CNRS Nantes University US2B US2B
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***  1PC3  ***

elNémo ID: 240228061418940321

Job options:

ID        	=	 240228061418940321
JOBID     	=	 1PC3
USERID    	=	 unknown
PRIVAT    	=	 0

NMODES    	=	 10
DQMIN     	=	 -100
DQMAX     	=	 100
DQSTEP    	=	 20
DOGRAPHS  	=	 0

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 1PC3
HEADER    TRANSPORT PROTEIN                       15-MAY-03   1PC3              
TITLE     CRYSTAL STRUCTURE OF THE EXTRACELLULAR PHOSPHATE ABC TRANSPORT        
TITLE    2 RECEPTOR (PSTS-1) AND IMMUNODOMINANT ANTIGEN OF M. TUBERCULOSIS.     
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PHOSPHATE-BINDING PROTEIN 1;                               
COMPND   3 CHAIN: A, B;                                                         
COMPND   4 SYNONYM: PBP-1, PSTS-1, PROTEIN ANTIGEN B, PAB, ANTIGEN AG78;        
COMPND   5 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: MYCOBACTERIUM TUBERCULOSIS;                     
SOURCE   3 ORGANISM_TAXID: 83332;                                               
SOURCE   4 STRAIN: H37RV;                                                       
SOURCE   5 GENE: PSTS1 OR PHOS1 OR RV0934 OR MT0961 OR MTCY08D9.05C;            
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI K12;                             
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 83333;                                      
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: K12;                                       
SOURCE   9 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PETMPBP                                   
KEYWDS    PHOSPHATE TRANSPORT RECEPTOR, IMMONODOMINANT ANTIGEN, MYCOBACTERIUM   
KEYWDS   2 TUBERCULOSIS, ION-DIPOLE INTERACTIONS, ELECTROSTATICS, TRANSPORT     
KEYWDS   3 PROTEIN                                                              
EXPDTA    X-RAY DIFFRACTION                                                     
NUMMDL    2                                                                     
AUTHOR    N.K.VYAS,M.N.VYAS,F.A.QUIOCHO                                         
REVDAT   4   16-AUG-23 1PC3    1       REMARK                                   
REVDAT   3   13-JUL-11 1PC3    1       VERSN                                    
REVDAT   2   24-FEB-09 1PC3    1       VERSN                                    
REVDAT   1   18-MAY-04 1PC3    0                                                
JRNL        AUTH   N.K.VYAS,M.N.VYAS,F.A.QUIOCHO                                
JRNL        TITL   CRYSTAL STRUCTURE OF M TUBERCULOSIS ABC PHOSPHATE TRANSPORT  
JRNL        TITL 2 RECEPTOR: SPECIFICITY AND CHARGE COMPENSATION DOMINATED BY   
JRNL        TITL 3 ION-DIPOLE INTERACTIONS.                                     
JRNL        REF    STRUCTURE                     V.  11   765 2003              
JRNL        REFN                   ISSN 0969-2126                               
JRNL        PMID   12842040                                                     
JRNL        DOI    10.1016/S0969-2126(03)00109-6                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.16 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.0                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : ENGH & HUBER                                    
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.16                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 18.64                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : 3450257.470                    
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : 0.0000                         
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 86.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 31350                          
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) : 0.220                           
REMARK   3   FREE R VALUE                     : 0.264                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1595                            
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.007                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 6                            
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.16                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.30                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 79.40                        
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : 4518                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2650                       
REMARK   3   BIN FREE R VALUE                    : 0.2840                       
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : 4.90                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : 232                          
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : 0.019                        
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4848                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 10                                      
REMARK   3   SOLVENT ATOMS            : 240                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 3.50                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 11.30                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -4.75000                                             
REMARK   3    B22 (A**2) : -1.70000                                             
REMARK   3    B33 (A**2) : 6.45000                                              
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) : 0.26                            
REMARK   3   ESD FROM SIGMAA              (A) : 0.26                            
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) : 0.32                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : 0.29                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.005                           
REMARK   3   BOND ANGLES            (DEGREES) : 1.200                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : 23.70                           
REMARK   3   IMPROPER ANGLES        (DEGREES) : 0.870                           
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) : 0.790 ; 1.500                
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : 1.270 ; 2.000                
REMARK   3   SIDE-CHAIN BOND              (A**2) : 1.860 ; 2.000                
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : 2.540 ; 2.500                
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : FLAT MODEL                                           
REMARK   3   KSOL        : 0.27                                                 
REMARK   3   BSOL        : 46.16                                                
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  : ION.PARAM                                      
REMARK   3  PARAMETER FILE  3  : WATER.PARAM                                    
REMARK   3  PARAMETER FILE  4  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : PROTEIN.TOP                                    
REMARK   3  TOPOLOGY FILE  2   : ION.TOP                                        
REMARK   3  TOPOLOGY FILE  3   : WATER.TOP                                      
REMARK   3  TOPOLOGY FILE  4   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 1PC3 COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 20-MAY-03.                  
REMARK 100 THE DEPOSITION ID IS D_1000019225.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 08-SEP-93                          
REMARK 200  TEMPERATURE           (KELVIN) : 281                                
REMARK 200  PH                             : 5.6                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU RU200                       
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          : SDMS                               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : STRATEGY                           
REMARK 200  DATA SCALING SOFTWARE          : SDMS                               
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 32319                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.110                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 18.640                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 85.5                               
REMARK 200  DATA REDUNDANCY                : 2.000                              
REMARK 200  R MERGE                    (I) : 0.06540                            
REMARK 200  R SYM                      (I) : 0.06540                            
REMARK 200   FOR THE DATA SET  : 8.0000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.11                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.30                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 79.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.08400                            
REMARK 200  R SYM FOR SHELL            (I) : 0.08400                            
REMARK 200   FOR SHELL         : 2.640                              
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: PDB ID 2ABH                                          
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.32                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: PEG 4000, AMMONIUM ACETATE, SODIUM       
REMARK 280  CITRATE, PH 5.6, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 277K    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 2                        
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z                                                 
REMARK 290       3555   -X+1/2,Y+1/2,-Z                                         
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        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000       62.70000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       36.15000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       62.70000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       36.15000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE                                                          
REMARK 300 THERE ARE 2 ALTERNATE CONFORMATIONS FOR MONOMER B                    
REMARK 300 AND ITS ASSOCIATED LIGANDS                                           
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 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465   1 GLY A     2                                                      
REMARK 465   1 SER A     3                                                      
REMARK 465   1 LYS A     4                                                      
REMARK 465   1 PRO A     5                                                      
REMARK 465   1 PRO A     6                                                      
REMARK 465   1 SER A     7                                                      
REMARK 465   1 GLY A     8                                                      
REMARK 465   1 SER A     9                                                      
REMARK 465   1 PRO A    10                                                      
REMARK 465   1 GLU A    11                                                      
REMARK 465   1 THR A    12                                                      
REMARK 465   1 GLY A    13                                                      
REMARK 465   1 ALA A    14                                                      
REMARK 465   1 GLY A    15                                                      
REMARK 465   1 ALA A    16                                                      
REMARK 465   1 GLY A    17                                                      
REMARK 465   1 THR A    18                                                      
REMARK 465   1 GLY B     2                                                      
REMARK 465   1 SER B     3                                                      
REMARK 465   1 LYS B     4                                                      
REMARK 465   1 PRO B     5                                                      
REMARK 465   1 PRO B     6                                                      
REMARK 465   1 SER B     7                                                      
REMARK 465   1 GLY B     8                                                      
REMARK 465   1 SER B     9                                                      
REMARK 465   1 PRO B    10                                                      
REMARK 465   1 GLU B    11                                                      
REMARK 465   1 THR B    12                                                      
REMARK 465   1 GLY B    13                                                      
REMARK 465   1 ALA B    14                                                      
REMARK 465   1 GLY B    15                                                      
REMARK 465   1 ALA B    16                                                      
REMARK 465   1 GLY B    17                                                      
REMARK 465   1 THR B    18                                                      
REMARK 465   2 GLY A     2                                                      
REMARK 465   2 SER A     3                                                      
REMARK 465   2 LYS A     4                                                      
REMARK 465   2 PRO A     5                                                      
REMARK 465   2 PRO A     6                                                      
REMARK 465   2 SER A     7                                                      
REMARK 465   2 GLY A     8                                                      
REMARK 465   2 SER A     9                                                      
REMARK 465   2 PRO A    10                                                      
REMARK 465   2 GLU A    11                                                      
REMARK 465   2 THR A    12                                                      
REMARK 465   2 GLY A    13                                                      
REMARK 465   2 ALA A    14                                                      
REMARK 465   2 GLY A    15                                                      
REMARK 465   2 ALA A    16                                                      
REMARK 465   2 GLY A    17                                                      
REMARK 465   2 THR A    18                                                      
REMARK 465   2 GLY B     2                                                      
REMARK 465   2 SER B     3                                                      
REMARK 465   2 LYS B     4                                                      
REMARK 465   2 PRO B     5                                                      
REMARK 465   2 PRO B     6                                                      
REMARK 465   2 SER B     7                                                      
REMARK 465   2 GLY B     8                                                      
REMARK 465   2 SER B     9                                                      
REMARK 465   2 PRO B    10                                                      
REMARK 465   2 GLU B    11                                                      
REMARK 465   2 THR B    12                                                      
REMARK 465   2 GLY B    13                                                      
REMARK 465   2 ALA B    14                                                      
REMARK 465   2 GLY B    15                                                      
REMARK 465   2 ALA B    16                                                      
REMARK 465   2 GLY B    17                                                      
REMARK 465   2 THR B    18                                                      
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  1 SER A  35      114.63    -27.88                                   
REMARK 500  1 SER A 105     -169.73   -128.89                                   
REMARK 500  1 GLN A 273       11.70     59.49                                   
REMARK 500  1 ASN A 298       -9.21    -58.97                                   
REMARK 500  1 THR A 318      -83.56   -122.08                                   
REMARK 500  1 THR B  21        3.36   -150.50                                   
REMARK 500  1 THR B  33      147.58   -170.77                                   
REMARK 500  1 SER B  35      116.03    -18.98                                   
REMARK 500  1 ALA B  74      -84.22    -73.06                                   
REMARK 500  1 THR B  76      -79.82    -48.69                                   
REMARK 500  1 VAL B 150      -13.04   -143.80                                   
REMARK 500  1 ASN B 151       99.11     57.61                                   
REMARK 500  1 SER B 187      141.36   -171.30                                   
REMARK 500  1 PRO B 188       42.92    -88.26                                   
REMARK 500  1 ALA B 198       21.99    -75.37                                   
REMARK 500  1 ALA B 202       56.69    -90.90                                   
REMARK 500  1 SER B 246       24.05    -72.79                                   
REMARK 500  1 PRO B 253       85.25    -62.85                                   
REMARK 500  1 LYS B 268       17.45   -141.00                                   
REMARK 500  1 GLN B 273       12.13     59.93                                   
REMARK 500  1 ASN B 290      168.45    175.42                                   
REMARK 500  1 THR B 318      -92.28   -128.58                                   
REMARK 500  1 PHE B 325      -70.88    -95.81                                   
REMARK 500  1 HIS B 330       36.63     71.37                                   
REMARK 500  2 SER A  35      114.63    -27.88                                   
REMARK 500  2 SER A 105     -169.73   -128.89                                   
REMARK 500  2 GLN A 273       11.70     59.49                                   
REMARK 500  2 ASN A 298       -9.21    -58.97                                   
REMARK 500  2 THR A 318      -83.56   -122.08                                   
REMARK 500  2 SER B  35      115.24    -20.76                                   
REMARK 500  2 VAL B 116       95.80    -52.41                                   
REMARK 500  2 VAL B 150      -36.59   -143.12                                   
REMARK 500  2 ASN B 151       75.39     74.93                                   
REMARK 500  2 ASP B 180       58.66   -143.20                                   
REMARK 500  2 SER B 187      136.03   -177.39                                   
REMARK 500  2 ALA B 198       72.18    -67.21                                   
REMARK 500  2 GLN B 273        6.66     56.71                                   
REMARK 500  2 ILE B 288       76.57   -108.27                                   
REMARK 500  2 LYS B 301      -79.36    -60.50                                   
REMARK 500  2 THR B 318      -75.49   -108.15                                   
REMARK 500  2 SER B 350     -147.80   -166.06                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 A 1352                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE PO4 B 2352                
DBREF  1PC3 A    2   351  UNP    P15712   PST1_MYCTU      25    374             
DBREF  1PC3 B    2   351  UNP    P15712   PST1_MYCTU      25    374             
SEQRES   1 A  350  GLY SER LYS PRO PRO SER GLY SER PRO GLU THR GLY ALA          
SEQRES   2 A  350  GLY ALA GLY THR VAL ALA THR THR PRO ALA SER SER PRO          
SEQRES   3 A  350  VAL THR LEU ALA GLU THR GLY SER THR LEU LEU TYR PRO          
SEQRES   4 A  350  LEU PHE ASN LEU TRP GLY PRO ALA PHE HIS GLU ARG TYR          
SEQRES   5 A  350  PRO ASN VAL THR ILE THR ALA GLN GLY THR GLY SER GLY          
SEQRES   6 A  350  ALA GLY ILE ALA GLN ALA ALA ALA GLY THR VAL ASN ILE          
SEQRES   7 A  350  GLY ALA SER ASP ALA TYR LEU SER GLU GLY ASP MET ALA          
SEQRES   8 A  350  ALA HIS LYS GLY LEU MET ASN ILE ALA LEU ALA ILE SER          
SEQRES   9 A  350  ALA GLN GLN VAL ASN TYR ASN LEU PRO GLY VAL SER GLU          
SEQRES  10 A  350  HIS LEU LYS LEU ASN GLY LYS VAL LEU ALA ALA MET TYR          
SEQRES  11 A  350  GLN GLY THR ILE LYS THR TRP ASP ASP PRO GLN ILE ALA          
SEQRES  12 A  350  ALA LEU ASN PRO GLY VAL ASN LEU PRO GLY THR ALA VAL          
SEQRES  13 A  350  VAL PRO LEU HIS ARG SER ASP GLY SER GLY ASP THR PHE          
SEQRES  14 A  350  LEU PHE THR GLN TYR LEU SER LYS GLN ASP PRO GLU GLY          
SEQRES  15 A  350  TRP GLY LYS SER PRO GLY PHE GLY THR THR VAL ASP PHE          
SEQRES  16 A  350  PRO ALA VAL PRO GLY ALA LEU GLY GLU ASN GLY ASN GLY          
SEQRES  17 A  350  GLY MET VAL THR GLY CYS ALA GLU THR PRO GLY CYS VAL          
SEQRES  18 A  350  ALA TYR ILE GLY ILE SER PHE LEU ASP GLN ALA SER GLN          
SEQRES  19 A  350  ARG GLY LEU GLY GLU ALA GLN LEU GLY ASN SER SER GLY          
SEQRES  20 A  350  ASN PHE LEU LEU PRO ASP ALA GLN SER ILE GLN ALA ALA          
SEQRES  21 A  350  ALA ALA GLY PHE ALA SER LYS THR PRO ALA ASN GLN ALA          
SEQRES  22 A  350  ILE SER MET ILE ASP GLY PRO ALA PRO ASP GLY TYR PRO          
SEQRES  23 A  350  ILE ILE ASN TYR GLU TYR ALA ILE VAL ASN ASN ARG GLN          
SEQRES  24 A  350  LYS ASP ALA ALA THR ALA GLN THR LEU GLN ALA PHE LEU          
SEQRES  25 A  350  HIS TRP ALA ILE THR ASP GLY ASN LYS ALA SER PHE LEU          
SEQRES  26 A  350  ASP GLN VAL HIS PHE GLN PRO LEU PRO PRO ALA VAL VAL          
SEQRES  27 A  350  LYS LEU SER ASP ALA LEU ILE ALA THR ILE SER SER              
SEQRES   1 B  350  GLY SER LYS PRO PRO SER GLY SER PRO GLU THR GLY ALA          
SEQRES   2 B  350  GLY ALA GLY THR VAL ALA THR THR PRO ALA SER SER PRO          
SEQRES   3 B  350  VAL THR LEU ALA GLU THR GLY SER THR LEU LEU TYR PRO          
SEQRES   4 B  350  LEU PHE ASN LEU TRP GLY PRO ALA PHE HIS GLU ARG TYR          
SEQRES   5 B  350  PRO ASN VAL THR ILE THR ALA GLN GLY THR GLY SER GLY          
SEQRES   6 B  350  ALA GLY ILE ALA GLN ALA ALA ALA GLY THR VAL ASN ILE          
SEQRES   7 B  350  GLY ALA SER ASP ALA TYR LEU SER GLU GLY ASP MET ALA          
SEQRES   8 B  350  ALA HIS LYS GLY LEU MET ASN ILE ALA LEU ALA ILE SER          
SEQRES   9 B  350  ALA GLN GLN VAL ASN TYR ASN LEU PRO GLY VAL SER GLU          
SEQRES  10 B  350  HIS LEU LYS LEU ASN GLY LYS VAL LEU ALA ALA MET TYR          
SEQRES  11 B  350  GLN GLY THR ILE LYS THR TRP ASP ASP PRO GLN ILE ALA          
SEQRES  12 B  350  ALA LEU ASN PRO GLY VAL ASN LEU PRO GLY THR ALA VAL          
SEQRES  13 B  350  VAL PRO LEU HIS ARG SER ASP GLY SER GLY ASP THR PHE          
SEQRES  14 B  350  LEU PHE THR GLN TYR LEU SER LYS GLN ASP PRO GLU GLY          
SEQRES  15 B  350  TRP GLY LYS SER PRO GLY PHE GLY THR THR VAL ASP PHE          
SEQRES  16 B  350  PRO ALA VAL PRO GLY ALA LEU GLY GLU ASN GLY ASN GLY          
SEQRES  17 B  350  GLY MET VAL THR GLY CYS ALA GLU THR PRO GLY CYS VAL          
SEQRES  18 B  350  ALA TYR ILE GLY ILE SER PHE LEU ASP GLN ALA SER GLN          
SEQRES  19 B  350  ARG GLY LEU GLY GLU ALA GLN LEU GLY ASN SER SER GLY          
SEQRES  20 B  350  ASN PHE LEU LEU PRO ASP ALA GLN SER ILE GLN ALA ALA          
SEQRES  21 B  350  ALA ALA GLY PHE ALA SER LYS THR PRO ALA ASN GLN ALA          
SEQRES  22 B  350  ILE SER MET ILE ASP GLY PRO ALA PRO ASP GLY TYR PRO          
SEQRES  23 B  350  ILE ILE ASN TYR GLU TYR ALA ILE VAL ASN ASN ARG GLN          
SEQRES  24 B  350  LYS ASP ALA ALA THR ALA GLN THR LEU GLN ALA PHE LEU          
SEQRES  25 B  350  HIS TRP ALA ILE THR ASP GLY ASN LYS ALA SER PHE LEU          
SEQRES  26 B  350  ASP GLN VAL HIS PHE GLN PRO LEU PRO PRO ALA VAL VAL          
SEQRES  27 B  350  LYS LEU SER ASP ALA LEU ILE ALA THR ILE SER SER              
HET    PO4  A1352       5                                                       
HET    PO4  B2352       5                                                       
HETNAM     PO4 PHOSPHATE ION                                                    
FORMUL   3  PO4    2(O4 P 3-)                                                   
FORMUL   5  HOH   *240(H2 O)                                                    
HELIX    1   1 LEU A   38  TYR A   53  1                                  16    
HELIX    2   2 GLY A   64  ALA A   74  1                                  11    
HELIX    3   3 SER A   87  HIS A   94  1                                   8    
HELIX    4   4 ASN A  123  GLN A  132  1                                  10    
HELIX    5   5 ASP A  140  ASN A  147  1                                   8    
HELIX    6   6 SER A  166  ASP A  180  1                                  15    
HELIX    7   7 ASN A  206  THR A  218  1                                  13    
HELIX    8   8 PHE A  229  ARG A  236  1                                   8    
HELIX    9   9 ASP A  254  ALA A  263  1                                  10    
HELIX   10  10 ASP A  302  ILE A  317  1                                  16    
HELIX   11  11 THR A  318  ASN A  321  5                                   4    
HELIX   12  12 LYS A  322  ASP A  327  1                                   6    
HELIX   13  13 PRO A  335  ALA A  347  1                                  13    
HELIX   14  14 LEU B   38  TYR B   53  1                                  16    
HELIX   15  15 THR B   63  GLY B   75  1                                  13    
HELIX   16  16 SER B   87  HIS B   94  1                                   8    
HELIX   17  17 ASN B  123  GLN B  132  1                                  10    
HELIX   18  18 ASP B  140  ALA B  145  1                                   6    
HELIX   19  19 SER B  166  ASP B  180  1                                  15    
HELIX   20  20 ASN B  206  THR B  218  1                                  13    
HELIX   21  21 PHE B  229  ARG B  236  1                                   8    
HELIX   22  22 ASP B  254  GLY B  264  1                                  11    
HELIX   23  23 ASP B  302  ILE B  317  1                                  16    
HELIX   24  24 LYS B  322  ASP B  327  1                                   6    
HELIX   25  25 PRO B  335  ILE B  349  1                                  15    
SHEET    1   A 7 VAL A  56  THR A  59  0                                        
SHEET    2   A 7 VAL A  28  GLY A  34  1  N  LEU A  30   O  THR A  57           
SHEET    3   A 7 ILE A  79  SER A  82  1  O  ALA A  81   N  THR A  33           
SHEET    4   A 7 ILE A 289  ASN A 297 -1  O  ILE A 295   N  GLY A  80           
SHEET    5   A 7 LEU A  97  TYR A 111 -1  N  SER A 105   O  ASN A 290           
SHEET    6   A 7 CYS A 221  GLY A 226 -1  O  ALA A 223   N  ASN A 110           
SHEET    7   A 7 VAL A 158  PRO A 159  1  N  VAL A 158   O  VAL A 222           
SHEET    1   B 6 VAL A  56  THR A  59  0                                        
SHEET    2   B 6 VAL A  28  GLY A  34  1  N  LEU A  30   O  THR A  57           
SHEET    3   B 6 ILE A  79  SER A  82  1  O  ALA A  81   N  THR A  33           
SHEET    4   B 6 ILE A 289  ASN A 297 -1  O  ILE A 295   N  GLY A  80           
SHEET    5   B 6 LEU A  97  TYR A 111 -1  N  SER A 105   O  ASN A 290           
SHEET    6   B 6 GLY A 239  GLU A 240 -1  O  GLY A 239   N  TYR A 111           
SHEET    1   C 3 LYS A 121  LEU A 122  0                                        
SHEET    2   C 3 GLN A 242  GLY A 244  1  O  GLN A 242   N  LEU A 122           
SHEET    3   C 3 PHE A 250  LEU A 251 -1  O  LEU A 251   N  LEU A 243           
SHEET    1   D 2 HIS A 161  ARG A 162  0                                        
SHEET    2   D 2 GLY A 204  GLU A 205  1  O  GLU A 205   N  HIS A 161           
SHEET    1   E 7 VAL B  56  THR B  59  0                                        
SHEET    2   E 7 VAL B  28  GLY B  34  1  N  LEU B  30   O  THR B  57           
SHEET    3   E 7 ILE B  79  SER B  82  1  O  ALA B  81   N  THR B  33           
SHEET    4   E 7 ILE B 289  ASN B 297 -1  O  ILE B 295   N  GLY B  80           
SHEET    5   E 7 LEU B  97  TYR B 111 -1  N  ALA B 103   O  GLU B 292           
SHEET    6   E 7 CYS B 221  GLY B 226 -1  O  ALA B 223   N  ASN B 110           
SHEET    7   E 7 VAL B 158  PRO B 159  1  N  VAL B 158   O  VAL B 222           
SHEET    1   F 6 VAL B  56  THR B  59  0                                        
SHEET    2   F 6 VAL B  28  GLY B  34  1  N  LEU B  30   O  THR B  57           
SHEET    3   F 6 ILE B  79  SER B  82  1  O  ALA B  81   N  THR B  33           
SHEET    4   F 6 ILE B 289  ASN B 297 -1  O  ILE B 295   N  GLY B  80           
SHEET    5   F 6 LEU B  97  TYR B 111 -1  N  ALA B 103   O  GLU B 292           
SHEET    6   F 6 GLY B 239  GLU B 240 -1  O  GLY B 239   N  TYR B 111           
SHEET    1   G 3 LYS B 121  LEU B 122  0                                        
SHEET    2   G 3 GLN B 242  GLY B 244  1  O  GLN B 242   N  LEU B 122           
SHEET    3   G 3 PHE B 250  LEU B 251 -1  O  LEU B 251   N  LEU B 243           
SHEET    1   H 2 HIS B 161  ARG B 162  0                                        
SHEET    2   H 2 GLY B 204  GLU B 205  1  O  GLU B 205   N  HIS B 161           
CISPEP   1 SER A  187    PRO A  188          1         0.39                     
CISPEP   2 SER B  187    PRO B  188          1        -0.08                     
CISPEP   3 SER A  187    PRO A  188          2         0.39                     
CISPEP   4 SER B  187    PRO B  188          2         0.32                     
SITE     1 AC1 10 SER A  35  THR A  36  LEU A  37  GLY A  64                    
SITE     2 AC1 10 SER A  65  ASP A  83  ARG A 162  SER A 166                    
SITE     3 AC1 10 GLY A 167  ASP A 168                                          
SITE     1 AC2 10 SER B  35  THR B  36  LEU B  37  GLY B  64                    
SITE     2 AC2 10 SER B  65  ASP B  83  ARG B 162  SER B 166                    
SITE     3 AC2 10 GLY B 167  ASP B 168                                          
CRYST1  125.400   72.300   73.400  90.00  90.00  90.00 P 21 21 2     8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.007974  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.013831  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.013624        0.00000                         
MODEL        1                                                                  
ATOM      1  N   VAL A  19      64.240  11.926   9.628  0.50 19.76           N  
ATOM      2  CA  VAL A  19      64.711  12.796   8.495  0.50 19.10           C  
ATOM      3  C   VAL A  19      63.708  12.756   7.345  0.50 16.99           C  
ATOM      4  O   VAL A  19      63.273  11.686   6.931  0.50 17.64           O  
ATOM      5  CB  VAL A  19      66.094  12.329   7.965  0.50 19.82           C  
ATOM      6  CG1 VAL A  19      65.983  10.918   7.405  0.50 21.64           C  
ATOM      7  CG2 VAL A  19      66.600  13.287   6.896  0.50 19.52           C  
ATOM      8  N   ALA A  20      63.340  13.922   6.833  0.50 15.27           N  
