37.533  35.885  11.370  1.00 11.41           C  
ATOM    427  N   LYS A  60      40.112  39.104  14.011  1.00  8.04           N  
ATOM    428  CA  LYS A  60      41.529  39.380  13.804  1.00  8.76           C  
ATOM    429  C   LYS A  60      42.128  39.973  15.083  1.00  8.75           C  
ATOM    430  O   LYS A  60      43.304  40.325  15.125  1.00  8.85           O  
ATOM    431  CB  LYS A  60      41.735  40.326  12.614  1.00  9.37           C  
ATOM    432  CG  LYS A  60      41.358  39.702  11.272  1.00  8.30           C  
ATOM    433  CD  LYS A  60      41.891  40.499  10.073  1.00 10.89           C  
ATOM    434  CE  LYS A  60      41.166  41.826   9.892  1.00  9.47           C  
ATOM    435  NZ  LYS A  60      41.582  42.523   8.629  1.00  9.72           N  
ATOM    436  N   GLN A  61      41.302  40.083  16.122  1.00  8.15           N  
ATOM    437  CA  GLN A  61      41.741  40.603  17.421  1.00  8.33           C  
ATOM    438  C   GLN A  61      42.590  39.539  18.109  1.00  6.89           C  
ATOM    439  O   GLN A  61      42.258  38.357  18.072  1.00  7.26           O  
ATOM    440  CB  GLN A  61      40.538  40.901  18.323  1.00  9.96           C  
ATOM    441  CG  GLN A  61      39.622  42.013  17.845  1.00 11.07           C  
ATOM    442  CD  GLN A  61      38.374  42.148  18.707  1.00 14.71           C  
ATOM    443  OE1 GLN A  61      37.640  43.134  18.607  1.00 16.95           O  
ATOM    444  NE2 GLN A  61      38.124  41.154  19.553  1.00 14.60           N  
ATOM    445  N   ILE A  62      43.675  39.949  18.750  1.00  6.92           N  
ATOM    446  CA  ILE A  62      44.511  38.981  19.445  1.00  6.32           C  
ATOM    447  C   ILE A  62      43.753  38.544  20.697  1.00  7.02           C  
ATOM    448  O   ILE A  62      43.247  39.376  21.453  1.00  8.78           O  
ATOM    449  CB  ILE A  62      45.883  39.593  19.808  1.00  6.68           C  
ATOM    450  CG1 ILE A  62      46.604  39.999  18.516  1.00  5.05           C  
ATOM    451  CG2 ILE A  62      46.731  38.579  20.578  1.00  6.65           C  
ATOM    452  CD1 ILE A  62      47.857  40.820  18.723  1.00  4.86           C  
ATOM    453  N   MET A  63      43.659  37.235  20.895  1.00  5.62           N  
ATOM    454  CA  MET A  63      42.935  36.677  22.031  1.00  5.76           C  
ATOM    455  C   MET A  63      43.865  36.068  23.076  1.00  6.85           C  
ATOM    456  O   MET A  63      45.027  35.785  22.795  1.00  5.95           O  
ATOM    457  CB  MET A  63      41.969  35.598  21.541  1.00  4.27           C  
ATOM    458  CG  MET A  63      41.050  36.039  20.423  1.00  5.43           C  
ATOM    459  SD  MET A  63      40.037  37.447  20.880  1.00 10.06           S  
ATOM    460  CE  MET A  63      38.906  36.684  22.032  1.00  7.59           C  
ATOM    461  N   PRO A  64      43.360  35.860  24.305  1.00  5.95           N  
ATOM    462  CA  PRO A  64      44.170  35.273  25.375  1.00  7.93           C  
ATOM    463  C   PRO A  64      44.705  33.914  24.942  1.00  6.55           C  
ATOM    464  O   PRO A  64      44.158  33.288  24.034  1.00  8.04           O  
ATOM    465  CB  PRO A  64      43.178  35.131  26.523  1.00  7.16           C  
ATOM    466  CG  PRO A  64      42.238  36.266  26.296  1.00  8.63           C  
ATOM    467  CD  PRO A  64      42.026  36.235  24.806  1.00  6.43           C  
ATOM    468  N   ASP A  65      45.765  33.458  25.600  1.00  6.49           N  
ATOM    469  CA  ASP A  65      46.345  32.159  25.285  1.00  7.43           C  
ATOM    470  C   ASP A  65      46.125  31.211  26.458  1.00  6.96           C  
ATOM    471  O   ASP A  65      46.637  30.093  26.476  1.00  7.97           O  
ATOM    472  CB  ASP A  65      47.840  32.301  24.964  1.00  5.61           C  
ATOM    473  CG  ASP A  65      48.654  32.838  26.133  1.00  9.18           C  
ATOM    474  OD1 ASP A  65      49.740  33.404  25.877  1.00  7.62           O  
ATOM    475  OD2 ASP A  65      48.227  32.685  27.299  1.00  5.52           O  
ATOM    476  N   THR A  66      45.342  31.669  27.433  1.00  7.76           N  
ATOM    477  CA  THR A  66      45.028  30.877  28.619  1.00  6.41           C  
ATOM    478  C   THR A  66      43.549  31.012  28.969  1.00  6.42           C  
ATOM    479  O   THR A  66      43.013  32.119  29.029  1.00  3.87           O  
ATOM    480  CB  THR A  66      45.880  31.321  29.810  1.00  6.00           C  
ATOM    481  OG1 THR A  66      47.258  31.081  29.507  1.00  6.96           O  
ATOM    482  CG2 THR A  66      45.498  30.550  31.068  1.00  7.54           C  
ATOM    483  N   TYR A  67      42.902  29.876  29.208  1.00  7.61           N  
ATOM    484  CA  TYR A  67      41.479  29.849  29.513  1.00  8.20           C  
ATOM    485  C   TYR A  67      41.130  28.918  30.669  1.00 10.31           C  
ATOM    486  O   TYR A  67      41.791  27.901  30.889  1.00  9.26           O  
ATOM    487  CB  TYR A  67      40.712  29.424  28.261  1.00 10.10           C  
ATOM    488  CG  TYR A  67      40.912  30.367  27.098  1.00  8.07           C  
ATOM    489  CD1 TYR A  67      40.035  31.430  26.885  1.00  9.07           C  
ATOM    490  CD2 TYR A  67      42.008  30.232  26.242  1.00  8.63           C  
ATOM    491  CE1 TYR A  67      40.240  32.338  25.853  1.00  8.73           C  
ATOM    492  CE2 TYR A  67      42.227  31.142  25.203  1.00  7.08           C  
ATOM    493  CZ  TYR A  67      41.334  32.192  25.019  1.00  9.45           C  
ATOM    494  OH  TYR A  67      41.532  33.106  24.014  1.00  8.90           O  
ATOM    495  N   LEU A  68      40.077  29.278  31.397  1.00  8.95           N  
ATOM    496  CA  LEU A  68      39.606  28.501  32.537  1.00 11.35           C  
ATOM    497  C   LEU A  68      38.138  28.131  32.408  1.00 10.99           C  
ATOM    498  O   LEU A  68      37.366  28.809  31.732  1.00 11.44           O  
ATOM    499  CB  LEU A  68      39.777  29.299  33.828  1.00 11.84           C  
ATOM    500  CG  LEU A  68      41.163  29.440  34.441  1.00 14.47           C  
ATOM    501  CD1 LEU A  68      41.125  30.539  35.497  1.00 16.68           C  
ATOM    502  CD2 LEU A  68      41.585  28.108  35.049  1.00 15.52           C  
ATOM    503  N   GLY A  69      37.769  27.047  33.076  1.00 12.26           N  
ATOM    504  CA  GLY A  69      36.392  26.594  33.083  1.00 11.51           C  
ATOM    505  C   GLY A  69      35.688  26.424  31.756  1.00 10.77           C  
ATOM    506  O   GLY A  69      34.501  26.730  31.651  1.00 11.57           O  
ATOM    507  N   ILE A  70      36.398  25.950  30.738  1.00  9.73           N  
ATOM    508  CA  ILE A  70      35.769  25.728  29.441  1.00  9.71           C  
ATOM    509  C   ILE A  70      35.163  24.323  29.483  1.00 10.71           C  
ATOM    510  O   ILE A  70      35.885  23.339  29.615  1.00  8.87           O  
ATOM    511  CB  ILE A  70      36.801  25.827  28.296  1.00  9.04           C  
ATOM    512  CG1 ILE A  70      37.508  27.184  28.355  1.00  9.00           C  
ATOM    513  CG2 ILE A  70      36.112  25.642  26.952  1.00  8.61           C  
ATOM    514  CD1 ILE A  70      36.561  28.373  28.416  1.00  7.30           C  
ATOM    515  N   LYS A  71      33.840  24.230  29.377  1.00 11.55           N  
ATOM    516  CA  LYS A  71      33.168  22.935  29.451  1.00 13.34           C  
ATOM    517  C   LYS A  71      33.532  21.891  28.402  1.00 13.49           C  
ATOM    518  O   LYS A  71      33.819  20.748  28.751  1.00 13.03           O  
ATOM    519  CB  LYS A  71      31.646  23.112  29.475  1.00 16.17           C  
ATOM    520  CG  LYS A  71      31.096  23.562  30.821  1.00 20.83           C  
ATOM    521  CD  LYS A  71      31.002  25.076  30.930  1.00 25.89           C  
ATOM    522  CE  LYS A  71      29.872  25.616  30.063  1.00 27.25           C  
ATOM    523  NZ  LYS A  71      29.750  27.097  30.162  1.00 26.99           N  
ATOM    524  N   LYS A  72      33.510  22.252  27.124  1.00 12.35           N  
ATOM    525  CA  LYS A  72      33.850  21.270  26.102  1.00 12.07           C  
ATOM    526  C   LYS A  72      34.818  21.811  25.061  1.00 12.34           C  
ATOM    527  O   LYS A  72      34.706  22.953  24.615  1.00 10.14           O  
ATOM    528  CB  LYS A  72      32.585  20.738  25.416  1.00 14.55           C  
ATOM    529  CG  LYS A  72      31.799  21.768  24.643  1.00 15.97           C  
ATOM    530  CD  LYS A  72      30.563  21.142  24.020  1.00 19.21           C  
ATOM    531  CE  LYS A  72      29.788  22.167  23.208  1.00 18.54           C  
ATOM    532  NZ  LYS A  72      28.561  21.593  22.599  1.00 19.75           N  
ATOM    533  N   VAL A  73      35.777  20.969  24.691  1.00 11.33           N  
ATOM    534  CA  VAL A  73      36.796  21.328  23.718  1.00 10.22           C  
ATOM    535  C   VAL A  73      36.970  20.210  22.696  1.00  8.46           C  
ATOM    536  O   VAL A  73      36.852  19.032  23.025  1.00  8.36           O  
ATOM    537  CB  VAL A  73      38.169  21.556  24.411  1.00 10.57           C  
ATOM    538  CG1 VAL A  73      39.224  21.952  23.381  1.00  7.84           C  
ATOM    539  CG2 VAL A  73      38.043  22.625  25.486  1.00  8.13           C  
ATOM    540  N   VAL A  74      37.237  20.587  21.452  1.00  8.44           N  
ATOM    541  CA  VAL A  74      37.484  19.610  20.400  1.00  6.95           C  
ATOM    542  C   VAL A  74      38.811  20.011  19.763  1.00  7.78           C  
ATOM    543  O   VAL A  74      39.040  21.191  19.496  1.00  8.11           O  
ATOM    544  CB  VAL A  74      36.358  19.601  19.333  1.00  6.58           C  
ATOM    545  CG1 VAL A  74      36.280  20.950  18.624  1.00  9.01           C  
ATOM    546  CG2 VAL A  74      36.603  18.484  18.339  1.00  8.78           C  
ATOM    547  N   ALA A  75      39.692  19.037  19.543  1.00  7.30           N  
ATOM    548  CA  ALA A  75      40.994  19.317  18.958  1.00  6.38           C  
ATOM    549  C   ALA A  75      41.284  18.428  17.761  1.00  4.83           C  
ATOM    550  O   ALA A  75      40.929  17.250  17.745  1.00  5.89           O  
ATOM    551  CB  ALA A  75      42.086  19.140  20.007  1.00  5.25           C  
ATOM    552  N   LEU A  76      41.926  19.018  16.760  1.00  6.41           N  
ATOM    553  CA  LEU A  76      42.306  18.319  15.541  1.00  5.64           C  
ATOM    554  C   LEU A  76      43.483  19.088  14.958  1.00  6.79           C  
ATOM    555  O   LEU A  76      43.759  20.215  15.377  1.00  7.76           O  
ATOM    556  CB  LEU A  76      41.142  18.272  14.547  1.00  7.15           C  
ATOM    557  CG  LEU A  76      40.591  19.573  13.964  1.00  5.87           C  
ATOM    558  CD1 LEU A  76      39.589  19.234  12.867  1.00  8.84           C  
ATOM    559  CD2 LEU A  76      39.938  20.413  15.049  1.00  7.49           C  
ATOM    560  N   SER A  77      44.177  18.505  13.990  1.00  6.39           N  
ATOM    561  CA  SER A  77      45.343  19.186  13.453  1.00  6.75           C  
ATOM    562  C   SER A  77      45.797  18.686  12.098  1.00  6.43           C  
ATOM    563  O   SER A  77      45.316  17.669  11.601  1.00  7.47           O  
ATOM    564  CB  SER A  77      46.499  19.028  14.447  1.00  6.59           C  
ATOM    565  OG  SER A  77      47.648  19.757  14.057  1.00  7.42           O  
ATOM    566  N   ASP A  78      46.732  19.430  11.513  1.00  6.16           N  
ATOM    567  CA  ASP A  78      47.346  19.077  10.243  1.00  4.82           C  
ATOM    568  C   ASP A  78      46.399  18.726   9.100  1.00  5.84           C  
ATOM    569  O   ASP A  78      46.539  17.679   8.472  1.00  4.79           O  
ATOM    570  CB  ASP A  78      48.324  17.928  10.483  1.00  5.83           C  
ATOM    571  CG  ASP A  78      49.440  18.309  11.438  1.00  3.86           C  
ATOM    572  OD1 ASP A  78      50.534  18.663  10.960  1.00  4.45           O  
ATOM    573  OD2 ASP A  78      49.219  18.275  12.666  1.00  4.23           O  
ATOM    574  N   VAL A  79      45.449  19.611   8.825  1.00  5.41           N  
ATOM    575  CA  VAL A  79      44.501  19.393   7.741  1.00  6.24           C  
ATOM    576  C   VAL A  79      45.247  19.381   6.409  1.00  5.57           C  
ATOM    577  O   VAL A  79      44.877  18.659   5.483  1.00  7.16           O  
ATOM    578  CB  VAL A  79      43.426  20.496   7.734  1.00  7.13           C  
ATOM    579  CG1 VAL A  79      42.500  20.329   6.536  1.00  6.10           C  
ATOM    580  CG2 VAL A  79      42.626  20.431   9.035  1.00  6.74           C  
ATOM    581  N   HIS A  80      46.309  20.177   6.328  1.00  5.91           N  
ATOM    582  CA  HIS A  80      47.133  20.265   5.126  1.00  5.35           C  
ATOM    583  C   HIS A  80      46.374  20.333   3.802  1.00  6.07           C  
ATOM    584  O   HIS A  80      46.565  19.493   2.919  1.00  6.13           O  
ATOM    585  CB  HIS A  80      48.127  19.099   5.086  1.00  5.59           C  
ATOM    586  CG  HIS A  80      49.285  19.269   6.014  1.00  5.38           C  
ATOM    587  ND1 HIS A  80      50.177  20.315   5.901  1.00  5.70           N  
ATOM    588  CD2 HIS A  80      49.685  18.547   7.086  1.00  2.90           C  
ATOM    589  CE1 HIS A  80      51.074  20.229   6.867  1.00  6.09           C  
ATOM    590  NE2 HIS A  80      50.796  19.166   7.600  1.00  3.63           N  
ATOM    591  N   GLY A  81      45.515  21.339   3.676  1.00  6.43           N  
ATOM    592  CA  GLY A  81      44.762  21.538   2.450  1.00  6.99           C  
ATOM    593  C   GLY A  81      43.707  20.516   2.059  1.00  7.27           C  
ATOM    594  O   GLY A  81      43.235  20.538   0.921  1.00  6.77           O  
ATOM    595  N   GLN A  82      43.338  19.620   2.970  1.00  6.57           N  
ATOM    596  CA  GLN A  82      42.316  18.617   2.671  1.00  7.53           C  
ATOM    597  C   GLN A  82      40.973  19.078   3.239  1.00  8.57           C  
ATOM    598  O   GLN A  82      40.534  18.620   4.295  1.00  9.62           O  
ATOM    599  CB  GLN A  82      42.713  17.261   3.268  1.00  9.31           C  
ATOM    600  CG  GLN A  82      44.020  16.714   2.710  1.00  8.45           C  
ATOM    601  CD  GLN A  82      43.936  16.377   1.231  1.00 12.59           C  
ATOM    602  OE1 GLN A  82      44.954  16.317   0.536  1.00 12.99           O  
ATOM    603  NE2 GLN A  82      42.723  16.140   0.747  1.00  7.64           N  
ATOM    604  N   TYR A  83      40.329  19.991   2.521  1.00  6.78           N  
ATOM    605  CA  TYR A  83      39.050  20.552   2.943  1.00  6.87           C  
ATOM    606  C   TYR A  83      37.904  19.542   3.011  1.00  5.43           C  
ATOM    607  O   TYR A  83      37.168  19.507   3.993  1.00  5.36           O  
ATOM    608  CB  TYR A  83      38.680  21.713   2.018  1.00  7.81           C  
ATOM    609  CG  TYR A  83      37.290  22.277   2.221  1.00 10.29           C  
ATOM    610  CD1 TYR A  83      36.261  21.968   1.335  1.00 12.52           C  
ATOM    611  CD2 TYR A  83      37.013  23.152   3.273  1.00 12.02           C  
ATOM    612  CE1 TYR A  83      34.995  22.517   1.480  1.00 12.77           C  
ATOM    613  CE2 TYR A  83      35.744  23.710   3.430  1.00 11.83           C  
ATOM    614  CZ  TYR A  83      34.741  23.389   2.524  1.00 14.55           C  
ATOM    615  OH  TYR A  83      33.491  23.957   2.637  1.00 15.61           O  
ATOM    616  N   ASP A  84      37.754  18.723   1.977  1.00  5.34           N  
ATOM    617  CA  ASP A  84      36.682  17.740   1.964  1.00  7.10           C  
ATOM    618  C   ASP A  84      36.751  16.811   3.175  1.00  7.48           C  
ATOM    619  O   ASP A  84      35.732  16.509   3.794  1.00  6.82           O  
ATOM    620  CB  ASP A  84      36.725  16.912   0.679  1.00  7.80           C  
ATOM    621  CG  ASP A  84      36.512  17.754  -0.565  1.00  9.14           C  
ATOM    622  OD1 ASP A  84      35.806  18.782  -0.475  1.00 11.36           O  
ATOM    623  OD2 ASP A  84      37.033  17.378  -1.635  1.00  9.42           O  
ATOM    624  N   VAL A  85      37.956  16.358   3.507  1.00  7.00           N  
ATOM    625  CA  VAL A  85      38.137  15.466   4.645  1.00  6.57           C  
ATOM    626  C   VAL A  85      37.747  16.178   5.931  1.00  6.49           C  
ATOM    627  O   VAL A  85      36.995  15.635   6.738  1.00  8.14           O  
ATOM    628  CB  VAL A  85      39.601  14.983   4.755  1.00  6.30           C  
ATOM    629  CG1 VAL A  85      39.790  14.170   6.031  1.00  8.19           C  
ATOM    630  CG2 VAL A  85      39.956  14.143   3.544  1.00  5.33           C  
ATOM    631  N   LEU A  86      38.255  17.392   6.118  1.00  5.21           N  
ATOM    632  CA  LEU A  86      37.945  18.175   7.309  1.00  5.46           C  
ATOM    633  C   LEU A  86      36.434  18.380   7.458  1.00  4.76           C  
ATOM    634  O   LEU A  86      35.863  18.151   8.522  1.00  3.76           O  
ATOM    635  CB  LEU A  86      38.640  19.542   7.243  1.00  4.56           C  
ATOM    636  CG  LEU A  86      38.262  20.571   8.318  1.00  5.28           C  
ATOM    637  CD1 LEU A  86      38.681  20.063   9.685  1.00  3.65           C  
ATOM    638  CD2 LEU A  86      38.941  21.909   8.024  1.00  4.97           C  
ATOM    639  N   LEU A  87      35.790  18.809   6.382  1.00  5.12           N  
ATOM    640  CA  LEU A  87      34.358  19.060   6.414  1.00  7.59           C  
ATOM    641  C   LEU A  87      33.581  17.795   6.773  1.00  6.44           C  
ATOM    642  O   LEU A  87      32.637  17.840   7.562  1.00  8.23           O  
ATOM    643  CB  LEU A  87      33.895  19.592   5.059  1.00  9.06           C  
ATOM    644  CG  LEU A  87      32.548  20.315   5.038  1.00 12.33           C  
ATOM    645  CD1 LEU A  87      32.672  21.667   5.739  1.00 12.87           C  
ATOM    646  CD2 LEU A  87      32.106  20.510   3.594  1.00 11.21           C  
ATOM    647  N   THR A  88      33.992  16.670   6.198  1.00  8.90           N  
ATOM    648  CA  THR A  88      33.337  15.386   6.447  1.00  8.04           C  
ATOM    649  C   THR A  88      33.460  15.001   7.916  1.00  9.02           C  
ATOM    650  O   THR A  88      32.483  14.594   8.546  1.00  7.05           O  
ATOM    651  CB  THR A  88      33.958  14.268   5.586  1.00  8.82           C  
ATOM    652  OG1 THR A  88      33.755  14.567   4.198  1.00  8.48           O  
ATOM    653  CG2 THR A  88      33.322  12.915   5.916  1.00  8.63           C  
ATOM    654  N   LEU A  89      34.668  15.131   8.454  1.00  8.46           N  
ATOM    655  CA  LEU A  89      34.928  14.802   9.853  1.00  8.71           C  
ATOM    656  C   LEU A  89      34.076  15.644  10.798  1.00  7.97           C  
ATOM    657  O   LEU A  89      33.461  15.118  11.728  1.00  8.54           O  
ATOM    658  CB  LEU A  89      36.414  15.017  10.178  1.00  6.64           C  
ATOM    659  CG  LEU A  89      36.810  14.940  11.659  1.00  6.24           C  
ATOM    660  CD1 LEU A  89      36.413  13.601  12.251  1.00  6.81           C  
ATOM    661  CD2 LEU A  89      38.309  15.160  11.787  1.00  7.98           C  
ATOM    662  N   LEU A  90      34.044  16.949  10.555  1.00  7.58           N  
ATOM    663  CA  LEU A  90      33.280  17.860  11.391  1.00  7.50           C  
ATOM    664  C   LEU A  90      31.779  17.611  11.324  1.00  7.61           C  
ATOM    665  O   LEU A  90      31.085  17.735  12.329  1.00  8.46           O  
ATOM    666  CB  LEU A  90      33.596  19.305  11.009  1.00  6.82           C  
ATOM    667  CG  LEU A  90      35.053  19.710  11.254  1.00  7.45           C  
ATOM    668  CD1 LEU A  90      35.240  21.189  10.926  1.00  7.67           C  
ATOM    669  CD2 LEU A  90      35.430  19.425  12.711  1.00  7.69           C  
ATOM    670  N   LYS A  91      31.274  17.262  10.145  1.00  7.06           N  
ATOM    671  CA  LYS A  91      29.848  16.985  10.011  1.00  8.75           C  
ATOM    672  C   LYS A  91      29.515  15.669  10.706  1.00  6.10           C  
ATOM    673  O   LYS A  91      28.521  15.568  11.420  1.00  8.29           O  
ATOM    674  CB  LYS A  91      29.449  16.894   8.540  1.00  8.67           C  
ATOM    675  CG  LYS A  91      29.443  18.227   7.811  1.00 10.28           C  
ATOM    676  CD  LYS A  91      29.187  18.012   6.336  1.00 10.43           C  
ATOM    677  CE  LYS A  91      29.144  19.333   5.591  1.00 14.32           C  
ATOM    678  NZ  LYS A  91      28.914  19.113   4.136  1.00 15.78           N  
ATOM    679  N   LYS A  92      30.350  14.661  10.481  1.00  7.51           N  
ATOM    680  CA  LYS A  92      30.150  13.351  11.095  1.00  7.21           C  
ATOM    681  C   LYS A  92      30.183  13.421  12.620  1.00  9.20           C  
ATOM    682  O   LYS A  92      29.471  12.675  13.298  1.00 10.05           O  
ATOM    683  CB  LYS A  92      31.207  12.361  10.595  1.00  6.86           C  
ATOM    684  CG  LYS A  92      30.959  11.846   9.181  1.00  6.40           C  
ATOM    685  CD  LYS A  92      29.709  10.972   9.133  1.00  8.85           C  
ATOM    686  CE  LYS A  92      29.428  10.456   7.733  1.00 11.37           C  
ATOM    687  NZ  LYS A  92      28.174   9.641   7.707  1.00 10.96           N  
ATOM    688  N   GLN A  93      31.007  14.315  13.163  1.00  8.00           N  
ATOM    689  CA  GLN A  93      31.106  14.461  14.611  1.00  8.20           C  
ATOM    690  C   GLN A  93      30.208  15.572  15.143  1.00  8.45           C  
ATOM    691  O   GLN A  93      30.296  15.953  16.307  1.00  8.30           O  
ATOM    692  CB  GLN A  93      32.563  14.702  15.020  1.00  8.35           C  
ATOM    693  CG  GLN A  93      33.430  13.453  14.890  1.00  9.13           C  
ATOM    694  CD  GLN A  93      33.065  12.384  15.905  1.00 10.53           C  
ATOM    695  OE1 GLN A  93      33.349  11.199  15.711  1.00 12.34           O  
ATOM    696  NE2 GLN A  93      32.442  12.797  16.998  1.00 12.58           N  
ATOM    697  N   LYS A  94      29.341  16.085  14.276  1.00  9.49           N  
ATOM    698  CA  LYS A  94      28.391  17.129  14.643  1.00  9.56           C  
ATOM    699  C   LYS A  94      28.974  18.405  15.237  1.00 10.29           C  
ATOM    700  O   LYS A  94      28.363  19.034  16.103  1.00 10.11           O  
ATOM    701  CB  LYS A  94      27.335  16.544  15.580  1.00 11.71           C  
ATOM    702  CG  LYS A  94      26.496  15.487  14.887  1.00 14.74           C  
ATOM    703  CD  LYS A  94      25.365  14.977  15.748  1.00 17.02           C  
ATOM    704  CE  LYS A  94      24.454  14.086  14.919  1.00 18.52           C  
ATOM    705  NZ  LYS A  94      25.203  12.941  14.322  1.00 18.72           N  
ATOM    706  N   ILE A  95      30.156  18.787  14.765  1.00  9.39           N  
ATOM    707  CA  ILE A  95      30.799  20.009  15.223  1.00  8.39           C  
ATOM    708  C   ILE A  95      30.179  21.150  14.419  1.00  8.18           C  
ATOM    709  O   ILE A  95      30.026  22.266  14.912  1.00  6.06           O  
ATOM    710  CB  ILE A  95      32.319  19.967  14.976  1.00  9.05           C  
ATOM    711  CG1 ILE A  95      32.906  18.703  15.606  1.00  9.27           C  
ATOM    712  CG2 ILE A  95      32.981  21.208  15.565  1.00  9.18           C  
ATOM    713  CD1 ILE A  95      32.633  18.577  17.103  1.00  7.85           C  
ATOM    714  N   ILE A  96      29.839  20.855  13.168  1.00  9.19           N  
ATOM    715  CA  ILE A  96      29.189  21.826  12.295  1.00 10.46           C  
ATOM    716  C   ILE A  96      27.893  21.175  11.839  1.00 12.17           C  
ATOM    717  O   ILE A  96      27.743  19.955  11.940  1.00 12.32           O  
ATOM    718  CB  ILE A  96      30.046  22.176  11.058  1.00 10.18           C  
ATOM    719  CG1 ILE A  96      30.435  20.903  10.309  1.00  9.77           C  
ATOM    720  CG2 ILE A  96      31.275  22.970  11.487  1.00  9.82           C  
ATOM    721  CD1 ILE A  96      31.274  21.157   9.073  1.00 10.32           C  
ATOM    722  N   ASP A  97      26.959  21.980  11.347  1.00 13.12           N  
ATOM    723  CA  ASP A  97      25.673  21.455  10.907  1.00 13.89           C  
ATOM    724  C   ASP A  97      25.663  21.058   9.437  1.00 14.34           C  
ATOM    725  O   ASP A  97      26.705  21.029   8.783  1.00 11.70           O  
ATOM    726  CB  ASP A  97      24.571  22.478  11.194  1.00 14.85           C  
ATOM    727  CG  ASP A  97      24.799  23.797  10.489  1.00 13.18           C  
ATOM    728  OD1 ASP A  97      24.203  24.803  10.922  1.00 15.40           O  
ATOM    729  OD2 ASP A  97      25.565  23.827   9.504  1.00 13.22           O  
ATOM    730  N   SER A  98      24.477  20.747   8.922  1.00 16.03           N  
ATOM    731  CA  SER A  98      24.330  20.329   7.534  1.00 18.11           C  
ATOM    732  C   SER A  98      24.869  21.344   6.530  1.00 18.90           C  
ATOM    733  O   SER A  98      25.382  20.968   5.476  1.00 17.18           O  
ATOM    734  CB  SER A  98      22.858  20.018   7.233  1.00 18.80           C  
ATOM    735  OG  SER A  98      22.001  21.042   7.708  1.00 22.14           O  
ATOM    736  N   ASP A  99      24.765  22.624   6.872  1.00 18.21           N  
ATOM    737  CA  ASP A  99      25.235  23.705   6.013  1.00 17.88           C  
ATOM    738  C   ASP A  99      26.714  24.008   6.212  1.00 17.20           C  
ATOM    739  O   ASP A  99      27.270  24.877   5.541  1.00 17.21           O  
ATOM    740  CB  ASP A  99      24.424  24.967   6.288  1.00 18.23           C  
ATOM    741  CG  ASP A  99      22.961  24.797   5.950  1.00 21.70           C  
ATOM    742  OD1 ASP A  99      22.108  25.245   6.745  1.00 22.42           O  
ATOM    743  OD2 ASP A  99      22.668  24.218   4.883  1.00 21.55           O  
ATOM    744  N   GLY A 100      27.345  23.301   7.142  1.00 15.93           N  
ATOM    745  CA  GLY A 100      28.757  23.521   7.400  1.00 14.94           C  
ATOM    746  C   GLY A 100      29.012  24.691   8.333  1.00 12.82           C  
ATOM    747  O   GLY A 100      30.111  25.239   8.363  1.00 13.75           O  
ATOM    748  N   ASN A 101      27.994  25.074   9.096  1.00 11.76           N  
ATOM    749  CA  ASN A 101      28.104  26.183  10.039  1.00  9.86           C  
ATOM    750  C   ASN A 101      28.316  25.689  11.463  1.00  9.15           C  
ATOM    751  O   ASN A 101      27.821  24.629  11.846  1.00  8.33           O  
ATOM    752  CB  ASN A 101      26.839  27.034   9.982  1.00 10.52           C  
ATOM    753  CG  ASN A 101      26.614  27.636   8.613  1.00 12.67           C  
ATOM    754  OD1 ASN A 101      25.480  27.892   8.211  1.00 16.25           O  
ATOM    755  ND2 ASN A 101      27.699  27.874   7.891  1.00 10.33           N  
ATOM    756  N   TRP A 102      29.053  26.475  12.240  1.00  8.27           N  
ATOM    757  CA  TRP A 102      29.345  26.156  13.629  1.00  8.09           C  
ATOM    758  C   TRP A 102      28.102  25.661  14.357  1.00  8.33           C  
ATOM    759  O   TRP A 102      27.059  26.314  14.341  1.00  9.16           O  
ATOM    760  CB  TRP A 102      29.899  27.394  14.330  1.00  6.46           C  
ATOM    761  CG  TRP A 102      30.220  27.204  15.782  1.00  5.87           C  
ATOM    762  CD1 TRP A 102      29.412  27.484  16.845  1.00  4.47           C  
ATOM    763  CD2 TRP A 102      31.460  26.742  16.330  1.00  6.75           C  
