CNRS Nantes University UFIP UFIP
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***  2x2e_chainA  ***

elNémo ID: 190813194333122817

Job options:

ID        	=	 190813194333122817
JOBID     	=	 2x2e_chainA
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:

HEADER 2x2e_chainA

HEADER    HYDROLASE                               12-JAN-10   2X2E              
TITLE     DYNAMIN GTPASE DIMER, LONG AXIS FORM                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DYNAMIN-1;                                                 
COMPND   3 CHAIN: A, D;                                                         
COMPND   4 FRAGMENT: GTPASE DOMAIN, RESIDUES 6-320, GTPASE EFFECTOR DOMAIN,     
COMPND   5 RESIDUES 726-750;                                                    
COMPND   6 EC: 3.6.5.5;                                                         
COMPND   7 ENGINEERED: YES;                                                     
COMPND   8 OTHER_DETAILS: EIGHT AMINO ACIDS LONG ARTIFICIAL POLYPEPTIDE LINKER  
COMPND   9 BETWEEN GTPASE DOMAIN AND GTPASE ACTIVATING DOMAIN, RESIDUES 321-328 
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3)                                  
KEYWDS    NITRATION, HYDROLASE, MEMBRANE FISSION, NUCLEOTIDE-BINDING,           
KEYWDS   2 ENDOCYTOSIS, MOTOR PROTEIN                                           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.S.CHAPPIE,S.ACHARYA,M.LEONARD,S.L.SCHMID,F.DYDA                     
REVDAT   5   08-MAY-19 2X2E    1       REMARK LINK                              
REVDAT   4   31-AUG-11 2X2E    1       COMPND REMARK DBREF  SEQADV              
REVDAT   4 2                   1       SEQRES VERSN                             
REVDAT   3   02-JUN-10 2X2E    1       JRNL                                     
REVDAT   2   12-MAY-10 2X2E    1       JRNL                                     
REVDAT   1   28-APR-10 2X2E    0                                                
JRNL        AUTH   J.S.CHAPPIE,S.ACHARYA,M.LEONARD,S.L.SCHMID,F.DYDA            
JRNL        TITL   G DOMAIN DIMERIZATION CONTROLS DYNAMIN'S ASSEMBLY-STIMULATED 
JRNL        TITL 2 GTPASE ACTIVITY.                                             
JRNL        REF    NATURE                        V. 465   435 2010              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   20428113                                                     
JRNL        DOI    10.1038/NATURE09032                                          
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.00 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : CNS 1.1                                              
REMARK   3   AUTHORS     : BRUNGER,ADAMS,CLORE,DELANO,GROS,GROSSE-              
REMARK   3               : KUNSTLEVE,JIANG,KUSZEWSKI,NILGES,PANNU,              
REMARK   3               : READ,RICE,SIMONSON,WARREN                            
REMARK   3                                                                      
REMARK   3  REFINEMENT TARGET : NULL                                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.00                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 30.00                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   DATA CUTOFF HIGH         (ABS(F)) : NULL                           
REMARK   3   DATA CUTOFF LOW          (ABS(F)) : NULL                           
REMARK   3   COMPLETENESS (WORKING+TEST)   (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 44405                          
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) : 0.185                           
REMARK   3   FREE R VALUE                     : 0.230                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 2.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 899                             
REMARK   3   ESTIMATED ERROR OF FREE R VALUE  : 0.010                           
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : NULL                         
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.00                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.05                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   REFLECTIONS IN BIN    (WORKING SET) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : NULL                         
REMARK   3   BIN FREE R VALUE                    : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET SIZE  (%) : NULL                         
REMARK   3   BIN FREE R VALUE TEST SET COUNT     : NULL                         
REMARK   3   ESTIMATED ERROR OF BIN FREE R VALUE : NULL                         
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5350                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 70                                      
REMARK   3   SOLVENT ATOMS            : 619                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 16.80                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : NULL                                                 
REMARK   3    B22 (A**2) : NULL                                                 
REMARK   3    B33 (A**2) : NULL                                                 
REMARK   3    B12 (A**2) : NULL                                                 
REMARK   3    B13 (A**2) : NULL                                                 
REMARK   3    B23 (A**2) : NULL                                                 
REMARK   3                                                                      
REMARK   3  ESTIMATED COORDINATE ERROR.                                         
REMARK   3   ESD FROM LUZZATI PLOT        (A) : NULL                            
REMARK   3   ESD FROM SIGMAA              (A) : NULL                            
REMARK   3   LOW RESOLUTION CUTOFF        (A) : NULL                            
REMARK   3                                                                      
REMARK   3  CROSS-VALIDATED ESTIMATED COORDINATE ERROR.                         
REMARK   3   ESD FROM C-V LUZZATI PLOT    (A) : NULL                            
REMARK   3   ESD FROM C-V SIGMAA          (A) : NULL                            
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES.                                   
REMARK   3   BOND LENGTHS                 (A) : 0.011                           
REMARK   3   BOND ANGLES            (DEGREES) : 2.630                           
REMARK   3   DIHEDRAL ANGLES        (DEGREES) : NULL                            
REMARK   3   IMPROPER ANGLES        (DEGREES) : NULL                            
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL MODEL : NULL                                      
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.    RMS    SIGMA                
REMARK   3   MAIN-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   MAIN-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN BOND              (A**2) : NULL  ; NULL                 
REMARK   3   SIDE-CHAIN ANGLE             (A**2) : NULL  ; NULL                 
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELING.                                              
REMARK   3   METHOD USED : NULL                                                 
REMARK   3   KSOL        : NULL                                                 
REMARK   3   BSOL        : NULL                                                 
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  : PARHCSDX.PRO                                   
REMARK   3  PARAMETER FILE  2  : NULL                                           
REMARK   3  TOPOLOGY FILE  1   : TOPHCSDX.PRO                                   
REMARK   3  TOPOLOGY FILE  2   : NULL                                           
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: NULL                                      
REMARK   4                                                                      
REMARK   4 2X2E COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 12-JAN-10.                  
REMARK 100 THE DEPOSITION ID IS D_1290042392.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 22-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.96863                            
REMARK 200  MONOCHROMATOR                  : SI111                              
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XSCALE                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 44405                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.000                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 30.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.8                               
REMARK 200  DATA REDUNDANCY                : 7.160                              
REMARK 200  R MERGE                    (I) : 0.07000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 21.4000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.00                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.05                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.6                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 7.25                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.20000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 11.70                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: SIRAS                        
REMARK 200 SOFTWARE USED: SHARPD, DM                                            
REMARK 200 STARTING MODEL: NONE                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 39.00                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.04                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: HANGING DROP VAPOR DIFFUSION IN 0.1M     
REMARK 280  TRIS PH 8.5, 25% PEG 3350, 200MM NACL, 25-35% NAF USING A DROP      
REMARK 280  SIZE OF 2-10 MICROL AND A RESERVOIR VOLUME OF 750 MICROL.           
REMARK 280  CRYSTALS GREW IN 4-5 DAYS AT EITHER 17C OR 20C., VAPOR DIFFUSION,   
REMARK 280  HANGING DROP                                                        
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       21.80500            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       90.77000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       40.51000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       90.77000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       21.80500            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       40.51000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5580 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 29890 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -68.8 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, D                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLY A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     GLU A     3                                                      
REMARK 465     PHE A     4                                                      
REMARK 465     SER A     5                                                      
REMARK 465     ASN A   744                                                      
REMARK 465     ILE A   745                                                      
REMARK 465     ASN A   746                                                      
REMARK 465     THR A   747                                                      
REMARK 465     THR A   748                                                      
REMARK 465     THR A   749                                                      
REMARK 465     VAL A   750                                                      
REMARK 465     GLY D     1                                                      
REMARK 465     PRO D     2                                                      
REMARK 465     GLU D     3                                                      
REMARK 465     PHE D     4                                                      
REMARK 465     SER D     5                                                      
REMARK 465     ASN D   744                                                      
REMARK 465     ILE D   745                                                      
REMARK 465     ASN D   746                                                      
REMARK 465     THR D   747                                                      
REMARK 465     THR D   748                                                      
REMARK 465     THR D   749                                                      
REMARK 465     VAL D   750                                                      
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    ASP A  30       74.84   -150.21                                   
REMARK 500    PHE A  56      -12.01   -156.21                                   
REMARK 500    CYS A  86       68.79   -108.30                                   
REMARK 500    LYS A 113        0.12     80.67                                   
REMARK 500    PRO A 319      -18.54    -48.10                                   
REMARK 500    ASP A 320      170.59     70.67                                   
REMARK 500    ASN D  26       90.32     18.99                                   
REMARK 500    ASP D  28       71.68   -100.35                                   
REMARK 500    ASP D  55       19.23     59.94                                   
REMARK 500    GLU D 313       37.16    -98.90                                   
REMARK 500    LYS D 315       23.00    165.88                                   
REMARK 500    ASN D 316     -101.22    -15.39                                   
REMARK 500    PRO D 319     -178.88    -60.90                                   
REMARK 500    LYS D 321      -64.30     20.11                                   
REMARK 500    HIS D 322     -149.18    -64.38                                   
REMARK 500    ILE D 742       23.23    -68.75                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A1746  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A1744   O1B                                                    
REMARK 620 2 SER A  45   OG   90.8                                              
REMARK 620 3 THR A  65   OG1 173.1  91.0                                        
REMARK 620 4 ALF A1745   F4   93.3 171.6  85.8                                  
REMARK 620 5 HOH A2139   O    91.0  92.2  95.5  80.4                            
REMARK 620 6 HOH A2331   O    81.6  90.0  91.7  97.9 172.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA A1747  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A1744   O3B                                                    
REMARK 620 2 ALF A1745   F3   57.9                                              
REMARK 620 3 SER A  41   OG  102.0  89.4                                        
REMARK 620 4 ALF A1745   F1   57.9  56.6 145.7                                  
REMARK 620 5 GLY A  60   O   114.2 168.6 100.7 112.7                            
REMARK 620 6 GLY A  62   O   141.2  83.9  82.5  97.1 102.5                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF A1745  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP A1744   O3B                                                    
REMARK 620 2 ALF A1745   F1   91.8                                              
REMARK 620 3 ALF A1745   F2   89.4 176.6                                        
REMARK 620 4 ALF A1745   F3   88.3  86.8  90.1                                  
REMARK 620 5 ALF A1745   F4   89.6  89.4  93.8 175.6                            
REMARK 620 6  MG A1746  MG    71.5  81.9 101.5 156.4  20.0                      
REMARK 620 7  NA A1747  NA    61.3  54.6 123.5  46.2 129.4 111.2                
REMARK 620 8 HOH A2071   O   178.5  89.3  89.5  90.8  91.4 109.7 118.7          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              NA D1747  NA                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP D1744   O3B                                                    
REMARK 620 2 SER D  41   OG   98.4                                              
REMARK 620 3 GLY D  60   O   113.1  99.8                                        
REMARK 620 4 ALF D1745   F1   59.3 145.2 113.2                                  
REMARK 620 5 ALF D1745   F3   58.1  88.6 169.0  57.3                            
REMARK 620 6 GLY D  62   O   145.6  87.5  99.0  97.5  88.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG D1746  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 GDP D1744   O1B                                                    
REMARK 620 2 THR D  65   OG1 173.2                                              
REMARK 620 3 HOH D2115   O    94.3  92.5                                        
REMARK 620 4 ALF D1745   F4   96.0  84.7  85.0                                  
REMARK 620 5 SER D  45   OG   92.0  88.1  87.8 169.6                            
REMARK 620 6 HOH D2287   O    85.0  88.2 176.1  99.0  88.4                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             ALF D1745  AL                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HOH D2051   O                                                      
REMARK 620 2 ALF D1745   F1   88.8                                              
REMARK 620 3 ALF D1745   F2   87.6 174.2                                        
REMARK 620 4 ALF D1745   F3   90.9  86.9  88.7                                  
REMARK 620 5 ALF D1745   F4   90.7  91.1  93.5 177.4                            
REMARK 620 6  NA D1747  NA   118.8  53.6 124.9  47.5 129.9                      
REMARK 620 7  MG D1746  MG   110.4  82.3 103.2 155.7  21.9 109.6                
REMARK 620 8 GDP D1744   O3B 178.1  92.8  90.7  88.2  90.2  61.7  70.8          
REMARK 620 N                    1     2     3     4     5     6     7           
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP A 1744                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF A 1745                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 1746                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA A 1747                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE GDP D 1744                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ALF D 1745                
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG D 1746                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NA D 1747                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 2X2F   RELATED DB: PDB                                   
REMARK 900 DYNAMIN 1 GTPASE DIMER, SHORT AXIS FORM                              
REMARK 900 RELATED ID: 2DYN   RELATED DB: PDB                                   
REMARK 900 DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)                         
REMARK 900 RELATED ID: 1DYN   RELATED DB: PDB                                   
REMARK 900 DYNAMIN (PLECKSTRIN HOMOLOGY DOMAIN) (DYNPH)                         
DBREF  2X2E A    6   320  UNP    Q05193   DYN1_HUMAN       6    320             
DBREF  2X2E A  726   750  UNP    Q05193   DYN1_HUMAN     726    750             
DBREF  2X2E D    6   320  UNP    Q05193   DYN1_HUMAN       6    320             
DBREF  2X2E D  726   750  UNP    Q05193   DYN1_HUMAN     726    750             
SEQADV 2X2E GLY A    1  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E PRO A    2  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E GLU A    3  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E PHE A    4  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E SER A    5  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E LYS A  321  UNP  Q05193              LINKER                         
SEQADV 2X2E HIS A  322  UNP  Q05193              LINKER                         
SEQADV 2X2E GLY A  323  UNP  Q05193              LINKER                         
SEQADV 2X2E THR A  324  UNP  Q05193              LINKER                         
SEQADV 2X2E ASP A  325  UNP  Q05193              LINKER                         
SEQADV 2X2E SER A  326  UNP  Q05193              LINKER                         
SEQADV 2X2E ARG A  327  UNP  Q05193              LINKER                         
SEQADV 2X2E VAL A  328  UNP  Q05193              LINKER                         
SEQADV 2X2E ASN A  744  UNP  Q05193    ASP   744 VARIANT                        
SEQADV 2X2E GLY D    1  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E PRO D    2  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E GLU D    3  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E PHE D    4  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E SER D    5  UNP  Q05193              CLONING ARTIFACT               
SEQADV 2X2E LYS D  321  UNP  Q05193              LINKER                         
SEQADV 2X2E HIS D  322  UNP  Q05193              LINKER                         
SEQADV 2X2E GLY D  323  UNP  Q05193              LINKER                         
SEQADV 2X2E THR D  324  UNP  Q05193              LINKER                         
SEQADV 2X2E ASP D  325  UNP  Q05193              LINKER                         
SEQADV 2X2E SER D  326  UNP  Q05193              LINKER                         
SEQADV 2X2E ARG D  327  UNP  Q05193              LINKER                         
SEQADV 2X2E VAL D  328  UNP  Q05193              LINKER                         
SEQADV 2X2E ASN D  744  UNP  Q05193    ASP   744 VARIANT                        
SEQRES   1 A  353  GLY PRO GLU PHE SER MSE GLU ASP LEU ILE PRO LEU VAL          
SEQRES   2 A  353  ASN ARG LEU GLN ASP ALA PHE SER ALA ILE GLY GLN ASN          
SEQRES   3 A  353  ALA ASP LEU ASP LEU PRO GLN ILE ALA VAL VAL GLY GLY          
SEQRES   4 A  353  GLN SER ALA GLY LYS SER SER VAL LEU GLU ASN PHE VAL          
SEQRES   5 A  353  GLY ARG ASP PHE LEU PRO ARG GLY SER GLY ILE VAL THR          
SEQRES   6 A  353  ARG ARG PRO LEU VAL LEU GLN LEU VAL ASN ALA THR THR          
SEQRES   7 A  353  GLU TYR ALA GLU PHE LEU HIS CYS LYS GLY LYS LYS PHE          
SEQRES   8 A  353  THR ASP PHE GLU GLU VAL ARG LEU GLU ILE GLU ALA GLU          
SEQRES   9 A  353  THR ASP ARG VAL THR GLY THR ASN LYS GLY ILE SER PRO          
SEQRES  10 A  353  VAL PRO ILE ASN LEU ARG VAL TYR SER PRO HIS VAL LEU          
SEQRES  11 A  353  ASN LEU THR LEU VAL ASP LEU PRO GLY MSE THR LYS VAL          
SEQRES  12 A  353  PRO VAL GLY ASP GLN PRO PRO ASP ILE GLU PHE GLN ILE          
SEQRES  13 A  353  ARG ASP MSE LEU MSE GLN PHE VAL THR LYS GLU ASN CYS          
SEQRES  14 A  353  LEU ILE LEU ALA VAL SER PRO ALA ASN SER ASP LEU ALA          
SEQRES  15 A  353  ASN SER ASP ALA LEU LYS VAL ALA LYS GLU VAL ASP PRO          