ATOM      9  CA  ALA A  20      62.379  13.990   5.737  0.50 15.51           C  
ATOM     10  C   ALA A  20      63.073  13.725   4.412  0.50 15.54           C  
ATOM     11  O   ALA A  20      63.973  14.456   4.014  0.50 17.10           O  
ATOM     12  CB  ALA A  20      61.710  15.358   5.710  0.50 15.54           C  
ATOM     13  N   THR A  21      62.650  12.684   3.718  0.50 15.27           N  
ATOM     14  CA  THR A  21      63.266  12.358   2.446  0.50 15.93           C  
ATOM     15  C   THR A  21      62.435  12.838   1.255  0.50 14.78           C  
ATOM     16  O   THR A  21      62.775  12.574   0.099  0.50 15.70           O  
ATOM     17  CB  THR A  21      63.487  10.851   2.338  0.50 16.67           C  
ATOM     18  OG1 THR A  21      62.228  10.186   2.465  0.50 18.47           O  
ATOM     19  CG2 THR A  21      64.425  10.375   3.448  0.50 17.73           C  
ATOM     20  N   THR A  22      61.354  13.555   1.536  0.50 12.99           N  
ATOM     21  CA  THR A  22      60.492  14.064   0.471  0.50 10.95           C  
ATOM     22  C   THR A  22      60.221  15.543   0.682  0.50  9.11           C  
ATOM     23  O   THR A  22      59.851  15.950   1.769  0.50  8.64           O  
ATOM     24  CB  THR A  22      59.123  13.330   0.441  0.50 11.86           C  
ATOM     25  OG1 THR A  22      59.322  11.939   0.160  0.50 14.08           O  
ATOM     26  CG2 THR A  22      58.223  13.929  -0.624  0.50 11.13           C  
ATOM     27  N   PRO A  23      60.392  16.363  -0.365  0.50  7.31           N  
ATOM     28  CA  PRO A  23      60.169  17.815  -0.325  0.50  6.69           C  
ATOM     29  C   PRO A  23      58.683  18.151  -0.218  0.50  6.26           C  
ATOM     30  O   PRO A  23      57.837  17.341  -0.585  0.50  7.02           O  
ATOM     31  CB  PRO A  23      60.716  18.298  -1.672  0.50  7.54           C  
ATOM     32  CG  PRO A  23      61.571  17.164  -2.167  0.50  8.12           C  
ATOM     33  CD  PRO A  23      60.877  15.939  -1.686  0.50  6.94           C  
ATOM     34  N   ALA A  24      58.367  19.342   0.277  0.50  5.72           N  
ATOM     35  CA  ALA A  24      56.979  19.775   0.356  0.50  6.90           C  
ATOM     36  C   ALA A  24      56.550  19.909  -1.103  0.50  8.64           C  
ATOM     37  O   ALA A  24      57.400  20.056  -1.984  0.50  9.08           O  
ATOM     38  CB  ALA A  24      56.886  21.119   1.044  0.50  6.42           C  
ATOM     39  N   SER A  25      55.248  19.875  -1.369  0.50  9.92           N  
ATOM     40  CA  SER A  25      54.769  19.985  -2.746  0.50 11.36           C  
ATOM     41  C   SER A  25      54.620  21.426  -3.226  0.50 11.80           C  
ATOM     42  O   SER A  25      54.586  21.685  -4.431  0.50 12.67           O  
ATOM     43  CB  SER A  25      53.430  19.255  -2.907  0.50 12.85           C  
ATOM     44  OG  SER A  25      52.391  19.950  -2.236  0.50 15.18           O  
ATOM     45  N   SER A  26      54.534  22.366  -2.292  0.50 11.56           N  
ATOM     46  CA  SER A  26      54.385  23.764  -2.661  0.50 11.01           C  
ATOM     47  C   SER A  26      55.731  24.314  -3.128  0.50 11.82           C  
ATOM     48  O   SER A  26      56.779  23.821  -2.728  0.50 11.55           O  
ATOM     49  CB  SER A  26      53.864  24.559  -1.471  0.50 11.16           C  
ATOM     50  OG  SER A  26      54.696  24.367  -0.343  0.50 11.47           O  
ATOM     51  N   PRO A  27      55.721  25.343  -3.991  0.50 11.90           N  
ATOM     52  CA  PRO A  27      57.001  25.878  -4.452  0.50 12.22           C  
ATOM     53  C   PRO A  27      57.849  26.401  -3.307  0.50 11.57           C  
ATOM     54  O   PRO A  27      57.367  27.149  -2.452  0.50 11.12           O  
ATOM     55  CB  PRO A  27      56.589  26.974  -5.430  0.50 11.69           C  
ATOM     56  CG  PRO A  27      55.308  27.454  -4.853  0.50 13.50           C  
ATOM     57  CD  PRO A  27      54.605  26.171  -4.476  0.50 11.97           C  
ATOM     58  N   VAL A  28      59.109  25.976  -3.291  0.50 10.90           N  
ATOM     59  CA  VAL A  28      60.062  26.401  -2.276  0.50 10.83           C  
ATOM     60  C   VAL A  28      61.394  26.742  -2.949  0.50 10.86           C  
ATOM     61  O   VAL A  28      61.810  26.080  -3.903  0.50 10.19           O  
ATOM     62  CB  VAL A  28      60.287  25.297  -1.224  0.50  9.49           C  
ATOM     63  CG1 VAL A  28      61.425  25.685  -0.279  0.50 11.35           C  
ATOM     64  CG2 VAL A  28      59.012  25.080  -0.426  0.50 10.58           C  
ATOM     65  N   THR A  29      62.041  27.793  -2.455  0.50 11.91           N  
ATOM     66  CA  THR A  29      63.334  28.224  -2.970  0.50 13.23           C  
ATOM     67  C   THR A  29      64.385  28.099  -1.874  0.50 13.06           C  
ATOM     68  O   THR A  29      64.224  28.642  -0.788  0.50 12.91           O  
ATOM     69  CB  THR A  29      63.316  29.696  -3.417  0.50 14.59           C  
ATOM     70  OG1 THR A  29      62.437  29.850  -4.537  0.50 15.57           O  
ATOM     71  CG2 THR A  29      64.722  30.139  -3.820  0.50 16.33           C  
ATOM     72  N   LEU A  30      65.452  27.363  -2.157  0.50 13.63           N  
ATOM     73  CA  LEU A  30      66.544  27.201  -1.208  0.50 12.32           C  
ATOM     74  C   LEU A  30      67.686  28.045  -1.749  0.50 11.45           C  
ATOM     75  O   LEU A  30      68.181  27.798  -2.851  0.50 12.35           O  
ATOM     76  CB  LEU A  30      66.979  25.736  -1.120  0.50 12.16           C  
ATOM     77  CG  LEU A  30      65.920  24.771  -0.584  0.50 11.97           C  
ATOM     78  CD1 LEU A  30      66.472  23.362  -0.597  0.50 11.55           C  
ATOM     79  CD2 LEU A  30      65.520  25.173   0.825  0.50 10.83           C  
ATOM     80  N   ALA A  31      68.085  29.051  -0.982  0.50  9.01           N  
ATOM     81  CA  ALA A  31      69.165  29.927  -1.389  0.50  8.06           C  
ATOM     82  C   ALA A  31      70.453  29.501  -0.717  0.50  6.48           C  
ATOM     83  O   ALA A  31      70.478  29.267   0.501  0.50  5.17           O  
ATOM     84  CB  ALA A  31      68.840  31.360  -1.020  0.50  8.06           C  
ATOM     85  N   GLU A  32      71.517  29.412  -1.514  0.50  4.97           N  
ATOM     86  CA  GLU A  32      72.839  29.026  -1.017  0.50  5.40           C  
ATOM     87  C   GLU A  32      73.874  30.080  -1.387  0.50  5.22           C  
ATOM     88  O   GLU A  32      73.726  30.773  -2.384  0.50  6.97           O  
ATOM     89  CB  GLU A  32      73.258  27.674  -1.614  0.50  2.22           C  
ATOM     90  CG  GLU A  32      74.617  27.148  -1.131  0.50  2.71           C  
ATOM     91  CD  GLU A  32      75.813  27.679  -1.937  0.50  2.53           C  
ATOM     92  OE1 GLU A  32      75.621  28.539  -2.822  0.50  1.66           O  
ATOM     93  OE2 GLU A  32      76.954  27.221  -1.688  0.50  1.94           O  
ATOM     94  N   THR A  33      74.913  30.205  -0.572  0.50  4.89           N  
ATOM     95  CA  THR A  33      76.002  31.138  -0.843  0.50  4.53           C  
ATOM     96  C   THR A  33      77.214  30.698  -0.035  0.50  4.25           C  
ATOM     97  O   THR A  33      77.074  30.086   1.038  0.50  3.85           O  
ATOM     98  CB  THR A  33      75.672  32.592  -0.426  0.50  4.01           C  
ATOM     99  OG1 THR A  33      76.634  33.474  -1.014  0.50  6.32           O  
ATOM    100  CG2 THR A  33      75.778  32.769   1.078  0.50  5.18           C  
ATOM    101  N   GLY A  34      78.402  31.004  -0.539  0.50  2.78           N  
ATOM    102  CA  GLY A  34      79.595  30.649   0.201  0.50  2.01           C  
ATOM    103  C   GLY A  34      80.754  30.069  -0.580  0.50  1.27           C  
ATOM    104  O   GLY A  34      81.044  30.481  -1.696  0.50  1.22           O  
ATOM    105  N   SER A  35      81.424  29.114   0.053  0.50  1.22           N  
ATOM    106  CA  SER A  35      82.588  28.430  -0.500  0.50  2.70           C  
ATOM    107  C   SER A  35      82.690  28.321  -2.020  0.50  2.22           C  
ATOM    108  O   SER A  35      81.881  27.646  -2.661  0.50  1.33           O  
ATOM    109  CB  SER A  35      82.668  27.014   0.079  0.50  1.78           C  
ATOM    110  OG  SER A  35      83.615  26.263  -0.643  0.50  1.22           O  
ATOM    111  N   THR A  36      83.690  28.968  -2.606  0.50  1.22           N  
ATOM    112  CA  THR A  36      83.845  28.832  -4.041  0.50  2.19           C  
ATOM    113  C   THR A  36      84.330  27.408  -4.307  0.50  1.77           C  
ATOM    114  O   THR A  36      84.143  26.872  -5.390  0.50  3.42           O  
ATOM    115  CB  THR A  36      84.848  29.843  -4.617  0.50  2.08           C  
ATOM    116  OG1 THR A  36      86.137  29.651  -4.019  0.50  1.22           O  
ATOM    117  CG2 THR A  36      84.353  31.258  -4.365  0.50  1.22           C  
ATOM    118  N   LEU A  37      84.936  26.778  -3.309  0.50  1.36           N  
ATOM    119  CA  LEU A  37      85.412  25.412  -3.486  0.50  2.55           C  
ATOM    120  C   LEU A  37      84.226  24.479  -3.747  0.50  2.71           C  
ATOM    121  O   LEU A  37      84.282  23.641  -4.636  0.50  1.57           O  
ATOM    122  CB  LEU A  37      86.204  24.959  -2.243  0.50  3.08           C  
ATOM    123  CG  LEU A  37      86.661  23.503  -2.030  0.50  4.24           C  
ATOM    124  CD1 LEU A  37      86.983  22.814  -3.338  0.50  4.73           C  
ATOM    125  CD2 LEU A  37      87.885  23.504  -1.119  0.50  1.73           C  
ATOM    126  N   LEU A  38      83.143  24.650  -2.992  0.50  3.47           N  
ATOM    127  CA  LEU A  38      81.957  23.805  -3.136  0.50  4.69           C  
ATOM    128  C   LEU A  38      81.019  24.250  -4.264  0.50  5.37           C  
ATOM    129  O   LEU A  38      80.185  23.471  -4.726  0.50  2.90           O  
ATOM    130  CB  LEU A  38      81.176  23.777  -1.815  0.50  4.18           C  
ATOM    131  CG  LEU A  38      79.955  22.843  -1.727  0.50  6.49           C  
ATOM    132  CD1 LEU A  38      80.394  21.407  -1.955  0.50  6.86           C  
ATOM    133  CD2 LEU A  38      79.287  22.963  -0.355  0.50  5.89           C  
ATOM    134  N   TYR A  39      81.172  25.499  -4.697  0.50  6.78           N  
ATOM    135  CA  TYR A  39      80.326  26.083  -5.740  0.50  8.08           C  
ATOM    136  C   TYR A  39      80.104  25.236  -7.004  0.50  7.59           C  
ATOM    137  O   TYR A  39      78.966  25.018  -7.402  0.50  8.10           O  
ATOM    138  CB  TYR A  39      80.859  27.472  -6.129  0.50  9.31           C  
ATOM    139  CG  TYR A  39      79.994  28.202  -7.137  0.50 12.04           C  
ATOM    140  CD1 TYR A  39      78.684  28.566  -6.825  0.50 12.86           C  
ATOM    141  CD2 TYR A  39      80.480  28.517  -8.406  0.50 13.15           C  
ATOM    142  CE1 TYR A  39      77.878  29.226  -7.751  0.50 14.63           C  
ATOM    143  CE2 TYR A  39      79.684  29.176  -9.339  0.50 14.34           C  
ATOM    144  CZ  TYR A  39      78.383  29.526  -9.005  0.50 14.61           C  
ATOM    145  OH  TYR A  39      77.585  30.165  -9.927  0.50 16.30           O  
ATOM    146  N   PRO A  40      81.177  24.757  -7.651  0.50  6.96           N  
ATOM    147  CA  PRO A  40      81.017  23.942  -8.860  0.50  7.30           C  
ATOM    148  C   PRO A  40      80.091  22.743  -8.640  0.50  8.06           C  
ATOM    149  O   PRO A  40      79.293  22.375  -9.512  0.50  8.30           O  
ATOM    150  CB  PRO A  40      82.437  23.487  -9.160  0.50  7.86           C  
ATOM    151  CG  PRO A  40      83.279  24.568  -8.577  0.50  7.24           C  
ATOM    152  CD  PRO A  40      82.596  24.859  -7.277  0.50  6.95           C  
ATOM    153  N   LEU A  41      80.197  22.122  -7.475  0.50  6.33           N  
ATOM    154  CA  LEU A  41      79.357  20.967  -7.192  0.50  6.98           C  
ATOM    155  C   LEU A  41      77.904  21.382  -6.993  0.50  6.13           C  
ATOM    156  O   LEU A  41      76.990  20.694  -7.434  0.50  4.97           O  
ATOM    157  CB  LEU A  41      79.865  20.228  -5.952  0.50  6.17           C  
ATOM    158  CG  LEU A  41      79.031  19.016  -5.514  0.50  6.24           C  
ATOM    159  CD1 LEU A  41      78.960  18.002  -6.634  0.50  5.45           C  
ATOM    160  CD2 LEU A  41      79.659  18.397  -4.273  0.50  3.90           C  
ATOM    161  N   PHE A  42      77.690  22.504  -6.320  0.50  6.02           N  
ATOM    162  CA  PHE A  42      76.333  22.962  -6.110  0.50  7.77           C  
ATOM    163  C   PHE A  42      75.686  23.286  -7.445  0.50  7.14           C  
ATOM    164  O   PHE A  42      74.467  23.288  -7.563  0.50  7.87           O  
ATOM    165  CB  PHE A  42      76.303  24.179  -5.188  0.50  8.23           C  
ATOM    166  CG  PHE A  42      75.562  23.936  -3.913  0.50  9.08           C  
ATOM    167  CD1 PHE A  42      74.181  24.043  -3.869  0.50  9.15           C  
ATOM    168  CD2 PHE A  42      76.241  23.537  -2.766  0.50 10.02           C  
ATOM    169  CE1 PHE A  42      73.481  23.755  -2.702  0.50 10.47           C  
ATOM    170  CE2 PHE A  42      75.547  23.245  -1.592  0.50  9.42           C  
ATOM    171  CZ  PHE A  42      74.169  23.354  -1.562  0.50  9.73           C  
ATOM    172  N   ASN A  43      76.496  23.550  -8.459  0.50  7.66           N  
ATOM    173  CA  ASN A  43      75.943  23.836  -9.774  0.50  8.48           C  
ATOM    174  C   ASN A  43      75.482  22.569 -10.458  0.50  7.67           C  
ATOM    175  O   ASN A  43      74.809  22.627 -11.484  0.50  7.55           O  
ATOM    176  CB  ASN A  43      76.967  24.537 -10.658  0.50 11.00           C  
ATOM    177  CG  ASN A  43      77.006  26.007 -10.417  0.50 12.18           C  
ATOM    178  OD1 ASN A  43      75.963  26.654 -10.375  0.50 14.82           O  
ATOM    179  ND2 ASN A  43      78.202  26.557 -10.259  0.50 15.35           N  
ATOM    180  N   LEU A  44      75.861  21.419  -9.905  0.50  7.16           N  
ATOM    181  CA  LEU A  44      75.439  20.140 -10.471  0.50  6.92           C  
ATOM    182  C   LEU A  44      74.266  19.642  -9.641  0.50  7.11           C  
ATOM    183  O   LEU A  44      73.216  19.270 -10.173  0.50  8.08           O  
ATOM    184  CB  LEU A  44      76.584  19.127 -10.433  0.50  4.59           C  
ATOM    185  CG  LEU A  44      77.819  19.524 -11.244  0.50  5.22           C  
ATOM    186  CD1 LEU A  44      78.843  18.403 -11.215  0.50  2.23           C  
ATOM    187  CD2 LEU A  44      77.397  19.838 -12.684  0.50  3.43           C  
ATOM    188  N   TRP A  45      74.441  19.652  -8.326  0.50  5.86           N  
ATOM    189  CA  TRP A  45      73.391  19.210  -7.429  0.50  5.34           C  
ATOM    190  C   TRP A  45      72.103  19.989  -7.653  0.50  5.51           C  
ATOM    191  O   TRP A  45      71.042  19.399  -7.769  0.50  5.72           O  
ATOM    192  CB  TRP A  45      73.813  19.401  -5.974  0.50  3.99           C  
ATOM    193  CG  TRP A  45      74.762  18.394  -5.458  0.50  2.24           C  
ATOM    194  CD1 TRP A  45      75.101  17.205  -6.036  0.50  1.98           C  
ATOM    195  CD2 TRP A  45      75.432  18.435  -4.198  0.50  2.32           C  
ATOM    196  NE1 TRP A  45      75.936  16.497  -5.206  0.50  2.68           N  
ATOM    197  CE2 TRP A  45      76.151  17.232  -4.068  0.50  3.02           C  
ATOM    198  CE3 TRP A  45      75.485  19.373  -3.158  0.50  4.65           C  
ATOM    199  CZ2 TRP A  45      76.919  16.942  -2.944  0.50  2.60           C  
ATOM    200  CZ3 TRP A  45      76.248  19.086  -2.045  0.50  3.17           C  
ATOM    201  CH2 TRP A  45      76.952  17.878  -1.944  0.50  3.61           C  
ATOM    202  N   GLY A  46      72.216  21.315  -7.684  0.50  6.25           N  
ATOM    203  CA  GLY A  46      71.069  22.187  -7.859  0.50  7.68           C  
ATOM    204  C   GLY A  46      70.130  21.811  -8.983  0.50  9.55           C  
ATOM    205  O   GLY A  46      68.920  21.696  -8.777  0.50 10.47           O  
ATOM    206  N   PRO A  47      70.656  21.633 -10.198  0.50 10.15           N  
ATOM    207  CA  PRO A  47      69.817  21.264 -11.340  0.50  9.92           C  
ATOM    208  C   PRO A  47      69.254  19.854 -11.234  0.50  9.98           C  
ATOM    209  O   PRO A  47      68.112  19.613 -11.611  0.50 11.45           O  
ATOM    210  CB  PRO A  47      70.767  21.414 -12.520  0.50 10.35           C  
ATOM    211  CG  PRO A  47      71.669  22.536 -12.071  0.50 10.89           C  
ATOM    212  CD  PRO A  47      71.965  22.136 -10.649  0.50  9.86           C  
ATOM    213  N   ALA A  48      70.052  18.923 -10.727  0.50  8.69           N  
ATOM    214  CA  ALA A  48      69.609  17.547 -10.605  0.50  8.44           C  
ATOM    215  C   ALA A  48      68.404  17.449  -9.694  0.50  8.19           C  
ATOM    216  O   ALA A  48      67.392  16.856 -10.046  0.50  8.67           O  
ATOM    217  CB  ALA A  48      70.734  16.675 -10.067  0.50  8.50           C  
ATOM    218  N   PHE A  49      68.510  18.043  -8.518  0.50  7.87           N  
ATOM    219  CA  PHE A  49      67.423  17.987  -7.551  0.50  8.46           C  
ATOM    220  C   PHE A  49      66.184  18.673  -8.092  0.50  9.44           C  
ATOM    221  O   PHE A  49      65.063  18.214  -7.871  0.50  8.04           O  
ATOM    222  CB  PHE A  49      67.838  18.659  -6.252  0.50  5.79           C  
ATOM    223  CG  PHE A  49      66.903  18.411  -5.126  0.50  4.22           C  
ATOM    224  CD1 PHE A  49      66.841  17.160  -4.519  0.50  2.83           C  
ATOM    225  CD2 PHE A  49      66.110  19.432  -4.639  0.50  2.47           C  
ATOM    226  CE1 PHE A  49      65.998  16.940  -3.433  0.50  3.84           C  
ATOM    227  CE2 PHE A  49      65.267  19.222  -3.557  0.50  2.70           C  
ATOM    228  CZ  PHE A  49      65.208  17.980  -2.951  0.50  3.05           C  
ATOM    229  N   HIS A  50      66.393  19.779  -8.794  0.50 11.27           N  
ATOM    230  CA  HIS A  50      65.287  20.531  -9.367  0.50 14.41           C  
ATOM    231  C   HIS A  50      64.596  19.709 -10.441  0.50 16.00           C  
ATOM    232  O   HIS A  50      63.376  19.696 -10.530  0.50 18.18           O  
ATOM    233  CB  HIS A  50      65.787  21.851  -9.946  0.50 12.62           C  
ATOM    234  CG  HIS A  50      64.720  22.651 -10.626  0.50 14.10           C  
ATOM    235  ND1 HIS A  50      64.445  22.534 -11.971  0.50 13.32           N  
ATOM    236  CD2 HIS A  50      63.840  23.559 -10.138  0.50 12.76           C  
ATOM    237  CE1 HIS A  50      63.442  23.337 -12.284  0.50 13.57           C  
ATOM    238  NE2 HIS A  50      63.058  23.969 -11.189  0.50 13.83           N  
ATOM    239  N   GLU A  51      65.379  19.017 -11.253  0.50 18.89           N  
ATOM    240  CA  GLU A  51      64.827  18.176 -12.305  0.50 22.07           C  
ATOM    241  C   GLU A  51      63.870  17.153 -11.707  0.50 21.87           C  
ATOM    242  O   GLU A  51      62.823  16.864 -12.274  0.50 22.14           O  
ATOM    243  CB  GLU A  51      65.964  17.450 -13.027  0.50 26.22           C  
ATOM    244  CG  GLU A  51      65.557  16.166 -13.740  0.50 33.86           C  
ATOM    245  CD  GLU A  51      65.568  16.297 -15.256  0.50 38.64           C  
ATOM    246  OE1 GLU A  51      66.629  16.665 -15.813  0.50 40.68           O  
ATOM    247  OE2 GLU A  51      64.519  16.026 -15.891  0.50 41.87           O  
ATOM    248  N   ARG A  52      64.246  16.617 -10.550  0.50 22.49           N  
ATOM    249  CA  ARG A  52      63.470  15.595  -9.847  0.50 22.89           C  
ATOM    250  C   ARG A  52      62.232  16.170  -9.170  0.50 21.59           C  
ATOM    251  O   ARG A  52      61.175  15.552  -9.160  0.50 22.08           O  
ATOM    252  CB  ARG A  52      64.359  14.925  -8.797  0.50 25.72           C  
ATOM    253  CG  ARG A  52      64.131  13.438  -8.590  0.50 31.16           C  
ATOM    254  CD  ARG A  52      62.724  13.125  -8.122  0.50 36.49           C  
ATOM    255  NE  ARG A  52      62.574  11.715  -7.763  0.50 41.29           N  
ATOM    256  CZ  ARG A  52      61.409  11.125  -7.503  0.50 42.78           C  
ATOM    257  NH1 ARG A  52      60.276  11.815  -7.575  0.50 43.53           N  
ATOM    258  NH2 ARG A  52      61.374   9.837  -7.181  0.50 44.69           N  
ATOM    259  N   TYR A  53      62.375  17.355  -8.597  0.50 19.66           N  
ATOM    260  CA  TYR A  53      61.273  18.015  -7.906  0.50 18.25           C  
ATOM    261  C   TYR A  53      61.197  19.433  -8.445  0.50 16.48           C  
ATOM    262  O   TYR A  53      61.735  20.357  -7.846  0.50 16.32           O  
ATOM    263  CB  TYR A  53      61.554  18.057  -6.411  0.50 17.23           C  
ATOM    264  CG  TYR A  53      61.833  16.708  -5.803  0.50 17.31           C  
ATOM    265  CD1 TYR A  53      60.793  15.887  -5.379  0.50 17.37           C  
ATOM    266  CD2 TYR A  53      63.138  16.260  -5.632  0.50 16.53           C  
ATOM    267  CE1 TYR A  53      61.043  14.660  -4.796  0.50 17.27           C  
ATOM    268  CE2 TYR A  53      63.399  15.036  -5.053  0.50 17.87           C  
ATOM    269  CZ  TYR A  53      62.346  14.241  -4.634  0.50 18.29           C  
ATOM    270  OH  TYR A  53      62.597  13.025  -4.039  0.50 21.71           O  
ATOM    271  N   PRO A  54      60.517  19.619  -9.586  0.50 15.77           N  
ATOM    272  CA  PRO A  54      60.349  20.907 -10.256  0.50 14.36           C  
ATOM    273  C   PRO A  54      59.845  22.050  -9.395  0.50 13.65           C  
ATOM    274  O   PRO A  54      60.067  23.209  -9.726  0.50 13.86           O  
ATOM    275  CB  PRO A  54      59.382  20.576 -11.388  0.50 14.01           C  
ATOM    276  CG  PRO A  54      59.712  19.163 -11.692  0.50 14.00           C  
ATOM    277  CD  PRO A  54      59.802  18.565 -10.327  0.50 14.18           C  
ATOM    278  N   ASN A  55      59.162  21.742  -8.300  0.50 13.50           N  
ATOM    279  CA  ASN A  55      58.634  22.805  -7.452  0.50 14.03           C  
ATOM    280  C   ASN A  55      59.692  23.418  -6.545  0.50 13.42           C  
ATOM    281  O   ASN A  55      59.434  24.413  -5.876  0.50 14.92           O  
ATOM    282  CB  ASN A  55      57.490  22.283  -6.584  0.50 14.20           C  
ATOM    283  CG  ASN A  55      57.962  21.292  -5.540  0.50 15.78           C  
ATOM    284  OD1 ASN A  55      58.372  20.175  -5.865  0.50 16.88           O  
ATOM    285  ND2 ASN A  55      57.915  21.700  -4.276  0.50 15.23           N  
ATOM    286  N   VAL A  56      60.878  22.829  -6.519  0.50 12.37           N  
ATOM    287  CA  VAL A  56      61.945  23.342  -5.672  0.50 12.00           C  
ATOM    288  C   VAL A  56      63.012  24.092  -6.454  0.50 12.63           C  
ATOM    289  O   VAL A  56      63.623  23.540  -7.368  0.50 13.64           O  
ATOM    290  CB  VAL A  56      62.635  22.205  -4.899  0.50 10.54           C  
ATOM    291  CG1 VAL A  56      63.805  22.764  -4.109  0.50  9.95           C  
ATOM    292  CG2 VAL A  56      61.636  21.533  -3.961  0.50  8.49           C  
ATOM    293  N   THR A  57      63.243  25.348  -6.086  0.50 13.38           N  
ATOM    294  CA  THR A  57      64.256  26.151  -6.755  0.50 13.83           C  
ATOM    295  C   THR A  57      65.495  26.308  -5.878  0.50 13.05           C  
ATOM    296  O   THR A  57      65.398  26.727  -4.729  0.50 13.00           O  
ATOM    297  CB  THR A  57      63.728  27.545  -7.091  0.50 15.06           C  
ATOM    298  OG1 THR A  57      62.605  27.435  -7.972  0.50 17.51           O  
ATOM    299  CG2 THR A  57      64.812  28.360  -7.776  0.50 16.43           C  
ATOM    300  N   ILE A  58      66.654  25.973  -6.436  0.50 12.37           N  
ATOM    301  CA  ILE A  58      67.936  26.068  -5.730  0.50 12.36           C  
ATOM    302  C   ILE A  58      68.792  27.163  -6.374  0.50 10.93           C  
ATOM    303  O   ILE A  58      69.004  27.135  -7.578  0.50 12.56           O  
ATOM    304  CB  ILE A  58      68.757  24.760  -5.865  0.50 12.11           C  
ATOM    305  CG1 ILE A  58      67.939  23.544  -5.420  0.50 12.38           C  
ATOM    306  CG2 ILE A  58      70.052  24.888  -5.088  0.50 12.80           C  
ATOM    307  CD1 ILE A  58      67.989  23.246  -3.945  0.50 13.91           C  
ATOM    308  N   THR A  59      69.276  28.127  -5.597  0.50  8.87           N  
ATOM    309  CA  THR A  59      70.147  29.154  -6.171  0.50  8.63           C  
ATOM    310  C   THR A  59      71.457  29.107  -5.392  0.50  8.72           C  
ATOM    311  O   THR A  59      71.465  28.801  -4.190  0.50  9.07           O  
ATOM    312  CB  THR A  59      69.547  30.586  -6.083  0.50  7.03           C  
ATOM    313  OG1 THR A  59      69.234  30.902  -4.725  0.50  9.65           O  
ATOM    314  CG2 THR A  59      68.286  30.693  -6.916  0.50  8.90           C  
ATOM    315  N   ALA A  60      72.566  29.394  -6.066  0.50  7.59           N  
ATOM    316  CA  ALA A  60      73.858  29.353  -5.403  0.50  8.50           C  
ATOM    317  C   ALA A  60      74.783  30.438  -5.926  0.50  9.49           C  
ATOM    318  O   ALA A  60      74.616  30.922  -7.050  0.50 10.34           O  
ATOM    319  CB  ALA A  60      74.490  27.993  -5.604  0.50  6.38           C  
ATOM    320  N   GLN A  61      75.755  30.816  -5.106  0.50  9.07           N  
ATOM    321  CA  GLN A  61      76.719  31.833  -5.488  0.50 10.99           C  
ATOM    322  C   GLN A  61      78.073  31.591  -4.831  0.50  9.27           C  
ATOM    323  O   GLN A  61      78.154  31.199  -3.657  0.50  7.82           O  
ATOM    324  CB  GLN A  61      76.192  33.225  -5.116  0.50 15.16           C  
ATOM    325  CG  GLN A  61      75.875  33.367  -3.647  0.50 20.68           C  
ATOM    326  CD  GLN A  61      75.132  34.649  -3.310  0.50 23.71           C  
ATOM    327  OE1 GLN A  61      75.640  35.747  -3.522  0.50 26.34           O  
ATOM    328  NE2 GLN A  61      73.920  34.510  -2.775  0.50 24.93           N  
ATOM    329  N   GLY A  62      79.138  31.815  -5.603  0.50  9.83           N  
ATOM    330  CA  GLY A  62      80.491  31.637  -5.090  0.50  9.76           C  
ATOM    331  C   GLY A  62      80.975  32.939  -4.483  0.50  9.33           C  
ATOM    332  O   GLY A  62      81.341  33.868  -5.204  0.50 10.67           O  
ATOM    333  N   THR A  63      80.967  33.006  -3.153  0.50  8.50           N  
ATOM    334  CA  THR A  63      81.373  34.207  -2.431  0.50  5.78           C  
ATOM    335  C   THR A  63      82.422  33.960  -1.339  0.50  5.37           C  
ATOM    336  O   THR A  63      82.819  34.900  -0.659  0.50  4.10           O  
ATOM    337  CB  THR A  63      80.156  34.843  -1.760  0.50  5.31           C  
ATOM    338  OG1 THR A  63      79.501  33.847  -0.964  0.50  2.45           O  
ATOM    339  CG2 THR A  63      79.177  35.380  -2.806  0.50  5.07           C  
ATOM    340  N   GLY A  64      82.848  32.708  -1.157  0.50  4.80           N  
ATOM    341  CA  GLY A  64      83.839  32.400  -0.132  0.50  3.47           C  
ATOM    342  C   GLY A  64      83.166  31.926   1.145  0.50  3.64           C  
ATOM    343  O   GLY A  64      82.051  32.356   1.445  0.50  1.59           O  
ATOM    344  N   SER A  65      83.838  31.058   1.901  0.50  3.34           N  
ATOM    345  CA  SER A  65      83.284  30.513   3.150  0.50  4.24           C  
ATOM    346  C   SER A  65      82.881  31.590   4.164  0.50  3.05           C  
ATOM    347  O   SER A  65      81.870  31.457   4.863  0.50  1.22           O  
ATOM    348  CB  SER A  65      84.291  29.552   3.799  0.50  3.58           C  
ATOM    349  OG  SER A  65      84.494  28.399   3.000  0.50  5.17           O  
ATOM    350  N   GLY A  66      83.670  32.657   4.234  0.50  3.29           N  
ATOM    351  CA  GLY A  66      83.372  33.734   5.168  0.50  3.81           C  
ATOM    352  C   GLY A  66      81.948  34.231   5.018  0.50  4.29           C  
ATOM    353  O   GLY A  66      81.178  34.275   5.987  0.50  6.12           O  
ATOM    354  N   ALA A  67      81.590  34.625   3.803  0.50  3.75           N  
ATOM    355  CA  ALA A  67      80.240  35.094   3.544  0.50  5.87           C  
ATOM    356  C   ALA A  67      79.270  33.957   3.867  0.50  7.48           C  
ATOM    357  O   ALA A  67      78.187  34.196   4.408  0.50  8.19           O  
ATOM    358  CB  ALA A  67      80.096  35.499   2.096  0.50  5.25           C  
ATOM    359  N   GLY A  68      79.664  32.723   3.541  0.50  6.85           N  
ATOM    360  CA  GLY A  68      78.812  31.576   3.810  0.50  8.02           C  
ATOM    361  C   GLY A  68      78.387  31.502   5.267  0.50  7.19           C  
ATOM    362  O   GLY A  68      77.206  31.382   5.575  0.50  7.71           O  
ATOM    363  N   ILE A  69      79.362  31.581   6.166  0.50  8.27           N  
ATOM    364  CA  ILE A  69      79.106  31.535   7.598  0.50  7.82           C  
ATOM    365  C   ILE A  69      78.346  32.763   8.067  0.50  8.74           C  
ATOM    366  O   ILE A  69      77.402  32.663   8.856  0.50  8.82           O  
ATOM    367  CB  ILE A  69      80.423  31.454   8.386  0.50  8.71           C  
ATOM    368  CG1 ILE A  69      81.056  30.072   8.193  0.50  8.07           C  
ATOM    369  CG2 ILE A  69      80.165  31.756   9.859  0.50  8.93           C  
ATOM    370  CD1 ILE A  69      82.400  29.903   8.884  0.50 10.59           C  
ATOM    371  N   ALA A  70      78.762  33.925   7.581  0.50  8.19           N  
ATOM    372  CA  ALA A  70      78.122  35.185   7.958  0.50  9.43           C  
ATOM    373  C   ALA A  70      76.652  35.247   7.574  0.50  8.45           C  
ATOM    374  O   ALA A  70      75.789  35.523   8.416  0.50  7.50           O  
ATOM    375  CB  ALA A  70      78.863  36.355   7.324  0.50  7.41           C  
ATOM    376  N   GLN A  71      76.360  34.980   6.307  0.50  8.82           N  
ATOM    377  CA  GLN A  71      74.985  35.043   5.847  0.50 10.27           C  
ATOM    378  C   GLN A  71      74.057  33.984   6.419  0.50 10.84           C  
ATOM    379  O   GLN A  71      72.886  34.266   6.671  0.50  9.59           O  
ATOM    380  CB  GLN A  71      74.946  35.013   4.332  0.50 11.58           C  
ATOM    381  CG  GLN A  71      75.789  36.111   3.736  0.50 15.13           C  
ATOM    382  CD  GLN A  71      75.359  36.476   2.343  0.50 17.62           C  
ATOM    383  OE1 GLN A  71      76.109  37.110   1.598  0.50 21.16           O  
ATOM    384  NE2 GLN A  71      74.139  36.097   1.980  0.50 18.53           N  
ATOM    385  N   ALA A  72      74.555  32.770   6.624  0.50 10.82           N  
ATOM    386  CA  ALA A  72      73.697  31.735   7.186  0.50 12.66           C  
ATOM    387  C   ALA A  72      73.340  32.145   8.610  0.50 12.48           C  
ATOM    388  O   ALA A  72      72.215  31.957   9.052  0.50 12.16           O  
ATOM    389  CB  ALA A  72      74.409  30.380   7.185  0.50 12.63           C  
ATOM    390  N   ALA A  73      74.309  32.721   9.315  0.50 14.00           N  
ATOM    391  CA  ALA A  73      74.109  33.166  10.691  0.50 14.84           C  
ATOM    392  C   ALA A  73      73.135  34.345  10.759  0.50 15.79           C  