ATOM    764  NE1 TRP A 102      30.074  27.232  18.023  1.00  6.27           N  
ATOM    765  CE2 TRP A 102      31.335  26.777  17.736  1.00  6.17           C  
ATOM    766  CE3 TRP A 102      32.670  26.306  15.769  1.00  8.92           C  
ATOM    767  CZ2 TRP A 102      32.375  26.395  18.593  1.00  7.08           C  
ATOM    768  CZ3 TRP A 102      33.707  25.923  16.624  1.00  7.05           C  
ATOM    769  CH2 TRP A 102      33.550  25.972  18.019  1.00  5.30           C  
ATOM    770  N   ALA A 103      28.226  24.503  14.994  1.00  8.04           N  
ATOM    771  CA  ALA A 103      27.118  23.909  15.728  1.00 10.61           C  
ATOM    772  C   ALA A 103      27.615  23.352  17.054  1.00 11.12           C  
ATOM    773  O   ALA A 103      26.957  22.512  17.670  1.00 10.47           O  
ATOM    774  CB  ALA A 103      26.486  22.796  14.894  1.00 10.17           C  
ATOM    775  N   PHE A 104      28.773  23.838  17.493  1.00 10.91           N  
ATOM    776  CA  PHE A 104      29.392  23.382  18.733  1.00  9.33           C  
ATOM    777  C   PHE A 104      29.065  24.295  19.914  1.00  8.88           C  
ATOM    778  O   PHE A 104      29.681  24.199  20.971  1.00  9.55           O  
ATOM    779  CB  PHE A 104      30.912  23.288  18.533  1.00  8.33           C  
ATOM    780  CG  PHE A 104      31.607  22.339  19.480  1.00  9.66           C  
ATOM    781  CD1 PHE A 104      31.166  21.025  19.626  1.00  9.95           C  
ATOM    782  CD2 PHE A 104      32.733  22.747  20.191  1.00  9.20           C  
ATOM    783  CE1 PHE A 104      31.837  20.131  20.467  1.00  8.79           C  
ATOM    784  CE2 PHE A 104      33.409  21.861  21.032  1.00  7.84           C  
ATOM    785  CZ  PHE A 104      32.957  20.550  21.167  1.00  7.84           C  
ATOM    786  N   GLY A 105      28.088  25.179  19.729  1.00  9.74           N  
ATOM    787  CA  GLY A 105      27.687  26.080  20.795  1.00  9.15           C  
ATOM    788  C   GLY A 105      28.794  26.902  21.432  1.00  9.18           C  
ATOM    789  O   GLY A 105      29.537  27.596  20.743  1.00 10.32           O  
ATOM    790  N   GLU A 106      28.900  26.826  22.755  1.00  9.04           N  
ATOM    791  CA  GLU A 106      29.912  27.575  23.489  1.00  9.38           C  
ATOM    792  C   GLU A 106      31.207  26.792  23.641  1.00  8.36           C  
ATOM    793  O   GLU A 106      32.100  27.188  24.389  1.00  8.85           O  
ATOM    794  CB  GLU A 106      29.383  27.963  24.874  1.00 12.43           C  
ATOM    795  CG  GLU A 106      28.250  28.979  24.843  1.00 14.59           C  
ATOM    796  CD  GLU A 106      27.802  29.404  26.233  1.00 18.25           C  
ATOM    797  OE1 GLU A 106      26.945  30.307  26.332  1.00 21.04           O  
ATOM    798  OE2 GLU A 106      28.303  28.837  27.227  1.00 19.90           O  
ATOM    799  N   GLY A 107      31.305  25.673  22.935  1.00  6.97           N  
ATOM    800  CA  GLY A 107      32.508  24.871  23.014  1.00  6.28           C  
ATOM    801  C   GLY A 107      33.662  25.552  22.304  1.00  7.18           C  
ATOM    802  O   GLY A 107      33.468  26.492  21.532  1.00  6.09           O  
ATOM    803  N   HIS A 108      34.873  25.078  22.570  1.00  6.43           N  
ATOM    804  CA  HIS A 108      36.052  25.635  21.934  1.00  7.00           C  
ATOM    805  C   HIS A 108      36.693  24.605  21.028  1.00  6.45           C  
ATOM    806  O   HIS A 108      36.756  23.422  21.356  1.00  6.66           O  
ATOM    807  CB  HIS A 108      37.085  26.073  22.975  1.00  7.52           C  
ATOM    808  CG  HIS A 108      36.680  27.280  23.758  1.00  7.97           C  
ATOM    809  ND1 HIS A 108      37.596  28.098  24.382  1.00  8.39           N  
ATOM    810  CD2 HIS A 108      35.462  27.810  24.017  1.00  6.54           C  
ATOM    811  CE1 HIS A 108      36.959  29.082  24.991  1.00  7.79           C  
ATOM    812  NE2 HIS A 108      35.663  28.930  24.786  1.00  7.27           N  
ATOM    813  N   MET A 109      37.155  25.060  19.874  1.00  5.82           N  
ATOM    814  CA  MET A 109      37.836  24.177  18.956  1.00  6.11           C  
ATOM    815  C   MET A 109      39.278  24.618  18.965  1.00  6.07           C  
ATOM    816  O   MET A 109      39.565  25.813  19.010  1.00  5.75           O  
ATOM    817  CB  MET A 109      37.311  24.311  17.533  1.00  5.64           C  
ATOM    818  CG  MET A 109      38.184  23.574  16.527  1.00  5.42           C  
ATOM    819  SD  MET A 109      37.675  23.810  14.819  1.00  7.12           S  
ATOM    820  CE  MET A 109      36.246  22.729  14.765  1.00  6.37           C  
ATOM    821  N   VAL A 110      40.181  23.653  18.937  1.00  4.98           N  
ATOM    822  CA  VAL A 110      41.593  23.968  18.900  1.00  4.87           C  
ATOM    823  C   VAL A 110      42.188  23.251  17.699  1.00  4.19           C  
ATOM    824  O   VAL A 110      42.256  22.027  17.676  1.00  5.15           O  
ATOM    825  CB  VAL A 110      42.332  23.492  20.167  1.00  4.30           C  
ATOM    826  CG1 VAL A 110      43.798  23.872  20.066  1.00  5.33           C  
ATOM    827  CG2 VAL A 110      41.701  24.096  21.413  1.00  3.58           C  
ATOM    828  N   MET A 111      42.572  24.010  16.680  1.00  5.76           N  
ATOM    829  CA  MET A 111      43.191  23.404  15.511  1.00  5.03           C  
ATOM    830  C   MET A 111      44.658  23.735  15.695  1.00  5.71           C  
ATOM    831  O   MET A 111      45.077  24.881  15.504  1.00  4.08           O  
ATOM    832  CB  MET A 111      42.654  24.008  14.215  1.00  4.20           C  
ATOM    833  CG  MET A 111      43.204  23.319  12.983  1.00  4.56           C  
ATOM    834  SD  MET A 111      42.375  23.811  11.485  1.00  5.21           S  
ATOM    835  CE  MET A 111      40.962  22.665  11.496  1.00  5.36           C  
ATOM    836  N   THR A 112      45.433  22.729  16.085  1.00  6.18           N  
ATOM    837  CA  THR A 112      46.844  22.930  16.371  1.00  6.02           C  
ATOM    838  C   THR A 112      47.787  23.107  15.190  1.00  7.30           C  
ATOM    839  O   THR A 112      48.863  22.509  15.151  1.00  5.61           O  
ATOM    840  CB  THR A 112      47.371  21.804  17.288  1.00  8.66           C  
ATOM    841  OG1 THR A 112      47.164  20.531  16.668  1.00  7.85           O  
ATOM    842  CG2 THR A 112      46.625  21.830  18.624  1.00  7.24           C  
ATOM    843  N   GLY A 113      47.367  23.928  14.232  1.00  6.48           N  
ATOM    844  CA  GLY A 113      48.200  24.235  13.085  1.00  7.24           C  
ATOM    845  C   GLY A 113      48.248  23.330  11.869  1.00  7.48           C  
ATOM    846  O   GLY A 113      47.589  22.291  11.784  1.00  5.46           O  
ATOM    847  N   ASP A 114      49.058  23.771  10.914  1.00  6.75           N  
ATOM    848  CA  ASP A 114      49.288  23.083   9.653  1.00  6.33           C  
ATOM    849  C   ASP A 114      48.095  22.916   8.718  1.00  6.19           C  
ATOM    850  O   ASP A 114      47.736  21.803   8.327  1.00  4.59           O  
ATOM    851  CB  ASP A 114      49.966  21.732   9.900  1.00  7.07           C  
ATOM    852  CG  ASP A 114      51.478  21.857  10.039  1.00  5.55           C  
ATOM    853  OD1 ASP A 114      52.163  20.817  10.020  1.00  8.14           O  
ATOM    854  OD2 ASP A 114      51.983  22.995  10.173  1.00  5.02           O  
ATOM    855  N   ILE A 115      47.485  24.042   8.368  1.00  5.92           N  
ATOM    856  CA  ILE A 115      46.382  24.073   7.417  1.00  5.67           C  
ATOM    857  C   ILE A 115      47.067  24.100   6.050  1.00  4.59           C  
ATOM    858  O   ILE A 115      46.650  23.423   5.115  1.00  5.77           O  
ATOM    859  CB  ILE A 115      45.542  25.363   7.552  1.00  4.02           C  
ATOM    860  CG1 ILE A 115      44.612  25.269   8.760  1.00  4.49           C  
ATOM    861  CG2 ILE A 115      44.733  25.609   6.280  1.00  6.20           C  
ATOM    862  CD1 ILE A 115      43.786  26.521   8.974  1.00  4.91           C  
ATOM    863  N   PHE A 116      48.132  24.892   5.954  1.00  5.18           N  
ATOM    864  CA  PHE A 116      48.891  25.040   4.712  1.00  7.22           C  
ATOM    865  C   PHE A 116      49.657  23.804   4.264  1.00  6.54           C  
ATOM    866  O   PHE A 116      49.939  22.901   5.054  1.00  7.06           O  
ATOM    867  CB  PHE A 116      49.934  26.162   4.833  1.00  6.50           C  
ATOM    868  CG  PHE A 116      49.364  27.545   4.803  1.00  7.00           C  
ATOM    869  CD1 PHE A 116      48.959  28.173   5.973  1.00  8.13           C  
ATOM    870  CD2 PHE A 116      49.241  28.230   3.597  1.00  7.61           C  
ATOM    871  CE1 PHE A 116      48.439  29.468   5.945  1.00  7.88           C  
ATOM    872  CE2 PHE A 116      48.722  29.522   3.557  1.00  8.68           C  
ATOM    873  CZ  PHE A 116      48.321  30.143   4.733  1.00  8.22           C  
ATOM    874  N   ASP A 117      50.002  23.810   2.980  1.00  7.16           N  
ATOM    875  CA  ASP A 117      50.821  22.786   2.337  1.00  7.98           C  
ATOM    876  C   ASP A 117      50.311  21.370   2.121  1.00  7.92           C  
ATOM    877  O   ASP A 117      49.447  20.874   2.840  1.00  7.24           O  
ATOM    878  CB  ASP A 117      52.177  22.748   3.042  1.00  7.94           C  
ATOM    879  CG  ASP A 117      52.920  24.061   2.914  1.00  9.65           C  
ATOM    880  OD1 ASP A 117      53.922  24.259   3.627  1.00  7.76           O  
ATOM    881  OD2 ASP A 117      52.494  24.899   2.086  1.00  7.05           O  
ATOM    882  N   ARG A 118      50.883  20.740   1.093  1.00  9.91           N  
ATOM    883  CA  ARG A 118      50.566  19.380   0.674  1.00  9.89           C  
ATOM    884  C   ARG A 118      49.247  19.270  -0.083  1.00 10.27           C  
ATOM    885  O   ARG A 118      49.225  18.848  -1.244  1.00  9.46           O  
ATOM    886  CB  ARG A 118      50.550  18.431   1.876  1.00 12.47           C  
ATOM    887  CG  ARG A 118      51.899  18.264   2.560  1.00 16.15           C  
ATOM    888  CD  ARG A 118      51.906  17.012   3.431  1.00 21.54           C  
ATOM    889  NE  ARG A 118      53.244  16.663   3.900  1.00 24.05           N  
ATOM    890  CZ  ARG A 118      53.883  17.296   4.876  1.00 25.38           C  
ATOM    891  NH1 ARG A 118      55.103  16.912   5.233  1.00 25.62           N  
ATOM    892  NH2 ARG A 118      53.294  18.302   5.504  1.00 25.89           N  
ATOM    893  N   GLY A 119      48.158  19.666   0.570  1.00  8.17           N  
ATOM    894  CA  GLY A 119      46.841  19.592  -0.038  1.00  8.75           C  
ATOM    895  C   GLY A 119      46.562  20.593  -1.144  1.00  9.22           C  
ATOM    896  O   GLY A 119      47.310  21.556  -1.339  1.00  8.12           O  
ATOM    897  N   HIS A 120      45.458  20.363  -1.849  1.00  6.70           N  
ATOM    898  CA  HIS A 120      45.037  21.193  -2.975  1.00  6.99           C  
ATOM    899  C   HIS A 120      43.838  22.096  -2.670  1.00  6.30           C  
ATOM    900  O   HIS A 120      43.334  22.784  -3.562  1.00  3.39           O  
ATOM    901  CB  HIS A 120      44.671  20.286  -4.148  1.00  6.73           C  
ATOM    902  CG  HIS A 120      43.573  19.321  -3.830  1.00  6.38           C  
ATOM    903  ND1 HIS A 120      43.648  18.431  -2.779  1.00  8.52           N  
ATOM    904  CD2 HIS A 120      42.359  19.130  -4.398  1.00  8.47           C  
ATOM    905  CE1 HIS A 120      42.526  17.737  -2.712  1.00  7.78           C  
ATOM    906  NE2 HIS A 120      41.727  18.142  -3.683  1.00  7.30           N  
ATOM    907  N   GLN A 121      43.374  22.094  -1.424  1.00  5.80           N  
ATOM    908  CA  GLN A 121      42.225  22.921  -1.055  1.00  3.22           C  
ATOM    909  C   GLN A 121      42.567  23.815   0.130  1.00  4.25           C  
ATOM    910  O   GLN A 121      41.774  23.970   1.058  1.00  4.89           O  
ATOM    911  CB  GLN A 121      41.040  22.024  -0.704  1.00  3.84           C  
ATOM    912  CG  GLN A 121      40.868  20.863  -1.662  1.00  4.48           C  
ATOM    913  CD  GLN A 121      39.674  20.003  -1.311  1.00  8.26           C  
ATOM    914  OE1 GLN A 121      38.655  20.027  -1.998  1.00 13.11           O  
ATOM    915  NE2 GLN A 121      39.789  19.249  -0.231  1.00  1.54           N  
ATOM    916  N   VAL A 122      43.753  24.413   0.083  1.00  3.64           N  
ATOM    917  CA  VAL A 122      44.222  25.270   1.161  1.00  4.53           C  
ATOM    918  C   VAL A 122      43.328  26.483   1.406  1.00  5.32           C  
ATOM    919  O   VAL A 122      42.933  26.739   2.540  1.00  5.64           O  
ATOM    920  CB  VAL A 122      45.673  25.727   0.896  1.00  3.96           C  
ATOM    921  CG1 VAL A 122      46.159  26.637   2.016  1.00  5.82           C  
ATOM    922  CG2 VAL A 122      46.578  24.500   0.791  1.00  6.16           C  
ATOM    923  N   ASN A 123      43.002  27.227   0.354  1.00  5.45           N  
ATOM    924  CA  ASN A 123      42.148  28.400   0.524  1.00  7.24           C  
ATOM    925  C   ASN A 123      40.755  28.013   1.002  1.00  6.35           C  
ATOM    926  O   ASN A 123      40.107  28.778   1.720  1.00  5.43           O  
ATOM    927  CB  ASN A 123      42.067  29.197  -0.780  1.00  6.39           C  
ATOM    928  CG  ASN A 123      43.330  29.989  -1.048  1.00  7.04           C  
ATOM    929  OD1 ASN A 123      43.885  29.944  -2.149  1.00  8.03           O  
ATOM    930  ND2 ASN A 123      43.792  30.725  -0.040  1.00  3.99           N  
ATOM    931  N   GLU A 124      40.292  26.831   0.606  1.00  3.29           N  
ATOM    932  CA  GLU A 124      38.979  26.369   1.049  1.00  4.75           C  
ATOM    933  C   GLU A 124      39.022  26.200   2.566  1.00  4.44           C  
ATOM    934  O   GLU A 124      38.118  26.639   3.279  1.00  2.42           O  
ATOM    935  CB  GLU A 124      38.615  25.029   0.397  1.00  5.44           C  
ATOM    936  CG  GLU A 124      38.181  25.100  -1.072  1.00  7.79           C  
ATOM    937  CD  GLU A 124      39.310  25.449  -2.034  1.00  8.73           C  
ATOM    938  OE1 GLU A 124      40.495  25.263  -1.686  1.00  8.05           O  
ATOM    939  OE2 GLU A 124      39.006  25.896  -3.159  1.00  7.57           O  
ATOM    940  N   VAL A 125      40.085  25.566   3.054  1.00  4.66           N  
ATOM    941  CA  VAL A 125      40.256  25.344   4.486  1.00  4.08           C  
ATOM    942  C   VAL A 125      40.378  26.677   5.232  1.00  5.33           C  
ATOM    943  O   VAL A 125      39.724  26.890   6.255  1.00  4.59           O  
ATOM    944  CB  VAL A 125      41.525  24.492   4.777  1.00  4.88           C  
ATOM    945  CG1 VAL A 125      41.688  24.289   6.273  1.00  3.62           C  
ATOM    946  CG2 VAL A 125      41.425  23.145   4.072  1.00  6.09           C  
ATOM    947  N   LEU A 126      41.213  27.575   4.715  1.00  5.13           N  
ATOM    948  CA  LEU A 126      41.413  28.877   5.345  1.00  5.45           C  
ATOM    949  C   LEU A 126      40.132  29.697   5.487  1.00  5.59           C  
ATOM    950  O   LEU A 126      39.807  30.174   6.577  1.00  5.51           O  
ATOM    951  CB  LEU A 126      42.448  29.689   4.563  1.00  6.56           C  
ATOM    952  CG  LEU A 126      43.878  29.150   4.577  1.00  7.39           C  
ATOM    953  CD1 LEU A 126      44.712  29.936   3.587  1.00  5.94           C  
ATOM    954  CD2 LEU A 126      44.462  29.245   5.982  1.00  6.45           C  
ATOM    955  N   TRP A 127      39.406  29.872   4.391  1.00  5.61           N  
ATOM    956  CA  TRP A 127      38.174  30.649   4.446  1.00  5.88           C  
ATOM    957  C   TRP A 127      37.102  29.967   5.289  1.00  5.98           C  
ATOM    958  O   TRP A 127      36.264  30.638   5.901  1.00  5.56           O  
ATOM    959  CB  TRP A 127      37.664  30.928   3.032  1.00  5.87           C  
ATOM    960  CG  TRP A 127      38.480  31.985   2.354  1.00  7.48           C  
ATOM    961  CD1 TRP A 127      39.241  31.846   1.226  1.00  8.80           C  
ATOM    962  CD2 TRP A 127      38.661  33.334   2.796  1.00  8.89           C  
ATOM    963  NE1 TRP A 127      39.885  33.028   0.942  1.00  6.99           N  
ATOM    964  CE2 TRP A 127      39.546  33.957   1.890  1.00  8.17           C  
ATOM    965  CE3 TRP A 127      38.161  34.079   3.876  1.00  9.62           C  
ATOM    966  CZ2 TRP A 127      39.944  35.295   2.028  1.00 10.82           C  
ATOM    967  CZ3 TRP A 127      38.558  35.412   4.014  1.00 11.13           C  
ATOM    968  CH2 TRP A 127      39.441  36.002   3.093  1.00  9.77           C  
ATOM    969  N   PHE A 128      37.120  28.639   5.321  1.00  4.06           N  
ATOM    970  CA  PHE A 128      36.151  27.911   6.132  1.00  6.67           C  
ATOM    971  C   PHE A 128      36.471  28.171   7.604  1.00  7.08           C  
ATOM    972  O   PHE A 128      35.584  28.492   8.399  1.00  6.44           O  
ATOM    973  CB  PHE A 128      36.221  26.410   5.856  1.00  8.07           C  
ATOM    974  CG  PHE A 128      35.505  25.579   6.882  1.00  9.40           C  
ATOM    975  CD1 PHE A 128      34.120  25.634   7.001  1.00 10.84           C  
ATOM    976  CD2 PHE A 128      36.221  24.768   7.757  1.00  9.79           C  
ATOM    977  CE1 PHE A 128      33.454  24.892   7.984  1.00 13.00           C  
ATOM    978  CE2 PHE A 128      35.569  24.022   8.741  1.00 10.78           C  
ATOM    979  CZ  PHE A 128      34.181  24.084   8.855  1.00 11.56           C  
ATOM    980  N   MET A 129      37.746  28.033   7.961  1.00  4.21           N  
ATOM    981  CA  MET A 129      38.169  28.258   9.338  1.00  6.43           C  
ATOM    982  C   MET A 129      37.935  29.705   9.767  1.00  7.49           C  
ATOM    983  O   MET A 129      37.561  29.965  10.910  1.00  6.90           O  
ATOM    984  CB  MET A 129      39.642  27.883   9.514  1.00  5.97           C  
ATOM    985  CG  MET A 129      39.903  26.381   9.472  1.00  5.33           C  
ATOM    986  SD  MET A 129      38.813  25.466  10.606  1.00  6.06           S  
ATOM    987  CE  MET A 129      39.351  26.103  12.217  1.00  5.17           C  
ATOM    988  N   TYR A 130      38.159  30.637   8.846  1.00  6.21           N  
ATOM    989  CA  TYR A 130      37.952  32.055   9.102  1.00  6.22           C  
ATOM    990  C   TYR A 130      36.475  32.263   9.443  1.00  5.62           C  
ATOM    991  O   TYR A 130      36.132  32.981  10.383  1.00  4.29           O  
ATOM    992  CB  TYR A 130      38.353  32.850   7.852  1.00  7.52           C  
ATOM    993  CG  TYR A 130      38.149  34.346   7.918  1.00  7.38           C  
ATOM    994  CD1 TYR A 130      36.880  34.907   7.762  1.00  6.32           C  
ATOM    995  CD2 TYR A 130      39.235  35.209   8.077  1.00  7.55           C  
ATOM    996  CE1 TYR A 130      36.699  36.290   7.751  1.00  7.41           C  
ATOM    997  CE2 TYR A 130      39.067  36.588   8.069  1.00  7.24           C  
ATOM    998  CZ  TYR A 130      37.797  37.124   7.902  1.00  9.06           C  
ATOM    999  OH  TYR A 130      37.630  38.492   7.864  1.00  8.64           O  
ATOM   1000  N   GLN A 131      35.602  31.613   8.680  1.00  7.51           N  
ATOM   1001  CA  GLN A 131      34.165  31.710   8.911  1.00  6.94           C  
ATOM   1002  C   GLN A 131      33.782  31.081  10.251  1.00  6.26           C  
ATOM   1003  O   GLN A 131      32.990  31.646  11.005  1.00  5.24           O  
ATOM   1004  CB  GLN A 131      33.405  31.015   7.777  1.00  7.86           C  
ATOM   1005  CG  GLN A 131      31.896  31.102   7.894  1.00  9.40           C  
ATOM   1006  CD  GLN A 131      31.197  30.623   6.635  1.00 10.81           C  
ATOM   1007  OE1 GLN A 131      31.085  29.423   6.385  1.00 12.10           O  
ATOM   1008  NE2 GLN A 131      30.741  31.567   5.824  1.00 13.65           N  
ATOM   1009  N   LEU A 132      34.337  29.907  10.537  1.00  5.64           N  
ATOM   1010  CA  LEU A 132      34.056  29.210  11.793  1.00  6.82           C  
ATOM   1011  C   LEU A 132      34.470  30.066  12.975  1.00  5.69           C  
ATOM   1012  O   LEU A 132      33.797  30.096  14.007  1.00  4.52           O  
ATOM   1013  CB  LEU A 132      34.825  27.889  11.877  1.00  7.14           C  
ATOM   1014  CG  LEU A 132      34.183  26.565  11.466  1.00 13.15           C  
ATOM   1015  CD1 LEU A 132      34.955  25.434  12.158  1.00  9.34           C  
ATOM   1016  CD2 LEU A 132      32.714  26.512  11.872  1.00  7.40           C  
ATOM   1017  N   ASP A 133      35.603  30.741  12.814  1.00  4.82           N  
ATOM   1018  CA  ASP A 133      36.155  31.616  13.841  1.00  5.64           C  
ATOM   1019  C   ASP A 133      35.083  32.616  14.267  1.00  6.26           C  
ATOM   1020  O   ASP A 133      34.797  32.785  15.457  1.00  6.65           O  
ATOM   1021  CB  ASP A 133      37.352  32.366  13.256  1.00  6.17           C  
ATOM   1022  CG  ASP A 133      38.273  32.938  14.310  1.00  8.04           C  
ATOM   1023  OD1 ASP A 133      37.856  33.099  15.479  1.00  7.28           O  
ATOM   1024  OD2 ASP A 133      39.428  33.249  13.951  1.00  8.05           O  
ATOM   1025  N   GLN A 134      34.495  33.288  13.283  1.00  7.21           N  
ATOM   1026  CA  GLN A 134      33.461  34.276  13.560  1.00  6.73           C  
ATOM   1027  C   GLN A 134      32.176  33.631  14.076  1.00  7.85           C  
ATOM   1028  O   GLN A 134      31.554  34.139  15.010  1.00  6.41           O  
ATOM   1029  CB  GLN A 134      33.151  35.094  12.305  1.00  8.99           C  
ATOM   1030  CG  GLN A 134      32.055  36.127  12.520  1.00 13.05           C  
ATOM   1031  CD  GLN A 134      32.443  37.192  13.536  1.00 14.68           C  
ATOM   1032  OE1 GLN A 134      33.264  38.067  13.256  1.00 16.89           O  
ATOM   1033  NE2 GLN A 134      31.858  37.116  14.726  1.00 17.44           N  
ATOM   1034  N   GLN A 135      31.778  32.517  13.464  1.00  7.16           N  
ATOM   1035  CA  GLN A 135      30.562  31.815  13.876  1.00  7.61           C  
ATOM   1036  C   GLN A 135      30.664  31.298  15.307  1.00  8.26           C  
ATOM   1037  O   GLN A 135      29.681  31.317  16.054  1.00  6.07           O  
ATOM   1038  CB  GLN A 135      30.265  30.656  12.916  1.00  7.33           C  
ATOM   1039  CG  GLN A 135      29.751  31.122  11.559  1.00  7.02           C  
ATOM   1040  CD  GLN A 135      29.540  29.991  10.570  1.00  8.37           C  
ATOM   1041  OE1 GLN A 135      28.964  30.191   9.500  1.00 11.92           O  
ATOM   1042  NE2 GLN A 135      30.017  28.804  10.911  1.00  2.93           N  
ATOM   1043  N   ALA A 136      31.852  30.842  15.694  1.00  6.34           N  
ATOM   1044  CA  ALA A 136      32.050  30.342  17.047  1.00  7.09           C  
ATOM   1045  C   ALA A 136      31.884  31.487  18.035  1.00  6.78           C  
ATOM   1046  O   ALA A 136      31.192  31.356  19.042  1.00  5.47           O  
ATOM   1047  CB  ALA A 136      33.437  29.723  17.192  1.00  6.53           C  
ATOM   1048  N   ARG A 137      32.520  32.614  17.741  1.00  6.77           N  
ATOM   1049  CA  ARG A 137      32.433  33.771  18.621  1.00  8.64           C  
ATOM   1050  C   ARG A 137      30.984  34.225  18.754  1.00 10.26           C  
ATOM   1051  O   ARG A 137      30.529  34.560  19.853  1.00 10.52           O  
ATOM   1052  CB  ARG A 137      33.299  34.908  18.082  1.00 11.05           C  
ATOM   1053  CG  ARG A 137      33.251  36.159  18.919  1.00 13.58           C  
ATOM   1054  CD  ARG A 137      34.405  37.074  18.581  1.00 14.12           C  
ATOM   1055  NE  ARG A 137      34.303  38.355  19.269  1.00 16.27           N  
ATOM   1056  CZ  ARG A 137      35.303  39.223  19.370  1.00 18.51           C  
ATOM   1057  NH1 ARG A 137      36.484  38.939  18.832  1.00 16.64           N  
ATOM   1058  NH2 ARG A 137      35.119  40.379  20.000  1.00 16.72           N  
ATOM   1059  N   ASP A 138      30.264  34.230  17.635  1.00  9.36           N  
ATOM   1060  CA  ASP A 138      28.861  34.625  17.632  1.00 10.73           C  
ATOM   1061  C   ASP A 138      28.050  33.714  18.551  1.00 10.48           C  
ATOM   1062  O   ASP A 138      27.079  34.152  19.162  1.00  9.85           O  
ATOM   1063  CB  ASP A 138      28.281  34.547  16.219  1.00 11.61           C  
ATOM   1064  CG  ASP A 138      28.804  35.638  15.305  1.00 14.39           C  
ATOM   1065  OD1 ASP A 138      28.563  35.545  14.082  1.00 15.36           O  
ATOM   1066  OD2 ASP A 138      29.445  36.589  15.802  1.00 14.91           O  
ATOM   1067  N   ALA A 139      28.453  32.451  18.648  1.00  8.00           N  
ATOM   1068  CA  ALA A 139      27.744  31.482  19.483  1.00  8.66           C  
ATOM   1069  C   ALA A 139      28.211  31.462  20.938  1.00  8.61           C  
ATOM   1070  O   ALA A 139      27.665  30.723  21.760  1.00  8.74           O  
ATOM   1071  CB  ALA A 139      27.881  30.090  18.885  1.00  7.31           C  
ATOM   1072  N   GLY A 140      29.215  32.271  21.260  1.00  7.77           N  
ATOM   1073  CA  GLY A 140      29.723  32.288  22.618  1.00  6.66           C  
ATOM   1074  C   GLY A 140      30.814  31.244  22.805  1.00  7.71           C  
ATOM   1075  O   GLY A 140      31.266  30.983  23.923  1.00  7.04           O  
ATOM   1076  N   GLY A 141      31.228  30.636  21.698  1.00  6.93           N  
ATOM   1077  CA  GLY A 141      32.279  29.635  21.742  1.00  7.03           C  
ATOM   1078  C   GLY A 141      33.561  30.240  21.200  1.00  8.71           C  
ATOM   1079  O   GLY A 141      33.717  31.462  21.180  1.00  7.54           O  
ATOM   1080  N   MET A 142      34.484  29.405  20.743  1.00  8.87           N  
ATOM   1081  CA  MET A 142      35.729  29.945  20.226  1.00  9.02           C  
ATOM   1082  C   MET A 142      36.502  28.964  19.368  1.00  7.34           C  
ATOM   1083  O   MET A 142      36.492  27.763  19.614  1.00  5.31           O  
ATOM   1084  CB  MET A 142      36.615  30.385  21.391  1.00 12.20           C  
ATOM   1085  CG  MET A 142      37.599  31.495  21.057  1.00 19.18           C  
ATOM   1086  SD  MET A 142      38.536  32.006  22.511  1.00 21.63           S  
ATOM   1087  CE  MET A 142      37.277  32.042  23.729  1.00 22.47           C  
ATOM   1088  N   VAL A 143      37.161  29.499  18.349  1.00  5.24           N  
ATOM   1089  CA  VAL A 143      38.003  28.703  17.474  1.00  5.56           C  
ATOM   1090  C   VAL A 143      39.419  29.179  17.752  1.00  5.41           C  
ATOM   1091  O   VAL A 143      39.717  30.365  17.615  1.00  5.37           O  
ATOM   1092  CB  VAL A 143      37.711  28.949  15.981  1.00  5.54           C  
ATOM   1093  CG1 VAL A 143      38.802  28.292  15.130  1.00  6.04           C  
ATOM   1094  CG2 VAL A 143      36.351  28.374  15.613  1.00  4.21           C  
ATOM   1095  N   HIS A 144      40.276  28.260  18.173  1.00  6.69           N  
ATOM   1096  CA  HIS A 144      41.661  28.593  18.443  1.00  6.66           C  
ATOM   1097  C   HIS A 144      42.478  28.028  17.295  1.00  5.82           C  
ATOM   1098  O   HIS A 144      42.766  26.839  17.273  1.00  5.78           O  
ATOM   1099  CB  HIS A 144      42.144  27.946  19.743  1.00  6.32           C  
ATOM   1100  CG  HIS A 144      41.406  28.402  20.957  1.00  6.86           C  