SEQRES  16 A  353  GLN GLY GLN ARG THR ILE GLY VAL ILE THR LYS LEU ASP          
SEQRES  17 A  353  LEU MSE ASP GLU GLY THR ASP ALA ARG ASP VAL LEU GLU          
SEQRES  18 A  353  ASN LYS LEU LEU PRO LEU ARG ARG GLY TYR ILE GLY VAL          
SEQRES  19 A  353  VAL ASN ARG SER GLN LYS ASP ILE ASP GLY LYS LYS ASP          
SEQRES  20 A  353  ILE THR ALA ALA LEU ALA ALA GLU ARG LYS PHE PHE LEU          
SEQRES  21 A  353  SER HIS PRO SER TYR ARG HIS LEU ALA ASP ARG MSE GLY          
SEQRES  22 A  353  THR PRO TYR LEU GLN LYS VAL LEU ASN GLN GLN LEU THR          
SEQRES  23 A  353  ASN HIS ILE ARG ASP THR LEU PRO GLY LEU ARG ASN LYS          
SEQRES  24 A  353  LEU GLN SER GLN LEU LEU SER ILE GLU LYS GLU VAL GLU          
SEQRES  25 A  353  GLU TYR LYS ASN PHE ARG PRO ASP LYS HIS GLY THR ASP          
SEQRES  26 A  353  SER ARG VAL ASP GLU MSE LEU ARG MSE TYR HIS ALA LEU          
SEQRES  27 A  353  LYS GLU ALA LEU SER ILE ILE GLY ASN ILE ASN THR THR          
SEQRES  28 A  353  THR VAL                                                      
SEQRES   1 D  353  GLY PRO GLU PHE SER MSE GLU ASP LEU ILE PRO LEU VAL          
SEQRES   2 D  353  ASN ARG LEU GLN ASP ALA PHE SER ALA ILE GLY GLN ASN          
SEQRES   3 D  353  ALA ASP LEU ASP LEU PRO GLN ILE ALA VAL VAL GLY GLY          
SEQRES   4 D  353  GLN SER ALA GLY LYS SER SER VAL LEU GLU ASN PHE VAL          
SEQRES   5 D  353  GLY ARG ASP PHE LEU PRO ARG GLY SER GLY ILE VAL THR          
SEQRES   6 D  353  ARG ARG PRO LEU VAL LEU GLN LEU VAL ASN ALA THR THR          
SEQRES   7 D  353  GLU TYR ALA GLU PHE LEU HIS CYS LYS GLY LYS LYS PHE          
SEQRES   8 D  353  THR ASP PHE GLU GLU VAL ARG LEU GLU ILE GLU ALA GLU          
SEQRES   9 D  353  THR ASP ARG VAL THR GLY THR ASN LYS GLY ILE SER PRO          
SEQRES  10 D  353  VAL PRO ILE ASN LEU ARG VAL TYR SER PRO HIS VAL LEU          
SEQRES  11 D  353  ASN LEU THR LEU VAL ASP LEU PRO GLY MSE THR LYS VAL          
SEQRES  12 D  353  PRO VAL GLY ASP GLN PRO PRO ASP ILE GLU PHE GLN ILE          
SEQRES  13 D  353  ARG ASP MSE LEU MSE GLN PHE VAL THR LYS GLU ASN CYS          
SEQRES  14 D  353  LEU ILE LEU ALA VAL SER PRO ALA ASN SER ASP LEU ALA          
SEQRES  15 D  353  ASN SER ASP ALA LEU LYS VAL ALA LYS GLU VAL ASP PRO          
SEQRES  16 D  353  GLN GLY GLN ARG THR ILE GLY VAL ILE THR LYS LEU ASP          
SEQRES  17 D  353  LEU MSE ASP GLU GLY THR ASP ALA ARG ASP VAL LEU GLU          
SEQRES  18 D  353  ASN LYS LEU LEU PRO LEU ARG ARG GLY TYR ILE GLY VAL          
SEQRES  19 D  353  VAL ASN ARG SER GLN LYS ASP ILE ASP GLY LYS LYS ASP          
SEQRES  20 D  353  ILE THR ALA ALA LEU ALA ALA GLU ARG LYS PHE PHE LEU          
SEQRES  21 D  353  SER HIS PRO SER TYR ARG HIS LEU ALA ASP ARG MSE GLY          
SEQRES  22 D  353  THR PRO TYR LEU GLN LYS VAL LEU ASN GLN GLN LEU THR          
SEQRES  23 D  353  ASN HIS ILE ARG ASP THR LEU PRO GLY LEU ARG ASN LYS          
SEQRES  24 D  353  LEU GLN SER GLN LEU LEU SER ILE GLU LYS GLU VAL GLU          
SEQRES  25 D  353  GLU TYR LYS ASN PHE ARG PRO ASP LYS HIS GLY THR ASP          
SEQRES  26 D  353  SER ARG VAL ASP GLU MSE LEU ARG MSE TYR HIS ALA LEU          
SEQRES  27 D  353  LYS GLU ALA LEU SER ILE ILE GLY ASN ILE ASN THR THR          
SEQRES  28 D  353  THR VAL                                                      
MODRES 2X2E MSE A    6  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  140  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  159  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  161  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  210  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  272  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  728  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE A  731  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D    6  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  140  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  159  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  161  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  210  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  272  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  728  MET  SELENOMETHIONINE                                   
MODRES 2X2E MSE D  731  MET  SELENOMETHIONINE                                   
HET    MSE  A   6       8                                                       
HET    MSE  A 140       8                                                       
HET    MSE  A 159       8                                                       
HET    MSE  A 161       8                                                       
HET    MSE  A 210       8                                                       
HET    MSE  A 272       8                                                       
HET    MSE  A 728       8                                                       
HET    MSE  A 731       8                                                       
HET    MSE  D   6       8                                                       
HET    MSE  D 140       8                                                       
HET    MSE  D 159       8                                                       
HET    MSE  D 161       8                                                       
HET    MSE  D 210       8                                                       
HET    MSE  D 272       8                                                       
HET    MSE  D 728       8                                                       
HET    MSE  D 731       8                                                       
HET    GDP  A1744      28                                                       
HET    ALF  A1745       5                                                       
HET     MG  A1746       1                                                       
HET     NA  A1747       1                                                       
HET    GDP  D1744      28                                                       
HET    ALF  D1745       5                                                       
HET     MG  D1746       1                                                       
HET     NA  D1747       1                                                       
HETNAM     MSE SELENOMETHIONINE                                                 
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     ALF TETRAFLUOROALUMINATE ION                                         
HETNAM      MG MAGNESIUM ION                                                    
HETNAM      NA SODIUM ION                                                       
FORMUL   1  MSE    16(C5 H11 N O2 SE)                                           
FORMUL   3  GDP    2(C10 H15 N5 O11 P2)                                         
FORMUL   4  ALF    2(AL F4 1-)                                                  
FORMUL   5   MG    2(MG 2+)                                                     
FORMUL   6   NA    2(NA 1+)                                                     
FORMUL  11  HOH   *619(H2 O)                                                    
HELIX    1   1 LEU A    9  ALA A   22  1                                  14
HELIX    2   2 GLN A   25  LEU A   29  1                                   5
HELIX    3   3 GLY A   43  ASN A   50  1                                   8
HELIX    4   4 ASP A   93  GLY A  110  1                                  18
HELIX    5   5 ASP A  151  THR A  165  1                                  15
HELIX    6   6 ASP A  180  ASP A  194  1                                  15
HELIX    7   7 LYS A  206  MSE A  210  1                                   5
HELIX    8   8 ALA A  216  GLU A  221  1                                   6
HELIX    9   9 SER A  238  GLY A  244  1                                   7
HELIX   10  10 ASP A  247  HIS A  262  1                                  16
HELIX   11  11 TYR A  265  ARG A  318  1                                  54
HELIX   12  12 ASP A  325  ILE A  742  1                                  21
SHEET    1   1 1 GLN A  33  VAL A  37  0
SHEET    2   2 1 LEU A  69  ASN A  75  0
SHEET    3   3 1 TYR A  80  PHE A  83  0
SHEET    4   4 1 ILE A 120  SER A 126  0
SHEET    5   5 1 LEU A 132  ASP A 136  0
SHEET    6   6 1 CYS A 169  PRO A 176  0
SHEET    7   7 1 THR A 200  THR A 205  0
SHEET    8   8 1 TYR A 231  GLY A 233  0
LINK         C   MSE A   6                 N   GLU A   7     1555   1555  1.33  
LINK         C   GLY A 139                 N   MSE A 140     1555   1555  1.33  
LINK         C   MSE A 140                 N   THR A 141     1555   1555  1.33  
LINK         C   ASP A 158                 N   MSE A 159     1555   1555  1.32  
LINK         C   MSE A 159                 N   LEU A 160     1555   1555  1.33  
LINK         C   LEU A 160                 N   MSE A 161     1555   1555  1.33  
LINK         C   MSE A 161                 N   GLN A 162     1555   1555  1.33  
LINK         C   LEU A 209                 N   MSE A 210     1555   1555  1.33  
LINK         C   MSE A 210                 N   ASP A 211     1555   1555  1.32  
LINK         C   ARG A 271                 N   MSE A 272     1555   1555  1.33  
LINK         C   MSE A 272                 N   GLY A 273     1555   1555  1.33  
LINK         C   GLU A 727                 N   MSE A 728     1555   1555  1.33  
LINK         C   MSE A 728                 N   LEU A 729     1555   1555  1.33  
LINK         C   ARG A 730                 N   MSE A 731     1555   1555  1.33  
LINK         C   MSE A 731                 N   TYR A 732     1555   1555  1.33  
LINK         O1B GDP A1744                MG    MG A1746     1555   1555  2.04  
LINK         O3B GDP A1744                NA    NA A1747     1555   1555  2.95  
LINK        AL   ALF A1745                 O3B GDP A1744     1555   1555  2.02  
LINK        AL   ALF A1745                MG    MG A1746     1555   1555  3.47  
LINK        AL   ALF A1745                NA    NA A1747     1555   1555  3.33  
LINK        AL   ALF A1745                 O   HOH A2071     1555   1555  2.07  
LINK        MG    MG A1746                 OG  SER A  45     1555   1555  1.94  
LINK        MG    MG A1746                 OG1 THR A  65     1555   1555  2.06  
LINK        MG    MG A1746                 F4  ALF A1745     1555   1555  1.89  
LINK        MG    MG A1746                 O   HOH A2139     1555   1555  2.06  
LINK        MG    MG A1746                 O   HOH A2331     1555   1555  2.06  
LINK        NA    NA A1747                 F3  ALF A1745     1555   1555  2.46  
LINK        NA    NA A1747                 OG  SER A  41     1555   1555  2.24  
LINK        NA    NA A1747                 F1  ALF A1745     1555   1555  2.72  
LINK        NA    NA A1747                 O   GLY A  60     1555   1555  2.22  
LINK        NA    NA A1747                 O   GLY A  62     1555   1555  2.30  
LINK         C   MSE D   6                 N   GLU D   7     1555   1555  1.33  
LINK         C   GLY D 139                 N   MSE D 140     1555   1555  1.33  
LINK         C   MSE D 140                 N   THR D 141     1555   1555  1.34  
LINK         C   ASP D 158                 N   MSE D 159     1555   1555  1.33  
LINK         C   MSE D 159                 N   LEU D 160     1555   1555  1.33  
LINK         C   LEU D 160                 N   MSE D 161     1555   1555  1.33  
LINK         C   MSE D 161                 N   GLN D 162     1555   1555  1.33  
LINK         C   LEU D 209                 N   MSE D 210     1555   1555  1.33  
LINK         C   MSE D 210                 N   ASP D 211     1555   1555  1.32  
LINK         C   ARG D 271                 N   MSE D 272     1555   1555  1.33  
LINK         C   MSE D 272                 N   GLY D 273     1555   1555  1.32  
LINK         C   GLU D 727                 N   MSE D 728     1555   1555  1.34  
LINK         C   MSE D 728                 N   LEU D 729     1555   1555  1.33  
LINK         C   ARG D 730                 N   MSE D 731     1555   1555  1.33  
LINK         C   MSE D 731                 N   TYR D 732     1555   1555  1.33  
LINK         O3B GDP D1744                NA    NA D1747     1555   1555  2.93  
LINK         O1B GDP D1744                MG    MG D1746     1555   1555  1.98  
LINK        AL   ALF D1745                 O   HOH D2051     1555   1555  2.11  
LINK        AL   ALF D1745                NA    NA D1747     1555   1555  3.29  
LINK        AL   ALF D1745                MG    MG D1746     1555   1555  3.45  
LINK        AL   ALF D1745                 O3B GDP D1744     1555   1555  2.03  
LINK        MG    MG D1746                 OG1 THR D  65     1555   1555  2.10  
LINK        MG    MG D1746                 O   HOH D2115     1555   1555  2.04  
LINK        MG    MG D1746                 F4  ALF D1745     1555   1555  1.90  
LINK        MG    MG D1746                 OG  SER D  45     1555   1555  2.08  
LINK        MG    MG D1746                 O   HOH D2287     1555   1555  2.08  
LINK        NA    NA D1747                 OG  SER D  41     1555   1555  2.26  
LINK        NA    NA D1747                 O   GLY D  60     1555   1555  2.22  
LINK        NA    NA D1747                 F1  ALF D1745     1555   1555  2.65  
LINK        NA    NA D1747                 F3  ALF D1745     1555   1555  2.46  
LINK        NA    NA D1747                 O   GLY D  62     1555   1555  2.25  
SITE     1 AC1 27 SER A  41  ALA A  42  GLY A  43  LYS A  44                    
SITE     2 AC1 27 SER A  45  SER A  46  ARG A  59  GLY A  60                    
SITE     3 AC1 27 SER A  61  LYS A 206  ASP A 208  LEU A 209                    
SITE     4 AC1 27 VAL A 235  ASN A 236  ARG A 237  SER A 238                    
SITE     5 AC1 27 GLN A 239  ILE A 242  ALF A1745   MG A1746                    
SITE     6 AC1 27  NA A1747  HOH A2139  HOH A2203  HOH A2242                    
SITE     7 AC1 27 HOH A2331  HOH A2332  ASP D 211                               
SITE     1 AC2 13 GLN A  40  SER A  41  LYS A  44  GLY A  62                    
SITE     2 AC2 13 VAL A  64  THR A  65  GLY A 139  GDP A1744                    
SITE     3 AC2 13  MG A1746   NA A1747  HOH A2071  HOH A2139                    
SITE     4 AC2 13 HOH A2331                                                     
SITE     1 AC3  6 SER A  45  THR A  65  GDP A1744  ALF A1745                    
SITE     2 AC3  6 HOH A2139  HOH A2331                                          
SITE     1 AC4  5 SER A  41  GLY A  60  GLY A  62  GDP A1744                    
SITE     2 AC4  5 ALF A1745                                                     
SITE     1 AC5 24 ASP A 211  HOH A2213  SER D  41  ALA D  42                    
SITE     2 AC5 24 GLY D  43  LYS D  44  SER D  45  SER D  46                    
SITE     3 AC5 24 ARG D  59  GLY D  60  LYS D 206  ASP D 208                    
SITE     4 AC5 24 LEU D 209  ASN D 236  ARG D 237  SER D 238                    
SITE     5 AC5 24 GLN D 239  ILE D 242  ALF D1745   MG D1746                    
SITE     6 AC5 24  NA D1747  HOH D2115  HOH D2206  HOH D2287                    
SITE     1 AC6 13 GLN D  40  SER D  41  LYS D  44  GLY D  62                    
SITE     2 AC6 13 VAL D  64  THR D  65  GLY D 139  GDP D1744                    
SITE     3 AC6 13  MG D1746   NA D1747  HOH D2051  HOH D2115                    
SITE     4 AC6 13 HOH D2287                                                     
SITE     1 AC7  6 SER D  45  THR D  65  GDP D1744  ALF D1745                    
SITE     2 AC7  6 HOH D2115  HOH D2287                                          
SITE     1 AC8  5 SER D  41  GLY D  60  GLY D  62  GDP D1744                    
SITE     2 AC8  5 ALF D1745                                                     
CRYST1   43.610   81.020  181.540  90.00  90.00  90.00 P 21 21 21    8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022931  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.012343  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005508        0.00000                         
MTRIX1   1 -0.996005  0.084553 -0.028705      -21.94120    1                    
MTRIX2   1  0.085815  0.995246 -0.046049        4.96450    1                    
MTRIX3   1  0.024675 -0.048329 -0.998527      104.00200    1                    
HETATM    1  N   MSE A   6     -23.036  -7.593  16.976  1.00 61.24           N
HETATM    2  CA  MSE A   6     -24.496  -7.679  16.928  1.00 61.91           C
HETATM    3  C   MSE A   6     -24.943  -7.589  15.470  1.00 59.86           C
HETATM    4  O   MSE A   6     -25.656  -8.458  14.958  1.00 59.54           O
HETATM    5  CB  MSE A   6     -25.135  -6.547  17.745  1.00 64.34           C
HETATM    6  CG  MSE A   6     -24.780  -6.519  19.233  1.00 63.57           C
HETATM    7 SE   MSE A   6     -22.969  -5.936  19.609  1.00 66.04          Se
HETATM    8  CE  MSE A   6     -22.249  -7.644  20.176  1.00 65.66           C
ATOM      9  N   GLU A   7     -24.561  -6.497  14.823  1.00 57.71           N
ATOM     10  CA  GLU A   7     -24.860  -6.295  13.411  1.00 55.47           C
ATOM     11  C   GLU A   7     -23.452  -6.333  12.801  1.00 54.40           C
ATOM     12  O   GLU A   7     -23.185  -5.783  11.725  1.00 56.18           O
ATOM     13  CB  GLU A   7     -25.524  -4.926  13.179  1.00 53.72           C
ATOM     14  CG  GLU A   7     -26.935  -4.749  13.770  1.00 48.92           C
ATOM     15  CD  GLU A   7     -26.963  -4.487  15.284  1.00 61.67           C
ATOM     16  OE1 GLU A   7     -26.531  -3.396  15.746  1.00 50.10           O
ATOM     17  OE2 GLU A   7     -27.454  -5.374  16.017  1.00 75.17           O
ATOM     18  N   ASP A   8     -22.567  -7.041  13.501  1.00 49.60           N
ATOM     19  CA  ASP A   8     -21.168  -7.163  13.140  1.00 44.68           C
ATOM     20  C   ASP A   8     -20.482  -5.880  12.672  1.00 40.13           C
ATOM     21  O   ASP A   8     -19.888  -5.769  11.600  1.00 37.78           O
ATOM     22  CB  ASP A   8     -20.894  -8.380  12.275  1.00 45.43           C
ATOM     23  CG  ASP A   8     -20.569  -9.615  13.121  1.00 52.03           C
ATOM     24  OD1 ASP A   8     -19.498  -9.605  13.767  1.00 56.01           O
ATOM     25  OD2 ASP A   8     -21.382 -10.575  13.171  1.00 49.76           O
ATOM     26  N   LEU A   9     -20.631  -4.881  13.519  1.00 36.11           N
ATOM     27  CA  LEU A   9     -19.992  -3.605  13.312  1.00 33.44           C
ATOM     28  C   LEU A   9     -18.714  -3.796  14.126  1.00 30.13           C
ATOM     29  O   LEU A   9     -17.804  -2.980  14.074  1.00 28.65           O
ATOM     30  CB  LEU A   9     -20.841  -2.479  13.903  1.00 33.66           C
ATOM     31  CG  LEU A   9     -20.949  -2.366  15.423  1.00 34.08           C
ATOM     32  CD1 LEU A   9     -21.701  -1.095  15.770  1.00 35.00           C
ATOM     33  CD2 LEU A   9     -21.632  -3.588  16.020  1.00 35.05           C
ATOM     34  N   ILE A  10     -18.653  -4.919  14.842  1.00 27.41           N
ATOM     35  CA  ILE A  10     -17.525  -5.245  15.684  1.00 27.50           C
ATOM     36  C   ILE A  10     -16.169  -5.067  15.000  1.00 26.51           C
ATOM     37  O   ILE A  10     -15.301  -4.398  15.546  1.00 27.94           O
ATOM     38  CB  ILE A  10     -17.672  -6.654  16.295  1.00 29.75           C
ATOM     39  CG1 ILE A  10     -18.806  -6.658  17.334  1.00 36.73           C
ATOM     40  CG2 ILE A  10     -16.361  -7.125  16.916  1.00 31.08           C
ATOM     41  CD1 ILE A  10     -18.655  -5.656  18.473  1.00 42.78           C
ATOM     42  N   PRO A  11     -15.989  -5.606  13.780  1.00 25.84           N
ATOM     43  CA  PRO A  11     -14.695  -5.447  13.101  1.00 25.29           C
ATOM     44  C   PRO A  11     -14.366  -3.973  12.857  1.00 23.67           C
ATOM     45  O   PRO A  11     -13.211  -3.548  12.980  1.00 22.11           O
ATOM     46  CB  PRO A  11     -14.918  -6.175  11.772  1.00 25.95           C
ATOM     47  CG  PRO A  11     -16.001  -7.194  12.103  1.00 26.10           C
ATOM     48  CD  PRO A  11     -16.926  -6.377  12.939  1.00 26.05           C
ATOM     49  N   LEU A  12     -15.397  -3.205  12.508  1.00 22.46           N
ATOM     50  CA  LEU A  12     -15.254  -1.783  12.239  1.00 20.80           C
ATOM     51  C   LEU A  12     -14.928  -1.006  13.499  1.00 17.77           C
ATOM     52  O   LEU A  12     -14.108  -0.093  13.478  1.00 17.95           O
ATOM     53  CB  LEU A  12     -16.526  -1.222  11.596  1.00 21.59           C
ATOM     54  CG  LEU A  12     -16.734  -1.479  10.105  1.00 25.03           C
ATOM     55  CD1 LEU A  12     -15.545  -0.905   9.334  1.00 27.19           C
ATOM     56  CD2 LEU A  12     -16.883  -2.956   9.802  1.00 26.71           C
ATOM     57  N   VAL A  13     -15.560  -1.369  14.606  1.00 14.78           N
ATOM     58  CA  VAL A  13     -15.299  -0.672  15.856  1.00 13.75           C
ATOM     59  C   VAL A  13     -13.899  -1.058  16.361  1.00 12.17           C
ATOM     60  O   VAL A  13     -13.132  -0.212  16.864  1.00 11.17           O
ATOM     61  CB  VAL A  13     -16.402  -0.984  16.892  1.00 14.08           C
ATOM     62  CG1 VAL A  13     -16.051  -0.395  18.210  1.00 14.21           C
ATOM     63  CG2 VAL A  13     -17.734  -0.392  16.415  1.00 13.92           C
ATOM     64  N   ASN A  14     -13.526  -2.310  16.123  1.00 10.89           N
ATOM     65  CA  ASN A  14     -12.208  -2.788  16.542  1.00 10.92           C
ATOM     66  C   ASN A  14     -11.076  -2.080  15.793  1.00 12.76           C
ATOM     67  O   ASN A  14     -10.018  -1.786  16.366  1.00 12.11           O
ATOM     68  CB  ASN A  14     -12.096  -4.288  16.299  1.00 10.07           C
ATOM     69  CG  ASN A  14     -12.809  -5.109  17.346  1.00 12.08           C
ATOM     70  OD1 ASN A  14     -12.861  -6.340  17.239  1.00 19.95           O
ATOM     71  ND2 ASN A  14     -13.364  -4.456  18.356  1.00 10.37           N
ATOM     72  N   ARG A  15     -11.277  -1.874  14.492  1.00 14.56           N
ATOM     73  CA  ARG A  15     -10.277  -1.220  13.661  1.00 13.76           C
ATOM     74  C   ARG A  15     -10.172   0.237  14.085  1.00 12.91           C
ATOM     75  O   ARG A  15      -9.074   0.779  14.187  1.00 13.91           O
ATOM     76  CB  ARG A  15     -10.640  -1.358  12.176  1.00 15.80           C
ATOM     77  CG  ARG A  15      -9.709  -0.613  11.232  1.00 32.82           C
ATOM     78  CD  ARG A  15     -10.069  -0.851   9.765  1.00 42.83           C
ATOM     79  NE  ARG A  15     -10.031  -2.275   9.450  1.00 45.02           N
ATOM     80  CZ  ARG A  15     -11.101  -2.999   9.143  1.00 44.56           C