ATOM    393  O   ALA A  73      72.379  34.482  11.720  0.50 16.06           O  
ATOM    394  CB  ALA A  73      75.449  33.556  11.312  0.50 14.14           C  
ATOM    395  N   ALA A  74      73.150  35.190   9.734  0.50 15.99           N  
ATOM    396  CA  ALA A  74      72.270  36.350   9.700  0.50 15.71           C  
ATOM    397  C   ALA A  74      70.892  35.972   9.194  0.50 15.70           C  
ATOM    398  O   ALA A  74      69.992  36.800   9.163  0.50 17.81           O  
ATOM    399  CB  ALA A  74      72.862  37.432   8.808  0.50 14.12           C  
ATOM    400  N   GLY A  75      70.728  34.721   8.787  0.50 15.26           N  
ATOM    401  CA  GLY A  75      69.440  34.292   8.276  0.50 14.83           C  
ATOM    402  C   GLY A  75      69.193  34.725   6.840  0.50 14.79           C  
ATOM    403  O   GLY A  75      68.092  34.556   6.318  0.50 14.98           O  
ATOM    404  N   THR A  76      70.214  35.270   6.190  0.50 12.96           N  
ATOM    405  CA  THR A  76      70.073  35.723   4.816  0.50 13.39           C  
ATOM    406  C   THR A  76      69.868  34.606   3.784  0.50 12.83           C  
ATOM    407  O   THR A  76      69.208  34.820   2.763  0.50 13.64           O  
ATOM    408  CB  THR A  76      71.276  36.582   4.421  0.50 13.31           C  
ATOM    409  OG1 THR A  76      71.294  37.754   5.242  0.50 15.17           O  
ATOM    410  CG2 THR A  76      71.179  37.009   2.976  0.50 14.77           C  
ATOM    411  N   VAL A  77      70.435  33.426   4.030  0.50 10.31           N  
ATOM    412  CA  VAL A  77      70.264  32.290   3.113  0.50  8.50           C  
ATOM    413  C   VAL A  77      69.942  31.053   3.933  0.50  7.64           C  
ATOM    414  O   VAL A  77      70.124  31.050   5.157  0.50  7.56           O  
ATOM    415  CB  VAL A  77      71.536  31.984   2.315  0.50  5.93           C  
ATOM    416  CG1 VAL A  77      71.850  33.126   1.380  0.50  4.94           C  
ATOM    417  CG2 VAL A  77      72.699  31.728   3.282  0.50  5.67           C  
ATOM    418  N   ASN A  78      69.473  30.002   3.267  0.50  6.12           N  
ATOM    419  CA  ASN A  78      69.145  28.762   3.963  0.50  6.91           C  
ATOM    420  C   ASN A  78      70.390  27.897   4.109  0.50  6.43           C  
ATOM    421  O   ASN A  78      70.552  27.168   5.087  0.50  7.08           O  
ATOM    422  CB  ASN A  78      68.088  27.978   3.193  0.50  5.47           C  
ATOM    423  CG  ASN A  78      66.921  28.830   2.796  0.50  5.73           C  
ATOM    424  OD1 ASN A  78      66.895  29.384   1.700  0.50  5.45           O  
ATOM    425  ND2 ASN A  78      65.946  28.956   3.689  0.50  5.25           N  
ATOM    426  N   ILE A  79      71.280  28.005   3.132  0.50  6.95           N  
ATOM    427  CA  ILE A  79      72.490  27.212   3.129  0.50  5.94           C  
ATOM    428  C   ILE A  79      73.758  28.032   2.971  0.50  5.71           C  
ATOM    429  O   ILE A  79      73.965  28.662   1.935  0.50  4.81           O  
ATOM    430  CB  ILE A  79      72.477  26.209   1.970  0.50  6.01           C  
ATOM    431  CG1 ILE A  79      71.134  25.481   1.943  0.50  6.59           C  
ATOM    432  CG2 ILE A  79      73.690  25.282   2.072  0.50  5.79           C  
ATOM    433  CD1 ILE A  79      71.231  23.963   2.020  0.50 10.74           C  
ATOM    434  N   GLY A  80      74.598  28.030   4.001  0.50  4.99           N  
ATOM    435  CA  GLY A  80      75.874  28.706   3.903  0.50  4.13           C  
ATOM    436  C   GLY A  80      76.828  27.570   3.563  0.50  4.58           C  
ATOM    437  O   GLY A  80      76.778  26.519   4.206  0.50  6.66           O  
ATOM    438  N   ALA A  81      77.659  27.732   2.542  0.50  2.79           N  
ATOM    439  CA  ALA A  81      78.601  26.679   2.174  0.50  2.87           C  
ATOM    440  C   ALA A  81      79.953  27.064   2.741  0.50  2.41           C  
ATOM    441  O   ALA A  81      80.416  28.185   2.531  0.50  2.84           O  
ATOM    442  CB  ALA A  81      78.680  26.555   0.678  0.50  3.11           C  
ATOM    443  N   SER A  82      80.591  26.137   3.444  0.50  2.22           N  
ATOM    444  CA  SER A  82      81.875  26.419   4.075  0.50  3.29           C  
ATOM    445  C   SER A  82      82.816  25.220   4.116  0.50  2.76           C  
ATOM    446  O   SER A  82      82.375  24.099   4.350  0.50  3.29           O  
ATOM    447  CB  SER A  82      81.627  26.899   5.508  0.50  1.68           C  
ATOM    448  OG  SER A  82      82.842  27.246   6.160  0.50  4.92           O  
ATOM    449  N   ASP A  83      84.110  25.458   3.900  0.50  2.01           N  
ATOM    450  CA  ASP A  83      85.104  24.382   3.962  0.50  1.22           C  
ATOM    451  C   ASP A  83      85.664  24.355   5.376  0.50  1.96           C  
ATOM    452  O   ASP A  83      86.443  23.474   5.733  0.50  2.55           O  
ATOM    453  CB  ASP A  83      86.262  24.635   3.009  0.50  1.22           C  
ATOM    454  CG  ASP A  83      85.825  25.255   1.709  0.50  2.50           C  
ATOM    455  OD1 ASP A  83      84.878  24.734   1.082  0.50  1.22           O  
ATOM    456  OD2 ASP A  83      86.444  26.265   1.309  0.50  3.71           O  
ATOM    457  N   ALA A  84      85.271  25.334   6.180  0.50  1.48           N  
ATOM    458  CA  ALA A  84      85.739  25.421   7.559  0.50  3.56           C  
ATOM    459  C   ALA A  84      84.573  25.156   8.501  0.50  3.03           C  
ATOM    460  O   ALA A  84      83.462  25.590   8.226  0.50  2.35           O  
ATOM    461  CB  ALA A  84      86.322  26.824   7.829  0.50  4.35           C  
ATOM    462  N   TYR A  85      84.817  24.434   9.594  0.50  3.41           N  
ATOM    463  CA  TYR A  85      83.759  24.170  10.564  0.50  4.70           C  
ATOM    464  C   TYR A  85      83.603  25.401  11.434  0.50  5.05           C  
ATOM    465  O   TYR A  85      84.465  26.273  11.432  0.50  6.52           O  
ATOM    466  CB  TYR A  85      84.085  22.967  11.452  0.50  3.29           C  
ATOM    467  CG  TYR A  85      85.517  22.926  11.945  0.50  3.50           C  
ATOM    468  CD1 TYR A  85      85.895  23.566  13.122  0.50  2.26           C  
ATOM    469  CD2 TYR A  85      86.499  22.273  11.210  0.50  2.75           C  
ATOM    470  CE1 TYR A  85      87.231  23.553  13.552  0.50  3.02           C  
ATOM    471  CE2 TYR A  85      87.833  22.259  11.631  0.50  3.05           C  
ATOM    472  CZ  TYR A  85      88.189  22.898  12.794  0.50  2.35           C  
ATOM    473  OH  TYR A  85      89.512  22.892  13.173  0.50  2.14           O  
ATOM    474  N   LEU A  86      82.501  25.470  12.167  0.50  6.96           N  
ATOM    475  CA  LEU A  86      82.225  26.591  13.057  0.50  9.82           C  
ATOM    476  C   LEU A  86      83.093  26.518  14.306  0.50 12.88           C  
ATOM    477  O   LEU A  86      83.222  25.463  14.921  0.50 13.91           O  
ATOM    478  CB  LEU A  86      80.752  26.579  13.460  0.50  8.90           C  
ATOM    479  CG  LEU A  86      79.764  26.863  12.331  0.50  8.33           C  
ATOM    480  CD1 LEU A  86      78.363  26.460  12.727  0.50  9.41           C  
ATOM    481  CD2 LEU A  86      79.823  28.341  11.988  0.50 10.26           C  
ATOM    482  N   SER A  87      83.693  27.640  14.679  0.50 16.36           N  
ATOM    483  CA  SER A  87      84.531  27.673  15.865  0.50 20.32           C  
ATOM    484  C   SER A  87      83.625  27.554  17.078  0.50 22.62           C  
ATOM    485  O   SER A  87      82.419  27.767  16.978  0.50 23.00           O  
ATOM    486  CB  SER A  87      85.301  28.992  15.940  0.50 20.47           C  
ATOM    487  OG  SER A  87      84.415  30.080  16.135  0.50 20.94           O  
ATOM    488  N   GLU A  88      84.207  27.218  18.223  0.50 25.80           N  
ATOM    489  CA  GLU A  88      83.435  27.081  19.452  0.50 29.11           C  
ATOM    490  C   GLU A  88      82.789  28.423  19.767  0.50 29.67           C  
ATOM    491  O   GLU A  88      81.744  28.492  20.416  0.50 30.60           O  
ATOM    492  CB  GLU A  88      84.353  26.649  20.598  0.50 33.59           C  
ATOM    493  CG  GLU A  88      85.003  25.281  20.382  0.50 38.92           C  
ATOM    494  CD  GLU A  88      86.087  24.967  21.403  0.50 42.82           C  
ATOM    495  OE1 GLU A  88      85.775  24.872  22.615  0.50 44.70           O  
ATOM    496  OE2 GLU A  88      87.259  24.814  20.990  0.50 44.94           O  
ATOM    497  N   GLY A  89      83.425  29.488  19.291  0.50 29.90           N  
ATOM    498  CA  GLY A  89      82.910  30.823  19.507  0.50 29.68           C  
ATOM    499  C   GLY A  89      81.704  31.074  18.627  0.50 30.61           C  
ATOM    500  O   GLY A  89      80.716  31.654  19.074  0.50 31.76           O  
ATOM    501  N   ASP A  90      81.780  30.642  17.371  0.50 30.27           N  
ATOM    502  CA  ASP A  90      80.670  30.821  16.441  0.50 29.55           C  
ATOM    503  C   ASP A  90      79.435  30.090  16.947  0.50 28.60           C  
ATOM    504  O   ASP A  90      78.323  30.603  16.879  0.50 28.33           O  
ATOM    505  CB  ASP A  90      81.034  30.275  15.061  0.50 31.64           C  
ATOM    506  CG  ASP A  90      82.076  31.108  14.362  0.50 32.56           C  
ATOM    507  OD1 ASP A  90      81.871  32.339  14.266  0.50 33.09           O  
ATOM    508  OD2 ASP A  90      83.088  30.529  13.903  0.50 33.89           O  
ATOM    509  N   MET A  91      79.640  28.878  17.445  0.50 28.21           N  
ATOM    510  CA  MET A  91      78.541  28.084  17.959  0.50 27.86           C  
ATOM    511  C   MET A  91      77.891  28.774  19.150  0.50 27.74           C  
ATOM    512  O   MET A  91      76.669  28.803  19.267  0.50 27.76           O  
ATOM    513  CB  MET A  91      79.038  26.694  18.359  0.50 27.87           C  
ATOM    514  CG  MET A  91      79.473  25.841  17.178  0.50 28.74           C  
ATOM    515  SD  MET A  91      80.114  24.224  17.658  0.50 28.11           S  
ATOM    516  CE  MET A  91      78.586  23.302  17.842  0.50 28.69           C  
ATOM    517  N   ALA A  92      78.712  29.341  20.028  0.50 27.16           N  
ATOM    518  CA  ALA A  92      78.196  30.020  21.212  0.50 26.32           C  
ATOM    519  C   ALA A  92      77.435  31.297  20.871  0.50 26.08           C  
ATOM    520  O   ALA A  92      76.454  31.630  21.539  0.50 27.22           O  
ATOM    521  CB  ALA A  92      79.337  30.338  22.172  0.50 26.21           C  
ATOM    522  N   ALA A  93      77.878  32.001  19.833  0.50 24.69           N  
ATOM    523  CA  ALA A  93      77.244  33.252  19.426  0.50 23.80           C  
ATOM    524  C   ALA A  93      75.943  33.076  18.648  0.50 24.01           C  
ATOM    525  O   ALA A  93      75.062  33.933  18.698  0.50 24.05           O  
ATOM    526  CB  ALA A  93      78.217  34.077  18.609  0.50 23.81           C  
ATOM    527  N   HIS A  94      75.814  31.974  17.922  0.50 24.18           N  
ATOM    528  CA  HIS A  94      74.601  31.746  17.155  0.50 24.54           C  
ATOM    529  C   HIS A  94      74.047  30.374  17.472  0.50 25.26           C  
ATOM    530  O   HIS A  94      74.331  29.398  16.781  0.50 25.60           O  
ATOM    531  CB  HIS A  94      74.880  31.856  15.653  0.50 24.81           C  
ATOM    532  CG  HIS A  94      75.689  33.055  15.278  0.50 24.82           C  
ATOM    533  ND1 HIS A  94      77.049  33.132  15.496  0.50 25.71           N  
ATOM    534  CD2 HIS A  94      75.331  34.237  14.724  0.50 25.24           C  
ATOM    535  CE1 HIS A  94      77.491  34.309  15.095  0.50 25.38           C  
ATOM    536  NE2 HIS A  94      76.468  34.999  14.622  0.50 24.41           N  
ATOM    537  N   LYS A  95      73.257  30.295  18.531  0.50 25.95           N  
ATOM    538  CA  LYS A  95      72.675  29.023  18.910  0.50 25.38           C  
ATOM    539  C   LYS A  95      71.733  28.555  17.809  0.50 23.69           C  
ATOM    540  O   LYS A  95      71.013  29.348  17.195  0.50 24.23           O  
ATOM    541  CB  LYS A  95      71.951  29.166  20.252  0.50 28.80           C  
ATOM    542  CG  LYS A  95      72.921  29.388  21.416  0.50 31.39           C  
ATOM    543  CD  LYS A  95      72.213  29.671  22.735  0.50 33.90           C  
ATOM    544  CE  LYS A  95      73.230  29.811  23.862  0.50 35.12           C  
ATOM    545  NZ  LYS A  95      72.621  30.253  25.141  0.50 36.10           N  
ATOM    546  N   GLY A  96      71.762  27.259  17.544  0.50 21.00           N  
ATOM    547  CA  GLY A  96      70.911  26.713  16.508  0.50 18.85           C  
ATOM    548  C   GLY A  96      71.664  26.542  15.204  0.50 16.07           C  
ATOM    549  O   GLY A  96      71.198  25.848  14.308  0.50 16.54           O  
ATOM    550  N   LEU A  97      72.827  27.177  15.097  0.50 13.52           N  
ATOM    551  CA  LEU A  97      73.640  27.079  13.891  0.50 11.42           C  
ATOM    552  C   LEU A  97      74.582  25.874  13.987  0.50 10.22           C  
ATOM    553  O   LEU A  97      75.279  25.691  14.985  0.50  9.75           O  
ATOM    554  CB  LEU A  97      74.453  28.359  13.704  0.50  9.39           C  
ATOM    555  CG  LEU A  97      74.833  28.694  12.269  0.50  9.65           C  
ATOM    556  CD1 LEU A  97      73.570  28.991  11.475  0.50  8.33           C  
ATOM    557  CD2 LEU A  97      75.767  29.883  12.242  0.50  7.76           C  
ATOM    558  N   MET A  98      74.593  25.047  12.949  0.50  8.95           N  
ATOM    559  CA  MET A  98      75.444  23.865  12.935  0.50  7.99           C  
ATOM    560  C   MET A  98      76.076  23.634  11.560  0.50  7.34           C  
ATOM    561  O   MET A  98      75.620  24.187  10.552  0.50  5.63           O  
ATOM    562  CB  MET A  98      74.621  22.640  13.369  0.50  8.77           C  
ATOM    563  CG  MET A  98      73.264  22.497  12.677  0.50  8.96           C  
ATOM    564  SD  MET A  98      72.079  21.336  13.448  0.50  6.45           S  
ATOM    565  CE  MET A  98      70.596  21.880  12.660  0.50  6.63           C  
ATOM    566  N   ASN A  99      77.145  22.841  11.520  0.50  4.87           N  
ATOM    567  CA  ASN A  99      77.794  22.545  10.251  0.50  5.00           C  
ATOM    568  C   ASN A  99      77.610  21.079   9.903  0.50  4.70           C  
ATOM    569  O   ASN A  99      78.021  20.194  10.658  0.50  4.36           O  
ATOM    570  CB  ASN A  99      79.283  22.918  10.285  0.50  1.70           C  
ATOM    571  CG  ASN A  99      79.981  22.545  11.600  0.50  3.10           C  
ATOM    572  OD1 ASN A  99      80.837  23.290  12.079  0.50  1.22           O  
ATOM    573  ND2 ASN A  99      79.642  21.391  12.168  0.50  3.50           N  
ATOM    574  N   ILE A 100      76.969  20.805   8.772  0.50  2.68           N  
ATOM    575  CA  ILE A 100      76.763  19.411   8.414  0.50  4.50           C  
ATOM    576  C   ILE A 100      77.656  19.010   7.237  0.50  2.92           C  
ATOM    577  O   ILE A 100      77.651  19.649   6.181  0.50  1.44           O  
ATOM    578  CB  ILE A 100      75.271  19.129   8.090  0.50  4.87           C  
ATOM    579  CG1 ILE A 100      74.929  19.666   6.716  0.50  8.56           C  
ATOM    580  CG2 ILE A 100      74.356  19.849   9.101  0.50  4.52           C  
ATOM    581  CD1 ILE A 100      74.045  18.743   5.921  0.50 10.18           C  
ATOM    582  N   ALA A 101      78.438  17.955   7.436  0.50  1.22           N  
ATOM    583  CA  ALA A 101      79.353  17.469   6.406  0.50  3.08           C  
ATOM    584  C   ALA A 101      78.580  16.951   5.203  0.50  1.88           C  
ATOM    585  O   ALA A 101      77.570  16.280   5.366  0.50  1.22           O  
ATOM    586  CB  ALA A 101      80.229  16.369   6.980  0.50  1.22           C  
ATOM    587  N   LEU A 102      79.062  17.250   3.998  0.50  1.86           N  
ATOM    588  CA  LEU A 102      78.375  16.835   2.775  0.50  2.63           C  
ATOM    589  C   LEU A 102      79.229  15.961   1.846  0.50  3.56           C  
ATOM    590  O   LEU A 102      78.697  15.173   1.058  0.50  2.89           O  
ATOM    591  CB  LEU A 102      77.913  18.068   2.005  0.50  1.75           C  
ATOM    592  CG  LEU A 102      76.984  19.059   2.712  0.50  2.49           C  
ATOM    593  CD1 LEU A 102      76.921  20.346   1.914  0.50  2.12           C  
ATOM    594  CD2 LEU A 102      75.601  18.452   2.867  0.50  2.28           C  
ATOM    595  N   ALA A 103      80.546  16.115   1.934  0.50  3.65           N  
ATOM    596  CA  ALA A 103      81.472  15.343   1.110  0.50  3.18           C  
ATOM    597  C   ALA A 103      82.863  15.662   1.599  0.50  3.08           C  
ATOM    598  O   ALA A 103      83.029  16.509   2.481  0.50  3.20           O  
ATOM    599  CB  ALA A 103      81.336  15.744  -0.351  0.50  3.38           C  
ATOM    600  N   ILE A 104      83.863  14.990   1.039  0.50  1.55           N  
ATOM    601  CA  ILE A 104      85.237  15.260   1.422  0.50  3.41           C  
ATOM    602  C   ILE A 104      85.964  15.877   0.230  0.50  2.09           C  
ATOM    603  O   ILE A 104      85.854  15.393  -0.884  0.50  1.38           O  
ATOM    604  CB  ILE A 104      85.994  13.978   1.836  0.50  3.62           C  
ATOM    605  CG1 ILE A 104      85.350  13.362   3.075  0.50  4.16           C  
ATOM    606  CG2 ILE A 104      87.470  14.311   2.091  0.50  1.22           C  
ATOM    607  CD1 ILE A 104      85.927  11.999   3.442  0.50  4.26           C  
ATOM    608  N   SER A 105      86.692  16.955   0.470  0.50  1.51           N  
ATOM    609  CA  SER A 105      87.433  17.606  -0.596  0.50  2.99           C  
ATOM    610  C   SER A 105      88.880  17.794  -0.145  0.50  2.31           C  
ATOM    611  O   SER A 105      89.291  17.241   0.881  0.50  1.80           O  
ATOM    612  CB  SER A 105      86.782  18.950  -0.942  0.50  1.52           C  
ATOM    613  OG  SER A 105      86.722  19.801   0.188  0.50  4.34           O  
ATOM    614  N   ALA A 106      89.649  18.561  -0.911  0.50  2.97           N  
ATOM    615  CA  ALA A 106      91.054  18.795  -0.583  0.50  3.40           C  
ATOM    616  C   ALA A 106      91.558  20.079  -1.222  0.50  3.83           C  
ATOM    617  O   ALA A 106      90.838  20.736  -1.984  0.50  2.43           O  
ATOM    618  CB  ALA A 106      91.913  17.618  -1.045  0.50  1.22           C  
ATOM    619  N   GLN A 107      92.811  20.408  -0.918  0.50  2.53           N  
ATOM    620  CA  GLN A 107      93.448  21.609  -1.434  0.50  2.92           C  
ATOM    621  C   GLN A 107      94.823  21.278  -2.010  0.50  2.91           C  
ATOM    622  O   GLN A 107      95.532  20.435  -1.475  0.50  3.99           O  
ATOM    623  CB  GLN A 107      93.625  22.604  -0.292  0.50  2.90           C  
ATOM    624  CG  GLN A 107      94.201  23.948  -0.680  0.50  2.10           C  
ATOM    625  CD  GLN A 107      94.305  24.861   0.513  0.50  2.72           C  
ATOM    626  OE1 GLN A 107      95.193  24.703   1.357  0.50  4.87           O  
ATOM    627  NE2 GLN A 107      93.385  25.806   0.612  0.50  1.22           N  
ATOM    628  N   GLN A 108      95.207  21.935  -3.093  0.50  1.61           N  
ATOM    629  CA  GLN A 108      96.531  21.693  -3.647  0.50  2.03           C  
ATOM    630  C   GLN A 108      97.289  23.013  -3.616  0.50  1.22           C  
ATOM    631  O   GLN A 108      96.698  24.067  -3.372  0.50  1.62           O  
ATOM    632  CB  GLN A 108      96.449  21.184  -5.087  0.50  1.22           C  
ATOM    633  CG  GLN A 108      96.077  22.242  -6.132  0.50  1.39           C  
ATOM    634  CD  GLN A 108      94.605  22.212  -6.498  0.50  1.22           C  
ATOM    635  OE1 GLN A 108      93.863  21.346  -6.038  0.50  1.22           O  
ATOM    636  NE2 GLN A 108      94.174  23.157  -7.332  0.50  1.22           N  
ATOM    637  N   VAL A 109      98.596  22.951  -3.830  0.50  1.22           N  
ATOM    638  CA  VAL A 109      99.429  24.151  -3.878  0.50  2.12           C  
ATOM    639  C   VAL A 109      99.921  24.242  -5.312  0.50  2.12           C  
ATOM    640  O   VAL A 109     100.626  23.350  -5.779  0.50  1.61           O  
ATOM    641  CB  VAL A 109     100.645  24.055  -2.927  0.50  2.38           C  
ATOM    642  CG1 VAL A 109     101.647  25.177  -3.220  0.50  2.52           C  
ATOM    643  CG2 VAL A 109     100.188  24.171  -1.487  0.50  2.34           C  
ATOM    644  N   ASN A 110      99.515  25.294  -6.018  0.50  2.23           N  
ATOM    645  CA  ASN A 110      99.928  25.507  -7.407  0.50  2.81           C  
ATOM    646  C   ASN A 110     101.011  26.565  -7.453  0.50  3.08           C  
ATOM    647  O   ASN A 110     101.085  27.424  -6.580  0.50  2.88           O  
ATOM    648  CB  ASN A 110      98.757  26.003  -8.266  0.50  3.06           C  
ATOM    649  CG  ASN A 110      97.741  24.917  -8.567  0.50  4.78           C  
ATOM    650  OD1 ASN A 110      96.578  25.005  -8.162  0.50  3.64           O  
ATOM    651  ND2 ASN A 110      98.172  23.891  -9.289  0.50  3.24           N  
ATOM    652  N   TYR A 111     101.845  26.523  -8.483  0.50  3.58           N  
ATOM    653  CA  TYR A 111     102.904  27.515  -8.611  0.50  4.40           C  
ATOM    654  C   TYR A 111     103.183  27.768 -10.077  0.50  4.30           C  
ATOM    655  O   TYR A 111     102.897  26.929 -10.922  0.50  5.36           O  
ATOM    656  CB  TYR A 111     104.182  27.056  -7.900  0.50  4.51           C  
ATOM    657  CG  TYR A 111     104.665  25.689  -8.311  0.50  3.50           C  
ATOM    658  CD1 TYR A 111     105.397  25.511  -9.490  0.50  4.69           C  
ATOM    659  CD2 TYR A 111     104.364  24.559  -7.543  0.50  3.55           C  
ATOM    660  CE1 TYR A 111     105.816  24.243  -9.897  0.50  2.36           C  
ATOM    661  CE2 TYR A 111     104.778  23.295  -7.937  0.50  2.04           C  
ATOM    662  CZ  TYR A 111     105.504  23.148  -9.120  0.50  3.38           C  
ATOM    663  OH  TYR A 111     105.904  21.900  -9.529  0.50  3.84           O  
ATOM    664  N   ASN A 112     103.742  28.929 -10.376  0.50  3.83           N  
ATOM    665  CA  ASN A 112     104.031  29.292 -11.748  0.50  6.04           C  
ATOM    666  C   ASN A 112     105.530  29.293 -12.051  0.50  6.50           C  
ATOM    667  O   ASN A 112     106.215  30.299 -11.863  0.50  6.71           O  
ATOM    668  CB  ASN A 112     103.439  30.671 -12.027  0.50  5.57           C  
ATOM    669  CG  ASN A 112     103.362  30.984 -13.499  0.50  7.11           C  
ATOM    670  OD1 ASN A 112     103.916  30.263 -14.326  0.50  8.57           O  
ATOM    671  ND2 ASN A 112     102.674  32.069 -13.838  0.50  5.48           N  
ATOM    672  N   LEU A 113     106.038  28.160 -12.518  0.50  7.47           N  
ATOM    673  CA  LEU A 113     107.449  28.049 -12.865  0.50  9.34           C  
ATOM    674  C   LEU A 113     107.550  27.395 -14.235  0.50 10.77           C  
ATOM    675  O   LEU A 113     107.736  26.191 -14.347  0.50 10.96           O  
ATOM    676  CB  LEU A 113     108.199  27.200 -11.836  0.50  8.29           C  
ATOM    677  CG  LEU A 113     108.446  27.775 -10.437  0.50  7.79           C  
ATOM    678  CD1 LEU A 113     108.992  26.681  -9.540  0.50  6.61           C  
ATOM    679  CD2 LEU A 113     109.422  28.933 -10.500  0.50  8.64           C  
ATOM    680  N   PRO A 114     107.414  28.182 -15.303  0.50 12.24           N  
ATOM    681  CA  PRO A 114     107.506  27.570 -16.628  0.50 14.05           C  
ATOM    682  C   PRO A 114     108.844  26.887 -16.857  0.50 15.34           C  
ATOM    683  O   PRO A 114     109.895  27.391 -16.457  0.50 14.67           O  
ATOM    684  CB  PRO A 114     107.262  28.747 -17.572  0.50 14.49           C  
ATOM    685  CG  PRO A 114     107.721  29.947 -16.760  0.50 14.44           C  
ATOM    686  CD  PRO A 114     107.186  29.634 -15.393  0.50 13.11           C  
ATOM    687  N   GLY A 115     108.804  25.724 -17.490  0.50 16.71           N  
ATOM    688  CA  GLY A 115     110.037  25.006 -17.746  0.50 19.02           C  
ATOM    689  C   GLY A 115     110.352  23.944 -16.711  0.50 19.85           C  
ATOM    690  O   GLY A 115     111.159  23.058 -16.972  0.50 20.61           O  
ATOM    691  N   VAL A 116     109.731  24.033 -15.537  0.50 19.92           N  
ATOM    692  CA  VAL A 116     109.952  23.047 -14.481  0.50 20.03           C  
ATOM    693  C   VAL A 116     108.901  21.939 -14.583  0.50 20.54           C  
ATOM    694  O   VAL A 116     107.793  22.072 -14.065  0.50 22.18           O  
ATOM    695  CB  VAL A 116     109.880  23.702 -13.082  0.50 19.40           C  
ATOM    696  CG1 VAL A 116     109.996  22.638 -11.987  0.50 18.47           C  
ATOM    697  CG2 VAL A 116     110.989  24.725 -12.942  0.50 17.52           C  
ATOM    698  N   SER A 117     109.264  20.849 -15.252  0.50 20.34           N  
ATOM    699  CA  SER A 117     108.379  19.706 -15.462  0.50 20.36           C  
ATOM    700  C   SER A 117     107.935  18.965 -14.205  0.50 20.05           C  
ATOM    701  O   SER A 117     106.784  18.538 -14.107  0.50 19.63           O  
ATOM    702  CB  SER A 117     109.052  18.682 -16.386  0.50 20.82           C  
ATOM    703  OG  SER A 117     109.266  19.203 -17.684  0.50 22.81           O  
ATOM    704  N   GLU A 118     108.849  18.803 -13.255  0.50 18.14           N  
ATOM    705  CA  GLU A 118     108.554  18.058 -12.036  0.50 17.65           C  
ATOM    706  C   GLU A 118     107.493  18.638 -11.113  0.50 15.85           C  
ATOM    707  O   GLU A 118     107.186  19.838 -11.155  0.50 15.84           O  
ATOM    708  CB  GLU A 118     109.837  17.848 -11.228  0.50 20.04           C  
ATOM    709  CG  GLU A 118     110.947  17.147 -11.995  0.50 23.88           C  
ATOM    710  CD  GLU A 118     111.917  18.112 -12.662  0.50 26.03           C  
ATOM    711  OE1 GLU A 118     111.477  19.161 -13.184  0.50 27.20           O  
ATOM    712  OE2 GLU A 118     113.129  17.808 -12.673  0.50 28.81           O  
ATOM    713  N   HIS A 119     106.915  17.755 -10.299  0.50 12.84           N  
ATOM    714  CA  HIS A 119     105.935  18.148  -9.291  0.50  8.96           C  
ATOM    715  C   HIS A 119     106.845  18.415  -8.098  0.50  7.14           C  
ATOM    716  O   HIS A 119     107.249  17.490  -7.397  0.50  7.10           O  
ATOM    717  CB  HIS A 119     104.990  16.994  -8.951  0.50  6.41           C  
ATOM    718  CG  HIS A 119     103.887  16.788  -9.943  0.50  5.49           C  
ATOM    719  ND1 HIS A 119     103.767  15.640 -10.695  0.50  5.23           N  
ATOM    720  CD2 HIS A 119     102.812  17.549 -10.252  0.50  3.82           C  
ATOM    721  CE1 HIS A 119     102.665  15.699 -11.419  0.50  4.33           C  
ATOM    722  NE2 HIS A 119     102.066  16.848 -11.168  0.50  4.51           N  
ATOM    723  N   LEU A 120     107.188  19.671  -7.881  0.50  4.47           N  
ATOM    724  CA  LEU A 120     108.084  20.012  -6.792  0.50  5.27           C  
ATOM    725  C   LEU A 120     107.565  19.524  -5.454  0.50  4.98           C  
ATOM    726  O   LEU A 120     106.358  19.508  -5.218  0.50  3.38           O  
ATOM    727  CB  LEU A 120     108.302  21.534  -6.741  0.50  5.95           C  
ATOM    728  CG  LEU A 120     109.044  22.147  -7.938  0.50  5.89           C  
ATOM    729  CD1 LEU A 120     109.135  23.665  -7.769  0.50  7.31           C  
ATOM    730  CD2 LEU A 120     110.440  21.527  -8.043  0.50  5.77           C  
ATOM    731  N   LYS A 121     108.483  19.120  -4.582  0.50  4.68           N  
ATOM    732  CA  LYS A 121     108.104  18.662  -3.261  0.50  5.29           C  
ATOM    733  C   LYS A 121     108.227  19.809  -2.267  0.50  5.31           C  
ATOM    734  O   LYS A 121     109.242  20.513  -2.231  0.50  6.78           O  
ATOM    735  CB  LYS A 121     108.987  17.493  -2.830  0.50  6.80           C  
ATOM    736  CG  LYS A 121     108.830  16.270  -3.723  0.50 10.18           C  
ATOM    737  CD  LYS A 121     109.335  15.000  -3.048  0.50 13.03           C  
ATOM    738  CE  LYS A 121     110.831  15.022  -2.814  0.50 14.76           C  
ATOM    739  NZ  LYS A 121     111.589  14.765  -4.082  0.50 21.38           N  
ATOM    740  N   LEU A 122     107.181  20.002  -1.474  0.50  3.96           N  
ATOM    741  CA  LEU A 122     107.149  21.058  -0.472  0.50  4.22           C  
ATOM    742  C   LEU A 122     106.451  20.537   0.778  0.50  3.94           C  
ATOM    743  O   LEU A 122     105.760  19.524   0.728  0.50  4.76           O  
ATOM    744  CB  LEU A 122     106.361  22.263  -1.000  0.50  2.44           C  
ATOM    745  CG  LEU A 122     106.807  22.959  -2.296  0.50  3.01           C  
ATOM    746  CD1 LEU A 122     105.713  23.893  -2.771  0.50  1.22           C  
ATOM    747  CD2 LEU A 122     108.113  23.716  -2.065  0.50  2.38           C  
ATOM    748  N   ASN A 123     106.638  21.221   1.899  0.50  3.09           N  
ATOM    749  CA  ASN A 123     105.954  20.841   3.124  0.50  3.24           C  
ATOM    750  C   ASN A 123     105.510  22.113   3.839  0.50  2.15           C  
ATOM    751  O   ASN A 123     105.744  23.212   3.343  0.50  4.26           O  
ATOM    752  CB  ASN A 123     106.843  19.970   4.023  0.50  1.54           C  
ATOM    753  CG  ASN A 123     108.149  20.632   4.382  0.50  1.72           C  
ATOM    754  OD1 ASN A 123     108.260  21.857   4.420  0.50  5.36           O  
ATOM    755  ND2 ASN A 123     109.143  19.825   4.672  0.50  2.36           N  
ATOM    756  N   GLY A 124     104.871  21.973   4.993  0.50  1.84           N  
ATOM    757  CA  GLY A 124     104.385  23.131   5.720  0.50  2.05           C  
ATOM    758  C   GLY A 124     105.474  24.041   6.254  0.50  4.17           C  
ATOM    759  O   GLY A 124     105.280  25.255   6.361  0.50  4.16           O  
ATOM    760  N   LYS A 125     106.622  23.461   6.591  0.50  4.56           N  
ATOM    761  CA  LYS A 125     107.747  24.235   7.107  0.50  7.07           C  
ATOM    762  C   LYS A 125     108.302  25.159   6.016  0.50  6.45           C  
ATOM    763  O   LYS A 125     108.561  26.334   6.261  0.50  6.09           O  
ATOM    764  CB  LYS A 125     108.857  23.295   7.577  0.50 10.36           C  
ATOM    765  CG  LYS A 125     109.600  23.774   8.804  0.50 15.48           C  
ATOM    766  CD  LYS A 125     109.029  23.145  10.067  0.50 18.48           C  
ATOM    767  CE  LYS A 125     109.290  21.634  10.089  0.50 21.45           C  
ATOM    768  NZ  LYS A 125     108.750  20.976  11.319  0.50 22.34           N  
ATOM    769  N   VAL A 126     108.483  24.627   4.809  0.50  6.17           N  
ATOM    770  CA  VAL A 126     109.022  25.428   3.715  0.50  5.17           C  
ATOM    771  C   VAL A 126     108.013  26.464   3.216  0.50  5.00           C  
ATOM    772  O   VAL A 126     108.394  27.582   2.850  0.50  6.30           O  
ATOM    773  CB  VAL A 126     109.486  24.526   2.552  0.50  5.22           C  
ATOM    774  CG1 VAL A 126     110.001  25.370   1.403  0.50  4.91           C  
ATOM    775  CG2 VAL A 126     110.590  23.614   3.030  0.50  6.54           C  
ATOM    776  N   LEU A 127     106.731  26.105   3.213  0.50  3.60           N  
ATOM    777  CA  LEU A 127     105.685  27.025   2.777  0.50  3.20           C  