ATOM   1101  ND1 HIS A 144      41.651  29.614  21.565  1.00  5.44           N  
ATOM   1102  CD2 HIS A 144      40.418  27.814  21.671  1.00  4.69           C  
ATOM   1103  CE1 HIS A 144      40.846  29.751  22.603  1.00  9.15           C  
ATOM   1104  NE2 HIS A 144      40.087  28.673  22.690  1.00  5.42           N  
ATOM   1105  N   LEU A 145      42.821  28.867  16.326  1.00  5.41           N  
ATOM   1106  CA  LEU A 145      43.646  28.395  15.232  1.00  4.48           C  
ATOM   1107  C   LEU A 145      45.067  28.725  15.654  1.00  4.70           C  
ATOM   1108  O   LEU A 145      45.424  29.894  15.772  1.00  4.37           O  
ATOM   1109  CB  LEU A 145      43.299  29.116  13.927  1.00  6.10           C  
ATOM   1110  CG  LEU A 145      44.222  28.759  12.761  1.00  7.57           C  
ATOM   1111  CD1 LEU A 145      44.312  27.242  12.615  1.00  8.31           C  
ATOM   1112  CD2 LEU A 145      43.700  29.401  11.482  1.00  8.48           C  
ATOM   1113  N   LEU A 146      45.860  27.691  15.918  1.00  5.37           N  
ATOM   1114  CA  LEU A 146      47.243  27.878  16.343  1.00  5.85           C  
ATOM   1115  C   LEU A 146      48.160  27.772  15.138  1.00  5.78           C  
ATOM   1116  O   LEU A 146      47.861  27.058  14.184  1.00  5.72           O  
ATOM   1117  CB  LEU A 146      47.643  26.814  17.365  1.00  5.76           C  
ATOM   1118  CG  LEU A 146      46.794  26.660  18.628  1.00  8.34           C  
ATOM   1119  CD1 LEU A 146      47.458  25.631  19.544  1.00  7.88           C  
ATOM   1120  CD2 LEU A 146      46.661  27.998  19.342  1.00  3.47           C  
ATOM   1121  N   MET A 147      49.274  28.491  15.189  1.00  5.54           N  
ATOM   1122  CA  MET A 147      50.245  28.480  14.108  1.00  6.61           C  
ATOM   1123  C   MET A 147      51.095  27.213  14.181  1.00  4.95           C  
ATOM   1124  O   MET A 147      51.679  26.909  15.225  1.00  5.85           O  
ATOM   1125  CB  MET A 147      51.160  29.704  14.213  1.00  6.87           C  
ATOM   1126  CG  MET A 147      50.456  31.038  14.078  1.00  5.99           C  
ATOM   1127  SD  MET A 147      49.961  31.363  12.382  1.00  8.85           S  
ATOM   1128  CE  MET A 147      51.519  31.844  11.657  1.00  9.18           C  
ATOM   1129  N   GLY A 148      51.142  26.476  13.073  1.00  4.31           N  
ATOM   1130  CA  GLY A 148      51.944  25.264  12.997  1.00  4.34           C  
ATOM   1131  C   GLY A 148      53.232  25.608  12.265  1.00  4.68           C  
ATOM   1132  O   GLY A 148      53.403  26.755  11.848  1.00  3.56           O  
ATOM   1133  N   ASN A 149      54.144  24.656  12.088  1.00  4.73           N  
ATOM   1134  CA  ASN A 149      55.376  25.010  11.399  1.00  5.24           C  
ATOM   1135  C   ASN A 149      55.139  25.363   9.936  1.00  5.66           C  
ATOM   1136  O   ASN A 149      55.904  26.119   9.353  1.00  7.21           O  
ATOM   1137  CB  ASN A 149      56.449  23.908  11.529  1.00  6.90           C  
ATOM   1138  CG  ASN A 149      56.076  22.620  10.830  1.00  6.03           C  
ATOM   1139  OD1 ASN A 149      56.856  22.090  10.032  1.00 10.27           O  
ATOM   1140  ND2 ASN A 149      54.899  22.097  11.134  1.00  4.51           N  
ATOM   1141  N   HIS A 150      54.075  24.845   9.334  1.00  5.37           N  
ATOM   1142  CA  HIS A 150      53.830  25.180   7.939  1.00  4.88           C  
ATOM   1143  C   HIS A 150      53.303  26.593   7.772  1.00  4.26           C  
ATOM   1144  O   HIS A 150      53.584  27.243   6.767  1.00  2.30           O  
ATOM   1145  CB  HIS A 150      52.904  24.151   7.308  1.00  6.39           C  
ATOM   1146  CG  HIS A 150      53.613  22.891   6.935  1.00  6.24           C  
ATOM   1147  ND1 HIS A 150      54.156  22.692   5.685  1.00  5.20           N  
ATOM   1148  CD2 HIS A 150      53.953  21.806   7.671  1.00  5.83           C  
ATOM   1149  CE1 HIS A 150      54.802  21.540   5.666  1.00  7.60           C  
ATOM   1150  NE2 HIS A 150      54.694  20.983   6.858  1.00  7.69           N  
ATOM   1151  N   GLU A 151      52.543  27.079   8.751  1.00  5.51           N  
ATOM   1152  CA  GLU A 151      52.057  28.455   8.673  1.00  5.72           C  
ATOM   1153  C   GLU A 151      53.279  29.366   8.743  1.00  5.46           C  
ATOM   1154  O   GLU A 151      53.365  30.373   8.035  1.00  4.24           O  
ATOM   1155  CB  GLU A 151      51.114  28.783   9.837  1.00  6.85           C  
ATOM   1156  CG  GLU A 151      49.684  28.313   9.631  1.00  5.45           C  
ATOM   1157  CD  GLU A 151      49.563  26.807   9.649  1.00  8.48           C  
ATOM   1158  OE1 GLU A 151      48.794  26.259   8.826  1.00  6.76           O  
ATOM   1159  OE2 GLU A 151      50.232  26.174  10.495  1.00  5.48           O  
ATOM   1160  N   GLN A 152      54.228  28.998   9.598  1.00  5.46           N  
ATOM   1161  CA  GLN A 152      55.453  29.773   9.768  1.00  5.38           C  
ATOM   1162  C   GLN A 152      56.317  29.726   8.513  1.00  6.31           C  
ATOM   1163  O   GLN A 152      56.902  30.731   8.106  1.00  5.97           O  
ATOM   1164  CB  GLN A 152      56.237  29.246  10.974  1.00  6.14           C  
ATOM   1165  CG  GLN A 152      55.567  29.563  12.309  1.00  6.55           C  
ATOM   1166  CD  GLN A 152      56.255  28.906  13.497  1.00  7.14           C  
ATOM   1167  OE1 GLN A 152      56.042  29.300  14.644  1.00  8.42           O  
ATOM   1168  NE2 GLN A 152      57.075  27.897  13.229  1.00  4.57           N  
ATOM   1169  N   MET A 153      56.376  28.557   7.890  1.00  6.95           N  
ATOM   1170  CA  MET A 153      57.168  28.374   6.683  1.00  8.67           C  
ATOM   1171  C   MET A 153      56.624  29.207   5.530  1.00  7.99           C  
ATOM   1172  O   MET A 153      57.362  29.960   4.892  1.00  8.03           O  
ATOM   1173  CB  MET A 153      57.175  26.896   6.304  1.00 10.17           C  
ATOM   1174  CG  MET A 153      57.905  26.029   7.309  1.00 10.67           C  
ATOM   1175  SD  MET A 153      57.456  24.295   7.155  1.00 15.18           S  
ATOM   1176  CE  MET A 153      58.509  23.823   5.830  1.00 14.49           C  
ATOM   1177  N   VAL A 154      55.330  29.073   5.270  1.00  6.68           N  
ATOM   1178  CA  VAL A 154      54.696  29.815   4.187  1.00  7.51           C  
ATOM   1179  C   VAL A 154      54.843  31.323   4.365  1.00  8.37           C  
ATOM   1180  O   VAL A 154      55.336  32.011   3.468  1.00  9.27           O  
ATOM   1181  CB  VAL A 154      53.197  29.453   4.066  1.00  6.26           C  
ATOM   1182  CG1 VAL A 154      52.486  30.427   3.135  1.00  5.31           C  
ATOM   1183  CG2 VAL A 154      53.057  28.036   3.534  1.00  8.82           C  
ATOM   1184  N   LEU A 155      54.423  31.843   5.513  1.00  8.47           N  
ATOM   1185  CA  LEU A 155      54.524  33.278   5.743  1.00  7.93           C  
ATOM   1186  C   LEU A 155      55.958  33.778   5.642  1.00  9.02           C  
ATOM   1187  O   LEU A 155      56.195  34.908   5.215  1.00  7.96           O  
ATOM   1188  CB  LEU A 155      53.941  33.653   7.107  1.00  7.64           C  
ATOM   1189  CG  LEU A 155      52.420  33.823   7.155  1.00 12.78           C  
ATOM   1190  CD1 LEU A 155      51.735  32.500   6.852  1.00 13.62           C  
ATOM   1191  CD2 LEU A 155      52.012  34.335   8.535  1.00 10.64           C  
ATOM   1192  N   GLY A 156      56.905  32.923   6.017  1.00  9.43           N  
ATOM   1193  CA  GLY A 156      58.311  33.288   5.980  1.00 10.85           C  
ATOM   1194  C   GLY A 156      59.027  33.058   4.662  1.00 10.49           C  
ATOM   1195  O   GLY A 156      60.143  33.539   4.482  1.00 11.36           O  
ATOM   1196  N   GLY A 157      58.414  32.321   3.740  1.00 11.02           N  
ATOM   1197  CA  GLY A 157      59.059  32.095   2.455  1.00  9.35           C  
ATOM   1198  C   GLY A 157      59.624  30.709   2.186  1.00  9.71           C  
ATOM   1199  O   GLY A 157      60.304  30.508   1.181  1.00 10.31           O  
ATOM   1200  N   ASP A 158      59.373  29.759   3.080  1.00  8.91           N  
ATOM   1201  CA  ASP A 158      59.838  28.386   2.880  1.00 10.35           C  
ATOM   1202  C   ASP A 158      58.652  27.690   2.211  1.00  8.85           C  
ATOM   1203  O   ASP A 158      57.733  27.236   2.889  1.00  7.33           O  
ATOM   1204  CB  ASP A 158      60.151  27.733   4.224  1.00 10.10           C  
ATOM   1205  CG  ASP A 158      60.694  26.323   4.080  1.00 12.16           C  
ATOM   1206  OD1 ASP A 158      60.727  25.797   2.945  1.00 13.08           O  
ATOM   1207  OD2 ASP A 158      61.086  25.741   5.111  1.00 11.58           O  
ATOM   1208  N   LEU A 159      58.690  27.605   0.883  1.00 10.13           N  
ATOM   1209  CA  LEU A 159      57.591  27.039   0.095  1.00 10.09           C  
ATOM   1210  C   LEU A 159      57.783  25.623  -0.448  1.00  9.77           C  
ATOM   1211  O   LEU A 159      57.116  25.228  -1.407  1.00  7.62           O  
ATOM   1212  CB  LEU A 159      57.304  27.978  -1.081  1.00 10.53           C  
ATOM   1213  CG  LEU A 159      57.352  29.474  -0.753  1.00 12.35           C  
ATOM   1214  CD1 LEU A 159      57.314  30.286  -2.036  1.00 13.17           C  
ATOM   1215  CD2 LEU A 159      56.187  29.842   0.160  1.00 11.45           C  
ATOM   1216  N   ARG A 160      58.669  24.855   0.170  1.00  8.87           N  
ATOM   1217  CA  ARG A 160      58.954  23.501  -0.284  1.00  9.53           C  
ATOM   1218  C   ARG A 160      57.764  22.543  -0.313  1.00 11.25           C  
ATOM   1219  O   ARG A 160      57.778  21.561  -1.056  1.00 11.45           O  
ATOM   1220  CB  ARG A 160      60.062  22.898   0.579  1.00 10.15           C  
ATOM   1221  CG  ARG A 160      61.417  23.559   0.407  1.00  9.71           C  
ATOM   1222  CD  ARG A 160      62.399  22.988   1.408  1.00 12.78           C  
ATOM   1223  NE  ARG A 160      61.941  23.205   2.780  1.00 15.60           N  
ATOM   1224  CZ  ARG A 160      62.440  22.584   3.844  1.00 20.06           C  
ATOM   1225  NH1 ARG A 160      63.420  21.702   3.700  1.00 20.31           N  
ATOM   1226  NH2 ARG A 160      61.957  22.843   5.053  1.00 20.34           N  
ATOM   1227  N   TYR A 161      56.734  22.817   0.480  1.00  8.76           N  
ATOM   1228  CA  TYR A 161      55.581  21.927   0.517  1.00  8.69           C  
ATOM   1229  C   TYR A 161      54.300  22.481  -0.083  1.00  7.56           C  
ATOM   1230  O   TYR A 161      53.253  21.843  -0.006  1.00  7.62           O  
ATOM   1231  CB  TYR A 161      55.332  21.473   1.954  1.00  9.56           C  
ATOM   1232  CG  TYR A 161      56.573  20.888   2.579  1.00 11.98           C  
ATOM   1233  CD1 TYR A 161      57.546  21.714   3.144  1.00 11.03           C  
ATOM   1234  CD2 TYR A 161      56.816  19.516   2.539  1.00 13.42           C  
ATOM   1235  CE1 TYR A 161      58.733  21.189   3.647  1.00 14.35           C  
ATOM   1236  CE2 TYR A 161      58.003  18.980   3.040  1.00 15.85           C  
ATOM   1237  CZ  TYR A 161      58.955  19.823   3.588  1.00 15.75           C  
ATOM   1238  OH  TYR A 161      60.139  19.303   4.062  1.00 19.77           O  
ATOM   1239  N   VAL A 162      54.382  23.661  -0.687  1.00  7.73           N  
ATOM   1240  CA  VAL A 162      53.214  24.265  -1.321  1.00  7.45           C  
ATOM   1241  C   VAL A 162      52.830  23.455  -2.558  1.00  8.43           C  
ATOM   1242  O   VAL A 162      53.686  23.122  -3.380  1.00 10.02           O  
ATOM   1243  CB  VAL A 162      53.503  25.710  -1.762  1.00 10.04           C  
ATOM   1244  CG1 VAL A 162      52.279  26.297  -2.454  1.00  7.59           C  
ATOM   1245  CG2 VAL A 162      53.899  26.549  -0.557  1.00  6.99           C  
ATOM   1246  N   HIS A 163      51.544  23.146  -2.691  1.00  7.64           N  
ATOM   1247  CA  HIS A 163      51.057  22.374  -3.829  1.00  8.26           C  
ATOM   1248  C   HIS A 163      51.322  23.143  -5.124  1.00  9.69           C  
ATOM   1249  O   HIS A 163      51.072  24.349  -5.211  1.00  9.49           O  
ATOM   1250  CB  HIS A 163      49.557  22.082  -3.666  1.00  5.73           C  
ATOM   1251  CG  HIS A 163      49.023  21.072  -4.637  1.00  6.35           C  
ATOM   1252  ND1 HIS A 163      48.925  21.317  -5.988  1.00  6.15           N  
ATOM   1253  CD2 HIS A 163      48.557  19.814  -4.449  1.00  5.94           C  
ATOM   1254  CE1 HIS A 163      48.421  20.255  -6.593  1.00  7.89           C  
ATOM   1255  NE2 HIS A 163      48.189  19.329  -5.681  1.00  8.53           N  
ATOM   1256  N   GLN A 164      51.847  22.428  -6.115  1.00  7.86           N  
ATOM   1257  CA  GLN A 164      52.182  22.983  -7.424  1.00  7.11           C  
ATOM   1258  C   GLN A 164      51.051  23.767  -8.098  1.00  7.65           C  
ATOM   1259  O   GLN A 164      51.312  24.676  -8.887  1.00  6.11           O  
ATOM   1260  CB  GLN A 164      52.628  21.847  -8.345  1.00  9.51           C  
ATOM   1261  CG  GLN A 164      53.058  22.256  -9.749  1.00 11.56           C  
ATOM   1262  CD  GLN A 164      53.381  21.047 -10.611  1.00 15.46           C  
ATOM   1263  OE1 GLN A 164      52.536  20.167 -10.803  1.00 14.69           O  
ATOM   1264  NE2 GLN A 164      54.607  20.991 -11.129  1.00 15.09           N  
ATOM   1265  N   ARG A 165      49.804  23.414  -7.797  1.00  6.85           N  
ATOM   1266  CA  ARG A 165      48.658  24.096  -8.399  1.00  7.97           C  
ATOM   1267  C   ARG A 165      48.616  25.589  -8.081  1.00  8.39           C  
ATOM   1268  O   ARG A 165      47.981  26.365  -8.801  1.00  7.70           O  
ATOM   1269  CB  ARG A 165      47.341  23.441  -7.954  1.00  7.20           C  
ATOM   1270  CG  ARG A 165      46.931  23.714  -6.511  1.00  6.40           C  
ATOM   1271  CD  ARG A 165      45.606  23.017  -6.200  1.00  4.72           C  
ATOM   1272  NE  ARG A 165      44.548  23.448  -7.106  1.00  5.96           N  
ATOM   1273  CZ  ARG A 165      43.633  24.365  -6.814  1.00  7.10           C  
ATOM   1274  NH1 ARG A 165      43.630  24.952  -5.623  1.00  5.34           N  
ATOM   1275  NH2 ARG A 165      42.726  24.710  -7.721  1.00  5.52           N  
ATOM   1276  N   TYR A 166      49.293  25.998  -7.012  1.00  7.86           N  
ATOM   1277  CA  TYR A 166      49.301  27.404  -6.636  1.00  7.35           C  
ATOM   1278  C   TYR A 166      50.273  28.272  -7.438  1.00  9.00           C  
ATOM   1279  O   TYR A 166      50.364  29.480  -7.215  1.00  5.71           O  
ATOM   1280  CB  TYR A 166      49.538  27.539  -5.126  1.00  7.42           C  
ATOM   1281  CG  TYR A 166      48.386  26.952  -4.339  1.00  5.23           C  
ATOM   1282  CD1 TYR A 166      48.556  25.819  -3.551  1.00  5.19           C  
ATOM   1283  CD2 TYR A 166      47.097  27.472  -4.473  1.00  5.50           C  
ATOM   1284  CE1 TYR A 166      47.472  25.206  -2.925  1.00  7.36           C  
ATOM   1285  CE2 TYR A 166      46.006  26.872  -3.853  1.00  5.16           C  
ATOM   1286  CZ  TYR A 166      46.201  25.736  -3.083  1.00  6.93           C  
ATOM   1287  OH  TYR A 166      45.125  25.118  -2.492  1.00  7.84           O  
ATOM   1288  N   ASP A 167      50.988  27.668  -8.383  1.00  8.75           N  
ATOM   1289  CA  ASP A 167      51.901  28.441  -9.219  1.00 10.51           C  
ATOM   1290  C   ASP A 167      51.064  29.329 -10.135  1.00 11.06           C  
ATOM   1291  O   ASP A 167      51.514  30.385 -10.583  1.00 13.05           O  
ATOM   1292  CB  ASP A 167      52.783  27.521 -10.064  1.00 10.14           C  
ATOM   1293  CG  ASP A 167      53.922  26.917  -9.272  1.00 11.27           C  
ATOM   1294  OD1 ASP A 167      54.598  26.021  -9.810  1.00 10.20           O  
ATOM   1295  OD2 ASP A 167      54.147  27.340  -8.118  1.00  9.47           O  
ATOM   1296  N   ILE A 168      49.845  28.882 -10.411  1.00  9.79           N  
ATOM   1297  CA  ILE A 168      48.912  29.622 -11.251  1.00 12.47           C  
ATOM   1298  C   ILE A 168      48.601  30.949 -10.565  1.00 11.67           C  
ATOM   1299  O   ILE A 168      48.657  32.014 -11.182  1.00 11.89           O  
ATOM   1300  CB  ILE A 168      47.585  28.840 -11.429  1.00 13.26           C  
ATOM   1301  CG1 ILE A 168      47.847  27.528 -12.168  1.00 16.40           C  
ATOM   1302  CG2 ILE A 168      46.556  29.698 -12.170  1.00 14.05           C  
ATOM   1303  CD1 ILE A 168      48.344  27.706 -13.587  1.00 19.86           C  
ATOM   1304  N   ALA A 169      48.278  30.874  -9.277  1.00 10.72           N  
ATOM   1305  CA  ALA A 169      47.950  32.066  -8.503  1.00  9.83           C  
ATOM   1306  C   ALA A 169      49.125  33.033  -8.407  1.00  9.48           C  
ATOM   1307  O   ALA A 169      48.969  34.225  -8.664  1.00  7.11           O  
ATOM   1308  CB  ALA A 169      47.476  31.668  -7.099  1.00 10.60           C  
ATOM   1309  N   THR A 170      50.299  32.524  -8.040  1.00  9.79           N  
ATOM   1310  CA  THR A 170      51.478  33.375  -7.917  1.00 10.72           C  
ATOM   1311  C   THR A 170      51.816  34.039  -9.250  1.00 10.48           C  
ATOM   1312  O   THR A 170      52.304  35.169  -9.284  1.00  9.40           O  
ATOM   1313  CB  THR A 170      52.715  32.578  -7.422  1.00 11.60           C  
ATOM   1314  OG1 THR A 170      53.065  31.580  -8.384  1.00 12.27           O  
ATOM   1315  CG2 THR A 170      52.419  31.902  -6.089  1.00 12.23           C  
ATOM   1316  N   THR A 171      51.547  33.341 -10.347  1.00 11.37           N  
ATOM   1317  CA  THR A 171      51.823  33.889 -11.672  1.00 12.20           C  
ATOM   1318  C   THR A 171      50.804  34.969 -12.050  1.00 10.78           C  
ATOM   1319  O   THR A 171      51.178  36.072 -12.444  1.00  9.85           O  
ATOM   1320  CB  THR A 171      51.804  32.781 -12.755  1.00 11.82           C  
ATOM   1321  OG1 THR A 171      52.895  31.875 -12.536  1.00 14.16           O  
ATOM   1322  CG2 THR A 171      51.937  33.388 -14.144  1.00 14.23           C  
ATOM   1323  N   LEU A 172      49.520  34.653 -11.910  1.00 10.12           N  
ATOM   1324  CA  LEU A 172      48.454  35.595 -12.260  1.00 11.57           C  
ATOM   1325  C   LEU A 172      48.381  36.830 -11.372  1.00 12.91           C  
ATOM   1326  O   LEU A 172      48.207  37.944 -11.869  1.00 13.32           O  
ATOM   1327  CB  LEU A 172      47.099  34.881 -12.266  1.00 11.55           C  
ATOM   1328  CG  LEU A 172      46.872  33.920 -13.437  1.00 11.98           C  
ATOM   1329  CD1 LEU A 172      45.508  33.255 -13.313  1.00 14.24           C  
ATOM   1330  CD2 LEU A 172      46.964  34.698 -14.753  1.00 16.06           C  
ATOM   1331  N   ILE A 173      48.509  36.637 -10.062  1.00 10.95           N  
ATOM   1332  CA  ILE A 173      48.461  37.755  -9.126  1.00 11.28           C  
ATOM   1333  C   ILE A 173      49.840  38.413  -9.050  1.00 12.21           C  
ATOM   1334  O   ILE A 173      50.038  39.420  -8.371  1.00 12.90           O  
ATOM   1335  CB  ILE A 173      48.006  37.277  -7.732  1.00  8.55           C  
ATOM   1336  CG1 ILE A 173      46.665  36.545  -7.864  1.00  9.32           C  
ATOM   1337  CG2 ILE A 173      47.871  38.462  -6.790  1.00  7.21           C  
ATOM   1338  CD1 ILE A 173      46.166  35.896  -6.577  1.00  8.38           C  
ATOM   1339  N   ASN A 174      50.789  37.824  -9.766  1.00 14.49           N  
ATOM   1340  CA  ASN A 174      52.151  38.333  -9.844  1.00 16.59           C  
ATOM   1341  C   ASN A 174      52.825  38.610  -8.504  1.00 16.87           C  
ATOM   1342  O   ASN A 174      53.146  39.754  -8.183  1.00 17.04           O  
ATOM   1343  CB  ASN A 174      52.178  39.609 -10.690  1.00 18.60           C  
ATOM   1344  CG  ASN A 174      53.585  40.023 -11.067  1.00 21.08           C  
ATOM   1345  OD1 ASN A 174      53.885  41.213 -11.183  1.00 23.07           O  
ATOM   1346  ND2 ASN A 174      54.456  39.041 -11.273  1.00 19.74           N  
ATOM   1347  N   ARG A 175      53.040  37.557  -7.726  1.00 16.65           N  
ATOM   1348  CA  ARG A 175      53.704  37.673  -6.436  1.00 15.54           C  
ATOM   1349  C   ARG A 175      53.932  36.280  -5.864  1.00 13.19           C  
ATOM   1350  O   ARG A 175      53.130  35.379  -6.086  1.00 13.08           O  
ATOM   1351  CB  ARG A 175      52.873  38.529  -5.475  1.00 17.57           C  
ATOM   1352  CG  ARG A 175      51.424  38.130  -5.352  1.00 21.17           C  
ATOM   1353  CD  ARG A 175      50.590  39.313  -4.873  1.00 24.27           C  
ATOM   1354  NE  ARG A 175      50.996  39.792  -3.552  1.00 26.34           N  
ATOM   1355  CZ  ARG A 175      50.459  40.847  -2.942  1.00 26.73           C  
ATOM   1356  NH1 ARG A 175      49.495  41.541  -3.535  1.00 26.42           N  
ATOM   1357  NH2 ARG A 175      50.873  41.200  -1.731  1.00 25.65           N  
ATOM   1358  N   PRO A 176      55.042  36.083  -5.134  1.00 13.48           N  
ATOM   1359  CA  PRO A 176      55.324  34.764  -4.557  1.00 12.08           C  
ATOM   1360  C   PRO A 176      54.266  34.308  -3.554  1.00 11.26           C  
ATOM   1361  O   PRO A 176      53.576  35.125  -2.937  1.00 10.53           O  
ATOM   1362  CB  PRO A 176      56.707  34.947  -3.934  1.00 13.12           C  
ATOM   1363  CG  PRO A 176      56.722  36.400  -3.563  1.00 13.72           C  
ATOM   1364  CD  PRO A 176      56.084  37.056  -4.763  1.00 13.34           C  
ATOM   1365  N   TYR A 177      54.146  32.995  -3.399  1.00  9.64           N  
ATOM   1366  CA  TYR A 177      53.161  32.412  -2.501  1.00  8.26           C  
ATOM   1367  C   TYR A 177      53.158  33.031  -1.105  1.00  7.61           C  
ATOM   1368  O   TYR A 177      52.093  33.280  -0.546  1.00  7.42           O  
ATOM   1369  CB  TYR A 177      53.376  30.900  -2.415  1.00  6.30           C  
ATOM   1370  CG  TYR A 177      52.244  30.143  -1.756  1.00  9.09           C  
ATOM   1371  CD1 TYR A 177      52.311  29.781  -0.411  1.00  7.74           C  
ATOM   1372  CD2 TYR A 177      51.112  29.768  -2.484  1.00  7.56           C  
ATOM   1373  CE1 TYR A 177      51.281  29.058   0.193  1.00  7.22           C  
ATOM   1374  CE2 TYR A 177      50.080  29.048  -1.891  1.00  8.83           C  
ATOM   1375  CZ  TYR A 177      50.174  28.696  -0.552  1.00  6.24           C  
ATOM   1376  OH  TYR A 177      49.165  27.972   0.039  1.00  7.76           O  
ATOM   1377  N   ASN A 178      54.336  33.299  -0.548  1.00  7.74           N  
ATOM   1378  CA  ASN A 178      54.403  33.887   0.785  1.00  8.58           C  
ATOM   1379  C   ASN A 178      53.765  35.274   0.819  1.00  9.93           C  
ATOM   1380  O   ASN A 178      53.218  35.689   1.846  1.00  8.67           O  
ATOM   1381  CB  ASN A 178      55.858  33.945   1.284  1.00 10.54           C  
ATOM   1382  CG  ASN A 178      56.785  34.667   0.324  1.00 10.20           C  
ATOM   1383  OD1 ASN A 178      57.336  35.719   0.648  1.00 13.18           O  
ATOM   1384  ND2 ASN A 178      56.965  34.100  -0.862  1.00  7.60           N  
ATOM   1385  N   LYS A 179      53.823  35.983  -0.306  1.00  8.99           N  
ATOM   1386  CA  LYS A 179      53.239  37.317  -0.391  1.00 10.44           C  
ATOM   1387  C   LYS A 179      51.745  37.250  -0.673  1.00 10.41           C  
ATOM   1388  O   LYS A 179      51.054  38.264  -0.656  1.00 11.80           O  
ATOM   1389  CB  LYS A 179      53.942  38.141  -1.473  1.00 13.29           C  
ATOM   1390  CG  LYS A 179      55.381  38.492  -1.124  1.00 13.35           C  
ATOM   1391  CD  LYS A 179      55.458  39.254   0.193  1.00 17.56           C  
ATOM   1392  CE  LYS A 179      56.902  39.529   0.598  1.00 18.74           C  
ATOM   1393  NZ  LYS A 179      56.998  40.164   1.942  1.00 20.33           N  
ATOM   1394  N   LEU A 180      51.252  36.046  -0.938  1.00  8.94           N  
ATOM   1395  CA  LEU A 180      49.834  35.845  -1.190  1.00  9.03           C  
ATOM   1396  C   LEU A 180      49.145  35.784   0.174  1.00  7.80           C  
ATOM   1397  O   LEU A 180      47.918  35.736   0.266  1.00  6.61           O  
ATOM   1398  CB  LEU A 180      49.630  34.539  -1.964  1.00 10.58           C  
ATOM   1399  CG  LEU A 180      48.963  34.565  -3.345  1.00 14.22           C  
ATOM   1400  CD1 LEU A 180      49.308  35.828  -4.115  1.00 12.48           C  
ATOM   1401  CD2 LEU A 180      49.395  33.319  -4.105  1.00 10.96           C  
ATOM   1402  N   TYR A 181      49.954  35.804   1.232  1.00  5.27           N  
ATOM   1403  CA  TYR A 181      49.451  35.751   2.604  1.00  6.45           C  
ATOM   1404  C   TYR A 181      50.230  36.710   3.498  1.00  6.43           C  
ATOM   1405  O   TYR A 181      50.416  36.463   4.696  1.00  6.49           O  
ATOM   1406  CB  TYR A 181      49.570  34.325   3.143  1.00  5.52           C  
ATOM   1407  CG  TYR A 181      48.772  33.329   2.339  1.00  5.24           C  
ATOM   1408  CD1 TYR A 181      47.394  33.214   2.508  1.00  5.54           C  
ATOM   1409  CD2 TYR A 181      49.389  32.535   1.374  1.00  4.92           C  
ATOM   1410  CE1 TYR A 181      46.648  32.332   1.732  1.00  5.53           C  
ATOM   1411  CE2 TYR A 181      48.654  31.649   0.591  1.00  6.60           C  
ATOM   1412  CZ  TYR A 181      47.286  31.553   0.776  1.00  6.80           C  
ATOM   1413  OH  TYR A 181      46.563  30.672   0.010  1.00  7.84           O  
ATOM   1414  N   GLY A 182      50.683  37.804   2.897  1.00  7.04           N  
ATOM   1415  CA  GLY A 182      51.442  38.798   3.626  1.00  7.33           C  
ATOM   1416  C   GLY A 182      50.554  39.649   4.507  1.00  7.72           C  
ATOM   1417  O   GLY A 182      49.336  39.469   4.537  1.00  5.70           O  
ATOM   1418  N   ALA A 183      51.176  40.592   5.207  1.00  7.95           N  
ATOM   1419  CA  ALA A 183      50.477  41.477   6.131  1.00  9.79           C  
ATOM   1420  C   ALA A 183      49.407  42.365   5.499  1.00  9.74           C  
ATOM   1421  O   ALA A 183      48.567  42.921   6.209  1.00  8.48           O  
ATOM   1422  CB  ALA A 183      51.493  42.342   6.871  1.00 10.29           C  
ATOM   1423  N   ASP A 184      49.433  42.507   4.178  1.00 11.45           N  
ATOM   1424  CA  ASP A 184      48.447  43.341   3.498  1.00 11.10           C  
ATOM   1425  C   ASP A 184      47.243  42.544   3.025  1.00 10.19           C  
ATOM   1426  O   ASP A 184      46.334  43.098   2.408  1.00 10.42           O  
ATOM   1427  CB  ASP A 184      49.073  44.049   2.295  1.00 16.47           C  
ATOM   1428  CG  ASP A 184      49.615  43.081   1.263  1.00 18.84           C  
ATOM   1429  OD1 ASP A 184      49.774  43.495   0.096  1.00 24.70           O  
ATOM   1430  OD2 ASP A 184      49.894  41.915   1.614  1.00 21.51           O  
ATOM   1431  N   THR A 185      47.241  41.246   3.310  1.00  9.41           N  
ATOM   1432  CA  THR A 185      46.143  40.378   2.910  1.00  6.65           C  
ATOM   1433  C   THR A 185      45.254  40.064   4.112  1.00  7.05           C  
ATOM   1434  O   THR A 185      45.726  40.002   5.248  1.00  4.59           O  
ATOM   1435  CB  THR A 185      46.663  39.053   2.315  1.00  6.57           C  
ATOM   1436  OG1 THR A 185      47.279  38.266   3.343  1.00  7.51           O  
ATOM   1437  CG2 THR A 185      47.684  39.333   1.215  1.00  5.72           C  
ATOM   1438  N   GLU A 186      43.964  39.870   3.858  1.00  5.75           N  