ATOM     81  NH1 ARG A  15     -12.300  -2.431   9.092  1.00 39.77           N
ATOM     82  NH2 ARG A  15     -10.982  -4.304   8.953  1.00 47.34           N
ATOM     83  N   LEU A  16     -11.309   0.845  14.406  1.00 12.25           N
ATOM     84  CA  LEU A  16     -11.323   2.237  14.864  1.00 11.67           C
ATOM     85  C   LEU A  16     -10.574   2.362  16.192  1.00 11.71           C
ATOM     86  O   LEU A  16      -9.717   3.235  16.362  1.00 11.69           O
ATOM     87  CB  LEU A  16     -12.760   2.723  15.054  1.00 11.70           C
ATOM     88  CG  LEU A  16     -12.881   4.130  15.635  1.00 10.18           C
ATOM     89  CD1 LEU A  16     -12.224   5.102  14.691  1.00  8.23           C
ATOM     90  CD2 LEU A  16     -14.342   4.494  15.852  1.00 12.87           C
ATOM     91  N   GLN A  17     -10.893   1.476  17.131  1.00 12.76           N
ATOM     92  CA  GLN A  17     -10.255   1.493  18.445  1.00 11.69           C
ATOM     93  C   GLN A  17      -8.746   1.341  18.308  1.00 10.84           C
ATOM     94  O   GLN A  17      -7.982   2.061  18.951  1.00 10.39           O
ATOM     95  CB  GLN A  17     -10.807   0.382  19.338  1.00 12.41           C
ATOM     96  CG  GLN A  17     -10.251   0.404  20.749  1.00  6.15           C
ATOM     97  CD  GLN A  17     -11.073  -0.478  21.669  1.00 13.32           C
ATOM     98  OE1 GLN A  17     -11.254  -1.676  21.406  1.00 13.14           O
ATOM     99  NE2 GLN A  17     -11.614   0.115  22.730  1.00 10.91           N
ATOM    100  N   ASP A  18      -8.331   0.424  17.438  1.00 10.84           N
ATOM    101  CA  ASP A  18      -6.913   0.205  17.195  1.00 10.92           C
ATOM    102  C   ASP A  18      -6.241   1.473  16.689  1.00 10.69           C
ATOM    103  O   ASP A  18      -5.137   1.807  17.127  1.00 13.18           O
ATOM    104  CB  ASP A  18      -6.715  -0.933  16.196  1.00 10.13           C
ATOM    105  CG  ASP A  18      -6.806  -2.322  16.854  1.00 13.09           C
ATOM    106  OD1 ASP A  18      -6.601  -3.315  16.139  1.00 17.94           O
ATOM    107  OD2 ASP A  18      -7.057  -2.428  18.078  1.00 15.63           O
ATOM    108  N   ALA A  19      -6.911   2.199  15.797  1.00  9.36           N
ATOM    109  CA  ALA A  19      -6.317   3.423  15.253  1.00  8.64           C
ATOM    110  C   ALA A  19      -6.023   4.460  16.342  1.00  8.99           C
ATOM    111  O   ALA A  19      -5.013   5.149  16.272  1.00  7.75           O
ATOM    112  CB  ALA A  19      -7.195   4.020  14.156  1.00  7.94           C
ATOM    113  N   PHE A  20      -6.918   4.594  17.316  1.00  8.45           N
ATOM    114  CA  PHE A  20      -6.716   5.541  18.401  1.00  8.10           C
ATOM    115  C   PHE A  20      -5.760   4.959  19.454  1.00  9.30           C
ATOM    116  O   PHE A  20      -4.879   5.667  19.960  1.00  9.42           O
ATOM    117  CB  PHE A  20      -8.059   5.946  19.024  1.00  7.75           C
ATOM    118  CG  PHE A  20      -8.824   6.951  18.192  1.00  7.50           C
ATOM    119  CD1 PHE A  20      -9.358   6.595  16.957  1.00  7.62           C
ATOM    120  CD2 PHE A  20      -8.978   8.262  18.632  1.00  6.97           C
ATOM    121  CE1 PHE A  20     -10.034   7.537  16.169  1.00  7.48           C
ATOM    122  CE2 PHE A  20      -9.653   9.215  17.864  1.00  6.53           C
ATOM    123  CZ  PHE A  20     -10.183   8.848  16.625  1.00  7.55           C
ATOM    124  N   SER A  21      -5.902   3.661  19.746  1.00 11.16           N
ATOM    125  CA  SER A  21      -5.044   3.007  20.727  1.00 10.15           C
ATOM    126  C   SER A  21      -3.575   3.098  20.338  1.00 10.99           C
ATOM    127  O   SER A  21      -2.733   3.333  21.195  1.00 12.13           O
ATOM    128  CB  SER A  21      -5.412   1.532  20.906  1.00  6.71           C
ATOM    129  OG  SER A  21      -6.686   1.399  21.496  1.00  9.75           O
ATOM    130  N   ALA A  22      -3.272   2.970  19.050  1.00  9.43           N
ATOM    131  CA  ALA A  22      -1.877   3.006  18.614  1.00  9.28           C
ATOM    132  C   ALA A  22      -1.158   4.294  19.005  1.00 10.13           C
ATOM    133  O   ALA A  22       0.046   4.294  19.222  1.00 12.60           O
ATOM    134  CB  ALA A  22      -1.764   2.753  17.098  1.00  8.90           C
ATOM    135  N   ILE A  23      -1.891   5.393  19.116  1.00 11.16           N
ATOM    136  CA  ILE A  23      -1.253   6.652  19.481  1.00 11.05           C
ATOM    137  C   ILE A  23      -1.763   7.215  20.809  1.00 12.39           C
ATOM    138  O   ILE A  23      -1.666   8.414  21.060  1.00 12.20           O
ATOM    139  CB  ILE A  23      -1.368   7.696  18.336  1.00  9.49           C
ATOM    140  CG1 ILE A  23      -2.835   8.106  18.146  1.00 10.02           C
ATOM    141  CG2 ILE A  23      -0.742   7.111  17.052  1.00  9.17           C
ATOM    142  CD1 ILE A  23      -3.083   9.072  17.002  1.00  7.82           C
ATOM    143  N   GLY A  24      -2.252   6.322  21.675  1.00 12.77           N
ATOM    144  CA  GLY A  24      -2.744   6.729  22.991  1.00 10.74           C
ATOM    145  C   GLY A  24      -3.808   7.822  23.029  1.00  9.57           C
ATOM    146  O   GLY A  24      -3.857   8.626  23.964  1.00  9.01           O
ATOM    147  N   GLN A  25      -4.695   7.812  22.047  1.00 10.12           N
ATOM    148  CA  GLN A  25      -5.755   8.803  21.973  1.00  8.82           C
ATOM    149  C   GLN A  25      -7.152   8.286  22.296  1.00  8.37           C
ATOM    150  O   GLN A  25      -8.157   8.872  21.865  1.00  9.34           O
ATOM    151  CB  GLN A  25      -5.756   9.447  20.596  1.00 13.26           C
ATOM    152  CG  GLN A  25      -5.010  10.755  20.589  1.00 18.16           C
ATOM    153  CD  GLN A  25      -5.089  11.454  19.272  1.00 15.63           C
ATOM    154  OE1 GLN A  25      -4.072  11.784  18.680  1.00 22.74           O
ATOM    155  NE2 GLN A  25      -6.298  11.706  18.807  1.00 16.18           N
ATOM    156  N   ASN A  26      -7.234   7.238  23.109  1.00  8.78           N
ATOM    157  CA  ASN A  26      -8.538   6.671  23.449  1.00 10.19           C
ATOM    158  C   ASN A  26      -9.458   7.599  24.228  1.00 12.04           C
ATOM    159  O   ASN A  26     -10.672   7.391  24.252  1.00 13.12           O
ATOM    160  CB  ASN A  26      -8.399   5.320  24.164  1.00  8.93           C
ATOM    161  CG  ASN A  26      -7.670   4.297  23.308  1.00 17.21           C
ATOM    162  OD1 ASN A  26      -8.285   3.518  22.558  1.00 16.64           O
ATOM    163  ND2 ASN A  26      -6.344   4.348  23.352  1.00 15.32           N
ATOM    164  N   ALA A  27      -8.902   8.642  24.830  1.00 13.56           N
ATOM    165  CA  ALA A  27      -9.733   9.590  25.569  1.00 15.05           C
ATOM    166  C   ALA A  27     -10.787  10.198  24.624  1.00 16.06           C
ATOM    167  O   ALA A  27     -11.858  10.621  25.071  1.00 17.44           O
ATOM    168  CB  ALA A  27      -8.865  10.714  26.185  1.00 14.73           C
ATOM    169  N   ASP A  28     -10.505  10.193  23.321  1.00 14.15           N
ATOM    170  CA  ASP A  28     -11.436  10.784  22.360  1.00 13.83           C
ATOM    171  C   ASP A  28     -12.643   9.926  21.995  1.00 13.37           C
ATOM    172  O   ASP A  28     -13.596  10.430  21.390  1.00 15.03           O
ATOM    173  CB  ASP A  28     -10.715  11.202  21.075  1.00 13.35           C
ATOM    174  CG  ASP A  28      -9.687  12.314  21.303  1.00 21.82           C
ATOM    175  OD1 ASP A  28      -8.750  12.413  20.480  1.00 23.74           O
ATOM    176  OD2 ASP A  28      -9.825  13.086  22.280  1.00 20.96           O
ATOM    177  N   LEU A  29     -12.616   8.648  22.346  1.00 10.77           N
ATOM    178  CA  LEU A  29     -13.730   7.773  21.997  1.00 12.07           C
ATOM    179  C   LEU A  29     -14.541   7.350  23.211  1.00 11.52           C
ATOM    180  O   LEU A  29     -14.125   7.543  24.362  1.00 11.99           O
ATOM    181  CB  LEU A  29     -13.202   6.486  21.325  1.00 12.98           C
ATOM    182  CG  LEU A  29     -12.272   6.658  20.129  1.00 11.94           C
ATOM    183  CD1 LEU A  29     -11.707   5.329  19.692  1.00 10.87           C
ATOM    184  CD2 LEU A  29     -13.064   7.352  19.002  1.00 13.26           C
ATOM    185  N   ASP A  30     -15.685   6.737  22.934  1.00 10.59           N
ATOM    186  CA  ASP A  30     -16.573   6.202  23.958  1.00 10.42           C
ATOM    187  C   ASP A  30     -17.244   5.027  23.257  1.00  9.50           C
ATOM    188  O   ASP A  30     -18.400   5.089  22.841  1.00  9.76           O
ATOM    189  CB  ASP A  30     -17.615   7.236  24.413  1.00 12.46           C
ATOM    190  CG  ASP A  30     -18.554   6.694  25.505  1.00 17.10           C
ATOM    191  OD1 ASP A  30     -18.285   5.596  26.060  1.00 17.66           O
ATOM    192  OD2 ASP A  30     -19.564   7.366  25.809  1.00 17.34           O
ATOM    193  N   LEU A  31     -16.482   3.962  23.108  1.00  9.02           N
ATOM    194  CA  LEU A  31     -16.941   2.762  22.440  1.00  8.40           C
ATOM    195  C   LEU A  31     -17.487   1.770  23.461  1.00  9.06           C
ATOM    196  O   LEU A  31     -17.102   1.775  24.637  1.00 10.15           O
ATOM    197  CB  LEU A  31     -15.781   2.154  21.651  1.00  8.16           C
ATOM    198  CG  LEU A  31     -15.107   3.082  20.632  1.00 10.03           C
ATOM    199  CD1 LEU A  31     -13.903   2.320  19.998  1.00 10.67           C
ATOM    200  CD2 LEU A  31     -16.086   3.476  19.523  1.00  9.62           C
ATOM    201  N   PRO A  32     -18.416   0.915  23.023  1.00 10.48           N
ATOM    202  CA  PRO A  32     -19.036  -0.083  23.889  1.00  9.66           C
ATOM    203  C   PRO A  32     -18.071  -1.187  24.283  1.00  9.26           C
ATOM    204  O   PRO A  32     -17.380  -1.751  23.441  1.00  9.98           O
ATOM    205  CB  PRO A  32     -20.196  -0.598  23.040  1.00  9.22           C
ATOM    206  CG  PRO A  32     -19.658  -0.491  21.637  1.00  9.71           C
ATOM    207  CD  PRO A  32     -18.939   0.840  21.644  1.00  9.85           C
ATOM    208  N   GLN A  33     -17.987  -1.441  25.578  1.00  7.36           N
ATOM    209  CA  GLN A  33     -17.118  -2.479  26.095  1.00  9.30           C
ATOM    210  C   GLN A  33     -17.489  -2.777  27.541  1.00 10.00           C
ATOM    211  O   GLN A  33     -18.350  -2.096  28.097  1.00 10.17           O
ATOM    212  CB  GLN A  33     -15.651  -2.069  25.966  1.00 12.60           C
ATOM    213  CG  GLN A  33     -15.302  -0.695  26.535  1.00  9.52           C
ATOM    214  CD  GLN A  33     -13.882  -0.281  26.163  1.00  7.35           C
ATOM    215  OE1 GLN A  33     -13.323   0.656  26.732  1.00 11.69           O
ATOM    216  NE2 GLN A  33     -13.286  -1.001  25.216  1.00  4.22           N
ATOM    217  N   ILE A  34     -16.904  -3.838  28.106  1.00  8.40           N
ATOM    218  CA  ILE A  34     -17.196  -4.246  29.470  1.00  8.14           C
ATOM    219  C   ILE A  34     -15.905  -4.215  30.280  1.00  8.46           C
ATOM    220  O   ILE A  34     -14.952  -4.938  29.972  1.00  8.79           O
ATOM    221  CB  ILE A  34     -17.746  -5.688  29.508  1.00  8.41           C
ATOM    222  CG1 ILE A  34     -19.020  -5.793  28.651  1.00  9.44           C
ATOM    223  CG2 ILE A  34     -18.073  -6.082  30.969  1.00  8.18           C
ATOM    224  CD1 ILE A  34     -19.488  -7.234  28.424  1.00 10.39           C
ATOM    225  N   ALA A  35     -15.892  -3.418  31.337  1.00  7.99           N
ATOM    226  CA  ALA A  35     -14.706  -3.289  32.178  1.00  8.19           C
ATOM    227  C   ALA A  35     -14.934  -3.942  33.543  1.00  9.39           C
ATOM    228  O   ALA A  35     -15.998  -3.811  34.138  1.00  9.55           O
ATOM    229  CB  ALA A  35     -14.355  -1.805  32.350  1.00  8.00           C
ATOM    230  N   VAL A  36     -13.934  -4.659  34.033  1.00 10.11           N
ATOM    231  CA  VAL A  36     -14.065  -5.306  35.323  1.00 10.70           C
ATOM    232  C   VAL A  36     -13.476  -4.459  36.468  1.00  9.84           C
ATOM    233  O   VAL A  36     -12.361  -3.920  36.369  1.00 10.26           O
ATOM    234  CB  VAL A  36     -13.416  -6.713  35.282  1.00 12.53           C
ATOM    235  CG1 VAL A  36     -11.907  -6.611  34.999  1.00 12.29           C
ATOM    236  CG2 VAL A  36     -13.700  -7.440  36.579  1.00 12.58           C
ATOM    237  N   VAL A  37     -14.244  -4.288  37.535  1.00  7.79           N
ATOM    238  CA  VAL A  37     -13.764  -3.519  38.684  1.00  6.25           C
ATOM    239  C   VAL A  37     -13.929  -4.358  39.929  1.00  6.09           C
ATOM    240  O   VAL A  37     -14.851  -5.159  40.024  1.00  3.31           O
ATOM    241  CB  VAL A  37     -14.548  -2.208  38.874  1.00  5.79           C
ATOM    242  CG1 VAL A  37     -14.393  -1.332  37.639  1.00  6.43           C
ATOM    243  CG2 VAL A  37     -16.023  -2.509  39.106  1.00  5.80           C
ATOM    244  N   GLY A  38     -13.003  -4.207  40.872  1.00  7.40           N
ATOM    245  CA  GLY A  38     -13.097  -4.957  42.114  1.00  5.78           C
ATOM    246  C   GLY A  38     -11.781  -4.904  42.856  1.00  4.55           C
ATOM    247  O   GLY A  38     -10.786  -4.363  42.335  1.00  4.01           O
ATOM    248  N   GLY A  39     -11.795  -5.353  44.102  1.00  5.29           N
ATOM    249  CA  GLY A  39     -10.574  -5.345  44.878  1.00  3.28           C
ATOM    250  C   GLY A  39      -9.547  -6.323  44.339  1.00  3.95           C
ATOM    251  O   GLY A  39      -9.834  -7.211  43.509  1.00  3.44           O
ATOM    252  N   GLN A  40      -8.330  -6.176  44.845  1.00  3.76           N
ATOM    253  CA  GLN A  40      -7.247  -7.014  44.436  1.00  3.38           C
ATOM    254  C   GLN A  40      -7.556  -8.482  44.676  1.00  3.89           C
ATOM    255  O   GLN A  40      -8.074  -8.859  45.722  1.00  4.81           O
ATOM    256  CB  GLN A  40      -5.953  -6.641  45.179  1.00  3.12           C
ATOM    257  CG  GLN A  40      -4.759  -7.469  44.699  1.00  2.72           C
ATOM    258  CD  GLN A  40      -3.429  -6.887  45.151  1.00  6.44           C
ATOM    259  OE1 GLN A  40      -3.045  -5.794  44.731  1.00  2.06           O
ATOM    260  NE2 GLN A  40      -2.727  -7.613  46.030  1.00 11.43           N
ATOM    261  N   SER A  41      -7.220  -9.286  43.669  1.00  4.96           N
ATOM    262  CA  SER A  41      -7.388 -10.736  43.723  1.00  6.33           C
ATOM    263  C   SER A  41      -8.820 -11.235  43.946  1.00  7.45           C
ATOM    264  O   SER A  41      -9.021 -12.338  44.470  1.00  8.18           O
ATOM    265  CB  SER A  41      -6.399 -11.351  44.741  1.00  4.49           C
ATOM    266  OG  SER A  41      -5.049 -11.250  44.249  1.00  4.68           O
ATOM    267  N   ALA A  42      -9.808 -10.447  43.499  1.00  7.57           N
ATOM    268  CA  ALA A  42     -11.207 -10.860  43.625  1.00  7.48           C
ATOM    269  C   ALA A  42     -11.563 -11.975  42.623  1.00  8.41           C
ATOM    270  O   ALA A  42     -12.608 -12.609  42.763  1.00  8.75           O
ATOM    271  CB  ALA A  42     -12.146  -9.652  43.399  1.00  7.14           C
ATOM    272  N   GLY A  43     -10.723 -12.163  41.599  1.00  8.16           N
ATOM    273  CA  GLY A  43     -10.957 -13.167  40.558  1.00  7.33           C
ATOM    274  C   GLY A  43     -11.428 -12.562  39.225  1.00  7.51           C
ATOM    275  O   GLY A  43     -12.072 -13.223  38.411  1.00  7.85           O
ATOM    276  N   LYS A  44     -11.129 -11.284  39.015  1.00  6.56           N
ATOM    277  CA  LYS A  44     -11.516 -10.565  37.799  1.00  4.53           C
ATOM    278  C   LYS A  44     -10.928 -11.175  36.505  1.00  3.90           C
ATOM    279  O   LYS A  44     -11.655 -11.493  35.552  1.00  5.80           O
ATOM    280  CB  LYS A  44     -11.102  -9.082  37.958  1.00  4.24           C
ATOM    281  CG  LYS A  44     -11.676  -8.438  39.249  1.00  2.12           C
ATOM    282  CD  LYS A  44     -11.347  -6.938  39.373  1.00  1.00           C
ATOM    283  CE  LYS A  44      -9.816  -6.717  39.477  1.00  2.86           C
ATOM    284  NZ  LYS A  44      -9.293  -7.508  40.624  1.00  2.70           N
ATOM    285  N   SER A  45      -9.613 -11.357  36.471  1.00  2.36           N
ATOM    286  CA  SER A  45      -8.968 -11.935  35.301  1.00  4.41           C
ATOM    287  C   SER A  45      -9.548 -13.350  35.069  1.00  5.95           C
ATOM    288  O   SER A  45      -9.835 -13.719  33.946  1.00  8.55           O
ATOM    289  CB  SER A  45      -7.437 -11.976  35.483  1.00  3.35           C
ATOM    290  OG  SER A  45      -6.890 -10.654  35.625  1.00  3.08           O
ATOM    291  N   SER A  46      -9.736 -14.124  36.129  1.00  5.17           N
ATOM    292  CA  SER A  46     -10.314 -15.469  35.974  1.00  4.69           C
ATOM    293  C   SER A  46     -11.687 -15.395  35.272  1.00  5.52           C
ATOM    294  O   SER A  46     -11.995 -16.194  34.373  1.00  6.43           O
ATOM    295  CB  SER A  46     -10.450 -16.149  37.338  1.00  3.66           C
ATOM    296  OG  SER A  46      -9.160 -16.392  37.874  1.00  2.41           O
ATOM    297  N   VAL A  47     -12.496 -14.426  35.655  1.00  5.78           N
ATOM    298  CA  VAL A  47     -13.812 -14.248  35.012  1.00  6.81           C
ATOM    299  C   VAL A  47     -13.691 -13.911  33.505  1.00  8.65           C
ATOM    300  O   VAL A  47     -14.355 -14.540  32.638  1.00  8.11           O
ATOM    301  CB  VAL A  47     -14.625 -13.144  35.759  1.00  6.02           C
ATOM    302  CG1 VAL A  47     -15.847 -12.700  34.914  1.00  5.71           C
ATOM    303  CG2 VAL A  47     -15.101 -13.724  37.096  1.00  5.81           C
ATOM    304  N   LEU A  48     -12.813 -12.968  33.177  1.00  8.90           N
ATOM    305  CA  LEU A  48     -12.640 -12.575  31.779  1.00  8.11           C
ATOM    306  C   LEU A  48     -12.089 -13.711  30.930  1.00  8.38           C
ATOM    307  O   LEU A  48     -12.584 -13.987  29.827  1.00  9.76           O
ATOM    308  CB  LEU A  48     -11.755 -11.332  31.651  1.00  8.63           C
ATOM    309  CG  LEU A  48     -12.364 -10.096  32.323  1.00  9.41           C
ATOM    310  CD1 LEU A  48     -11.532  -8.833  31.986  1.00  9.64           C
ATOM    311  CD2 LEU A  48     -13.786  -9.939  31.829  1.00  8.48           C
ATOM    312  N   GLU A  49     -11.075 -14.385  31.459  1.00  6.34           N
ATOM    313  CA  GLU A  49     -10.452 -15.492  30.750  1.00  5.45           C
ATOM    314  C   GLU A  49     -11.467 -16.547  30.329  1.00  6.32           C
ATOM    315  O   GLU A  49     -11.364 -17.110  29.239  1.00  7.59           O
ATOM    316  CB  GLU A  49      -9.383 -16.129  31.623  1.00  3.40           C
ATOM    317  CG  GLU A  49      -8.653 -17.276  30.969  1.00  6.78           C
ATOM    318  CD  GLU A  49      -7.565 -17.820  31.870  1.00  6.58           C
ATOM    319  OE1 GLU A  49      -7.878 -18.438  32.911  1.00 13.67           O
ATOM    320  OE2 GLU A  49      -6.396 -17.591  31.555  1.00  7.22           O
ATOM    321  N   ASN A  50     -12.463 -16.797  31.170  1.00  5.77           N
ATOM    322  CA  ASN A  50     -13.466 -17.793  30.827  1.00  5.50           C
ATOM    323  C   ASN A  50     -14.217 -17.470  29.528  1.00  9.07           C
ATOM    324  O   ASN A  50     -14.796 -18.381  28.905  1.00 11.61           O
ATOM    325  CB  ASN A  50     -14.460 -17.986  31.974  1.00  6.10           C
ATOM    326  CG  ASN A  50     -13.842 -18.739  33.174  1.00 13.44           C
ATOM    327  OD1 ASN A  50     -12.834 -19.434  33.044  1.00 19.35           O
ATOM    328  ND2 ASN A  50     -14.427 -18.567  34.335  1.00 14.12           N
ATOM    329  N   PHE A  51     -14.250 -16.195  29.119  1.00  7.08           N
ATOM    330  CA  PHE A  51     -14.954 -15.846  27.869  1.00  7.18           C
ATOM    331  C   PHE A  51     -14.326 -16.527  26.662  1.00  8.35           C
ATOM    332  O   PHE A  51     -15.004 -16.777  25.660  1.00  9.16           O
ATOM    333  CB  PHE A  51     -14.946 -14.345  27.608  1.00  7.13           C
ATOM    334  CG  PHE A  51     -16.025 -13.612  28.318  1.00  7.39           C
ATOM    335  CD1 PHE A  51     -17.183 -13.217  27.635  1.00  7.03           C
ATOM    336  CD2 PHE A  51     -15.885 -13.280  29.661  1.00  7.02           C
ATOM    337  CE1 PHE A  51     -18.195 -12.486  28.299  1.00  6.67           C
ATOM    338  CE2 PHE A  51     -16.886 -12.557  30.325  1.00  6.70           C
ATOM    339  CZ  PHE A  51     -18.042 -12.163  29.635  1.00  6.57           C
ATOM    340  N   VAL A  52     -13.030 -16.791  26.769  1.00  8.05           N
ATOM    341  CA  VAL A  52     -12.254 -17.422  25.718  1.00  9.02           C
ATOM    342  C   VAL A  52     -12.173 -18.939  25.912  1.00 11.91           C
ATOM    343  O   VAL A  52     -12.103 -19.697  24.947  1.00 15.73           O
ATOM    344  CB  VAL A  52     -10.834 -16.807  25.677  1.00  8.88           C
ATOM    345  CG1 VAL A  52      -9.957 -17.552  24.707  1.00  8.53           C
ATOM    346  CG2 VAL A  52     -10.933 -15.337  25.246  1.00  9.20           C
ATOM    347  N   GLY A  53     -12.150 -19.389  27.159  1.00 10.10           N
ATOM    348  CA  GLY A  53     -12.100 -20.828  27.394  1.00  9.33           C
ATOM    349  C   GLY A  53     -10.734 -21.484  27.244  1.00 10.04           C
ATOM    350  O   GLY A  53     -10.633 -22.712  27.185  1.00 10.43           O
ATOM    351  N   ARG A  54      -9.692 -20.674  27.140  1.00 10.57           N
ATOM    352  CA  ARG A  54      -8.312 -21.156  27.035  1.00 11.42           C
ATOM    353  C   ARG A  54      -7.545 -20.334  28.073  1.00 11.52           C
ATOM    354  O   ARG A  54      -7.921 -19.203  28.363  1.00 11.59           O
ATOM    355  CB  ARG A  54      -7.718 -20.832  25.649  1.00 17.59           C
ATOM    356  CG  ARG A  54      -8.515 -21.327  24.445  1.00 22.64           C
ATOM    357  CD  ARG A  54      -8.010 -22.664  23.944  1.00 27.93           C
ATOM    358  NE  ARG A  54      -6.647 -22.544  23.429  1.00 43.57           N
ATOM    359  CZ  ARG A  54      -6.209 -23.113  22.308  1.00 54.28           C
ATOM    360  NH1 ARG A  54      -7.029 -23.851  21.563  1.00 61.86           N
ATOM    361  NH2 ARG A  54      -4.942 -22.957  21.939  1.00 52.62           N
ATOM    362  N   ASP A  55      -6.472 -20.882  28.628  1.00 12.45           N
ATOM    363  CA  ASP A  55      -5.692 -20.148  29.613  1.00 12.91           C
ATOM    364  C   ASP A  55      -4.783 -19.206  28.845  1.00 13.67           C
ATOM    365  O   ASP A  55      -4.074 -19.631  27.914  1.00 17.21           O
ATOM    366  CB  ASP A  55      -4.858 -21.098  30.482  1.00 13.50           C
ATOM    367  CG  ASP A  55      -5.728 -22.086  31.289  1.00 15.27           C