ATOM    778  C   LEU A 127     105.511  28.167   3.777  0.50  2.98           C  
ATOM    779  O   LEU A 127     105.236  29.299   3.389  0.50  1.22           O  
ATOM    780  CB  LEU A 127     104.360  26.287   2.590  0.50  1.28           C  
ATOM    781  CG  LEU A 127     104.334  25.486   1.286  0.50  3.17           C  
ATOM    782  CD1 LEU A 127     103.385  24.314   1.391  0.50  2.00           C  
ATOM    783  CD2 LEU A 127     103.947  26.416   0.144  0.50  2.08           C  
ATOM    784  N   ALA A 128     105.668  27.879   5.065  0.50  3.59           N  
ATOM    785  CA  ALA A 128     105.529  28.937   6.053  0.50  4.96           C  
ATOM    786  C   ALA A 128     106.654  29.952   5.829  0.50  4.93           C  
ATOM    787  O   ALA A 128     106.436  31.157   5.911  0.50  5.16           O  
ATOM    788  CB  ALA A 128     105.604  28.366   7.459  0.50  5.54           C  
ATOM    789  N   ALA A 129     107.851  29.454   5.536  0.50  4.06           N  
ATOM    790  CA  ALA A 129     109.004  30.319   5.299  0.50  3.69           C  
ATOM    791  C   ALA A 129     108.743  31.229   4.102  0.50  3.58           C  
ATOM    792  O   ALA A 129     109.100  32.412   4.127  0.50  4.28           O  
ATOM    793  CB  ALA A 129     110.235  29.476   5.059  0.50  3.33           C  
ATOM    794  N   MET A 130     108.122  30.679   3.057  0.50  2.38           N  
ATOM    795  CA  MET A 130     107.786  31.460   1.865  0.50  3.70           C  
ATOM    796  C   MET A 130     106.792  32.568   2.210  0.50  3.25           C  
ATOM    797  O   MET A 130     106.968  33.728   1.828  0.50  2.11           O  
ATOM    798  CB  MET A 130     107.200  30.553   0.781  0.50  4.43           C  
ATOM    799  CG  MET A 130     108.255  29.688   0.096  0.50  4.65           C  
ATOM    800  SD  MET A 130     107.596  28.315  -0.853  0.50 10.13           S  
ATOM    801  CE  MET A 130     106.817  29.166  -2.139  0.50  8.07           C  
ATOM    802  N   TYR A 131     105.755  32.213   2.955  0.50  3.43           N  
ATOM    803  CA  TYR A 131     104.764  33.198   3.337  0.50  3.60           C  
ATOM    804  C   TYR A 131     105.242  34.167   4.416  0.50  3.56           C  
ATOM    805  O   TYR A 131     104.600  35.185   4.667  0.50  3.29           O  
ATOM    806  CB  TYR A 131     103.474  32.487   3.738  0.50  2.22           C  
ATOM    807  CG  TYR A 131     102.647  32.139   2.512  0.50  2.43           C  
ATOM    808  CD1 TYR A 131     102.859  30.946   1.824  0.50  1.32           C  
ATOM    809  CD2 TYR A 131     101.714  33.043   1.992  0.50  1.22           C  
ATOM    810  CE1 TYR A 131     102.173  30.658   0.650  0.50  1.22           C  
ATOM    811  CE2 TYR A 131     101.019  32.766   0.815  0.50  1.22           C  
ATOM    812  CZ  TYR A 131     101.261  31.568   0.148  0.50  2.90           C  
ATOM    813  OH  TYR A 131     100.626  31.292  -1.041  0.50  1.22           O  
ATOM    814  N   GLN A 132     106.376  33.862   5.039  0.50  3.47           N  
ATOM    815  CA  GLN A 132     106.928  34.740   6.060  0.50  5.51           C  
ATOM    816  C   GLN A 132     108.027  35.608   5.466  0.50  5.99           C  
ATOM    817  O   GLN A 132     108.559  36.493   6.132  0.50  5.14           O  
ATOM    818  CB  GLN A 132     107.487  33.929   7.226  0.50  5.43           C  
ATOM    819  CG  GLN A 132     106.414  33.202   7.995  0.50  9.06           C  
ATOM    820  CD  GLN A 132     106.968  32.404   9.130  0.50 10.40           C  
ATOM    821  OE1 GLN A 132     107.892  31.612   8.949  0.50 14.21           O  
ATOM    822  NE2 GLN A 132     106.408  32.598  10.319  0.50 13.76           N  
ATOM    823  N   GLY A 133     108.377  35.340   4.214  0.50  6.39           N  
ATOM    824  CA  GLY A 133     109.395  36.137   3.563  0.50  8.34           C  
ATOM    825  C   GLY A 133     110.826  35.705   3.785  0.50  9.10           C  
ATOM    826  O   GLY A 133     111.742  36.392   3.333  0.50  8.78           O  
ATOM    827  N   THR A 134     111.039  34.584   4.471  0.50 10.14           N  
ATOM    828  CA  THR A 134     112.399  34.119   4.693  0.50 10.51           C  
ATOM    829  C   THR A 134     112.929  33.340   3.483  0.50  9.72           C  
ATOM    830  O   THR A 134     114.137  33.244   3.287  0.50  8.99           O  
ATOM    831  CB  THR A 134     112.519  33.308   6.014  0.50 11.16           C  
ATOM    832  OG1 THR A 134     111.660  32.170   5.984  0.50 13.07           O  
ATOM    833  CG2 THR A 134     112.126  34.190   7.199  0.50 11.78           C  
ATOM    834  N   ILE A 135     112.040  32.778   2.668  0.50  9.08           N  
ATOM    835  CA  ILE A 135     112.495  32.116   1.446  0.50  8.36           C  
ATOM    836  C   ILE A 135     112.084  33.110   0.376  0.50  8.30           C  
ATOM    837  O   ILE A 135     110.897  33.337   0.169  0.50  7.77           O  
ATOM    838  CB  ILE A 135     111.786  30.760   1.144  0.50  8.90           C  
ATOM    839  CG1 ILE A 135     112.346  29.623   2.007  0.50 10.39           C  
ATOM    840  CG2 ILE A 135     112.085  30.354  -0.298  0.50  6.70           C  
ATOM    841  CD1 ILE A 135     112.836  30.053   3.355  0.50 15.46           C  
ATOM    842  N   LYS A 136     113.058  33.702  -0.305  0.50  9.17           N  
ATOM    843  CA  LYS A 136     112.757  34.712  -1.318  0.50  9.80           C  
ATOM    844  C   LYS A 136     112.878  34.284  -2.775  0.50  7.59           C  
ATOM    845  O   LYS A 136     112.396  34.989  -3.658  0.50  7.23           O  
ATOM    846  CB  LYS A 136     113.649  35.936  -1.095  0.50 11.60           C  
ATOM    847  CG  LYS A 136     113.766  36.359   0.351  0.50 15.66           C  
ATOM    848  CD  LYS A 136     114.802  37.460   0.509  0.50 20.07           C  
ATOM    849  CE  LYS A 136     115.293  37.547   1.952  0.50 23.55           C  
ATOM    850  NZ  LYS A 136     115.955  36.271   2.390  0.50 26.57           N  
ATOM    851  N   THR A 137     113.521  33.147  -3.031  0.50  6.28           N  
ATOM    852  CA  THR A 137     113.713  32.667  -4.396  0.50  5.12           C  
ATOM    853  C   THR A 137     113.432  31.172  -4.511  0.50  4.84           C  
ATOM    854  O   THR A 137     113.556  30.431  -3.538  0.50  5.56           O  
ATOM    855  CB  THR A 137     115.157  32.948  -4.855  0.50  3.45           C  
ATOM    856  OG1 THR A 137     116.074  32.252  -4.009  0.50  5.38           O  
ATOM    857  CG2 THR A 137     115.461  34.412  -4.746  0.50  2.90           C  
ATOM    858  N   TRP A 138     113.069  30.717  -5.705  0.50  6.18           N  
ATOM    859  CA  TRP A 138     112.755  29.302  -5.892  0.50  6.20           C  
ATOM    860  C   TRP A 138     113.940  28.335  -5.872  0.50  6.76           C  
ATOM    861  O   TRP A 138     113.737  27.118  -5.888  0.50  7.01           O  
ATOM    862  CB  TRP A 138     111.933  29.093  -7.171  0.50  5.21           C  
ATOM    863  CG  TRP A 138     110.480  29.400  -6.973  0.50  4.11           C  
ATOM    864  CD1 TRP A 138     109.860  30.599  -7.175  0.50  3.36           C  
ATOM    865  CD2 TRP A 138     109.478  28.511  -6.457  0.50  3.35           C  
ATOM    866  NE1 TRP A 138     108.539  30.515  -6.813  0.50  5.21           N  
ATOM    867  CE2 TRP A 138     108.276  29.246  -6.369  0.50  4.28           C  
ATOM    868  CE3 TRP A 138     109.482  27.165  -6.058  0.50  3.60           C  
ATOM    869  CZ2 TRP A 138     107.078  28.679  -5.896  0.50  3.58           C  
ATOM    870  CZ3 TRP A 138     108.288  26.598  -5.585  0.50  2.06           C  
ATOM    871  CH2 TRP A 138     107.106  27.358  -5.509  0.50  1.54           C  
ATOM    872  N   ASP A 139     115.166  28.856  -5.840  0.50  5.79           N  
ATOM    873  CA  ASP A 139     116.329  27.982  -5.770  0.50  6.71           C  
ATOM    874  C   ASP A 139     116.933  28.041  -4.376  0.50  6.64           C  
ATOM    875  O   ASP A 139     118.086  27.668  -4.168  0.50  7.24           O  
ATOM    876  CB  ASP A 139     117.385  28.348  -6.825  0.50  7.78           C  
ATOM    877  CG  ASP A 139     117.999  29.712  -6.602  0.50 10.26           C  
ATOM    878  OD1 ASP A 139     117.629  30.404  -5.633  0.50 12.14           O  
ATOM    879  OD2 ASP A 139     118.861  30.101  -7.416  0.50 14.71           O  
ATOM    880  N   ASP A 140     116.139  28.505  -3.415  0.50  5.96           N  
ATOM    881  CA  ASP A 140     116.590  28.589  -2.028  0.50  5.70           C  
ATOM    882  C   ASP A 140     117.050  27.214  -1.554  0.50  6.01           C  
ATOM    883  O   ASP A 140     116.476  26.193  -1.934  0.50  5.71           O  
ATOM    884  CB  ASP A 140     115.449  29.066  -1.130  0.50  3.89           C  
ATOM    885  CG  ASP A 140     115.854  29.128   0.334  0.50  5.35           C  
ATOM    886  OD1 ASP A 140     115.845  28.070   1.002  0.50  4.82           O  
ATOM    887  OD2 ASP A 140     116.197  30.231   0.811  0.50  4.13           O  
ATOM    888  N   PRO A 141     118.097  27.164  -0.717  0.50  7.43           N  
ATOM    889  CA  PRO A 141     118.599  25.877  -0.214  0.50  7.00           C  
ATOM    890  C   PRO A 141     117.528  24.929   0.340  0.50  6.65           C  
ATOM    891  O   PRO A 141     117.562  23.730   0.068  0.50  6.15           O  
ATOM    892  CB  PRO A 141     119.613  26.301   0.841  0.50  6.51           C  
ATOM    893  CG  PRO A 141     120.233  27.511   0.194  0.50  7.80           C  
ATOM    894  CD  PRO A 141     119.010  28.264  -0.347  0.50  7.54           C  
ATOM    895  N   GLN A 142     116.581  25.456   1.112  0.50  6.39           N  
ATOM    896  CA  GLN A 142     115.527  24.619   1.670  0.50  7.13           C  
ATOM    897  C   GLN A 142     114.675  23.947   0.597  0.50  6.23           C  
ATOM    898  O   GLN A 142     114.085  22.906   0.845  0.50  6.43           O  
ATOM    899  CB  GLN A 142     114.614  25.435   2.589  0.50  8.75           C  
ATOM    900  CG  GLN A 142     115.244  25.831   3.911  0.50 11.28           C  
ATOM    901  CD  GLN A 142     114.278  26.598   4.792  0.50 13.71           C  
ATOM    902  OE1 GLN A 142     113.292  26.045   5.285  0.50 14.92           O  
ATOM    903  NE2 GLN A 142     114.548  27.884   4.983  0.50 15.53           N  
ATOM    904  N   ILE A 143     114.587  24.541  -0.588  0.50  5.76           N  
ATOM    905  CA  ILE A 143     113.789  23.936  -1.652  0.50  6.33           C  
ATOM    906  C   ILE A 143     114.626  22.923  -2.410  0.50  6.45           C  
ATOM    907  O   ILE A 143     114.158  21.840  -2.767  0.50  6.75           O  
ATOM    908  CB  ILE A 143     113.284  24.978  -2.674  0.50  6.07           C  
ATOM    909  CG1 ILE A 143     112.387  25.991  -1.974  0.50  7.79           C  
ATOM    910  CG2 ILE A 143     112.514  24.280  -3.800  0.50  3.10           C  
ATOM    911  CD1 ILE A 143     111.721  26.955  -2.912  0.50  7.88           C  
ATOM    912  N   ALA A 144     115.875  23.278  -2.662  0.50  6.53           N  
ATOM    913  CA  ALA A 144     116.763  22.391  -3.387  0.50  6.17           C  
ATOM    914  C   ALA A 144     117.007  21.111  -2.588  0.50  6.38           C  
ATOM    915  O   ALA A 144     117.175  20.035  -3.167  0.50  6.46           O  
ATOM    916  CB  ALA A 144     118.075  23.105  -3.674  0.50  4.41           C  
ATOM    917  N   ALA A 145     117.026  21.218  -1.260  0.50  5.31           N  
ATOM    918  CA  ALA A 145     117.261  20.039  -0.426  0.50  6.05           C  
ATOM    919  C   ALA A 145     116.152  18.987  -0.590  0.50  4.70           C  
ATOM    920  O   ALA A 145     116.398  17.792  -0.503  0.50  5.59           O  
ATOM    921  CB  ALA A 145     117.400  20.447   1.042  0.50  3.81           C  
ATOM    922  N   LEU A 146     114.935  19.442  -0.842  0.50  4.66           N  
ATOM    923  CA  LEU A 146     113.804  18.547  -1.020  0.50  4.12           C  
ATOM    924  C   LEU A 146     113.647  18.071  -2.464  0.50  3.36           C  
ATOM    925  O   LEU A 146     112.907  17.133  -2.722  0.50  3.25           O  
ATOM    926  CB  LEU A 146     112.512  19.259  -0.596  0.50  3.98           C  
ATOM    927  CG  LEU A 146     112.281  19.590   0.883  0.50  5.21           C  
ATOM    928  CD1 LEU A 146     110.996  20.420   1.048  0.50  3.46           C  
ATOM    929  CD2 LEU A 146     112.158  18.299   1.663  0.50  4.20           C  
ATOM    930  N   ASN A 147     114.336  18.715  -3.405  0.50  2.04           N  
ATOM    931  CA  ASN A 147     114.196  18.355  -4.812  0.50  3.83           C  
ATOM    932  C   ASN A 147     115.523  18.200  -5.511  0.50  4.74           C  
ATOM    933  O   ASN A 147     115.845  18.950  -6.438  0.50  1.96           O  
ATOM    934  CB  ASN A 147     113.385  19.420  -5.540  0.50  3.66           C  
ATOM    935  CG  ASN A 147     112.038  19.640  -4.918  0.50  2.99           C  
ATOM    936  OD1 ASN A 147     111.096  18.889  -5.171  0.50  4.65           O  
ATOM    937  ND2 ASN A 147     111.936  20.658  -4.078  0.50  1.82           N  
ATOM    938  N   PRO A 148     116.310  17.207  -5.088  0.50  6.45           N  
ATOM    939  CA  PRO A 148     117.624  16.937  -5.675  0.50  9.25           C  
ATOM    940  C   PRO A 148     117.537  16.668  -7.173  0.50 10.71           C  
ATOM    941  O   PRO A 148     116.620  16.000  -7.651  0.50 10.75           O  
ATOM    942  CB  PRO A 148     118.101  15.703  -4.903  0.50  8.48           C  
ATOM    943  CG  PRO A 148     117.326  15.764  -3.606  0.50  7.62           C  
ATOM    944  CD  PRO A 148     115.966  16.193  -4.081  0.50  7.12           C  
ATOM    945  N   GLY A 149     118.487  17.209  -7.923  0.50 14.07           N  
ATOM    946  CA  GLY A 149     118.492  16.981  -9.355  0.50 17.41           C  
ATOM    947  C   GLY A 149     117.652  17.919 -10.192  0.50 19.55           C  
ATOM    948  O   GLY A 149     117.836  18.001 -11.407  0.50 21.06           O  
ATOM    949  N   VAL A 150     116.723  18.629  -9.567  0.50 20.53           N  
ATOM    950  CA  VAL A 150     115.887  19.559 -10.312  0.50 21.77           C  
ATOM    951  C   VAL A 150     116.619  20.895 -10.454  0.50 22.09           C  
ATOM    952  O   VAL A 150     117.223  21.386  -9.498  0.50 21.68           O  
ATOM    953  CB  VAL A 150     114.528  19.776  -9.600  0.50 21.40           C  
ATOM    954  CG1 VAL A 150     113.708  20.838 -10.315  0.50 22.71           C  
ATOM    955  CG2 VAL A 150     113.755  18.471  -9.568  0.50 22.18           C  
ATOM    956  N   ASN A 151     116.580  21.465 -11.655  0.50 22.56           N  
ATOM    957  CA  ASN A 151     117.223  22.749 -11.904  0.50 23.74           C  
ATOM    958  C   ASN A 151     116.220  23.832 -11.522  0.50 21.66           C  
ATOM    959  O   ASN A 151     115.337  24.173 -12.308  0.50 22.29           O  
ATOM    960  CB  ASN A 151     117.590  22.887 -13.387  0.50 28.27           C  
ATOM    961  CG  ASN A 151     118.416  21.715 -13.898  0.50 33.24           C  
ATOM    962  OD1 ASN A 151     119.454  21.372 -13.322  0.50 36.24           O  
ATOM    963  ND2 ASN A 151     117.959  21.095 -14.987  0.50 34.51           N  
ATOM    964  N   LEU A 152     116.349  24.353 -10.308  0.50 18.00           N  
ATOM    965  CA  LEU A 152     115.452  25.387  -9.815  0.50 15.27           C  
ATOM    966  C   LEU A 152     115.929  26.772 -10.219  0.50 13.41           C  
ATOM    967  O   LEU A 152     117.085  27.123  -9.993  0.50 12.85           O  
ATOM    968  CB  LEU A 152     115.360  25.302  -8.290  0.50 13.91           C  
ATOM    969  CG  LEU A 152     114.864  23.959  -7.748  0.50 13.30           C  
ATOM    970  CD1 LEU A 152     115.197  23.820  -6.270  0.50 12.54           C  
ATOM    971  CD2 LEU A 152     113.380  23.858  -7.990  0.50 13.00           C  
ATOM    972  N   PRO A 153     115.036  27.593 -10.804  0.50 12.24           N  
ATOM    973  CA  PRO A 153     115.378  28.953 -11.236  0.50 11.18           C  
ATOM    974  C   PRO A 153     115.551  29.903 -10.054  0.50 10.00           C  
ATOM    975  O   PRO A 153     115.143  29.595  -8.936  0.50 10.51           O  
ATOM    976  CB  PRO A 153     114.189  29.340 -12.099  0.50 11.11           C  
ATOM    977  CG  PRO A 153     113.053  28.694 -11.358  0.50 11.14           C  
ATOM    978  CD  PRO A 153     113.602  27.321 -11.027  0.50 11.82           C  
ATOM    979  N   GLY A 154     116.158  31.057 -10.300  0.50  9.45           N  
ATOM    980  CA  GLY A 154     116.339  32.024  -9.230  0.50  8.61           C  
ATOM    981  C   GLY A 154     115.152  32.966  -9.117  0.50  7.29           C  
ATOM    982  O   GLY A 154     115.245  34.020  -8.499  0.50  7.87           O  
ATOM    983  N   THR A 155     114.030  32.577  -9.712  0.50  6.82           N  
ATOM    984  CA  THR A 155     112.808  33.382  -9.707  0.50  6.43           C  
ATOM    985  C   THR A 155     112.377  33.711  -8.291  0.50  5.09           C  
ATOM    986  O   THR A 155     112.470  32.871  -7.395  0.50  5.89           O  
ATOM    987  CB  THR A 155     111.659  32.634 -10.393  0.50  6.74           C  
ATOM    988  OG1 THR A 155     112.131  32.076 -11.622  0.50  9.38           O  
ATOM    989  CG2 THR A 155     110.504  33.579 -10.699  0.50  7.07           C  
ATOM    990  N   ALA A 156     111.908  34.939  -8.097  0.50  5.41           N  
ATOM    991  CA  ALA A 156     111.462  35.399  -6.788  0.50  5.85           C  
ATOM    992  C   ALA A 156     110.144  34.749  -6.446  0.50  5.44           C  
ATOM    993  O   ALA A 156     109.313  34.511  -7.320  0.50  6.78           O  
ATOM    994  CB  ALA A 156     111.300  36.899  -6.788  0.50  6.43           C  
ATOM    995  N   VAL A 157     109.944  34.454  -5.174  0.50  4.69           N  
ATOM    996  CA  VAL A 157     108.695  33.839  -4.760  0.50  4.86           C  
ATOM    997  C   VAL A 157     107.666  34.942  -4.524  0.50  4.23           C  
ATOM    998  O   VAL A 157     108.006  35.990  -3.991  0.50  3.31           O  
ATOM    999  CB  VAL A 157     108.887  33.047  -3.456  0.50  5.19           C  
ATOM   1000  CG1 VAL A 157     107.568  32.410  -3.019  0.50  4.06           C  
ATOM   1001  CG2 VAL A 157     109.967  31.992  -3.665  0.50  6.09           C  
ATOM   1002  N   VAL A 158     106.424  34.707  -4.946  0.50  2.72           N  
ATOM   1003  CA  VAL A 158     105.350  35.674  -4.753  0.50  4.58           C  
ATOM   1004  C   VAL A 158     104.226  34.893  -4.066  0.50  4.16           C  
ATOM   1005  O   VAL A 158     103.412  34.220  -4.719  0.50  4.59           O  
ATOM   1006  CB  VAL A 158     104.860  36.265  -6.097  0.50  3.94           C  
ATOM   1007  CG1 VAL A 158     103.958  37.450  -5.833  0.50  4.84           C  
ATOM   1008  CG2 VAL A 158     106.046  36.706  -6.948  0.50  4.59           C  
ATOM   1009  N   PRO A 159     104.175  34.969  -2.729  0.50  4.02           N  
ATOM   1010  CA  PRO A 159     103.164  34.255  -1.952  0.50  4.25           C  
ATOM   1011  C   PRO A 159     101.808  34.919  -1.982  0.50  3.87           C  
ATOM   1012  O   PRO A 159     101.569  35.901  -1.283  0.50  4.78           O  
ATOM   1013  CB  PRO A 159     103.785  34.227  -0.558  0.50  5.17           C  
ATOM   1014  CG  PRO A 159     104.456  35.593  -0.485  0.50  4.00           C  
ATOM   1015  CD  PRO A 159     105.075  35.750  -1.855  0.50  4.04           C  
ATOM   1016  N   LEU A 160     100.915  34.372  -2.795  0.50  3.97           N  
ATOM   1017  CA  LEU A 160      99.573  34.927  -2.926  0.50  3.47           C  
ATOM   1018  C   LEU A 160      98.639  34.365  -1.855  0.50  3.63           C  
ATOM   1019  O   LEU A 160      98.821  33.233  -1.387  0.50  3.79           O  
ATOM   1020  CB  LEU A 160      98.993  34.611  -4.305  0.50  1.22           C  
ATOM   1021  CG  LEU A 160      99.756  35.114  -5.530  0.50  2.72           C  
ATOM   1022  CD1 LEU A 160      98.976  34.710  -6.798  0.50  1.88           C  
ATOM   1023  CD2 LEU A 160      99.921  36.637  -5.446  0.50  1.22           C  
ATOM   1024  N   HIS A 161      97.639  35.161  -1.475  0.50  2.84           N  
ATOM   1025  CA  HIS A 161      96.655  34.756  -0.481  0.50  3.27           C  
ATOM   1026  C   HIS A 161      95.292  35.326  -0.869  0.50  3.48           C  
ATOM   1027  O   HIS A 161      95.203  36.284  -1.628  0.50  4.62           O  
ATOM   1028  CB  HIS A 161      97.068  35.228   0.918  0.50  1.22           C  
ATOM   1029  CG  HIS A 161      97.217  36.712   1.052  0.50  2.53           C  
ATOM   1030  ND1 HIS A 161      96.147  37.581   1.015  0.50  2.62           N  
ATOM   1031  CD2 HIS A 161      98.320  37.483   1.212  0.50  1.54           C  
ATOM   1032  CE1 HIS A 161      96.585  38.820   1.146  0.50  4.18           C  
ATOM   1033  NE2 HIS A 161      97.902  38.786   1.269  0.50  4.12           N  
ATOM   1034  N   ARG A 162      94.232  34.700  -0.368  0.50  3.42           N  
ATOM   1035  CA  ARG A 162      92.863  35.110  -0.642  0.50  3.23           C  
ATOM   1036  C   ARG A 162      92.544  36.414   0.064  0.50  2.64           C  
ATOM   1037  O   ARG A 162      92.880  36.602   1.238  0.50  2.55           O  
ATOM   1038  CB  ARG A 162      91.898  34.020  -0.146  0.50  2.08           C  
ATOM   1039  CG  ARG A 162      91.954  32.739  -0.966  0.50  1.69           C  
ATOM   1040  CD  ARG A 162      91.246  32.967  -2.275  0.50  2.01           C  
ATOM   1041  NE  ARG A 162      89.816  33.114  -2.053  0.50  4.35           N  
ATOM   1042  CZ  ARG A 162      88.968  32.093  -1.937  0.50  6.08           C  
ATOM   1043  NH1 ARG A 162      89.418  30.840  -2.027  0.50  4.14           N  
ATOM   1044  NH2 ARG A 162      87.672  32.322  -1.740  0.50  5.35           N  
ATOM   1045  N   SER A 163      91.883  37.323  -0.652  0.50  1.60           N  
ATOM   1046  CA  SER A 163      91.512  38.598  -0.083  0.50  1.44           C  
ATOM   1047  C   SER A 163      90.192  38.505   0.677  0.50  1.92           C  
ATOM   1048  O   SER A 163      89.968  39.254   1.621  0.50  2.05           O  
ATOM   1049  CB  SER A 163      91.450  39.655  -1.181  0.50  1.22           C  
ATOM   1050  OG  SER A 163      90.587  39.261  -2.235  0.50  1.22           O  
ATOM   1051  N   ASP A 164      89.331  37.570   0.283  0.50  2.17           N  
ATOM   1052  CA  ASP A 164      88.031  37.386   0.938  0.50  2.93           C  
ATOM   1053  C   ASP A 164      88.076  36.285   2.018  0.50  3.20           C  
ATOM   1054  O   ASP A 164      88.913  35.380   1.940  0.50  1.67           O  
ATOM   1055  CB  ASP A 164      87.000  37.012  -0.117  0.50  1.22           C  
ATOM   1056  CG  ASP A 164      87.433  35.803  -0.934  0.50  4.49           C  
ATOM   1057  OD1 ASP A 164      88.587  35.805  -1.401  0.50  2.35           O  
ATOM   1058  OD2 ASP A 164      86.628  34.864  -1.117  0.50  5.54           O  
ATOM   1059  N   GLY A 165      87.182  36.372   3.016  0.50  2.92           N  
ATOM   1060  CA  GLY A 165      87.132  35.374   4.084  0.50  2.12           C  
ATOM   1061  C   GLY A 165      86.996  34.051   3.367  0.50  2.48           C  
ATOM   1062  O   GLY A 165      86.021  33.853   2.635  0.50  1.22           O  
ATOM   1063  N   SER A 166      87.943  33.142   3.588  0.50  1.88           N  
ATOM   1064  CA  SER A 166      87.960  31.883   2.837  0.50  2.52           C  
ATOM   1065  C   SER A 166      88.245  30.583   3.560  0.50  2.55           C  
ATOM   1066  O   SER A 166      89.096  30.523   4.436  0.50  1.22           O  
ATOM   1067  CB  SER A 166      88.966  32.042   1.684  0.50  1.22           C  
ATOM   1068  OG  SER A 166      89.640  30.829   1.399  0.50  2.85           O  
ATOM   1069  N   GLY A 167      87.529  29.535   3.155  0.50  2.78           N  
ATOM   1070  CA  GLY A 167      87.733  28.223   3.742  0.50  1.50           C  
ATOM   1071  C   GLY A 167      89.105  27.706   3.343  0.50  3.46           C  
ATOM   1072  O   GLY A 167      89.779  27.039   4.137  0.50  3.14           O  
ATOM   1073  N   ASP A 168      89.527  28.007   2.115  0.50  1.22           N  
ATOM   1074  CA  ASP A 168      90.838  27.563   1.661  0.50  2.89           C  
ATOM   1075  C   ASP A 168      91.917  28.199   2.537  0.50  2.48           C  
ATOM   1076  O   ASP A 168      92.921  27.564   2.842  0.50  1.22           O  
ATOM   1077  CB  ASP A 168      91.059  27.919   0.193  0.50  1.22           C  
ATOM   1078  CG  ASP A 168      90.374  26.942  -0.761  0.50  3.05           C  
ATOM   1079  OD1 ASP A 168      90.944  25.865  -1.052  0.50  4.43           O  
ATOM   1080  OD2 ASP A 168      89.258  27.245  -1.232  0.50  1.77           O  
ATOM   1081  N   THR A 169      91.709  29.442   2.962  0.50  1.22           N  
ATOM   1082  CA  THR A 169      92.691  30.076   3.829  0.50  2.78           C  
ATOM   1083  C   THR A 169      92.769  29.300   5.142  0.50  2.58           C  
ATOM   1084  O   THR A 169      93.852  29.019   5.654  0.50  1.22           O  
ATOM   1085  CB  THR A 169      92.328  31.541   4.140  0.50  1.22           C  
ATOM   1086  OG1 THR A 169      92.415  32.308   2.940  0.50  2.65           O  
ATOM   1087  CG2 THR A 169      93.307  32.134   5.158  0.50  1.22           C  
ATOM   1088  N   PHE A 170      91.606  28.955   5.680  0.50  3.07           N  
ATOM   1089  CA  PHE A 170      91.528  28.203   6.929  0.50  2.90           C  
ATOM   1090  C   PHE A 170      92.318  26.892   6.772  0.50  2.65           C  
ATOM   1091  O   PHE A 170      93.180  26.563   7.600  0.50  1.35           O  
ATOM   1092  CB  PHE A 170      90.050  27.920   7.239  0.50  1.79           C  
ATOM   1093  CG  PHE A 170      89.805  27.295   8.583  0.50  2.73           C  
ATOM   1094  CD1 PHE A 170      89.678  28.086   9.721  0.50  5.06           C  
ATOM   1095  CD2 PHE A 170      89.648  25.917   8.702  0.50  1.32           C  
ATOM   1096  CE1 PHE A 170      89.389  27.504  10.974  0.50  6.19           C  
ATOM   1097  CE2 PHE A 170      89.361  25.328   9.933  0.50  2.53           C  
ATOM   1098  CZ  PHE A 170      89.229  26.122  11.073  0.50  5.43           C  
ATOM   1099  N   LEU A 171      92.040  26.153   5.698  0.50  1.84           N  
ATOM   1100  CA  LEU A 171      92.733  24.882   5.464  0.50  2.25           C  
ATOM   1101  C   LEU A 171      94.238  25.046   5.288  0.50  3.07           C  
ATOM   1102  O   LEU A 171      95.029  24.303   5.880  0.50  2.82           O  
ATOM   1103  CB  LEU A 171      92.178  24.170   4.228  0.50  1.22           C  
ATOM   1104  CG  LEU A 171      90.676  23.897   4.145  0.50  2.86           C  
ATOM   1105  CD1 LEU A 171      90.406  22.987   2.951  0.50  1.73           C  
ATOM   1106  CD2 LEU A 171      90.182  23.260   5.433  0.50  1.22           C  
ATOM   1107  N   PHE A 172      94.642  26.007   4.467  0.50  1.66           N  
ATOM   1108  CA  PHE A 172      96.061  26.229   4.230  0.50  2.04           C  
ATOM   1109  C   PHE A 172      96.801  26.588   5.521  0.50  2.47           C  
ATOM   1110  O   PHE A 172      97.811  25.960   5.875  0.50  1.22           O  
ATOM   1111  CB  PHE A 172      96.245  27.345   3.201  0.50  1.22           C  
ATOM   1112  CG  PHE A 172      97.669  27.542   2.761  0.50  2.29           C  
ATOM   1113  CD1 PHE A 172      98.340  26.545   2.058  0.50  1.72           C  
ATOM   1114  CD2 PHE A 172      98.335  28.740   3.036  0.50  3.73           C  
ATOM   1115  CE1 PHE A 172      99.649  26.738   1.635  0.50  1.22           C  
ATOM   1116  CE2 PHE A 172      99.654  28.948   2.615  0.50  1.22           C  
ATOM   1117  CZ  PHE A 172     100.307  27.948   1.916  0.50  2.94           C  
ATOM   1118  N   THR A 173      96.290  27.592   6.226  0.50  2.86           N  
ATOM   1119  CA  THR A 173      96.915  28.048   7.460  0.50  3.27           C  
ATOM   1120  C   THR A 173      96.901  27.027   8.603  0.50  3.04           C  
ATOM   1121  O   THR A 173      97.678  27.153   9.556  0.50  4.21           O  
ATOM   1122  CB  THR A 173      96.320  29.413   7.920  0.50  2.47           C  
ATOM   1123  OG1 THR A 173      94.901  29.321   8.069  0.50  1.22           O  
ATOM   1124  CG2 THR A 173      96.641  30.489   6.891  0.50  1.91           C  
ATOM   1125  N   GLN A 174      96.033  26.017   8.524  0.50  3.56           N  
ATOM   1126  CA  GLN A 174      96.029  24.985   9.560  0.50  2.50           C  
ATOM   1127  C   GLN A 174      97.191  24.042   9.260  0.50  2.77           C  
ATOM   1128  O   GLN A 174      97.864  23.549  10.169  0.50  3.07           O  
ATOM   1129  CB  GLN A 174      94.724  24.195   9.574  0.50  1.49           C  
ATOM   1130  CG  GLN A 174      93.609  24.854  10.377  0.50  2.82           C  
ATOM   1131  CD  GLN A 174      92.604  23.847  10.921  0.50  4.05           C  
ATOM   1132  OE1 GLN A 174      92.227  22.886  10.241  0.50  2.63           O  
ATOM   1133  NE2 GLN A 174      92.154  24.073  12.149  0.50  4.17           N  
ATOM   1134  N   TYR A 175      97.425  23.791   7.976  0.50  1.98           N  
ATOM   1135  CA  TYR A 175      98.526  22.928   7.557  0.50  3.45           C  
ATOM   1136  C   TYR A 175      99.839  23.558   8.035  0.50  3.02           C  
ATOM   1137  O   TYR A 175     100.683  22.899   8.648  0.50  2.84           O  
ATOM   1138  CB  TYR A 175      98.531  22.814   6.038  0.50  1.85           C  
ATOM   1139  CG  TYR A 175      99.674  22.014   5.472  0.50  1.22           C  
ATOM   1140  CD1 TYR A 175      99.900  20.698   5.875  0.50  2.15           C  
ATOM   1141  CD2 TYR A 175     100.505  22.554   4.504  0.50  1.22           C  
ATOM   1142  CE1 TYR A 175     100.926  19.934   5.319  0.50  1.22           C  
ATOM   1143  CE2 TYR A 175     101.542  21.806   3.944  0.50  1.22           C  
ATOM   1144  CZ  TYR A 175     101.743  20.498   4.353  0.50  1.22           C  
ATOM   1145  OH  TYR A 175     102.752  19.748   3.790  0.50  3.05           O  
ATOM   1146  N   LEU A 176      99.987  24.846   7.744  0.50  2.97           N  
ATOM   1147  CA  LEU A 176     101.162  25.627   8.130  0.50  4.50           C  
ATOM   1148  C   LEU A 176     101.287  25.655   9.661  0.50  4.75           C  
ATOM   1149  O   LEU A 176     102.379  25.540  10.201  0.50  4.53           O  
ATOM   1150  CB  LEU A 176     101.033  27.059   7.578  0.50  4.01           C  
ATOM   1151  CG  LEU A 176     101.895  27.497   6.381  0.50  6.75           C  
ATOM   1152  CD1 LEU A 176     101.826  26.476   5.264  0.50  7.68           C  
ATOM   1153  CD2 LEU A 176     101.425  28.856   5.885  0.50  5.34           C  
ATOM   1154  N   SER A 177     100.165  25.797  10.362  0.50  4.72           N  
ATOM   1155  CA  SER A 177     100.203  25.839  11.820  0.50  6.13           C  
ATOM   1156  C   SER A 177     100.569  24.484  12.432  0.50  6.86           C  
ATOM   1157  O   SER A 177     101.292  24.426  13.427  0.50  6.71           O  
ATOM   1158  CB  SER A 177      98.855  26.304  12.373  0.50  5.41           C  
ATOM   1159  OG  SER A 177      98.647  27.680  12.107  0.50  7.28           O  
ATOM   1160  N   LYS A 178     100.074  23.398  11.845  0.50  7.79           N  
ATOM   1161  CA  LYS A 178     100.367  22.062  12.364  0.50  8.31           C  
ATOM   1162  C   LYS A 178     101.802  21.649  12.118  0.50  7.21           C  