ATOM   1439  CA  GLU A 186      43.019  39.566   4.929  1.00  5.15           C  
ATOM   1440  C   GLU A 186      43.465  38.330   5.713  1.00  6.25           C  
ATOM   1441  O   GLU A 186      43.556  38.361   6.945  1.00  4.57           O  
ATOM   1442  CB  GLU A 186      41.621  39.332   4.347  1.00  4.99           C  
ATOM   1443  CG  GLU A 186      40.553  39.058   5.396  1.00  6.55           C  
ATOM   1444  CD  GLU A 186      40.239  40.276   6.251  1.00  6.73           C  
ATOM   1445  OE1 GLU A 186      39.495  40.135   7.244  1.00  6.50           O  
ATOM   1446  OE2 GLU A 186      40.727  41.380   5.928  1.00  6.54           O  
ATOM   1447  N   ILE A 187      43.748  37.248   4.994  1.00  5.29           N  
ATOM   1448  CA  ILE A 187      44.179  36.002   5.626  1.00  4.41           C  
ATOM   1449  C   ILE A 187      45.467  36.196   6.417  1.00  5.37           C  
ATOM   1450  O   ILE A 187      45.586  35.710   7.542  1.00  5.90           O  
ATOM   1451  CB  ILE A 187      44.377  34.886   4.570  1.00  6.62           C  
ATOM   1452  CG1 ILE A 187      43.027  34.550   3.925  1.00  6.69           C  
ATOM   1453  CG2 ILE A 187      44.994  33.638   5.209  1.00  4.30           C  
ATOM   1454  CD1 ILE A 187      41.967  34.079   4.915  1.00  7.61           C  
ATOM   1455  N   GLY A 188      46.421  36.916   5.831  1.00  5.18           N  
ATOM   1456  CA  GLY A 188      47.686  37.163   6.502  1.00  6.83           C  
ATOM   1457  C   GLY A 188      47.525  37.913   7.811  1.00  7.01           C  
ATOM   1458  O   GLY A 188      48.164  37.588   8.809  1.00  6.95           O  
ATOM   1459  N   GLN A 189      46.664  38.924   7.807  1.00  8.18           N  
ATOM   1460  CA  GLN A 189      46.409  39.726   8.997  1.00  8.38           C  
ATOM   1461  C   GLN A 189      45.751  38.852  10.060  1.00  7.80           C  
ATOM   1462  O   GLN A 189      46.081  38.922  11.243  1.00  5.81           O  
ATOM   1463  CB  GLN A 189      45.508  40.909   8.622  1.00 10.21           C  
ATOM   1464  CG  GLN A 189      46.166  41.832   7.595  1.00 12.73           C  
ATOM   1465  CD  GLN A 189      45.202  42.771   6.891  1.00 12.79           C  
ATOM   1466  OE1 GLN A 189      45.597  43.505   5.982  1.00 14.56           O  
ATOM   1467  NE2 GLN A 189      43.941  42.756   7.303  1.00 13.53           N  
ATOM   1468  N   TRP A 190      44.825  38.015   9.614  1.00  6.81           N  
ATOM   1469  CA  TRP A 190      44.113  37.097  10.490  1.00  5.73           C  
ATOM   1470  C   TRP A 190      45.106  36.130  11.142  1.00  5.10           C  
ATOM   1471  O   TRP A 190      45.118  35.957  12.365  1.00  4.84           O  
ATOM   1472  CB  TRP A 190      43.077  36.349   9.648  1.00  5.46           C  
ATOM   1473  CG  TRP A 190      42.338  35.244  10.325  1.00  4.53           C  
ATOM   1474  CD1 TRP A 190      41.552  35.332  11.444  1.00  5.06           C  
ATOM   1475  CD2 TRP A 190      42.244  33.893   9.869  1.00  6.26           C  
ATOM   1476  NE1 TRP A 190      40.966  34.110  11.705  1.00  4.97           N  
ATOM   1477  CE2 TRP A 190      41.375  33.211  10.753  1.00  6.86           C  
ATOM   1478  CE3 TRP A 190      42.806  33.189   8.791  1.00  5.92           C  
ATOM   1479  CZ2 TRP A 190      41.053  31.859  10.591  1.00  6.69           C  
ATOM   1480  CZ3 TRP A 190      42.485  31.845   8.631  1.00  9.39           C  
ATOM   1481  CH2 TRP A 190      41.615  31.195   9.527  1.00  7.61           C  
ATOM   1482  N   LEU A 191      45.957  35.517  10.325  1.00  4.50           N  
ATOM   1483  CA  LEU A 191      46.942  34.568  10.828  1.00  5.59           C  
ATOM   1484  C   LEU A 191      47.919  35.209  11.802  1.00  4.42           C  
ATOM   1485  O   LEU A 191      48.271  34.622  12.827  1.00  4.59           O  
ATOM   1486  CB  LEU A 191      47.710  33.935   9.660  1.00  6.53           C  
ATOM   1487  CG  LEU A 191      46.908  32.959   8.788  1.00  7.86           C  
ATOM   1488  CD1 LEU A 191      47.730  32.543   7.571  1.00  5.15           C  
ATOM   1489  CD2 LEU A 191      46.517  31.741   9.615  1.00  5.78           C  
ATOM   1490  N   ARG A 192      48.341  36.426  11.487  1.00  5.33           N  
ATOM   1491  CA  ARG A 192      49.288  37.143  12.323  1.00  6.26           C  
ATOM   1492  C   ARG A 192      48.736  37.570  13.687  1.00  6.84           C  
ATOM   1493  O   ARG A 192      49.462  38.126  14.506  1.00  5.70           O  
ATOM   1494  CB  ARG A 192      49.831  38.347  11.552  1.00  6.47           C  
ATOM   1495  CG  ARG A 192      50.726  37.943  10.377  1.00  5.76           C  
ATOM   1496  CD  ARG A 192      51.251  39.145   9.607  1.00  5.16           C  
ATOM   1497  NE  ARG A 192      52.289  38.763   8.647  1.00  6.78           N  
ATOM   1498  CZ  ARG A 192      52.079  38.021   7.562  1.00  9.80           C  
ATOM   1499  NH1 ARG A 192      53.088  37.726   6.753  1.00  8.22           N  
ATOM   1500  NH2 ARG A 192      50.862  37.579   7.274  1.00  8.18           N  
ATOM   1501  N   SER A 193      47.460  37.298  13.937  1.00  7.56           N  
ATOM   1502  CA  SER A 193      46.852  37.648  15.223  1.00  6.87           C  
ATOM   1503  C   SER A 193      46.726  36.413  16.117  1.00  7.83           C  
ATOM   1504  O   SER A 193      46.350  36.518  17.293  1.00  6.45           O  
ATOM   1505  CB  SER A 193      45.454  38.242  15.013  1.00  8.27           C  
ATOM   1506  OG  SER A 193      44.518  37.237  14.638  1.00  5.70           O  
ATOM   1507  N   LYS A 194      47.048  35.248  15.563  1.00  5.69           N  
ATOM   1508  CA  LYS A 194      46.918  33.996  16.297  1.00  5.69           C  
ATOM   1509  C   LYS A 194      48.051  33.643  17.245  1.00  5.72           C  
ATOM   1510  O   LYS A 194      49.168  34.149  17.131  1.00  5.14           O  
ATOM   1511  CB  LYS A 194      46.717  32.842  15.317  1.00  4.68           C  
ATOM   1512  CG  LYS A 194      45.526  33.036  14.399  1.00  4.79           C  
ATOM   1513  CD  LYS A 194      44.253  33.260  15.204  1.00  3.94           C  
ATOM   1514  CE  LYS A 194      43.060  33.473  14.285  1.00  3.37           C  
ATOM   1515  NZ  LYS A 194      41.815  33.704  15.059  1.00  6.62           N  
ATOM   1516  N   ASN A 195      47.736  32.752  18.179  1.00  5.47           N  
ATOM   1517  CA  ASN A 195      48.699  32.271  19.156  1.00  5.40           C  
ATOM   1518  C   ASN A 195      49.355  31.028  18.588  1.00  5.67           C  
ATOM   1519  O   ASN A 195      48.975  30.551  17.518  1.00  4.59           O  
ATOM   1520  CB  ASN A 195      48.000  31.930  20.474  1.00  6.40           C  
ATOM   1521  CG  ASN A 195      47.448  33.155  21.166  1.00  5.83           C  
ATOM   1522  OD1 ASN A 195      48.182  34.108  21.437  1.00  5.81           O  
ATOM   1523  ND2 ASN A 195      46.149  33.141  21.457  1.00  6.77           N  
ATOM   1524  N   THR A 196      50.336  30.499  19.309  1.00  6.26           N  
ATOM   1525  CA  THR A 196      51.045  29.309  18.862  1.00  5.92           C  
ATOM   1526  C   THR A 196      50.954  28.246  19.951  1.00  6.67           C  
ATOM   1527  O   THR A 196      50.953  27.049  19.671  1.00  7.67           O  
ATOM   1528  CB  THR A 196      52.517  29.645  18.548  1.00  5.56           C  
ATOM   1529  OG1 THR A 196      52.566  30.704  17.582  1.00  5.69           O  
ATOM   1530  CG2 THR A 196      53.236  28.434  17.976  1.00  4.48           C  
ATOM   1531  N   ILE A 197      50.857  28.700  21.197  1.00  6.17           N  
ATOM   1532  CA  ILE A 197      50.736  27.806  22.340  1.00  6.45           C  
ATOM   1533  C   ILE A 197      49.640  28.332  23.256  1.00  5.79           C  
ATOM   1534  O   ILE A 197      49.633  29.509  23.607  1.00  6.90           O  
ATOM   1535  CB  ILE A 197      52.041  27.750  23.150  1.00  5.79           C  
ATOM   1536  CG1 ILE A 197      53.224  27.497  22.215  1.00  9.56           C  
ATOM   1537  CG2 ILE A 197      51.954  26.649  24.193  1.00  6.89           C  
ATOM   1538  CD1 ILE A 197      54.565  27.697  22.868  1.00  7.24           C  
ATOM   1539  N   ILE A 198      48.702  27.472  23.632  1.00  5.90           N  
ATOM   1540  CA  ILE A 198      47.645  27.903  24.531  1.00  5.35           C  
ATOM   1541  C   ILE A 198      47.366  26.849  25.586  1.00  6.48           C  
ATOM   1542  O   ILE A 198      47.774  25.695  25.458  1.00  5.62           O  
ATOM   1543  CB  ILE A 198      46.329  28.215  23.790  1.00  4.24           C  
ATOM   1544  CG1 ILE A 198      45.774  26.952  23.136  1.00  2.97           C  
ATOM   1545  CG2 ILE A 198      46.559  29.325  22.775  1.00  5.98           C  
ATOM   1546  CD1 ILE A 198      44.414  27.166  22.480  1.00  3.32           C  
ATOM   1547  N   LYS A 199      46.677  27.270  26.637  1.00  5.83           N  
ATOM   1548  CA  LYS A 199      46.323  26.389  27.736  1.00  6.98           C  
ATOM   1549  C   LYS A 199      44.837  26.564  28.033  1.00  5.81           C  
ATOM   1550  O   LYS A 199      44.372  27.674  28.272  1.00  8.59           O  
ATOM   1551  CB  LYS A 199      47.154  26.750  28.973  1.00  8.16           C  
ATOM   1552  CG  LYS A 199      46.868  25.916  30.213  1.00  9.12           C  
ATOM   1553  CD  LYS A 199      47.635  26.461  31.409  1.00 11.18           C  
ATOM   1554  CE  LYS A 199      47.330  25.681  32.671  1.00 13.54           C  
ATOM   1555  NZ  LYS A 199      48.038  26.260  33.855  1.00 15.14           N  
ATOM   1556  N   ILE A 200      44.092  25.470  27.986  1.00  7.31           N  
ATOM   1557  CA  ILE A 200      42.668  25.510  28.289  1.00  7.84           C  
ATOM   1558  C   ILE A 200      42.456  24.516  29.421  1.00  7.66           C  
ATOM   1559  O   ILE A 200      42.760  23.331  29.280  1.00  8.83           O  
ATOM   1560  CB  ILE A 200      41.812  25.104  27.077  1.00  5.91           C  
ATOM   1561  CG1 ILE A 200      42.058  26.077  25.921  1.00  8.11           C  
ATOM   1562  CG2 ILE A 200      40.336  25.122  27.457  1.00  6.16           C  
ATOM   1563  CD1 ILE A 200      41.273  25.742  24.668  1.00  6.71           C  
ATOM   1564  N   ASN A 201      41.943  24.998  30.548  1.00  9.09           N  
ATOM   1565  CA  ASN A 201      41.734  24.132  31.699  1.00  6.87           C  
ATOM   1566  C   ASN A 201      43.089  23.523  32.083  1.00  8.82           C  
ATOM   1567  O   ASN A 201      44.075  24.244  32.250  1.00  8.53           O  
ATOM   1568  CB  ASN A 201      40.729  23.032  31.351  1.00  7.74           C  
ATOM   1569  CG  ASN A 201      39.378  23.589  30.929  1.00  8.74           C  
ATOM   1570  OD1 ASN A 201      38.568  22.889  30.316  1.00 10.60           O  
ATOM   1571  ND2 ASN A 201      39.127  24.853  31.260  1.00  3.17           N  
ATOM   1572  N   ASP A 202      43.145  22.202  32.205  1.00  9.27           N  
ATOM   1573  CA  ASP A 202      44.385  21.524  32.577  1.00 10.02           C  
ATOM   1574  C   ASP A 202      45.090  20.890  31.381  1.00  8.85           C  
ATOM   1575  O   ASP A 202      45.771  19.870  31.521  1.00  8.77           O  
ATOM   1576  CB  ASP A 202      44.097  20.441  33.619  1.00 11.55           C  
ATOM   1577  CG  ASP A 202      43.093  19.413  33.127  1.00 13.76           C  
ATOM   1578  OD1 ASP A 202      43.017  18.322  33.730  1.00 15.12           O  
ATOM   1579  OD2 ASP A 202      42.374  19.696  32.144  1.00 12.84           O  
ATOM   1580  N   VAL A 203      44.935  21.491  30.208  1.00  7.05           N  
ATOM   1581  CA  VAL A 203      45.556  20.950  29.001  1.00  5.93           C  
ATOM   1582  C   VAL A 203      46.321  22.020  28.230  1.00  5.98           C  
ATOM   1583  O   VAL A 203      45.860  23.159  28.106  1.00  6.99           O  
ATOM   1584  CB  VAL A 203      44.494  20.343  28.064  1.00  5.65           C  
ATOM   1585  CG1 VAL A 203      45.166  19.639  26.890  1.00  3.70           C  
ATOM   1586  CG2 VAL A 203      43.607  19.384  28.840  1.00  3.18           C  
ATOM   1587  N   LEU A 204      47.493  21.648  27.718  1.00  4.16           N  
ATOM   1588  CA  LEU A 204      48.319  22.568  26.943  1.00  4.39           C  
ATOM   1589  C   LEU A 204      48.255  22.121  25.484  1.00  5.29           C  
ATOM   1590  O   LEU A 204      48.326  20.924  25.197  1.00  7.22           O  
ATOM   1591  CB  LEU A 204      49.770  22.520  27.431  1.00  3.24           C  
ATOM   1592  CG  LEU A 204      50.655  23.701  27.033  1.00  5.23           C  
ATOM   1593  CD1 LEU A 204      50.162  24.952  27.758  1.00  5.79           C  
ATOM   1594  CD2 LEU A 204      52.108  23.412  27.390  1.00  6.78           C  
ATOM   1595  N   TYR A 205      48.120  23.081  24.571  1.00  4.35           N  
ATOM   1596  CA  TYR A 205      48.036  22.784  23.142  1.00  5.49           C  
ATOM   1597  C   TYR A 205      49.072  23.548  22.319  1.00  5.79           C  
ATOM   1598  O   TYR A 205      49.292  24.738  22.534  1.00  5.87           O  
ATOM   1599  CB  TYR A 205      46.654  23.156  22.591  1.00  5.89           C  
ATOM   1600  CG  TYR A 205      45.471  22.542  23.301  1.00  4.96           C  
ATOM   1601  CD1 TYR A 205      45.078  22.989  24.560  1.00  6.44           C  
ATOM   1602  CD2 TYR A 205      44.728  21.532  22.697  1.00  4.30           C  
ATOM   1603  CE1 TYR A 205      43.965  22.443  25.201  1.00  6.64           C  
ATOM   1604  CE2 TYR A 205      43.614  20.979  23.328  1.00  5.49           C  
ATOM   1605  CZ  TYR A 205      43.241  21.439  24.580  1.00  6.21           C  
ATOM   1606  OH  TYR A 205      42.148  20.885  25.209  1.00  4.48           O  
ATOM   1607  N   MET A 206      49.689  22.856  21.367  1.00  7.50           N  
ATOM   1608  CA  MET A 206      50.673  23.452  20.466  1.00  8.10           C  
ATOM   1609  C   MET A 206      50.889  22.481  19.311  1.00  6.81           C  
ATOM   1610  O   MET A 206      50.504  21.315  19.390  1.00  7.59           O  
ATOM   1611  CB  MET A 206      52.008  23.730  21.171  1.00  9.05           C  
ATOM   1612  CG  MET A 206      52.900  22.516  21.337  1.00 11.09           C  
ATOM   1613  SD  MET A 206      52.587  21.614  22.851  1.00 14.74           S  
ATOM   1614  CE  MET A 206      51.037  20.877  22.561  1.00 19.02           C  
ATOM   1615  N   HIS A 207      51.512  22.949  18.240  1.00  5.18           N  
ATOM   1616  CA  HIS A 207      51.707  22.092  17.080  1.00  6.25           C  
ATOM   1617  C   HIS A 207      52.641  20.901  17.265  1.00  5.46           C  
ATOM   1618  O   HIS A 207      52.249  19.763  17.023  1.00  5.88           O  
ATOM   1619  CB  HIS A 207      52.188  22.913  15.886  1.00  5.30           C  
ATOM   1620  CG  HIS A 207      52.228  22.133  14.612  1.00  5.88           C  
ATOM   1621  ND1 HIS A 207      51.099  21.572  14.054  1.00  6.14           N  
ATOM   1622  CD2 HIS A 207      53.261  21.776  13.813  1.00  5.21           C  
ATOM   1623  CE1 HIS A 207      51.436  20.899  12.969  1.00  6.82           C  
ATOM   1624  NE2 HIS A 207      52.742  21.007  12.800  1.00  4.62           N  
ATOM   1625  N   GLY A 208      53.872  21.160  17.688  1.00  7.26           N  
ATOM   1626  CA  GLY A 208      54.833  20.080  17.851  1.00  8.55           C  
ATOM   1627  C   GLY A 208      54.957  19.494  19.241  1.00  8.65           C  
ATOM   1628  O   GLY A 208      54.721  18.303  19.444  1.00  8.96           O  
ATOM   1629  N   GLY A 209      55.336  20.332  20.197  1.00  8.18           N  
ATOM   1630  CA  GLY A 209      55.495  19.880  21.564  1.00  8.32           C  
ATOM   1631  C   GLY A 209      56.483  20.772  22.285  1.00  9.53           C  
ATOM   1632  O   GLY A 209      57.228  21.518  21.649  1.00  8.39           O  
ATOM   1633  N   ILE A 210      56.489  20.705  23.612  1.00  9.83           N  
ATOM   1634  CA  ILE A 210      57.398  21.514  24.409  1.00  9.24           C  
ATOM   1635  C   ILE A 210      58.563  20.657  24.895  1.00  8.71           C  
ATOM   1636  O   ILE A 210      58.354  19.603  25.494  1.00  7.77           O  
ATOM   1637  CB  ILE A 210      56.688  22.112  25.649  1.00  9.71           C  
ATOM   1638  CG1 ILE A 210      55.462  22.925  25.222  1.00  8.61           C  
ATOM   1639  CG2 ILE A 210      57.668  22.984  26.433  1.00 12.20           C  
ATOM   1640  CD1 ILE A 210      55.777  24.090  24.317  1.00  6.80           C  
ATOM   1641  N   SER A 211      59.783  21.107  24.625  1.00  9.71           N  
ATOM   1642  CA  SER A 211      60.977  20.387  25.055  1.00 10.88           C  
ATOM   1643  C   SER A 211      61.478  21.014  26.348  1.00 12.85           C  
ATOM   1644  O   SER A 211      61.020  22.089  26.742  1.00 11.41           O  
ATOM   1645  CB  SER A 211      62.069  20.469  23.987  1.00 10.34           C  
ATOM   1646  OG  SER A 211      62.419  21.812  23.716  1.00 11.55           O  
ATOM   1647  N   SER A 212      62.419  20.346  27.008  1.00 14.35           N  
ATOM   1648  CA  SER A 212      62.966  20.856  28.260  1.00 15.86           C  
ATOM   1649  C   SER A 212      63.678  22.190  28.086  1.00 14.64           C  
ATOM   1650  O   SER A 212      63.858  22.931  29.050  1.00 14.78           O  
ATOM   1651  CB  SER A 212      63.925  19.834  28.878  1.00 16.59           C  
ATOM   1652  OG  SER A 212      63.211  18.705  29.352  1.00 21.35           O  
ATOM   1653  N   GLU A 213      64.079  22.505  26.860  1.00 15.19           N  
ATOM   1654  CA  GLU A 213      64.769  23.763  26.617  1.00 14.48           C  
ATOM   1655  C   GLU A 213      63.866  24.936  26.953  1.00 13.96           C  
ATOM   1656  O   GLU A 213      64.337  26.013  27.312  1.00 12.04           O  
ATOM   1657  CB  GLU A 213      65.214  23.875  25.165  1.00 14.06           C  
ATOM   1658  CG  GLU A 213      66.076  25.096  24.911  1.00 16.81           C  
ATOM   1659  CD  GLU A 213      66.658  25.116  23.519  1.00 15.39           C  
ATOM   1660  OE1 GLU A 213      66.835  24.025  22.942  1.00 17.84           O  
ATOM   1661  OE2 GLU A 213      66.949  26.216  23.008  1.00 17.48           O  
ATOM   1662  N   TRP A 214      62.563  24.722  26.821  1.00 14.22           N  
ATOM   1663  CA  TRP A 214      61.592  25.759  27.126  1.00 13.79           C  
ATOM   1664  C   TRP A 214      61.756  26.196  28.574  1.00 14.16           C  
ATOM   1665  O   TRP A 214      61.666  27.382  28.892  1.00 14.09           O  
ATOM   1666  CB  TRP A 214      60.174  25.228  26.908  1.00 13.39           C  
ATOM   1667  CG  TRP A 214      59.105  26.123  27.452  1.00 12.97           C  
ATOM   1668  CD1 TRP A 214      58.728  26.258  28.759  1.00 13.31           C  
ATOM   1669  CD2 TRP A 214      58.281  27.017  26.702  1.00 11.20           C  
ATOM   1670  NE1 TRP A 214      57.716  27.180  28.868  1.00 11.29           N  
ATOM   1671  CE2 TRP A 214      57.421  27.662  27.620  1.00 11.26           C  
ATOM   1672  CE3 TRP A 214      58.184  27.338  25.341  1.00  9.77           C  
ATOM   1673  CZ2 TRP A 214      56.474  28.609  27.220  1.00  9.59           C  
ATOM   1674  CZ3 TRP A 214      57.241  28.282  24.942  1.00  8.27           C  
ATOM   1675  CH2 TRP A 214      56.399  28.905  25.881  1.00  9.07           C  
ATOM   1676  N   ILE A 215      61.987  25.220  29.444  1.00 14.38           N  
ATOM   1677  CA  ILE A 215      62.160  25.477  30.866  1.00 15.87           C  
ATOM   1678  C   ILE A 215      63.502  26.150  31.115  1.00 15.14           C  
ATOM   1679  O   ILE A 215      63.599  27.068  31.926  1.00 15.44           O  
ATOM   1680  CB  ILE A 215      62.080  24.167  31.672  1.00 14.95           C  
ATOM   1681  CG1 ILE A 215      60.721  23.504  31.433  1.00 15.27           C  
ATOM   1682  CG2 ILE A 215      62.285  24.450  33.155  1.00 15.67           C  
ATOM   1683  CD1 ILE A 215      60.515  22.212  32.194  1.00 15.44           C  
ATOM   1684  N   SER A 216      64.530  25.695  30.404  1.00 15.88           N  
ATOM   1685  CA  SER A 216      65.868  26.267  30.542  1.00 18.31           C  
ATOM   1686  C   SER A 216      65.831  27.755  30.226  1.00 17.29           C  
ATOM   1687  O   SER A 216      66.514  28.551  30.866  1.00 17.16           O  
ATOM   1688  CB  SER A 216      66.850  25.590  29.579  1.00 18.01           C  
ATOM   1689  OG  SER A 216      66.876  24.190  29.768  1.00 24.08           O  
ATOM   1690  N   ARG A 217      65.025  28.120  29.235  1.00 16.04           N  
ATOM   1691  CA  ARG A 217      64.908  29.509  28.813  1.00 16.25           C  
ATOM   1692  C   ARG A 217      63.881  30.310  29.609  1.00 15.66           C  
ATOM   1693  O   ARG A 217      63.682  31.496  29.355  1.00 16.88           O  
ATOM   1694  CB  ARG A 217      64.596  29.566  27.311  1.00 15.43           C  
ATOM   1695  CG  ARG A 217      65.725  28.998  26.452  1.00 14.64           C  
ATOM   1696  CD  ARG A 217      65.428  29.085  24.960  1.00 16.57           C  
ATOM   1697  NE  ARG A 217      66.583  28.694  24.152  1.00 17.81           N  
ATOM   1698  CZ  ARG A 217      67.672  29.441  23.987  1.00 20.25           C  
ATOM   1699  NH1 ARG A 217      67.760  30.628  24.571  1.00 21.33           N  
ATOM   1700  NH2 ARG A 217      68.678  29.000  23.240  1.00 21.66           N  
ATOM   1701  N   GLU A 218      63.242  29.656  30.573  1.00 16.48           N  
ATOM   1702  CA  GLU A 218      62.255  30.299  31.436  1.00 16.97           C  
ATOM   1703  C   GLU A 218      61.173  31.034  30.648  1.00 16.85           C  
ATOM   1704  O   GLU A 218      60.712  32.103  31.047  1.00 14.92           O  
ATOM   1705  CB  GLU A 218      62.958  31.276  32.384  1.00 18.73           C  
ATOM   1706  CG  GLU A 218      64.130  30.660  33.139  1.00 20.88           C  
ATOM   1707  CD  GLU A 218      64.914  31.682  33.939  1.00 23.18           C  
ATOM   1708  OE1 GLU A 218      65.272  32.733  33.369  1.00 24.87           O  
ATOM   1709  OE2 GLU A 218      65.183  31.431  35.134  1.00 24.98           O  
ATOM   1710  N   LEU A 219      60.769  30.447  29.529  1.00 14.99           N  
ATOM   1711  CA  LEU A 219      59.739  31.036  28.686  1.00 13.72           C  
ATOM   1712  C   LEU A 219      58.365  30.938  29.329  1.00 11.76           C  
ATOM   1713  O   LEU A 219      58.162  30.173  30.270  1.00 12.49           O  
ATOM   1714  CB  LEU A 219      59.722  30.328  27.328  1.00 13.21           C  
ATOM   1715  CG  LEU A 219      60.849  30.740  26.382  1.00 13.59           C  
ATOM   1716  CD1 LEU A 219      61.084  29.676  25.325  1.00 13.17           C  
ATOM   1717  CD2 LEU A 219      60.486  32.071  25.753  1.00 15.44           C  
ATOM   1718  N   THR A 220      57.431  31.736  28.820  1.00 11.21           N  
ATOM   1719  CA  THR A 220      56.052  31.737  29.298  1.00 10.20           C  
ATOM   1720  C   THR A 220      55.192  31.782  28.043  1.00  8.57           C  
ATOM   1721  O   THR A 220      55.655  32.235  26.998  1.00  8.51           O  
ATOM   1722  CB  THR A 220      55.741  32.979  30.142  1.00 10.57           C  
ATOM   1723  OG1 THR A 220      55.857  34.147  29.325  1.00 11.72           O  
ATOM   1724  CG2 THR A 220      56.713  33.081  31.314  1.00 10.37           C  
ATOM   1725  N   LEU A 221      53.949  31.321  28.132  1.00  8.31           N  
ATOM   1726  CA  LEU A 221      53.090  31.331  26.955  1.00  8.50           C  
ATOM   1727  C   LEU A 221      52.986  32.726  26.353  1.00  9.08           C  
ATOM   1728  O   LEU A 221      53.070  32.893  25.138  1.00  9.18           O  
ATOM   1729  CB  LEU A 221      51.685  30.829  27.288  1.00  8.16           C  
ATOM   1730  CG  LEU A 221      51.480  29.401  27.796  1.00 13.96           C  
ATOM   1731  CD1 LEU A 221      50.052  28.993  27.472  1.00  9.74           C  
ATOM   1732  CD2 LEU A 221      52.461  28.432  27.149  1.00 12.02           C  
ATOM   1733  N   ASP A 222      52.808  33.725  27.212  1.00  8.89           N  
ATOM   1734  CA  ASP A 222      52.669  35.105  26.771  1.00  9.94           C  
ATOM   1735  C   ASP A 222      53.888  35.642  26.028  1.00  9.46           C  
ATOM   1736  O   ASP A 222      53.756  36.265  24.978  1.00  6.87           O  
ATOM   1737  CB  ASP A 222      52.354  35.997  27.974  1.00 14.34           C  
ATOM   1738  CG  ASP A 222      52.205  37.451  27.595  1.00 19.74           C  
ATOM   1739  OD1 ASP A 222      53.168  38.221  27.803  1.00 23.22           O  
ATOM   1740  OD2 ASP A 222      51.129  37.822  27.082  1.00 21.32           O  
ATOM   1741  N   LYS A 223      55.074  35.404  26.575  1.00  9.81           N  
ATOM   1742  CA  LYS A 223      56.302  35.884  25.945  1.00 10.00           C  
ATOM   1743  C   LYS A 223      56.543  35.192  24.607  1.00  7.66           C  
ATOM   1744  O   LYS A 223      56.962  35.825  23.638  1.00  7.71           O  
ATOM   1745  CB  LYS A 223      57.489  35.656  26.886  1.00 13.29           C  
ATOM   1746  CG  LYS A 223      58.822  36.160  26.359  1.00 19.34           C  
ATOM   1747  CD  LYS A 223      59.799  36.378  27.509  1.00 24.37           C  
ATOM   1748  CE  LYS A 223      61.217  36.617  27.013  1.00 27.05           C  
ATOM   1749  NZ  LYS A 223      61.809  35.364  26.465  1.00 30.42           N  
ATOM   1750  N   ALA A 224      56.260  33.894  24.558  1.00  6.97           N  
ATOM   1751  CA  ALA A 224      56.447  33.114  23.341  1.00  6.54           C  
ATOM   1752  C   ALA A 224      55.452  33.513  22.254  1.00  7.11           C  
ATOM   1753  O   ALA A 224      55.832  33.778  21.113  1.00  6.04           O  
ATOM   1754  CB  ALA A 224      56.313  31.633  23.654  1.00  5.62           C  
ATOM   1755  N   ASN A 225      54.173  33.557  22.602  1.00  6.50           N  
ATOM   1756  CA  ASN A 225      53.172  33.924  21.615  1.00  7.13           C  
ATOM   1757  C   ASN A 225      53.434  35.309  21.041  1.00  6.00           C  
ATOM   1758  O   ASN A 225      53.228  35.538  19.850  1.00  9.03           O  
ATOM   1759  CB  ASN A 225      51.769  33.844  22.215  1.00  6.46           C  
ATOM   1760  CG  ASN A 225      51.308  32.414  22.398  1.00  8.76           C  
ATOM   1761  OD1 ASN A 225      51.510  31.574  21.519  1.00  5.53           O  
ATOM   1762  ND2 ASN A 225      50.683  32.127  23.534  1.00  5.75           N  
ATOM   1763  N   ALA A 226      53.911  36.223  21.879  1.00  8.56           N  
ATOM   1764  CA  ALA A 226      54.202  37.580  21.430  1.00  8.06           C  
ATOM   1765  C   ALA A 226      55.365  37.581  20.443  1.00  8.71           C  
ATOM   1766  O   ALA A 226      55.304  38.224  19.395  1.00  8.59           O  
ATOM   1767  CB  ALA A 226      54.532  38.464  22.624  1.00  7.42           C  
ATOM   1768  N   LEU A 227      56.431  36.864  20.783  1.00  8.65           N  
ATOM   1769  CA  LEU A 227      57.591  36.793  19.903  1.00  9.74           C  
ATOM   1770  C   LEU A 227      57.213  36.170  18.561  1.00  8.50           C  
ATOM   1771  O   LEU A 227      57.633  36.647  17.506  1.00  8.50           O  
ATOM   1772  CB  LEU A 227      58.709  35.982  20.564  1.00 10.19           C  
ATOM   1773  CG  LEU A 227      59.450  36.690  21.704  1.00 11.36           C  
ATOM   1774  CD1 LEU A 227      60.367  35.708  22.409  1.00 12.06           C  
ATOM   1775  CD2 LEU A 227      60.240  37.862  21.143  1.00  8.69           C  