ATOM    368  OD1 ASP A  55      -6.953 -21.926  31.347  1.00 17.28           O
ATOM    369  OD2 ASP A  55      -5.179 -23.033  31.861  1.00 18.06           O
ATOM    370  N   PHE A  56      -4.874 -17.918  29.159  1.00 10.79           N
ATOM    371  CA  PHE A  56      -4.051 -16.930  28.475  1.00  8.31           C
ATOM    372  C   PHE A  56      -3.827 -15.655  29.274  1.00  7.78           C
ATOM    373  O   PHE A  56      -3.000 -14.830  28.894  1.00  6.53           O
ATOM    374  CB  PHE A  56      -4.664 -16.561  27.128  1.00  7.43           C
ATOM    375  CG  PHE A  56      -5.888 -15.682  27.231  1.00  6.37           C
ATOM    376  CD1 PHE A  56      -5.829 -14.349  26.848  1.00  6.60           C
ATOM    377  CD2 PHE A  56      -7.108 -16.211  27.645  1.00  6.34           C
ATOM    378  CE1 PHE A  56      -6.980 -13.535  26.859  1.00  8.30           C
ATOM    379  CE2 PHE A  56      -8.280 -15.409  27.668  1.00  7.15           C
ATOM    380  CZ  PHE A  56      -8.212 -14.057  27.266  1.00  7.73           C
ATOM    381  N   LEU A  57      -4.576 -15.474  30.354  1.00  8.26           N
ATOM    382  CA  LEU A  57      -4.403 -14.275  31.173  1.00  8.32           C
ATOM    383  C   LEU A  57      -3.639 -14.566  32.461  1.00  7.97           C
ATOM    384  O   LEU A  57      -3.994 -15.485  33.171  1.00  9.24           O
ATOM    385  CB  LEU A  57      -5.762 -13.685  31.556  1.00  8.03           C
ATOM    386  CG  LEU A  57      -6.640 -13.097  30.465  1.00  6.36           C
ATOM    387  CD1 LEU A  57      -7.950 -12.531  31.089  1.00  5.47           C
ATOM    388  CD2 LEU A  57      -5.833 -11.981  29.840  1.00  6.11           C
ATOM    389  N   PRO A  58      -2.603 -13.768  32.797  1.00  8.34           N
ATOM    390  CA  PRO A  58      -1.866 -14.018  34.045  1.00  8.66           C
ATOM    391  C   PRO A  58      -2.861 -13.896  35.200  1.00  8.70           C
ATOM    392  O   PRO A  58      -3.664 -12.952  35.227  1.00  9.71           O
ATOM    393  CB  PRO A  58      -0.847 -12.861  34.082  1.00  8.90           C
ATOM    394  CG  PRO A  58      -0.542 -12.642  32.601  1.00  6.83           C
ATOM    395  CD  PRO A  58      -1.957 -12.707  32.002  1.00  7.80           C
ATOM    396  N   ARG A  59      -2.849 -14.879  36.108  1.00  8.09           N
ATOM    397  CA  ARG A  59      -3.749 -14.921  37.267  1.00  6.96           C
ATOM    398  C   ARG A  59      -2.979 -15.358  38.514  1.00 10.85           C
ATOM    399  O   ARG A  59      -1.916 -15.991  38.398  1.00 12.00           O
ATOM    400  CB  ARG A  59      -4.893 -15.924  37.027  1.00  7.93           C
ATOM    401  CG  ARG A  59      -5.391 -15.953  35.576  1.00 16.06           C
ATOM    402  CD  ARG A  59      -6.815 -16.433  35.345  1.00 11.63           C
ATOM    403  NE  ARG A  59      -7.223 -17.638  36.064  1.00 23.55           N
ATOM    404  CZ  ARG A  59      -6.734 -18.858  35.891  1.00 21.39           C
ATOM    405  NH1 ARG A  59      -5.767 -19.100  35.011  1.00 26.42           N
ATOM    406  NH2 ARG A  59      -7.264 -19.856  36.578  1.00 20.07           N
ATOM    407  N   GLY A  60      -3.543 -15.054  39.690  1.00 10.22           N
ATOM    408  CA  GLY A  60      -2.928 -15.409  40.962  1.00  9.09           C
ATOM    409  C   GLY A  60      -3.124 -14.410  42.105  1.00  7.61           C
ATOM    410  O   GLY A  60      -3.545 -13.243  41.889  1.00  7.49           O
ATOM    411  N   SER A  61      -2.854 -14.871  43.327  1.00  6.77           N
ATOM    412  CA  SER A  61      -2.946 -14.052  44.534  1.00  8.73           C
ATOM    413  C   SER A  61      -1.822 -13.025  44.445  1.00 10.56           C
ATOM    414  O   SER A  61      -0.864 -13.225  43.688  1.00 12.40           O
ATOM    415  CB  SER A  61      -2.773 -14.922  45.786  1.00 13.52           C
ATOM    416  OG  SER A  61      -3.830 -15.864  45.858  1.00 24.58           O
ATOM    417  N   GLY A  62      -1.893 -11.978  45.260  1.00 10.83           N
ATOM    418  CA  GLY A  62      -0.897 -10.913  45.187  1.00 10.47           C
ATOM    419  C   GLY A  62      -1.291 -10.044  43.992  1.00 10.14           C
ATOM    420  O   GLY A  62      -2.355 -10.275  43.371  1.00 10.62           O
ATOM    421  N   ILE A  63      -0.508  -9.015  43.678  1.00  8.35           N
ATOM    422  CA  ILE A  63      -0.865  -8.195  42.529  1.00  8.62           C
ATOM    423  C   ILE A  63      -0.308  -8.851  41.239  1.00  9.17           C
ATOM    424  O   ILE A  63       0.877  -9.109  41.127  1.00 11.64           O
ATOM    425  CB  ILE A  63      -0.380  -6.735  42.692  1.00  8.48           C
ATOM    426  CG1 ILE A  63      -0.840  -5.889  41.498  1.00  7.51           C
ATOM    427  CG2 ILE A  63       1.146  -6.685  42.884  1.00  8.48           C
ATOM    428  CD1 ILE A  63      -0.744  -4.410  41.743  1.00  6.72           C
ATOM    429  N   VAL A  64      -1.191  -9.200  40.309  1.00  5.26           N
ATOM    430  CA  VAL A  64      -0.764  -9.840  39.070  1.00  3.69           C
ATOM    431  C   VAL A  64      -1.093  -8.922  37.886  1.00  4.13           C
ATOM    432  O   VAL A  64      -0.217  -8.541  37.148  1.00  5.53           O
ATOM    433  CB  VAL A  64      -1.417 -11.221  38.913  1.00  4.23           C
ATOM    434  CG1 VAL A  64      -1.036 -11.810  37.550  1.00  4.48           C
ATOM    435  CG2 VAL A  64      -0.944 -12.152  40.058  1.00  4.53           C
ATOM    436  N   THR A  65      -2.364  -8.585  37.685  1.00  4.19           N
ATOM    437  CA  THR A  65      -2.686  -7.654  36.609  1.00  1.68           C
ATOM    438  C   THR A  65      -2.200  -6.274  37.066  1.00  3.03           C
ATOM    439  O   THR A  65      -2.603  -5.811  38.130  1.00  6.12           O
ATOM    440  CB  THR A  65      -4.193  -7.595  36.352  1.00  1.00           C
ATOM    441  OG1 THR A  65      -4.675  -8.925  36.135  1.00  3.24           O
ATOM    442  CG2 THR A  65      -4.458  -6.747  35.093  1.00  2.80           C
ATOM    443  N   ARG A  66      -1.382  -5.613  36.253  1.00  2.27           N
ATOM    444  CA  ARG A  66      -0.810  -4.322  36.632  1.00  3.40           C
ATOM    445  C   ARG A  66      -0.932  -3.232  35.580  1.00  5.76           C
ATOM    446  O   ARG A  66      -0.437  -2.121  35.779  1.00  5.80           O
ATOM    447  CB  ARG A  66       0.668  -4.508  37.026  1.00  4.58           C
ATOM    448  CG  ARG A  66       0.817  -5.405  38.240  1.00 11.90           C
ATOM    449  CD  ARG A  66       2.228  -5.457  38.730  1.00 20.24           C
ATOM    450  NE  ARG A  66       3.090  -6.134  37.786  1.00 23.78           N
ATOM    451  CZ  ARG A  66       4.348  -5.781  37.537  1.00 27.62           C
ATOM    452  NH1 ARG A  66       4.914  -4.735  38.164  1.00 17.57           N
ATOM    453  NH2 ARG A  66       5.039  -6.480  36.649  1.00 15.62           N
ATOM    454  N   ARG A  67      -1.540  -3.582  34.446  1.00  5.82           N
ATOM    455  CA  ARG A  67      -1.798  -2.648  33.359  1.00  6.12           C
ATOM    456  C   ARG A  67      -3.164  -3.064  32.815  1.00  6.91           C
ATOM    457  O   ARG A  67      -3.572  -4.211  32.974  1.00  6.93           O
ATOM    458  CB  ARG A  67      -0.771  -2.811  32.225  1.00  5.68           C
ATOM    459  CG  ARG A  67       0.635  -2.322  32.529  1.00 10.23           C
ATOM    460  CD  ARG A  67       1.570  -2.610  31.321  1.00  7.84           C
ATOM    461  NE  ARG A  67       1.169  -1.827  30.158  1.00  4.77           N
ATOM    462  CZ  ARG A  67       1.733  -1.912  28.954  1.00 11.95           C
ATOM    463  NH1 ARG A  67       2.751  -2.749  28.744  1.00 11.02           N
ATOM    464  NH2 ARG A  67       1.228  -1.212  27.936  1.00 12.71           N
ATOM    465  N   PRO A  68      -3.918  -2.114  32.244  1.00  6.90           N
ATOM    466  CA  PRO A  68      -5.230  -2.430  31.677  1.00  4.88           C
ATOM    467  C   PRO A  68      -4.999  -3.332  30.476  1.00  4.75           C
ATOM    468  O   PRO A  68      -3.969  -3.207  29.802  1.00  5.58           O
ATOM    469  CB  PRO A  68      -5.715  -1.069  31.155  1.00  5.42           C
ATOM    470  CG  PRO A  68      -5.052  -0.074  32.048  1.00  6.30           C
ATOM    471  CD  PRO A  68      -3.641  -0.666  32.173  1.00  6.52           C
ATOM    472  N   LEU A  69      -5.908  -4.271  30.235  1.00  5.70           N
ATOM    473  CA  LEU A  69      -5.822  -5.108  29.037  1.00  6.22           C
ATOM    474  C   LEU A  69      -7.118  -4.895  28.239  1.00  6.77           C
ATOM    475  O   LEU A  69      -8.210  -5.201  28.756  1.00  6.52           O
ATOM    476  CB  LEU A  69      -5.711  -6.595  29.377  1.00  6.22           C
ATOM    477  CG  LEU A  69      -5.664  -7.476  28.110  1.00  7.46           C
ATOM    478  CD1 LEU A  69      -4.256  -7.449  27.539  1.00  7.90           C
ATOM    479  CD2 LEU A  69      -6.054  -8.907  28.427  1.00  7.26           C
ATOM    480  N   VAL A  70      -7.022  -4.276  27.054  1.00  7.11           N
ATOM    481  CA  VAL A  70      -8.215  -4.063  26.222  1.00  7.55           C
ATOM    482  C   VAL A  70      -8.265  -5.289  25.295  1.00  7.33           C
ATOM    483  O   VAL A  70      -7.428  -5.458  24.392  1.00  8.58           O
ATOM    484  CB  VAL A  70      -8.195  -2.715  25.430  1.00  8.01           C
ATOM    485  CG1 VAL A  70      -9.501  -2.552  24.628  1.00  7.79           C
ATOM    486  CG2 VAL A  70      -8.092  -1.517  26.410  1.00  7.85           C
ATOM    487  N   LEU A  71      -9.203  -6.172  25.595  1.00  5.40           N
ATOM    488  CA  LEU A  71      -9.346  -7.440  24.894  1.00  6.10           C
ATOM    489  C   LEU A  71     -10.524  -7.505  23.936  1.00  5.47           C
ATOM    490  O   LEU A  71     -11.678  -7.591  24.351  1.00  6.21           O
ATOM    491  CB  LEU A  71      -9.437  -8.560  25.940  1.00  6.01           C
ATOM    492  CG  LEU A  71      -9.708 -10.013  25.552  1.00  6.74           C
ATOM    493  CD1 LEU A  71      -8.627 -10.576  24.649  1.00  5.01           C
ATOM    494  CD2 LEU A  71      -9.820 -10.830  26.825  1.00  7.87           C
ATOM    495  N   GLN A  72     -10.223  -7.506  22.654  1.00  5.72           N
ATOM    496  CA  GLN A  72     -11.268  -7.568  21.652  1.00  7.19           C
ATOM    497  C   GLN A  72     -11.527  -9.026  21.268  1.00  7.79           C
ATOM    498  O   GLN A  72     -10.645  -9.695  20.725  1.00  5.52           O
ATOM    499  CB  GLN A  72     -10.853  -6.769  20.398  1.00 10.70           C
ATOM    500  CG  GLN A  72     -10.587  -5.274  20.649  1.00  6.36           C
ATOM    501  CD  GLN A  72      -9.837  -4.622  19.503  1.00 12.43           C
ATOM    502  OE1 GLN A  72      -9.294  -5.313  18.636  1.00  9.99           O
ATOM    503  NE2 GLN A  72      -9.790  -3.289  19.494  1.00 14.54           N
ATOM    504  N   LEU A  73     -12.719  -9.524  21.568  1.00  8.32           N
ATOM    505  CA  LEU A  73     -13.051 -10.892  21.198  1.00  9.20           C
ATOM    506  C   LEU A  73     -13.848 -10.871  19.895  1.00  9.78           C
ATOM    507  O   LEU A  73     -14.835 -10.133  19.775  1.00  8.56           O
ATOM    508  CB  LEU A  73     -13.868 -11.579  22.297  1.00  9.63           C
ATOM    509  CG  LEU A  73     -13.213 -11.593  23.689  1.00  9.28           C
ATOM    510  CD1 LEU A  73     -14.059 -12.476  24.655  1.00  9.26           C
ATOM    511  CD2 LEU A  73     -11.805 -12.161  23.551  1.00  7.50           C
ATOM    512  N   VAL A  74     -13.389 -11.647  18.914  1.00  9.79           N
ATOM    513  CA  VAL A  74     -14.064 -11.736  17.625  1.00 10.66           C
ATOM    514  C   VAL A  74     -14.375 -13.193  17.272  1.00  9.50           C
ATOM    515  O   VAL A  74     -13.484 -14.044  17.242  1.00 10.64           O
ATOM    516  CB  VAL A  74     -13.185 -11.157  16.484  1.00 11.84           C
ATOM    517  CG1 VAL A  74     -13.902 -11.313  15.124  1.00 12.18           C
ATOM    518  CG2 VAL A  74     -12.847  -9.682  16.757  1.00 11.76           C
ATOM    519  N   ASN A  75     -15.624 -13.485  16.955  1.00  7.06           N
ATOM    520  CA  ASN A  75     -15.943 -14.856  16.572  1.00 10.55           C
ATOM    521  C   ASN A  75     -15.392 -15.112  15.142  1.00 14.76           C
ATOM    522  O   ASN A  75     -15.666 -14.347  14.206  1.00 16.37           O
ATOM    523  CB  ASN A  75     -17.451 -15.075  16.586  1.00 11.78           C
ATOM    524  CG  ASN A  75     -17.814 -16.528  16.377  1.00 10.84           C
ATOM    525  OD1 ASN A  75     -17.958 -17.280  17.333  1.00 13.69           O
ATOM    526  ND2 ASN A  75     -17.922 -16.936  15.124  1.00 14.04           N
ATOM    527  N   ALA A  76     -14.622 -16.176  14.970  1.00 14.01           N
ATOM    528  CA  ALA A  76     -14.045 -16.497  13.667  1.00 14.54           C
ATOM    529  C   ALA A  76     -13.923 -18.009  13.511  1.00 15.55           C
ATOM    530  O   ALA A  76     -14.052 -18.746  14.491  1.00 18.22           O
ATOM    531  CB  ALA A  76     -12.668 -15.830  13.506  1.00 14.17           C
ATOM    532  N   THR A  77     -13.657 -18.469  12.293  1.00 13.62           N
ATOM    533  CA  THR A  77     -13.544 -19.907  12.039  1.00 13.59           C
ATOM    534  C   THR A  77     -12.323 -20.526  12.689  1.00 17.56           C
ATOM    535  O   THR A  77     -12.343 -21.699  13.080  1.00 19.00           O
ATOM    536  CB  THR A  77     -13.550 -20.212  10.519  1.00 11.51           C
ATOM    537  OG1 THR A  77     -14.789 -19.759   9.967  1.00 15.45           O
ATOM    538  CG2 THR A  77     -13.426 -21.681  10.272  1.00 15.09           C
ATOM    539  N   THR A  78     -11.243 -19.765  12.782  1.00 17.93           N
ATOM    540  CA  THR A  78     -10.050 -20.301  13.422  1.00 20.72           C
ATOM    541  C   THR A  78      -9.669 -19.485  14.669  1.00 17.32           C
ATOM    542  O   THR A  78     -10.160 -18.378  14.856  1.00 19.92           O
ATOM    543  CB  THR A  78      -8.890 -20.386  12.447  1.00 24.33           C
ATOM    544  OG1 THR A  78      -7.828 -21.157  13.040  1.00 27.52           O
ATOM    545  CG2 THR A  78      -8.421 -18.984  12.064  1.00 21.65           C
ATOM    546  N   GLU A  79      -8.828 -20.052  15.523  1.00 13.53           N
ATOM    547  CA  GLU A  79      -8.419 -19.426  16.769  1.00 12.63           C
ATOM    548  C   GLU A  79      -6.955 -18.966  16.765  1.00 12.11           C
ATOM    549  O   GLU A  79      -6.041 -19.711  16.420  1.00 11.27           O
ATOM    550  CB  GLU A  79      -8.672 -20.427  17.911  1.00 13.07           C
ATOM    551  CG  GLU A  79      -8.654 -19.891  19.331  1.00 20.47           C
ATOM    552  CD  GLU A  79      -9.400 -20.815  20.308  1.00 33.26           C
ATOM    553  OE1 GLU A  79      -9.092 -22.022  20.349  1.00 33.42           O
ATOM    554  OE2 GLU A  79     -10.302 -20.333  21.031  1.00 51.79           O
ATOM    555  N   TYR A  80      -6.747 -17.706  17.108  1.00 12.59           N
ATOM    556  CA  TYR A  80      -5.412 -17.136  17.189  1.00 10.52           C
ATOM    557  C   TYR A  80      -5.564 -15.763  17.817  1.00  9.37           C
ATOM    558  O   TYR A  80      -6.706 -15.266  17.967  1.00  8.32           O
ATOM    559  CB  TYR A  80      -4.743 -17.067  15.808  1.00 11.07           C
ATOM    560  CG  TYR A  80      -5.343 -16.070  14.841  1.00 10.65           C
ATOM    561  CD1 TYR A  80      -4.787 -14.809  14.685  1.00  9.46           C
ATOM    562  CD2 TYR A  80      -6.442 -16.404  14.060  1.00 11.15           C
ATOM    563  CE1 TYR A  80      -5.314 -13.898  13.765  1.00 11.08           C
ATOM    564  CE2 TYR A  80      -6.973 -15.496  13.143  1.00 10.43           C
ATOM    565  CZ  TYR A  80      -6.405 -14.253  13.006  1.00 10.92           C
ATOM    566  OH  TYR A  80      -6.955 -13.357  12.131  1.00 11.76           O
ATOM    567  N   ALA A  81      -4.439 -15.119  18.121  1.00  9.64           N
ATOM    568  CA  ALA A  81      -4.475 -13.821  18.778  1.00  8.14           C
ATOM    569  C   ALA A  81      -3.436 -12.902  18.183  1.00  7.79           C
ATOM    570  O   ALA A  81      -2.452 -13.367  17.587  1.00  6.72           O
ATOM    571  CB  ALA A  81      -4.204 -14.004  20.274  1.00  7.26           C
ATOM    572  N   GLU A  82      -3.692 -11.603  18.282  1.00  9.62           N
ATOM    573  CA  GLU A  82      -2.759 -10.587  17.781  1.00 10.64           C
ATOM    574  C   GLU A  82      -2.667  -9.456  18.786  1.00  9.40           C
ATOM    575  O   GLU A  82      -3.703  -9.028  19.309  1.00  9.38           O
ATOM    576  CB  GLU A  82      -3.273  -9.948  16.478  1.00 15.07           C
ATOM    577  CG  GLU A  82      -3.546 -10.855  15.309  1.00 25.16           C
ATOM    578  CD  GLU A  82      -4.019 -10.082  14.072  1.00 33.61           C
ATOM    579  OE1 GLU A  82      -4.926  -9.214  14.197  1.00 20.55           O
ATOM    580  OE2 GLU A  82      -3.473 -10.344  12.973  1.00 38.02           O
ATOM    581  N   PHE A  83      -1.457  -8.977  19.068  1.00  7.61           N
ATOM    582  CA  PHE A  83      -1.264  -7.825  19.964  1.00  7.90           C
ATOM    583  C   PHE A  83      -0.957  -6.608  19.075  1.00 10.44           C
ATOM    584  O   PHE A  83      -0.164  -6.698  18.120  1.00 12.75           O
ATOM    585  CB  PHE A  83      -0.051  -7.999  20.905  1.00  7.47           C
ATOM    586  CG  PHE A  83      -0.266  -8.985  22.025  1.00  8.63           C
ATOM    587  CD1 PHE A  83       0.155 -10.311  21.897  1.00  8.96           C
ATOM    588  CD2 PHE A  83      -0.849  -8.575  23.222  1.00  8.45           C
ATOM    589  CE1 PHE A  83       0.005 -11.217  22.947  1.00  7.94           C
ATOM    590  CE2 PHE A  83      -1.006  -9.462  24.277  1.00  8.07           C
ATOM    591  CZ  PHE A  83      -0.568 -10.804  24.130  1.00  8.35           C
ATOM    592  N   LEU A  84      -1.525  -5.464  19.433  1.00  9.71           N
ATOM    593  CA  LEU A  84      -1.286  -4.239  18.705  1.00 11.93           C
ATOM    594  C   LEU A  84       0.205  -3.876  18.759  1.00 13.73           C
ATOM    595  O   LEU A  84       0.733  -3.337  17.808  1.00 15.81           O
ATOM    596  CB  LEU A  84      -2.102  -3.100  19.323  1.00 13.23           C
ATOM    597  CG  LEU A  84      -2.141  -1.789  18.534  1.00 16.25           C
ATOM    598  CD1 LEU A  84      -2.561  -2.097  17.085  1.00 16.92           C
ATOM    599  CD2 LEU A  84      -3.135  -0.804  19.194  1.00 15.14           C
ATOM    600  N   HIS A  85       0.877  -4.158  19.868  1.00 16.01           N
ATOM    601  CA  HIS A  85       2.297  -3.815  19.995  1.00 17.58           C
ATOM    602  C   HIS A  85       3.233  -4.836  19.323  1.00 20.72           C
ATOM    603  O   HIS A  85       4.425  -4.578  19.194  1.00 20.84           O
ATOM    604  CB  HIS A  85       2.689  -3.632  21.477  1.00 16.73           C
ATOM    605  CG  HIS A  85       2.846  -4.920  22.226  1.00 15.07           C
ATOM    606  ND1 HIS A  85       1.795  -5.547  22.866  1.00 14.65           N
ATOM    607  CD2 HIS A  85       3.923  -5.723  22.398  1.00 14.06           C
ATOM    608  CE1 HIS A  85       2.218  -6.681  23.396  1.00 13.99           C
ATOM    609  NE2 HIS A  85       3.505  -6.811  23.124  1.00 13.75           N
ATOM    610  N   CYS A  86       2.691  -5.986  18.917  1.00 25.31           N
ATOM    611  CA  CYS A  86       3.474  -7.052  18.253  1.00 28.62           C
ATOM    612  C   CYS A  86       3.081  -7.092  16.785  1.00 27.82           C
ATOM    613  O   CYS A  86       2.452  -8.043  16.316  1.00 26.23           O
ATOM    614  CB  CYS A  86       3.190  -8.428  18.861  1.00 30.34           C
ATOM    615  SG  CYS A  86       3.815  -8.684  20.500  1.00 31.92           S
ATOM    616  N   LYS A  87       3.466  -6.040  16.082  1.00 27.87           N
ATOM    617  CA  LYS A  87       3.181  -5.867  14.672  1.00 28.79           C
ATOM    618  C   LYS A  87       3.397  -7.110  13.825  1.00 27.78           C
ATOM    619  O   LYS A  87       4.444  -7.738  13.900  1.00 27.27           O
ATOM    620  CB  LYS A  87       4.053  -4.737  14.118  1.00 37.67           C
ATOM    621  CG  LYS A  87       4.024  -3.447  14.945  1.00 48.83           C
ATOM    622  CD  LYS A  87       5.134  -2.486  14.499  1.00 55.55           C
ATOM    623  CE  LYS A  87       5.231  -1.260  15.402  1.00 57.44           C
ATOM    624  NZ  LYS A  87       6.370  -0.376  14.995  1.00 59.13           N
ATOM    625  N   GLY A  88       2.356  -7.494  13.098  1.00 27.40           N
ATOM    626  CA  GLY A  88       2.422  -8.614  12.180  1.00 26.04           C
ATOM    627  C   GLY A  88       2.630 -10.017  12.685  1.00 23.91           C
ATOM    628  O   GLY A  88       2.888 -10.915  11.882  1.00 24.23           O
ATOM    629  N   LYS A  89       2.528 -10.211  13.994  1.00 20.65           N
ATOM    630  CA  LYS A  89       2.696 -11.523  14.588  1.00 18.09           C
ATOM    631  C   LYS A  89       1.324 -12.099  14.924  1.00 16.27           C
ATOM    632  O   LYS A  89       0.380 -11.341  15.201  1.00 14.87           O
ATOM    633  CB  LYS A  89       3.504 -11.394  15.885  1.00 22.46           C
ATOM    634  CG  LYS A  89       4.380 -12.573  16.200  1.00 38.95           C
ATOM    635  CD  LYS A  89       5.503 -12.681  15.172  1.00 54.07           C
ATOM    636  CE  LYS A  89       6.384 -11.425  15.167  1.00 53.37           C
ATOM    637  NZ  LYS A  89       7.576 -11.590  14.271  1.00 51.62           N
ATOM    638  N   LYS A  90       1.210 -13.428  14.863  1.00 14.32           N
ATOM    639  CA  LYS A  90      -0.013 -14.125  15.228  1.00 13.20           C
ATOM    640  C   LYS A  90       0.393 -15.217  16.222  1.00 13.11           C
ATOM    641  O   LYS A  90       1.472 -15.804  16.099  1.00 13.28           O
ATOM    642  CB  LYS A  90      -0.712 -14.725  14.002  1.00 13.79           C
ATOM    643  CG  LYS A  90      -1.172 -13.665  12.985  1.00 15.98           C
ATOM    644  CD  LYS A  90      -2.091 -14.274  11.945  1.00 19.12           C
ATOM    645  CE  LYS A  90      -2.582 -13.222  10.953  1.00 24.29           C
ATOM    646  NZ  LYS A  90      -3.864 -12.626  11.402  1.00 44.87           N
ATOM    647  N   PHE A  91      -0.427 -15.411  17.248  1.00 10.40           N
ATOM    648  CA  PHE A  91      -0.160 -16.408  18.274  1.00 10.40           C
ATOM    649  C   PHE A  91      -1.238 -17.452  18.239  1.00 10.05           C
ATOM    650  O   PHE A  91      -2.425 -17.096  18.199  1.00  9.23           O
ATOM    651  CB  PHE A  91      -0.253 -15.787  19.685  1.00  9.81           C
ATOM    652  CG  PHE A  91       0.866 -14.850  20.035  1.00  9.60           C
ATOM    653  CD1 PHE A  91       0.893 -13.568  19.534  1.00 10.20           C
ATOM    654  CD2 PHE A  91       1.883 -15.258  20.889  1.00 11.02           C
ATOM    655  CE1 PHE A  91       1.922 -12.679  19.863  1.00 11.01           C