ATOM   1163  O   LYS A 178     102.424  21.018  12.966  0.50  4.17           O  
ATOM   1164  CB  LYS A 178      99.449  21.002  11.743  0.50 11.17           C  
ATOM   1165  CG  LYS A 178      97.982  21.190  12.054  0.50 16.06           C  
ATOM   1166  CD  LYS A 178      97.172  19.965  11.658  0.50 21.34           C  
ATOM   1167  CE  LYS A 178      97.154  18.898  12.768  0.50 24.97           C  
ATOM   1168  NZ  LYS A 178      98.493  18.310  13.108  0.50 26.71           N  
ATOM   1169  N   GLN A 179     102.334  22.008  10.957  0.50  6.51           N  
ATOM   1170  CA  GLN A 179     103.696  21.617  10.644  0.50  7.12           C  
ATOM   1171  C   GLN A 179     104.752  22.567  11.200  0.50  6.94           C  
ATOM   1172  O   GLN A 179     105.898  22.174  11.358  0.50  7.29           O  
ATOM   1173  CB  GLN A 179     103.860  21.450   9.131  0.50  6.21           C  
ATOM   1174  CG  GLN A 179     102.941  20.385   8.526  0.50  5.09           C  
ATOM   1175  CD  GLN A 179     103.643  19.561   7.455  0.50  6.72           C  
ATOM   1176  OE1 GLN A 179     104.455  20.084   6.689  0.50  5.66           O  
ATOM   1177  NE2 GLN A 179     103.324  18.271   7.391  0.50  5.19           N  
ATOM   1178  N   ASP A 180     104.368  23.806  11.506  0.50  6.50           N  
ATOM   1179  CA  ASP A 180     105.308  24.787  12.054  0.50  7.76           C  
ATOM   1180  C   ASP A 180     104.721  25.363  13.344  0.50  8.10           C  
ATOM   1181  O   ASP A 180     104.500  26.571  13.457  0.50  7.54           O  
ATOM   1182  CB  ASP A 180     105.539  25.924  11.055  0.50  8.49           C  
ATOM   1183  CG  ASP A 180     106.611  26.902  11.520  0.50  9.39           C  
ATOM   1184  OD1 ASP A 180     107.485  26.500  12.311  0.50  9.66           O  
ATOM   1185  OD2 ASP A 180     106.588  28.070  11.088  0.50  9.98           O  
ATOM   1186  N   PRO A 181     104.489  24.499  14.345  0.50  8.38           N  
ATOM   1187  CA  PRO A 181     103.917  24.871  15.646  0.50  9.20           C  
ATOM   1188  C   PRO A 181     104.600  26.056  16.345  0.50 10.12           C  
ATOM   1189  O   PRO A 181     103.929  26.921  16.891  0.50 10.53           O  
ATOM   1190  CB  PRO A 181     104.041  23.585  16.463  0.50  8.41           C  
ATOM   1191  CG  PRO A 181     104.193  22.502  15.441  0.50  8.05           C  
ATOM   1192  CD  PRO A 181     105.041  23.136  14.392  0.50  7.58           C  
ATOM   1193  N   GLU A 182     105.927  26.093  16.320  0.50 10.77           N  
ATOM   1194  CA  GLU A 182     106.649  27.169  16.984  0.50 12.34           C  
ATOM   1195  C   GLU A 182     106.787  28.449  16.179  0.50 11.88           C  
ATOM   1196  O   GLU A 182     107.225  29.476  16.693  0.50 12.92           O  
ATOM   1197  CB  GLU A 182     108.073  26.717  17.316  0.50 15.00           C  
ATOM   1198  CG  GLU A 182     108.116  25.572  18.329  0.50 15.00           C  
ATOM   1199  CD  GLU A 182     107.678  25.998  19.732  0.50 55.00           C  
ATOM   1200  OE1 GLU A 182     107.934  27.190  20.153  0.50 55.00           O  
ATOM   1201  OE2 GLU A 182     107.054  25.165  20.493  0.50 55.00           O  
ATOM   1202  N   GLY A 183     106.435  28.391  14.905  0.50 11.91           N  
ATOM   1203  CA  GLY A 183     106.530  29.575  14.075  0.50 11.07           C  
ATOM   1204  C   GLY A 183     105.140  30.034  13.690  0.50 10.75           C  
ATOM   1205  O   GLY A 183     104.445  30.687  14.482  0.50 11.12           O  
ATOM   1206  N   TRP A 184     104.719  29.673  12.482  0.50  9.01           N  
ATOM   1207  CA  TRP A 184     103.398  30.055  12.011  0.50  8.59           C  
ATOM   1208  C   TRP A 184     102.325  29.703  13.043  0.50  8.74           C  
ATOM   1209  O   TRP A 184     101.393  30.464  13.267  0.50  7.89           O  
ATOM   1210  CB  TRP A 184     103.087  29.361  10.693  0.50  6.33           C  
ATOM   1211  CG  TRP A 184     101.916  29.969  10.008  0.50  6.55           C  
ATOM   1212  CD1 TRP A 184     100.600  29.782  10.309  0.50  6.52           C  
ATOM   1213  CD2 TRP A 184     101.956  30.924   8.943  0.50  5.40           C  
ATOM   1214  NE1 TRP A 184      99.814  30.566   9.497  0.50  6.49           N  
ATOM   1215  CE2 TRP A 184     100.621  31.278   8.651  0.50  6.02           C  
ATOM   1216  CE3 TRP A 184     102.994  31.519   8.208  0.50  4.59           C  
ATOM   1217  CZ2 TRP A 184     100.292  32.204   7.652  0.50  6.29           C  
ATOM   1218  CZ3 TRP A 184     102.668  32.438   7.217  0.50  3.61           C  
ATOM   1219  CH2 TRP A 184     101.328  32.771   6.950  0.50  6.62           C  
ATOM   1220  N   GLY A 185     102.467  28.546  13.674  0.50  9.36           N  
ATOM   1221  CA  GLY A 185     101.495  28.138  14.670  0.50 11.81           C  
ATOM   1222  C   GLY A 185     101.216  29.194  15.724  0.50 13.18           C  
ATOM   1223  O   GLY A 185     100.068  29.378  16.128  0.50 13.35           O  
ATOM   1224  N   LYS A 186     102.253  29.895  16.172  0.50 14.15           N  
ATOM   1225  CA  LYS A 186     102.082  30.927  17.193  0.50 15.68           C  
ATOM   1226  C   LYS A 186     101.545  32.230  16.623  0.50 13.82           C  
ATOM   1227  O   LYS A 186     100.779  32.927  17.279  0.50 13.39           O  
ATOM   1228  CB  LYS A 186     103.406  31.186  17.914  0.50 18.31           C  
ATOM   1229  CG  LYS A 186     103.838  30.048  18.817  0.50 23.95           C  
ATOM   1230  CD  LYS A 186     105.111  30.394  19.578  0.50 28.91           C  
ATOM   1231  CE  LYS A 186     105.488  29.290  20.560  0.50 31.40           C  
ATOM   1232  NZ  LYS A 186     106.806  29.554  21.218  0.50 33.77           N  
ATOM   1233  N   SER A 187     101.962  32.555  15.403  0.50 12.22           N  
ATOM   1234  CA  SER A 187     101.513  33.764  14.723  0.50 10.85           C  
ATOM   1235  C   SER A 187     101.830  33.653  13.230  0.50  9.73           C  
ATOM   1236  O   SER A 187     102.956  33.346  12.850  0.50  8.99           O  
ATOM   1237  CB  SER A 187     102.212  34.987  15.302  0.50 11.54           C  
ATOM   1238  OG  SER A 187     101.867  36.145  14.566  0.50 14.03           O  
ATOM   1239  N   PRO A 188     100.854  33.957  12.365  0.50  8.18           N  
ATOM   1240  CA  PRO A 188      99.496  34.399  12.696  0.50  7.48           C  
ATOM   1241  C   PRO A 188      98.449  33.311  12.930  0.50  7.18           C  
ATOM   1242  O   PRO A 188      97.260  33.608  12.954  0.50  9.15           O  
ATOM   1243  CB  PRO A 188      99.136  35.263  11.503  0.50  7.62           C  
ATOM   1244  CG  PRO A 188      99.723  34.459  10.375  0.50  8.67           C  
ATOM   1245  CD  PRO A 188     101.098  34.060  10.916  0.50  7.69           C  
ATOM   1246  N   GLY A 189      98.857  32.057  13.084  0.50  6.36           N  
ATOM   1247  CA  GLY A 189      97.860  31.025  13.320  0.50  4.93           C  
ATOM   1248  C   GLY A 189      96.959  30.775  12.118  0.50  4.20           C  
ATOM   1249  O   GLY A 189      97.351  31.022  10.978  0.50  2.71           O  
ATOM   1250  N   PHE A 190      95.742  30.301  12.359  0.50  2.43           N  
ATOM   1251  CA  PHE A 190      94.835  29.993  11.258  0.50  3.91           C  
ATOM   1252  C   PHE A 190      93.466  30.630  11.403  0.50  2.93           C  
ATOM   1253  O   PHE A 190      93.135  31.176  12.452  0.50  4.01           O  
ATOM   1254  CB  PHE A 190      94.676  28.472  11.149  0.50  4.92           C  
ATOM   1255  CG  PHE A 190      94.047  27.850  12.366  0.50  5.61           C  
ATOM   1256  CD1 PHE A 190      92.663  27.768  12.484  0.50  4.44           C  
ATOM   1257  CD2 PHE A 190      94.840  27.383  13.411  0.50  4.83           C  
ATOM   1258  CE1 PHE A 190      92.078  27.230  13.624  0.50  5.99           C  
ATOM   1259  CE2 PHE A 190      94.267  26.846  14.550  0.50  5.92           C  
ATOM   1260  CZ  PHE A 190      92.881  26.767  14.659  0.50  4.94           C  
ATOM   1261  N   GLY A 191      92.670  30.544  10.341  0.50  2.31           N  
ATOM   1262  CA  GLY A 191      91.333  31.107  10.351  0.50  2.22           C  
ATOM   1263  C   GLY A 191      90.879  31.342   8.921  0.50  2.58           C  
ATOM   1264  O   GLY A 191      91.635  31.065   7.987  0.50  1.22           O  
ATOM   1265  N   THR A 192      89.658  31.837   8.736  0.50  1.89           N  
ATOM   1266  CA  THR A 192      89.147  32.111   7.392  0.50  4.53           C  
ATOM   1267  C   THR A 192      89.710  33.443   6.896  0.50  4.78           C  
ATOM   1268  O   THR A 192      89.778  33.713   5.689  0.50  3.88           O  
ATOM   1269  CB  THR A 192      87.619  32.157   7.388  0.50  3.67           C  
ATOM   1270  OG1 THR A 192      87.166  32.995   8.463  0.50  5.33           O  
ATOM   1271  CG2 THR A 192      87.053  30.743   7.557  0.50  2.71           C  
ATOM   1272  N   THR A 193      90.094  34.270   7.859  0.50  5.86           N  
ATOM   1273  CA  THR A 193      90.712  35.562   7.612  0.50  8.25           C  
ATOM   1274  C   THR A 193      91.952  35.528   8.493  0.50  7.84           C  
ATOM   1275  O   THR A 193      91.867  35.228   9.682  0.50  8.20           O  
ATOM   1276  CB  THR A 193      89.828  36.744   8.055  0.50  8.98           C  
ATOM   1277  OG1 THR A 193      88.683  36.842   7.201  0.50 12.58           O  
ATOM   1278  CG2 THR A 193      90.617  38.040   7.970  0.50 11.08           C  
ATOM   1279  N   VAL A 194      93.105  35.811   7.906  0.50  7.92           N  
ATOM   1280  CA  VAL A 194      94.356  35.784   8.647  0.50  7.97           C  
ATOM   1281  C   VAL A 194      95.200  36.993   8.277  0.50  8.48           C  
ATOM   1282  O   VAL A 194      95.141  37.464   7.139  0.50  8.12           O  
ATOM   1283  CB  VAL A 194      95.134  34.482   8.321  0.50  7.19           C  
ATOM   1284  CG1 VAL A 194      96.557  34.575   8.807  0.50  5.17           C  
ATOM   1285  CG2 VAL A 194      94.437  33.283   8.973  0.50  6.41           C  
ATOM   1286  N   ASP A 195      95.959  37.513   9.238  0.50  8.74           N  
ATOM   1287  CA  ASP A 195      96.835  38.651   8.970  0.50 10.63           C  
ATOM   1288  C   ASP A 195      98.108  38.118   8.316  0.50  7.84           C  
ATOM   1289  O   ASP A 195      99.072  37.809   9.006  0.50  7.32           O  
ATOM   1290  CB  ASP A 195      97.223  39.373  10.267  0.50 14.35           C  
ATOM   1291  CG  ASP A 195      96.061  40.115  10.896  0.50 19.71           C  
ATOM   1292  OD1 ASP A 195      95.336  40.823  10.164  0.50 22.65           O  
ATOM   1293  OD2 ASP A 195      95.877  40.002  12.129  0.50 22.28           O  
ATOM   1294  N   PHE A 196      98.120  37.996   6.997  0.50  6.45           N  
ATOM   1295  CA  PHE A 196      99.317  37.487   6.342  0.50  6.44           C  
ATOM   1296  C   PHE A 196     100.485  38.425   6.541  0.50  5.93           C  
ATOM   1297  O   PHE A 196     100.313  39.639   6.560  0.50  4.84           O  
ATOM   1298  CB  PHE A 196      99.070  37.278   4.852  0.50  5.51           C  
ATOM   1299  CG  PHE A 196      98.394  35.979   4.537  0.50  4.39           C  
ATOM   1300  CD1 PHE A 196      99.139  34.819   4.371  0.50  3.31           C  
ATOM   1301  CD2 PHE A 196      97.010  35.904   4.468  0.50  3.76           C  
ATOM   1302  CE1 PHE A 196      98.506  33.598   4.146  0.50  4.68           C  
ATOM   1303  CE2 PHE A 196      96.368  34.691   4.243  0.50  3.99           C  
ATOM   1304  CZ  PHE A 196      97.114  33.535   4.085  0.50  3.91           C  
ATOM   1305  N   PRO A 197     101.692  37.868   6.727  0.50  6.70           N  
ATOM   1306  CA  PRO A 197     102.887  38.695   6.925  0.50  7.01           C  
ATOM   1307  C   PRO A 197     103.044  39.650   5.740  0.50  6.37           C  
ATOM   1308  O   PRO A 197     102.901  39.242   4.587  0.50  6.17           O  
ATOM   1309  CB  PRO A 197     104.006  37.659   7.005  0.50  7.54           C  
ATOM   1310  CG  PRO A 197     103.313  36.481   7.662  0.50  6.18           C  
ATOM   1311  CD  PRO A 197     101.999  36.437   6.911  0.50  6.13           C  
ATOM   1312  N   ALA A 198     103.313  40.921   6.029  0.50  4.75           N  
ATOM   1313  CA  ALA A 198     103.472  41.917   4.984  0.50  5.08           C  
ATOM   1314  C   ALA A 198     104.843  41.801   4.342  0.50  3.95           C  
ATOM   1315  O   ALA A 198     105.729  42.606   4.626  0.50  3.39           O  
ATOM   1316  CB  ALA A 198     103.293  43.319   5.560  0.50  5.08           C  
ATOM   1317  N   VAL A 199     105.025  40.806   3.477  0.50  2.76           N  
ATOM   1318  CA  VAL A 199     106.313  40.625   2.812  0.50  2.65           C  
ATOM   1319  C   VAL A 199     106.171  40.950   1.334  0.50  2.36           C  
ATOM   1320  O   VAL A 199     105.062  41.032   0.825  0.50  3.34           O  
ATOM   1321  CB  VAL A 199     106.845  39.182   3.008  0.50  2.16           C  
ATOM   1322  CG1 VAL A 199     107.007  38.901   4.503  0.50  3.32           C  
ATOM   1323  CG2 VAL A 199     105.897  38.170   2.392  0.50  1.61           C  
ATOM   1324  N   PRO A 200     107.288  41.167   0.624  0.50  2.37           N  
ATOM   1325  CA  PRO A 200     107.141  41.483  -0.801  0.50  1.71           C  
ATOM   1326  C   PRO A 200     106.362  40.410  -1.552  0.50  2.40           C  
ATOM   1327  O   PRO A 200     106.718  39.233  -1.515  0.50  1.25           O  
ATOM   1328  CB  PRO A 200     108.583  41.588  -1.284  0.50  1.22           C  
ATOM   1329  CG  PRO A 200     109.328  42.037  -0.055  0.50  1.44           C  
ATOM   1330  CD  PRO A 200     108.703  41.208   1.037  0.50  1.22           C  
ATOM   1331  N   GLY A 201     105.290  40.809  -2.225  0.50  1.50           N  
ATOM   1332  CA  GLY A 201     104.514  39.838  -2.967  0.50  2.33           C  
ATOM   1333  C   GLY A 201     103.336  39.240  -2.216  0.50  1.32           C  
ATOM   1334  O   GLY A 201     102.653  38.379  -2.753  0.50  1.71           O  
ATOM   1335  N   ALA A 202     103.104  39.667  -0.976  0.50  2.34           N  
ATOM   1336  CA  ALA A 202     101.973  39.162  -0.197  0.50  2.68           C  
ATOM   1337  C   ALA A 202     100.725  39.889  -0.729  0.50  3.78           C  
ATOM   1338  O   ALA A 202     100.211  40.838  -0.119  0.50  4.49           O  
ATOM   1339  CB  ALA A 202     102.185  39.456   1.272  0.50  1.22           C  
ATOM   1340  N   LEU A 203     100.254  39.434  -1.886  0.50  3.57           N  
ATOM   1341  CA  LEU A 203      99.115  40.038  -2.572  0.50  3.44           C  
ATOM   1342  C   LEU A 203      97.821  39.254  -2.398  0.50  3.09           C  
ATOM   1343  O   LEU A 203      97.839  38.027  -2.328  0.50  1.78           O  
ATOM   1344  CB  LEU A 203      99.461  40.156  -4.055  0.50  3.31           C  
ATOM   1345  CG  LEU A 203     100.762  40.936  -4.288  0.50  1.35           C  
ATOM   1346  CD1 LEU A 203     101.319  40.693  -5.672  0.50  1.22           C  
ATOM   1347  CD2 LEU A 203     100.475  42.411  -4.063  0.50  3.22           C  
ATOM   1348  N   GLY A 204      96.696  39.962  -2.342  0.50  2.12           N  
ATOM   1349  CA  GLY A 204      95.424  39.279  -2.163  0.50  3.83           C  
ATOM   1350  C   GLY A 204      94.613  39.079  -3.431  0.50  3.59           C  
ATOM   1351  O   GLY A 204      94.532  39.979  -4.262  0.50  4.18           O  
ATOM   1352  N   GLU A 205      94.021  37.894  -3.581  0.50  3.37           N  
ATOM   1353  CA  GLU A 205      93.196  37.589  -4.747  0.50  4.10           C  
ATOM   1354  C   GLU A 205      91.834  37.142  -4.242  0.50  3.45           C  
ATOM   1355  O   GLU A 205      91.729  36.507  -3.187  0.50  3.08           O  
ATOM   1356  CB  GLU A 205      93.809  36.464  -5.590  0.50  3.54           C  
ATOM   1357  CG  GLU A 205      95.268  36.665  -5.953  0.50  5.01           C  
ATOM   1358  CD  GLU A 205      95.495  37.751  -6.992  0.50  5.29           C  
ATOM   1359  OE1 GLU A 205      94.524  38.183  -7.648  0.50  6.18           O  
ATOM   1360  OE2 GLU A 205      96.657  38.164  -7.159  0.50  6.64           O  
ATOM   1361  N   ASN A 206      90.793  37.475  -5.000  0.50  3.66           N  
ATOM   1362  CA  ASN A 206      89.432  37.126  -4.637  0.50  3.62           C  
ATOM   1363  C   ASN A 206      89.008  35.771  -5.208  0.50  2.68           C  
ATOM   1364  O   ASN A 206      89.142  35.521  -6.407  0.50  1.42           O  
ATOM   1365  CB  ASN A 206      88.480  38.222  -5.126  0.50  2.98           C  
ATOM   1366  CG  ASN A 206      87.025  37.919  -4.811  0.50  3.93           C  
ATOM   1367  OD1 ASN A 206      86.539  38.148  -3.693  0.50  3.76           O  
ATOM   1368  ND2 ASN A 206      86.322  37.388  -5.798  0.50  1.22           N  
ATOM   1369  N   GLY A 207      88.501  34.902  -4.332  0.50  3.88           N  
ATOM   1370  CA  GLY A 207      88.034  33.575  -4.734  0.50  3.71           C  
ATOM   1371  C   GLY A 207      89.073  32.661  -5.354  0.50  4.47           C  
ATOM   1372  O   GLY A 207      90.182  33.089  -5.683  0.50  5.65           O  
ATOM   1373  N   ASN A 208      88.732  31.391  -5.509  0.50  3.25           N  
ATOM   1374  CA  ASN A 208      89.660  30.442  -6.115  0.50  3.07           C  
ATOM   1375  C   ASN A 208      90.010  30.856  -7.542  0.50  2.90           C  
ATOM   1376  O   ASN A 208      91.143  30.702  -7.984  0.50  3.14           O  
ATOM   1377  CB  ASN A 208      89.055  29.029  -6.116  0.50  1.22           C  
ATOM   1378  CG  ASN A 208      89.339  28.281  -4.828  0.50  2.31           C  
ATOM   1379  OD1 ASN A 208      90.497  28.019  -4.508  0.50  1.22           O  
ATOM   1380  ND2 ASN A 208      88.285  27.934  -4.076  0.50  1.22           N  
ATOM   1381  N   GLY A 209      89.025  31.374  -8.265  0.50  2.73           N  
ATOM   1382  CA  GLY A 209      89.267  31.781  -9.634  0.50  3.87           C  
ATOM   1383  C   GLY A 209      90.372  32.811  -9.654  0.50  3.66           C  
ATOM   1384  O   GLY A 209      91.323  32.699 -10.421  0.50  4.10           O  
ATOM   1385  N   GLY A 210      90.245  33.810  -8.787  0.50  2.98           N  
ATOM   1386  CA  GLY A 210      91.244  34.860  -8.695  0.50  3.16           C  
ATOM   1387  C   GLY A 210      92.622  34.337  -8.369  0.50  3.30           C  
ATOM   1388  O   GLY A 210      93.623  34.890  -8.835  0.50  3.42           O  
ATOM   1389  N   MET A 211      92.690  33.281  -7.566  0.50  2.69           N  
ATOM   1390  CA  MET A 211      93.985  32.705  -7.213  0.50  3.63           C  
ATOM   1391  C   MET A 211      94.607  32.043  -8.453  0.50  2.98           C  
ATOM   1392  O   MET A 211      95.801  32.190  -8.689  0.50  1.22           O  
ATOM   1393  CB  MET A 211      93.841  31.670  -6.084  0.50  2.58           C  
ATOM   1394  CG  MET A 211      93.471  32.246  -4.722  0.50  3.02           C  
ATOM   1395  SD  MET A 211      94.766  33.225  -3.934  0.50  5.62           S  
ATOM   1396  CE  MET A 211      95.772  31.967  -3.145  0.50  4.64           C  
ATOM   1397  N   VAL A 212      93.796  31.312  -9.226  0.50  2.01           N  
ATOM   1398  CA  VAL A 212      94.288  30.655 -10.435  0.50  2.33           C  
ATOM   1399  C   VAL A 212      94.817  31.731 -11.376  0.50  2.46           C  
ATOM   1400  O   VAL A 212      95.962  31.673 -11.809  0.50  4.05           O  
ATOM   1401  CB  VAL A 212      93.181  29.879 -11.185  0.50  2.39           C  
ATOM   1402  CG1 VAL A 212      93.721  29.392 -12.518  0.50  2.83           C  
ATOM   1403  CG2 VAL A 212      92.696  28.698 -10.359  0.50  2.54           C  
ATOM   1404  N   THR A 213      93.962  32.702 -11.688  0.50  2.29           N  
ATOM   1405  CA  THR A 213      94.295  33.825 -12.563  0.50  3.40           C  
ATOM   1406  C   THR A 213      95.522  34.592 -12.066  0.50  2.59           C  
ATOM   1407  O   THR A 213      96.422  34.912 -12.839  0.50  1.91           O  
ATOM   1408  CB  THR A 213      93.103  34.801 -12.651  0.50  4.57           C  
ATOM   1409  OG1 THR A 213      92.042  34.184 -13.383  0.50  6.70           O  
ATOM   1410  CG2 THR A 213      93.500  36.086 -13.340  0.50  4.84           C  
ATOM   1411  N   GLY A 214      95.559  34.891 -10.775  0.50  1.96           N  
ATOM   1412  CA  GLY A 214      96.699  35.620 -10.243  0.50  2.41           C  
ATOM   1413  C   GLY A 214      97.999  34.859 -10.392  0.50  2.85           C  
ATOM   1414  O   GLY A 214      99.023  35.402 -10.808  0.50  2.50           O  
ATOM   1415  N   CYS A 215      97.955  33.580 -10.057  0.50  2.88           N  
ATOM   1416  CA  CYS A 215      99.133  32.732 -10.125  0.50  3.41           C  
ATOM   1417  C   CYS A 215      99.690  32.573 -11.545  0.50  3.33           C  
ATOM   1418  O   CYS A 215     100.903  32.577 -11.745  0.50  1.22           O  
ATOM   1419  CB  CYS A 215      98.797  31.351  -9.541  0.50  2.18           C  
ATOM   1420  SG  CYS A 215     100.248  30.384  -9.077  0.50  1.24           S  
ATOM   1421  N   ALA A 216      98.792  32.426 -12.518  0.50  4.37           N  
ATOM   1422  CA  ALA A 216      99.172  32.246 -13.911  0.50  5.92           C  
ATOM   1423  C   ALA A 216      99.736  33.518 -14.517  0.50  7.43           C  
ATOM   1424  O   ALA A 216     100.477  33.477 -15.501  0.50  6.62           O  
ATOM   1425  CB  ALA A 216      97.975  31.795 -14.711  0.50  5.71           C  
ATOM   1426  N   GLU A 217      99.378  34.642 -13.915  0.50  7.88           N  
ATOM   1427  CA  GLU A 217      99.801  35.958 -14.376  0.50 11.20           C  
ATOM   1428  C   GLU A 217     101.300  36.187 -14.375  0.50 11.46           C  
ATOM   1429  O   GLU A 217     101.872  36.678 -15.350  0.50 11.98           O  
ATOM   1430  CB  GLU A 217      99.153  37.020 -13.504  0.50 12.51           C  
ATOM   1431  CG  GLU A 217      98.937  38.337 -14.186  0.50 16.65           C  
ATOM   1432  CD  GLU A 217      97.970  39.202 -13.412  0.50 18.04           C  
ATOM   1433  OE1 GLU A 217      98.394  39.814 -12.410  0.50 19.15           O  
ATOM   1434  OE2 GLU A 217      96.779  39.246 -13.797  0.50 20.67           O  
ATOM   1435  N   THR A 218     101.948  35.821 -13.282  0.50 11.71           N  
ATOM   1436  CA  THR A 218     103.368  36.051 -13.187  0.50 12.25           C  
ATOM   1437  C   THR A 218     104.167  34.874 -12.633  0.50 11.29           C  
ATOM   1438  O   THR A 218     103.847  34.336 -11.571  0.50 11.68           O  
ATOM   1439  CB  THR A 218     103.608  37.322 -12.345  0.50 14.21           C  
ATOM   1440  OG1 THR A 218     104.966  37.366 -11.891  0.50 15.07           O  
ATOM   1441  CG2 THR A 218     102.667  37.347 -11.157  0.50 15.63           C  
ATOM   1442  N   PRO A 219     105.217  34.453 -13.365  0.50  9.68           N  
ATOM   1443  CA  PRO A 219     106.088  33.341 -12.974  0.50  8.12           C  
ATOM   1444  C   PRO A 219     106.647  33.602 -11.587  0.50  6.28           C  
ATOM   1445  O   PRO A 219     107.031  34.727 -11.280  0.50  5.65           O  
ATOM   1446  CB  PRO A 219     107.176  33.361 -14.043  0.50  8.15           C  
ATOM   1447  CG  PRO A 219     106.429  33.872 -15.258  0.50  8.81           C  
ATOM   1448  CD  PRO A 219     105.616  34.999 -14.678  0.50  9.15           C  
ATOM   1449  N   GLY A 220     106.674  32.565 -10.755  0.50  4.88           N  
ATOM   1450  CA  GLY A 220     107.172  32.702  -9.396  0.50  4.67           C  
ATOM   1451  C   GLY A 220     106.079  32.721  -8.337  0.50  3.02           C  
ATOM   1452  O   GLY A 220     106.362  32.629  -7.148  0.50  3.71           O  
ATOM   1453  N   CYS A 221     104.826  32.835  -8.760  0.50  3.42           N  
ATOM   1454  CA  CYS A 221     103.704  32.866  -7.826  0.50  4.56           C  
ATOM   1455  C   CYS A 221     103.426  31.512  -7.182  0.50  4.44           C  
ATOM   1456  O   CYS A 221     103.667  30.470  -7.785  0.50  4.18           O  
ATOM   1457  CB  CYS A 221     102.443  33.340  -8.546  0.50  3.90           C  
ATOM   1458  SG  CYS A 221     102.430  35.099  -8.890  0.50  6.82           S  
ATOM   1459  N   VAL A 222     102.911  31.542  -5.955  0.50  4.44           N  
ATOM   1460  CA  VAL A 222     102.555  30.341  -5.209  0.50  4.50           C  
ATOM   1461  C   VAL A 222     101.139  30.600  -4.720  0.50  4.01           C  
ATOM   1462  O   VAL A 222     100.840  31.715  -4.294  0.50  3.64           O  
ATOM   1463  CB  VAL A 222     103.445  30.149  -3.960  0.50  5.66           C  
ATOM   1464  CG1 VAL A 222     103.371  28.696  -3.471  0.50  6.71           C  
ATOM   1465  CG2 VAL A 222     104.847  30.541  -4.271  0.50  9.33           C  
ATOM   1466  N   ALA A 223     100.268  29.596  -4.779  0.50  2.66           N  
ATOM   1467  CA  ALA A 223      98.896  29.791  -4.321  0.50  3.12           C  
ATOM   1468  C   ALA A 223      98.236  28.518  -3.843  0.50  2.31           C  
ATOM   1469  O   ALA A 223      98.438  27.457  -4.427  0.50  3.03           O  
ATOM   1470  CB  ALA A 223      98.046  30.396  -5.440  0.50  1.22           C  
ATOM   1471  N   TYR A 224      97.443  28.632  -2.779  0.50  2.13           N  
ATOM   1472  CA  TYR A 224      96.695  27.495  -2.265  0.50  1.97           C  
ATOM   1473  C   TYR A 224      95.352  27.604  -2.988  0.50  2.07           C  
ATOM   1474  O   TYR A 224      94.698  28.659  -2.969  0.50  2.89           O  
ATOM   1475  CB  TYR A 224      96.566  27.566  -0.733  0.50  1.22           C  
ATOM   1476  CG  TYR A 224      96.076  28.884  -0.157  0.50  2.70           C  
ATOM   1477  CD1 TYR A 224      94.720  29.125   0.040  0.50  1.22           C  
ATOM   1478  CD2 TYR A 224      96.979  29.877   0.220  0.50  2.05           C  
ATOM   1479  CE1 TYR A 224      94.275  30.323   0.604  0.50  2.02           C  
ATOM   1480  CE2 TYR A 224      96.543  31.077   0.782  0.50  2.53           C  
ATOM   1481  CZ  TYR A 224      95.197  31.295   0.971  0.50  2.48           C  
ATOM   1482  OH  TYR A 224      94.777  32.479   1.529  0.50  1.22           O  
ATOM   1483  N   ILE A 225      94.966  26.521  -3.654  0.50  1.22           N  
ATOM   1484  CA  ILE A 225      93.753  26.490  -4.471  0.50  2.24           C  
ATOM   1485  C   ILE A 225      92.970  25.194  -4.284  0.50  1.22           C  
ATOM   1486  O   ILE A 225      93.559  24.113  -4.272  0.50  1.22           O  
ATOM   1487  CB  ILE A 225      94.127  26.600  -5.972  0.50  1.22           C  
ATOM   1488  CG1 ILE A 225      95.012  27.828  -6.200  0.50  4.13           C  
ATOM   1489  CG2 ILE A 225      92.868  26.645  -6.833  0.50  1.25           C  
ATOM   1490  CD1 ILE A 225      95.418  28.030  -7.650  0.50  3.01           C  
ATOM   1491  N   GLY A 226      91.647  25.315  -4.156  0.50  1.71           N  
ATOM   1492  CA  GLY A 226      90.779  24.157  -3.973  0.50  1.22           C  
ATOM   1493  C   GLY A 226      90.832  23.145  -5.115  0.50  1.53           C  
ATOM   1494  O   GLY A 226      90.976  23.525  -6.279  0.50  3.40           O  
ATOM   1495  N   ILE A 227      90.680  21.863  -4.789  0.50  1.64           N  
ATOM   1496  CA  ILE A 227      90.756  20.796  -5.784  0.50  2.87           C  
ATOM   1497  C   ILE A 227      89.751  20.869  -6.951  0.50  2.58           C  
ATOM   1498  O   ILE A 227      90.019  20.345  -8.033  0.50  2.65           O  
ATOM   1499  CB  ILE A 227      90.669  19.399  -5.094  0.50  2.74           C  
ATOM   1500  CG1 ILE A 227      91.006  18.291  -6.094  0.50  5.12           C  
ATOM   1501  CG2 ILE A 227      89.287  19.158  -4.535  0.50  1.42           C  
ATOM   1502  CD1 ILE A 227      92.472  18.048  -6.251  0.50  6.33           C  
ATOM   1503  N   SER A 228      88.604  21.509  -6.747  0.50  3.43           N  
ATOM   1504  CA  SER A 228      87.617  21.622  -7.822  0.50  5.35           C  
ATOM   1505  C   SER A 228      88.080  22.632  -8.881  0.50  5.85           C  
ATOM   1506  O   SER A 228      87.406  22.862  -9.884  0.50  4.86           O  
ATOM   1507  CB  SER A 228      86.254  22.035  -7.256  0.50  3.76           C  
ATOM   1508  OG  SER A 228      86.365  23.235  -6.527  0.50  6.86           O  
ATOM   1509  N   PHE A 229      89.233  23.243  -8.645  0.50  5.49           N  
ATOM   1510  CA  PHE A 229      89.787  24.185  -9.605  0.50  5.59           C  
ATOM   1511  C   PHE A 229      91.102  23.617 -10.148  0.50  5.35           C  
ATOM   1512  O   PHE A 229      91.855  24.301 -10.854  0.50  4.07           O  
ATOM   1513  CB  PHE A 229      90.033  25.543  -8.945  0.50  5.82           C  
ATOM   1514  CG  PHE A 229      88.785  26.341  -8.730  0.50  5.48           C  
ATOM   1515  CD1 PHE A 229      87.869  25.977  -7.755  0.50  4.13           C  
ATOM   1516  CD2 PHE A 229      88.509  27.445  -9.533  0.50  6.16           C  
ATOM   1517  CE1 PHE A 229      86.693  26.700  -7.586  0.50  6.78           C  
ATOM   1518  CE2 PHE A 229      87.327  28.177  -9.366  0.50  4.19           C  
ATOM   1519  CZ  PHE A 229      86.423  27.802  -8.394  0.50  4.70           C  
ATOM   1520  N   LEU A 230      91.364  22.358  -9.815  0.50  4.54           N  
ATOM   1521  CA  LEU A 230      92.579  21.691 -10.249  0.50  6.15           C  
ATOM   1522  C   LEU A 230      92.679  21.692 -11.768  0.50  6.20           C  
ATOM   1523  O   LEU A 230      93.706  22.065 -12.330  0.50  6.77           O  
ATOM   1524  CB  LEU A 230      92.610  20.252  -9.720  0.50  5.19           C  
ATOM   1525  CG  LEU A 230      93.798  19.380 -10.139  0.50  4.17           C  
ATOM   1526  CD1 LEU A 230      95.064  20.046  -9.686  0.50  5.26           C  
ATOM   1527  CD2 LEU A 230      93.681  17.983  -9.540  0.50  3.01           C  
ATOM   1528  N   ASP A 231      91.607  21.293 -12.435  0.50  6.95           N  
ATOM   1529  CA  ASP A 231      91.615  21.242 -13.888  0.50  8.49           C  
ATOM   1530  C   ASP A 231      91.944  22.589 -14.499  0.50  7.91           C  
ATOM   1531  O   ASP A 231      92.766  22.667 -15.413  0.50  8.05           O  
ATOM   1532  CB  ASP A 231      90.270  20.761 -14.405  0.50 10.59           C  
ATOM   1533  CG  ASP A 231      89.914  19.382 -13.896  0.50 12.98           C  
ATOM   1534  OD1 ASP A 231      90.810  18.668 -13.395  0.50 14.18           O  
ATOM   1535  OD2 ASP A 231      88.727  19.010 -14.009  0.50 16.69           O  
ATOM   1536  N   GLN A 232      91.308  23.647 -14.001  0.50  8.25           N  
ATOM   1537  CA  GLN A 232      91.566  24.996 -14.508  0.50  9.47           C  
ATOM   1538  C   GLN A 232      93.022  25.384 -14.321  0.50  8.25           C  
ATOM   1539  O   GLN A 232      93.661  25.892 -15.244  0.50  9.19           O  
ATOM   1540  CB  GLN A 232      90.687  26.034 -13.801  0.50 13.10           C  
ATOM   1541  CG  GLN A 232      89.277  26.132 -14.341  0.50 19.22           C  
ATOM   1542  CD  GLN A 232      88.239  25.542 -13.402  0.50 22.51           C  
ATOM   1543  OE1 GLN A 232      88.231  24.330 -13.131  0.50 26.29           O  
ATOM   1544  NE2 GLN A 232      87.354  26.398 -12.896  0.50 22.81           N  
ATOM   1545  N   ALA A 233      93.550  25.138 -13.127  0.50  6.51           N  
ATOM   1546  CA  ALA A 233      94.935  25.474 -12.825  0.50  5.92           C  
ATOM   1547  C   ALA A 233      95.888  24.807 -13.815  0.50  6.83           C  