ATOM   1776  N   TYR A 228      56.419  35.103  18.602  1.00  7.88           N  
ATOM   1777  CA  TYR A 228      55.984  34.441  17.379  1.00  6.88           C  
ATOM   1778  C   TYR A 228      55.267  35.426  16.459  1.00  7.30           C  
ATOM   1779  O   TYR A 228      55.544  35.491  15.261  1.00  7.24           O  
ATOM   1780  CB  TYR A 228      55.043  33.274  17.705  1.00  6.57           C  
ATOM   1781  CG  TYR A 228      55.742  31.978  18.067  1.00  7.69           C  
ATOM   1782  CD1 TYR A 228      55.415  31.288  19.235  1.00  4.82           C  
ATOM   1783  CD2 TYR A 228      56.721  31.433  17.231  1.00  5.82           C  
ATOM   1784  CE1 TYR A 228      56.045  30.088  19.564  1.00  5.64           C  
ATOM   1785  CE2 TYR A 228      57.354  30.238  17.548  1.00  5.86           C  
ATOM   1786  CZ  TYR A 228      57.012  29.570  18.714  1.00  5.69           C  
ATOM   1787  OH  TYR A 228      57.631  28.383  19.027  1.00  8.17           O  
ATOM   1788  N   ARG A 229      54.341  36.195  17.018  1.00  8.21           N  
ATOM   1789  CA  ARG A 229      53.601  37.158  16.213  1.00  7.53           C  
ATOM   1790  C   ARG A 229      54.487  38.269  15.677  1.00  8.82           C  
ATOM   1791  O   ARG A 229      54.334  38.698  14.532  1.00 10.47           O  
ATOM   1792  CB  ARG A 229      52.456  37.774  17.023  1.00  8.24           C  
ATOM   1793  CG  ARG A 229      51.205  36.921  17.088  1.00  7.21           C  
ATOM   1794  CD  ARG A 229      50.068  37.695  17.729  1.00  6.19           C  
ATOM   1795  NE  ARG A 229      50.244  37.866  19.169  1.00  8.08           N  
ATOM   1796  CZ  ARG A 229      49.929  36.944  20.074  1.00  7.02           C  
ATOM   1797  NH1 ARG A 229      49.418  35.784  19.686  1.00 10.69           N  
ATOM   1798  NH2 ARG A 229      50.123  37.177  21.366  1.00  9.08           N  
ATOM   1799  N   ALA A 230      55.423  38.726  16.497  1.00  8.97           N  
ATOM   1800  CA  ALA A 230      56.306  39.813  16.095  1.00 12.41           C  
ATOM   1801  C   ALA A 230      57.417  39.413  15.131  1.00 13.18           C  
ATOM   1802  O   ALA A 230      57.992  40.270  14.448  1.00 13.78           O  
ATOM   1803  CB  ALA A 230      56.913  40.458  17.333  1.00 12.00           C  
ATOM   1804  N   ASN A 231      57.713  38.121  15.051  1.00 13.55           N  
ATOM   1805  CA  ASN A 231      58.800  37.670  14.194  1.00 13.78           C  
ATOM   1806  C   ASN A 231      58.475  36.676  13.089  1.00 15.05           C  
ATOM   1807  O   ASN A 231      59.386  36.140  12.455  1.00 14.87           O  
ATOM   1808  CB  ASN A 231      59.910  37.102  15.071  1.00 14.57           C  
ATOM   1809  CG  ASN A 231      60.542  38.157  15.947  1.00 15.54           C  
ATOM   1810  OD1 ASN A 231      61.406  38.909  15.498  1.00 15.39           O  
ATOM   1811  ND2 ASN A 231      60.096  38.237  17.198  1.00 14.95           N  
ATOM   1812  N   VAL A 232      57.197  36.422  12.841  1.00 13.98           N  
ATOM   1813  CA  VAL A 232      56.856  35.477  11.791  1.00 15.32           C  
ATOM   1814  C   VAL A 232      57.306  36.033  10.436  1.00 17.06           C  
ATOM   1815  O   VAL A 232      57.495  35.279   9.483  1.00 18.45           O  
ATOM   1816  CB  VAL A 232      55.338  35.182  11.757  1.00 15.70           C  
ATOM   1817  CG1 VAL A 232      54.574  36.404  11.284  1.00 14.31           C  
ATOM   1818  CG2 VAL A 232      55.064  33.985  10.858  1.00 15.51           C  
ATOM   1819  N   ASP A 233      57.498  37.349  10.369  1.00 17.99           N  
ATOM   1820  CA  ASP A 233      57.929  38.010   9.136  1.00 20.66           C  
ATOM   1821  C   ASP A 233      59.420  38.328   9.118  1.00 22.63           C  
ATOM   1822  O   ASP A 233      59.905  38.989   8.197  1.00 24.75           O  
ATOM   1823  CB  ASP A 233      57.145  39.311   8.923  1.00 18.24           C  
ATOM   1824  CG  ASP A 233      55.701  39.066   8.553  1.00 19.07           C  
ATOM   1825  OD1 ASP A 233      55.467  38.417   7.515  1.00 19.80           O  
ATOM   1826  OD2 ASP A 233      54.801  39.517   9.296  1.00 20.79           O  
ATOM   1827  N   ALA A 234      60.145  37.867  10.130  1.00 22.65           N  
ATOM   1828  CA  ALA A 234      61.577  38.123  10.204  1.00 23.49           C  
ATOM   1829  C   ALA A 234      62.340  37.280   9.189  1.00 23.89           C  
ATOM   1830  O   ALA A 234      61.853  36.245   8.731  1.00 24.07           O  
ATOM   1831  CB  ALA A 234      62.087  37.837  11.609  1.00 24.54           C  
ATOM   1832  N   SER A 235      63.535  37.736   8.830  1.00 25.23           N  
ATOM   1833  CA  SER A 235      64.368  37.011   7.881  1.00 27.35           C  
ATOM   1834  C   SER A 235      64.885  35.764   8.584  1.00 27.11           C  
ATOM   1835  O   SER A 235      65.021  35.751   9.806  1.00 28.64           O  
ATOM   1836  CB  SER A 235      65.546  37.882   7.434  1.00 26.92           C  
ATOM   1837  OG  SER A 235      66.325  38.299   8.543  1.00 26.81           O  
ATOM   1838  N   LYS A 236      65.164  34.712   7.823  1.00 27.72           N  
ATOM   1839  CA  LYS A 236      65.670  33.487   8.425  1.00 27.43           C  
ATOM   1840  C   LYS A 236      66.962  33.821   9.165  1.00 26.61           C  
ATOM   1841  O   LYS A 236      67.223  33.292  10.245  1.00 26.09           O  
ATOM   1842  CB  LYS A 236      65.933  32.424   7.355  1.00 27.40           C  
ATOM   1843  CG  LYS A 236      66.257  31.056   7.927  1.00 29.05           C  
ATOM   1844  CD  LYS A 236      66.503  30.026   6.834  1.00 31.35           C  
ATOM   1845  CE  LYS A 236      66.816  28.664   7.433  1.00 31.54           C  
ATOM   1846  NZ  LYS A 236      66.993  27.616   6.387  1.00 34.03           N  
ATOM   1847  N   LYS A 237      67.758  34.713   8.580  1.00 25.38           N  
ATOM   1848  CA  LYS A 237      69.018  35.140   9.183  1.00 24.88           C  
ATOM   1849  C   LYS A 237      68.778  35.698  10.580  1.00 23.04           C  
ATOM   1850  O   LYS A 237      69.441  35.310  11.541  1.00 22.95           O  
ATOM   1851  CB  LYS A 237      69.685  36.221   8.322  1.00 26.07           C  
ATOM   1852  CG  LYS A 237      70.608  35.700   7.226  1.00 28.05           C  
ATOM   1853  CD  LYS A 237      71.886  35.111   7.818  1.00 30.06           C  
ATOM   1854  CE  LYS A 237      72.894  34.727   6.732  1.00 30.12           C  
ATOM   1855  NZ  LYS A 237      72.358  33.707   5.789  1.00 29.01           N  
ATOM   1856  N   SER A 238      67.823  36.615  10.684  1.00 22.36           N  
ATOM   1857  CA  SER A 238      67.502  37.237  11.961  1.00 21.65           C  
ATOM   1858  C   SER A 238      66.994  36.221  12.976  1.00 19.51           C  
ATOM   1859  O   SER A 238      67.333  36.289  14.158  1.00 20.40           O  
ATOM   1860  CB  SER A 238      66.458  38.344  11.761  1.00 23.17           C  
ATOM   1861  OG  SER A 238      65.267  37.840  11.178  1.00 26.81           O  
ATOM   1862  N   LEU A 239      66.190  35.272  12.509  1.00 18.69           N  
ATOM   1863  CA  LEU A 239      65.629  34.248  13.381  1.00 18.06           C  
ATOM   1864  C   LEU A 239      66.701  33.312  13.928  1.00 19.03           C  
ATOM   1865  O   LEU A 239      66.696  32.969  15.112  1.00 17.67           O  
ATOM   1866  CB  LEU A 239      64.577  33.434  12.625  1.00 17.83           C  
ATOM   1867  CG  LEU A 239      63.348  34.191  12.105  1.00 17.66           C  
ATOM   1868  CD1 LEU A 239      62.451  33.233  11.331  1.00 16.80           C  
ATOM   1869  CD2 LEU A 239      62.589  34.807  13.270  1.00 18.35           C  
ATOM   1870  N   LYS A 240      67.624  32.901  13.067  1.00 20.02           N  
ATOM   1871  CA  LYS A 240      68.681  31.998  13.491  1.00 21.62           C  
ATOM   1872  C   LYS A 240      69.762  32.735  14.273  1.00 22.27           C  
ATOM   1873  O   LYS A 240      70.488  32.127  15.056  1.00 22.63           O  
ATOM   1874  CB  LYS A 240      69.293  31.291  12.276  1.00 22.80           C  
ATOM   1875  CG  LYS A 240      68.260  30.810  11.266  1.00 24.64           C  
ATOM   1876  CD  LYS A 240      68.591  29.442  10.698  1.00 27.20           C  
ATOM   1877  CE  LYS A 240      68.341  28.347  11.724  1.00 28.86           C  
ATOM   1878  NZ  LYS A 240      68.534  26.984  11.149  1.00 31.76           N  
ATOM   1879  N   ALA A 241      69.862  34.046  14.067  1.00 22.67           N  
ATOM   1880  CA  ALA A 241      70.860  34.852  14.762  1.00 23.74           C  
ATOM   1881  C   ALA A 241      70.507  35.021  16.236  1.00 24.27           C  
ATOM   1882  O   ALA A 241      71.387  34.993  17.096  1.00 24.90           O  
ATOM   1883  CB  ALA A 241      70.993  36.216  14.095  1.00 23.76           C  
ATOM   1884  N   ASP A 242      69.220  35.205  16.521  1.00 24.44           N  
ATOM   1885  CA  ASP A 242      68.747  35.362  17.894  1.00 22.43           C  
ATOM   1886  C   ASP A 242      68.514  33.954  18.431  1.00 23.02           C  
ATOM   1887  O   ASP A 242      67.640  33.244  17.939  1.00 23.44           O  
ATOM   1888  CB  ASP A 242      67.433  36.145  17.914  1.00 22.40           C  
ATOM   1889  CG  ASP A 242      66.974  36.474  19.319  1.00 22.76           C  
ATOM   1890  OD1 ASP A 242      67.461  37.472  19.887  1.00 24.61           O  
ATOM   1891  OD2 ASP A 242      66.137  35.727  19.862  1.00 21.26           O  
ATOM   1892  N   ASP A 243      69.281  33.543  19.438  1.00 23.07           N  
ATOM   1893  CA  ASP A 243      69.135  32.187  19.962  1.00 23.65           C  
ATOM   1894  C   ASP A 243      67.763  31.869  20.547  1.00 21.14           C  
ATOM   1895  O   ASP A 243      67.361  30.706  20.578  1.00 18.92           O  
ATOM   1896  CB  ASP A 243      70.227  31.874  20.992  1.00 27.34           C  
ATOM   1897  CG  ASP A 243      70.068  32.656  22.268  1.00 29.65           C  
ATOM   1898  OD1 ASP A 243      70.205  33.897  22.226  1.00 33.40           O  
ATOM   1899  OD2 ASP A 243      69.807  32.025  23.315  1.00 31.91           O  
ATOM   1900  N   LEU A 244      67.044  32.888  21.010  1.00 18.01           N  
ATOM   1901  CA  LEU A 244      65.716  32.654  21.563  1.00 17.66           C  
ATOM   1902  C   LEU A 244      64.762  32.386  20.400  1.00 15.10           C  
ATOM   1903  O   LEU A 244      64.005  31.417  20.421  1.00 14.48           O  
ATOM   1904  CB  LEU A 244      65.232  33.867  22.364  1.00 18.66           C  
ATOM   1905  CG  LEU A 244      64.046  33.632  23.309  1.00 19.14           C  
ATOM   1906  CD1 LEU A 244      63.742  34.909  24.073  1.00 19.08           C  
ATOM   1907  CD2 LEU A 244      62.826  33.182  22.533  1.00 20.91           C  
ATOM   1908  N   LEU A 245      64.796  33.250  19.390  1.00 14.37           N  
ATOM   1909  CA  LEU A 245      63.935  33.070  18.226  1.00 14.20           C  
ATOM   1910  C   LEU A 245      64.342  31.790  17.509  1.00 14.00           C  
ATOM   1911  O   LEU A 245      63.503  31.082  16.950  1.00 12.73           O  
ATOM   1912  CB  LEU A 245      64.052  34.264  17.275  1.00 13.85           C  
ATOM   1913  CG  LEU A 245      63.572  35.618  17.812  1.00 14.17           C  
ATOM   1914  CD1 LEU A 245      63.775  36.688  16.751  1.00 14.30           C  
ATOM   1915  CD2 LEU A 245      62.102  35.529  18.207  1.00 17.73           C  
ATOM   1916  N   ASN A 246      65.638  31.494  17.539  1.00 14.05           N  
ATOM   1917  CA  ASN A 246      66.159  30.295  16.897  1.00 13.60           C  
ATOM   1918  C   ASN A 246      65.481  29.078  17.514  1.00 12.66           C  
ATOM   1919  O   ASN A 246      65.018  28.186  16.806  1.00 10.94           O  
ATOM   1920  CB  ASN A 246      67.678  30.212  17.087  1.00 17.01           C  
ATOM   1921  CG  ASN A 246      68.291  29.015  16.382  1.00 18.12           C  
ATOM   1922  OD1 ASN A 246      68.135  28.845  15.175  1.00 21.32           O  
ATOM   1923  ND2 ASN A 246      68.997  28.184  17.134  1.00 21.52           N  
ATOM   1924  N   PHE A 247      65.413  29.049  18.840  1.00 10.82           N  
ATOM   1925  CA  PHE A 247      64.779  27.937  19.520  1.00 10.83           C  
ATOM   1926  C   PHE A 247      63.295  27.871  19.183  1.00 10.27           C  
ATOM   1927  O   PHE A 247      62.782  26.821  18.801  1.00 10.09           O  
ATOM   1928  CB  PHE A 247      64.959  28.059  21.038  1.00 11.80           C  
ATOM   1929  CG  PHE A 247      63.999  27.216  21.828  1.00 12.03           C  
ATOM   1930  CD1 PHE A 247      62.969  27.807  22.553  1.00 12.38           C  
ATOM   1931  CD2 PHE A 247      64.095  25.829  21.814  1.00 12.74           C  
ATOM   1932  CE1 PHE A 247      62.046  27.028  23.251  1.00 13.34           C  
ATOM   1933  CE2 PHE A 247      63.176  25.039  22.510  1.00 13.98           C  
ATOM   1934  CZ  PHE A 247      62.150  25.640  23.228  1.00 12.86           C  
ATOM   1935  N   LEU A 248      62.611  29.001  19.319  1.00  9.57           N  
ATOM   1936  CA  LEU A 248      61.182  29.054  19.057  1.00 10.44           C  
ATOM   1937  C   LEU A 248      60.755  28.636  17.660  1.00 10.76           C  
ATOM   1938  O   LEU A 248      59.786  27.895  17.505  1.00  8.60           O  
ATOM   1939  CB  LEU A 248      60.643  30.459  19.334  1.00  9.52           C  
ATOM   1940  CG  LEU A 248      60.624  30.929  20.790  1.00  9.16           C  
ATOM   1941  CD1 LEU A 248      59.953  32.292  20.854  1.00  8.58           C  
ATOM   1942  CD2 LEU A 248      59.866  29.931  21.658  1.00  7.71           C  
ATOM   1943  N   PHE A 249      61.476  29.108  16.650  1.00 11.55           N  
ATOM   1944  CA  PHE A 249      61.126  28.812  15.266  1.00 11.49           C  
ATOM   1945  C   PHE A 249      61.670  27.541  14.631  1.00 12.92           C  
ATOM   1946  O   PHE A 249      61.250  27.195  13.529  1.00 12.21           O  
ATOM   1947  CB  PHE A 249      61.514  29.988  14.367  1.00 10.91           C  
ATOM   1948  CG  PHE A 249      60.574  31.151  14.450  1.00 10.31           C  
ATOM   1949  CD1 PHE A 249      60.615  32.026  15.530  1.00  9.85           C  
ATOM   1950  CD2 PHE A 249      59.632  31.362  13.451  1.00  8.93           C  
ATOM   1951  CE1 PHE A 249      59.726  33.096  15.611  1.00  9.02           C  
ATOM   1952  CE2 PHE A 249      58.736  32.429  13.523  1.00  8.56           C  
ATOM   1953  CZ  PHE A 249      58.785  33.297  14.604  1.00  9.85           C  
ATOM   1954  N   PHE A 250      62.580  26.834  15.294  1.00 14.29           N  
ATOM   1955  CA  PHE A 250      63.130  25.644  14.658  1.00 15.51           C  
ATOM   1956  C   PHE A 250      63.055  24.297  15.379  1.00 15.66           C  
ATOM   1957  O   PHE A 250      62.278  24.110  16.315  1.00 15.07           O  
ATOM   1958  CB  PHE A 250      64.567  25.942  14.220  1.00 14.99           C  
ATOM   1959  CG  PHE A 250      64.680  27.169  13.356  1.00 16.97           C  
ATOM   1960  CD1 PHE A 250      65.338  28.305  13.813  1.00 15.80           C  
ATOM   1961  CD2 PHE A 250      64.063  27.212  12.108  1.00 16.04           C  
ATOM   1962  CE1 PHE A 250      65.376  29.468  13.043  1.00 16.10           C  
ATOM   1963  CE2 PHE A 250      64.095  28.369  11.332  1.00 16.56           C  
ATOM   1964  CZ  PHE A 250      64.753  29.500  11.804  1.00 15.83           C  
ATOM   1965  N   GLY A 251      63.872  23.365  14.892  1.00 16.48           N  
ATOM   1966  CA  GLY A 251      63.943  21.999  15.387  1.00 14.63           C  
ATOM   1967  C   GLY A 251      63.453  21.546  16.751  1.00 14.58           C  
ATOM   1968  O   GLY A 251      62.648  20.621  16.844  1.00 15.44           O  
ATOM   1969  N   ASN A 252      63.941  22.173  17.813  1.00 14.13           N  
ATOM   1970  CA  ASN A 252      63.564  21.774  19.164  1.00 12.80           C  
ATOM   1971  C   ASN A 252      62.426  22.618  19.731  1.00 11.95           C  
ATOM   1972  O   ASN A 252      61.975  22.395  20.855  1.00 10.73           O  
ATOM   1973  CB  ASN A 252      64.795  21.865  20.072  1.00 15.52           C  
ATOM   1974  CG  ASN A 252      64.665  21.022  21.320  1.00 15.26           C  
ATOM   1975  OD1 ASN A 252      64.361  19.833  21.245  1.00 16.95           O  
ATOM   1976  ND2 ASN A 252      64.906  21.629  22.477  1.00 17.05           N  
ATOM   1977  N   GLY A 253      61.954  23.567  18.928  1.00  9.99           N  
ATOM   1978  CA  GLY A 253      60.887  24.459  19.350  1.00  8.56           C  
ATOM   1979  C   GLY A 253      59.472  23.909  19.377  1.00  6.74           C  
ATOM   1980  O   GLY A 253      59.211  22.797  18.911  1.00  6.09           O  
ATOM   1981  N   PRO A 254      58.520  24.691  19.913  1.00  5.76           N  
ATOM   1982  CA  PRO A 254      57.112  24.298  20.013  1.00  6.36           C  
ATOM   1983  C   PRO A 254      56.433  23.862  18.717  1.00  5.25           C  
ATOM   1984  O   PRO A 254      55.551  23.011  18.748  1.00  8.10           O  
ATOM   1985  CB  PRO A 254      56.451  25.534  20.618  1.00  5.09           C  
ATOM   1986  CG  PRO A 254      57.525  26.097  21.476  1.00  6.82           C  
ATOM   1987  CD  PRO A 254      58.751  25.977  20.597  1.00  6.53           C  
ATOM   1988  N   THR A 255      56.831  24.436  17.584  1.00  6.67           N  
ATOM   1989  CA  THR A 255      56.206  24.082  16.312  1.00  6.08           C  
ATOM   1990  C   THR A 255      56.892  22.960  15.536  1.00  6.45           C  
ATOM   1991  O   THR A 255      56.319  22.427  14.587  1.00  5.57           O  
ATOM   1992  CB  THR A 255      56.091  25.307  15.385  1.00  8.26           C  
ATOM   1993  OG1 THR A 255      57.390  25.879  15.179  1.00  7.88           O  
ATOM   1994  CG2 THR A 255      55.160  26.345  15.993  1.00  9.64           C  
ATOM   1995  N   TRP A 256      58.103  22.586  15.941  1.00  7.61           N  
ATOM   1996  CA  TRP A 256      58.826  21.520  15.247  1.00  8.16           C  
ATOM   1997  C   TRP A 256      59.173  20.294  16.087  1.00  8.75           C  
ATOM   1998  O   TRP A 256      59.399  19.216  15.542  1.00  9.43           O  
ATOM   1999  CB  TRP A 256      60.127  22.058  14.645  1.00  8.36           C  
ATOM   2000  CG  TRP A 256      59.943  22.911  13.437  1.00  9.32           C  
ATOM   2001  CD1 TRP A 256      59.739  24.259  13.404  1.00  8.90           C  
ATOM   2002  CD2 TRP A 256      59.980  22.475  12.074  1.00 10.50           C  
ATOM   2003  NE1 TRP A 256      59.656  24.693  12.101  1.00 10.09           N  
ATOM   2004  CE2 TRP A 256      59.799  23.618  11.264  1.00  9.81           C  
ATOM   2005  CE3 TRP A 256      60.151  21.228  11.457  1.00 11.81           C  
ATOM   2006  CZ2 TRP A 256      59.785  23.553   9.865  1.00 10.89           C  
ATOM   2007  CZ3 TRP A 256      60.137  21.161  10.066  1.00 11.26           C  
ATOM   2008  CH2 TRP A 256      59.955  22.319   9.286  1.00 10.75           C  
ATOM   2009  N   TYR A 257      59.229  20.460  17.403  1.00  8.30           N  
ATOM   2010  CA  TYR A 257      59.589  19.368  18.307  1.00  8.72           C  
ATOM   2011  C   TYR A 257      58.735  18.099  18.168  1.00  8.27           C  
ATOM   2012  O   TYR A 257      57.508  18.147  18.241  1.00  8.49           O  
ATOM   2013  CB  TYR A 257      59.538  19.877  19.751  1.00  9.62           C  
ATOM   2014  CG  TYR A 257      60.051  18.910  20.791  1.00  7.36           C  
ATOM   2015  CD1 TYR A 257      61.360  18.427  20.743  1.00 10.02           C  
ATOM   2016  CD2 TYR A 257      59.234  18.495  21.841  1.00  9.39           C  
ATOM   2017  CE1 TYR A 257      61.841  17.549  21.728  1.00 10.61           C  
ATOM   2018  CE2 TYR A 257      59.702  17.628  22.824  1.00 10.14           C  
ATOM   2019  CZ  TYR A 257      61.005  17.158  22.763  1.00 11.56           C  
ATOM   2020  OH  TYR A 257      61.462  16.302  23.745  1.00 13.39           O  
ATOM   2021  N   ARG A 258      59.400  16.962  17.975  1.00  9.50           N  
ATOM   2022  CA  ARG A 258      58.710  15.681  17.835  1.00  9.51           C  
ATOM   2023  C   ARG A 258      59.184  14.728  18.921  1.00 10.40           C  
ATOM   2024  O   ARG A 258      58.951  13.519  18.837  1.00  9.82           O  
ATOM   2025  CB  ARG A 258      59.014  15.043  16.474  1.00 10.36           C  
ATOM   2026  CG  ARG A 258      58.699  15.889  15.256  1.00 10.17           C  
ATOM   2027  CD  ARG A 258      59.101  15.134  13.990  1.00 10.53           C  
ATOM   2028  NE  ARG A 258      58.877  15.901  12.768  1.00 11.88           N  
ATOM   2029  CZ  ARG A 258      57.690  16.074  12.194  1.00 12.21           C  
ATOM   2030  NH1 ARG A 258      57.592  16.790  11.081  1.00 15.00           N  
ATOM   2031  NH2 ARG A 258      56.605  15.528  12.725  1.00 13.93           N  
ATOM   2032  N   GLY A 259      59.846  15.277  19.934  1.00  9.32           N  
ATOM   2033  CA  GLY A 259      60.378  14.465  21.015  1.00 10.87           C  
ATOM   2034  C   GLY A 259      59.415  13.529  21.715  1.00 12.06           C  
ATOM   2035  O   GLY A 259      59.822  12.467  22.200  1.00 10.20           O  
ATOM   2036  N   TYR A 260      58.144  13.909  21.784  1.00 10.14           N  
ATOM   2037  CA  TYR A 260      57.155  13.071  22.448  1.00 11.12           C  
ATOM   2038  C   TYR A 260      56.934  11.755  21.720  1.00 11.48           C  
ATOM   2039  O   TYR A 260      56.380  10.816  22.286  1.00 11.74           O  
ATOM   2040  CB  TYR A 260      55.814  13.795  22.564  1.00 10.95           C  
ATOM   2041  CG  TYR A 260      55.863  15.100  23.316  1.00 11.57           C  
ATOM   2042  CD1 TYR A 260      56.821  15.328  24.300  1.00 13.35           C  
ATOM   2043  CD2 TYR A 260      54.915  16.095  23.075  1.00 12.06           C  
ATOM   2044  CE1 TYR A 260      56.835  16.511  25.030  1.00 13.04           C  
ATOM   2045  CE2 TYR A 260      54.920  17.281  23.798  1.00 11.66           C  
ATOM   2046  CZ  TYR A 260      55.882  17.482  24.774  1.00 12.27           C  
ATOM   2047  OH  TYR A 260      55.888  18.651  25.493  1.00 11.44           O  
ATOM   2048  N   PHE A 261      57.365  11.688  20.466  1.00 11.19           N  
ATOM   2049  CA  PHE A 261      57.194  10.474  19.681  1.00 10.57           C  
ATOM   2050  C   PHE A 261      58.521   9.766  19.440  1.00 12.37           C  
ATOM   2051  O   PHE A 261      58.633   8.911  18.563  1.00 14.37           O  
ATOM   2052  CB  PHE A 261      56.524  10.806  18.347  1.00 10.08           C  
ATOM   2053  CG  PHE A 261      55.231  11.555  18.497  1.00  9.29           C  
ATOM   2054  CD1 PHE A 261      55.222  12.943  18.583  1.00  8.66           C  
ATOM   2055  CD2 PHE A 261      54.026  10.870  18.602  1.00 11.46           C  
ATOM   2056  CE1 PHE A 261      54.031  13.642  18.773  1.00  8.88           C  
ATOM   2057  CE2 PHE A 261      52.826  11.559  18.794  1.00 11.49           C  
ATOM   2058  CZ  PHE A 261      52.832  12.949  18.879  1.00 11.08           C  
ATOM   2059  N   SER A 262      59.525  10.137  20.226  1.00 13.71           N  
ATOM   2060  CA  SER A 262      60.851   9.546  20.124  1.00 14.36           C  
ATOM   2061  C   SER A 262      60.900   8.270  20.957  1.00 14.43           C  
ATOM   2062  O   SER A 262      60.195   8.150  21.958  1.00 13.05           O  
ATOM   2063  CB  SER A 262      61.900  10.537  20.636  1.00 15.39           C  
ATOM   2064  OG  SER A 262      63.185   9.941  20.685  1.00 20.60           O  
ATOM   2065  N   GLU A 263      61.730   7.320  20.538  1.00 15.60           N  
ATOM   2066  CA  GLU A 263      61.878   6.056  21.252  1.00 17.00           C  
ATOM   2067  C   GLU A 263      62.500   6.278  22.620  1.00 16.91           C  
ATOM   2068  O   GLU A 263      62.195   5.571  23.575  1.00 19.12           O  
ATOM   2069  CB  GLU A 263      62.810   5.105  20.497  1.00 19.49           C  
ATOM   2070  CG  GLU A 263      62.384   4.691  19.115  1.00 22.10           C  
ATOM   2071  CD  GLU A 263      63.411   3.779  18.468  1.00 21.52           C  
ATOM   2072  OE1 GLU A 263      64.499   4.266  18.090  1.00 22.20           O  
ATOM   2073  OE2 GLU A 263      63.135   2.569  18.354  1.00 21.31           O  
ATOM   2074  N   THR A 264      63.386   7.263  22.699  1.00 16.92           N  
ATOM   2075  CA  THR A 264      64.105   7.547  23.932  1.00 17.20           C  
ATOM   2076  C   THR A 264      63.445   8.511  24.908  1.00 16.64           C  
ATOM   2077  O   THR A 264      63.951   8.717  26.009  1.00 15.43           O  
ATOM   2078  CB  THR A 264      65.508   8.068  23.610  1.00 17.70           C  
ATOM   2079  OG1 THR A 264      65.402   9.216  22.761  1.00 21.04           O  
ATOM   2080  CG2 THR A 264      66.320   6.993  22.896  1.00 19.16           C  
ATOM   2081  N   PHE A 265      62.324   9.105  24.517  1.00 16.01           N  
ATOM   2082  CA  PHE A 265      61.637  10.033  25.407  1.00 15.33           C  
ATOM   2083  C   PHE A 265      60.926   9.233  26.499  1.00 14.56           C  
ATOM   2084  O   PHE A 265      60.297   8.212  26.214  1.00 14.03           O  
ATOM   2085  CB  PHE A 265      60.636  10.877  24.614  1.00 14.68           C  
ATOM   2086  CG  PHE A 265      60.042  12.007  25.402  1.00 14.07           C  
ATOM   2087  CD1 PHE A 265      58.724  11.951  25.840  1.00 12.61           C  
ATOM   2088  CD2 PHE A 265      60.807  13.126  25.714  1.00 13.81           C  
ATOM   2089  CE1 PHE A 265      58.171  12.991  26.577  1.00 12.21           C  
ATOM   2090  CE2 PHE A 265      60.265  14.174  26.452  1.00 15.86           C  
ATOM   2091  CZ  PHE A 265      58.945  14.107  26.885  1.00 14.30           C  
ATOM   2092  N   THR A 266      61.025   9.694  27.744  1.00 14.68           N  
ATOM   2093  CA  THR A 266      60.413   8.988  28.869  1.00 14.58           C  
ATOM   2094  C   THR A 266      59.264   9.731  29.544  1.00 14.31           C  
ATOM   2095  O   THR A 266      59.208  10.960  29.535  1.00 13.58           O  
ATOM   2096  CB  THR A 266      61.458   8.674  29.958  1.00 16.28           C  
ATOM   2097  OG1 THR A 266      61.873   9.893  30.590  1.00 17.17           O  
ATOM   2098  CG2 THR A 266      62.673   7.992  29.346  1.00 17.53           C  
ATOM   2099  N   GLU A 267      58.350   8.969  30.137  1.00 13.82           N  
ATOM   2100  CA  GLU A 267      57.211   9.550  30.834  1.00 14.47           C  
ATOM   2101  C   GLU A 267      57.717  10.403  31.997  1.00 13.71           C  
ATOM   2102  O   GLU A 267      57.085  11.385  32.379  1.00 14.36           O  
ATOM   2103  CB  GLU A 267      56.282   8.442  31.339  1.00 14.96           C  
ATOM   2104  CG  GLU A 267      55.092   8.941  32.144  1.00 16.87           C  
ATOM   2105  CD  GLU A 267      53.928   7.966  32.136  1.00 17.53           C  
ATOM   2106  OE1 GLU A 267      53.022   8.113  32.982  1.00 18.41           O  
ATOM   2107  OE2 GLU A 267      53.914   7.061  31.275  1.00 20.93           O  
ATOM   2108  N   ALA A 268      58.864  10.024  32.551  1.00 11.93           N  
ATOM   2109  CA  ALA A 268      59.456  10.773  33.651  1.00 13.33           C  
ATOM   2110  C   ALA A 268      59.762  12.198  33.198  1.00 12.84           C  
ATOM   2111  O   ALA A 268      59.430  13.161  33.887  1.00 11.21           O  
ATOM   2112  CB  ALA A 268      60.731  10.091  34.125  1.00 14.91           C  