ATOM    656  CE2 PHE A  91       2.924 -14.386  21.235  1.00 12.01           C
ATOM    657  CZ  PHE A  91       2.944 -13.094  20.719  1.00 12.09           C
ATOM    658  N   THR A  92      -0.867 -18.727  18.249  1.00  9.86           N
ATOM    659  CA  THR A  92      -1.905 -19.741  18.352  1.00 11.36           C
ATOM    660  C   THR A  92      -1.652 -20.560  19.624  1.00 10.20           C
ATOM    661  O   THR A  92      -2.421 -21.473  19.955  1.00 10.27           O
ATOM    662  CB  THR A  92      -2.028 -20.661  17.111  1.00 13.57           C
ATOM    663  OG1 THR A  92      -0.791 -21.336  16.892  1.00 18.42           O
ATOM    664  CG2 THR A  92      -2.398 -19.846  15.853  1.00 15.40           C
ATOM    665  N   ASP A  93      -0.536 -20.284  20.298  1.00  8.71           N
ATOM    666  CA  ASP A  93      -0.231 -20.981  21.543  1.00  9.67           C
ATOM    667  C   ASP A  93      -0.656 -19.991  22.599  1.00 10.45           C
ATOM    668  O   ASP A  93       0.011 -18.969  22.801  1.00 10.60           O
ATOM    669  CB  ASP A  93       1.270 -21.264  21.703  1.00 11.26           C
ATOM    670  CG  ASP A  93       1.586 -22.067  22.977  1.00 18.32           C
ATOM    671  OD1 ASP A  93       2.621 -22.770  23.008  1.00 22.24           O
ATOM    672  OD2 ASP A  93       0.819 -21.988  23.961  1.00 19.27           O
ATOM    673  N   PHE A  94      -1.745 -20.293  23.292  1.00 11.61           N
ATOM    674  CA  PHE A  94      -2.216 -19.358  24.293  1.00 12.80           C
ATOM    675  C   PHE A  94      -1.306 -19.182  25.507  1.00 12.57           C
ATOM    676  O   PHE A  94      -1.361 -18.150  26.165  1.00 12.74           O
ATOM    677  CB  PHE A  94      -3.670 -19.613  24.637  1.00 14.64           C
ATOM    678  CG  PHE A  94      -4.619 -19.145  23.558  1.00 18.67           C
ATOM    679  CD1 PHE A  94      -5.239 -17.906  23.649  1.00 20.75           C
ATOM    680  CD2 PHE A  94      -4.848 -19.918  22.431  1.00 22.02           C
ATOM    681  CE1 PHE A  94      -6.076 -17.433  22.626  1.00 22.45           C
ATOM    682  CE2 PHE A  94      -5.685 -19.457  21.393  1.00 23.69           C
ATOM    683  CZ  PHE A  94      -6.298 -18.205  21.498  1.00 22.67           C
ATOM    684  N   GLU A  95      -0.443 -20.158  25.785  1.00 11.72           N
ATOM    685  CA  GLU A  95       0.506 -19.994  26.900  1.00 10.73           C
ATOM    686  C   GLU A  95       1.529 -18.915  26.467  1.00 10.75           C
ATOM    687  O   GLU A  95       2.030 -18.144  27.281  1.00 10.82           O
ATOM    688  CB  GLU A  95       1.180 -21.330  27.250  1.00 10.89           C
ATOM    689  CG  GLU A  95       2.399 -21.246  28.212  1.00 19.21           C
ATOM    690  CD  GLU A  95       2.133 -20.487  29.519  1.00 30.46           C
ATOM    691  OE1 GLU A  95       0.961 -20.233  29.880  1.00 35.20           O
ATOM    692  OE2 GLU A  95       3.117 -20.128  30.194  1.00 29.05           O
ATOM    693  N   GLU A  96       1.781 -18.822  25.167  1.00 10.66           N
ATOM    694  CA  GLU A  96       2.688 -17.792  24.645  1.00 10.54           C
ATOM    695  C   GLU A  96       1.997 -16.429  24.767  1.00 10.11           C
ATOM    696  O   GLU A  96       2.646 -15.404  25.000  1.00 10.32           O
ATOM    697  CB  GLU A  96       3.074 -18.098  23.188  1.00 12.64           C
ATOM    698  CG  GLU A  96       4.192 -19.159  23.078  1.00 20.77           C
ATOM    699  CD  GLU A  96       5.538 -18.655  23.633  1.00 43.60           C
ATOM    700  OE1 GLU A  96       5.992 -17.561  23.226  1.00 53.45           O
ATOM    701  OE2 GLU A  96       6.152 -19.354  24.469  1.00 50.40           O
ATOM    702  N   VAL A  97       0.670 -16.422  24.648  1.00  8.13           N
ATOM    703  CA  VAL A  97      -0.078 -15.177  24.811  1.00  6.28           C
ATOM    704  C   VAL A  97       0.041 -14.727  26.273  1.00  6.56           C
ATOM    705  O   VAL A  97       0.293 -13.544  26.554  1.00  7.32           O
ATOM    706  CB  VAL A  97      -1.565 -15.355  24.429  1.00  5.58           C
ATOM    707  CG1 VAL A  97      -2.351 -14.084  24.787  1.00  5.46           C
ATOM    708  CG2 VAL A  97      -1.685 -15.622  22.901  1.00  5.16           C
ATOM    709  N   ARG A  98      -0.128 -15.671  27.201  1.00  7.86           N
ATOM    710  CA  ARG A  98      -0.023 -15.373  28.641  1.00  9.80           C
ATOM    711  C   ARG A  98       1.363 -14.790  28.953  1.00 10.89           C
ATOM    712  O   ARG A  98       1.482 -13.752  29.604  1.00 10.81           O
ATOM    713  CB  ARG A  98      -0.267 -16.628  29.494  1.00  8.10           C
ATOM    714  CG  ARG A  98      -0.569 -16.320  30.979  1.00  9.30           C
ATOM    715  CD  ARG A  98      -0.661 -17.589  31.842  1.00  9.34           C
ATOM    716  NE  ARG A  98       0.626 -18.259  31.934  1.00 13.20           N
ATOM    717  CZ  ARG A  98       1.665 -17.797  32.627  1.00 28.20           C
ATOM    718  NH1 ARG A  98       1.572 -16.667  33.327  1.00 39.95           N
ATOM    719  NH2 ARG A  98       2.838 -18.402  32.534  1.00 14.20           N
ATOM    720  N   LEU A  99       2.401 -15.443  28.445  1.00 10.19           N
ATOM    721  CA  LEU A  99       3.769 -14.979  28.661  1.00  9.51           C
ATOM    722  C   LEU A  99       4.002 -13.578  28.085  1.00  9.07           C
ATOM    723  O   LEU A  99       4.756 -12.777  28.660  1.00  8.60           O
ATOM    724  CB  LEU A  99       4.755 -15.979  28.056  1.00  9.95           C
ATOM    725  CG  LEU A  99       4.787 -17.315  28.815  1.00 11.26           C
ATOM    726  CD1 LEU A  99       5.364 -18.438  27.950  1.00 13.87           C
ATOM    727  CD2 LEU A  99       5.575 -17.153  30.092  1.00 12.28           C
ATOM    728  N   GLU A 100       3.377 -13.275  26.947  1.00  9.95           N
ATOM    729  CA  GLU A 100       3.544 -11.955  26.331  1.00  9.82           C
ATOM    730  C   GLU A 100       2.924 -10.864  27.175  1.00 10.38           C
ATOM    731  O   GLU A 100       3.492  -9.773  27.301  1.00 11.54           O
ATOM    732  CB  GLU A 100       2.956 -11.886  24.920  1.00  9.62           C
ATOM    733  CG  GLU A 100       3.203 -10.525  24.237  1.00 19.17           C
ATOM    734  CD  GLU A 100       4.688 -10.128  24.170  1.00 26.23           C
ATOM    735  OE1 GLU A 100       5.561 -11.017  24.127  1.00 17.88           O
ATOM    736  OE2 GLU A 100       4.982  -8.920  24.160  1.00 21.83           O
ATOM    737  N   ILE A 101       1.733 -11.133  27.712  1.00  9.11           N
ATOM    738  CA  ILE A 101       1.074 -10.153  28.571  1.00  8.12           C
ATOM    739  C   ILE A 101       1.999  -9.913  29.772  1.00  8.73           C
ATOM    740  O   ILE A 101       2.300  -8.767  30.115  1.00  8.80           O
ATOM    741  CB  ILE A 101      -0.302 -10.651  29.052  1.00  5.55           C
ATOM    742  CG1 ILE A 101      -1.276 -10.686  27.867  1.00  6.33           C
ATOM    743  CG2 ILE A 101      -0.823  -9.756  30.161  1.00  3.70           C
ATOM    744  CD1 ILE A 101      -2.546 -11.513  28.137  1.00  8.05           C
ATOM    745  N   GLU A 102       2.487 -10.996  30.371  1.00  8.54           N
ATOM    746  CA  GLU A 102       3.382 -10.883  31.525  1.00  9.37           C
ATOM    747  C   GLU A 102       4.658 -10.078  31.180  1.00 10.14           C
ATOM    748  O   GLU A 102       5.020  -9.137  31.888  1.00 12.19           O
ATOM    749  CB  GLU A 102       3.721 -12.296  32.027  1.00 11.82           C
ATOM    750  CG  GLU A 102       4.776 -12.378  33.090  1.00 28.01           C
ATOM    751  CD  GLU A 102       4.964 -13.807  33.576  1.00 44.45           C
ATOM    752  OE1 GLU A 102       4.262 -14.206  34.537  1.00 46.45           O
ATOM    753  OE2 GLU A 102       5.797 -14.530  32.977  1.00 33.81           O
ATOM    754  N   ALA A 103       5.281 -10.395  30.049  1.00  9.32           N
ATOM    755  CA  ALA A 103       6.503  -9.701  29.604  1.00  8.47           C
ATOM    756  C   ALA A 103       6.256  -8.217  29.278  1.00  8.74           C
ATOM    757  O   ALA A 103       7.001  -7.315  29.698  1.00  8.29           O
ATOM    758  CB  ALA A 103       7.093 -10.426  28.403  1.00  7.66           C
ATOM    759  N   GLU A 104       5.200  -7.957  28.525  1.00  7.96           N
ATOM    760  CA  GLU A 104       4.873  -6.593  28.167  1.00  8.29           C
ATOM    761  C   GLU A 104       4.500  -5.797  29.429  1.00  9.67           C
ATOM    762  O   GLU A 104       4.772  -4.600  29.532  1.00 10.41           O
ATOM    763  CB  GLU A 104       3.773  -6.587  27.095  1.00  8.20           C
ATOM    764  CG  GLU A 104       3.284  -5.229  26.673  1.00 11.05           C
ATOM    765  CD  GLU A 104       4.374  -4.317  26.113  1.00 10.90           C
ATOM    766  OE1 GLU A 104       4.156  -3.089  26.149  1.00 17.05           O
ATOM    767  OE2 GLU A 104       5.432  -4.818  25.648  1.00 11.82           O
ATOM    768  N   THR A 105       3.996  -6.483  30.442  1.00 10.76           N
ATOM    769  CA  THR A 105       3.662  -5.801  31.683  1.00  9.26           C
ATOM    770  C   THR A 105       4.972  -5.482  32.424  1.00  9.66           C
ATOM    771  O   THR A 105       5.186  -4.355  32.879  1.00 10.37           O
ATOM    772  CB  THR A 105       2.762  -6.662  32.579  1.00  7.04           C
ATOM    773  OG1 THR A 105       1.469  -6.806  31.959  1.00  5.03           O
ATOM    774  CG2 THR A 105       2.605  -5.986  33.955  1.00  7.38           C
ATOM    775  N   ASP A 106       5.852  -6.468  32.516  1.00  9.90           N
ATOM    776  CA  ASP A 106       7.121  -6.267  33.208  1.00 10.31           C
ATOM    777  C   ASP A 106       7.940  -5.181  32.518  1.00 11.53           C
ATOM    778  O   ASP A 106       8.593  -4.376  33.187  1.00 13.96           O
ATOM    779  CB  ASP A 106       7.929  -7.566  33.268  1.00  7.37           C
ATOM    780  CG  ASP A 106       7.272  -8.629  34.109  1.00 20.03           C
ATOM    781  OD1 ASP A 106       7.685  -9.809  33.979  1.00 23.58           O
ATOM    782  OD2 ASP A 106       6.373  -8.296  34.919  1.00 23.17           O
ATOM    783  N   ARG A 107       7.843  -5.114  31.195  1.00 10.48           N
ATOM    784  CA  ARG A 107       8.602  -4.133  30.424  1.00 12.89           C
ATOM    785  C   ARG A 107       8.311  -2.709  30.861  1.00 15.31           C
ATOM    786  O   ARG A 107       9.204  -1.875  30.909  1.00 16.26           O
ATOM    787  CB  ARG A 107       8.326  -4.283  28.920  1.00 15.16           C
ATOM    788  CG  ARG A 107       9.155  -3.361  28.054  1.00 13.65           C
ATOM    789  CD  ARG A 107       8.827  -3.526  26.569  1.00 18.44           C
ATOM    790  NE  ARG A 107       7.557  -2.901  26.205  1.00 19.28           N
ATOM    791  CZ  ARG A 107       7.391  -1.593  26.010  1.00 25.61           C
ATOM    792  NH1 ARG A 107       8.414  -0.764  26.155  1.00 27.18           N
ATOM    793  NH2 ARG A 107       6.205  -1.113  25.644  1.00 24.69           N
ATOM    794  N   VAL A 108       7.058  -2.441  31.192  1.00 18.23           N
ATOM    795  CA  VAL A 108       6.651  -1.105  31.603  1.00 21.02           C
ATOM    796  C   VAL A 108       6.532  -0.876  33.119  1.00 23.13           C
ATOM    797  O   VAL A 108       6.767   0.222  33.592  1.00 24.28           O
ATOM    798  CB  VAL A 108       5.322  -0.730  30.920  1.00 20.77           C
ATOM    799  CG1 VAL A 108       4.902   0.680  31.330  1.00 21.47           C
ATOM    800  CG2 VAL A 108       5.480  -0.839  29.389  1.00 20.73           C
ATOM    801  N   THR A 109       6.168  -1.901  33.880  1.00 23.91           N
ATOM    802  CA  THR A 109       6.008  -1.737  35.324  1.00 20.79           C
ATOM    803  C   THR A 109       7.142  -2.327  36.174  1.00 22.75           C
ATOM    804  O   THR A 109       7.237  -2.050  37.387  1.00 25.30           O
ATOM    805  CB  THR A 109       4.695  -2.378  35.801  1.00 17.65           C
ATOM    806  OG1 THR A 109       4.774  -3.799  35.615  1.00 25.79           O
ATOM    807  CG2 THR A 109       3.493  -1.861  34.988  1.00 12.73           C
ATOM    808  N   GLY A 110       8.007  -3.123  35.557  1.00 21.05           N
ATOM    809  CA  GLY A 110       9.070  -3.755  36.313  1.00 22.84           C
ATOM    810  C   GLY A 110       8.493  -4.961  37.040  1.00 25.31           C
ATOM    811  O   GLY A 110       7.330  -5.307  36.841  1.00 25.05           O
ATOM    812  N   THR A 111       9.280  -5.591  37.903  1.00 27.18           N
ATOM    813  CA  THR A 111       8.832  -6.781  38.628  1.00 28.21           C
ATOM    814  C   THR A 111       8.795  -6.487  40.126  1.00 25.03           C
ATOM    815  O   THR A 111       8.864  -7.393  40.955  1.00 23.78           O
ATOM    816  CB  THR A 111       9.780  -7.994  38.364  1.00 32.81           C
ATOM    817  OG1 THR A 111      11.109  -7.675  38.799  1.00 33.30           O
ATOM    818  CG2 THR A 111       9.815  -8.335  36.882  1.00 33.19           C
ATOM    819  N   ASN A 112       8.629  -5.212  40.460  1.00 24.33           N
ATOM    820  CA  ASN A 112       8.593  -4.789  41.852  1.00 26.02           C
ATOM    821  C   ASN A 112       7.243  -4.211  42.309  1.00 24.24           C
ATOM    822  O   ASN A 112       7.210  -3.284  43.119  1.00 24.92           O
ATOM    823  CB  ASN A 112       9.725  -3.797  42.125  1.00 31.79           C
ATOM    824  CG  ASN A 112       9.731  -2.636  41.140  1.00 49.01           C
ATOM    825  OD1 ASN A 112       9.125  -2.714  40.059  1.00 45.32           O
ATOM    826  ND2 ASN A 112      10.422  -1.559  41.500  1.00 53.36           N
ATOM    827  N   LYS A 113       6.151  -4.724  41.736  1.00 20.99           N
ATOM    828  CA  LYS A 113       4.768  -4.365  42.107  1.00 18.56           C
ATOM    829  C   LYS A 113       4.090  -3.092  41.591  1.00 16.51           C
ATOM    830  O   LYS A 113       2.930  -2.828  41.944  1.00 15.14           O
ATOM    831  CB  LYS A 113       4.599  -4.394  43.632  1.00 20.29           C
ATOM    832  CG  LYS A 113       5.266  -5.569  44.350  1.00 24.76           C
ATOM    833  CD  LYS A 113       4.742  -6.909  43.903  1.00 30.39           C
ATOM    834  CE  LYS A 113       5.345  -8.020  44.775  1.00 44.38           C
ATOM    835  NZ  LYS A 113       4.888  -9.374  44.366  1.00 44.72           N
ATOM    836  N   GLY A 114       4.784  -2.301  40.784  1.00 14.81           N
ATOM    837  CA  GLY A 114       4.176  -1.078  40.299  1.00 12.22           C
ATOM    838  C   GLY A 114       3.190  -1.310  39.171  1.00 11.59           C
ATOM    839  O   GLY A 114       3.195  -2.357  38.540  1.00 12.76           O
ATOM    840  N   ILE A 115       2.346  -0.326  38.908  1.00 11.54           N
ATOM    841  CA  ILE A 115       1.366  -0.433  37.834  1.00 11.86           C
ATOM    842  C   ILE A 115       1.608   0.681  36.814  1.00 12.63           C
ATOM    843  O   ILE A 115       2.453   1.560  37.019  1.00 13.03           O
ATOM    844  CB  ILE A 115      -0.088  -0.258  38.385  1.00 11.40           C
ATOM    845  CG1 ILE A 115      -0.190   1.024  39.224  1.00 15.41           C
ATOM    846  CG2 ILE A 115      -0.484  -1.432  39.278  1.00  8.23           C
ATOM    847  CD1 ILE A 115      -0.496   2.266  38.448  1.00 23.19           C
ATOM    848  N   SER A 116       0.837   0.658  35.735  1.00 10.50           N
ATOM    849  CA  SER A 116       0.905   1.694  34.724  1.00 10.83           C
ATOM    850  C   SER A 116      -0.436   1.710  34.011  1.00 10.32           C
ATOM    851  O   SER A 116      -0.991   0.659  33.711  1.00 10.39           O
ATOM    852  CB  SER A 116       2.031   1.432  33.717  1.00 10.09           C
ATOM    853  OG  SER A 116       1.672   1.956  32.460  1.00  7.44           O
ATOM    854  N   PRO A 117      -0.951   2.906  33.695  1.00 10.05           N
ATOM    855  CA  PRO A 117      -2.242   2.965  33.006  1.00  9.46           C
ATOM    856  C   PRO A 117      -2.176   2.729  31.491  1.00  8.43           C
ATOM    857  O   PRO A 117      -3.223   2.656  30.848  1.00  8.74           O
ATOM    858  CB  PRO A 117      -2.765   4.370  33.369  1.00  9.04           C
ATOM    859  CG  PRO A 117      -1.501   5.198  33.412  1.00  9.65           C
ATOM    860  CD  PRO A 117      -0.415   4.253  33.980  1.00  9.60           C
ATOM    861  N   VAL A 118      -0.978   2.539  30.920  1.00  5.98           N
ATOM    862  CA  VAL A 118      -0.879   2.341  29.463  1.00  5.45           C
ATOM    863  C   VAL A 118      -1.460   0.963  29.143  1.00  6.77           C
ATOM    864  O   VAL A 118      -0.938  -0.064  29.597  1.00  7.99           O
ATOM    865  CB  VAL A 118       0.595   2.429  28.944  1.00  6.23           C
ATOM    866  CG1 VAL A 118       0.624   2.286  27.396  1.00  6.62           C
ATOM    867  CG2 VAL A 118       1.262   3.775  29.413  1.00  6.36           C
ATOM    868  N   PRO A 119      -2.483   0.906  28.283  1.00  7.92           N
ATOM    869  CA  PRO A 119      -3.098  -0.390  27.956  1.00  7.49           C
ATOM    870  C   PRO A 119      -2.307  -1.350  27.099  1.00  7.72           C
ATOM    871  O   PRO A 119      -1.456  -0.959  26.304  1.00  5.79           O
ATOM    872  CB  PRO A 119      -4.376   0.001  27.174  1.00  7.47           C
ATOM    873  CG  PRO A 119      -4.609   1.482  27.497  1.00  7.99           C
ATOM    874  CD  PRO A 119      -3.163   2.005  27.567  1.00  8.52           C
ATOM    875  N   ILE A 120      -2.604  -2.630  27.279  1.00  8.71           N
ATOM    876  CA  ILE A 120      -2.026  -3.668  26.447  1.00  8.01           C
ATOM    877  C   ILE A 120      -3.264  -3.941  25.578  1.00  8.29           C
ATOM    878  O   ILE A 120      -4.368  -4.083  26.130  1.00  7.74           O
ATOM    879  CB  ILE A 120      -1.665  -4.922  27.255  1.00  7.57           C
ATOM    880  CG1 ILE A 120      -0.477  -4.599  28.172  1.00 10.44           C
ATOM    881  CG2 ILE A 120      -1.283  -6.059  26.294  1.00  7.92           C
ATOM    882  CD1 ILE A 120      -0.037  -5.734  29.032  1.00  5.12           C
ATOM    883  N   ASN A 121      -3.097  -3.960  24.253  1.00  7.85           N
ATOM    884  CA  ASN A 121      -4.211  -4.180  23.322  1.00  7.84           C
ATOM    885  C   ASN A 121      -4.085  -5.570  22.709  1.00  8.34           C
ATOM    886  O   ASN A 121      -3.094  -5.882  22.037  1.00  9.41           O
ATOM    887  CB  ASN A 121      -4.241  -3.076  22.252  1.00  8.42           C
ATOM    888  CG  ASN A 121      -4.517  -1.692  22.856  1.00  9.71           C
ATOM    889  OD1 ASN A 121      -5.626  -1.406  23.302  1.00 15.82           O
ATOM    890  ND2 ASN A 121      -3.494  -0.863  22.932  1.00  8.55           N
ATOM    891  N   LEU A 122      -5.098  -6.394  22.952  1.00  5.91           N
ATOM    892  CA  LEU A 122      -5.095  -7.777  22.517  1.00  6.52           C
ATOM    893  C   LEU A 122      -6.392  -8.153  21.814  1.00  6.90           C
ATOM    894  O   LEU A 122      -7.465  -7.785  22.288  1.00  8.07           O
ATOM    895  CB  LEU A 122      -4.940  -8.678  23.769  1.00  6.97           C
ATOM    896  CG  LEU A 122      -5.045 -10.201  23.566  1.00  7.47           C
ATOM    897  CD1 LEU A 122      -4.045 -10.666  22.494  1.00  7.92           C
ATOM    898  CD2 LEU A 122      -4.822 -10.934  24.898  1.00  6.07           C
ATOM    899  N   ARG A 123      -6.298  -8.892  20.705  1.00  6.96           N
ATOM    900  CA  ARG A 123      -7.489  -9.358  20.002  1.00  5.96           C
ATOM    901  C   ARG A 123      -7.400 -10.872  19.874  1.00  7.66           C
ATOM    902  O   ARG A 123      -6.358 -11.403  19.493  1.00  9.15           O
ATOM    903  CB  ARG A 123      -7.631  -8.721  18.602  1.00  5.21           C
ATOM    904  CG  ARG A 123      -8.896  -9.192  17.833  1.00  6.04           C
ATOM    905  CD  ARG A 123      -9.290  -8.241  16.667  1.00 13.39           C
ATOM    906  NE  ARG A 123      -8.165  -7.936  15.789  1.00 18.56           N
ATOM    907  CZ  ARG A 123      -7.572  -6.743  15.705  1.00 26.75           C
ATOM    908  NH1 ARG A 123      -8.000  -5.722  16.434  1.00 22.09           N
ATOM    909  NH2 ARG A 123      -6.493  -6.592  14.946  1.00 33.84           N
ATOM    910  N   VAL A 124      -8.491 -11.568  20.168  1.00  5.85           N
ATOM    911  CA  VAL A 124      -8.491 -13.028  20.078  1.00  6.31           C
ATOM    912  C   VAL A 124      -9.643 -13.441  19.172  1.00  6.89           C
ATOM    913  O   VAL A 124     -10.791 -13.025  19.395  1.00  6.97           O
ATOM    914  CB  VAL A 124      -8.691 -13.684  21.480  1.00  6.93           C
ATOM    915  CG1 VAL A 124      -8.927 -15.200  21.332  1.00  7.44           C
ATOM    916  CG2 VAL A 124      -7.484 -13.424  22.394  1.00  5.95           C
ATOM    917  N   TYR A 125      -9.314 -14.164  18.099  1.00  7.18           N
ATOM    918  CA  TYR A 125     -10.300 -14.685  17.147  1.00  6.80           C
ATOM    919  C   TYR A 125     -10.583 -16.131  17.584  1.00  6.83           C
ATOM    920  O   TYR A 125      -9.655 -16.873  17.937  1.00  5.60           O
ATOM    921  CB  TYR A 125      -9.722 -14.718  15.732  1.00  6.69           C
ATOM    922  CG  TYR A 125      -9.486 -13.368  15.111  1.00  8.55           C
ATOM    923  CD1 TYR A 125     -10.505 -12.699  14.429  1.00  8.20           C
ATOM    924  CD2 TYR A 125      -8.244 -12.762  15.193  1.00  9.56           C
ATOM    925  CE1 TYR A 125     -10.271 -11.448  13.837  1.00  9.89           C
ATOM    926  CE2 TYR A 125      -8.001 -11.509  14.613  1.00 10.68           C
ATOM    927  CZ  TYR A 125      -9.013 -10.867  13.937  1.00 13.29           C
ATOM    928  OH  TYR A 125      -8.740  -9.648  13.348  1.00 19.01           O
ATOM    929  N   SER A 126     -11.850 -16.540  17.549  1.00  7.58           N
ATOM    930  CA  SER A 126     -12.195 -17.895  17.969  1.00  8.91           C
ATOM    931  C   SER A 126     -13.630 -18.270  17.638  1.00 10.11           C
ATOM    932  O   SER A 126     -14.536 -17.457  17.743  1.00  9.09           O
ATOM    933  CB  SER A 126     -11.979 -18.041  19.479  1.00 12.19           C
ATOM    934  OG  SER A 126     -12.535 -19.251  19.986  1.00 13.83           O
ATOM    935  N   PRO A 127     -13.852 -19.538  17.250  1.00 10.28           N
ATOM    936  CA  PRO A 127     -15.215 -19.973  16.929  1.00  9.90           C
ATOM    937  C   PRO A 127     -16.064 -20.073  18.199  1.00 10.77           C
ATOM    938  O   PRO A 127     -17.293 -20.134  18.139  1.00  9.43           O
ATOM    939  CB  PRO A 127     -14.988 -21.350  16.283  1.00 10.39           C
ATOM    940  CG  PRO A 127     -13.725 -21.867  16.971  1.00 10.23           C
ATOM    941  CD  PRO A 127     -12.858 -20.603  16.980  1.00  9.29           C
ATOM    942  N   HIS A 128     -15.410 -20.024  19.359  1.00 14.74           N