ATOM   1548  O   ALA A 233      96.797  25.448 -14.337  0.50  6.68           O  
ATOM   1549  CB  ALA A 233      95.278  25.059 -11.398  0.50  3.90           C  
ATOM   1550  N   SER A 234      95.671  23.520 -14.076  0.50  8.38           N  
ATOM   1551  CA  SER A 234      96.508  22.772 -15.008  0.50  9.90           C  
ATOM   1552  C   SER A 234      96.430  23.363 -16.404  0.50 12.07           C  
ATOM   1553  O   SER A 234      97.456  23.572 -17.051  0.50 12.19           O  
ATOM   1554  CB  SER A 234      96.071  21.311 -15.061  0.50  9.42           C  
ATOM   1555  OG  SER A 234      96.232  20.697 -13.799  0.50 12.65           O  
ATOM   1556  N   GLN A 235      95.205  23.625 -16.861  0.50 14.20           N  
ATOM   1557  CA  GLN A 235      94.977  24.197 -18.178  0.50 15.83           C  
ATOM   1558  C   GLN A 235      95.712  25.515 -18.345  0.50 15.63           C  
ATOM   1559  O   GLN A 235      96.061  25.895 -19.456  0.50 15.64           O  
ATOM   1560  CB  GLN A 235      93.484  24.391 -18.401  0.50 18.20           C  
ATOM   1561  CG  GLN A 235      92.753  23.077 -18.640  0.50 23.85           C  
ATOM   1562  CD  GLN A 235      91.255  23.259 -18.725  0.50 27.48           C  
ATOM   1563  OE1 GLN A 235      90.756  24.035 -19.544  0.50 29.23           O  
ATOM   1564  NE2 GLN A 235      90.523  22.545 -17.873  0.50 29.68           N  
ATOM   1565  N   ARG A 236      95.943  26.214 -17.241  0.50 15.97           N  
ATOM   1566  CA  ARG A 236      96.661  27.479 -17.299  0.50 16.71           C  
ATOM   1567  C   ARG A 236      98.154  27.229 -17.281  0.50 14.47           C  
ATOM   1568  O   ARG A 236      98.937  28.163 -17.343  0.50 14.40           O  
ATOM   1569  CB  ARG A 236      96.289  28.394 -16.120  0.50 19.92           C  
ATOM   1570  CG  ARG A 236      94.917  29.032 -16.237  0.50 24.95           C  
ATOM   1571  CD  ARG A 236      94.726  29.717 -17.577  0.50 29.30           C  
ATOM   1572  NE  ARG A 236      93.406  30.313 -17.665  0.50 35.05           N  
ATOM   1573  CZ  ARG A 236      93.056  31.431 -17.045  0.50 38.06           C  
ATOM   1574  NH1 ARG A 236      93.943  32.099 -16.322  0.50 39.06           N  
ATOM   1575  NH2 ARG A 236      91.825  31.908 -17.169  0.50 39.37           N  
ATOM   1576  N   GLY A 237      98.539  25.965 -17.171  0.50 12.40           N  
ATOM   1577  CA  GLY A 237      99.949  25.615 -17.155  0.50 11.03           C  
ATOM   1578  C   GLY A 237     100.654  25.755 -15.816  0.50  9.38           C  
ATOM   1579  O   GLY A 237     101.873  25.896 -15.769  0.50 10.20           O  
ATOM   1580  N   LEU A 238      99.896  25.719 -14.727  0.50  8.20           N  
ATOM   1581  CA  LEU A 238     100.479  25.841 -13.399  0.50  6.05           C  
ATOM   1582  C   LEU A 238     101.017  24.489 -12.914  0.50  5.66           C  
ATOM   1583  O   LEU A 238     100.462  23.436 -13.243  0.50  4.55           O  
ATOM   1584  CB  LEU A 238      99.423  26.348 -12.411  0.50  5.37           C  
ATOM   1585  CG  LEU A 238      98.735  27.670 -12.768  0.50  5.15           C  
ATOM   1586  CD1 LEU A 238      97.726  28.017 -11.687  0.50  5.07           C  
ATOM   1587  CD2 LEU A 238      99.770  28.778 -12.909  0.50  3.72           C  
ATOM   1588  N   GLY A 239     102.100  24.524 -12.136  0.50  4.22           N  
ATOM   1589  CA  GLY A 239     102.650  23.297 -11.592  0.50  4.81           C  
ATOM   1590  C   GLY A 239     101.823  22.899 -10.378  0.50  4.23           C  
ATOM   1591  O   GLY A 239     101.069  23.714  -9.840  0.50  3.75           O  
ATOM   1592  N   GLU A 240     101.943  21.651  -9.946  0.50  4.43           N  
ATOM   1593  CA  GLU A 240     101.196  21.176  -8.785  0.50  4.80           C  
ATOM   1594  C   GLU A 240     102.178  20.484  -7.862  0.50  4.19           C  
ATOM   1595  O   GLU A 240     102.849  19.527  -8.253  0.50  3.58           O  
ATOM   1596  CB  GLU A 240     100.106  20.198  -9.212  0.50  5.73           C  
ATOM   1597  CG  GLU A 240      99.169  19.769  -8.088  0.50  5.71           C  
ATOM   1598  CD  GLU A 240      98.333  18.568  -8.490  0.50  8.34           C  
ATOM   1599  OE1 GLU A 240      98.518  18.082  -9.629  0.50  7.94           O  
ATOM   1600  OE2 GLU A 240      97.499  18.104  -7.674  0.50  9.28           O  
ATOM   1601  N   ALA A 241     102.260  20.971  -6.631  0.50  2.44           N  
ATOM   1602  CA  ALA A 241     103.199  20.417  -5.665  0.50  3.49           C  
ATOM   1603  C   ALA A 241     102.777  19.125  -5.001  0.50  3.14           C  
ATOM   1604  O   ALA A 241     101.592  18.829  -4.883  0.50  4.31           O  
ATOM   1605  CB  ALA A 241     103.500  21.456  -4.571  0.50  1.49           C  
ATOM   1606  N   GLN A 242     103.788  18.364  -4.586  0.50  3.43           N  
ATOM   1607  CA  GLN A 242     103.630  17.126  -3.840  0.50  2.76           C  
ATOM   1608  C   GLN A 242     103.850  17.675  -2.444  0.50  2.34           C  
ATOM   1609  O   GLN A 242     104.881  18.297  -2.201  0.50  2.19           O  
ATOM   1610  CB  GLN A 242     104.769  16.146  -4.141  0.50  3.71           C  
ATOM   1611  CG  GLN A 242     104.651  15.358  -5.418  0.50  4.61           C  
ATOM   1612  CD  GLN A 242     105.796  14.376  -5.573  0.50  5.02           C  
ATOM   1613  OE1 GLN A 242     106.860  14.719  -6.078  0.50  6.08           O  
ATOM   1614  NE2 GLN A 242     105.587  13.154  -5.111  0.50  5.52           N  
ATOM   1615  N   LEU A 243     102.908  17.470  -1.532  0.50  1.43           N  
ATOM   1616  CA  LEU A 243     103.066  18.003  -0.175  0.50  3.02           C  
ATOM   1617  C   LEU A 243     103.447  16.932   0.813  0.50  2.03           C  
ATOM   1618  O   LEU A 243     102.896  15.831   0.782  0.50  2.90           O  
ATOM   1619  CB  LEU A 243     101.778  18.688   0.299  0.50  2.67           C  
ATOM   1620  CG  LEU A 243     101.381  19.985  -0.410  0.50  3.54           C  
ATOM   1621  CD1 LEU A 243     100.168  20.588   0.277  0.50  1.23           C  
ATOM   1622  CD2 LEU A 243     102.547  20.960  -0.388  0.50  1.86           C  
ATOM   1623  N   GLY A 244     104.383  17.253   1.701  0.50  1.62           N  
ATOM   1624  CA  GLY A 244     104.816  16.268   2.675  0.50  2.56           C  
ATOM   1625  C   GLY A 244     103.838  16.087   3.819  0.50  3.36           C  
ATOM   1626  O   GLY A 244     103.292  17.076   4.330  0.50  3.60           O  
ATOM   1627  N   ASN A 245     103.601  14.837   4.220  0.50  3.34           N  
ATOM   1628  CA  ASN A 245     102.701  14.571   5.345  0.50  4.04           C  
ATOM   1629  C   ASN A 245     103.581  14.275   6.560  0.50  4.05           C  
ATOM   1630  O   ASN A 245     104.803  14.309   6.447  0.50  5.34           O  
ATOM   1631  CB  ASN A 245     101.722  13.414   5.045  0.50  1.22           C  
ATOM   1632  CG  ASN A 245     102.409  12.059   4.850  0.50  2.98           C  
ATOM   1633  OD1 ASN A 245     103.535  11.838   5.299  0.50  3.80           O  
ATOM   1634  ND2 ASN A 245     101.710  11.136   4.192  0.50  1.22           N  
ATOM   1635  N   SER A 246     102.980  14.002   7.715  0.50  5.69           N  
ATOM   1636  CA  SER A 246     103.757  13.766   8.928  0.50  7.76           C  
ATOM   1637  C   SER A 246     104.556  12.462   8.940  0.50  9.33           C  
ATOM   1638  O   SER A 246     105.452  12.294   9.761  0.50 10.67           O  
ATOM   1639  CB  SER A 246     102.853  13.859  10.170  0.50  7.34           C  
ATOM   1640  OG  SER A 246     101.722  13.011  10.067  0.50  9.84           O  
ATOM   1641  N   SER A 247     104.254  11.553   8.024  0.50  9.36           N  
ATOM   1642  CA  SER A 247     104.982  10.293   7.954  0.50  9.82           C  
ATOM   1643  C   SER A 247     106.196  10.414   7.034  0.50 10.02           C  
ATOM   1644  O   SER A 247     106.851   9.418   6.719  0.50  9.97           O  
ATOM   1645  CB  SER A 247     104.061   9.176   7.455  0.50  8.88           C  
ATOM   1646  OG  SER A 247     103.042   8.899   8.405  0.50 10.78           O  
ATOM   1647  N   GLY A 248     106.491  11.632   6.589  0.50 10.33           N  
ATOM   1648  CA  GLY A 248     107.639  11.830   5.716  0.50 10.76           C  
ATOM   1649  C   GLY A 248     107.377  11.575   4.241  0.50 11.02           C  
ATOM   1650  O   GLY A 248     108.287  11.646   3.418  0.50 10.96           O  
ATOM   1651  N   ASN A 249     106.130  11.277   3.904  0.50 10.37           N  
ATOM   1652  CA  ASN A 249     105.747  11.021   2.521  0.50 10.68           C  
ATOM   1653  C   ASN A 249     105.312  12.300   1.823  0.50  8.94           C  
ATOM   1654  O   ASN A 249     104.794  13.207   2.456  0.50  8.85           O  
ATOM   1655  CB  ASN A 249     104.585  10.025   2.484  0.50 11.95           C  
ATOM   1656  CG  ASN A 249     105.045   8.582   2.442  0.50 15.60           C  
ATOM   1657  OD1 ASN A 249     106.109   8.229   2.971  0.50 15.49           O  
ATOM   1658  ND2 ASN A 249     104.232   7.727   1.814  0.50 15.76           N  
ATOM   1659  N   PHE A 250     105.508  12.357   0.511  0.50  8.36           N  
ATOM   1660  CA  PHE A 250     105.102  13.511  -0.276  0.50  8.68           C  
ATOM   1661  C   PHE A 250     104.063  13.006  -1.255  0.50  9.29           C  
ATOM   1662  O   PHE A 250     104.361  12.124  -2.059  0.50  9.94           O  
ATOM   1663  CB  PHE A 250     106.293  14.105  -1.015  0.50  7.04           C  
ATOM   1664  CG  PHE A 250     107.271  14.800  -0.109  0.50  8.50           C  
ATOM   1665  CD1 PHE A 250     108.212  14.075   0.613  0.50  7.30           C  
ATOM   1666  CD2 PHE A 250     107.213  16.182   0.064  0.50  6.84           C  
ATOM   1667  CE1 PHE A 250     109.076  14.714   1.494  0.50  7.86           C  
ATOM   1668  CE2 PHE A 250     108.073  16.830   0.944  0.50  5.72           C  
ATOM   1669  CZ  PHE A 250     109.006  16.097   1.662  0.50  6.37           C  
ATOM   1670  N   LEU A 251     102.848  13.551  -1.171  0.50  8.30           N  
ATOM   1671  CA  LEU A 251     101.742  13.113  -2.019  0.50  7.20           C  
ATOM   1672  C   LEU A 251     101.029  14.197  -2.824  0.50  6.52           C  
ATOM   1673  O   LEU A 251     101.015  15.371  -2.459  0.50  5.13           O  
ATOM   1674  CB  LEU A 251     100.677  12.404  -1.173  0.50  7.77           C  
ATOM   1675  CG  LEU A 251     100.943  11.165  -0.306  0.50  8.63           C  
ATOM   1676  CD1 LEU A 251     101.796  10.173  -1.073  0.50  8.73           C  
ATOM   1677  CD2 LEU A 251     101.627  11.575   0.981  0.50 11.18           C  
ATOM   1678  N   LEU A 252     100.417  13.758  -3.920  0.50  6.53           N  
ATOM   1679  CA  LEU A 252      99.625  14.598  -4.817  0.50  6.46           C  
ATOM   1680  C   LEU A 252      98.188  14.387  -4.351  0.50  5.94           C  
ATOM   1681  O   LEU A 252      97.863  13.343  -3.780  0.50  4.95           O  
ATOM   1682  CB  LEU A 252      99.726  14.078  -6.252  0.50  5.72           C  
ATOM   1683  CG  LEU A 252     100.403  14.867  -7.368  0.50  6.86           C  
ATOM   1684  CD1 LEU A 252     101.243  16.009  -6.814  0.50  6.60           C  
ATOM   1685  CD2 LEU A 252     101.258  13.898  -8.162  0.50  6.95           C  
ATOM   1686  N   PRO A 253      97.308  15.371  -4.572  0.50  5.93           N  
ATOM   1687  CA  PRO A 253      95.948  15.081  -4.110  0.50  6.41           C  
ATOM   1688  C   PRO A 253      95.183  14.316  -5.185  0.50  6.98           C  
ATOM   1689  O   PRO A 253      94.896  14.852  -6.255  0.50  8.08           O  
ATOM   1690  CB  PRO A 253      95.361  16.465  -3.872  0.50  5.35           C  
ATOM   1691  CG  PRO A 253      96.053  17.285  -4.919  0.50  4.28           C  
ATOM   1692  CD  PRO A 253      97.483  16.810  -4.812  0.50  4.34           C  
ATOM   1693  N   ASP A 254      94.884  13.051  -4.914  0.50  6.79           N  
ATOM   1694  CA  ASP A 254      94.113  12.240  -5.839  0.50  6.65           C  
ATOM   1695  C   ASP A 254      93.297  11.295  -4.987  0.50  5.95           C  
ATOM   1696  O   ASP A 254      93.466  11.263  -3.762  0.50  4.87           O  
ATOM   1697  CB  ASP A 254      95.005  11.461  -6.837  0.50  7.27           C  
ATOM   1698  CG  ASP A 254      96.013  10.539  -6.162  0.50  9.23           C  
ATOM   1699  OD1 ASP A 254      95.791  10.130  -5.007  0.50 11.05           O  
ATOM   1700  OD2 ASP A 254      97.035  10.203  -6.803  0.50 10.06           O  
ATOM   1701  N   ALA A 255      92.419  10.539  -5.637  0.50  5.01           N  
ATOM   1702  CA  ALA A 255      91.534   9.592  -4.979  0.50  6.22           C  
ATOM   1703  C   ALA A 255      92.255   8.744  -3.949  0.50  5.95           C  
ATOM   1704  O   ALA A 255      91.844   8.668  -2.796  0.50  5.43           O  
ATOM   1705  CB  ALA A 255      90.876   8.696  -6.019  0.50  6.50           C  
ATOM   1706  N   GLN A 256      93.338   8.116  -4.375  0.50  5.39           N  
ATOM   1707  CA  GLN A 256      94.124   7.262  -3.503  0.50  7.69           C  
ATOM   1708  C   GLN A 256      94.595   7.927  -2.216  0.50  4.98           C  
ATOM   1709  O   GLN A 256      94.345   7.426  -1.121  0.50  4.97           O  
ATOM   1710  CB  GLN A 256      95.342   6.739  -4.257  0.50 11.13           C  
ATOM   1711  CG  GLN A 256      95.144   5.394  -4.900  0.50 19.12           C  
ATOM   1712  CD  GLN A 256      96.151   4.388  -4.385  0.50 22.67           C  
ATOM   1713  OE1 GLN A 256      97.362   4.538  -4.594  0.50 23.26           O  
ATOM   1714  NE2 GLN A 256      95.660   3.361  -3.691  0.50 24.08           N  
ATOM   1715  N   SER A 257      95.289   9.048  -2.347  0.50  3.25           N  
ATOM   1716  CA  SER A 257      95.809   9.731  -1.171  0.50  3.88           C  
ATOM   1717  C   SER A 257      94.705  10.297  -0.278  0.50  3.25           C  
ATOM   1718  O   SER A 257      94.857  10.338   0.947  0.50  3.56           O  
ATOM   1719  CB  SER A 257      96.775  10.840  -1.589  0.50  3.29           C  
ATOM   1720  OG  SER A 257      96.142  11.788  -2.423  0.50  1.22           O  
ATOM   1721  N   ILE A 258      93.593  10.725  -0.873  0.50  2.98           N  
ATOM   1722  CA  ILE A 258      92.510  11.271  -0.058  0.50  3.85           C  
ATOM   1723  C   ILE A 258      91.724  10.159   0.631  0.50  3.00           C  
ATOM   1724  O   ILE A 258      91.297  10.315   1.775  0.50  1.27           O  
ATOM   1725  CB  ILE A 258      91.556  12.148  -0.886  0.50  5.01           C  
ATOM   1726  CG1 ILE A 258      90.376  12.593  -0.029  0.50  6.05           C  
ATOM   1727  CG2 ILE A 258      91.055  11.386  -2.079  0.50  9.05           C  
ATOM   1728  CD1 ILE A 258      89.457  13.552  -0.725  0.50 10.74           C  
ATOM   1729  N   GLN A 259      91.524   9.038  -0.058  0.50  1.22           N  
ATOM   1730  CA  GLN A 259      90.815   7.920   0.556  0.50  3.96           C  
ATOM   1731  C   GLN A 259      91.654   7.398   1.718  0.50  3.69           C  
ATOM   1732  O   GLN A 259      91.120   6.962   2.740  0.50  3.65           O  
ATOM   1733  CB  GLN A 259      90.576   6.813  -0.470  0.50  2.06           C  
ATOM   1734  CG  GLN A 259      89.480   7.173  -1.468  0.50  1.22           C  
ATOM   1735  CD  GLN A 259      89.433   6.242  -2.650  0.50  1.94           C  
ATOM   1736  OE1 GLN A 259      88.560   6.362  -3.508  0.50  3.70           O  
ATOM   1737  NE2 GLN A 259      90.369   5.311  -2.709  0.50  1.22           N  
ATOM   1738  N   ALA A 260      92.971   7.468   1.561  0.50  1.57           N  
ATOM   1739  CA  ALA A 260      93.894   7.012   2.592  0.50  2.27           C  
ATOM   1740  C   ALA A 260      93.927   7.983   3.782  0.50  2.01           C  
ATOM   1741  O   ALA A 260      94.004   7.558   4.930  0.50  1.69           O  
ATOM   1742  CB  ALA A 260      95.291   6.855   1.999  0.50  1.23           C  
ATOM   1743  N   ALA A 261      93.849   9.286   3.513  0.50  1.78           N  
ATOM   1744  CA  ALA A 261      93.882  10.270   4.594  0.50  2.61           C  
ATOM   1745  C   ALA A 261      92.588  10.256   5.404  0.50  2.56           C  
ATOM   1746  O   ALA A 261      92.603  10.450   6.626  0.50  1.83           O  
ATOM   1747  CB  ALA A 261      94.129  11.663   4.027  0.50  1.22           C  
ATOM   1748  N   ALA A 262      91.469  10.026   4.718  0.50  1.22           N  
ATOM   1749  CA  ALA A 262      90.158   9.991   5.356  0.50  3.52           C  
ATOM   1750  C   ALA A 262      90.007   8.795   6.319  0.50  4.63           C  
ATOM   1751  O   ALA A 262      89.307   8.884   7.337  0.50  3.75           O  
ATOM   1752  CB  ALA A 262      89.065   9.959   4.284  0.50  1.37           C  
ATOM   1753  N   ALA A 263      90.665   7.685   6.005  0.50  4.83           N  
ATOM   1754  CA  ALA A 263      90.593   6.500   6.855  0.50  7.16           C  
ATOM   1755  C   ALA A 263      91.053   6.852   8.257  0.50  8.28           C  
ATOM   1756  O   ALA A 263      90.666   6.213   9.222  0.50  8.46           O  
ATOM   1757  CB  ALA A 263      91.464   5.390   6.293  0.50  6.27           C  
ATOM   1758  N   GLY A 264      91.880   7.886   8.362  0.50  9.35           N  
ATOM   1759  CA  GLY A 264      92.380   8.291   9.656  0.50 11.03           C  
ATOM   1760  C   GLY A 264      91.327   8.917  10.550  0.50 11.55           C  
ATOM   1761  O   GLY A 264      91.473   8.918  11.772  0.50 12.44           O  
ATOM   1762  N   PHE A 265      90.253   9.435   9.962  0.50 10.82           N  
ATOM   1763  CA  PHE A 265      89.226  10.078  10.772  0.50 11.19           C  
ATOM   1764  C   PHE A 265      87.809   9.547  10.611  0.50 11.41           C  
ATOM   1765  O   PHE A 265      86.884  10.093  11.212  0.50 14.11           O  
ATOM   1766  CB  PHE A 265      89.224  11.584  10.509  0.50  7.72           C  
ATOM   1767  CG  PHE A 265      90.582  12.214  10.581  0.50  6.93           C  
ATOM   1768  CD1 PHE A 265      91.408  12.233   9.464  0.50  5.19           C  
ATOM   1769  CD2 PHE A 265      91.034  12.792  11.764  0.50  6.28           C  
ATOM   1770  CE1 PHE A 265      92.665  12.818   9.520  0.50  7.40           C  
ATOM   1771  CE2 PHE A 265      92.288  13.379  11.837  0.50  7.22           C  
ATOM   1772  CZ  PHE A 265      93.110  13.394  10.711  0.50  6.86           C  
ATOM   1773  N   ALA A 266      87.634   8.488   9.824  0.50 11.56           N  
ATOM   1774  CA  ALA A 266      86.308   7.907   9.595  0.50 12.50           C  
ATOM   1775  C   ALA A 266      85.574   7.469  10.867  0.50 12.55           C  
ATOM   1776  O   ALA A 266      84.347   7.552  10.937  0.50 12.90           O  
ATOM   1777  CB  ALA A 266      86.411   6.731   8.640  0.50 11.82           C  
ATOM   1778  N   SER A 267      86.315   6.991  11.861  0.50 12.46           N  
ATOM   1779  CA  SER A 267      85.711   6.552  13.115  0.50 13.12           C  
ATOM   1780  C   SER A 267      85.931   7.562  14.231  0.50 11.75           C  
ATOM   1781  O   SER A 267      85.521   7.331  15.364  0.50 12.79           O  
ATOM   1782  CB  SER A 267      86.303   5.212  13.558  0.50 14.78           C  
ATOM   1783  OG  SER A 267      86.029   4.179  12.624  0.50 21.21           O  
ATOM   1784  N   LYS A 268      86.574   8.677  13.915  0.50  9.77           N  
ATOM   1785  CA  LYS A 268      86.867   9.688  14.919  0.50  9.03           C  
ATOM   1786  C   LYS A 268      86.140  11.015  14.725  0.50  6.44           C  
ATOM   1787  O   LYS A 268      86.557  12.022  15.281  0.50  5.98           O  
ATOM   1788  CB  LYS A 268      88.379   9.958  14.964  0.50 11.97           C  
ATOM   1789  CG  LYS A 268      89.238   8.713  15.114  0.50 16.64           C  
ATOM   1790  CD  LYS A 268      90.698   8.991  14.744  0.50 20.14           C  
ATOM   1791  CE  LYS A 268      91.516   7.692  14.706  0.50 22.95           C  
ATOM   1792  NZ  LYS A 268      92.926   7.899  14.230  0.50 23.93           N  
ATOM   1793  N   THR A 269      85.064  11.035  13.946  0.50  4.52           N  
ATOM   1794  CA  THR A 269      84.326  12.283  13.744  0.50  4.58           C  
ATOM   1795  C   THR A 269      83.326  12.499  14.890  0.50  4.49           C  
ATOM   1796  O   THR A 269      82.510  11.625  15.182  0.50  6.28           O  
ATOM   1797  CB  THR A 269      83.553  12.272  12.393  0.50  3.34           C  
ATOM   1798  OG1 THR A 269      84.477  12.104  11.309  0.50  2.74           O  
ATOM   1799  CG2 THR A 269      82.807  13.586  12.193  0.50  2.91           C  
ATOM   1800  N   PRO A 270      83.378  13.669  15.550  0.50  4.83           N  
ATOM   1801  CA  PRO A 270      82.501  14.051  16.671  0.50  4.87           C  
ATOM   1802  C   PRO A 270      81.058  14.200  16.210  0.50  4.65           C  
ATOM   1803  O   PRO A 270      80.809  14.361  15.021  0.50  4.30           O  
ATOM   1804  CB  PRO A 270      83.056  15.406  17.112  0.50  4.49           C  
ATOM   1805  CG  PRO A 270      84.441  15.442  16.562  0.50  5.90           C  
ATOM   1806  CD  PRO A 270      84.317  14.757  15.237  0.50  4.07           C  
ATOM   1807  N   ALA A 271      80.112  14.182  17.149  0.50  5.76           N  
ATOM   1808  CA  ALA A 271      78.700  14.324  16.805  0.50  5.49           C  
ATOM   1809  C   ALA A 271      78.379  15.663  16.152  0.50  5.54           C  
ATOM   1810  O   ALA A 271      77.434  15.754  15.370  0.50  6.45           O  
ATOM   1811  CB  ALA A 271      77.828  14.143  18.044  0.50  6.98           C  
ATOM   1812  N   ASN A 272      79.136  16.707  16.469  0.50  5.34           N  
ATOM   1813  CA  ASN A 272      78.857  18.000  15.858  0.50  6.12           C  
ATOM   1814  C   ASN A 272      79.644  18.201  14.572  0.50  6.18           C  
ATOM   1815  O   ASN A 272      79.541  19.248  13.931  0.50  8.00           O  
ATOM   1816  CB  ASN A 272      79.129  19.142  16.833  0.50  7.25           C  
ATOM   1817  CG  ASN A 272      80.598  19.309  17.157  0.50  8.63           C  
ATOM   1818  OD1 ASN A 272      81.451  18.562  16.684  0.50 10.13           O  
ATOM   1819  ND2 ASN A 272      80.899  20.307  17.972  0.50  9.74           N  
ATOM   1820  N   GLN A 273      80.413  17.178  14.206  0.50  4.10           N  
ATOM   1821  CA  GLN A 273      81.228  17.142  12.985  0.50  3.96           C  
ATOM   1822  C   GLN A 273      82.301  18.202  12.789  0.50  3.06           C  
ATOM   1823  O   GLN A 273      82.852  18.332  11.691  0.50  4.11           O  
ATOM   1824  CB  GLN A 273      80.321  17.123  11.758  0.50  2.76           C  
ATOM   1825  CG  GLN A 273      79.416  15.920  11.705  0.50  1.22           C  
ATOM   1826  CD  GLN A 273      78.606  15.857  10.420  0.50  2.72           C  
ATOM   1827  OE1 GLN A 273      78.099  16.871   9.948  0.50  1.98           O  
ATOM   1828  NE2 GLN A 273      78.473  14.659   9.856  0.50  1.22           N  
ATOM   1829  N   ALA A 274      82.609  18.962  13.831  0.50  3.19           N  
ATOM   1830  CA  ALA A 274      83.647  19.978  13.708  0.50  3.61           C  
ATOM   1831  C   ALA A 274      84.954  19.253  13.988  0.50  4.49           C  
ATOM   1832  O   ALA A 274      85.299  18.963  15.137  0.50  5.04           O  
ATOM   1833  CB  ALA A 274      83.422  21.112  14.716  0.50  4.11           C  
ATOM   1834  N   ILE A 275      85.685  18.943  12.930  0.50  2.96           N  
ATOM   1835  CA  ILE A 275      86.924  18.224  13.092  0.50  4.12           C  
ATOM   1836  C   ILE A 275      87.894  18.598  11.984  0.50  3.78           C  
ATOM   1837  O   ILE A 275      87.518  18.756  10.824  0.50  4.47           O  
ATOM   1838  CB  ILE A 275      86.659  16.692  13.082  0.50  4.72           C  
ATOM   1839  CG1 ILE A 275      87.966  15.923  13.225  0.50  6.66           C  
ATOM   1840  CG2 ILE A 275      85.940  16.285  11.813  0.50  3.36           C  
ATOM   1841  CD1 ILE A 275      88.511  15.955  14.627  0.50  9.46           C  
ATOM   1842  N   SER A 276      89.148  18.770  12.358  0.50  2.27           N  
ATOM   1843  CA  SER A 276      90.165  19.094  11.398  0.50  3.10           C  
ATOM   1844  C   SER A 276      90.808  17.786  10.967  0.50  2.09           C  
ATOM   1845  O   SER A 276      91.224  16.995  11.801  0.50  1.60           O  
ATOM   1846  CB  SER A 276      91.204  20.006  12.036  0.50  2.10           C  
ATOM   1847  OG  SER A 276      92.298  20.208  11.161  0.50  4.88           O  
ATOM   1848  N   MET A 277      90.865  17.545   9.665  0.50  3.10           N  
ATOM   1849  CA  MET A 277      91.496  16.332   9.154  0.50  4.33           C  
ATOM   1850  C   MET A 277      92.812  16.688   8.474  0.50  3.39           C  
ATOM   1851  O   MET A 277      93.306  15.955   7.628  0.50  1.82           O  
ATOM   1852  CB  MET A 277      90.571  15.606   8.171  0.50  4.25           C  
ATOM   1853  CG  MET A 277      89.304  15.054   8.816  0.50  3.72           C  
ATOM   1854  SD  MET A 277      88.388  13.911   7.731  0.50  6.19           S  
ATOM   1855  CE  MET A 277      87.656  15.055   6.547  0.50  2.70           C  
ATOM   1856  N   ILE A 278      93.374  17.824   8.868  0.50  3.84           N  
ATOM   1857  CA  ILE A 278      94.627  18.306   8.312  0.50  5.30           C  
ATOM   1858  C   ILE A 278      95.817  17.539   8.885  0.50  7.03           C  
ATOM   1859  O   ILE A 278      95.842  17.204  10.073  0.50  5.79           O  
ATOM   1860  CB  ILE A 278      94.825  19.809   8.627  0.50  6.15           C  
ATOM   1861  CG1 ILE A 278      93.673  20.628   8.041  0.50  6.09           C  
ATOM   1862  CG2 ILE A 278      96.166  20.286   8.085  0.50  4.82           C  
ATOM   1863  CD1 ILE A 278      93.586  20.611   6.548  0.50  6.39           C  
ATOM   1864  N   ASP A 279      96.798  17.266   8.027  0.50  6.27           N  
ATOM   1865  CA  ASP A 279      98.023  16.562   8.403  0.50  6.15           C  
ATOM   1866  C   ASP A 279      97.822  15.352   9.312  0.50  5.15           C  
ATOM   1867  O   ASP A 279      98.412  15.267  10.389  0.50  2.92           O  
ATOM   1868  CB  ASP A 279      98.991  17.543   9.059  0.50  8.12           C  
ATOM   1869  CG  ASP A 279     100.419  17.017   9.101  0.50  9.79           C  
ATOM   1870  OD1 ASP A 279     100.774  16.149   8.268  0.50 12.74           O  
ATOM   1871  OD2 ASP A 279     101.191  17.483   9.963  0.50 11.69           O  
ATOM   1872  N   GLY A 280      97.005  14.409   8.847  0.50  4.68           N  
ATOM   1873  CA  GLY A 280      96.717  13.201   9.601  0.50  4.03           C  
ATOM   1874  C   GLY A 280      97.863  12.206   9.679  0.50  4.94           C  
ATOM   1875  O   GLY A 280      98.922  12.417   9.081  0.50  3.97           O  
ATOM   1876  N   PRO A 281      97.668  11.083  10.390  0.50  4.96           N  
ATOM   1877  CA  PRO A 281      98.718  10.076  10.534  0.50  6.13           C  
ATOM   1878  C   PRO A 281      98.823   9.017   9.438  0.50  5.76           C  
ATOM   1879  O   PRO A 281      99.787   8.258   9.405  0.50  7.01           O  
ATOM   1880  CB  PRO A 281      98.407   9.474  11.894  0.50  5.35           C  
ATOM   1881  CG  PRO A 281      96.914   9.442  11.881  0.50  5.44           C  
ATOM   1882  CD  PRO A 281      96.516  10.771  11.260  0.50  6.25           C  
ATOM   1883  N   ALA A 282      97.850   8.953   8.543  0.50  5.22           N  
ATOM   1884  CA  ALA A 282      97.915   7.948   7.489  0.50  5.50           C  
ATOM   1885  C   ALA A 282      99.207   8.126   6.676  0.50  4.70           C  
ATOM   1886  O   ALA A 282      99.432   9.161   6.049  0.50  5.33           O  
ATOM   1887  CB  ALA A 282      96.697   8.050   6.587  0.50  2.62           C  
ATOM   1888  N   PRO A 283     100.069   7.104   6.676  0.50  4.69           N  
ATOM   1889  CA  PRO A 283     101.347   7.131   5.948  0.50  5.49           C  
ATOM   1890  C   PRO A 283     101.206   7.581   4.496  0.50  3.74           C  
ATOM   1891  O   PRO A 283     102.011   8.366   3.991  0.50  2.48           O  
ATOM   1892  CB  PRO A 283     101.833   5.682   6.040  0.50  5.78           C  
ATOM   1893  CG  PRO A 283     101.174   5.174   7.303  0.50  6.30           C  
ATOM   1894  CD  PRO A 283      99.796   5.756   7.209  0.50  5.29           C  
ATOM   1895  N   ASP A 284     100.165   7.078   3.840  0.50  3.44           N  
ATOM   1896  CA  ASP A 284      99.896   7.374   2.431  0.50  3.61           C  
ATOM   1897  C   ASP A 284      98.842   8.431   2.200  0.50  3.07           C  
ATOM   1898  O   ASP A 284      98.374   8.586   1.067  0.50  1.56           O  
ATOM   1899  CB  ASP A 284      99.452   6.091   1.729  0.50  2.91           C  
ATOM   1900  CG  ASP A 284     100.489   5.004   1.839  0.50  1.22           C  
ATOM   1901  OD1 ASP A 284     101.667   5.314   1.584  0.50  1.22           O  
ATOM   1902  OD2 ASP A 284     100.138   3.859   2.184  0.50  1.66           O  
ATOM   1903  N   GLY A 285      98.473   9.158   3.254  0.50  1.80           N  
ATOM   1904  CA  GLY A 285      97.425  10.159   3.120  0.50  2.14           C  
ATOM   1905  C   GLY A 285      97.845  11.583   2.813  0.50  2.00           C  
ATOM   1906  O   GLY A 285      98.844  12.073   3.339  0.50  1.22           O  
ATOM   1907  N   TYR A 286      97.069  12.244   1.953  0.50  2.30           N  
ATOM   1908  CA  TYR A 286      97.321  13.630   1.562  0.50  2.19           C  
ATOM   1909  C   TYR A 286      97.098  14.500   2.810  0.50  2.07           C  
ATOM   1910  O   TYR A 286      96.141  14.294   3.553  0.50  2.73           O  
ATOM   1911  CB  TYR A 286      96.361  14.032   0.434  0.50  1.22           C  
ATOM   1912  CG  TYR A 286      96.674  15.388  -0.155  0.50  2.89           C  
ATOM   1913  CD1 TYR A 286      97.808  15.582  -0.945  0.50  1.22           C  
ATOM   1914  CD2 TYR A 286      95.868  16.489   0.122  0.50  1.22           C  
ATOM   1915  CE1 TYR A 286      98.131  16.839  -1.437  0.50  1.98           C  
ATOM   1916  CE2 TYR A 286      96.180  17.738  -0.366  0.50  2.34           C  
ATOM   1917  CZ  TYR A 286      97.313  17.910  -1.145  0.50  1.22           C  
ATOM   1918  OH  TYR A 286      97.616  19.157  -1.634  0.50  2.50           O  
ATOM   1919  N   PRO A 287      97.969  15.489   3.049  0.50  1.22           N  
ATOM   1920  CA  PRO A 287      97.803  16.328   4.239  0.50  2.28           C  
ATOM   1921  C   PRO A 287      96.673  17.353   4.314  0.50  2.37           C  
ATOM   1922  O   PRO A 287      96.266  17.719   5.414  0.50  3.51           O  
ATOM   1923  CB  PRO A 287      99.189  16.958   4.408  0.50  1.22           C  
ATOM   1924  CG  PRO A 287      99.690  17.053   3.015  0.50  1.22           C  
ATOM   1925  CD  PRO A 287      99.261  15.752   2.390  0.50  1.22           C  
ATOM   1926  N   ILE A 288      96.155  17.825   3.182  0.50  2.46           N  
ATOM   1927  CA  ILE A 288      95.077  18.800   3.257  0.50  2.56           C  
ATOM   1928  C   ILE A 288      93.777  18.281   2.689  0.50  1.22           C  
ATOM   1929  O   ILE A 288      93.542  18.397   1.489  0.50  2.19           O  
ATOM   1930  CB  ILE A 288      95.364  20.113   2.489  0.50  3.49           C  
ATOM   1931  CG1 ILE A 288      96.861  20.386   2.396  0.50  7.36           C  