ATOM   2113  N   GLU A 269      60.399  12.332  32.037  1.00 13.30           N  
ATOM   2114  CA  GLU A 269      60.724  13.656  31.523  1.00 13.73           C  
ATOM   2115  C   GLU A 269      59.434  14.396  31.197  1.00 13.37           C  
ATOM   2116  O   GLU A 269      59.321  15.603  31.424  1.00 11.22           O  
ATOM   2117  CB  GLU A 269      61.610  13.558  30.275  1.00 15.13           C  
ATOM   2118  CG  GLU A 269      61.756  14.883  29.541  1.00 20.42           C  
ATOM   2119  CD  GLU A 269      62.941  14.919  28.599  1.00 22.64           C  
ATOM   2120  OE1 GLU A 269      63.175  13.919  27.888  1.00 23.70           O  
ATOM   2121  OE2 GLU A 269      63.631  15.961  28.562  1.00 22.03           O  
ATOM   2122  N   LEU A 270      58.457  13.665  30.668  1.00 11.47           N  
ATOM   2123  CA  LEU A 270      57.173  14.263  30.330  1.00 10.06           C  
ATOM   2124  C   LEU A 270      56.576  14.894  31.581  1.00 10.51           C  
ATOM   2125  O   LEU A 270      56.091  16.028  31.547  1.00  7.91           O  
ATOM   2126  CB  LEU A 270      56.214  13.199  29.789  1.00 10.57           C  
ATOM   2127  CG  LEU A 270      54.819  13.705  29.409  1.00 11.06           C  
ATOM   2128  CD1 LEU A 270      54.945  14.761  28.312  1.00 10.95           C  
ATOM   2129  CD2 LEU A 270      53.960  12.544  28.936  1.00 11.56           C  
ATOM   2130  N   ASP A 271      56.621  14.155  32.687  1.00 10.70           N  
ATOM   2131  CA  ASP A 271      56.082  14.639  33.952  1.00 12.32           C  
ATOM   2132  C   ASP A 271      56.652  15.990  34.361  1.00 12.51           C  
ATOM   2133  O   ASP A 271      55.923  16.845  34.864  1.00 11.58           O  
ATOM   2134  CB  ASP A 271      56.339  13.629  35.074  1.00 13.23           C  
ATOM   2135  CG  ASP A 271      55.525  12.366  34.918  1.00 15.86           C  
ATOM   2136  OD1 ASP A 271      54.351  12.468  34.510  1.00 15.22           O  
ATOM   2137  OD2 ASP A 271      56.053  11.273  35.214  1.00 17.79           O  
ATOM   2138  N   THR A 272      57.950  16.186  34.151  1.00 12.35           N  
ATOM   2139  CA  THR A 272      58.579  17.450  34.524  1.00 13.05           C  
ATOM   2140  C   THR A 272      57.982  18.591  33.712  1.00 12.75           C  
ATOM   2141  O   THR A 272      57.833  19.708  34.208  1.00 12.43           O  
ATOM   2142  CB  THR A 272      60.107  17.430  34.291  1.00 13.96           C  
ATOM   2143  OG1 THR A 272      60.380  17.417  32.884  1.00 15.98           O  
ATOM   2144  CG2 THR A 272      60.729  16.197  34.938  1.00 10.55           C  
ATOM   2145  N   ILE A 273      57.638  18.300  32.462  1.00 12.41           N  
ATOM   2146  CA  ILE A 273      57.054  19.302  31.585  1.00 11.71           C  
ATOM   2147  C   ILE A 273      55.609  19.568  31.992  1.00 11.20           C  
ATOM   2148  O   ILE A 273      55.180  20.718  32.068  1.00  8.07           O  
ATOM   2149  CB  ILE A 273      57.116  18.840  30.120  1.00 10.89           C  
ATOM   2150  CG1 ILE A 273      58.582  18.671  29.709  1.00 12.94           C  
ATOM   2151  CG2 ILE A 273      56.416  19.846  29.225  1.00 11.59           C  
ATOM   2152  CD1 ILE A 273      58.780  18.176  28.292  1.00 14.75           C  
ATOM   2153  N   LEU A 274      54.862  18.503  32.262  1.00 11.59           N  
ATOM   2154  CA  LEU A 274      53.477  18.656  32.682  1.00 12.73           C  
ATOM   2155  C   LEU A 274      53.447  19.515  33.940  1.00 12.55           C  
ATOM   2156  O   LEU A 274      52.685  20.472  34.036  1.00 11.57           O  
ATOM   2157  CB  LEU A 274      52.850  17.291  32.980  1.00 12.99           C  
ATOM   2158  CG  LEU A 274      52.537  16.385  31.786  1.00 14.18           C  
ATOM   2159  CD1 LEU A 274      52.020  15.049  32.292  1.00 13.91           C  
ATOM   2160  CD2 LEU A 274      51.509  17.050  30.883  1.00 13.08           C  
ATOM   2161  N   GLN A 275      54.300  19.169  34.898  1.00 13.20           N  
ATOM   2162  CA  GLN A 275      54.374  19.898  36.158  1.00 14.87           C  
ATOM   2163  C   GLN A 275      54.746  21.367  35.984  1.00 13.59           C  
ATOM   2164  O   GLN A 275      54.239  22.235  36.699  1.00 13.85           O  
ATOM   2165  CB  GLN A 275      55.393  19.236  37.090  1.00 18.63           C  
ATOM   2166  CG  GLN A 275      55.449  19.887  38.457  1.00 25.13           C  
ATOM   2167  CD  GLN A 275      54.136  19.745  39.204  1.00 29.07           C  
ATOM   2168  OE1 GLN A 275      53.887  20.441  40.189  1.00 31.85           O  
ATOM   2169  NE2 GLN A 275      53.287  18.831  38.738  1.00 31.16           N  
ATOM   2170  N   HIS A 276      55.638  21.643  35.040  1.00 12.80           N  
ATOM   2171  CA  HIS A 276      56.081  23.010  34.799  1.00 12.36           C  
ATOM   2172  C   HIS A 276      54.929  23.925  34.392  1.00 11.34           C  
ATOM   2173  O   HIS A 276      54.890  25.090  34.788  1.00 10.06           O  
ATOM   2174  CB  HIS A 276      57.174  23.027  33.724  1.00 12.02           C  
ATOM   2175  CG  HIS A 276      57.779  24.376  33.496  1.00 13.67           C  
ATOM   2176  ND1 HIS A 276      57.345  25.234  32.508  1.00 14.72           N  
ATOM   2177  CD2 HIS A 276      58.785  25.018  34.136  1.00 12.49           C  
ATOM   2178  CE1 HIS A 276      58.058  26.345  32.548  1.00 14.40           C  
ATOM   2179  NE2 HIS A 276      58.939  26.240  33.527  1.00 16.54           N  
ATOM   2180  N   PHE A 277      53.997  23.400  33.603  1.00 10.55           N  
ATOM   2181  CA  PHE A 277      52.852  24.187  33.158  1.00  9.85           C  
ATOM   2182  C   PHE A 277      51.636  23.918  34.028  1.00 10.98           C  
ATOM   2183  O   PHE A 277      50.592  24.538  33.847  1.00 11.22           O  
ATOM   2184  CB  PHE A 277      52.477  23.864  31.707  1.00  9.55           C  
ATOM   2185  CG  PHE A 277      53.520  24.238  30.700  1.00  8.97           C  
ATOM   2186  CD1 PHE A 277      54.493  23.321  30.312  1.00  9.26           C  
ATOM   2187  CD2 PHE A 277      53.509  25.497  30.108  1.00  9.17           C  
ATOM   2188  CE1 PHE A 277      55.436  23.653  29.342  1.00  8.85           C  
ATOM   2189  CE2 PHE A 277      54.448  25.841  29.139  1.00  9.12           C  
ATOM   2190  CZ  PHE A 277      55.413  24.917  28.754  1.00  9.87           C  
ATOM   2191  N   ASN A 278      51.768  22.983  34.962  1.00 12.54           N  
ATOM   2192  CA  ASN A 278      50.664  22.636  35.843  1.00 12.75           C  
ATOM   2193  C   ASN A 278      49.477  22.146  35.013  1.00 12.90           C  
ATOM   2194  O   ASN A 278      48.357  22.637  35.153  1.00 12.60           O  
ATOM   2195  CB  ASN A 278      50.250  23.850  36.682  1.00 17.15           C  
ATOM   2196  CG  ASN A 278      49.261  23.494  37.779  1.00 20.67           C  
ATOM   2197  OD1 ASN A 278      48.669  24.375  38.404  1.00 23.67           O  
ATOM   2198  ND2 ASN A 278      49.083  22.199  38.025  1.00 23.53           N  
ATOM   2199  N   VAL A 279      49.735  21.196  34.122  1.00 10.82           N  
ATOM   2200  CA  VAL A 279      48.676  20.626  33.297  1.00  9.75           C  
ATOM   2201  C   VAL A 279      48.701  19.114  33.448  1.00  9.99           C  
ATOM   2202  O   VAL A 279      49.662  18.553  33.973  1.00 10.53           O  
ATOM   2203  CB  VAL A 279      48.842  20.989  31.807  1.00  6.94           C  
ATOM   2204  CG1 VAL A 279      48.589  22.475  31.611  1.00  4.75           C  
ATOM   2205  CG2 VAL A 279      50.233  20.607  31.325  1.00  6.48           C  
ATOM   2206  N   ASN A 280      47.643  18.456  32.992  1.00  8.73           N  
ATOM   2207  CA  ASN A 280      47.557  17.008  33.098  1.00  9.75           C  
ATOM   2208  C   ASN A 280      47.755  16.343  31.747  1.00 10.44           C  
ATOM   2209  O   ASN A 280      48.087  15.160  31.669  1.00  8.73           O  
ATOM   2210  CB  ASN A 280      46.204  16.615  33.684  1.00  9.94           C  
ATOM   2211  CG  ASN A 280      46.091  16.961  35.151  1.00 12.01           C  
ATOM   2212  OD1 ASN A 280      45.065  17.463  35.608  1.00 14.29           O  
ATOM   2213  ND2 ASN A 280      47.150  16.686  35.902  1.00 10.34           N  
ATOM   2214  N   HIS A 281      47.567  17.114  30.683  1.00  9.54           N  
ATOM   2215  CA  HIS A 281      47.715  16.580  29.337  1.00  8.28           C  
ATOM   2216  C   HIS A 281      48.312  17.608  28.391  1.00  6.40           C  
ATOM   2217  O   HIS A 281      48.252  18.812  28.636  1.00  6.40           O  
ATOM   2218  CB  HIS A 281      46.351  16.164  28.778  1.00  9.65           C  
ATOM   2219  CG  HIS A 281      45.579  15.236  29.664  1.00  9.30           C  
ATOM   2220  ND1 HIS A 281      45.868  13.893  29.770  1.00  7.49           N  
ATOM   2221  CD2 HIS A 281      44.522  15.460  30.481  1.00  9.95           C  
ATOM   2222  CE1 HIS A 281      45.022  13.328  30.613  1.00  8.55           C  
ATOM   2223  NE2 HIS A 281      44.195  14.256  31.058  1.00  8.79           N  
ATOM   2224  N   ILE A 282      48.888  17.118  27.304  1.00  5.69           N  
ATOM   2225  CA  ILE A 282      49.441  17.987  26.275  1.00  5.51           C  
ATOM   2226  C   ILE A 282      48.946  17.419  24.954  1.00  4.98           C  
ATOM   2227  O   ILE A 282      49.165  16.248  24.649  1.00  4.89           O  
ATOM   2228  CB  ILE A 282      50.976  18.009  26.283  1.00  5.54           C  
ATOM   2229  CG1 ILE A 282      51.482  18.504  27.642  1.00  8.31           C  
ATOM   2230  CG2 ILE A 282      51.472  18.940  25.185  1.00  8.31           C  
ATOM   2231  CD1 ILE A 282      52.999  18.510  27.785  1.00  9.15           C  
ATOM   2232  N   VAL A 283      48.243  18.251  24.195  1.00  6.89           N  
ATOM   2233  CA  VAL A 283      47.687  17.858  22.906  1.00  5.39           C  
ATOM   2234  C   VAL A 283      48.555  18.453  21.806  1.00  7.23           C  
ATOM   2235  O   VAL A 283      48.723  19.668  21.741  1.00  6.63           O  
ATOM   2236  CB  VAL A 283      46.247  18.382  22.765  1.00  6.21           C  
ATOM   2237  CG1 VAL A 283      45.671  17.999  21.416  1.00  4.73           C  
ATOM   2238  CG2 VAL A 283      45.393  17.817  23.888  1.00  7.75           C  
ATOM   2239  N   VAL A 284      49.098  17.594  20.948  1.00  6.89           N  
ATOM   2240  CA  VAL A 284      49.974  18.036  19.870  1.00  6.13           C  
ATOM   2241  C   VAL A 284      49.599  17.429  18.520  1.00  5.43           C  
ATOM   2242  O   VAL A 284      48.977  16.373  18.453  1.00  7.24           O  
ATOM   2243  CB  VAL A 284      51.443  17.640  20.152  1.00  8.43           C  
ATOM   2244  CG1 VAL A 284      51.870  18.119  21.527  1.00  9.09           C  
ATOM   2245  CG2 VAL A 284      51.595  16.132  20.064  1.00  6.96           C  
ATOM   2246  N   GLY A 285      49.990  18.107  17.447  1.00  5.92           N  
ATOM   2247  CA  GLY A 285      49.739  17.595  16.108  1.00  7.05           C  
ATOM   2248  C   GLY A 285      51.127  17.318  15.566  1.00  6.48           C  
ATOM   2249  O   GLY A 285      51.907  16.622  16.221  1.00  8.21           O  
ATOM   2250  N   HIS A 286      51.425  17.846  14.380  1.00  6.69           N  
ATOM   2251  CA  HIS A 286      52.748  17.742  13.751  1.00  7.17           C  
ATOM   2252  C   HIS A 286      53.273  16.363  13.338  1.00  9.02           C  
ATOM   2253  O   HIS A 286      53.726  16.186  12.206  1.00  6.98           O  
ATOM   2254  CB  HIS A 286      53.773  18.434  14.664  1.00  6.70           C  
ATOM   2255  CG  HIS A 286      55.116  18.647  14.035  1.00  8.78           C  
ATOM   2256  ND1 HIS A 286      55.275  19.203  12.783  1.00  6.98           N  
ATOM   2257  CD2 HIS A 286      56.365  18.437  14.515  1.00  6.47           C  
ATOM   2258  CE1 HIS A 286      56.564  19.327  12.519  1.00  9.24           C  
ATOM   2259  NE2 HIS A 286      57.247  18.870  13.555  1.00  7.43           N  
ATOM   2260  N   THR A 287      53.235  15.396  14.250  1.00  8.30           N  
ATOM   2261  CA  THR A 287      53.724  14.053  13.947  1.00  7.62           C  
ATOM   2262  C   THR A 287      52.526  13.147  13.678  1.00  7.21           C  
ATOM   2263  O   THR A 287      51.811  12.746  14.594  1.00  9.56           O  
ATOM   2264  CB  THR A 287      54.573  13.518  15.110  1.00  6.68           C  
ATOM   2265  OG1 THR A 287      55.561  14.500  15.453  1.00  9.38           O  
ATOM   2266  CG2 THR A 287      55.286  12.232  14.710  1.00  5.93           C  
ATOM   2267  N   SER A 288      52.324  12.844  12.399  1.00  8.56           N  
ATOM   2268  CA  SER A 288      51.197  12.051  11.914  1.00  9.07           C  
ATOM   2269  C   SER A 288      50.996  10.642  12.467  1.00  9.72           C  
ATOM   2270  O   SER A 288      51.905   9.809  12.439  1.00 10.93           O  
ATOM   2271  CB  SER A 288      51.264  11.991  10.390  1.00 10.55           C  
ATOM   2272  OG  SER A 288      51.478  13.287   9.856  1.00 12.74           O  
ATOM   2273  N   GLN A 289      49.782  10.385  12.951  1.00  8.75           N  
ATOM   2274  CA  GLN A 289      49.410   9.086  13.505  1.00  9.32           C  
ATOM   2275  C   GLN A 289      48.294   8.508  12.643  1.00 11.05           C  
ATOM   2276  O   GLN A 289      47.690   9.227  11.844  1.00 11.53           O  
ATOM   2277  CB  GLN A 289      48.920   9.239  14.948  1.00  8.92           C  
ATOM   2278  CG  GLN A 289      49.909   9.953  15.854  1.00 10.51           C  
ATOM   2279  CD  GLN A 289      51.260   9.268  15.883  1.00 12.08           C  
ATOM   2280  OE1 GLN A 289      52.304   9.921  15.815  1.00 12.51           O  
ATOM   2281  NE2 GLN A 289      51.249   7.945  15.993  1.00  9.89           N  
ATOM   2282  N   GLU A 290      48.021   7.217  12.806  1.00 12.56           N  
ATOM   2283  CA  GLU A 290      46.974   6.553  12.032  1.00 13.65           C  
ATOM   2284  C   GLU A 290      45.586   6.883  12.576  1.00 13.21           C  
ATOM   2285  O   GLU A 290      44.570   6.633  11.920  1.00 11.77           O  
ATOM   2286  CB  GLU A 290      47.178   5.034  12.058  1.00 17.63           C  
ATOM   2287  CG  GLU A 290      48.561   4.560  11.618  1.00 24.13           C  
ATOM   2288  CD  GLU A 290      48.895   4.912  10.177  1.00 29.08           C  
ATOM   2289  OE1 GLU A 290      49.957   4.463   9.687  1.00 31.14           O  
ATOM   2290  OE2 GLU A 290      48.105   5.635   9.531  1.00 33.12           O  
ATOM   2291  N   ARG A 291      45.554   7.453  13.776  1.00 11.02           N  
ATOM   2292  CA  ARG A 291      44.306   7.818  14.439  1.00 11.56           C  
ATOM   2293  C   ARG A 291      44.655   8.698  15.634  1.00 10.81           C  
ATOM   2294  O   ARG A 291      45.825   8.811  16.003  1.00  9.19           O  
ATOM   2295  CB  ARG A 291      43.604   6.557  14.949  1.00 12.91           C  
ATOM   2296  CG  ARG A 291      44.460   5.777  15.943  1.00 16.32           C  
ATOM   2297  CD  ARG A 291      43.884   4.412  16.295  1.00 19.19           C  
ATOM   2298  NE  ARG A 291      44.926   3.528  16.820  1.00 25.86           N  
ATOM   2299  CZ  ARG A 291      45.574   3.726  17.964  1.00 26.28           C  
ATOM   2300  NH1 ARG A 291      46.513   2.876  18.360  1.00 27.20           N  
ATOM   2301  NH2 ARG A 291      45.275   4.767  18.723  1.00 28.95           N  
ATOM   2302  N   VAL A 292      43.654   9.330  16.236  1.00  9.15           N  
ATOM   2303  CA  VAL A 292      43.922  10.139  17.416  1.00  9.02           C  
ATOM   2304  C   VAL A 292      44.296   9.117  18.484  1.00 10.50           C  
ATOM   2305  O   VAL A 292      43.586   8.128  18.681  1.00 11.71           O  
ATOM   2306  CB  VAL A 292      42.682  10.938  17.861  1.00  8.67           C  
ATOM   2307  CG1 VAL A 292      42.875  11.456  19.275  1.00  6.44           C  
ATOM   2308  CG2 VAL A 292      42.464  12.118  16.912  1.00  5.02           C  
ATOM   2309  N   LEU A 293      45.416   9.334  19.158  1.00  9.77           N  
ATOM   2310  CA  LEU A 293      45.845   8.383  20.171  1.00  9.25           C  
ATOM   2311  C   LEU A 293      46.593   9.025  21.327  1.00  8.56           C  
ATOM   2312  O   LEU A 293      47.062  10.164  21.231  1.00  8.73           O  
ATOM   2313  CB  LEU A 293      46.707   7.297  19.518  1.00  8.59           C  
ATOM   2314  CG  LEU A 293      47.942   7.742  18.729  1.00  9.53           C  
ATOM   2315  CD1 LEU A 293      49.075   8.088  19.689  1.00  8.28           C  
ATOM   2316  CD2 LEU A 293      48.375   6.624  17.792  1.00  6.20           C  
ATOM   2317  N   GLY A 294      46.688   8.282  22.425  1.00  8.98           N  
ATOM   2318  CA  GLY A 294      47.374   8.781  23.597  1.00  8.10           C  
ATOM   2319  C   GLY A 294      48.660   8.028  23.863  1.00  9.16           C  
ATOM   2320  O   GLY A 294      48.794   6.847  23.530  1.00  7.34           O  
ATOM   2321  N   LEU A 295      49.616   8.733  24.449  1.00  8.95           N  
ATOM   2322  CA  LEU A 295      50.905   8.158  24.794  1.00 10.47           C  
ATOM   2323  C   LEU A 295      51.169   8.480  26.256  1.00  9.86           C  
ATOM   2324  O   LEU A 295      50.623   9.445  26.793  1.00 11.01           O  
ATOM   2325  CB  LEU A 295      52.003   8.759  23.917  1.00 11.28           C  
ATOM   2326  CG  LEU A 295      51.876   8.491  22.415  1.00 13.97           C  
ATOM   2327  CD1 LEU A 295      52.822   9.397  21.651  1.00 14.66           C  
ATOM   2328  CD2 LEU A 295      52.178   7.030  22.128  1.00 13.29           C  
ATOM   2329  N   PHE A 296      51.997   7.661  26.895  1.00  9.01           N  
ATOM   2330  CA  PHE A 296      52.355   7.841  28.297  1.00 10.56           C  
ATOM   2331  C   PHE A 296      51.129   7.995  29.187  1.00 11.46           C  
ATOM   2332  O   PHE A 296      50.942   9.023  29.840  1.00 10.12           O  
ATOM   2333  CB  PHE A 296      53.272   9.054  28.453  1.00 11.23           C  
ATOM   2334  CG  PHE A 296      54.426   9.061  27.495  1.00 10.63           C  
ATOM   2335  CD1 PHE A 296      54.420   9.896  26.384  1.00 11.33           C  
ATOM   2336  CD2 PHE A 296      55.514   8.214  27.690  1.00 12.31           C  
ATOM   2337  CE1 PHE A 296      55.484   9.887  25.478  1.00 12.27           C  
ATOM   2338  CE2 PHE A 296      56.578   8.199  26.793  1.00 10.30           C  
ATOM   2339  CZ  PHE A 296      56.565   9.035  25.688  1.00  9.70           C  
ATOM   2340  N   HIS A 297      50.303   6.955  29.212  1.00 11.86           N  
ATOM   2341  CA  HIS A 297      49.088   6.963  30.008  1.00 13.46           C  
ATOM   2342  C   HIS A 297      48.236   8.183  29.683  1.00 12.93           C  
ATOM   2343  O   HIS A 297      47.691   8.840  30.574  1.00 12.07           O  
ATOM   2344  CB  HIS A 297      49.430   6.919  31.499  1.00 15.27           C  
ATOM   2345  CG  HIS A 297      50.118   5.656  31.912  1.00 18.92           C  
ATOM   2346  ND1 HIS A 297      51.418   5.365  31.554  1.00 19.22           N  
ATOM   2347  CD2 HIS A 297      49.671   4.583  32.607  1.00 19.86           C  
ATOM   2348  CE1 HIS A 297      51.740   4.167  32.009  1.00 20.57           C  
ATOM   2349  NE2 HIS A 297      50.698   3.671  32.651  1.00 20.25           N  
ATOM   2350  N   ASN A 298      48.142   8.472  28.390  1.00 11.42           N  
ATOM   2351  CA  ASN A 298      47.351   9.584  27.880  1.00 11.78           C  
ATOM   2352  C   ASN A 298      47.766  10.972  28.345  1.00 10.89           C  
ATOM   2353  O   ASN A 298      46.974  11.907  28.291  1.00 11.75           O  
ATOM   2354  CB  ASN A 298      45.876   9.341  28.198  1.00 12.90           C  
ATOM   2355  CG  ASN A 298      45.330   8.121  27.487  1.00 11.86           C  
ATOM   2356  OD1 ASN A 298      44.341   7.528  27.912  1.00 17.61           O  
ATOM   2357  ND2 ASN A 298      45.972   7.744  26.388  1.00 13.80           N  
ATOM   2358  N   LYS A 299      49.008  11.117  28.791  1.00 10.90           N  
ATOM   2359  CA  LYS A 299      49.494  12.422  29.223  1.00  9.49           C  
ATOM   2360  C   LYS A 299      49.778  13.256  27.977  1.00  8.87           C  
ATOM   2361  O   LYS A 299      49.849  14.485  28.026  1.00  8.46           O  
ATOM   2362  CB  LYS A 299      50.744  12.258  30.087  1.00  8.74           C  
ATOM   2363  CG  LYS A 299      50.431  11.605  31.430  1.00 11.13           C  
ATOM   2364  CD  LYS A 299      51.685  11.335  32.247  1.00 11.33           C  
ATOM   2365  CE  LYS A 299      51.323  10.780  33.620  1.00 12.21           C  
ATOM   2366  NZ  LYS A 299      52.530  10.433  34.420  1.00 10.54           N  
ATOM   2367  N   VAL A 300      49.948  12.569  26.856  1.00 10.13           N  
ATOM   2368  CA  VAL A 300      50.163  13.226  25.577  1.00  9.59           C  
ATOM   2369  C   VAL A 300      49.131  12.648  24.620  1.00  9.10           C  
ATOM   2370  O   VAL A 300      48.993  11.428  24.515  1.00  8.50           O  
ATOM   2371  CB  VAL A 300      51.571  12.956  25.002  1.00  9.72           C  
ATOM   2372  CG1 VAL A 300      51.592  13.288  23.521  1.00  9.33           C  
ATOM   2373  CG2 VAL A 300      52.608  13.803  25.738  1.00  9.42           C  
ATOM   2374  N   ILE A 301      48.387  13.519  23.946  1.00  7.68           N  
ATOM   2375  CA  ILE A 301      47.390  13.058  22.992  1.00  8.27           C  
ATOM   2376  C   ILE A 301      47.742  13.590  21.615  1.00  7.32           C  
ATOM   2377  O   ILE A 301      47.784  14.801  21.400  1.00  6.35           O  
ATOM   2378  CB  ILE A 301      45.974  13.537  23.342  1.00  9.11           C  
ATOM   2379  CG1 ILE A 301      45.634  13.176  24.792  1.00  9.38           C  
ATOM   2380  CG2 ILE A 301      44.975  12.895  22.389  1.00  7.07           C  
ATOM   2381  CD1 ILE A 301      45.647  11.692  25.076  1.00  9.16           C  
ATOM   2382  N   ALA A 302      48.004  12.674  20.690  1.00  6.65           N  
ATOM   2383  CA  ALA A 302      48.359  13.037  19.329  1.00  7.16           C  
ATOM   2384  C   ALA A 302      47.081  13.280  18.540  1.00  8.47           C  
ATOM   2385  O   ALA A 302      46.223  12.395  18.448  1.00  6.12           O  
ATOM   2386  CB  ALA A 302      49.173  11.918  18.691  1.00  8.36           C  
ATOM   2387  N   VAL A 303      46.951  14.481  17.981  1.00  8.38           N  
ATOM   2388  CA  VAL A 303      45.766  14.818  17.207  1.00  9.50           C  
ATOM   2389  C   VAL A 303      46.005  15.025  15.713  1.00  8.95           C  
ATOM   2390  O   VAL A 303      45.147  15.561  15.015  1.00  9.98           O  
ATOM   2391  CB  VAL A 303      45.029  16.045  17.794  1.00  8.45           C  
ATOM   2392  CG1 VAL A 303      44.517  15.708  19.184  1.00 10.50           C  
ATOM   2393  CG2 VAL A 303      45.942  17.252  17.835  1.00  9.44           C  
ATOM   2394  N   ASP A 304      47.179  14.635  15.224  1.00  7.04           N  
ATOM   2395  CA  ASP A 304      47.428  14.700  13.788  1.00  8.20           C  
ATOM   2396  C   ASP A 304      47.068  13.275  13.382  1.00  7.20           C  
ATOM   2397  O   ASP A 304      47.857  12.348  13.567  1.00  7.10           O  
ATOM   2398  CB  ASP A 304      48.898  14.980  13.458  1.00  6.76           C  
ATOM   2399  CG  ASP A 304      49.176  14.920  11.959  1.00  8.90           C  
ATOM   2400  OD1 ASP A 304      50.295  15.272  11.533  1.00  8.44           O  
ATOM   2401  OD2 ASP A 304      48.268  14.515  11.203  1.00  6.26           O  
ATOM   2402  N   SER A 305      45.855  13.111  12.866  1.00  7.01           N  
ATOM   2403  CA  SER A 305      45.336  11.811  12.466  1.00  7.47           C  
ATOM   2404  C   SER A 305      45.531  11.520  10.983  1.00  7.32           C  
ATOM   2405  O   SER A 305      44.783  10.742  10.392  1.00  8.86           O  
ATOM   2406  CB  SER A 305      43.850  11.734  12.809  1.00  7.58           C  
ATOM   2407  OG  SER A 305      43.130  12.748  12.131  1.00  8.31           O  
ATOM   2408  N   SER A 306      46.535  12.156  10.390  1.00  6.82           N  
ATOM   2409  CA  SER A 306      46.861  11.968   8.980  1.00  6.47           C  
ATOM   2410  C   SER A 306      45.785  12.416   7.991  1.00  6.18           C  
ATOM   2411  O   SER A 306      45.530  11.751   6.982  1.00  6.32           O  
ATOM   2412  CB  SER A 306      47.231  10.508   8.719  1.00  6.54           C  
ATOM   2413  OG  SER A 306      48.387  10.152   9.460  1.00  3.69           O  
ATOM   2414  N   ILE A 307      45.154  13.548   8.281  1.00  7.30           N  
ATOM   2415  CA  ILE A 307      44.144  14.092   7.384  1.00  7.44           C  
ATOM   2416  C   ILE A 307      44.861  14.474   6.087  1.00  8.27           C  
ATOM   2417  O   ILE A 307      44.254  14.527   5.015  1.00  8.44           O  
ATOM   2418  CB  ILE A 307      43.470  15.346   8.003  1.00  6.72           C  
ATOM   2419  CG1 ILE A 307      42.591  14.927   9.188  1.00  7.33           C  
ATOM   2420  CG2 ILE A 307      42.647  16.083   6.954  1.00  6.46           C  
ATOM   2421  CD1 ILE A 307      41.953  16.086   9.932  1.00  6.66           C  
ATOM   2422  N   LYS A 308      46.165  14.720   6.193  1.00  7.73           N  
ATOM   2423  CA  LYS A 308      46.972  15.106   5.039  1.00  8.00           C  
ATOM   2424  C   LYS A 308      46.930  14.063   3.923  1.00  7.64           C  
ATOM   2425  O   LYS A 308      47.089  14.404   2.754  1.00  7.85           O  
ATOM   2426  CB  LYS A 308      48.430  15.349   5.454  1.00  7.74           C  
ATOM   2427  CG  LYS A 308      49.175  14.094   5.888  1.00  8.14           C  
ATOM   2428  CD  LYS A 308      50.605  14.404   6.324  1.00  7.76           C  
ATOM   2429  CE  LYS A 308      51.343  13.132   6.726  1.00  9.95           C  
ATOM   2430  NZ  LYS A 308      52.759  13.380   7.132  1.00 11.95           N  
ATOM   2431  N   VAL A 309      46.717  12.800   4.284  1.00  7.05           N  
ATOM   2432  CA  VAL A 309      46.654  11.722   3.296  1.00  9.52           C  
ATOM   2433  C   VAL A 309      45.412  11.847   2.408  1.00  8.95           C  
ATOM   2434  O   VAL A 309      45.323  11.222   1.351  1.00 10.01           O  
ATOM   2435  CB  VAL A 309      46.670  10.337   3.988  1.00  8.44           C  
ATOM   2436  CG1 VAL A 309      46.639   9.221   2.949  1.00 11.70           C  
ATOM   2437  CG2 VAL A 309      47.914  10.216   4.852  1.00 11.61           C  
ATOM   2438  N   GLY A 310      44.452  12.652   2.849  1.00 10.02           N  
ATOM   2439  CA  GLY A 310      43.251  12.885   2.066  1.00 10.88           C  
ATOM   2440  C   GLY A 310      42.177  11.813   2.000  1.00 10.56           C  
ATOM   2441  O   GLY A 310      41.385  11.808   1.057  1.00 11.59           O  
ATOM   2442  N   LYS A 311      42.131  10.920   2.983  1.00  9.65           N  
ATOM   2443  CA  LYS A 311      41.122   9.865   2.993  1.00 11.63           C  
ATOM   2444  C   LYS A 311      40.250   9.899   4.244  1.00 11.02           C  
ATOM   2445  O   LYS A 311      39.066   9.574   4.190  1.00 10.62           O  
ATOM   2446  CB  LYS A 311      41.781   8.488   2.876  1.00 14.27           C  
ATOM   2447  CG  LYS A 311      42.527   8.263   1.571  1.00 19.90           C  
ATOM   2448  CD  LYS A 311      42.941   6.803   1.396  1.00 25.71           C  
ATOM   2449  CE  LYS A 311      41.739   5.883   1.142  1.00 28.23           C  
ATOM   2450  NZ  LYS A 311      40.805   5.752   2.306  1.00 29.34           N  