ATOM    943  CA  HIS A 128     -16.124 -20.167  20.625  1.00 16.85           C
ATOM    944  C   HIS A 128     -16.465 -18.878  21.373  1.00 15.87           C
ATOM    945  O   HIS A 128     -17.124 -18.924  22.425  1.00 14.87           O
ATOM    946  CB  HIS A 128     -15.321 -21.081  21.556  1.00 17.99           C
ATOM    947  CG  HIS A 128     -14.926 -22.375  20.920  1.00 19.20           C
ATOM    948  ND1 HIS A 128     -15.841 -23.221  20.327  1.00 19.90           N
ATOM    949  CD2 HIS A 128     -13.710 -22.949  20.748  1.00 20.32           C
ATOM    950  CE1 HIS A 128     -15.208 -24.262  19.815  1.00 20.41           C
ATOM    951  NE2 HIS A 128     -13.913 -24.121  20.057  1.00 20.77           N
ATOM    952  N   VAL A 129     -16.050 -17.730  20.844  1.00 11.75           N
ATOM    953  CA  VAL A 129     -16.306 -16.498  21.571  1.00  9.26           C
ATOM    954  C   VAL A 129     -17.403 -15.622  20.989  1.00  9.58           C
ATOM    955  O   VAL A 129     -17.809 -15.773  19.830  1.00  7.54           O
ATOM    956  CB  VAL A 129     -15.000 -15.662  21.738  1.00  8.01           C
ATOM    957  CG1 VAL A 129     -13.906 -16.529  22.364  1.00  7.13           C
ATOM    958  CG2 VAL A 129     -14.511 -15.082  20.370  1.00  6.92           C
ATOM    959  N   LEU A 130     -17.917 -14.756  21.850  1.00 10.72           N
ATOM    960  CA  LEU A 130     -18.921 -13.772  21.491  1.00 12.55           C
ATOM    961  C   LEU A 130     -18.179 -12.589  20.839  1.00 13.04           C
ATOM    962  O   LEU A 130     -16.938 -12.491  20.923  1.00 13.54           O
ATOM    963  CB  LEU A 130     -19.600 -13.278  22.769  1.00 13.18           C
ATOM    964  CG  LEU A 130     -20.394 -14.319  23.554  1.00 15.39           C
ATOM    965  CD1 LEU A 130     -20.570 -13.867  24.987  1.00 14.13           C
ATOM    966  CD2 LEU A 130     -21.746 -14.553  22.865  1.00 18.15           C
ATOM    967  N   ASN A 131     -18.923 -11.688  20.204  1.00 10.96           N
ATOM    968  CA  ASN A 131     -18.309 -10.517  19.593  1.00 10.62           C
ATOM    969  C   ASN A 131     -18.494  -9.364  20.581  1.00 11.27           C
ATOM    970  O   ASN A 131     -19.607  -8.862  20.755  1.00 12.01           O
ATOM    971  CB  ASN A 131     -18.980 -10.177  18.259  1.00 10.15           C
ATOM    972  CG  ASN A 131     -18.803 -11.264  17.229  1.00 13.41           C
ATOM    973  OD1 ASN A 131     -19.703 -12.076  17.009  1.00 25.08           O
ATOM    974  ND2 ASN A 131     -17.643 -11.304  16.606  1.00  9.01           N
ATOM    975  N   LEU A 132     -17.421  -9.013  21.284  1.00 10.62           N
ATOM    976  CA  LEU A 132     -17.454  -7.945  22.275  1.00  9.56           C
ATOM    977  C   LEU A 132     -16.054  -7.641  22.772  1.00  9.00           C
ATOM    978  O   LEU A 132     -15.114  -8.413  22.542  1.00  7.42           O
ATOM    979  CB  LEU A 132     -18.375  -8.299  23.452  1.00  9.61           C
ATOM    980  CG  LEU A 132     -18.359  -9.722  24.036  1.00  9.87           C
ATOM    981  CD1 LEU A 132     -17.082  -9.947  24.843  1.00 10.96           C
ATOM    982  CD2 LEU A 132     -19.577  -9.880  24.954  1.00 10.01           C
ATOM    983  N   THR A 133     -15.917  -6.515  23.454  1.00  8.66           N
ATOM    984  CA  THR A 133     -14.630  -6.096  23.980  1.00  8.04           C
ATOM    985  C   THR A 133     -14.662  -6.020  25.503  1.00  9.31           C
ATOM    986  O   THR A 133     -15.591  -5.427  26.091  1.00 10.26           O
ATOM    987  CB  THR A 133     -14.261  -4.731  23.404  1.00  9.09           C
ATOM    988  OG1 THR A 133     -14.204  -4.839  21.978  1.00 14.13           O
ATOM    989  CG2 THR A 133     -12.910  -4.251  23.947  1.00  4.43           C
ATOM    990  N   LEU A 134     -13.657  -6.616  26.141  1.00  8.32           N
ATOM    991  CA  LEU A 134     -13.567  -6.624  27.598  1.00  8.28           C
ATOM    992  C   LEU A 134     -12.328  -5.850  27.991  1.00  8.31           C
ATOM    993  O   LEU A 134     -11.368  -5.765  27.210  1.00  8.69           O
ATOM    994  CB  LEU A 134     -13.408  -8.068  28.123  1.00  8.61           C
ATOM    995  CG  LEU A 134     -14.460  -9.095  27.705  1.00  7.76           C
ATOM    996  CD1 LEU A 134     -14.092 -10.513  28.134  1.00  8.91           C
ATOM    997  CD2 LEU A 134     -15.764  -8.698  28.305  1.00  6.11           C
ATOM    998  N   VAL A 135     -12.334  -5.307  29.202  1.00  6.29           N
ATOM    999  CA  VAL A 135     -11.184  -4.587  29.705  1.00  4.12           C
ATOM   1000  C   VAL A 135     -10.815  -5.148  31.061  1.00  4.03           C
ATOM   1001  O   VAL A 135     -11.577  -5.014  32.031  1.00  5.24           O
ATOM   1002  CB  VAL A 135     -11.463  -3.093  29.900  1.00  2.28           C
ATOM   1003  CG1 VAL A 135     -10.187  -2.410  30.354  1.00  1.16           C
ATOM   1004  CG2 VAL A 135     -11.970  -2.454  28.596  1.00  2.20           C
ATOM   1005  N   ASP A 136      -9.668  -5.803  31.131  1.00  3.30           N
ATOM   1006  CA  ASP A 136      -9.204  -6.343  32.406  1.00  5.16           C
ATOM   1007  C   ASP A 136      -8.461  -5.190  33.090  1.00  5.87           C
ATOM   1008  O   ASP A 136      -7.719  -4.461  32.422  1.00  6.65           O
ATOM   1009  CB  ASP A 136      -8.240  -7.513  32.178  1.00  3.68           C
ATOM   1010  CG  ASP A 136      -8.064  -8.402  33.436  1.00  8.01           C
ATOM   1011  OD1 ASP A 136      -8.822  -8.248  34.419  1.00  7.24           O
ATOM   1012  OD2 ASP A 136      -7.174  -9.282  33.412  1.00  8.52           O
ATOM   1013  N   LEU A 137      -8.577  -5.095  34.411  1.00  6.47           N
ATOM   1014  CA  LEU A 137      -7.931  -4.007  35.177  1.00  6.47           C
ATOM   1015  C   LEU A 137      -7.407  -4.474  36.529  1.00  5.72           C
ATOM   1016  O   LEU A 137      -7.930  -5.432  37.107  1.00  7.17           O
ATOM   1017  CB  LEU A 137      -8.937  -2.870  35.418  1.00  6.25           C
ATOM   1018  CG  LEU A 137      -9.414  -2.139  34.146  1.00  7.50           C
ATOM   1019  CD1 LEU A 137     -10.734  -1.392  34.365  1.00  6.95           C
ATOM   1020  CD2 LEU A 137      -8.350  -1.156  33.749  1.00  7.20           C
ATOM   1021  N   PRO A 138      -6.339  -3.825  37.037  1.00  5.50           N
ATOM   1022  CA  PRO A 138      -5.774  -4.200  38.341  1.00  5.17           C
ATOM   1023  C   PRO A 138      -6.840  -3.915  39.395  1.00  5.91           C
ATOM   1024  O   PRO A 138      -7.631  -2.965  39.254  1.00  8.11           O
ATOM   1025  CB  PRO A 138      -4.596  -3.240  38.495  1.00  5.04           C
ATOM   1026  CG  PRO A 138      -4.165  -2.991  37.069  1.00  4.42           C
ATOM   1027  CD  PRO A 138      -5.520  -2.773  36.395  1.00  4.53           C
ATOM   1028  N   GLY A 139      -6.874  -4.760  40.422  1.00  4.38           N
ATOM   1029  CA  GLY A 139      -7.854  -4.609  41.485  1.00  5.33           C
ATOM   1030  C   GLY A 139      -7.447  -3.515  42.457  1.00  5.89           C
ATOM   1031  O   GLY A 139      -6.252  -3.297  42.649  1.00  4.73           O
HETATM 1032  N   MSE A 140      -8.427  -2.862  43.083  1.00  5.09           N
HETATM 1033  CA  MSE A 140      -8.168  -1.783  44.030  1.00  6.65           C
HETATM 1034  C   MSE A 140      -7.518  -2.283  45.327  1.00  7.45           C
HETATM 1035  O   MSE A 140      -7.731  -3.431  45.734  1.00  7.15           O
HETATM 1036  CB  MSE A 140      -9.476  -1.040  44.328  1.00  8.24           C
HETATM 1037  CG  MSE A 140      -9.964  -0.207  43.157  1.00 12.10           C
HETATM 1038 SE   MSE A 140     -11.834   0.360  43.410  1.00 15.83          Se
HETATM 1039  CE  MSE A 140     -12.749  -1.044  42.413  1.00 15.08           C
ATOM   1040  N   THR A 141      -6.731  -1.424  45.972  1.00  8.13           N
ATOM   1041  CA  THR A 141      -6.043  -1.796  47.209  1.00  7.82           C
ATOM   1042  C   THR A 141      -6.157  -0.676  48.220  1.00 11.05           C
ATOM   1043  O   THR A 141      -6.661   0.421  47.902  1.00 11.39           O
ATOM   1044  CB  THR A 141      -4.537  -2.089  46.979  1.00  8.32           C
ATOM   1045  OG1 THR A 141      -3.862  -0.897  46.561  1.00  8.83           O
ATOM   1046  CG2 THR A 141      -4.342  -3.150  45.903  1.00  8.87           C
ATOM   1047  N   LYS A 142      -5.646  -0.937  49.423  1.00 11.74           N
ATOM   1048  CA  LYS A 142      -5.689   0.023  50.520  1.00 11.23           C
ATOM   1049  C   LYS A 142      -4.319   0.387  51.086  1.00 13.97           C
ATOM   1050  O   LYS A 142      -4.153   1.478  51.627  1.00 15.55           O
ATOM   1051  CB  LYS A 142      -6.567  -0.504  51.649  1.00  8.93           C
ATOM   1052  CG  LYS A 142      -8.038  -0.599  51.303  1.00 12.91           C
ATOM   1053  CD  LYS A 142      -8.538   0.760  50.843  1.00 26.24           C
ATOM   1054  CE  LYS A 142     -10.041   0.785  50.658  1.00 35.79           C
ATOM   1055  NZ  LYS A 142     -10.515   2.173  50.413  1.00 38.28           N
ATOM   1056  N   VAL A 143      -3.351  -0.521  51.017  1.00 14.48           N
ATOM   1057  CA  VAL A 143      -2.017  -0.218  51.544  1.00 15.42           C
ATOM   1058  C   VAL A 143      -0.941  -0.673  50.585  1.00 15.05           C
ATOM   1059  O   VAL A 143      -1.040  -1.765  50.034  1.00 13.89           O
ATOM   1060  CB  VAL A 143      -1.764  -0.864  52.931  1.00 16.43           C
ATOM   1061  CG1 VAL A 143      -2.732  -0.331  53.922  1.00 17.16           C
ATOM   1062  CG2 VAL A 143      -1.871  -2.371  52.870  1.00 16.47           C
ATOM   1063  N   PRO A 144       0.058   0.196  50.309  1.00 14.91           N
ATOM   1064  CA  PRO A 144       1.149  -0.137  49.397  1.00 16.35           C
ATOM   1065  C   PRO A 144       2.018  -1.269  49.913  1.00 20.38           C
ATOM   1066  O   PRO A 144       1.993  -1.594  51.099  1.00 20.87           O
ATOM   1067  CB  PRO A 144       1.933   1.173  49.281  1.00 14.97           C
ATOM   1068  CG  PRO A 144       1.659   1.869  50.591  1.00 14.29           C
ATOM   1069  CD  PRO A 144       0.183   1.585  50.795  1.00 14.27           C
ATOM   1070  N   VAL A 145       2.770  -1.874  49.001  1.00 25.66           N
ATOM   1071  CA  VAL A 145       3.646  -2.978  49.352  1.00 28.52           C
ATOM   1072  C   VAL A 145       4.802  -3.010  48.357  1.00 29.90           C
ATOM   1073  O   VAL A 145       4.717  -2.401  47.293  1.00 29.25           O
ATOM   1074  CB  VAL A 145       2.844  -4.312  49.362  1.00 29.09           C
ATOM   1075  CG1 VAL A 145       2.393  -4.705  47.951  1.00 29.43           C
ATOM   1076  CG2 VAL A 145       3.657  -5.382  49.976  1.00 29.97           C
ATOM   1077  N   GLY A 146       5.905  -3.664  48.715  1.00 33.25           N
ATOM   1078  CA  GLY A 146       7.047  -3.719  47.810  1.00 34.56           C
ATOM   1079  C   GLY A 146       7.516  -2.321  47.433  1.00 34.87           C
ATOM   1080  O   GLY A 146       7.690  -1.474  48.298  1.00 34.57           O
ATOM   1081  N   ASP A 147       7.684  -2.060  46.141  1.00 36.86           N
ATOM   1082  CA  ASP A 147       8.116  -0.737  45.702  1.00 37.90           C
ATOM   1083  C   ASP A 147       6.982   0.129  45.179  1.00 37.60           C
ATOM   1084  O   ASP A 147       7.178   0.987  44.310  1.00 39.85           O
ATOM   1085  CB  ASP A 147       9.244  -0.846  44.676  1.00 42.07           C
ATOM   1086  CG  ASP A 147      10.607  -1.066  45.332  1.00 52.21           C
ATOM   1087  OD1 ASP A 147      11.620  -1.115  44.592  1.00 54.35           O
ATOM   1088  OD2 ASP A 147      10.663  -1.183  46.586  1.00 51.42           O
ATOM   1089  N   GLN A 148       5.788  -0.087  45.717  1.00 33.68           N
ATOM   1090  CA  GLN A 148       4.638   0.692  45.294  1.00 30.22           C
ATOM   1091  C   GLN A 148       4.652   2.036  46.011  1.00 26.11           C
ATOM   1092  O   GLN A 148       5.054   2.129  47.169  1.00 23.51           O
ATOM   1093  CB  GLN A 148       3.334  -0.043  45.639  1.00 30.63           C
ATOM   1094  CG  GLN A 148       3.102  -1.344  44.876  1.00 23.45           C
ATOM   1095  CD  GLN A 148       1.852  -2.075  45.341  1.00 13.51           C
ATOM   1096  OE1 GLN A 148       1.357  -1.839  46.438  1.00 10.84           O
ATOM   1097  NE2 GLN A 148       1.328  -2.948  44.497  1.00  4.47           N
ATOM   1098  N   PRO A 149       4.202   3.095  45.328  1.00 23.60           N
ATOM   1099  CA  PRO A 149       4.166   4.427  45.931  1.00 21.89           C
ATOM   1100  C   PRO A 149       3.069   4.562  46.985  1.00 21.31           C
ATOM   1101  O   PRO A 149       2.064   3.839  46.952  1.00 19.91           O
ATOM   1102  CB  PRO A 149       3.924   5.341  44.734  1.00 22.70           C
ATOM   1103  CG  PRO A 149       3.225   4.457  43.739  1.00 23.47           C
ATOM   1104  CD  PRO A 149       3.934   3.149  43.882  1.00 23.90           C
ATOM   1105  N   PRO A 150       3.251   5.490  47.949  1.00 19.75           N
ATOM   1106  CA  PRO A 150       2.258   5.703  49.004  1.00 18.50           C
ATOM   1107  C   PRO A 150       0.822   5.873  48.497  1.00 17.16           C
ATOM   1108  O   PRO A 150      -0.115   5.415  49.157  1.00 17.13           O
ATOM   1109  CB  PRO A 150       2.753   6.980  49.684  1.00 18.94           C
ATOM   1110  CG  PRO A 150       4.243   6.847  49.588  1.00 19.22           C
ATOM   1111  CD  PRO A 150       4.422   6.369  48.143  1.00 19.16           C
ATOM   1112  N   ASP A 151       0.648   6.473  47.315  1.00 15.62           N
ATOM   1113  CA  ASP A 151      -0.702   6.696  46.784  1.00 14.37           C
ATOM   1114  C   ASP A 151      -1.183   5.636  45.781  1.00 13.64           C
ATOM   1115  O   ASP A 151      -2.045   5.899  44.936  1.00 14.49           O
ATOM   1116  CB  ASP A 151      -0.805   8.110  46.178  1.00 16.19           C
ATOM   1117  CG  ASP A 151       0.049   8.288  44.925  1.00 17.81           C
ATOM   1118  OD1 ASP A 151       1.031   7.540  44.734  1.00 21.23           O
ATOM   1119  OD2 ASP A 151      -0.273   9.179  44.113  1.00 21.87           O
ATOM   1120  N   ILE A 152      -0.623   4.437  45.871  1.00 11.99           N
ATOM   1121  CA  ILE A 152      -1.001   3.339  44.976  1.00 10.94           C
ATOM   1122  C   ILE A 152      -2.533   3.108  44.891  1.00 10.97           C
ATOM   1123  O   ILE A 152      -3.063   2.837  43.802  1.00 10.86           O
ATOM   1124  CB  ILE A 152      -0.279   2.051  45.390  1.00  9.62           C
ATOM   1125  CG1 ILE A 152      -0.509   0.951  44.358  1.00 13.95           C
ATOM   1126  CG2 ILE A 152      -0.703   1.645  46.801  1.00  7.75           C
ATOM   1127  CD1 ILE A 152       0.087   1.247  43.005  1.00 13.77           C
ATOM   1128  N   GLU A 153      -3.238   3.283  46.011  1.00 10.90           N
ATOM   1129  CA  GLU A 153      -4.694   3.119  46.028  1.00 11.88           C
ATOM   1130  C   GLU A 153      -5.297   4.095  45.009  1.00 13.57           C
ATOM   1131  O   GLU A 153      -6.088   3.711  44.143  1.00 14.58           O
ATOM   1132  CB  GLU A 153      -5.283   3.413  47.418  1.00  9.54           C
ATOM   1133  CG  GLU A 153      -6.810   3.392  47.448  1.00  9.19           C
ATOM   1134  CD  GLU A 153      -7.436   3.690  48.820  1.00 20.22           C
ATOM   1135  OE1 GLU A 153      -6.714   3.810  49.849  1.00 16.34           O
ATOM   1136  OE2 GLU A 153      -8.683   3.813  48.862  1.00 17.45           O
ATOM   1137  N   PHE A 154      -4.905   5.358  45.117  1.00 15.09           N
ATOM   1138  CA  PHE A 154      -5.393   6.386  44.210  1.00 16.42           C
ATOM   1139  C   PHE A 154      -4.995   6.141  42.743  1.00 13.86           C
ATOM   1140  O   PHE A 154      -5.816   6.329  41.850  1.00 14.39           O
ATOM   1141  CB  PHE A 154      -4.947   7.783  44.672  1.00 19.02           C
ATOM   1142  CG  PHE A 154      -5.300   8.874  43.703  1.00 25.60           C
ATOM   1143  CD1 PHE A 154      -6.553   9.485  43.748  1.00 28.77           C
ATOM   1144  CD2 PHE A 154      -4.402   9.246  42.694  1.00 29.05           C
ATOM   1145  CE1 PHE A 154      -6.917  10.451  42.796  1.00 30.63           C
ATOM   1146  CE2 PHE A 154      -4.749  10.203  41.739  1.00 30.62           C
ATOM   1147  CZ  PHE A 154      -6.014  10.809  41.789  1.00 31.27           C
ATOM   1148  N   GLN A 155      -3.752   5.745  42.483  1.00  9.34           N
ATOM   1149  CA  GLN A 155      -3.327   5.493  41.108  1.00  8.29           C
ATOM   1150  C   GLN A 155      -4.175   4.373  40.460  1.00  7.71           C
ATOM   1151  O   GLN A 155      -4.606   4.487  39.317  1.00  7.60           O
ATOM   1152  CB  GLN A 155      -1.837   5.121  41.050  1.00 13.24           C
ATOM   1153  CG  GLN A 155      -0.849   6.317  41.101  1.00 25.35           C
ATOM   1154  CD  GLN A 155       0.623   5.898  40.958  1.00 42.67           C
ATOM   1155  OE1 GLN A 155       1.508   6.452  41.627  1.00 53.07           O
ATOM   1156  NE2 GLN A 155       0.892   4.932  40.079  1.00 35.79           N
ATOM   1157  N   ILE A 156      -4.429   3.304  41.203  1.00  6.07           N
ATOM   1158  CA  ILE A 156      -5.210   2.201  40.675  1.00  5.21           C
ATOM   1159  C   ILE A 156      -6.672   2.613  40.424  1.00  5.67           C
ATOM   1160  O   ILE A 156      -7.226   2.268  39.391  1.00  7.68           O
ATOM   1161  CB  ILE A 156      -5.110   0.943  41.586  1.00  5.04           C
ATOM   1162  CG1 ILE A 156      -3.702   0.327  41.452  1.00  3.16           C
ATOM   1163  CG2 ILE A 156      -6.175  -0.122  41.179  1.00  2.49           C
ATOM   1164  CD1 ILE A 156      -3.394  -0.749  42.555  1.00  4.79           C
ATOM   1165  N   ARG A 157      -7.293   3.325  41.371  1.00  7.35           N
ATOM   1166  CA  ARG A 157      -8.671   3.769  41.179  1.00  8.31           C
ATOM   1167  C   ARG A 157      -8.729   4.772  40.009  1.00 10.13           C
ATOM   1168  O   ARG A 157      -9.618   4.679  39.155  1.00 10.06           O
ATOM   1169  CB  ARG A 157      -9.271   4.367  42.474  1.00  5.73           C
ATOM   1170  CG  ARG A 157     -10.733   4.871  42.322  1.00  9.86           C
ATOM   1171  CD  ARG A 157     -11.342   5.338  43.674  1.00 13.47           C
ATOM   1172  NE  ARG A 157     -12.745   5.764  43.578  1.00 13.20           N
ATOM   1173  CZ  ARG A 157     -13.162   6.887  42.993  1.00 11.36           C
ATOM   1174  NH1 ARG A 157     -12.283   7.724  42.424  1.00  6.54           N
ATOM   1175  NH2 ARG A 157     -14.459   7.188  42.995  1.00 12.91           N
ATOM   1176  N   ASP A 158      -7.749   5.678  39.908  1.00 10.20           N
ATOM   1177  CA  ASP A 158      -7.774   6.647  38.791  1.00 10.64           C
ATOM   1178  C   ASP A 158      -7.763   5.921  37.432  1.00 11.72           C
ATOM   1179  O   ASP A 158      -8.468   6.288  36.491  1.00 13.57           O
ATOM   1180  CB  ASP A 158      -6.573   7.596  38.845  1.00 10.05           C
ATOM   1181  CG  ASP A 158      -6.668   8.709  37.795  1.00 17.57           C
ATOM   1182  OD1 ASP A 158      -7.572   9.555  37.914  1.00 19.72           O
ATOM   1183  OD2 ASP A 158      -5.868   8.725  36.840  1.00 20.21           O
HETATM 1184  N   MSE A 159      -6.946   4.887  37.334  1.00 10.77           N
HETATM 1185  CA  MSE A 159      -6.834   4.113  36.108  1.00 10.97           C
HETATM 1186  C   MSE A 159      -8.183   3.491  35.696  1.00 11.32           C
HETATM 1187  O   MSE A 159      -8.597   3.610  34.545  1.00 13.52           O
HETATM 1188  CB  MSE A 159      -5.744   3.042  36.298  1.00 12.43           C
HETATM 1189  CG  MSE A 159      -5.764   1.851  35.360  1.00 14.20           C
HETATM 1190 SE   MSE A 159      -4.153   0.755  35.619  1.00 18.41          Se
HETATM 1191  CE  MSE A 159      -4.114   0.610  37.549  1.00 17.31           C
ATOM   1192  N   LEU A 160      -8.881   2.845  36.622  1.00  8.42           N
ATOM   1193  CA  LEU A 160     -10.150   2.235  36.239  1.00  8.09           C
ATOM   1194  C   LEU A 160     -11.231   3.295  35.990  1.00  8.36           C
ATOM   1195  O   LEU A 160     -12.110   3.098  35.153  1.00  8.87           O
ATOM   1196  CB  LEU A 160     -10.600   1.151  37.244  1.00  8.72           C
ATOM   1197  CG  LEU A 160     -10.919   1.487  38.692  1.00 11.32           C
ATOM   1198  CD1 LEU A 160     -12.279   2.164  38.789  1.00 12.69           C
ATOM   1199  CD2 LEU A 160     -10.905   0.215  39.538  1.00 11.98           C
HETATM 1200  N   MSE A 161     -11.112   4.444  36.653  1.00  9.90           N
HETATM 1201  CA  MSE A 161     -12.084   5.534  36.485  1.00 10.76           C
HETATM 1202  C   MSE A 161     -12.110   6.028  35.048  1.00  9.50           C
HETATM 1203  O   MSE A 161     -13.166   6.357  34.524  1.00 10.06           O
HETATM 1204  CB  MSE A 161     -11.792   6.713  37.426  1.00 13.07           C
HETATM 1205  CG  MSE A 161     -12.185   6.481  38.888  1.00 15.93           C
HETATM 1206 SE   MSE A 161     -14.122   6.143  39.194  1.00 20.76          Se
HETATM 1207  CE  MSE A 161     -14.763   7.975  39.098  1.00 19.75           C
ATOM   1208  N   GLN A 162     -10.956   6.054  34.394  1.00  8.39           N
ATOM   1209  CA  GLN A 162     -10.924   6.523  33.017  1.00  7.13           C
ATOM   1210  C   GLN A 162     -11.792   5.640  32.127  1.00  7.00           C
ATOM   1211  O   GLN A 162     -12.335   6.105  31.126  1.00  6.48           O
ATOM   1212  CB  GLN A 162      -9.488   6.574  32.483  1.00  3.88           C
ATOM   1213  CG  GLN A 162      -8.531   7.340  33.410  1.00 12.31           C
ATOM   1214  CD  GLN A 162      -9.107   8.695  33.852  1.00 34.59           C
ATOM   1215  OE1 GLN A 162      -9.370   9.576  33.020  1.00 34.96           O
ATOM   1216  NE2 GLN A 162      -9.316   8.859  35.167  1.00 34.06           N
ATOM   1217  N   PHE A 163     -11.914   4.361  32.480  1.00  7.29           N
ATOM   1218  CA  PHE A 163     -12.729   3.454  31.669  1.00  6.00           C
ATOM   1219  C   PHE A 163     -14.189   3.501  32.076  1.00  6.53           C
ATOM   1220  O   PHE A 163     -15.059   3.735  31.231  1.00  9.26           O
ATOM   1221  CB  PHE A 163     -12.241   1.995  31.786  1.00  5.49           C
ATOM   1222  CG  PHE A 163     -10.933   1.735  31.097  1.00  4.57           C
ATOM   1223  CD1 PHE A 163      -9.734   1.910  31.772  1.00  3.84           C
ATOM   1224  CD2 PHE A 163     -10.905   1.347  29.762  1.00  5.19           C
ATOM   1225  CE1 PHE A 163      -8.515   1.711  31.147  1.00  3.48           C
ATOM   1226  CE2 PHE A 163      -9.693   1.142  29.117  1.00  5.34           C
ATOM   1227  CZ  PHE A 163      -8.493   1.324  29.813  1.00  4.92           C
ATOM   1228  N   VAL A 164     -14.462   3.373  33.373  1.00  5.36           N
ATOM   1229  CA  VAL A 164     -15.852   3.305  33.832  1.00  4.91           C