ATOM   1932  CG2 ILE A 288      94.638  21.281   3.196  0.50  1.37           C  
ATOM   1933  CD1 ILE A 288      97.423  21.179   3.513  0.50  9.00           C  
ATOM   1934  N   ILE A 289      92.948  17.688   3.541  0.50  1.22           N  
ATOM   1935  CA  ILE A 289      91.635  17.211   3.128  0.50  1.38           C  
ATOM   1936  C   ILE A 289      90.694  17.816   4.145  0.50  2.24           C  
ATOM   1937  O   ILE A 289      91.126  18.257   5.211  0.50  1.22           O  
ATOM   1938  CB  ILE A 289      91.487  15.653   3.140  0.50  4.67           C  
ATOM   1939  CG1 ILE A 289      91.725  15.088   4.544  0.50  4.76           C  
ATOM   1940  CG2 ILE A 289      92.442  15.030   2.121  0.50  2.83           C  
ATOM   1941  CD1 ILE A 289      91.333  13.605   4.671  0.50  5.10           C  
ATOM   1942  N   ASN A 290      89.409  17.839   3.826  0.50  1.70           N  
ATOM   1943  CA  ASN A 290      88.446  18.441   4.720  0.50  1.95           C  
ATOM   1944  C   ASN A 290      87.046  18.041   4.304  0.50  1.22           C  
ATOM   1945  O   ASN A 290      86.815  17.626   3.173  0.50  1.72           O  
ATOM   1946  CB  ASN A 290      88.541  19.957   4.596  0.50  1.22           C  
ATOM   1947  CG  ASN A 290      87.984  20.460   3.265  0.50  1.45           C  
ATOM   1948  OD1 ASN A 290      88.601  20.297   2.202  0.50  1.69           O  
ATOM   1949  ND2 ASN A 290      86.793  21.059   3.318  0.50  4.42           N  
ATOM   1950  N   TYR A 291      86.116  18.183   5.233  0.50  2.66           N  
ATOM   1951  CA  TYR A 291      84.714  17.938   4.952  0.50  2.62           C  
ATOM   1952  C   TYR A 291      84.188  19.251   4.377  0.50  2.11           C  
ATOM   1953  O   TYR A 291      84.643  20.323   4.770  0.50  2.31           O  
ATOM   1954  CB  TYR A 291      83.946  17.674   6.239  0.50  1.22           C  
ATOM   1955  CG  TYR A 291      84.164  16.312   6.833  0.50  2.77           C  
ATOM   1956  CD1 TYR A 291      83.963  15.162   6.070  0.50  1.22           C  
ATOM   1957  CD2 TYR A 291      84.560  16.172   8.163  0.50  1.22           C  
ATOM   1958  CE1 TYR A 291      84.153  13.910   6.611  0.50  2.86           C  
ATOM   1959  CE2 TYR A 291      84.749  14.922   8.720  0.50  2.25           C  
ATOM   1960  CZ  TYR A 291      84.545  13.795   7.937  0.50  2.44           C  
ATOM   1961  OH  TYR A 291      84.753  12.558   8.479  0.50  3.31           O  
ATOM   1962  N   GLU A 292      83.261  19.182   3.438  0.50  1.22           N  
ATOM   1963  CA  GLU A 292      82.653  20.396   2.915  0.50  2.17           C  
ATOM   1964  C   GLU A 292      81.408  20.494   3.783  0.50  2.72           C  
ATOM   1965  O   GLU A 292      80.721  19.497   3.996  0.50  1.22           O  
ATOM   1966  CB  GLU A 292      82.298  20.235   1.444  0.50  1.22           C  
ATOM   1967  CG  GLU A 292      83.525  20.231   0.558  0.50  1.22           C  
ATOM   1968  CD  GLU A 292      84.083  21.628   0.354  0.50  2.62           C  
ATOM   1969  OE1 GLU A 292      84.616  22.216   1.330  0.50  1.22           O  
ATOM   1970  OE2 GLU A 292      83.975  22.143  -0.783  0.50  1.22           O  
ATOM   1971  N   TYR A 293      81.131  21.688   4.291  0.50  1.98           N  
ATOM   1972  CA  TYR A 293      80.017  21.898   5.197  0.50  2.49           C  
ATOM   1973  C   TYR A 293      78.852  22.744   4.703  0.50  2.60           C  
ATOM   1974  O   TYR A 293      79.037  23.722   3.976  0.50  1.22           O  
ATOM   1975  CB  TYR A 293      80.541  22.563   6.475  0.50  1.85           C  
ATOM   1976  CG  TYR A 293      81.488  21.728   7.306  0.50  1.30           C  
ATOM   1977  CD1 TYR A 293      81.009  20.719   8.142  0.50  1.22           C  
ATOM   1978  CD2 TYR A 293      82.858  21.969   7.287  0.50  1.22           C  
ATOM   1979  CE1 TYR A 293      81.873  19.976   8.946  0.50  1.65           C  
ATOM   1980  CE2 TYR A 293      83.732  21.236   8.083  0.50  1.22           C  
ATOM   1981  CZ  TYR A 293      83.229  20.242   8.915  0.50  2.52           C  
ATOM   1982  OH  TYR A 293      84.075  19.539   9.752  0.50  4.79           O  
ATOM   1983  N   ALA A 294      77.649  22.352   5.110  0.50  1.34           N  
ATOM   1984  CA  ALA A 294      76.470  23.144   4.817  0.50  3.71           C  
ATOM   1985  C   ALA A 294      76.229  23.771   6.191  0.50  2.80           C  
ATOM   1986  O   ALA A 294      76.046  23.060   7.170  0.50  3.01           O  
ATOM   1987  CB  ALA A 294      75.284  22.265   4.406  0.50  4.48           C  
ATOM   1988  N   ILE A 295      76.304  25.096   6.273  0.50  3.44           N  
ATOM   1989  CA  ILE A 295      76.063  25.797   7.528  0.50  4.92           C  
ATOM   1990  C   ILE A 295      74.590  26.143   7.508  0.50  5.28           C  
ATOM   1991  O   ILE A 295      74.147  26.952   6.684  0.50  5.51           O  
ATOM   1992  CB  ILE A 295      76.886  27.097   7.634  0.50  4.61           C  
ATOM   1993  CG1 ILE A 295      78.365  26.801   7.375  0.50  4.54           C  
ATOM   1994  CG2 ILE A 295      76.719  27.696   9.025  0.50  1.63           C  
ATOM   1995  CD1 ILE A 295      78.969  25.802   8.340  0.50  3.45           C  
ATOM   1996  N   VAL A 296      73.824  25.524   8.402  0.50  6.21           N  
ATOM   1997  CA  VAL A 296      72.390  25.752   8.427  0.50  8.06           C  
ATOM   1998  C   VAL A 296      71.842  25.955   9.831  0.50  8.73           C  
ATOM   1999  O   VAL A 296      72.354  25.401  10.805  0.50  7.98           O  
ATOM   2000  CB  VAL A 296      71.652  24.565   7.775  0.50  7.93           C  
ATOM   2001  CG1 VAL A 296      72.196  24.323   6.374  0.50  6.89           C  
ATOM   2002  CG2 VAL A 296      71.835  23.314   8.621  0.50  7.74           C  
ATOM   2003  N   ASN A 297      70.787  26.752   9.930  0.50 10.57           N  
ATOM   2004  CA  ASN A 297      70.189  26.998  11.228  0.50 12.72           C  
ATOM   2005  C   ASN A 297      69.091  25.990  11.507  0.50 13.50           C  
ATOM   2006  O   ASN A 297      68.270  25.656  10.644  0.50 10.78           O  
ATOM   2007  CB  ASN A 297      69.631  28.419  11.320  0.50 15.21           C  
ATOM   2008  CG  ASN A 297      69.192  28.775  12.732  0.50 16.82           C  
ATOM   2009  OD1 ASN A 297      68.037  28.591  13.101  0.50 18.84           O  
ATOM   2010  ND2 ASN A 297      70.124  29.263  13.534  0.50 18.52           N  
ATOM   2011  N   ASN A 298      69.109  25.518  12.743  0.50 15.76           N  
ATOM   2012  CA  ASN A 298      68.176  24.544  13.279  0.50 18.16           C  
ATOM   2013  C   ASN A 298      66.685  24.963  13.236  0.50 18.32           C  
ATOM   2014  O   ASN A 298      65.797  24.152  13.493  0.50 18.48           O  
ATOM   2015  CB  ASN A 298      68.650  24.223  14.696  0.50 20.89           C  
ATOM   2016  CG  ASN A 298      67.546  24.161  15.671  0.50 24.03           C  
ATOM   2017  OD1 ASN A 298      67.052  23.079  15.989  0.50 30.57           O  
ATOM   2018  ND2 ASN A 298      67.126  25.318  16.163  0.50 25.22           N  
ATOM   2019  N   ARG A 299      66.406  26.218  12.900  0.50 17.96           N  
ATOM   2020  CA  ARG A 299      65.025  26.681  12.802  0.50 19.09           C  
ATOM   2021  C   ARG A 299      64.799  27.427  11.494  0.50 17.90           C  
ATOM   2022  O   ARG A 299      65.496  28.397  11.201  0.50 18.91           O  
ATOM   2023  CB  ARG A 299      64.660  27.574  13.992  0.50 20.90           C  
ATOM   2024  CG  ARG A 299      64.529  26.805  15.297  0.50 25.88           C  
ATOM   2025  CD  ARG A 299      63.411  27.364  16.157  0.50 30.55           C  
ATOM   2026  NE  ARG A 299      63.832  28.476  17.009  0.50 35.53           N  
ATOM   2027  CZ  ARG A 299      64.365  28.340  18.224  0.50 37.97           C  
ATOM   2028  NH1 ARG A 299      64.551  27.134  18.749  0.50 39.39           N  
ATOM   2029  NH2 ARG A 299      64.701  29.417  18.928  0.50 39.29           N  
ATOM   2030  N   GLN A 300      63.828  26.964  10.708  0.50 15.33           N  
ATOM   2031  CA  GLN A 300      63.521  27.577   9.423  0.50 14.25           C  
ATOM   2032  C   GLN A 300      62.215  28.382   9.391  0.50 13.86           C  
ATOM   2033  O   GLN A 300      61.393  28.321  10.304  0.50 11.68           O  
ATOM   2034  CB  GLN A 300      63.482  26.507   8.326  0.50 14.16           C  
ATOM   2035  CG  GLN A 300      64.809  25.755   8.109  0.50 13.68           C  
ATOM   2036  CD  GLN A 300      65.940  26.666   7.678  0.50 12.89           C  
ATOM   2037  OE1 GLN A 300      65.841  27.363   6.669  0.50 13.51           O  
ATOM   2038  NE2 GLN A 300      67.028  26.660   8.440  0.50 12.02           N  
ATOM   2039  N   LYS A 301      62.046  29.123   8.304  0.50 14.19           N  
ATOM   2040  CA  LYS A 301      60.887  29.985   8.065  0.50 16.33           C  
ATOM   2041  C   LYS A 301      59.512  29.351   8.336  0.50 15.80           C  
ATOM   2042  O   LYS A 301      58.661  29.952   9.001  0.50 15.01           O  
ATOM   2043  CB  LYS A 301      60.974  30.504   6.616  0.50 18.28           C  
ATOM   2044  CG  LYS A 301      59.678  30.983   5.998  0.50 23.35           C  
ATOM   2045  CD  LYS A 301      59.161  32.232   6.680  0.50 27.44           C  
ATOM   2046  CE  LYS A 301      57.828  32.658   6.086  0.50 30.22           C  
ATOM   2047  NZ  LYS A 301      57.286  33.871   6.762  0.50 31.91           N  
ATOM   2048  N   ASP A 302      59.299  28.145   7.816  0.50 14.70           N  
ATOM   2049  CA  ASP A 302      58.028  27.445   7.983  0.50 13.98           C  
ATOM   2050  C   ASP A 302      58.228  25.945   7.786  0.50 13.86           C  
ATOM   2051  O   ASP A 302      59.338  25.484   7.501  0.50 12.99           O  
ATOM   2052  CB  ASP A 302      57.012  27.952   6.961  0.50 14.21           C  
ATOM   2053  CG  ASP A 302      57.553  27.913   5.544  0.50 16.10           C  
ATOM   2054  OD1 ASP A 302      58.289  26.958   5.217  0.50 15.71           O  
ATOM   2055  OD2 ASP A 302      57.240  28.829   4.754  0.50 17.19           O  
ATOM   2056  N   ALA A 303      57.147  25.187   7.916  0.50 12.30           N  
ATOM   2057  CA  ALA A 303      57.223  23.738   7.780  0.50 12.33           C  
ATOM   2058  C   ALA A 303      57.628  23.281   6.392  0.50 11.46           C  
ATOM   2059  O   ALA A 303      58.401  22.343   6.255  0.50 12.45           O  
ATOM   2060  CB  ALA A 303      55.893  23.108   8.151  0.50 12.48           C  
ATOM   2061  N   ALA A 304      57.107  23.941   5.366  0.50 10.47           N  
ATOM   2062  CA  ALA A 304      57.415  23.556   3.995  0.50  9.38           C  
ATOM   2063  C   ALA A 304      58.893  23.707   3.685  0.50  8.12           C  
ATOM   2064  O   ALA A 304      59.507  22.830   3.068  0.50  6.96           O  
ATOM   2065  CB  ALA A 304      56.583  24.383   3.013  0.50  9.00           C  
ATOM   2066  N   THR A 305      59.463  24.820   4.128  0.50  8.33           N  
ATOM   2067  CA  THR A 305      60.871  25.101   3.892  0.50  8.05           C  
ATOM   2068  C   THR A 305      61.781  24.183   4.694  0.50  7.35           C  
ATOM   2069  O   THR A 305      62.802  23.720   4.188  0.50  8.42           O  
ATOM   2070  CB  THR A 305      61.181  26.556   4.226  0.50  8.22           C  
ATOM   2071  OG1 THR A 305      60.325  27.392   3.444  0.50  9.28           O  
ATOM   2072  CG2 THR A 305      62.635  26.887   3.901  0.50  8.64           C  
ATOM   2073  N   ALA A 306      61.423  23.918   5.944  0.50  6.06           N  
ATOM   2074  CA  ALA A 306      62.233  23.027   6.758  0.50  5.26           C  
ATOM   2075  C   ALA A 306      62.250  21.631   6.123  0.50  4.68           C  
ATOM   2076  O   ALA A 306      63.304  20.993   6.034  0.50  3.88           O  
ATOM   2077  CB  ALA A 306      61.672  22.950   8.186  0.50  4.36           C  
ATOM   2078  N   GLN A 307      61.089  21.168   5.664  0.50  4.12           N  
ATOM   2079  CA  GLN A 307      61.001  19.831   5.080  0.50  4.91           C  
ATOM   2080  C   GLN A 307      61.785  19.691   3.789  0.50  3.68           C  
ATOM   2081  O   GLN A 307      62.411  18.657   3.543  0.50  1.82           O  
ATOM   2082  CB  GLN A 307      59.540  19.427   4.839  0.50  4.55           C  
ATOM   2083  CG  GLN A 307      59.391  17.965   4.404  0.50  4.47           C  
ATOM   2084  CD  GLN A 307      57.951  17.465   4.449  0.50  6.99           C  
ATOM   2085  OE1 GLN A 307      57.318  17.458   5.506  0.50  8.90           O  
ATOM   2086  NE2 GLN A 307      57.430  17.040   3.299  0.50  5.05           N  
ATOM   2087  N   THR A 308      61.757  20.739   2.976  0.50  4.15           N  
ATOM   2088  CA  THR A 308      62.461  20.734   1.701  0.50  4.70           C  
ATOM   2089  C   THR A 308      63.962  20.813   1.914  0.50  2.84           C  
ATOM   2090  O   THR A 308      64.715  20.164   1.209  0.50  3.79           O  
ATOM   2091  CB  THR A 308      62.000  21.904   0.815  0.50  5.20           C  
ATOM   2092  OG1 THR A 308      60.572  21.874   0.726  0.50  8.20           O  
ATOM   2093  CG2 THR A 308      62.578  21.783  -0.604  0.50  4.39           C  
ATOM   2094  N   LEU A 309      64.401  21.599   2.888  0.50  3.24           N  
ATOM   2095  CA  LEU A 309      65.830  21.708   3.155  0.50  3.19           C  
ATOM   2096  C   LEU A 309      66.330  20.348   3.643  0.50  4.08           C  
ATOM   2097  O   LEU A 309      67.403  19.889   3.242  0.50  1.73           O  
ATOM   2098  CB  LEU A 309      66.099  22.777   4.206  0.50  3.65           C  
ATOM   2099  CG  LEU A 309      67.563  22.985   4.591  0.50  4.36           C  
ATOM   2100  CD1 LEU A 309      68.400  23.273   3.355  0.50  2.85           C  
ATOM   2101  CD2 LEU A 309      67.650  24.146   5.597  0.50  6.34           C  
ATOM   2102  N   GLN A 310      65.542  19.694   4.497  0.50  3.98           N  
ATOM   2103  CA  GLN A 310      65.921  18.367   4.988  0.50  4.40           C  
ATOM   2104  C   GLN A 310      66.010  17.407   3.794  0.50  2.85           C  
ATOM   2105  O   GLN A 310      67.009  16.711   3.606  0.50  2.43           O  
ATOM   2106  CB  GLN A 310      64.898  17.846   6.008  0.50  4.09           C  
ATOM   2107  CG  GLN A 310      65.194  18.230   7.454  0.50  7.70           C  
ATOM   2108  CD  GLN A 310      64.368  17.426   8.442  0.50  9.15           C  
ATOM   2109  OE1 GLN A 310      64.105  16.251   8.213  0.50 10.94           O  
ATOM   2110  NE2 GLN A 310      63.970  18.047   9.548  0.50  8.20           N  
ATOM   2111  N   ALA A 311      64.965  17.387   2.982  0.50  2.28           N  
ATOM   2112  CA  ALA A 311      64.930  16.523   1.813  0.50  3.74           C  
ATOM   2113  C   ALA A 311      66.174  16.716   0.948  0.50  4.31           C  
ATOM   2114  O   ALA A 311      66.823  15.740   0.551  0.50  4.82           O  
ATOM   2115  CB  ALA A 311      63.666  16.808   0.981  0.50  2.58           C  
ATOM   2116  N   PHE A 312      66.505  17.974   0.661  0.50  4.75           N  
ATOM   2117  CA  PHE A 312      67.661  18.278  -0.179  0.50  4.12           C  
ATOM   2118  C   PHE A 312      68.983  17.829   0.418  0.50  4.19           C  
ATOM   2119  O   PHE A 312      69.781  17.178  -0.255  0.50  5.56           O  
ATOM   2120  CB  PHE A 312      67.735  19.773  -0.479  0.50  3.11           C  
ATOM   2121  CG  PHE A 312      68.961  20.161  -1.260  0.50  2.99           C  
ATOM   2122  CD1 PHE A 312      69.067  19.852  -2.611  0.50  1.22           C  
ATOM   2123  CD2 PHE A 312      70.019  20.805  -0.641  0.50  3.19           C  
ATOM   2124  CE1 PHE A 312      70.216  20.183  -3.332  0.50  3.70           C  
ATOM   2125  CE2 PHE A 312      71.172  21.140  -1.353  0.50  4.06           C  
ATOM   2126  CZ  PHE A 312      71.271  20.831  -2.700  0.50  3.47           C  
ATOM   2127  N   LEU A 313      69.218  18.176   1.677  0.50  3.38           N  
ATOM   2128  CA  LEU A 313      70.457  17.798   2.351  0.50  4.20           C  
ATOM   2129  C   LEU A 313      70.664  16.268   2.426  0.50  3.67           C  
ATOM   2130  O   LEU A 313      71.767  15.766   2.207  0.50  3.64           O  
ATOM   2131  CB  LEU A 313      70.473  18.423   3.749  0.50  4.86           C  
ATOM   2132  CG  LEU A 313      71.270  19.713   4.010  0.50  6.66           C  
ATOM   2133  CD1 LEU A 313      71.362  20.583   2.772  0.50  7.25           C  
ATOM   2134  CD2 LEU A 313      70.613  20.457   5.168  0.50  6.73           C  
ATOM   2135  N   HIS A 314      69.609  15.528   2.744  0.50  3.75           N  
ATOM   2136  CA  HIS A 314      69.700  14.071   2.811  0.50  4.04           C  
ATOM   2137  C   HIS A 314      69.962  13.516   1.409  0.50  3.22           C  
ATOM   2138  O   HIS A 314      70.710  12.552   1.233  0.50  1.22           O  
ATOM   2139  CB  HIS A 314      68.407  13.474   3.355  0.50  4.05           C  
ATOM   2140  CG  HIS A 314      68.395  11.979   3.361  0.50  2.61           C  
ATOM   2141  ND1 HIS A 314      69.166  11.234   4.225  0.50  3.57           N  
ATOM   2142  CD2 HIS A 314      67.729  11.090   2.586  0.50  3.34           C  
ATOM   2143  CE1 HIS A 314      68.977   9.948   3.985  0.50  3.66           C  
ATOM   2144  NE2 HIS A 314      68.110   9.834   2.994  0.50  5.34           N  
ATOM   2145  N   TRP A 315      69.325  14.124   0.413  0.50  3.48           N  
ATOM   2146  CA  TRP A 315      69.528  13.720  -0.981  0.50  4.02           C  
ATOM   2147  C   TRP A 315      71.006  13.909  -1.337  0.50  1.98           C  
ATOM   2148  O   TRP A 315      71.663  13.016  -1.866  0.50  1.22           O  
ATOM   2149  CB  TRP A 315      68.680  14.591  -1.916  0.50  3.35           C  
ATOM   2150  CG  TRP A 315      68.961  14.343  -3.378  0.50  4.74           C  
ATOM   2151  CD1 TRP A 315      68.366  13.415  -4.186  0.50  5.17           C  
ATOM   2152  CD2 TRP A 315      69.922  15.023  -4.190  0.50  4.59           C  
ATOM   2153  NE1 TRP A 315      68.895  13.480  -5.455  0.50  3.96           N  
ATOM   2154  CE2 TRP A 315      69.853  14.456  -5.486  0.50  4.26           C  
ATOM   2155  CE3 TRP A 315      70.839  16.054  -3.950  0.50  5.20           C  
ATOM   2156  CZ2 TRP A 315      70.666  14.887  -6.541  0.50  3.53           C  
ATOM   2157  CZ3 TRP A 315      71.652  16.485  -5.004  0.50  5.20           C  
ATOM   2158  CH2 TRP A 315      71.555  15.897  -6.284  0.50  4.74           C  
ATOM   2159  N   ALA A 316      71.512  15.094  -1.021  0.50  2.74           N  
ATOM   2160  CA  ALA A 316      72.891  15.465  -1.296  0.50  2.42           C  
ATOM   2161  C   ALA A 316      73.914  14.490  -0.722  0.50  2.22           C  
ATOM   2162  O   ALA A 316      74.922  14.196  -1.373  0.50  1.22           O  
ATOM   2163  CB  ALA A 316      73.161  16.863  -0.771  0.50  1.22           C  
ATOM   2164  N   ILE A 317      73.664  13.983   0.484  0.50  2.26           N  
ATOM   2165  CA  ILE A 317      74.608  13.056   1.107  0.50  3.89           C  
ATOM   2166  C   ILE A 317      74.384  11.589   0.743  0.50  2.98           C  
ATOM   2167  O   ILE A 317      75.083  10.709   1.227  0.50  3.12           O  
ATOM   2168  CB  ILE A 317      74.625  13.192   2.651  0.50  2.98           C  
ATOM   2169  CG1 ILE A 317      73.234  12.933   3.224  0.50  3.54           C  
ATOM   2170  CG2 ILE A 317      75.148  14.562   3.036  0.50  1.22           C  
ATOM   2171  CD1 ILE A 317      73.224  12.858   4.716  0.50  5.21           C  
ATOM   2172  N   THR A 318      73.400  11.315  -0.098  0.50  3.32           N  
ATOM   2173  CA  THR A 318      73.178   9.942  -0.520  0.50  4.12           C  
ATOM   2174  C   THR A 318      73.289   9.957  -2.039  0.50  3.42           C  
ATOM   2175  O   THR A 318      74.359   9.691  -2.573  0.50  4.84           O  
ATOM   2176  CB  THR A 318      71.797   9.387  -0.042  0.50  3.08           C  
ATOM   2177  OG1 THR A 318      70.733  10.231  -0.493  0.50  3.46           O  
ATOM   2178  CG2 THR A 318      71.761   9.300   1.467  0.50  2.22           C  
ATOM   2179  N   ASP A 319      72.216  10.302  -2.742  0.50  3.13           N  
ATOM   2180  CA  ASP A 319      72.294  10.355  -4.198  0.50  4.76           C  
ATOM   2181  C   ASP A 319      73.370  11.356  -4.643  0.50  3.80           C  
ATOM   2182  O   ASP A 319      74.153  11.079  -5.553  0.50  3.46           O  
ATOM   2183  CB  ASP A 319      70.932  10.737  -4.776  0.50  6.57           C  
ATOM   2184  CG  ASP A 319      69.939   9.595  -4.708  0.50  9.83           C  
ATOM   2185  OD1 ASP A 319      70.374   8.428  -4.803  0.50 11.70           O  
ATOM   2186  OD2 ASP A 319      68.726   9.861  -4.566  0.50 13.74           O  
ATOM   2187  N   GLY A 320      73.414  12.512  -3.988  0.50  3.09           N  
ATOM   2188  CA  GLY A 320      74.405  13.512  -4.340  0.50  4.12           C  
ATOM   2189  C   GLY A 320      75.857  13.096  -4.139  0.50  3.92           C  
ATOM   2190  O   GLY A 320      76.750  13.740  -4.684  0.50  4.44           O  
ATOM   2191  N   ASN A 321      76.098  12.037  -3.364  0.50  4.21           N  
ATOM   2192  CA  ASN A 321      77.458  11.546  -3.102  0.50  4.94           C  
ATOM   2193  C   ASN A 321      77.917  10.469  -4.095  0.50  4.78           C  
ATOM   2194  O   ASN A 321      78.978   9.869  -3.913  0.50  3.80           O  
ATOM   2195  CB  ASN A 321      77.576  10.980  -1.674  0.50  2.57           C  
ATOM   2196  CG  ASN A 321      78.189  11.973  -0.680  0.50  3.20           C  
ATOM   2197  OD1 ASN A 321      78.973  11.580   0.192  0.50  1.22           O  
ATOM   2198  ND2 ASN A 321      77.825  13.251  -0.795  0.50  1.22           N  
ATOM   2199  N   LYS A 322      77.125  10.202  -5.129  0.50  5.44           N  
ATOM   2200  CA  LYS A 322      77.538   9.212  -6.116  0.50  7.24           C  
ATOM   2201  C   LYS A 322      78.650   9.778  -6.972  0.50  6.56           C  
ATOM   2202  O   LYS A 322      78.733  10.987  -7.185  0.50  6.10           O  
ATOM   2203  CB  LYS A 322      76.367   8.771  -6.994  0.50 10.34           C  
ATOM   2204  CG  LYS A 322      75.499   7.704  -6.321  0.50 15.01           C  
ATOM   2205  CD  LYS A 322      74.317   7.315  -7.180  0.50 20.64           C  
ATOM   2206  CE  LYS A 322      73.388   6.355  -6.442  0.50 23.27           C  
ATOM   2207  NZ  LYS A 322      72.151   6.066  -7.242  0.50 26.35           N  
ATOM   2208  N   ALA A 323      79.510   8.888  -7.455  0.50  7.52           N  
ATOM   2209  CA  ALA A 323      80.653   9.266  -8.272  0.50  8.69           C  
ATOM   2210  C   ALA A 323      80.314  10.144  -9.479  0.50  9.28           C  
ATOM   2211  O   ALA A 323      81.105  11.002  -9.856  0.50  9.08           O  
ATOM   2212  CB  ALA A 323      81.394   8.015  -8.718  0.50  8.85           C  
ATOM   2213  N   SER A 324      79.155   9.928 -10.092  0.50  9.74           N  
ATOM   2214  CA  SER A 324      78.752  10.736 -11.240  0.50 10.98           C  
ATOM   2215  C   SER A 324      78.841  12.217 -10.894  0.50 10.95           C  
ATOM   2216  O   SER A 324      79.123  13.047 -11.760  0.50 11.55           O  
ATOM   2217  CB  SER A 324      77.318  10.409 -11.650  0.50 12.81           C  
ATOM   2218  OG  SER A 324      76.749   9.484 -10.741  0.50 17.55           O  
ATOM   2219  N   PHE A 325      78.582  12.546  -9.630  0.50  9.37           N  
ATOM   2220  CA  PHE A 325      78.653  13.930  -9.184  0.50  8.37           C  
ATOM   2221  C   PHE A 325      80.033  14.285  -8.657  0.50  6.93           C  
ATOM   2222  O   PHE A 325      80.691  15.172  -9.183  0.50  8.52           O  
ATOM   2223  CB  PHE A 325      77.641  14.213  -8.065  0.50  7.17           C  
ATOM   2224  CG  PHE A 325      76.214  14.197  -8.510  0.50  6.74           C  
ATOM   2225  CD1 PHE A 325      75.714  15.211  -9.321  0.50  6.59           C  
ATOM   2226  CD2 PHE A 325      75.357  13.181  -8.097  0.50  7.03           C  
ATOM   2227  CE1 PHE A 325      74.384  15.223  -9.716  0.50  5.89           C  
ATOM   2228  CE2 PHE A 325      74.012  13.181  -8.489  0.50  6.65           C  
ATOM   2229  CZ  PHE A 325      73.527  14.208  -9.301  0.50  6.97           C  
ATOM   2230  N   LEU A 326      80.474  13.581  -7.625  0.50  5.69           N  
ATOM   2231  CA  LEU A 326      81.750  13.895  -6.999  0.50  6.52           C  
ATOM   2232  C   LEU A 326      82.977  13.781  -7.876  0.50  7.32           C  
ATOM   2233  O   LEU A 326      83.886  14.597  -7.777  0.50  6.54           O  
ATOM   2234  CB  LEU A 326      81.940  13.064  -5.728  0.50  4.59           C  
ATOM   2235  CG  LEU A 326      80.854  13.199  -4.648  0.50  3.00           C  
ATOM   2236  CD1 LEU A 326      81.395  12.598  -3.359  0.50  3.12           C  
ATOM   2237  CD2 LEU A 326      80.455  14.671  -4.409  0.50  3.46           C  
ATOM   2238  N   ASP A 327      83.016  12.795  -8.755  0.50  9.80           N  
ATOM   2239  CA  ASP A 327      84.192  12.659  -9.593  0.50 12.42           C  
ATOM   2240  C   ASP A 327      84.465  13.875 -10.481  0.50 11.92           C  
ATOM   2241  O   ASP A 327      85.596  14.094 -10.913  0.50 11.38           O  
ATOM   2242  CB  ASP A 327      84.096  11.418 -10.465  0.50 15.64           C  
ATOM   2243  CG  ASP A 327      85.453  10.924 -10.875  0.50 20.92           C  
ATOM   2244  OD1 ASP A 327      86.193  10.475  -9.968  0.50 23.49           O  
ATOM   2245  OD2 ASP A 327      85.792  11.004 -12.083  0.50 22.72           O  
ATOM   2246  N   GLN A 328      83.434  14.668 -10.743  0.50 10.73           N  
ATOM   2247  CA  GLN A 328      83.592  15.842 -11.583  0.50 11.29           C  
ATOM   2248  C   GLN A 328      84.399  16.962 -10.923  0.50 10.05           C  
ATOM   2249  O   GLN A 328      85.073  17.721 -11.617  0.50 12.38           O  
ATOM   2250  CB  GLN A 328      82.213  16.349 -12.024  0.50 12.97           C  
ATOM   2251  CG  GLN A 328      81.486  15.329 -12.906  0.50 15.64           C  
ATOM   2252  CD  GLN A 328      80.216  15.866 -13.537  0.50 17.45           C  
ATOM   2253  OE1 GLN A 328      80.225  16.920 -14.174  0.50 17.80           O  
ATOM   2254  NE2 GLN A 328      79.116  15.133 -13.377  0.50 17.06           N  
ATOM   2255  N   VAL A 329      84.342  17.067  -9.596  0.50  6.69           N  
ATOM   2256  CA  VAL A 329      85.093  18.101  -8.885  0.50  4.59           C  
ATOM   2257  C   VAL A 329      86.204  17.510  -8.041  0.50  3.64           C  
ATOM   2258  O   VAL A 329      86.798  18.210  -7.223  0.50  3.37           O  
ATOM   2259  CB  VAL A 329      84.198  18.939  -7.953  0.50  3.96           C  
ATOM   2260  CG1 VAL A 329      83.276  19.821  -8.773  0.50  2.97           C  
ATOM   2261  CG2 VAL A 329      83.396  18.024  -7.048  0.50  1.22           C  
ATOM   2262  N   HIS A 330      86.457  16.218  -8.229  0.50  2.10           N  
ATOM   2263  CA  HIS A 330      87.520  15.509  -7.522  0.50  4.06           C  
ATOM   2264  C   HIS A 330      87.316  15.316  -6.018  0.50  2.76           C  
ATOM   2265  O   HIS A 330      88.277  15.331  -5.258  0.50  3.22           O  
ATOM   2266  CB  HIS A 330      88.862  16.210  -7.773  0.50  3.82           C  
ATOM   2267  CG  HIS A 330      89.211  16.342  -9.223  0.50  6.53           C  
ATOM   2268  ND1 HIS A 330      89.384  17.564  -9.840  0.50  7.92           N  
ATOM   2269  CD2 HIS A 330      89.386  15.407 -10.188  0.50  6.50           C  
ATOM   2270  CE1 HIS A 330      89.647  17.377 -11.123  0.50  7.89           C  
ATOM   2271  NE2 HIS A 330      89.654  16.076 -11.360  0.50  8.40           N  
ATOM   2272  N   PHE A 331      86.069  15.130  -5.595  0.50  3.63           N  
ATOM   2273  CA  PHE A 331      85.750  14.909  -4.180  0.50  2.86           C  
ATOM   2274  C   PHE A 331      85.519  13.420  -3.942  0.50  1.99           C  
ATOM   2275  O   PHE A 331      85.393  12.631  -4.883  0.50  1.22           O  
ATOM   2276  CB  PHE A 331      84.467  15.637  -3.762  0.50  2.03           C  
ATOM   2277  CG  PHE A 331      84.543  17.139  -3.829  0.50  1.58           C  
ATOM   2278  CD1 PHE A 331      85.633  17.784  -4.408  0.50  2.25           C  
ATOM   2279  CD2 PHE A 331      83.483  17.905  -3.346  0.50  1.22           C  
ATOM   2280  CE1 PHE A 331      85.663  19.177  -4.511  0.50  2.62           C  
ATOM   2281  CE2 PHE A 331      83.496  19.291  -3.442  0.50  1.91           C  
ATOM   2282  CZ  PHE A 331      84.593  19.934  -4.029  0.50  3.21           C  
ATOM   2283  N   GLN A 332      85.451  13.052  -2.670  0.50  1.83           N  
ATOM   2284  CA  GLN A 332      85.213  11.672  -2.260  0.50  1.98           C  
ATOM   2285  C   GLN A 332      83.948  11.664  -1.426  0.50  1.22           C  
ATOM   2286  O   GLN A 332      83.595  12.679  -0.823  0.50  1.22           O  
ATOM   2287  CB  GLN A 332      86.388  11.169  -1.428  0.50  2.13           C  
ATOM   2288  CG  GLN A 332      87.641  10.943  -2.250  0.50  2.02           C  
ATOM   2289  CD  GLN A 332      87.462   9.812  -3.241  0.50  3.45           C  
ATOM   2290  OE1 GLN A 332      87.910   9.897  -4.383  0.50  6.60           O  
ATOM   2291  NE2 GLN A 332      86.810   8.742  -2.808  0.50  1.41           N  
ATOM   2292  N   PRO A 333      83.242  10.523  -1.379  0.50  1.87           N  
ATOM   2293  CA  PRO A 333      82.010  10.475  -0.582  0.50  1.22           C  
ATOM   2294  C   PRO A 333      82.282  10.306   0.903  0.50  2.55           C  
ATOM   2295  O   PRO A 333      83.363   9.875   1.301  0.50  1.22           O  
ATOM   2296  CB  PRO A 333      81.264   9.272  -1.157  0.50  1.22           C  
ATOM   2297  CG  PRO A 333      82.394   8.331  -1.525  0.50  1.22           C  
ATOM   2298  CD  PRO A 333      83.428   9.276  -2.153  0.50  1.62           C  
ATOM   2299  N   LEU A 334      81.290  10.659   1.713  0.50  1.22           N  
ATOM   2300  CA  LEU A 334      81.386  10.523   3.154  0.50  2.74           C  
ATOM   2301  C   LEU A 334      81.259   9.040   3.503  0.50  2.77           C  
ATOM   2302  O   LEU A 334      80.429   8.347   2.929  0.50  1.22           O  
ATOM   2303  CB  LEU A 334      80.232  11.253   3.827  0.50  1.22           C  
ATOM   2304  CG  LEU A 334      79.987  12.748   3.657  0.50  1.22           C  
ATOM   2305  CD1 LEU A 334      78.719  13.119   4.428  0.50  1.84           C  
ATOM   2306  CD2 LEU A 334      81.163  13.528   4.189  0.50  1.22           C  
ATOM   2307  N   PRO A 335      82.102   8.526   4.419  0.50  1.85           N  
ATOM   2308  CA  PRO A 335      81.961   7.107   4.766  0.50  1.22           C  
ATOM   2309  C   PRO A 335      80.630   6.972   5.524  0.50  1.83           C  
ATOM   2310  O   PRO A 335      80.152   7.933   6.135  0.50  3.25           O  
ATOM   2311  CB  PRO A 335      83.202   6.827   5.626  0.50  1.37           C  
ATOM   2312  CG  PRO A 335      83.559   8.150   6.186  0.50  2.95           C  
ATOM   2313  CD  PRO A 335      83.281   9.124   5.066  0.50  1.22           C  
ATOM   2314  N   PRO A 336      80.018   5.785   5.505  0.50  1.22           N  
ATOM   2315  CA  PRO A 336      78.735   5.607   6.191  0.50  2.16           C  
ATOM   2316  C   PRO A 336      78.547   6.109   7.617  0.50  1.95           C  