ATOM   2451  N   SER A 312      40.832  10.286   5.372  1.00  9.42           N  
ATOM   2452  CA  SER A 312      40.071  10.344   6.612  1.00  9.01           C  
ATOM   2453  C   SER A 312      40.796  11.142   7.678  1.00  8.88           C  
ATOM   2454  O   SER A 312      41.921  11.592   7.475  1.00  8.07           O  
ATOM   2455  CB  SER A 312      39.811   8.936   7.145  1.00 10.49           C  
ATOM   2456  OG  SER A 312      41.023   8.310   7.529  1.00 12.40           O  
ATOM   2457  N   GLY A 313      40.130  11.297   8.817  1.00  8.66           N  
ATOM   2458  CA  GLY A 313      40.692  12.024   9.938  1.00  9.30           C  
ATOM   2459  C   GLY A 313      39.864  11.792  11.189  1.00  9.15           C  
ATOM   2460  O   GLY A 313      38.751  11.262  11.130  1.00  7.45           O  
ATOM   2461  N   GLU A 314      40.417  12.177  12.332  1.00  9.50           N  
ATOM   2462  CA  GLU A 314      39.729  12.024  13.604  1.00  7.94           C  
ATOM   2463  C   GLU A 314      39.975  13.265  14.442  1.00  7.72           C  
ATOM   2464  O   GLU A 314      40.781  14.125  14.075  1.00  6.82           O  
ATOM   2465  CB  GLU A 314      40.242  10.783  14.343  1.00  8.68           C  
ATOM   2466  CG  GLU A 314      39.965   9.479  13.611  1.00  7.53           C  
ATOM   2467  CD  GLU A 314      40.475   8.260  14.357  1.00  9.68           C  
ATOM   2468  OE1 GLU A 314      40.235   7.129  13.877  1.00  9.79           O  
ATOM   2469  OE2 GLU A 314      41.115   8.430  15.417  1.00  9.82           O  
ATOM   2470  N   LEU A 315      39.272  13.363  15.560  1.00  6.03           N  
ATOM   2471  CA  LEU A 315      39.424  14.505  16.448  1.00  6.30           C  
ATOM   2472  C   LEU A 315      39.366  14.048  17.898  1.00  6.25           C  
ATOM   2473  O   LEU A 315      38.983  12.913  18.182  1.00  8.24           O  
ATOM   2474  CB  LEU A 315      38.330  15.549  16.166  1.00  7.14           C  
ATOM   2475  CG  LEU A 315      36.858  15.115  16.197  1.00  7.60           C  
ATOM   2476  CD1 LEU A 315      36.397  14.944  17.637  1.00  4.19           C  
ATOM   2477  CD2 LEU A 315      36.000  16.168  15.505  1.00  8.27           C  
ATOM   2478  N   LEU A 316      39.766  14.937  18.802  1.00  7.24           N  
ATOM   2479  CA  LEU A 316      39.754  14.666  20.233  1.00  7.22           C  
ATOM   2480  C   LEU A 316      38.710  15.558  20.885  1.00  9.31           C  
ATOM   2481  O   LEU A 316      38.647  16.756  20.611  1.00  6.85           O  
ATOM   2482  CB  LEU A 316      41.122  14.966  20.852  1.00  8.31           C  
ATOM   2483  CG  LEU A 316      41.227  14.923  22.386  1.00  7.63           C  
ATOM   2484  CD1 LEU A 316      41.075  13.495  22.902  1.00  6.37           C  
ATOM   2485  CD2 LEU A 316      42.576  15.488  22.806  1.00  6.96           C  
ATOM   2486  N   LEU A 317      37.890  14.958  21.740  1.00  9.62           N  
ATOM   2487  CA  LEU A 317      36.849  15.673  22.456  1.00 10.85           C  
ATOM   2488  C   LEU A 317      37.198  15.614  23.933  1.00 10.16           C  
ATOM   2489  O   LEU A 317      37.397  14.531  24.485  1.00 10.67           O  
ATOM   2490  CB  LEU A 317      35.487  15.005  22.213  1.00 12.21           C  
ATOM   2491  CG  LEU A 317      34.220  15.587  22.857  1.00 14.78           C  
ATOM   2492  CD1 LEU A 317      33.007  14.779  22.397  1.00 15.76           C  
ATOM   2493  CD2 LEU A 317      34.320  15.551  24.372  1.00 19.11           C  
ATOM   2494  N   LEU A 318      37.288  16.780  24.566  1.00 10.50           N  
ATOM   2495  CA  LEU A 318      37.590  16.859  25.990  1.00 11.37           C  
ATOM   2496  C   LEU A 318      36.371  17.475  26.672  1.00 12.05           C  
ATOM   2497  O   LEU A 318      36.115  18.674  26.555  1.00 10.63           O  
ATOM   2498  CB  LEU A 318      38.831  17.723  26.234  1.00 10.46           C  
ATOM   2499  CG  LEU A 318      40.095  17.335  25.465  1.00 11.87           C  
ATOM   2500  CD1 LEU A 318      40.130  18.094  24.139  1.00 10.30           C  
ATOM   2501  CD2 LEU A 318      41.329  17.682  26.281  1.00 11.59           C  
ATOM   2502  N   GLU A 319      35.615  16.642  27.378  1.00 12.68           N  
ATOM   2503  CA  GLU A 319      34.403  17.095  28.043  1.00 16.24           C  
ATOM   2504  C   GLU A 319      34.133  16.216  29.253  1.00 16.99           C  
ATOM   2505  O   GLU A 319      34.401  15.015  29.227  1.00 17.90           O  
ATOM   2506  CB  GLU A 319      33.228  17.005  27.061  1.00 17.31           C  
ATOM   2507  CG  GLU A 319      31.932  17.656  27.513  1.00 18.03           C  
ATOM   2508  CD  GLU A 319      30.836  17.559  26.455  1.00 19.21           C  
ATOM   2509  OE1 GLU A 319      29.821  18.277  26.572  1.00 18.93           O  
ATOM   2510  OE2 GLU A 319      30.988  16.759  25.507  1.00 18.89           O  
ATOM   2511  N   ASN A 320      33.609  16.819  30.313  1.00 18.49           N  
ATOM   2512  CA  ASN A 320      33.296  16.082  31.531  1.00 19.76           C  
ATOM   2513  C   ASN A 320      34.511  15.305  32.044  1.00 20.28           C  
ATOM   2514  O   ASN A 320      34.380  14.194  32.564  1.00 20.99           O  
ATOM   2515  CB  ASN A 320      32.127  15.126  31.269  1.00 20.02           C  
ATOM   2516  CG  ASN A 320      30.897  15.844  30.729  1.00 21.68           C  
ATOM   2517  OD1 ASN A 320      30.406  16.798  31.333  1.00 21.46           O  
ATOM   2518  ND2 ASN A 320      30.393  15.384  29.588  1.00 21.61           N  
ATOM   2519  N   ASN A 321      35.689  15.906  31.889  1.00 20.95           N  
ATOM   2520  CA  ASN A 321      36.949  15.318  32.335  1.00 20.77           C  
ATOM   2521  C   ASN A 321      37.341  14.023  31.640  1.00 19.81           C  
ATOM   2522  O   ASN A 321      38.142  13.249  32.163  1.00 20.06           O  
ATOM   2523  CB  ASN A 321      36.925  15.104  33.851  1.00 23.72           C  
ATOM   2524  CG  ASN A 321      37.373  16.333  34.616  1.00 28.02           C  
ATOM   2525  OD1 ASN A 321      37.143  16.447  35.822  1.00 31.26           O  
ATOM   2526  ND2 ASN A 321      38.032  17.257  33.922  1.00 28.09           N  
ATOM   2527  N   ARG A 322      36.777  13.784  30.464  1.00 18.13           N  
ATOM   2528  CA  ARG A 322      37.109  12.588  29.706  1.00 17.20           C  
ATOM   2529  C   ARG A 322      37.817  12.986  28.422  1.00 15.52           C  
ATOM   2530  O   ARG A 322      37.685  14.116  27.952  1.00 13.39           O  
ATOM   2531  CB  ARG A 322      35.851  11.788  29.361  1.00 19.21           C  
ATOM   2532  CG  ARG A 322      35.117  11.233  30.566  1.00 22.93           C  
ATOM   2533  CD  ARG A 322      34.112  10.178  30.141  1.00 27.12           C  
ATOM   2534  NE  ARG A 322      33.236  10.665  29.081  1.00 29.77           N  
ATOM   2535  CZ  ARG A 322      32.261   9.950  28.529  1.00 31.72           C  
ATOM   2536  NH1 ARG A 322      32.033   8.709  28.939  1.00 33.55           N  
ATOM   2537  NH2 ARG A 322      31.516  10.474  27.564  1.00 32.62           N  
ATOM   2538  N   LEU A 323      38.589  12.056  27.878  1.00 13.95           N  
ATOM   2539  CA  LEU A 323      39.300  12.271  26.629  1.00 12.80           C  
ATOM   2540  C   LEU A 323      38.633  11.288  25.683  1.00 13.56           C  
ATOM   2541  O   LEU A 323      38.689  10.074  25.898  1.00 12.91           O  
ATOM   2542  CB  LEU A 323      40.784  11.939  26.788  1.00 14.13           C  
ATOM   2543  CG  LEU A 323      41.565  12.824  27.765  1.00 14.80           C  
ATOM   2544  CD1 LEU A 323      43.007  12.343  27.863  1.00 14.04           C  
ATOM   2545  CD2 LEU A 323      41.522  14.266  27.291  1.00 13.68           C  
ATOM   2546  N   ILE A 324      37.987  11.810  24.646  1.00 12.33           N  
ATOM   2547  CA  ILE A 324      37.280  10.960  23.703  1.00 10.80           C  
ATOM   2548  C   ILE A 324      37.781  11.081  22.272  1.00 11.93           C  
ATOM   2549  O   ILE A 324      38.069  12.173  21.782  1.00 10.21           O  
ATOM   2550  CB  ILE A 324      35.768  11.257  23.753  1.00 11.68           C  
ATOM   2551  CG1 ILE A 324      35.237  10.911  25.146  1.00 13.97           C  
ATOM   2552  CG2 ILE A 324      35.032  10.463  22.684  1.00 10.79           C  
ATOM   2553  CD1 ILE A 324      33.798  11.312  25.381  1.00 18.65           C  
ATOM   2554  N   ARG A 325      37.891   9.931  21.620  1.00 10.17           N  
ATOM   2555  CA  ARG A 325      38.345   9.849  20.243  1.00 10.85           C  
ATOM   2556  C   ARG A 325      37.123   9.883  19.327  1.00 10.45           C  
ATOM   2557  O   ARG A 325      36.222   9.049  19.446  1.00  8.99           O  
ATOM   2558  CB  ARG A 325      39.122   8.545  20.043  1.00 11.45           C  
ATOM   2559  CG  ARG A 325      39.549   8.237  18.616  1.00 11.06           C  
ATOM   2560  CD  ARG A 325      40.095   6.817  18.533  1.00 11.42           C  
ATOM   2561  NE  ARG A 325      40.317   6.380  17.156  1.00  9.55           N  
ATOM   2562  CZ  ARG A 325      40.303   5.109  16.770  1.00 11.37           C  
ATOM   2563  NH1 ARG A 325      40.075   4.147  17.658  1.00 10.00           N  
ATOM   2564  NH2 ARG A 325      40.515   4.797  15.498  1.00 10.43           N  
ATOM   2565  N   GLY A 326      37.087  10.866  18.432  1.00  9.07           N  
ATOM   2566  CA  GLY A 326      35.977  10.976  17.501  1.00  9.78           C  
ATOM   2567  C   GLY A 326      36.418  10.429  16.158  1.00  9.52           C  
ATOM   2568  O   GLY A 326      37.229  11.053  15.475  1.00  9.63           O  
ATOM   2569  N   LEU A 327      35.894   9.265  15.776  1.00  8.27           N  
ATOM   2570  CA  LEU A 327      36.274   8.645  14.510  1.00  8.38           C  
ATOM   2571  C   LEU A 327      35.651   9.319  13.298  1.00  7.82           C  
ATOM   2572  O   LEU A 327      34.667  10.050  13.411  1.00  6.60           O  
ATOM   2573  CB  LEU A 327      35.924   7.151  14.511  1.00  9.42           C  
ATOM   2574  CG  LEU A 327      36.722   6.257  15.471  1.00  9.58           C  
ATOM   2575  CD1 LEU A 327      36.222   6.455  16.899  1.00 12.15           C  
ATOM   2576  CD2 LEU A 327      36.562   4.803  15.063  1.00 11.62           C  
ATOM   2577  N   TYR A 328      36.237   9.057  12.136  1.00  7.08           N  
ATOM   2578  CA  TYR A 328      35.779   9.633  10.880  1.00  8.81           C  
ATOM   2579  C   TYR A 328      34.348   9.228  10.555  1.00 10.20           C  
ATOM   2580  O   TYR A 328      33.605   9.994   9.943  1.00 11.06           O  
ATOM   2581  CB  TYR A 328      36.702   9.190   9.745  1.00  8.90           C  
ATOM   2582  CG  TYR A 328      36.590  10.016   8.488  1.00 10.37           C  
ATOM   2583  CD1 TYR A 328      36.362   9.411   7.253  1.00 10.09           C  
ATOM   2584  CD2 TYR A 328      36.756  11.401   8.524  1.00 10.91           C  
ATOM   2585  CE1 TYR A 328      36.304  10.160   6.083  1.00  8.25           C  
ATOM   2586  CE2 TYR A 328      36.702  12.162   7.356  1.00 10.88           C  
ATOM   2587  CZ  TYR A 328      36.477  11.531   6.142  1.00  9.51           C  
ATOM   2588  OH  TYR A 328      36.439  12.272   4.986  1.00  8.91           O  
ATOM   2589  N   ASP A 329      33.960   8.027  10.971  1.00 11.15           N  
ATOM   2590  CA  ASP A 329      32.619   7.539  10.693  1.00 11.60           C  
ATOM   2591  C   ASP A 329      31.562   8.090  11.643  1.00 12.02           C  
ATOM   2592  O   ASP A 329      30.397   7.706  11.569  1.00 12.77           O  
ATOM   2593  CB  ASP A 329      32.593   6.007  10.709  1.00 11.40           C  
ATOM   2594  CG  ASP A 329      32.816   5.423  12.094  1.00 12.97           C  
ATOM   2595  OD1 ASP A 329      32.695   4.187  12.227  1.00 15.50           O  
ATOM   2596  OD2 ASP A 329      33.105   6.182  13.042  1.00 11.82           O  
ATOM   2597  N   GLY A 330      31.966   8.988  12.535  1.00 11.10           N  
ATOM   2598  CA  GLY A 330      31.012   9.580  13.455  1.00 10.25           C  
ATOM   2599  C   GLY A 330      30.877   8.914  14.811  1.00 11.16           C  
ATOM   2600  O   GLY A 330      30.175   9.421  15.682  1.00 12.26           O  
ATOM   2601  N   THR A 331      31.531   7.776  14.997  1.00 11.81           N  
ATOM   2602  CA  THR A 331      31.464   7.083  16.279  1.00 13.28           C  
ATOM   2603  C   THR A 331      32.572   7.599  17.188  1.00 13.81           C  
ATOM   2604  O   THR A 331      33.467   8.320  16.744  1.00 11.57           O  
ATOM   2605  CB  THR A 331      31.634   5.559  16.112  1.00 13.57           C  
ATOM   2606  OG1 THR A 331      32.935   5.271  15.585  1.00 13.41           O  
ATOM   2607  CG2 THR A 331      30.575   5.008  15.165  1.00 13.44           C  
ATOM   2608  N   ARG A 332      32.503   7.231  18.462  1.00 14.35           N  
ATOM   2609  CA  ARG A 332      33.503   7.651  19.436  1.00 16.28           C  
ATOM   2610  C   ARG A 332      34.005   6.506  20.292  1.00 17.23           C  
ATOM   2611  O   ARG A 332      33.335   5.485  20.457  1.00 16.44           O  
ATOM   2612  CB  ARG A 332      32.946   8.731  20.364  1.00 19.12           C  
ATOM   2613  CG  ARG A 332      31.433   8.778  20.443  1.00 22.38           C  
ATOM   2614  CD  ARG A 332      30.909   9.549  19.259  1.00 24.59           C  
ATOM   2615  NE  ARG A 332      31.680  10.776  19.111  1.00 23.98           N  
ATOM   2616  CZ  ARG A 332      31.716  11.736  20.026  1.00 27.19           C  
ATOM   2617  NH1 ARG A 332      31.020  11.606  21.146  1.00 27.96           N  
ATOM   2618  NH2 ARG A 332      32.450  12.823  19.828  1.00 30.90           N  
ATOM   2619  N   GLU A 333      35.200   6.698  20.832  1.00 16.78           N  
ATOM   2620  CA  GLU A 333      35.836   5.729  21.707  1.00 18.74           C  
ATOM   2621  C   GLU A 333      36.507   6.527  22.811  1.00 17.81           C  
ATOM   2622  O   GLU A 333      37.232   7.485  22.542  1.00 17.05           O  
ATOM   2623  CB  GLU A 333      36.885   4.913  20.954  1.00 20.30           C  
ATOM   2624  CG  GLU A 333      36.317   3.974  19.906  1.00 25.19           C  
ATOM   2625  CD  GLU A 333      37.381   3.094  19.286  1.00 29.35           C  
ATOM   2626  OE1 GLU A 333      37.050   2.318  18.363  1.00 32.36           O  
ATOM   2627  OE2 GLU A 333      38.551   3.177  19.724  1.00 32.12           O  
ATOM   2628  N   THR A 334      36.256   6.140  24.053  1.00 17.70           N  
ATOM   2629  CA  THR A 334      36.842   6.830  25.191  1.00 19.43           C  
ATOM   2630  C   THR A 334      38.304   6.428  25.365  1.00 19.23           C  
ATOM   2631  O   THR A 334      38.631   5.243  25.337  1.00 21.63           O  
ATOM   2632  CB  THR A 334      36.078   6.494  26.485  1.00 19.76           C  
ATOM   2633  OG1 THR A 334      34.702   6.864  26.337  1.00 22.07           O  
ATOM   2634  CG2 THR A 334      36.672   7.241  27.669  1.00 22.43           C  
ATOM   2635  N   LEU A 335      39.181   7.417  25.525  1.00 18.89           N  
ATOM   2636  CA  LEU A 335      40.603   7.154  25.738  1.00 20.19           C  
ATOM   2637  C   LEU A 335      40.827   7.067  27.242  1.00 20.45           C  
ATOM   2638  O   LEU A 335      41.585   6.224  27.722  1.00 20.35           O  
ATOM   2639  CB  LEU A 335      41.466   8.284  25.165  1.00 20.17           C  
ATOM   2640  CG  LEU A 335      41.569   8.444  23.645  1.00 20.84           C  
ATOM   2641  CD1 LEU A 335      42.232   7.226  23.032  1.00 22.11           C  
ATOM   2642  CD2 LEU A 335      40.188   8.650  23.067  1.00 24.18           C  
ATOM   2643  N   GLN A 336      40.158   7.959  27.971  1.00 20.75           N  
ATOM   2644  CA  GLN A 336      40.232   8.018  29.429  1.00 23.52           C  
ATOM   2645  C   GLN A 336      38.891   8.441  30.016  1.00 23.11           C  
ATOM   2646  O   GLN A 336      38.381   7.729  30.912  1.00 24.59           O  
ATOM   2647  CB  GLN A 336      41.314   9.003  29.890  1.00 25.34           C  
ATOM   2648  CG  GLN A 336      42.701   8.392  29.957  1.00 29.02           C  
ATOM   2649  CD  GLN A 336      43.620   9.102  30.933  1.00 31.00           C  
ATOM   2650  OE1 GLN A 336      44.767   8.692  31.124  1.00 33.06           O  
ATOM   2651  NE2 GLN A 336      43.124  10.166  31.562  1.00 30.95           N  
TER    2652      GLN A 336                                                      
HETATM 2653 CA    CA A2001      51.765  18.746   9.412  1.00  9.83          CA  
HETATM 2654 CA    CA A2002      54.013  20.302  11.373  1.00  0.34          CA  
HETATM 2655  C   ACY A1001      55.285  18.175   8.811  1.00 25.51           C  
HETATM 2656  O   ACY A1001      54.155  18.468   8.226  1.00 24.99           O  
HETATM 2657  OXT ACY A1001      55.566  17.043   9.187  1.00 24.88           O  
HETATM 2658  CH3 ACY A1001      56.234  19.329   9.005  1.00 24.26           C  
HETATM 2659  O   HOH A 401      34.546  26.185  -0.028  1.00 17.57           O  
HETATM 2660  O   HOH A 402      35.818  27.317   2.119  1.00 10.17           O  
HETATM 2661  O   HOH A 403      30.929  30.198   0.292  1.00 20.23           O  
HETATM 2662  O   HOH A 404      60.069  17.111   9.121  1.00 20.89           O  
HETATM 2663  O   HOH A 405      47.720  24.394 -12.258  1.00 28.46           O  
HETATM 2664  O   HOH A 406      44.938  20.802  -8.612  1.00 28.49           O  
HETATM 2665  O   HOH A 407      40.687  25.615  -5.187  1.00  7.64           O  
HETATM 2666  O   HOH A 408      42.749  26.411  -2.562  1.00  3.71           O  
HETATM 2667  O   HOH A 409      46.953  28.311  -1.088  1.00  5.10           O  
HETATM 2668  O   HOH A 410      40.139  28.484  -3.001  1.00  3.61           O  
HETATM 2669  O   HOH A 411      43.458  33.443   0.501  1.00  3.79           O  
HETATM 2670  O   HOH A 412      43.420  37.179   2.133  1.00  4.93           O  
HETATM 2671  O   HOH A 413      68.621   4.364  21.824  1.00  6.10           O  
HETATM 2672  O   HOH A 414      38.015  41.347 -13.038  1.00  5.12           O  
HETATM 2673  O   HOH A 415      35.274  42.772 -11.317  1.00 13.35           O  
HETATM 2674  O   HOH A 416      32.788  43.409 -10.420  1.00 12.54           O  
HETATM 2675  O   HOH A 417      33.958  40.304  -4.363  1.00 10.83           O  
HETATM 2676  O   HOH A 418      32.491  37.370   9.557  1.00 25.50           O  
HETATM 2677  O   HOH A 419      35.812  45.851  16.216  1.00 34.44           O  
HETATM 2678  O   HOH A 420      33.393  47.438  15.415  1.00 29.51           O  
HETATM 2679  O   HOH A 421      36.421  32.179  17.432  1.00  5.81           O  
HETATM 2680  O   HOH A 422      41.904  31.741  17.051  1.00  4.08           O  
HETATM 2681  O   HOH A 423      42.790  36.079  16.461  1.00  6.96           O  
HETATM 2682  O   HOH A 424      44.263  35.440  18.683  1.00  7.87           O  
HETATM 2683  O   HOH A 425      44.834  39.469  23.906  1.00 14.33           O  
HETATM 2684  O   HOH A 426      51.506  39.975  20.445  1.00 17.46           O  
HETATM 2685  O   HOH A 427      47.752  36.396  23.452  1.00 36.34           O  
HETATM 2686  O   HOH A 428      32.447  26.627  28.866  1.00 13.81           O  
HETATM 2687  O   HOH A 429      32.426  24.931  26.434  1.00 11.41           O  
HETATM 2688  O   HOH A 430      45.125  22.098  10.354  1.00  4.11           O  
HETATM 2689  O   HOH A 431      43.111  15.339  13.329  1.00  3.33           O  
HETATM 2690  O   HOH A 432      45.470  15.131  10.905  1.00  8.98           O  
HETATM 2691  O   HOH A 433      47.752  15.202   8.604  1.00  3.97           O  
HETATM 2692  O   HOH A 434      40.080  16.797   1.125  1.00  7.74           O  
HETATM 2693  O   HOH A 435      30.042  13.803   6.658  1.00 13.82           O  
HETATM 2694  O   HOH A 436      50.116  25.493   0.898  1.00  3.89           O  
HETATM 2695  O   HOH A 437      49.460  23.178  -0.581  1.00  6.20           O  
HETATM 2696  O   HOH A 438      45.705  16.660  -2.698  1.00 15.14           O  
HETATM 2697  O   HOH A 439      45.391  31.292  18.140  1.00  5.88           O  
HETATM 2698  O   HOH A 440      53.869  31.271  15.136  1.00  6.61           O  
HETATM 2699  O   HOH A 441      51.657  33.347  18.308  1.00  2.61           O  
HETATM 2700  O   HOH A 442      59.300  27.609  11.697  1.00 10.92           O  
HETATM 2701  O   HOH A 443      54.022  36.434   4.292  1.00  9.30           O  
HETATM 2702  O   HOH A 444      54.006  40.952   5.282  1.00  8.85           O  
HETATM 2703  O   HOH A 445      56.216  25.010   2.259  1.00  8.47           O  
HETATM 2704  O   HOH A 446      55.752  24.330  -7.901  1.00  9.59           O  
HETATM 2705  O   HOH A 447      46.014  42.102 -12.517  1.00  8.36           O  
HETATM 2706  O   HOH A 448      55.983  31.404  -4.968  1.00 13.27           O  
HETATM 2707  O   HOH A 449      51.628  39.902   1.275  1.00 25.34           O  
HETATM 2708  O   HOH A 450      43.695  31.716  21.508  1.00 10.30           O  
HETATM 2709  O   HOH A 451      41.167  21.687  27.495  1.00  6.47           O  
HETATM 2710  O   HOH A 452      39.530  20.383  29.049  1.00 12.95           O  
HETATM 2711  O   HOH A 453      40.360  18.571  31.054  1.00 12.32           O  
HETATM 2712  O   HOH A 454      51.597  25.546  17.559  1.00  7.36           O  
HETATM 2713  O   HOH A 455      56.653  16.262  20.331  1.00 13.12           O  
HETATM 2714  O   HOH A 456      54.673  16.478  17.241  1.00  6.01           O  
HETATM 2715  O   HOH A 457      59.690  23.018  22.275  1.00  6.96           O  
HETATM 2716  O   HOH A 458      56.233  28.468  31.035  1.00 11.98           O  
HETATM 2717  O   HOH A 459      55.370  40.049  12.281  1.00 29.96           O  
HETATM 2718  O   HOH A 460      68.952  28.618  20.099  1.00 24.84           O  
HETATM 2719  O   HOH A 461      59.701  25.238  16.696  1.00  6.92           O  
HETATM 2720  O   HOH A 462      56.752   8.058  22.134  1.00 17.86           O  
HETATM 2721  O   HOH A 463      60.123  11.632  17.122  1.00 16.03           O  
HETATM 2722  O   HOH A 464      54.984   8.520  15.566  1.00 16.81           O  
HETATM 2723  O   HOH A 465      63.413  11.591  28.704  1.00 22.91           O  
HETATM 2724  O   HOH A 466      59.690  13.375  36.535  1.00 19.50           O  
HETATM 2725  O   HOH A 467      50.064  14.018  16.370  1.00  4.85           O  
HETATM 2726  O   HOH A 468      49.843   5.965  14.541  1.00  9.14           O  
HETATM 2727  O   HOH A 469      38.541   7.131  11.867  1.00  8.99           O  
HETATM 2728  O   HOH A 470      45.373   5.708  22.334  1.00  7.61           O  
HETATM 2729  O   HOH A 471      50.969   4.284  28.121  1.00 19.73           O  
HETATM 2730  O   HOH A 472      43.804  10.303   5.203  1.00  9.23           O  
HETATM 2731  O   HOH A 473      36.655  20.138  28.679  1.00  9.35           O  
HETATM 2732  O   HOH A 474      39.987  23.772  -9.372  1.00 17.68           O  
HETATM 2733  O   HOH A 475      41.694  47.089  -1.858  1.00 21.34           O  
HETATM 2734  O   HOH A 476      26.216  38.200 -10.815  1.00 33.60           O  
HETATM 2735  O   HOH A 477      31.283  31.727 -10.443  1.00 32.97           O  
HETATM 2736  O   HOH A 478      44.194  27.097  31.961  1.00 17.07           O  
HETATM 2737  O   HOH A 479      33.427  16.972   2.429  1.00 18.19           O  
HETATM 2738  O   HOH A 480      26.261  26.295  17.902  1.00  9.69           O  
HETATM 2739  O   HOH A 481      39.354  47.182  -5.605  1.00 18.56           O  
HETATM 2740  O   HOH A 482      35.808  25.216 -20.646  1.00 35.61           O  
HETATM 2741  O   HOH A 483      35.977  33.749   0.572  1.00 11.52           O  
HETATM 2742  O   HOH A 484      45.215  35.471   1.037  1.00  5.55           O  
HETATM 2743  O   HOH A 485      46.166  28.746  -8.060  1.00 10.55           O  
HETATM 2744  O   HOH A 486      37.409  22.121  -3.501  1.00 19.25           O  
HETATM 2745  O   HOH A 487      30.962  27.406  -2.198  1.00 26.36           O  
HETATM 2746  O   HOH A 488      41.040  39.980  23.643  1.00 18.93           O  
HETATM 2747  O   HOH A 489      40.866  33.783  29.402  1.00  7.70           O  
HETATM 2748  O   HOH A 490      39.470  32.184  31.170  1.00  9.00           O  
HETATM 2749  O   HOH A 491      33.577  23.609  33.754  1.00 28.71           O  
HETATM 2750  O   HOH A 492      47.326  16.912   1.848  1.00  5.36           O  
HETATM 2751  O   HOH A 493      30.518  17.513  23.124  1.00 32.26           O  
HETATM 2752  O   HOH A 494      27.287  30.956  15.182  1.00 12.32           O  
HETATM 2753  O   HOH A 495      36.660  34.307  19.417  1.00 13.07           O  
HETATM 2754  O   HOH A 496      33.182  33.623  22.579  1.00 10.22           O  
HETATM 2755  O   HOH A 497      60.950  27.378  -0.683  1.00 14.75           O  
HETATM 2756  O   HOH A 498      50.521  34.609  14.674  1.00  4.95           O  
HETATM 2757  O   HOH A 499      60.086  23.697  36.409  1.00 24.92           O  
HETATM 2758  O   HOH A 500      53.608  29.739  30.693  1.00  9.72           O  
HETATM 2759  O   HOH A 501      61.648  41.922  16.017  1.00 30.64           O  
HETATM 2760  O   HOH A 502      58.396  32.200   9.706  1.00 20.99           O  
HETATM 2761  O   HOH A 503      62.340  16.858  17.485  1.00 14.05           O  
HETATM 2762  O   HOH A 504      63.100   8.004  17.934  1.00 19.86           O  
HETATM 2763  O   HOH A 505      56.121  15.217  41.393  1.00 33.29           O  
HETATM 2764  O   HOH A 506      48.670   6.214  26.633  1.00 17.18           O  
HETATM 2765  O   HOH A 507      40.713   7.678  10.340  1.00 23.34           O  
HETATM 2766  O   HOH A 508      37.446  50.564  -4.206  1.00 31.73           O  
HETATM 2767  O   HOH A 509      46.798  38.279 -14.821  1.00 29.41           O  
HETATM 2768  O   HOH A 510      26.129  33.034 -11.846  1.00 34.17           O  
HETATM 2769  O   HOH A 511      36.681  25.578  -4.231  1.00 22.08           O  
HETATM 2770  O   HOH A 512      33.853  31.369   4.209  1.00 22.79           O  
HETATM 2771  O   HOH A 513      43.325  32.933  19.163  1.00 13.14           O  
HETATM 2772  O   HOH A 514      33.273  18.853   0.483  1.00 29.58           O  
HETATM 2773  O   HOH A 515      35.802  10.976   2.461  1.00 12.37           O  
HETATM 2774  O   HOH A 516      34.700  11.527  -1.168  1.00 14.59           O  
HETATM 2775  O   HOH A 517      36.595  13.144   0.155  1.00 21.93           O  
HETATM 2776  O   HOH A 518      32.689   8.908   7.414  1.00  9.01           O  
HETATM 2777  O   HOH A 519      33.147  29.361  25.702  1.00 22.67           O  
HETATM 2778  O   HOH A 520      51.450  18.141  -2.974  1.00 15.34           O  
HETATM 2779  O   HOH A 521      53.432  19.584  -1.833  1.00 21.18           O  
HETATM 2780  O   HOH A 522      39.647  34.963  16.599  1.00 14.17           O  
HETATM 2781  O   HOH A 523      53.140  33.867  14.330  1.00 11.41           O  
HETATM 2782  O   HOH A 524      57.804  36.416   3.362  1.00 26.38           O  
HETATM 2783  O   HOH A 525      63.909  29.626   3.647  1.00 28.67           O  
HETATM 2784  O   HOH A 526      59.162  33.574  -2.223  1.00 13.13           O  
HETATM 2785  O   HOH A 527      54.366  25.012  -5.350  1.00 26.56           O  
HETATM 2786  O   HOH A 528      38.178  42.196   8.012  1.00 14.13           O  
HETATM 2787  O   HOH A 529      46.951  41.163  12.216  1.00 12.05           O  