ATOM   1230  C   VAL A 164     -16.666   4.596  33.859  1.00  6.69           C
ATOM   1231  O   VAL A 164     -17.903   4.559  34.007  1.00  7.79           O
ATOM   1232  CB  VAL A 164     -15.991   2.505  35.192  1.00  4.56           C
ATOM   1233  CG1 VAL A 164     -15.435   1.095  35.033  1.00  4.45           C
ATOM   1234  CG2 VAL A 164     -15.256   3.202  36.317  1.00  4.82           C
ATOM   1235  N   THR A 165     -16.004   5.744  33.756  1.00  6.47           N
ATOM   1236  CA  THR A 165     -16.757   6.987  33.752  1.00  7.73           C
ATOM   1237  C   THR A 165     -17.426   7.201  32.403  1.00  9.14           C
ATOM   1238  O   THR A 165     -18.359   8.001  32.297  1.00  8.73           O
ATOM   1239  CB  THR A 165     -15.871   8.232  34.064  1.00 10.30           C
ATOM   1240  OG1 THR A 165     -14.673   8.173  33.296  1.00 22.16           O
ATOM   1241  CG2 THR A 165     -15.514   8.288  35.529  1.00  8.39           C
ATOM   1242  N   LYS A 166     -16.960   6.491  31.378  1.00  9.22           N
ATOM   1243  CA  LYS A 166     -17.518   6.620  30.025  1.00  8.55           C
ATOM   1244  C   LYS A 166     -18.918   5.980  29.954  1.00  8.00           C
ATOM   1245  O   LYS A 166     -19.143   4.869  30.451  1.00  6.86           O
ATOM   1246  CB  LYS A 166     -16.575   5.978  28.985  1.00  5.78           C
ATOM   1247  CG  LYS A 166     -15.187   6.675  28.850  1.00  6.65           C
ATOM   1248  CD  LYS A 166     -14.418   6.149  27.621  1.00  7.58           C
ATOM   1249  CE  LYS A 166     -13.040   6.812  27.452  1.00  4.92           C
ATOM   1250  NZ  LYS A 166     -12.318   6.263  26.281  1.00  7.78           N
ATOM   1251  N   GLU A 167     -19.842   6.662  29.287  1.00  8.86           N
ATOM   1252  CA  GLU A 167     -21.217   6.172  29.188  1.00  8.52           C
ATOM   1253  C   GLU A 167     -21.394   4.837  28.464  1.00  7.53           C
ATOM   1254  O   GLU A 167     -22.303   4.089  28.782  1.00  8.41           O
ATOM   1255  CB  GLU A 167     -22.126   7.247  28.572  1.00 12.16           C
ATOM   1256  CG  GLU A 167     -22.097   8.603  29.302  1.00 17.56           C
ATOM   1257  CD  GLU A 167     -22.743   8.595  30.692  1.00 30.71           C
ATOM   1258  OE1 GLU A 167     -23.637   7.770  30.958  1.00 24.79           O
ATOM   1259  OE2 GLU A 167     -22.360   9.442  31.532  1.00 34.59           O
ATOM   1260  N   ASN A 168     -20.522   4.491  27.530  1.00  7.54           N
ATOM   1261  CA  ASN A 168     -20.706   3.214  26.829  1.00  8.20           C
ATOM   1262  C   ASN A 168     -19.938   2.024  27.415  1.00  9.09           C
ATOM   1263  O   ASN A 168     -19.841   0.959  26.794  1.00 10.68           O
ATOM   1264  CB  ASN A 168     -20.420   3.365  25.332  1.00  6.71           C
ATOM   1265  CG  ASN A 168     -21.466   4.230  24.623  1.00 20.99           C
ATOM   1266  OD1 ASN A 168     -22.606   4.335  25.074  1.00 19.59           O
ATOM   1267  ND2 ASN A 168     -21.069   4.874  23.530  1.00 29.07           N
ATOM   1268  N   CYS A 169     -19.443   2.188  28.638  1.00  8.51           N
ATOM   1269  CA  CYS A 169     -18.684   1.129  29.280  1.00  8.83           C
ATOM   1270  C   CYS A 169     -19.533   0.392  30.295  1.00  8.71           C
ATOM   1271  O   CYS A 169     -20.039   1.019  31.235  1.00  9.79           O
ATOM   1272  CB  CYS A 169     -17.466   1.715  29.987  1.00  9.46           C
ATOM   1273  SG  CYS A 169     -16.359   0.444  30.698  1.00 10.55           S
ATOM   1274  N   LEU A 170     -19.811  -0.887  30.054  1.00  5.84           N
ATOM   1275  CA  LEU A 170     -20.560  -1.653  31.050  1.00  6.19           C
ATOM   1276  C   LEU A 170     -19.576  -1.980  32.181  1.00  7.30           C
ATOM   1277  O   LEU A 170     -18.354  -2.132  31.954  1.00  7.13           O
ATOM   1278  CB  LEU A 170     -21.146  -2.940  30.478  1.00  6.66           C
ATOM   1279  CG  LEU A 170     -22.341  -2.831  29.535  1.00 11.22           C
ATOM   1280  CD1 LEU A 170     -23.171  -4.106  29.649  1.00 15.13           C
ATOM   1281  CD2 LEU A 170     -23.202  -1.656  29.880  1.00 12.38           C
ATOM   1282  N   ILE A 171     -20.107  -2.094  33.387  1.00  8.14           N
ATOM   1283  CA  ILE A 171     -19.313  -2.339  34.574  1.00  7.76           C
ATOM   1284  C   ILE A 171     -19.576  -3.726  35.179  1.00  9.56           C
ATOM   1285  O   ILE A 171     -20.681  -4.021  35.664  1.00 10.21           O
ATOM   1286  CB  ILE A 171     -19.615  -1.272  35.630  1.00  6.69           C
ATOM   1287  CG1 ILE A 171     -19.451   0.116  35.030  1.00  3.41           C
ATOM   1288  CG2 ILE A 171     -18.676  -1.421  36.828  1.00  5.97           C
ATOM   1289  CD1 ILE A 171     -19.963   1.222  35.946  1.00  9.96           C
ATOM   1290  N   LEU A 172     -18.557  -4.574  35.129  1.00  9.00           N
ATOM   1291  CA  LEU A 172     -18.653  -5.896  35.689  1.00  9.27           C
ATOM   1292  C   LEU A 172     -18.095  -5.765  37.098  1.00  8.53           C
ATOM   1293  O   LEU A 172     -16.865  -5.704  37.277  1.00  9.32           O
ATOM   1294  CB  LEU A 172     -17.820  -6.855  34.843  1.00  9.86           C
ATOM   1295  CG  LEU A 172     -18.052  -8.355  35.033  1.00 12.78           C
ATOM   1296  CD1 LEU A 172     -19.552  -8.654  34.974  1.00 14.88           C
ATOM   1297  CD2 LEU A 172     -17.321  -9.085  33.910  1.00 10.63           C
ATOM   1298  N   ALA A 173     -19.001  -5.648  38.078  1.00  7.00           N
ATOM   1299  CA  ALA A 173     -18.635  -5.467  39.486  1.00  4.98           C
ATOM   1300  C   ALA A 173     -18.363  -6.799  40.147  1.00  3.76           C
ATOM   1301  O   ALA A 173     -19.291  -7.520  40.541  1.00  3.39           O
ATOM   1302  CB  ALA A 173     -19.728  -4.729  40.228  1.00  4.58           C
ATOM   1303  N   VAL A 174     -17.082  -7.088  40.333  1.00  3.50           N
ATOM   1304  CA  VAL A 174     -16.676  -8.372  40.896  1.00  3.86           C
ATOM   1305  C   VAL A 174     -16.391  -8.344  42.398  1.00  5.78           C
ATOM   1306  O   VAL A 174     -15.531  -7.571  42.833  1.00  6.13           O
ATOM   1307  CB  VAL A 174     -15.421  -8.874  40.163  1.00  3.64           C
ATOM   1308  CG1 VAL A 174     -14.978 -10.246  40.709  1.00  4.29           C
ATOM   1309  CG2 VAL A 174     -15.694  -8.976  38.687  1.00  3.11           C
ATOM   1310  N   SER A 175     -17.121  -9.161  43.171  1.00  6.79           N
ATOM   1311  CA  SER A 175     -16.902  -9.287  44.627  1.00  6.38           C
ATOM   1312  C   SER A 175     -16.716 -10.779  45.041  1.00  5.29           C
ATOM   1313  O   SER A 175     -17.524 -11.646  44.647  1.00  6.88           O
ATOM   1314  CB  SER A 175     -18.075  -8.702  45.446  1.00  5.64           C
ATOM   1315  OG  SER A 175     -18.383  -7.358  45.069  1.00 10.55           O
ATOM   1316  N   PRO A 176     -15.718 -11.071  45.903  1.00  3.02           N
ATOM   1317  CA  PRO A 176     -15.468 -12.449  46.357  1.00  3.25           C
ATOM   1318  C   PRO A 176     -16.463 -12.827  47.463  1.00  4.52           C
ATOM   1319  O   PRO A 176     -16.702 -12.046  48.379  1.00  6.47           O
ATOM   1320  CB  PRO A 176     -14.040 -12.383  46.881  1.00  2.59           C
ATOM   1321  CG  PRO A 176     -13.964 -10.961  47.492  1.00  4.33           C
ATOM   1322  CD  PRO A 176     -14.796 -10.107  46.538  1.00  4.15           C
ATOM   1323  N   ALA A 177     -17.031 -14.026  47.393  1.00  4.42           N
ATOM   1324  CA  ALA A 177     -18.030 -14.445  48.397  1.00  4.99           C
ATOM   1325  C   ALA A 177     -17.471 -14.585  49.817  1.00  4.34           C
ATOM   1326  O   ALA A 177     -18.229 -14.599  50.776  1.00  3.87           O
ATOM   1327  CB  ALA A 177     -18.691 -15.782  47.982  1.00  4.19           C
ATOM   1328  N   ASN A 178     -16.164 -14.767  49.939  1.00  5.75           N
ATOM   1329  CA  ASN A 178     -15.560 -14.946  51.254  1.00  8.42           C
ATOM   1330  C   ASN A 178     -15.240 -13.645  52.009  1.00  6.69           C
ATOM   1331  O   ASN A 178     -14.387 -13.628  52.902  1.00  5.02           O
ATOM   1332  CB  ASN A 178     -14.345 -15.893  51.182  1.00  2.54           C
ATOM   1333  CG  ASN A 178     -13.301 -15.424  50.213  1.00  6.00           C
ATOM   1334  OD1 ASN A 178     -13.449 -14.376  49.543  1.00  4.60           O
ATOM   1335  ND2 ASN A 178     -12.220 -16.182  50.127  1.00  2.25           N
ATOM   1336  N   SER A 179     -15.891 -12.553  51.604  1.00  6.49           N
ATOM   1337  CA  SER A 179     -15.774 -11.258  52.298  1.00  7.19           C
ATOM   1338  C   SER A 179     -17.219 -10.740  52.320  1.00  6.35           C
ATOM   1339  O   SER A 179     -17.983 -11.010  51.396  1.00  6.54           O
ATOM   1340  CB  SER A 179     -14.899 -10.261  51.524  1.00 10.85           C
ATOM   1341  OG  SER A 179     -14.776  -9.031  52.233  1.00 14.17           O
ATOM   1342  N   ASP A 180     -17.627 -10.076  53.393  1.00  6.70           N
ATOM   1343  CA  ASP A 180     -18.990  -9.557  53.434  1.00  7.64           C
ATOM   1344  C   ASP A 180     -19.166  -8.618  52.227  1.00  7.78           C
ATOM   1345  O   ASP A 180     -18.246  -7.864  51.881  1.00  8.12           O
ATOM   1346  CB  ASP A 180     -19.242  -8.785  54.738  1.00  6.99           C
ATOM   1347  CG  ASP A 180     -19.582  -9.696  55.930  1.00 11.35           C
ATOM   1348  OD1 ASP A 180     -20.025  -9.158  56.961  1.00 15.87           O
ATOM   1349  OD2 ASP A 180     -19.392 -10.922  55.872  1.00 12.20           O
ATOM   1350  N   LEU A 181     -20.309  -8.704  51.557  1.00  6.69           N
ATOM   1351  CA  LEU A 181     -20.592  -7.836  50.415  1.00  7.23           C
ATOM   1352  C   LEU A 181     -20.449  -6.335  50.797  1.00  6.87           C
ATOM   1353  O   LEU A 181     -20.076  -5.504  49.969  1.00  6.40           O
ATOM   1354  CB  LEU A 181     -22.021  -8.106  49.881  1.00  7.12           C
ATOM   1355  CG  LEU A 181     -22.378  -7.491  48.524  1.00  6.61           C
ATOM   1356  CD1 LEU A 181     -21.548  -8.129  47.407  1.00  5.21           C
ATOM   1357  CD2 LEU A 181     -23.855  -7.684  48.240  1.00  5.84           C
ATOM   1358  N   ALA A 182     -20.730  -5.994  52.049  1.00  4.95           N
ATOM   1359  CA  ALA A 182     -20.609  -4.601  52.492  1.00  5.46           C
ATOM   1360  C   ALA A 182     -19.173  -4.065  52.312  1.00  7.55           C
ATOM   1361  O   ALA A 182     -18.958  -2.843  52.269  1.00  8.41           O
ATOM   1362  CB  ALA A 182     -21.041  -4.465  53.951  1.00  5.18           C
ATOM   1363  N   ASN A 183     -18.213  -4.987  52.171  1.00  7.88           N
ATOM   1364  CA  ASN A 183     -16.797  -4.655  51.987  1.00  6.84           C
ATOM   1365  C   ASN A 183     -16.403  -4.466  50.534  1.00  5.49           C
ATOM   1366  O   ASN A 183     -15.227  -4.208  50.231  1.00  2.06           O
ATOM   1367  CB  ASN A 183     -15.918  -5.792  52.512  1.00  9.19           C
ATOM   1368  CG  ASN A 183     -15.889  -5.853  54.000  1.00 10.57           C
ATOM   1369  OD1 ASN A 183     -16.012  -4.832  54.670  1.00 11.36           O
ATOM   1370  ND2 ASN A 183     -15.714  -7.056  54.541  1.00 18.36           N
ATOM   1371  N   SER A 184     -17.371  -4.578  49.630  1.00  7.69           N
ATOM   1372  CA  SER A 184     -17.062  -4.496  48.200  1.00  9.08           C
ATOM   1373  C   SER A 184     -16.529  -3.197  47.583  1.00  8.43           C
ATOM   1374  O   SER A 184     -17.280  -2.238  47.404  1.00  7.63           O
ATOM   1375  CB  SER A 184     -18.280  -4.938  47.373  1.00  6.94           C
ATOM   1376  OG  SER A 184     -17.932  -4.983  45.998  1.00  7.96           O
ATOM   1377  N   ASP A 185     -15.272  -3.228  47.144  1.00  7.35           N
ATOM   1378  CA  ASP A 185     -14.653  -2.097  46.453  1.00  7.72           C
ATOM   1379  C   ASP A 185     -15.408  -1.912  45.112  1.00  7.80           C
ATOM   1380  O   ASP A 185     -15.601  -0.780  44.626  1.00  7.76           O
ATOM   1381  CB  ASP A 185     -13.192  -2.426  46.112  1.00 12.41           C
ATOM   1382  CG  ASP A 185     -12.386  -2.888  47.332  1.00 23.86           C
ATOM   1383  OD1 ASP A 185     -11.545  -2.100  47.795  1.00 24.25           O
ATOM   1384  OD2 ASP A 185     -12.604  -4.019  47.824  1.00 26.87           O
ATOM   1385  N   ALA A 186     -15.774  -3.033  44.497  1.00  7.36           N
ATOM   1386  CA  ALA A 186     -16.480  -3.032  43.210  1.00  6.09           C
ATOM   1387  C   ALA A 186     -17.798  -2.293  43.277  1.00  6.54           C
ATOM   1388  O   ALA A 186     -18.067  -1.391  42.468  1.00  8.65           O
ATOM   1389  CB  ALA A 186     -16.728  -4.474  42.758  1.00  5.59           C
ATOM   1390  N   LEU A 187     -18.626  -2.666  44.241  1.00  5.26           N
ATOM   1391  CA  LEU A 187     -19.931  -2.041  44.356  1.00  4.83           C
ATOM   1392  C   LEU A 187     -19.843  -0.554  44.696  1.00  4.57           C
ATOM   1393  O   LEU A 187     -20.662   0.241  44.246  1.00  4.35           O
ATOM   1394  CB  LEU A 187     -20.771  -2.808  45.375  1.00  4.57           C
ATOM   1395  CG  LEU A 187     -21.125  -4.224  44.863  1.00  5.27           C
ATOM   1396  CD1 LEU A 187     -21.996  -4.937  45.887  1.00  6.98           C
ATOM   1397  CD2 LEU A 187     -21.883  -4.139  43.539  1.00  1.03           C
ATOM   1398  N   LYS A 188     -18.863  -0.176  45.507  1.00  4.95           N
ATOM   1399  CA  LYS A 188     -18.717   1.227  45.857  1.00  3.99           C
ATOM   1400  C   LYS A 188     -18.398   2.067  44.631  1.00  6.47           C
ATOM   1401  O   LYS A 188     -19.064   3.102  44.389  1.00  8.72           O
ATOM   1402  CB  LYS A 188     -17.620   1.431  46.911  1.00  1.00           C
ATOM   1403  CG  LYS A 188     -17.451   2.894  47.304  1.00  2.59           C
ATOM   1404  CD  LYS A 188     -16.208   3.118  48.193  1.00  5.71           C
ATOM   1405  CE  LYS A 188     -16.081   4.612  48.530  1.00  9.67           C
ATOM   1406  NZ  LYS A 188     -15.015   4.873  49.525  1.00  6.51           N
ATOM   1407  N   VAL A 189     -17.382   1.666  43.859  1.00  7.84           N
ATOM   1408  CA  VAL A 189     -17.053   2.453  42.672  1.00  8.84           C
ATOM   1409  C   VAL A 189     -18.204   2.396  41.655  1.00  8.16           C
ATOM   1410  O   VAL A 189     -18.523   3.405  41.028  1.00  7.70           O
ATOM   1411  CB  VAL A 189     -15.717   2.038  41.952  1.00 12.00           C
ATOM   1412  CG1 VAL A 189     -14.533   1.971  42.899  1.00 16.60           C
ATOM   1413  CG2 VAL A 189     -15.879   0.755  41.165  1.00 11.02           C
ATOM   1414  N   ALA A 190     -18.834   1.231  41.489  1.00  8.47           N
ATOM   1415  CA  ALA A 190     -19.943   1.117  40.525  1.00  8.92           C
ATOM   1416  C   ALA A 190     -21.072   2.068  40.899  1.00  8.90           C
ATOM   1417  O   ALA A 190     -21.632   2.757  40.046  1.00 10.52           O
ATOM   1418  CB  ALA A 190     -20.478  -0.341  40.442  1.00  8.61           C
ATOM   1419  N   LYS A 191     -21.395   2.127  42.184  1.00  8.85           N
ATOM   1420  CA  LYS A 191     -22.461   3.012  42.628  1.00  8.42           C
ATOM   1421  C   LYS A 191     -22.063   4.480  42.491  1.00  9.01           C
ATOM   1422  O   LYS A 191     -22.907   5.343  42.236  1.00 10.51           O
ATOM   1423  CB  LYS A 191     -22.910   2.664  44.053  1.00 11.96           C
ATOM   1424  CG  LYS A 191     -23.663   1.337  44.097  1.00 24.11           C
ATOM   1425  CD  LYS A 191     -24.102   0.948  45.489  1.00 34.25           C
ATOM   1426  CE  LYS A 191     -25.104  -0.185  45.429  1.00 45.24           C
ATOM   1427  NZ  LYS A 191     -26.403   0.212  44.800  1.00 51.15           N
ATOM   1428  N   GLU A 192     -20.770   4.759  42.565  1.00  8.96           N
ATOM   1429  CA  GLU A 192     -20.320   6.139  42.412  1.00 10.17           C
ATOM   1430  C   GLU A 192     -20.472   6.657  40.978  1.00 11.32           C
ATOM   1431  O   GLU A 192     -20.964   7.773  40.775  1.00 12.21           O
ATOM   1432  CB  GLU A 192     -18.871   6.289  42.886  1.00 11.83           C
ATOM   1433  CG  GLU A 192     -18.724   6.309  44.421  1.00 11.54           C
ATOM   1434  CD  GLU A 192     -17.274   6.308  44.861  1.00 17.78           C
ATOM   1435  OE1 GLU A 192     -16.483   5.493  44.326  1.00 20.32           O
ATOM   1436  OE2 GLU A 192     -16.927   7.136  45.724  1.00 15.13           O
ATOM   1437  N   VAL A 193     -20.142   5.834  39.977  1.00  9.98           N
ATOM   1438  CA  VAL A 193     -20.242   6.289  38.589  1.00  9.45           C
ATOM   1439  C   VAL A 193     -21.586   5.950  37.921  1.00 10.54           C
ATOM   1440  O   VAL A 193     -22.012   6.625  36.982  1.00 11.91           O
ATOM   1441  CB  VAL A 193     -19.055   5.755  37.704  1.00  8.75           C
ATOM   1442  CG1 VAL A 193     -17.687   5.993  38.396  1.00  8.82           C
ATOM   1443  CG2 VAL A 193     -19.228   4.299  37.411  1.00  8.03           C
ATOM   1444  N   ASP A 194     -22.278   4.944  38.452  1.00  9.51           N
ATOM   1445  CA  ASP A 194     -23.560   4.488  37.897  1.00  9.00           C
ATOM   1446  C   ASP A 194     -24.513   4.259  39.079  1.00  9.95           C
ATOM   1447  O   ASP A 194     -24.963   3.154  39.303  1.00  9.63           O
ATOM   1448  CB  ASP A 194     -23.299   3.181  37.098  1.00  6.20           C
ATOM   1449  CG  ASP A 194     -24.572   2.544  36.525  1.00  9.30           C
ATOM   1450  OD1 ASP A 194     -25.522   3.292  36.217  1.00  7.45           O
ATOM   1451  OD2 ASP A 194     -24.621   1.290  36.372  1.00  7.96           O
ATOM   1452  N   PRO A 195     -24.924   5.338  39.769  1.00 11.76           N
ATOM   1453  CA  PRO A 195     -25.820   5.220  40.930  1.00 13.19           C
ATOM   1454  C   PRO A 195     -27.095   4.409  40.729  1.00 14.23           C
ATOM   1455  O   PRO A 195     -27.406   3.550  41.567  1.00 14.96           O
ATOM   1456  CB  PRO A 195     -26.093   6.683  41.334  1.00 13.03           C
ATOM   1457  CG  PRO A 195     -25.917   7.433  40.070  1.00 14.00           C
ATOM   1458  CD  PRO A 195     -24.713   6.751  39.413  1.00 13.26           C
ATOM   1459  N   GLN A 196     -27.758   4.596  39.589  1.00 12.77           N
ATOM   1460  CA  GLN A 196     -28.995   3.871  39.282  1.00 13.96           C
ATOM   1461  C   GLN A 196     -28.758   2.440  38.764  1.00 14.51           C
ATOM   1462  O   GLN A 196     -29.716   1.719  38.434  1.00 14.23           O
ATOM   1463  CB  GLN A 196     -29.847   4.663  38.280  1.00 19.99           C
ATOM   1464  CG  GLN A 196     -30.154   6.093  38.714  1.00 34.57           C
ATOM   1465  CD  GLN A 196     -30.978   6.162  39.989  1.00 52.02           C
ATOM   1466  OE1 GLN A 196     -30.535   5.742  41.057  1.00 52.31           O
ATOM   1467  NE2 GLN A 196     -32.180   6.715  39.884  1.00 64.69           N
ATOM   1468  N   GLY A 197     -27.491   2.038  38.662  1.00 12.97           N
ATOM   1469  CA  GLY A 197     -27.172   0.693  38.219  1.00 11.17           C
ATOM   1470  C   GLY A 197     -27.594   0.338  36.804  1.00 12.47           C
ATOM   1471  O   GLY A 197     -27.714  -0.849  36.480  1.00 13.43           O
ATOM   1472  N   GLN A 198     -27.772   1.349  35.952  1.00 11.66           N
ATOM   1473  CA  GLN A 198     -28.186   1.129  34.567  1.00 10.51           C
ATOM   1474  C   GLN A 198     -27.220   0.284  33.720  1.00  9.16           C
ATOM   1475  O   GLN A 198     -27.660  -0.397  32.794  1.00 10.88           O
ATOM   1476  CB  GLN A 198     -28.440   2.472  33.862  1.00 16.27           C
ATOM   1477  CG  GLN A 198     -29.761   3.155  34.235  1.00 32.97           C
ATOM   1478  CD  GLN A 198     -30.970   2.458  33.622  1.00 45.74           C
ATOM   1479  OE1 GLN A 198     -30.831   1.436  32.948  1.00 42.30           O
ATOM   1480  NE2 GLN A 198     -32.159   3.016  33.841  1.00 49.46           N
ATOM   1481  N   ARG A 199     -25.921   0.338  34.027  1.00  5.08           N
ATOM   1482  CA  ARG A 199     -24.912  -0.408  33.279  1.00  4.80           C
ATOM   1483  C   ARG A 199     -23.960  -1.224  34.180  1.00  7.78           C
ATOM   1484  O   ARG A 199     -22.795  -1.430  33.832  1.00  8.23           O
ATOM   1485  CB  ARG A 199     -24.102   0.559  32.389  1.00  2.44           C
ATOM   1486  CG  ARG A 199     -23.423   1.730  33.125  1.00  3.66           C
ATOM   1487  CD  ARG A 199     -22.886   2.798  32.128  1.00  5.95           C
ATOM   1488  NE  ARG A 199     -22.405   4.003  32.813  1.00  9.44           N
ATOM   1489  CZ  ARG A 199     -21.145   4.199  33.208  1.00  9.38           C
ATOM   1490  NH1 ARG A 199     -20.217   3.281  32.981  1.00  6.59           N
ATOM   1491  NH2 ARG A 199     -20.818   5.298  33.876  1.00  5.16           N
ATOM   1492  N   THR A 200     -24.465  -1.704  35.313  1.00  8.27           N
ATOM   1493  CA  THR A 200     -23.651  -2.470  36.269  1.00  9.30           C
ATOM   1494  C   THR A 200     -24.175  -3.902  36.439  1.00  9.77           C
ATOM   1495  O   THR A 200     -25.361  -4.084  36.697  1.00 10.31           O
ATOM   1496  CB  THR A 200     -23.709  -1.819  37.706  1.00  7.58           C
ATOM   1497  OG1 THR A 200     -23.085  -0.536  37.698  1.00  8.42           O
ATOM   1498  CG2 THR A 200     -23.012  -2.692  38.748  1.00  5.89           C
ATOM   1499  N   ILE A 201     -23.296  -4.897  36.320  1.00  8.50           N
ATOM   1500  CA  ILE A 201     -23.679  -6.291  36.540  1.00  8.72           C
ATOM   1501  C   ILE A 201     -22.792  -6.854  37.662  1.00  8.83           C
ATOM   1502  O   ILE A 201     -21.554  -6.747  37.617  1.00  7.60           O
ATOM   1503  CB  ILE A 201     -23.555  -7.154  35.250  1.00  8.78           C
ATOM   1504  CG1 ILE A 201     -24.442  -6.545  34.150  1.00 11.31           C
ATOM   1505  CG2 ILE A 201     -24.016  -8.614  35.534  1.00  8.06           C
ATOM   1506  CD1 ILE A 201     -24.468  -7.362  32.894  1.00 22.29           C
ATOM   1507  N   GLY A 202     -23.434  -7.394  38.694  1.00  9.51           N
ATOM   1508  CA  GLY A 202     -22.705  -7.921  39.834  1.00  9.29           C
ATOM   1509  C   GLY A 202     -22.346  -9.378  39.654  1.00  9.39           C
ATOM   1510  O   GLY A 202     -23.153 -10.160  39.122  1.00 10.10           O
ATOM   1511  N   VAL A 203     -21.110  -9.714  40.011  1.00  7.64           N
ATOM   1512  CA  VAL A 203     -20.592 -11.066  39.929  1.00  7.85           C
ATOM   1513  C   VAL A 203     -20.000 -11.402  41.288  1.00  8.57           C
ATOM   1514  O   VAL A 203     -19.233 -10.596  41.856  1.00  9.07           O
ATOM   1515  CB  VAL A 203     -19.484 -11.200  38.887  1.00  7.48           C
ATOM   1516  CG1 VAL A 203     -18.910 -12.646  38.909  1.00  7.41           C