ATOM   2317  O   PRO A 336      77.506   6.673   7.928  0.50  2.45           O  
ATOM   2318  CB  PRO A 336      78.446   4.108   6.038  0.50  1.22           C  
ATOM   2319  CG  PRO A 336      79.762   3.505   5.646  0.50  2.56           C  
ATOM   2320  CD  PRO A 336      80.457   4.547   4.844  0.50  1.42           C  
ATOM   2321  N   ALA A 337      79.522   5.932   8.496  0.50  2.28           N  
ATOM   2322  CA  ALA A 337      79.318   6.407   9.858  0.50  3.02           C  
ATOM   2323  C   ALA A 337      79.103   7.909   9.867  0.50  2.91           C  
ATOM   2324  O   ALA A 337      78.347   8.426  10.680  0.50  2.94           O  
ATOM   2325  CB  ALA A 337      80.505   6.043  10.734  0.50  2.69           C  
ATOM   2326  N   VAL A 338      79.758   8.615   8.948  0.50  3.75           N  
ATOM   2327  CA  VAL A 338      79.632  10.070   8.887  0.50  4.15           C  
ATOM   2328  C   VAL A 338      78.297  10.466   8.262  0.50  4.13           C  
ATOM   2329  O   VAL A 338      77.665  11.441   8.678  0.50  6.03           O  
ATOM   2330  CB  VAL A 338      80.814  10.682   8.099  0.50  3.67           C  
ATOM   2331  CG1 VAL A 338      80.680  12.202   8.015  0.50  1.67           C  
ATOM   2332  CG2 VAL A 338      82.113  10.305   8.776  0.50  2.61           C  
ATOM   2333  N   VAL A 339      77.857   9.697   7.273  0.50  4.24           N  
ATOM   2334  CA  VAL A 339      76.579   9.956   6.626  0.50  4.82           C  
ATOM   2335  C   VAL A 339      75.503   9.905   7.709  0.50  6.55           C  
ATOM   2336  O   VAL A 339      74.574  10.723   7.739  0.50  6.79           O  
ATOM   2337  CB  VAL A 339      76.268   8.881   5.569  0.50  4.36           C  
ATOM   2338  CG1 VAL A 339      74.812   9.000   5.110  0.50  1.59           C  
ATOM   2339  CG2 VAL A 339      77.233   9.021   4.386  0.50  2.23           C  
ATOM   2340  N   LYS A 340      75.642   8.940   8.609  0.50  6.63           N  
ATOM   2341  CA  LYS A 340      74.682   8.786   9.687  0.50  9.32           C  
ATOM   2342  C   LYS A 340      74.661  10.028  10.582  0.50  8.27           C  
ATOM   2343  O   LYS A 340      73.590  10.519  10.931  0.50  9.52           O  
ATOM   2344  CB  LYS A 340      75.015   7.527  10.495  0.50 12.35           C  
ATOM   2345  CG  LYS A 340      73.866   6.997  11.334  0.50 16.87           C  
ATOM   2346  CD  LYS A 340      73.899   5.464  11.382  0.50 21.68           C  
ATOM   2347  CE  LYS A 340      72.812   4.880  12.295  0.50 23.35           C  
ATOM   2348  NZ  LYS A 340      73.082   5.116  13.754  0.50 25.46           N  
ATOM   2349  N   LEU A 341      75.839  10.545  10.934  0.50  7.31           N  
ATOM   2350  CA  LEU A 341      75.939  11.731  11.784  0.50  6.20           C  
ATOM   2351  C   LEU A 341      75.309  12.954  11.111  0.50  5.88           C  
ATOM   2352  O   LEU A 341      74.633  13.747  11.767  0.50  7.55           O  
ATOM   2353  CB  LEU A 341      77.405  12.016  12.134  0.50  4.19           C  
ATOM   2354  CG  LEU A 341      78.144  10.966  12.975  0.50  3.85           C  
ATOM   2355  CD1 LEU A 341      79.609  11.370  13.106  0.50  4.35           C  
ATOM   2356  CD2 LEU A 341      77.509  10.834  14.356  0.50  4.30           C  
ATOM   2357  N   SER A 342      75.532  13.108   9.809  0.50  4.32           N  
ATOM   2358  CA  SER A 342      74.943  14.219   9.069  0.50  3.63           C  
ATOM   2359  C   SER A 342      73.424  14.123   9.137  0.50  2.77           C  
ATOM   2360  O   SER A 342      72.741  15.107   9.409  0.50  1.85           O  
ATOM   2361  CB  SER A 342      75.379  14.178   7.604  0.50  2.22           C  
ATOM   2362  OG  SER A 342      76.758  14.471   7.466  0.50  3.94           O  
ATOM   2363  N   ASP A 343      72.899  12.928   8.876  0.50  3.36           N  
ATOM   2364  CA  ASP A 343      71.462  12.705   8.907  0.50  4.68           C  
ATOM   2365  C   ASP A 343      70.886  13.085  10.263  0.50  3.74           C  
ATOM   2366  O   ASP A 343      69.841  13.707  10.346  0.50  2.25           O  
ATOM   2367  CB  ASP A 343      71.136  11.241   8.620  0.50  6.56           C  
ATOM   2368  CG  ASP A 343      70.576  11.027   7.220  0.50  7.10           C  
ATOM   2369  OD1 ASP A 343      70.080  11.999   6.612  0.50  7.97           O  
ATOM   2370  OD2 ASP A 343      70.612   9.877   6.735  0.50  7.53           O  
ATOM   2371  N   ALA A 344      71.580  12.706  11.327  0.50  4.80           N  
ATOM   2372  CA  ALA A 344      71.124  13.022  12.672  0.50  5.38           C  
ATOM   2373  C   ALA A 344      70.981  14.539  12.846  0.50  5.77           C  
ATOM   2374  O   ALA A 344      70.079  15.009  13.538  0.50  7.04           O  
ATOM   2375  CB  ALA A 344      72.106  12.452  13.697  0.50  3.67           C  
ATOM   2376  N   LEU A 345      71.860  15.312  12.223  0.50  5.18           N  
ATOM   2377  CA  LEU A 345      71.775  16.768  12.351  0.50  6.55           C  
ATOM   2378  C   LEU A 345      70.687  17.329  11.429  0.50  6.33           C  
ATOM   2379  O   LEU A 345      69.955  18.249  11.805  0.50  5.45           O  
ATOM   2380  CB  LEU A 345      73.122  17.410  12.012  0.50  5.79           C  
ATOM   2381  CG  LEU A 345      74.321  17.019  12.881  0.50  5.61           C  
ATOM   2382  CD1 LEU A 345      75.602  17.369  12.140  0.50  3.70           C  
ATOM   2383  CD2 LEU A 345      74.247  17.709  14.232  0.50  3.95           C  
ATOM   2384  N   ILE A 346      70.597  16.770  10.224  0.50  5.84           N  
ATOM   2385  CA  ILE A 346      69.595  17.193   9.249  0.50  7.37           C  
ATOM   2386  C   ILE A 346      68.210  17.108   9.879  0.50  7.86           C  
ATOM   2387  O   ILE A 346      67.359  17.981   9.677  0.50  8.24           O  
ATOM   2388  CB  ILE A 346      69.549  16.259   8.029  0.50  7.17           C  
ATOM   2389  CG1 ILE A 346      70.909  16.203   7.329  0.50  8.98           C  
ATOM   2390  CG2 ILE A 346      68.455  16.727   7.074  0.50  8.35           C  
ATOM   2391  CD1 ILE A 346      71.279  17.460   6.665  0.50 10.86           C  
ATOM   2392  N   ALA A 347      68.005  16.031  10.632  0.50  7.19           N  
ATOM   2393  CA  ALA A 347      66.739  15.734  11.283  0.50  9.16           C  
ATOM   2394  C   ALA A 347      66.294  16.715  12.351  0.50  8.77           C  
ATOM   2395  O   ALA A 347      65.148  16.668  12.771  0.50  9.34           O  
ATOM   2396  CB  ALA A 347      66.783  14.320  11.879  0.50  9.30           C  
ATOM   2397  N   THR A 348      67.176  17.595  12.805  0.50  8.72           N  
ATOM   2398  CA  THR A 348      66.771  18.541  13.835  0.50  9.40           C  
ATOM   2399  C   THR A 348      66.281  19.827  13.201  0.50 10.50           C  
ATOM   2400  O   THR A 348      65.862  20.745  13.902  0.50 13.25           O  
ATOM   2401  CB  THR A 348      67.919  18.876  14.776  0.50  8.03           C  
ATOM   2402  OG1 THR A 348      68.919  19.604  14.056  0.50 11.10           O  
ATOM   2403  CG2 THR A 348      68.529  17.606  15.343  0.50  6.62           C  
ATOM   2404  N   ILE A 349      66.324  19.888  11.873  0.50 11.35           N  
ATOM   2405  CA  ILE A 349      65.885  21.078  11.156  0.50 11.43           C  
ATOM   2406  C   ILE A 349      64.366  21.176  11.247  0.50 12.81           C  
ATOM   2407  O   ILE A 349      63.654  20.355  10.664  0.50 11.32           O  
ATOM   2408  CB  ILE A 349      66.263  21.024   9.662  0.50 11.12           C  
ATOM   2409  CG1 ILE A 349      67.784  20.842   9.488  0.50  9.76           C  
ATOM   2410  CG2 ILE A 349      65.723  22.275   8.961  0.50  8.62           C  
ATOM   2411  CD1 ILE A 349      68.553  22.090   9.235  0.50  8.96           C  
ATOM   2412  N   SER A 350      63.885  22.199  11.955  0.50 14.06           N  
ATOM   2413  CA  SER A 350      62.454  22.412  12.158  0.50 15.79           C  
ATOM   2414  C   SER A 350      62.009  23.862  11.910  0.50 16.97           C  
ATOM   2415  O   SER A 350      62.745  24.665  11.332  0.50 17.22           O  
ATOM   2416  CB  SER A 350      62.095  22.008  13.585  0.50 15.81           C  
ATOM   2417  OG  SER A 350      60.696  21.985  13.762  0.50 18.78           O  
ATOM   2418  N   SER A 351      60.795  24.188  12.352  0.50 18.23           N  
ATOM   2419  CA  SER A 351      60.243  25.534  12.191  0.50 18.42           C  
ATOM   2420  C   SER A 351      59.278  25.838  13.334  0.50 19.43           C  
ATOM   2421  O   SER A 351      59.009  24.973  14.174  0.50 20.56           O  
ATOM   2422  CB  SER A 351      59.499  25.649  10.861  0.50 18.41           C  
ATOM   2423  OG  SER A 351      58.342  24.836  10.870  0.50 18.44           O  
ATOM   2424  OXT SER A 351      58.784  26.985  13.365  0.50 11.20           O  
TER    2425      SER A 351                                                      
TER    4850      SER B 351                                                      
ENDMDL                                                                          
MODEL        2                                                                  
ATOM      1  N   VAL A  19      64.240  11.926   9.628  0.50 19.76           N  
ATOM      2  CA  VAL A  19      64.711  12.796   8.495  0.50 19.10           C  
ATOM      3  C   VAL A  19      63.708  12.756   7.345  0.50 16.99           C  
ATOM      4  O   VAL A  19      63.273  11.686   6.931  0.50 17.64           O  
ATOM      5  CB  VAL A  19      66.094  12.329   7.965  0.50 19.82           C  
ATOM      6  CG1 VAL A  19      65.983  10.918   7.405  0.50 21.64           C  
ATOM      7  CG2 VAL A  19      66.600  13.287   6.896  0.50 19.52           C  
ATOM      8  N   ALA A  20      63.340  13.922   6.833  0.50 15.27           N  
ATOM      9  CA  ALA A  20      62.379  13.990   5.737  0.50 15.51           C  
ATOM     10  C   ALA A  20      63.073  13.725   4.412  0.50 15.54           C  
ATOM     11  O   ALA A  20      63.973  14.456   4.014  0.50 17.10           O  
ATOM     12  CB  ALA A  20      61.710  15.358   5.710  0.50 15.54           C  
ATOM     13  N   THR A  21      62.650  12.684   3.718  0.50 15.27           N  
ATOM     14  CA  THR A  21      63.266  12.358   2.446  0.50 15.93           C  
ATOM     15  C   THR A  21      62.435  12.838   1.255  0.50 14.78           C  
ATOM     16  O   THR A  21      62.775  12.574   0.099  0.50 15.70           O  
ATOM     17  CB  THR A  21      63.487  10.851   2.338  0.50 16.67           C  
ATOM     18  OG1 THR A  21      62.228  10.186   2.465  0.50 18.47           O  
ATOM     19  CG2 THR A  21      64.425  10.375   3.448  0.50 17.73           C  
ATOM     20  N   THR A  22      61.354  13.555   1.536  0.50 12.99           N  
ATOM     21  CA  THR A  22      60.492  14.064   0.471  0.50 10.95           C  
ATOM     22  C   THR A  22      60.221  15.543   0.682  0.50  9.11           C  
ATOM     23  O   THR A  22      59.851  15.950   1.769  0.50  8.64           O  
ATOM     24  CB  THR A  22      59.123  13.330   0.441  0.50 11.86           C  
ATOM     25  OG1 THR A  22      59.322  11.939   0.160  0.50 14.08           O  
ATOM     26  CG2 THR A  22      58.223  13.929  -0.624  0.50 11.13           C  
ATOM     27  N   PRO A  23      60.392  16.363  -0.365  0.50  7.31           N  
ATOM     28  CA  PRO A  23      60.169  17.815  -0.325  0.50  6.69           C  
ATOM     29  C   PRO A  23      58.683  18.151  -0.218  0.50  6.26           C  
ATOM     30  O   PRO A  23      57.837  17.341  -0.585  0.50  7.02           O  
ATOM     31  CB  PRO A  23      60.716  18.298  -1.672  0.50  7.54           C  
ATOM     32  CG  PRO A  23      61.571  17.164  -2.167  0.50  8.12           C  
ATOM     33  CD  PRO A  23      60.877  15.939  -1.686  0.50  6.94           C  
ATOM     34  N   ALA A  24      58.367  19.342   0.277  0.50  5.72           N  
ATOM     35  CA  ALA A  24      56.979  19.775   0.356  0.50  6.90           C  
ATOM     36  C   ALA A  24      56.550  19.909  -1.103  0.50  8.64           C  
ATOM     37  O   ALA A  24      57.400  20.056  -1.984  0.50  9.08           O  
ATOM     38  CB  ALA A  24      56.886  21.119   1.044  0.50  6.42           C  
ATOM     39  N   SER A  25      55.248  19.875  -1.369  0.50  9.92           N  
ATOM     40  CA  SER A  25      54.769  19.985  -2.746  0.50 11.36           C  
ATOM     41  C   SER A  25      54.620  21.426  -3.226  0.50 11.80           C  
ATOM     42  O   SER A  25      54.586  21.685  -4.431  0.50 12.67           O  
ATOM     43  CB  SER A  25      53.430  19.255  -2.907  0.50 12.85           C  
ATOM     44  OG  SER A  25      52.391  19.950  -2.236  0.50 15.18           O  
ATOM     45  N   SER A  26      54.534  22.366  -2.292  0.50 11.56           N  
ATOM     46  CA  SER A  26      54.385  23.764  -2.661  0.50 11.01           C  
ATOM     47  C   SER A  26      55.731  24.314  -3.128  0.50 11.82           C  
ATOM     48  O   SER A  26      56.779  23.821  -2.728  0.50 11.55           O  
ATOM     49  CB  SER A  26      53.864  24.559  -1.471  0.50 11.16           C  
ATOM     50  OG  SER A  26      54.696  24.367  -0.343  0.50 11.47           O  
ATOM     51  N   PRO A  27      55.721  25.343  -3.991  0.50 11.90           N  
ATOM     52  CA  PRO A  27      57.001  25.878  -4.452  0.50 12.22           C  
ATOM     53  C   PRO A  27      57.849  26.401  -3.307  0.50 11.57           C  
ATOM     54  O   PRO A  27      57.367  27.149  -2.452  0.50 11.12           O  
ATOM     55  CB  PRO A  27      56.589  26.974  -5.430  0.50 11.69           C  
ATOM     56  CG  PRO A  27      55.308  27.454  -4.853  0.50 13.50           C  
ATOM     57  CD  PRO A  27      54.605  26.171  -4.476  0.50 11.97           C  
ATOM     58  N   VAL A  28      59.109  25.976  -3.291  0.50 10.90           N  
ATOM     59  CA  VAL A  28      60.062  26.401  -2.276  0.50 10.83           C  
ATOM     60  C   VAL A  28      61.394  26.742  -2.949  0.50 10.86           C  
ATOM     61  O   VAL A  28      61.810  26.080  -3.903  0.50 10.19           O  
ATOM     62  CB  VAL A  28      60.287  25.297  -1.224  0.50  9.49           C  
ATOM     63  CG1 VAL A  28      61.425  25.685  -0.279  0.50 11.35           C  
ATOM     64  CG2 VAL A  28      59.012  25.080  -0.426  0.50 10.58           C  
ATOM     65  N   THR A  29      62.041  27.793  -2.455  0.50 11.91           N  
ATOM     66  CA  THR A  29      63.334  28.224  -2.970  0.50 13.23           C  
ATOM     67  C   THR A  29      64.385  28.099  -1.874  0.50 13.06           C  
ATOM     68  O   THR A  29      64.224  28.642  -0.788  0.50 12.91           O  
ATOM     69  CB  THR A  29      63.316  29.696  -3.417  0.50 14.59           C  
ATOM     70  OG1 THR A  29      62.437  29.850  -4.537  0.50 15.57           O  
ATOM     71  CG2 THR A  29      64.722  30.139  -3.820  0.50 16.33           C  
ATOM     72  N   LEU A  30      65.452  27.363  -2.157  0.50 13.63           N  
ATOM     73  CA  LEU A  30      66.544  27.201  -1.208  0.50 12.32           C  
ATOM     74  C   LEU A  30      67.686  28.045  -1.749  0.50 11.45           C  
ATOM     75  O   LEU A  30      68.181  27.798  -2.851  0.50 12.35           O  
ATOM     76  CB  LEU A  30      66.979  25.736  -1.120  0.50 12.16           C  
ATOM     77  CG  LEU A  30      65.920  24.771  -0.584  0.50 11.97           C  
ATOM     78  CD1 LEU A  30      66.472  23.362  -0.597  0.50 11.55           C  
ATOM     79  CD2 LEU A  30      65.520  25.173   0.825  0.50 10.83           C  
ATOM     80  N   ALA A  31      68.085  29.051  -0.982  0.50  9.01           N  
ATOM     81  CA  ALA A  31      69.165  29.927  -1.389  0.50  8.06           C  
ATOM     82  C   ALA A  31      70.453  29.501  -0.717  0.50  6.48           C  
ATOM     83  O   ALA A  31      70.478  29.267   0.501  0.50  5.17           O  
ATOM     84  CB  ALA A  31      68.840  31.360  -1.020  0.50  8.06           C  
ATOM     85  N   GLU A  32      71.517  29.412  -1.514  0.50  4.97           N  
ATOM     86  CA  GLU A  32      72.839  29.026  -1.017  0.50  5.40           C  
ATOM     87  C   GLU A  32      73.874  30.080  -1.387  0.50  5.22           C  
ATOM     88  O   GLU A  32      73.726  30.773  -2.384  0.50  6.97           O  
ATOM     89  CB  GLU A  32      73.258  27.674  -1.614  0.50  2.22           C  
ATOM     90  CG  GLU A  32      74.617  27.148  -1.131  0.50  2.71           C  
ATOM     91  CD  GLU A  32      75.813  27.679  -1.937  0.50  2.53           C  
ATOM     92  OE1 GLU A  32      75.621  28.539  -2.822  0.50  1.66           O  
ATOM     93  OE2 GLU A  32      76.954  27.221  -1.688  0.50  1.94           O  
ATOM     94  N   THR A  33      74.913  30.205  -0.572  0.50  4.89           N  
ATOM     95  CA  THR A  33      76.002  31.138  -0.843  0.50  4.53           C  
ATOM     96  C   THR A  33      77.214  30.698  -0.035  0.50  4.25           C  
ATOM     97  O   THR A  33      77.074  30.086   1.038  0.50  3.85           O  
ATOM     98  CB  THR A  33      75.672  32.592  -0.426  0.50  4.01           C  
ATOM     99  OG1 THR A  33      76.634  33.474  -1.014  0.50  6.32           O  
ATOM    100  CG2 THR A  33      75.778  32.769   1.078  0.50  5.18           C  
ATOM    101  N   GLY A  34      78.402  31.004  -0.539  0.50  2.78           N  
ATOM    102  CA  GLY A  34      79.595  30.649   0.201  0.50  2.01           C  
ATOM    103  C   GLY A  34      80.754  30.069  -0.580  0.50  1.27           C  
ATOM    104  O   GLY A  34      81.044  30.481  -1.696  0.50  1.22           O  
ATOM    105  N   SER A  35      81.424  29.114   0.053  0.50  1.22           N  
ATOM    106  CA  SER A  35      82.588  28.430  -0.500  0.50  2.70           C  
ATOM    107  C   SER A  35      82.690  28.321  -2.020  0.50  2.22           C  
ATOM    108  O   SER A  35      81.881  27.646  -2.661  0.50  1.33           O  
ATOM    109  CB  SER A  35      82.668  27.014   0.079  0.50  1.78           C  
ATOM    110  OG  SER A  35      83.615  26.263  -0.643  0.50  1.22           O  
ATOM    111  N   THR A  36      83.690  28.968  -2.606  0.50  1.22           N  
ATOM    112  CA  THR A  36      83.845  28.832  -4.041  0.50  2.19           C  
ATOM    113  C   THR A  36      84.330  27.408  -4.307  0.50  1.77           C  
ATOM    114  O   THR A  36      84.143  26.872  -5.390  0.50  3.42           O  
ATOM    115  CB  THR A  36      84.848  29.843  -4.617  0.50  2.08           C  
ATOM    116  OG1 THR A  36      86.137  29.651  -4.019  0.50  1.22           O  
ATOM    117  CG2 THR A  36      84.353  31.258  -4.365  0.50  1.22           C  
ATOM    118  N   LEU A  37      84.936  26.778  -3.309  0.50  1.36           N  
ATOM    119  CA  LEU A  37      85.412  25.412  -3.486  0.50  2.55           C  
ATOM    120  C   LEU A  37      84.226  24.479  -3.747  0.50  2.71           C  
ATOM    121  O   LEU A  37      84.282  23.641  -4.636  0.50  1.57           O  
ATOM    122  CB  LEU A  37      86.204  24.959  -2.243  0.50  3.08           C  
ATOM    123  CG  LEU A  37      86.661  23.503  -2.030  0.50  4.24           C  
ATOM    124  CD1 LEU A  37      86.983  22.814  -3.338  0.50  4.73           C  
ATOM    125  CD2 LEU A  37      87.885  23.504  -1.119  0.50  1.73           C  
ATOM    126  N   LEU A  38      83.143  24.650  -2.992  0.50  3.47           N  
ATOM    127  CA  LEU A  38      81.957  23.805  -3.136  0.50  4.69           C  
ATOM    128  C   LEU A  38      81.019  24.250  -4.264  0.50  5.37           C  
ATOM    129  O   LEU A  38      80.185  23.471  -4.726  0.50  2.90           O  
ATOM    130  CB  LEU A  38      81.176  23.777  -1.815  0.50  4.18           C  
ATOM    131  CG  LEU A  38      79.955  22.843  -1.727  0.50  6.49           C  
ATOM    132  CD1 LEU A  38      80.394  21.407  -1.955  0.50  6.86           C  
ATOM    133  CD2 LEU A  38      79.287  22.963  -0.355  0.50  5.89           C  
ATOM    134  N   TYR A  39      81.172  25.499  -4.697  0.50  6.78           N  
ATOM    135  CA  TYR A  39      80.326  26.083  -5.740  0.50  8.08           C  
ATOM    136  C   TYR A  39      80.104  25.236  -7.004  0.50  7.59           C  
ATOM    137  O   TYR A  39      78.966  25.018  -7.402  0.50  8.10           O  
ATOM    138  CB  TYR A  39      80.859  27.472  -6.129  0.50  9.31           C  
ATOM    139  CG  TYR A  39      79.994  28.202  -7.137  0.50 12.04           C  
ATOM    140  CD1 TYR A  39      78.684  28.566  -6.825  0.50 12.86           C  
ATOM    141  CD2 TYR A  39      80.480  28.517  -8.406  0.50 13.15           C  
ATOM    142  CE1 TYR A  39      77.878  29.226  -7.751  0.50 14.63           C  
ATOM    143  CE2 TYR A  39      79.684  29.176  -9.339  0.50 14.34           C  
ATOM    144  CZ  TYR A  39      78.383  29.526  -9.005  0.50 14.61           C  
ATOM    145  OH  TYR A  39      77.585  30.165  -9.927  0.50 16.30           O  
ATOM    146  N   PRO A  40      81.177  24.757  -7.651  0.50  6.96           N  
ATOM    147  CA  PRO A  40      81.017  23.942  -8.860  0.50  7.30           C  
ATOM    148  C   PRO A  40      80.091  22.743  -8.640  0.50  8.06           C  
ATOM    149  O   PRO A  40      79.293  22.375  -9.512  0.50  8.30           O  
ATOM    150  CB  PRO A  40      82.437  23.487  -9.160  0.50  7.86           C  
ATOM    151  CG  PRO A  40      83.279  24.568  -8.577  0.50  7.24           C  
ATOM    152  CD  PRO A  40      82.596  24.859  -7.277  0.50  6.95           C  
ATOM    153  N   LEU A  41      80.197  22.122  -7.475  0.50  6.33           N  
ATOM    154  CA  LEU A  41      79.357  20.967  -7.192  0.50  6.98           C  
ATOM    155  C   LEU A  41      77.904  21.382  -6.993  0.50  6.13           C  
ATOM    156  O   LEU A  41      76.990  20.694  -7.434  0.50  4.97           O  
ATOM    157  CB  LEU A  41      79.865  20.228  -5.952  0.50  6.17           C  
ATOM    158  CG  LEU A  41      79.031  19.016  -5.514  0.50  6.24           C  
ATOM    159  CD1 LEU A  41      78.960  18.002  -6.634  0.50  5.45           C  
ATOM    160  CD2 LEU A  41      79.659  18.397  -4.273  0.50  3.90           C  
ATOM    161  N   PHE A  42      77.690  22.504  -6.320  0.50  6.02           N  
ATOM    162  CA  PHE A  42      76.333  22.962  -6.110  0.50  7.77           C  
ATOM    163  C   PHE A  42      75.686  23.286  -7.445  0.50  7.14           C  
ATOM    164  O   PHE A  42      74.467  23.288  -7.563  0.50  7.87           O  
ATOM    165  CB  PHE A  42      76.303  24.179  -5.188  0.50  8.23           C  
ATOM    166  CG  PHE A  42      75.562  23.936  -3.913  0.50  9.08           C  
ATOM    167  CD1 PHE A  42      74.181  24.043  -3.869  0.50  9.15           C  
ATOM    168  CD2 PHE A  42      76.241  23.537  -2.766  0.50 10.02           C  
ATOM    169  CE1 PHE A  42      73.481  23.755  -2.702  0.50 10.47           C  
ATOM    170  CE2 PHE A  42      75.547  23.245  -1.592  0.50  9.42           C  
ATOM    171  CZ  PHE A  42      74.169  23.354  -1.562  0.50  9.73           C  
ATOM    172  N   ASN A  43      76.496  23.550  -8.459  0.50  7.66           N  
ATOM    173  CA  ASN A  43      75.943  23.836  -9.774  0.50  8.48           C  
ATOM    174  C   ASN A  43      75.482  22.569 -10.458  0.50  7.67           C  
ATOM    175  O   ASN A  43      74.809  22.627 -11.484  0.50  7.55           O  
ATOM    176  CB  ASN A  43      76.967  24.537 -10.658  0.50 11.00           C  
ATOM    177  CG  ASN A  43      77.006  26.007 -10.417  0.50 12.18           C  
ATOM    178  OD1 ASN A  43      75.963  26.654 -10.375  0.50 14.82           O  
ATOM    179  ND2 ASN A  43      78.202  26.557 -10.259  0.50 15.35           N  
ATOM    180  N   LEU A  44      75.861  21.419  -9.905  0.50  7.16           N  
ATOM    181  CA  LEU A  44      75.439  20.140 -10.471  0.50  6.92           C  
ATOM    182  C   LEU A  44      74.266  19.642  -9.641  0.50  7.11           C  
ATOM    183  O   LEU A  44      73.216  19.270 -10.173  0.50  8.08           O  
ATOM    184  CB  LEU A  44      76.584  19.127 -10.433  0.50  4.59           C  
ATOM    185  CG  LEU A  44      77.819  19.524 -11.244  0.50  5.22           C  
ATOM    186  CD1 LEU A  44      78.843  18.403 -11.215  0.50  2.23           C  
ATOM    187  CD2 LEU A  44      77.397  19.838 -12.684  0.50  3.43           C  
ATOM    188  N   TRP A  45      74.441  19.652  -8.326  0.50  5.86           N  
ATOM    189  CA  TRP A  45      73.391  19.210  -7.429  0.50  5.34           C  
ATOM    190  C   TRP A  45      72.103  19.989  -7.653  0.50  5.51           C  
ATOM    191  O   TRP A  45      71.042  19.399  -7.769  0.50  5.72           O  
ATOM    192  CB  TRP A  45      73.813  19.401  -5.974  0.50  3.99           C  
ATOM    193  CG  TRP A  45      74.762  18.394  -5.458  0.50  2.24           C  
ATOM    194  CD1 TRP A  45      75.101  17.205  -6.036  0.50  1.98           C  
ATOM    195  CD2 TRP A  45      75.432  18.435  -4.198  0.50  2.32           C  
ATOM    196  NE1 TRP A  45      75.936  16.497  -5.206  0.50  2.68           N  
ATOM    197  CE2 TRP A  45      76.151  17.232  -4.068  0.50  3.02           C  
ATOM    198  CE3 TRP A  45      75.485  19.373  -3.158  0.50  4.65           C  
ATOM    199  CZ2 TRP A  45      76.919  16.942  -2.944  0.50  2.60           C  
ATOM    200  CZ3 TRP A  45      76.248  19.086  -2.045  0.50  3.17           C  
ATOM    201  CH2 TRP A  45      76.952  17.878  -1.944  0.50  3.61           C  
ATOM    202  N   GLY A  46      72.216  21.315  -7.684  0.50  6.25           N  
ATOM    203  CA  GLY A  46      71.069  22.187  -7.859  0.50  7.68           C  
ATOM    204  C   GLY A  46      70.130  21.811  -8.983  0.50  9.55           C  
ATOM    205  O   GLY A  46      68.920  21.696  -8.777  0.50 10.47           O  
ATOM    206  N   PRO A  47      70.656  21.633 -10.198  0.50 10.15           N  
ATOM    207  CA  PRO A  47      69.817  21.264 -11.340  0.50  9.92           C  
ATOM    208  C   PRO A  47      69.254  19.854 -11.234  0.50  9.98           C  
ATOM    209  O   PRO A  47      68.112  19.613 -11.611  0.50 11.45           O  
ATOM    210  CB  PRO A  47      70.767  21.414 -12.520  0.50 10.35           C  
ATOM    211  CG  PRO A  47      71.669  22.536 -12.071  0.50 10.89           C  
ATOM    212  CD  PRO A  47      71.965  22.136 -10.649  0.50  9.86           C  
ATOM    213  N   ALA A  48      70.052  18.923 -10.727  0.50  8.69           N  
ATOM    214  CA  ALA A  48      69.609  17.547 -10.605  0.50  8.44           C  
ATOM    215  C   ALA A  48      68.404  17.449  -9.694  0.50  8.19           C  
ATOM    216  O   ALA A  48      67.392  16.856 -10.046  0.50  8.67           O  
ATOM    217  CB  ALA A  48      70.734  16.675 -10.067  0.50  8.50           C  
ATOM    218  N   PHE A  49      68.510  18.043  -8.518  0.50  7.87           N  
ATOM    219  CA  PHE A  49      67.423  17.987  -7.551  0.50  8.46           C  
ATOM    220  C   PHE A  49      66.184  18.673  -8.092  0.50  9.44           C  
ATOM    221  O   PHE A  49      65.063  18.214  -7.871  0.50  8.04           O  
ATOM    222  CB  PHE A  49      67.838  18.659  -6.252  0.50  5.79           C  
ATOM    223  CG  PHE A  49      66.903  18.411  -5.126  0.50  4.22           C  
ATOM    224  CD1 PHE A  49      66.841  17.160  -4.519  0.50  2.83           C  
ATOM    225  CD2 PHE A  49      66.110  19.432  -4.639  0.50  2.47           C  
ATOM    226  CE1 PHE A  49      65.998  16.940  -3.433  0.50  3.84           C  
ATOM    227  CE2 PHE A  49      65.267  19.222  -3.557  0.50  2.70           C  
ATOM    228  CZ  PHE A  49      65.208  17.980  -2.951  0.50  3.05           C  
ATOM    229  N   HIS A  50      66.393  19.779  -8.794  0.50 11.27           N  
ATOM    230  CA  HIS A  50      65.287  20.531  -9.367  0.50 14.41           C  
ATOM    231  C   HIS A  50      64.596  19.709 -10.441  0.50 16.00           C  
ATOM    232  O   HIS A  50      63.376  19.696 -10.530  0.50 18.18           O  
ATOM    233  CB  HIS A  50      65.787  21.851  -9.946  0.50 12.62           C  
ATOM    234  CG  HIS A  50      64.720  22.651 -10.626  0.50 14.10           C  
ATOM    235  ND1 HIS A  50      64.445  22.534 -11.971  0.50 13.32           N  
ATOM    236  CD2 HIS A  50      63.840  23.559 -10.138  0.50 12.76           C  
ATOM    237  CE1 HIS A  50      63.442  23.337 -12.284  0.50 13.57           C  
ATOM    238  NE2 HIS A  50      63.058  23.969 -11.189  0.50 13.83           N  
ATOM    239  N   GLU A  51      65.379  19.017 -11.253  0.50 18.89           N  
ATOM    240  CA  GLU A  51      64.827  18.176 -12.305  0.50 22.07           C  
ATOM    241  C   GLU A  51      63.870  17.153 -11.707  0.50 21.87           C  
ATOM    242  O   GLU A  51      62.823  16.864 -12.274  0.50 22.14           O  
ATOM    243  CB  GLU A  51      65.964  17.450 -13.027  0.50 26.22           C  
ATOM    244  CG  GLU A  51      65.557  16.166 -13.740  0.50 33.86           C  
ATOM    245  CD  GLU A  51      65.568  16.297 -15.256  0.50 38.64           C  
ATOM    246  OE1 GLU A  51      66.629  16.665 -15.813  0.50 40.68           O  
ATOM    247  OE2 GLU A  51      64.519  16.026 -15.891  0.50 41.87           O  
ATOM    248  N   ARG A  52      64.246  16.617 -10.550  0.50 22.49           N  
ATOM    249  CA  ARG A  52      63.470  15.595  -9.847  0.50 22.89           C  
ATOM    250  C   ARG A  52      62.232  16.170  -9.170  0.50 21.59           C  
ATOM    251  O   ARG A  52      61.175  15.552  -9.160  0.50 22.08           O  
ATOM    252  CB  ARG A  52      64.359  14.925  -8.797  0.50 25.72           C  
ATOM    253  CG  ARG A  52      64.131  13.438  -8.590  0.50 31.16           C  
ATOM    254  CD  ARG A  52      62.724  13.125  -8.122  0.50 36.49           C  
ATOM    255  NE  ARG A  52      62.574  11.715  -7.763  0.50 41.29           N  
ATOM    256  CZ  ARG A  52      61.409  11.125  -7.503  0.50 42.78           C  
ATOM    257  NH1 ARG A  52      60.276  11.815  -7.575  0.50 43.53           N  
ATOM    258  NH2 ARG A  52      61.374   9.837  -7.181  0.50 44.69           N  
ATOM    259  N   TYR A  53      62.375  17.355  -8.597  0.50 19.66           N  
ATOM    260  CA  TYR A  53      61.273  18.015  -7.906  0.50 18.25           C  
ATOM    261  C   TYR A  53      61.197  19.433  -8.445  0.50 16.48           C  
ATOM    262  O   TYR A  53      61.735  20.357  -7.846  0.50 16.32           O  
ATOM    263  CB  TYR A  53      61.554  18.057  -6.411  0.50 17.23           C  
ATOM    264  CG  TYR A  53      61.833  16.708  -5.803  0.50 17.31           C  
ATOM    265  CD1 TYR A  53      60.793  15.887  -5.379  0.50 17.37           C  
ATOM    266  CD2 TYR A  53      63.138  16.260  -5.632  0.50 16.53           C  
ATOM    267  CE1 TYR A  53      61.043  14.660  -4.796  0.50 17.27           C  
ATOM    268  CE2 TYR A  53      63.399  15.036  -5.053  0.50 17.87           C  
ATOM    269  CZ  TYR A  53      62.346  14.241  -4.634  0.50 18.29           C  
ATOM    270  OH  TYR A  53      62.597  13.025  -4.039  0.50 21.71           O  
ATOM    271  N   PRO A  54      60.517  19.619  -9.586  0.50 15.77           N  
ATOM    272  CA  PRO A  54  



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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: April 25th, 2023.