HETATM 2788  O   HOH A 530      49.943  40.754  15.425  1.00 22.72           O  
HETATM 2789  O   HOH A 531      39.333  25.296  34.604  1.00 14.52           O  
HETATM 2790  O   HOH A 532      62.946  17.722  25.828  1.00 17.62           O  
HETATM 2791  O   HOH A 533      61.869  39.826   6.374  1.00 27.99           O  
HETATM 2792  O   HOH A 534      64.763  24.679  18.167  1.00 19.58           O  
HETATM 2793  O   HOH A 535      61.981  18.659  14.656  1.00 17.84           O  
HETATM 2794  O   HOH A 536      59.915   7.308  32.750  1.00 14.26           O  
HETATM 2795  O   HOH A 537      47.781  13.170  33.494  1.00 17.30           O  
HETATM 2796  O   HOH A 538      53.155   5.304  25.740  1.00 20.94           O  
HETATM 2797  O   HOH A 539      42.968   8.897  11.283  1.00 19.71           O  
HETATM 2798  O   HOH A 540      33.996   2.972  16.839  1.00 19.65           O  
HETATM 2799  O   HOH A 541      30.084   5.938  19.393  1.00 16.86           O  
HETATM 2800  O   HOH A 542      41.455  23.711  34.620  1.00 30.73           O  
HETATM 2801  O   HOH A 543      35.650  46.578  -9.262  1.00 13.38           O  
HETATM 2802  O   HOH A 544      33.592  48.361  -9.481  1.00 21.26           O  
HETATM 2803  O   HOH A 545      35.255  20.376  -2.558  1.00 16.86           O  
HETATM 2804  O   HOH A 546      31.037  17.104   3.248  1.00 26.37           O  
HETATM 2805  O   HOH A 547      48.849  15.404  -0.350  1.00 33.22           O  
HETATM 2806  O   HOH A 548      17.403  28.223  17.956  1.00 36.81           O  
HETATM 2807  O   HOH A 549      25.712  28.637  30.308  1.00 38.95           O  
HETATM 2808  O   HOH A 550      61.264  32.502  -0.324  1.00 23.97           O  
HETATM 2809  O   HOH A 551      66.136  31.392  -4.744  1.00 18.56           O  
HETATM 2810  O   HOH A 552      59.188  37.487  -1.101  1.00 22.88           O  
HETATM 2811  O   HOH A 553      50.422  25.254 -11.438  1.00 12.73           O  
HETATM 2812  O   HOH A 554      56.656  36.657  -7.967  1.00 38.36           O  
HETATM 2813  O   HOH A 555      55.115  37.628  29.573  1.00 22.83           O  
HETATM 2814  O   HOH A 556      34.011  44.788  -8.257  1.00 14.01           O  
HETATM 2815  O   HOH A 557      49.403   4.619  21.695  1.00 19.09           O  
HETATM 2816  O   HOH A 558      53.506   3.376  29.098  1.00 20.56           O  
HETATM 2817  O   HOH A 559      46.975   6.598   7.267  1.00 35.91           O  
HETATM 2818  O   HOH A 560      43.788   9.138   8.394  1.00 13.83           O  
HETATM 2819  O   HOH A 561      36.759  17.998  30.663  1.00 20.00           O  
HETATM 2820  O   HOH A 562      32.911   7.348  23.544  1.00 24.64           O  
HETATM 2821  O   HOH A 563      37.729  22.853 -11.731  1.00 31.94           O  
HETATM 2822  O   HOH A 564      35.915  45.648   2.195  1.00 17.26           O  
HETATM 2823  O   HOH A 565      37.554  44.873   7.215  1.00 19.03           O  
HETATM 2824  O   HOH A 566      38.294  54.274   7.020  1.00 39.03           O  
HETATM 2825  O   HOH A 567      35.570  56.633   6.554  1.00 33.30           O  
HETATM 2826  O   HOH A 568      39.166  56.784   7.447  1.00 39.72           O  
HETATM 2827  O   HOH A 569      31.557  45.605  -7.407  1.00 17.75           O  
HETATM 2828  O   HOH A 570      31.883  48.747   1.085  1.00 32.05           O  
HETATM 2829  O   HOH A 571      49.098  41.894  -6.112  1.00 19.41           O  
HETATM 2830  O   HOH A 572      47.559  43.733  -4.725  1.00 28.35           O  
HETATM 2831  O   HOH A 573      28.788  32.143 -14.267  1.00 25.30           O  
HETATM 2832  O   HOH A 574      29.497  29.656 -15.637  1.00 29.18           O  
HETATM 2833  O   HOH A 575      32.807  29.453 -16.425  1.00 28.18           O  
HETATM 2834  O   HOH A 576      32.812  28.718 -13.838  1.00 25.50           O  
HETATM 2835  O   HOH A 577      34.865  26.134 -16.996  1.00 20.05           O  
HETATM 2836  O   HOH A 578      34.685  23.737 -18.684  1.00 33.39           O  
HETATM 2837  O   HOH A 579      47.996  44.352 -12.687  1.00 12.72           O  
HETATM 2838  O   HOH A 580      46.073  40.940 -14.913  1.00 14.79           O  
HETATM 2839  O   HOH A 581      48.007  40.634 -11.496  1.00 11.15           O  
HETATM 2840  O   HOH A 582      49.664  39.316 -18.048  1.00 14.28           O  
HETATM 2841  O   HOH A 583      48.166  37.530 -16.917  1.00 18.87           O  
HETATM 2842  O   HOH A 584      50.043  35.464 -16.666  1.00 23.14           O  
HETATM 2843  O   HOH A 585      45.877  35.968 -18.320  1.00 28.12           O  
HETATM 2844  O   HOH A 586      48.210  42.123 -16.364  1.00 21.38           O  
HETATM 2845  O   HOH A 587      49.211  41.725 -18.700  1.00 16.56           O  
HETATM 2846  O   HOH A 588      52.279  38.246 -18.843  1.00 22.52           O  
HETATM 2847  O   HOH A 589      53.178  41.242 -18.155  1.00 17.31           O  
HETATM 2848  O   HOH A 590      30.700  43.136  -6.503  1.00 21.60           O  
HETATM 2849  O   HOH A 591      31.783  41.485  -8.834  1.00 27.55           O  
HETATM 2850  O   HOH A 592      32.554  42.600  -4.813  1.00 24.46           O  
HETATM 2851  O   HOH A 593      31.197  42.494  -2.527  1.00 18.76           O  
HETATM 2852  O   HOH A 594      21.126  43.637   1.687  1.00 32.28           O  
HETATM 2853  O   HOH A 595      22.411  42.597   5.744  1.00 36.49           O  
HETATM 2854  O   HOH A 596      29.162  34.758   2.355  1.00 30.27           O  
HETATM 2855  O   HOH A 597      30.903  34.184   6.018  1.00 18.32           O  
HETATM 2856  O   HOH A 598      34.017  28.411   3.723  1.00 15.31           O  
HETATM 2857  O   HOH A 599      28.290  35.243  -6.366  1.00 33.52           O  
HETATM 2858  O   HOH A 600      31.359  23.031   1.392  1.00 18.14           O  
HETATM 2859  O   HOH A 601      31.688  20.886  -0.154  1.00 25.22           O  
HETATM 2860  O   HOH A 602      32.838  21.404  -2.717  1.00 29.95           O  
HETATM 2861  O   HOH A 603      38.063  36.298  18.480  1.00 11.44           O  
HETATM 2862  O   HOH A 604      45.156  42.301  15.833  1.00 10.47           O  
HETATM 2863  O   HOH A 605      44.822  42.878  11.529  1.00 22.86           O  
HETATM 2864  O   HOH A 606      40.414  44.840   9.124  1.00 21.63           O  
HETATM 2865  O   HOH A 607      39.576  47.271  13.971  1.00 37.00           O  
HETATM 2866  O   HOH A 608      49.483  42.250  10.347  1.00 28.94           O  
HETATM 2867  O   HOH A 609      48.020  44.450  13.473  1.00 19.91           O  
HETATM 2868  O   HOH A 610      38.109  22.676  33.999  1.00 26.91           O  
HETATM 2869  O   HOH A 611      37.857  18.307  37.499  1.00 32.46           O  
HETATM 2870  O   HOH A 612      39.904  20.480  34.183  1.00 24.61           O  
HETATM 2871  O   HOH A 613      35.156  30.341  31.470  1.00 23.82           O  
HETATM 2872  O   HOH A 614      36.111  23.102  32.291  1.00 26.85           O  
HETATM 2873  O   HOH A 615      33.061  19.372  30.775  1.00 16.81           O  
HETATM 2874  O   HOH A 616      29.664  24.254  26.376  1.00 13.49           O  
HETATM 2875  O   HOH A 617      28.557  22.106  27.427  1.00 22.47           O  
HETATM 2876  O   HOH A 618      27.668  24.821  24.396  1.00 14.29           O  
HETATM 2877  O   HOH A 619      27.026  21.290  25.142  1.00 22.87           O  
HETATM 2878  O   HOH A 620      32.000  13.014   2.741  1.00 11.14           O  
HETATM 2879  O   HOH A 621      30.070  14.893   4.294  1.00 16.30           O  
HETATM 2880  O   HOH A 622      30.349  11.312   4.564  1.00 17.92           O  
HETATM 2881  O   HOH A 623      33.466   9.324   2.880  1.00 14.57           O  
HETATM 2882  O   HOH A 624      31.773   9.214   4.987  1.00  9.73           O  
HETATM 2883  O   HOH A 625      30.442   6.562   4.598  1.00 14.98           O  
HETATM 2884  O   HOH A 626      31.598   5.318   6.656  1.00 27.63           O  
HETATM 2885  O   HOH A 627      33.960   6.584   7.068  1.00 13.86           O  
HETATM 2886  O   HOH A 628      35.872   5.617   8.461  1.00 18.05           O  
HETATM 2887  O   HOH A 629      38.143   5.843   7.402  1.00 20.77           O  
HETATM 2888  O   HOH A 630      55.041  29.030 -13.163  1.00 33.29           O  
HETATM 2889  O   HOH A 631      26.516  13.633  12.025  1.00 13.86           O  
HETATM 2890  O   HOH A 632      23.049  11.595  13.344  1.00 13.82           O  
HETATM 2891  O   HOH A 633      25.655  20.017  16.708  1.00 20.99           O  
HETATM 2892  O   HOH A 634      24.549  25.608  13.763  1.00 18.89           O  
HETATM 2893  O   HOH A 635      30.921  14.520  18.456  1.00 22.79           O  
HETATM 2894  O   HOH A 636      23.628  27.642  14.942  1.00 23.29           O  
HETATM 2895  O   HOH A 637      26.989  28.951  13.060  1.00 12.87           O  
HETATM 2896  O   HOH A 638      24.483  29.071  12.084  1.00 22.18           O  
HETATM 2897  O   HOH A 639      23.262  26.883   9.316  1.00 26.17           O  
HETATM 2898  O   HOH A 640      20.751  17.718   9.892  1.00 21.60           O  
HETATM 2899  O   HOH A 641      29.306  19.586   1.178  1.00 16.79           O  
HETATM 2900  O   HOH A 642      29.682  23.274   3.951  1.00 24.90           O  
HETATM 2901  O   HOH A 643      32.702  26.069   3.889  1.00 24.66           O  
HETATM 2902  O   HOH A 644      31.020  25.569   5.703  1.00 27.90           O  
HETATM 2903  O   HOH A 645      27.561  21.486   4.115  1.00 26.26           O  
HETATM 2904  O   HOH A 646      29.024  27.210   5.319  1.00 19.15           O  
HETATM 2905  O   HOH A 647      41.065  22.596  -5.074  1.00 11.33           O  
HETATM 2906  O   HOH A 648      41.558  21.117  -7.257  1.00 29.81           O  
HETATM 2907  O   HOH A 649      26.457  33.309  13.057  1.00 20.62           O  
HETATM 2908  O   HOH A 650      26.690  34.349  23.881  1.00 31.61           O  
HETATM 2909  O   HOH A 651      25.616  29.144  21.583  1.00 19.95           O  
HETATM 2910  O   HOH A 652      25.399  33.580  21.631  1.00 35.07           O  
HETATM 2911  O   HOH A 653      23.625  34.671  18.827  1.00 33.83           O  
HETATM 2912  O   HOH A 654      24.625  27.429  23.637  1.00 30.24           O  
HETATM 2913  O   HOH A 655      63.178  29.593   0.778  1.00 32.19           O  
HETATM 2914  O   HOH A 656      65.149  31.029  -0.438  1.00 29.67           O  
HETATM 2915  O   HOH A 657      66.059  28.816  -1.895  1.00 17.79           O  
HETATM 2916  O   HOH A 658      63.632  32.019  -4.566  1.00 23.62           O  
HETATM 2917  O   HOH A 659      53.217  27.397  -5.613  1.00 30.92           O  
HETATM 2918  O   HOH A 660      55.409  28.755  -4.904  1.00 16.08           O  
HETATM 2919  O   HOH A 661      55.425  39.138   4.269  1.00 13.64           O  
HETATM 2920  O   HOH A 662      63.533  14.905  23.428  1.00 24.95           O  
HETATM 2921  O   HOH A 663      65.496  20.392  25.239  1.00 21.46           O  
HETATM 2922  O   HOH A 664      65.166  22.436  31.294  1.00 17.73           O  
HETATM 2923  O   HOH A 665      66.007  23.750  33.425  1.00 24.14           O  
HETATM 2924  O   HOH A 666      54.986  27.654  33.205  1.00 19.98           O  
HETATM 2925  O   HOH A 667      53.952  40.520  19.238  1.00 12.08           O  
HETATM 2926  O   HOH A 668      55.559  41.771  20.693  1.00 20.47           O  
HETATM 2927  O   HOH A 669      57.669  38.709  23.993  1.00 16.03           O  
HETATM 2928  O   HOH A 670      49.882  36.031  24.669  1.00 27.84           O  
HETATM 2929  O   HOH A 671      57.791  39.827  11.755  1.00 22.86           O  
HETATM 2930  O   HOH A 672      63.733  39.102  14.012  1.00 18.17           O  
HETATM 2931  O   HOH A 673      70.970  35.940  20.576  1.00 26.98           O  
HETATM 2932  O   HOH A 674      67.822  34.908  24.961  1.00 22.66           O  
HETATM 2933  O   HOH A 675      66.641  32.678  26.027  1.00 24.39           O  
HETATM 2934  O   HOH A 676      67.065  26.296  18.201  1.00 27.83           O  
HETATM 2935  O   HOH A 677      68.055  26.277  20.644  1.00 22.04           O  
HETATM 2936  O   HOH A 678      64.251  37.395  21.340  1.00 22.54           O  
HETATM 2937  O   HOH A 679      71.758  31.986  17.512  1.00 20.83           O  
HETATM 2938  O   HOH A 680      61.629  26.844   7.574  1.00 13.55           O  
HETATM 2939  O   HOH A 681      63.184  24.748   9.375  1.00 22.38           O  
HETATM 2940  O   HOH A 682      66.369  24.944  10.473  1.00 37.34           O  
HETATM 2941  O   HOH A 683      63.246  22.360   7.682  1.00 18.43           O  
HETATM 2942  O   HOH A 684      68.396  26.445  13.996  1.00 28.39           O  
HETATM 2943  O   HOH A 685      63.131  23.408  11.876  1.00 23.96           O  
HETATM 2944  O   HOH A 686      67.044  24.417  16.441  1.00 43.05           O  
HETATM 2945  O   HOH A 687      64.577  18.313  19.011  1.00 22.12           O  
HETATM 2946  O   HOH A 688      67.980  18.683  22.128  1.00 30.35           O  
HETATM 2947  O   HOH A 689      58.284  12.530  11.830  1.00 25.88           O  
HETATM 2948  O   HOH A 690      61.223  12.395  13.325  1.00 35.41           O  
HETATM 2949  O   HOH A 691      64.474   5.861  31.852  1.00 17.92           O  
HETATM 2950  O   HOH A 692      62.783   7.595  33.430  1.00 25.77           O  
HETATM 2951  O   HOH A 693      58.094  11.429  37.107  1.00 18.68           O  
HETATM 2952  O   HOH A 694      58.882   7.290  35.069  1.00 30.49           O  
HETATM 2953  O   HOH A 695      57.484  17.577  38.547  1.00 30.12           O  
HETATM 2954  O   HOH A 696      62.034  12.431  37.571  1.00 24.67           O  
HETATM 2955  O   HOH A 697      59.122  20.619  36.483  1.00 28.42           O  
HETATM 2956  O   HOH A 698      63.809  19.284  37.380  1.00 33.55           O  
HETATM 2957  O   HOH A 699      64.749  15.268  36.902  1.00 32.66           O  
HETATM 2958  O   HOH A 700      50.784  19.816  38.037  1.00 34.41           O  
HETATM 2959  O   HOH A 701      47.326  10.641  32.740  1.00 25.22           O  
HETATM 2960  O   HOH A 702      43.510  13.459  33.652  1.00 26.81           O  
HETATM 2961  O   HOH A 703      45.637  13.308  35.131  1.00 29.45           O  
HETATM 2962  O   HOH A 704      48.900   3.525  15.439  1.00 28.61           O  
HETATM 2963  O   HOH A 705      51.140   4.657  19.656  1.00 17.44           O  
HETATM 2964  O   HOH A 706      63.514  39.319  19.796  1.00 27.11           O  
HETATM 2965  O   HOH A 707      44.708   5.626  24.982  1.00 15.67           O  
HETATM 2966  O   HOH A 708      55.224   5.054  30.180  1.00 20.29           O  
HETATM 2967  O   HOH A 709      58.240   6.211  29.446  1.00 30.06           O  
HETATM 2968  O   HOH A 710      57.715   4.517  27.481  1.00 23.87           O  
HETATM 2969  O   HOH A 711      51.501  13.204   2.865  1.00 26.59           O  
HETATM 2970  O   HOH A 712      42.251   6.507   6.234  1.00 28.24           O  
HETATM 2971  O   HOH A 713      38.787  11.087   0.079  1.00 26.51           O  
HETATM 2972  O   HOH A 714      35.218   2.778   8.681  1.00 16.79           O  
HETATM 2973  O   HOH A 715      36.332   5.670  11.139  1.00 12.74           O  
HETATM 2974  O   HOH A 716      36.719   3.252  11.908  1.00 16.81           O  
HETATM 2975  O   HOH A 717      38.957  16.217  29.701  1.00 20.31           O  
HETATM 2976  O   HOH A 718      32.566  13.397  28.191  1.00 20.62           O  
HETATM 2977  O   HOH A 719      28.216  14.106  18.944  1.00 32.93           O  
HETATM 2978  O   HOH A 720      26.861  16.403  19.508  1.00 23.26           O  
HETATM 2979  O   HOH A 721      43.208   3.832  12.100  1.00 21.00           O  
HETATM 2980  O   HOH A 722      45.143   2.472  13.491  1.00 32.92           O  
HETATM 2981  O   HOH A 723      33.599   4.340  24.834  1.00 27.46           O  
HETATM 2982  O   HOH A 724      51.322  39.688 -15.451  1.00 28.39           O  
HETATM 2983  O   HOH A 725      59.810  28.566   9.231  1.00 17.73           O  
HETATM 2984  O   HOH A 726      59.828  30.525   6.357  1.00 18.79           O  
HETATM 2985  O   HOH A 727      62.227  30.689   5.618  1.00 32.04           O  
HETATM 2986  O   HOH A 728      52.785  20.065  -5.533  1.00 30.70           O  
HETATM 2987  O   HOH A 729      50.294  22.202 -14.325  1.00 33.70           O  
HETATM 2988  O   HOH A 730      51.722  29.533 -13.742  1.00 25.99           O  
HETATM 2989  O   HOH A 731      49.073  30.860 -14.555  1.00 24.38           O  
HETATM 2990  O   HOH A 732      57.886  37.979 -11.338  1.00 35.16           O  
HETATM 2991  O   HOH A 733      56.221  42.767 -11.399  1.00 29.70           O  
HETATM 2992  O   HOH A 734      55.019  35.552  -9.773  1.00 29.13           O  
HETATM 2993  O   HOH A 735      60.619  35.767  -2.935  1.00 25.73           O  
HETATM 2994  O   HOH A 736      58.371  39.827  -3.007  1.00 31.91           O  
HETATM 2995  O   HOH A 737      47.455  41.366  14.829  1.00 20.53           O  
HETATM 2996  O   HOH A 738      41.387  16.136  33.237  1.00 32.09           O  
HETATM 2997  O   HOH A 739      63.440  33.585  27.320  1.00 25.88           O  
HETATM 2998  O   HOH A 740      57.621  43.351  19.438  1.00 13.28           O  
HETATM 2999  O   HOH A 741      61.275  40.483  18.347  1.00 20.05           O  
HETATM 3000  O   HOH A 742      59.633  41.721  20.097  1.00 21.50           O  
HETATM 3001  O   HOH A 743      52.354   6.610  18.110  1.00 18.79           O  
HETATM 3002  O   HOH A 744      49.867   2.767  18.224  1.00 30.58           O  
HETATM 3003  O   HOH A 745      66.924  38.532  22.318  1.00 25.45           O  
HETATM 3004  O   HOH A 746      64.001  41.167  11.480  1.00 25.12           O  
HETATM 3005  O   HOH A 747      71.556  33.698  11.126  1.00 25.43           O  
HETATM 3006  O   HOH A 748      74.876  36.336  14.755  1.00 38.25           O  
HETATM 3007  O   HOH A 749      68.175  22.614  20.833  1.00 25.54           O  
HETATM 3008  O   HOH A 750      28.703  27.469  -7.412  1.00 23.35           O  
HETATM 3009  O   HOH A 751      43.357   5.667  19.995  1.00 12.24           O  
HETATM 3010  O   HOH A 752      34.231   6.931  31.327  1.00 28.08           O  
HETATM 3011  O   HOH A 753      36.115   9.037  32.843  1.00 25.82           O  
HETATM 3012  O   HOH A 754      33.534  29.551  33.214  1.00 38.26           O  
HETATM 3013  O   HOH A 755      36.965  31.092  29.977  1.00 32.69           O  
HETATM 3014  O   HOH A 756      28.390  19.041  21.902  1.00 22.61           O  
HETATM 3015  O   HOH A 757      54.717  13.143  10.647  1.00 12.67           O  
HETATM 3016  O   HOH A 758      53.767  15.296   8.887  1.00 15.38           O  
HETATM 3017  O   HOH A 759      54.753   9.581  12.220  1.00 29.42           O  
HETATM 3018  O   HOH A 760      34.602  25.744  -2.483  1.00 25.82           O  
HETATM 3019  O   HOH A 761      38.096  15.217  -2.191  1.00 27.18           O  
HETATM 3020  O   HOH A 762      35.336  13.654   2.140  1.00 25.93           O  
HETATM 3021  O   HOH A 763      28.175  12.024   3.731  1.00 15.08           O  
HETATM 3022  O   HOH A 764      24.796  28.395   5.034  1.00 28.88           O  
HETATM 3023  O   HOH A 765      30.594  16.290  20.768  1.00 27.53           O  
HETATM 3024  O   HOH A 766      29.216  17.744  18.915  1.00 26.74           O  
HETATM 3025  O   HOH A 767      21.485  20.706  11.436  1.00 25.02           O  
HETATM 3026  O   HOH A 768      31.325  27.741   8.646  1.00 15.98           O  
HETATM 3027  O   HOH A 769      30.248  32.302  26.168  1.00 25.56           O  
HETATM 3028  O   HOH A 770      33.848  33.331  25.119  1.00 35.10           O  
HETATM 3029  O   HOH A 771      59.980  37.109  -5.270  1.00 25.81           O  
HETATM 3030  O   HOH A 772      51.493  16.593   9.285  1.00  7.30           O  
HETATM 3031  O   HOH A 773      58.893  18.756   7.440  1.00 26.55           O  
HETATM 3032  O   HOH A 774      53.233  18.431  10.851  1.00 21.19           O  
HETATM 3033  O   HOH A 775      44.731   7.667   5.203  1.00 20.26           O  
HETATM 3034  O   HOH A 776      45.388   6.083   3.052  1.00 32.55           O  
HETATM 3035  O   HOH A 777      50.276   8.592   8.336  1.00 25.38           O  
HETATM 3036  O   HOH A 778      53.126  10.191   7.629  1.00 29.37           O  
HETATM 3037  O   HOH A 779      44.746   6.337   9.364  1.00 22.47           O  
HETATM 3038  O   HOH A 780      47.097  13.453  -0.392  1.00 37.40           O  
HETATM 3039  O   HOH A 781      48.171  16.107  -2.704  1.00 29.75           O  
HETATM 3040  O   HOH A 782      49.702  16.504  -4.733  1.00 28.12           O  
HETATM 3041  O   HOH A 783      33.712  22.296  -5.964  1.00 34.99           O  
HETATM 3042  O   HOH A 784      64.476  19.197   4.935  1.00 26.82           O  
HETATM 3043  O   HOH A 785      61.910  13.600  10.944  1.00 25.13           O  
HETATM 3044  O   HOH A 786      62.647  14.071  14.751  1.00 31.27           O  
HETATM 3045  O   HOH A 787      35.870  25.571  -6.747  1.00 26.04           O  
HETATM 3046  O   HOH A 788      29.528  31.104 -12.179  1.00 34.44           O  
HETATM 3047  O   HOH A 789      58.642  13.646   9.351  1.00 30.57           O  
HETATM 3048  O   HOH A 790      63.636  20.805  11.913  1.00 28.35           O  
HETATM 3049  O   HOH A 791      54.712  20.226  -3.936  1.00 38.13           O  
HETATM 3050  O   HOH A 792      56.205  22.352  -3.695  1.00 25.86           O  
HETATM 3051  O   HOH A 793      50.649  17.375 -18.882  1.00 30.98           O  
HETATM 3052  O   HOH A 794      46.712  24.252 -15.333  1.00 33.21           O  
HETATM 3053  O   HOH A 795      49.567  25.519 -15.953  1.00 31.98           O  
HETATM 3054  O   HOH A 796      51.960  43.407 -10.532  1.00 25.86           O  
HETATM 3055  O   HOH A 797      50.486  42.114 -12.495  1.00 26.93           O  
HETATM 3056  O   HOH A 798      61.178  35.980  -9.869  1.00 27.11           O  
HETATM 3057  O   HOH A 799      59.022  35.437  -8.121  1.00 33.47           O  
HETATM 3058  O   HOH A 800      57.281  39.532  -7.026  1.00 31.72           O  
HETATM 3059  O   HOH A 801      55.345  41.139  -7.036  1.00 29.32           O  
HETATM 3060  O   HOH A 802      29.414   6.854   8.604  1.00 23.25           O  
HETATM 3061  O   HOH A 803      62.846  31.493  -2.147  1.00 23.46           O  
HETATM 3062  O   HOH A 804      63.652  28.442   7.274  1.00 26.81           O  
HETATM 3063  O   HOH A 805      64.611  34.533   4.914  1.00 33.73           O  
HETATM 3064  O   HOH A 806      25.862  31.897  23.749  1.00 33.88           O  
HETATM 3065  O   HOH A 807      24.964  34.109  15.046  1.00 35.51           O  
HETATM 3066  O   HOH A 808      35.350  31.425  25.980  1.00 31.45           O  
HETATM 3067  O   HOH A 809      32.813  29.196  30.011  1.00 32.59           O  
HETATM 3068  O   HOH A 810      30.304  37.947  17.865  1.00 24.37           O  
HETATM 3069  O   HOH A 811      29.201  34.388  10.276  1.00 29.55           O  
HETATM 3070  O   HOH A 812      27.958  32.679   8.739  1.00 26.47           O  
HETATM 3071  O   HOH A 813      30.246  37.285  20.826  1.00 39.16           O  
HETATM 3072  O   HOH A 814      28.370  34.976   6.322  1.00 31.14           O  
HETATM 3073  O   HOH A 815      29.815  31.632   3.312  1.00 29.49           O  
HETATM 3074  O   HOH A 816      26.494  31.408   4.967  1.00 29.81           O  
HETATM 3075  O   HOH A 817      27.348  29.036   5.560  1.00 27.49           O  
HETATM 3076  O   HOH A 818      21.947  28.732   4.639  1.00 29.86           O  
HETATM 3077  O   HOH A 819      30.911  11.742  23.636  1.00 34.64           O  
HETATM 3078  O   HOH A 820      31.580  11.074  31.151  1.00 33.43           O  
HETATM 3079  O   HOH A 821      34.660  11.380  34.041  1.00 32.12           O  
HETATM 3080  O   HOH A 822      28.298   6.200  26.120  1.00 31.06           O  
HETATM 3081  O   HOH A 823      29.247   4.181  28.570  1.00 27.25           O  
HETATM 3082  O   HOH A 824      27.619   8.290  23.161  1.00 35.10           O  
HETATM 3083  O   HOH A 825      59.430  42.422   0.245  1.00 33.67           O  
HETATM 3084  O   HOH A 826      59.983   4.996  31.128  1.00 22.24           O  
HETATM 3085  O   HOH A 827      55.600   4.626  26.039  1.00 25.38           O  
HETATM 3086  O   HOH A 828      56.024   5.916  23.561  1.00 22.57           O  
HETATM 3087  O   HOH A 829      57.830  45.564  21.381  1.00 23.05           O  
HETATM 3088  O   HOH A 830      53.068  12.313  38.019  1.00 21.68           O  
HETATM 3089  O   HOH A 831      50.800  10.142  36.573  1.00 27.72           O  
HETATM 3090  O   HOH A 832      55.606  15.779  38.492  1.00 31.96           O  
HETATM 3091  O   HOH A 833      68.531  38.502  15.176  1.00 21.24           O  
HETATM 3092  O   HOH A 834      66.490   5.163  19.895  1.00 17.65           O  
HETATM 3093  O   HOH A 835      63.745  20.763  33.274  1.00 27.44           O  
HETATM 3094  O   HOH A 836      38.119  26.718  36.850  1.00 27.49           O  
HETATM 3095  O   HOH A 837      30.352  19.619  31.115  1.00 24.95           O  
HETATM 3096  O   HOH A 838      29.916  20.053  28.390  1.00 28.91           O  
HETATM 3097  O   HOH A 839      62.888  18.543  31.999  1.00 27.05           O  
HETATM 3098  O   HOH A 840      64.698  14.045  25.756  1.00 32.74           O  
HETATM 3099  O   HOH A 841      50.477  27.380  33.419  1.00 23.30           O  
HETATM 3100  O   HOH A 842      40.663  43.706  14.907  1.00 28.32           O  
HETATM 3101  O   HOH A 843      38.623   9.290  33.097  1.00 25.07           O  
HETATM 3102  O   HOH A 844      38.246  19.344  32.251  1.00 35.30           O  
HETATM 3103  O   HOH A 845      37.560  45.405   4.459  1.00 18.85           O  
HETATM 3104  O   HOH A 846      46.557  46.016   2.162  1.00 18.56           O  
HETATM 3105  O   HOH A 847      46.994  49.839   3.909  1.00 24.24           O  
CONECT  172  337                                                                
CONECT  337  172                                                                
CONECT  572 2653                                                                
CONECT  590 2653                                                                
CONECT  853 2653 2654                                                           
CONECT 1140 2654                                                                
CONECT 1624 2654                                                                
CONECT 2256 2654                                                                
CONECT 2653  572  590  853 2654                                                 
CONECT 2653 2656 3030 3032                                                      
CONECT 2654  853 1140 1624 2256                                                 
CONECT 2654 2653 3032                                                           
CONECT 2655 2656 2657 2658                                                      
CONECT 2656 2653 2655                                                           
CONECT 2657 2655                                                                
CONECT 2658 2655                                                                
CONECT 3030 2653                                                                
CONECT 3032 2653 2654                                                           
MASTER      323    0    3   15   17    0    7    6 3104    1   18   27          
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.