ATOM   1517  CG2 VAL A 203     -20.040 -10.890  37.515  1.00  8.45           C
ATOM   1518  N   ILE A 204     -20.329 -12.586  41.798  1.00  8.40           N
ATOM   1519  CA  ILE A 204     -19.841 -13.016  43.115  1.00  7.49           C
ATOM   1520  C   ILE A 204     -18.994 -14.248  42.845  1.00  6.31           C
ATOM   1521  O   ILE A 204     -19.506 -15.258  42.322  1.00  7.36           O
ATOM   1522  CB  ILE A 204     -21.012 -13.406  44.046  1.00  7.76           C
ATOM   1523  CG1 ILE A 204     -21.933 -12.195  44.332  1.00  4.74           C
ATOM   1524  CG2 ILE A 204     -20.480 -14.039  45.337  1.00  8.40           C
ATOM   1525  CD1 ILE A 204     -21.267 -11.026  45.050  1.00  4.86           C
ATOM   1526  N   THR A 205     -17.697 -14.139  43.104  1.00  3.15           N
ATOM   1527  CA  THR A 205     -16.773 -15.243  42.861  1.00  5.43           C
ATOM   1528  C   THR A 205     -16.470 -15.988  44.169  1.00  6.67           C
ATOM   1529  O   THR A 205     -16.982 -15.646  45.243  1.00  6.98           O
ATOM   1530  CB  THR A 205     -15.416 -14.677  42.371  1.00  6.80           C
ATOM   1531  OG1 THR A 205     -14.898 -13.801  43.379  1.00  4.38           O
ATOM   1532  CG2 THR A 205     -15.580 -13.861  41.043  1.00  6.89           C
ATOM   1533  N   LYS A 206     -15.619 -17.004  44.067  1.00  5.81           N
ATOM   1534  CA  LYS A 206     -15.161 -17.729  45.234  1.00  6.01           C
ATOM   1535  C   LYS A 206     -16.239 -18.279  46.167  1.00  6.91           C
ATOM   1536  O   LYS A 206     -16.008 -18.397  47.371  1.00  7.23           O
ATOM   1537  CB  LYS A 206     -14.195 -16.821  46.021  1.00  1.00           C
ATOM   1538  CG  LYS A 206     -12.954 -16.417  45.218  1.00  1.00           C
ATOM   1539  CD  LYS A 206     -11.962 -15.603  46.031  1.00  1.00           C
ATOM   1540  CE  LYS A 206     -10.699 -15.319  45.204  1.00  8.72           C
ATOM   1541  NZ  LYS A 206      -9.638 -14.640  46.030  1.00 18.94           N
ATOM   1542  N   LEU A 207     -17.392 -18.656  45.621  1.00  6.43           N
ATOM   1543  CA  LEU A 207     -18.455 -19.210  46.477  1.00  5.85           C
ATOM   1544  C   LEU A 207     -18.013 -20.525  47.143  1.00  5.51           C
ATOM   1545  O   LEU A 207     -18.498 -20.890  48.219  1.00  7.41           O
ATOM   1546  CB  LEU A 207     -19.748 -19.404  45.667  1.00  6.30           C
ATOM   1547  CG  LEU A 207     -20.402 -18.044  45.397  1.00  3.08           C
ATOM   1548  CD1 LEU A 207     -21.086 -17.970  44.022  1.00  1.09           C
ATOM   1549  CD2 LEU A 207     -21.363 -17.736  46.530  1.00  3.09           C
ATOM   1550  N   ASP A 208     -17.053 -21.209  46.532  1.00  4.89           N
ATOM   1551  CA  ASP A 208     -16.537 -22.450  47.078  1.00  3.89           C
ATOM   1552  C   ASP A 208     -15.621 -22.239  48.307  1.00  5.69           C
ATOM   1553  O   ASP A 208     -15.270 -23.209  48.989  1.00  6.06           O
ATOM   1554  CB  ASP A 208     -15.782 -23.248  45.998  1.00  3.88           C
ATOM   1555  CG  ASP A 208     -14.609 -22.466  45.387  1.00  6.60           C
ATOM   1556  OD1 ASP A 208     -13.532 -23.053  45.170  1.00  4.64           O
ATOM   1557  OD2 ASP A 208     -14.769 -21.258  45.139  1.00  9.39           O
ATOM   1558  N   LEU A 209     -15.287 -20.984  48.609  1.00  5.44           N
ATOM   1559  CA  LEU A 209     -14.380 -20.652  49.723  1.00  4.70           C
ATOM   1560  C   LEU A 209     -15.043 -20.145  50.997  1.00  6.90           C
ATOM   1561  O   LEU A 209     -14.358 -19.873  51.988  1.00  8.32           O
ATOM   1562  CB  LEU A 209     -13.349 -19.600  49.276  1.00  3.27           C
ATOM   1563  CG  LEU A 209     -12.477 -20.028  48.098  1.00  1.00           C
ATOM   1564  CD1 LEU A 209     -11.405 -18.976  47.859  1.00  1.00           C
ATOM   1565  CD2 LEU A 209     -11.851 -21.369  48.428  1.00  2.87           C
HETATM 1566  N   MSE A 210     -16.365 -20.049  51.002  1.00  5.98           N
HETATM 1567  CA  MSE A 210     -17.027 -19.562  52.188  1.00  6.72           C
HETATM 1568  C   MSE A 210     -16.871 -20.474  53.393  1.00  6.46           C
HETATM 1569  O   MSE A 210     -16.797 -21.695  53.285  1.00  5.42           O
HETATM 1570  CB  MSE A 210     -18.511 -19.297  51.925  1.00  8.41           C
HETATM 1571  CG  MSE A 210     -18.761 -18.286  50.833  1.00 10.42           C
HETATM 1572 SE   MSE A 210     -20.656 -17.802  50.714  1.00 13.28          Se
HETATM 1573  CE  MSE A 210     -20.742 -16.641  52.278  1.00 11.01           C
ATOM   1574  N   ASP A 211     -16.836 -19.830  54.545  1.00  7.12           N
ATOM   1575  CA  ASP A 211     -16.712 -20.483  55.834  1.00  7.33           C
ATOM   1576  C   ASP A 211     -17.867 -21.482  56.009  1.00  9.07           C
ATOM   1577  O   ASP A 211     -19.003 -21.186  55.640  1.00  9.67           O
ATOM   1578  CB  ASP A 211     -16.805 -19.395  56.907  1.00  5.38           C
ATOM   1579  CG  ASP A 211     -16.521 -19.909  58.319  1.00 10.92           C
ATOM   1580  OD1 ASP A 211     -17.187 -19.418  59.273  1.00 14.56           O
ATOM   1581  OD2 ASP A 211     -15.609 -20.747  58.488  1.00 13.84           O
ATOM   1582  N   GLU A 212     -17.590 -22.651  56.571  1.00  8.48           N
ATOM   1583  CA  GLU A 212     -18.665 -23.614  56.802  1.00  8.48           C
ATOM   1584  C   GLU A 212     -19.714 -23.011  57.735  1.00  8.69           C
ATOM   1585  O   GLU A 212     -19.392 -22.316  58.719  1.00  8.67           O
ATOM   1586  CB  GLU A 212     -18.116 -24.900  57.408  1.00 11.19           C
ATOM   1587  CG  GLU A 212     -17.258 -25.679  56.440  1.00 29.99           C
ATOM   1588  CD  GLU A 212     -16.774 -26.995  57.009  1.00 49.93           C
ATOM   1589  OE1 GLU A 212     -16.456 -27.045  58.219  1.00 49.32           O
ATOM   1590  OE2 GLU A 212     -16.696 -27.977  56.238  1.00 59.36           O
ATOM   1591  N   GLY A 213     -20.978 -23.279  57.435  1.00  8.43           N
ATOM   1592  CA  GLY A 213     -22.028 -22.737  58.261  1.00  6.25           C
ATOM   1593  C   GLY A 213     -22.536 -21.422  57.698  1.00 10.08           C
ATOM   1594  O   GLY A 213     -23.411 -20.817  58.302  1.00 10.44           O
ATOM   1595  N   THR A 214     -22.003 -20.976  56.551  1.00 10.56           N
ATOM   1596  CA  THR A 214     -22.462 -19.719  55.969  1.00 11.28           C
ATOM   1597  C   THR A 214     -22.744 -19.922  54.480  1.00 13.10           C
ATOM   1598  O   THR A 214     -22.356 -20.937  53.904  1.00 14.50           O
ATOM   1599  CB  THR A 214     -21.417 -18.579  56.116  1.00 12.43           C
ATOM   1600  OG1 THR A 214     -20.305 -18.817  55.240  1.00 17.09           O
ATOM   1601  CG2 THR A 214     -20.900 -18.487  57.542  1.00 13.41           C
ATOM   1602  N   ASP A 215     -23.449 -18.973  53.875  1.00 10.55           N
ATOM   1603  CA  ASP A 215     -23.752 -19.028  52.446  1.00  8.99           C
ATOM   1604  C   ASP A 215     -24.064 -17.607  51.999  1.00  8.10           C
ATOM   1605  O   ASP A 215     -24.338 -16.732  52.826  1.00  8.81           O
ATOM   1606  CB  ASP A 215     -24.946 -19.938  52.172  1.00  7.86           C
ATOM   1607  CG  ASP A 215     -26.240 -19.425  52.811  1.00 12.85           C
ATOM   1608  OD1 ASP A 215     -26.789 -18.420  52.333  1.00 13.10           O
ATOM   1609  OD2 ASP A 215     -26.712 -20.031  53.782  1.00 23.34           O
ATOM   1610  N   ALA A 216     -24.096 -17.404  50.693  1.00  6.45           N
ATOM   1611  CA  ALA A 216     -24.378 -16.091  50.120  1.00  4.26           C
ATOM   1612  C   ALA A 216     -25.775 -16.065  49.467  1.00  4.69           C
ATOM   1613  O   ALA A 216     -26.021 -15.318  48.515  1.00  4.96           O
ATOM   1614  CB  ALA A 216     -23.285 -15.726  49.105  1.00  3.22           C
ATOM   1615  N   ARG A 217     -26.706 -16.841  50.018  1.00  6.52           N
ATOM   1616  CA  ARG A 217     -28.051 -16.864  49.443  1.00  8.42           C
ATOM   1617  C   ARG A 217     -28.663 -15.468  49.358  1.00  9.88           C
ATOM   1618  O   ARG A 217     -29.196 -15.083  48.317  1.00 11.06           O
ATOM   1619  CB  ARG A 217     -29.000 -17.778  50.227  1.00  7.19           C
ATOM   1620  CG  ARG A 217     -30.400 -17.860  49.555  1.00  8.63           C
ATOM   1621  CD  ARG A 217     -31.280 -18.923  50.172  1.00 11.81           C
ATOM   1622  NE  ARG A 217     -31.616 -18.612  51.557  1.00 21.27           N
ATOM   1623  CZ  ARG A 217     -32.636 -17.844  51.937  1.00 28.68           C
ATOM   1624  NH1 ARG A 217     -33.443 -17.295  51.028  1.00 28.21           N
ATOM   1625  NH2 ARG A 217     -32.844 -17.613  53.233  1.00 24.02           N
ATOM   1626  N   ASP A 218     -28.597 -14.717  50.451  1.00 11.73           N
ATOM   1627  CA  ASP A 218     -29.172 -13.379  50.459  1.00 12.32           C
ATOM   1628  C   ASP A 218     -28.636 -12.502  49.336  1.00 10.81           C
ATOM   1629  O   ASP A 218     -29.410 -11.797  48.664  1.00 10.40           O
ATOM   1630  CB  ASP A 218     -28.979 -12.705  51.814  1.00 19.89           C
ATOM   1631  CG  ASP A 218     -29.740 -13.418  52.936  1.00 34.44           C
ATOM   1632  OD1 ASP A 218     -30.728 -14.128  52.637  1.00 35.98           O
ATOM   1633  OD2 ASP A 218     -29.348 -13.270  54.115  1.00 38.44           O
ATOM   1634  N   VAL A 219     -27.329 -12.550  49.089  1.00  9.53           N
ATOM   1635  CA  VAL A 219     -26.817 -11.703  48.028  1.00  9.48           C
ATOM   1636  C   VAL A 219     -27.188 -12.189  46.644  1.00 10.27           C
ATOM   1637  O   VAL A 219     -27.629 -11.384  45.821  1.00 12.43           O
ATOM   1638  CB  VAL A 219     -25.295 -11.365  48.128  1.00  9.57           C
ATOM   1639  CG1 VAL A 219     -24.641 -12.040  49.295  1.00  9.92           C
ATOM   1640  CG2 VAL A 219     -24.568 -11.616  46.789  1.00  8.55           C
ATOM   1641  N   LEU A 220     -27.112 -13.499  46.412  1.00  8.83           N
ATOM   1642  CA  LEU A 220     -27.418 -14.044  45.089  1.00  8.44           C
ATOM   1643  C   LEU A 220     -28.896 -13.911  44.711  1.00  9.06           C
ATOM   1644  O   LEU A 220     -29.241 -13.964  43.540  1.00  8.64           O
ATOM   1645  CB  LEU A 220     -26.950 -15.499  44.982  1.00  7.47           C
ATOM   1646  CG  LEU A 220     -25.439 -15.666  45.239  1.00  6.81           C
ATOM   1647  CD1 LEU A 220     -25.097 -17.121  45.215  1.00  7.80           C
ATOM   1648  CD2 LEU A 220     -24.636 -14.930  44.166  1.00  7.83           C
ATOM   1649  N   GLU A 221     -29.754 -13.766  45.712  1.00  9.40           N
ATOM   1650  CA  GLU A 221     -31.179 -13.583  45.478  1.00 10.94           C
ATOM   1651  C   GLU A 221     -31.488 -12.089  45.241  1.00 13.44           C
ATOM   1652  O   GLU A 221     -32.651 -11.693  45.175  1.00 14.66           O
ATOM   1653  CB  GLU A 221     -31.987 -14.110  46.665  1.00  9.16           C
ATOM   1654  CG  GLU A 221     -32.089 -15.647  46.675  1.00  5.07           C
ATOM   1655  CD  GLU A 221     -32.953 -16.199  47.784  1.00 10.64           C
ATOM   1656  OE1 GLU A 221     -33.340 -15.443  48.702  1.00 20.56           O
ATOM   1657  OE2 GLU A 221     -33.212 -17.422  47.762  1.00 20.49           O
ATOM   1658  N   ASN A 222     -30.436 -11.267  45.226  1.00 13.46           N
ATOM   1659  CA  ASN A 222     -30.550  -9.824  44.991  1.00 12.32           C
ATOM   1660  C   ASN A 222     -31.303  -9.138  46.138  1.00 13.93           C
ATOM   1661  O   ASN A 222     -31.956  -8.118  45.937  1.00 14.88           O
ATOM   1662  CB  ASN A 222     -31.244  -9.551  43.635  1.00 12.81           C
ATOM   1663  CG  ASN A 222     -30.877  -8.181  43.034  1.00 14.80           C
ATOM   1664  OD1 ASN A 222     -29.809  -7.644  43.309  1.00 11.03           O
ATOM   1665  ND2 ASN A 222     -31.756  -7.637  42.179  1.00 17.16           N
ATOM   1666  N   LYS A 223     -31.184  -9.690  47.345  1.00 14.07           N
ATOM   1667  CA  LYS A 223     -31.858  -9.159  48.528  1.00 14.17           C
ATOM   1668  C   LYS A 223     -30.994  -8.332  49.477  1.00 14.98           C
ATOM   1669  O   LYS A 223     -31.435  -7.288  49.981  1.00 15.06           O
ATOM   1670  CB  LYS A 223     -32.506 -10.307  49.315  1.00 13.09           C
ATOM   1671  CG  LYS A 223     -33.697 -10.916  48.587  1.00 24.50           C
ATOM   1672  CD  LYS A 223     -34.124 -12.249  49.186  1.00 36.22           C
ATOM   1673  CE  LYS A 223     -35.437 -12.738  48.567  1.00 49.64           C
ATOM   1674  NZ  LYS A 223     -35.711 -14.189  48.811  1.00 44.54           N
ATOM   1675  N   LEU A 224     -29.768  -8.788  49.726  1.00 14.68           N
ATOM   1676  CA  LEU A 224     -28.898  -8.080  50.644  1.00 14.95           C
ATOM   1677  C   LEU A 224     -28.640  -6.668  50.170  1.00 16.84           C
ATOM   1678  O   LEU A 224     -28.826  -5.729  50.925  1.00 18.97           O
ATOM   1679  CB  LEU A 224     -27.564  -8.811  50.846  1.00 14.59           C
ATOM   1680  CG  LEU A 224     -26.643  -8.107  51.855  1.00 13.27           C
ATOM   1681  CD1 LEU A 224     -27.354  -7.989  53.217  1.00 15.37           C
ATOM   1682  CD2 LEU A 224     -25.298  -8.851  51.988  1.00  9.02           C
ATOM   1683  N   LEU A 225     -28.158  -6.520  48.945  1.00 17.11           N
ATOM   1684  CA  LEU A 225     -27.879  -5.196  48.396  1.00 17.32           C
ATOM   1685  C   LEU A 225     -28.378  -5.293  46.970  1.00 18.11           C
ATOM   1686  O   LEU A 225     -27.649  -5.687  46.059  1.00 19.19           O
ATOM   1687  CB  LEU A 225     -26.376  -4.913  48.431  1.00 17.57           C
ATOM   1688  CG  LEU A 225     -25.985  -3.440  48.508  1.00 21.03           C
ATOM   1689  CD1 LEU A 225     -24.509  -3.332  48.838  1.00 24.35           C
ATOM   1690  CD2 LEU A 225     -26.306  -2.708  47.226  1.00 19.27           C
ATOM   1691  N   PRO A 226     -29.641  -4.929  46.753  1.00 17.53           N
ATOM   1692  CA  PRO A 226     -30.187  -5.021  45.396  1.00 16.85           C
ATOM   1693  C   PRO A 226     -29.474  -4.210  44.329  1.00 16.52           C
ATOM   1694  O   PRO A 226     -29.084  -3.058  44.564  1.00 16.66           O
ATOM   1695  CB  PRO A 226     -31.637  -4.569  45.582  1.00 16.64           C
ATOM   1696  CG  PRO A 226     -31.942  -4.987  46.981  1.00 17.19           C
ATOM   1697  CD  PRO A 226     -30.682  -4.540  47.714  1.00 16.70           C
ATOM   1698  N   LEU A 227     -29.323  -4.833  43.160  1.00 13.94           N
ATOM   1699  CA  LEU A 227     -28.708  -4.227  41.993  1.00 13.08           C
ATOM   1700  C   LEU A 227     -29.769  -4.327  40.901  1.00 13.36           C
ATOM   1701  O   LEU A 227     -30.420  -5.370  40.766  1.00 13.22           O
ATOM   1702  CB  LEU A 227     -27.489  -5.043  41.574  1.00 13.92           C
ATOM   1703  CG  LEU A 227     -26.157  -4.312  41.390  1.00 16.72           C
ATOM   1704  CD1 LEU A 227     -25.959  -3.260  42.464  1.00 18.43           C
ATOM   1705  CD2 LEU A 227     -25.000  -5.336  41.374  1.00 16.55           C
ATOM   1706  N   ARG A 228     -29.942  -3.258  40.120  1.00 12.62           N
ATOM   1707  CA  ARG A 228     -30.924  -3.255  39.043  1.00 12.19           C
ATOM   1708  C   ARG A 228     -30.795  -4.484  38.168  1.00 13.92           C
ATOM   1709  O   ARG A 228     -31.785  -5.155  37.884  1.00 12.65           O
ATOM   1710  CB  ARG A 228     -30.784  -2.008  38.169  1.00 13.44           C
ATOM   1711  CG  ARG A 228     -31.682  -2.038  36.931  1.00 18.91           C
ATOM   1712  CD  ARG A 228     -31.491  -0.824  36.037  1.00 27.08           C
ATOM   1713  NE  ARG A 228     -32.040   0.360  36.670  1.00 41.06           N
ATOM   1714  CZ  ARG A 228     -33.322   0.708  36.620  1.00 42.97           C
ATOM   1715  NH1 ARG A 228     -34.186  -0.032  35.942  1.00 35.48           N
ATOM   1716  NH2 ARG A 228     -33.755   1.744  37.329  1.00 44.05           N
ATOM   1717  N   ARG A 229     -29.563  -4.821  37.796  1.00 14.59           N
ATOM   1718  CA  ARG A 229     -29.318  -5.963  36.919  1.00 15.50           C
ATOM   1719  C   ARG A 229     -29.063  -7.285  37.639  1.00 16.36           C
ATOM   1720  O   ARG A 229     -28.867  -8.318  36.988  1.00 19.19           O
ATOM   1721  CB  ARG A 229     -28.157  -5.661  35.967  1.00 15.90           C
ATOM   1722  CG  ARG A 229     -28.339  -4.386  35.140  1.00 22.35           C
ATOM   1723  CD  ARG A 229     -29.536  -4.419  34.187  1.00 12.78           C
ATOM   1724  NE  ARG A 229     -29.520  -3.205  33.371  1.00 18.19           N
ATOM   1725  CZ  ARG A 229     -30.583  -2.613  32.829  1.00 24.76           C
ATOM   1726  NH1 ARG A 229     -31.809  -3.106  32.998  1.00 22.77           N
ATOM   1727  NH2 ARG A 229     -30.406  -1.507  32.109  1.00 20.97           N
ATOM   1728  N   GLY A 230     -29.022  -7.239  38.965  1.00 12.83           N
ATOM   1729  CA  GLY A 230     -28.827  -8.433  39.766  1.00 10.86           C
ATOM   1730  C   GLY A 230     -27.405  -8.932  39.923  1.00 10.81           C
ATOM   1731  O   GLY A 230     -26.446  -8.278  39.468  1.00 11.62           O
ATOM   1732  N   TYR A 231     -27.284 -10.134  40.494  1.00  9.33           N
ATOM   1733  CA  TYR A 231     -25.990 -10.789  40.737  1.00  9.32           C
ATOM   1734  C   TYR A 231     -25.960 -12.184  40.131  1.00 10.93           C
ATOM   1735  O   TYR A 231     -26.966 -12.916  40.160  1.00 13.03           O
ATOM   1736  CB  TYR A 231     -25.738 -10.985  42.243  1.00  7.56           C
ATOM   1737  CG  TYR A 231     -25.551  -9.705  43.020  1.00  7.38           C
ATOM   1738  CD1 TYR A 231     -26.645  -8.910  43.349  1.00  7.53           C
ATOM   1739  CD2 TYR A 231     -24.279  -9.273  43.401  1.00  7.40           C
ATOM   1740  CE1 TYR A 231     -26.489  -7.695  44.033  1.00  7.61           C
ATOM   1741  CE2 TYR A 231     -24.108  -8.057  44.109  1.00  5.65           C
ATOM   1742  CZ  TYR A 231     -25.222  -7.276  44.408  1.00  8.78           C
ATOM   1743  OH  TYR A 231     -25.078  -6.064  45.065  1.00 14.76           O
ATOM   1744  N   ILE A 232     -24.770 -12.594  39.715  1.00  9.63           N
ATOM   1745  CA  ILE A 232     -24.566 -13.919  39.158  1.00  8.38           C
ATOM   1746  C   ILE A 232     -23.330 -14.496  39.859  1.00  7.80           C
ATOM   1747  O   ILE A 232     -22.282 -13.825  39.932  1.00  6.58           O
ATOM   1748  CB  ILE A 232     -24.322 -13.838  37.646  1.00  8.76           C
ATOM   1749  CG1 ILE A 232     -25.581 -13.282  36.958  1.00  9.73           C
ATOM   1750  CG2 ILE A 232     -23.905 -15.202  37.080  1.00  8.74           C
ATOM   1751  CD1 ILE A 232     -25.434 -13.067  35.475  1.00 10.48           C
ATOM   1752  N   GLY A 233     -23.468 -15.700  40.415  1.00  6.01           N
ATOM   1753  CA  GLY A 233     -22.336 -16.332  41.081  1.00  5.01           C
ATOM   1754  C   GLY A 233     -21.534 -17.257  40.169  1.00  5.10           C
ATOM   1755  O   GLY A 233     -22.089 -17.903  39.245  1.00  5.44           O
ATOM   1756  N   VAL A 234     -20.228 -17.310  40.397  1.00  3.99           N
ATOM   1757  CA  VAL A 234     -19.354 -18.165  39.618  1.00  3.19           C
ATOM   1758  C   VAL A 234     -18.350 -18.834  40.554  1.00  5.30           C
ATOM   1759  O   VAL A 234     -18.134 -18.389  41.688  1.00  5.52           O
ATOM   1760  CB  VAL A 234     -18.541 -17.370  38.525  1.00  2.21           C
ATOM   1761  CG1 VAL A 234     -19.474 -16.775  37.478  1.00  1.00           C
ATOM   1762  CG2 VAL A 234     -17.712 -16.225  39.167  1.00  2.69           C
ATOM   1763  N   VAL A 235     -17.808 -19.965  40.112  1.00  6.16           N
ATOM   1764  CA  VAL A 235     -16.782 -20.656  40.873  1.00  6.37           C
ATOM   1765  C   VAL A 235     -15.667 -20.944  39.875  1.00  6.39           C
ATOM   1766  O   VAL A 235     -15.809 -21.788  38.973  1.00  5.40           O
ATOM   1767  CB  VAL A 235     -17.277 -21.971  41.479  1.00  6.08           C
ATOM   1768  CG1 VAL A 235     -16.104 -22.675  42.206  1.00  5.75           C
ATOM   1769  CG2 VAL A 235     -18.431 -21.691  42.463  1.00  5.71           C
ATOM   1770  N   ASN A 236     -14.598 -20.169  39.983  1.00  4.61           N
ATOM   1771  CA  ASN A 236     -13.448 -20.320  39.093  1.00  4.43           C
ATOM   1772  C   ASN A 236     -12.449 -21.288  39.726  1.00  7.16           C
ATOM   1773  O   ASN A 236     -12.684 -21.832  40.830  1.00  6.92           O
ATOM   1774  CB  ASN A 236     -12.767 -18.957  38.866  1.00  1.00           C
ATOM   1775  CG  ASN A 236     -13.744 -17.871  38.434  1.00 12.00           C
ATOM   1776  OD1 ASN A 236     -14.472 -18.035  37.450  1.00 11.15           O
ATOM   1777  ND2 ASN A 236     -13.753 -16.749  39.160  1.00 14.30           N
ATOM   1778  N   ARG A 237     -11.304 -21.466  39.064  1.00  6.19           N
ATOM   1779  CA  ARG A 237     -10.284 -22.371  39.573  1.00  6.91           C
ATOM   1780  C   ARG A 237      -9.477 -21.813  40.745  1.00  5.30           C
ATOM   1781  O   ARG A 237      -9.230 -20.612  40.821  1.00  5.51           O
ATOM   1782  CB  ARG A 237      -9.333 -22.775  38.438  1.00  8.44           C
ATOM   1783  CG  ARG A 237      -9.967 -23.747  37.424  1.00  5.43           C
ATOM   1784  CD  ARG A 237      -9.082 -23.911  36.160  1.00  2.82           C
ATOM   1785  NE  ARG A 237      -8.893 -22.622  35.502  1.00 10.02           N
ATOM   1786  CZ  ARG A 237      -8.153 -22.426  34.417  1.00  8.61           C
ATOM   1787  NH1 ARG A 237      -7.503 -23.442  33.842  1.00  6.70           N
ATOM   1788  NH2 ARG A 237      -8.118 -21.217  33.872  1.00 10.05           N
ATOM   1789  N   SER A 238      -9.102 -22.701  41.664  1.00  2.94           N
ATOM   1790  CA  SER A 238      -8.280 -22.351  42.813  1.00  4.20           C
ATOM   1791  C   SER A 238      -6.843 -22.297  42.307  1.00  7.00           C
ATOM   1792  O   SER A 238      -6.574 -22.711  41.169  1.00  7.94           O
ATOM   1793  CB  SER A 238      -8.369 -23.466  43.859  1.00  3.52           C
ATOM   1794  OG  SER A 238      -7.941 -24.715  43.313  1.00  5.69           O
ATOM   1795  N   GLN A 239      -5.917 -21.840  43.157  1.00  7.51           N
ATOM   1796  CA  GLN A 239      -4.503 -21.784  42.782  1.00  7.36           C
ATOM   1797  C   GLN A 239      -4.002 -23.218  42.628  1.00  8.46           C
ATOM   1798  O   GLN A 239      -3.240 -23.517  41.714  1.00  9.45           O
ATOM   1799  CB  GLN A 239      -3.674 -21.048  43.852  1.00  7.14           C
ATOM   1800  CG  GLN A 239      -2.193 -20.829  43.451  1.00 11.63           C
ATOM   1801  CD  GLN A 239      -2.033 -20.044  42.152  1.00 12.76           C
ATOM   1802  OE1 GLN A 239      -2.587 -18.968  41.992  1.00 14.69           O
ATOM   1803  NE2 GLN A 239      -1.269 -20.590  41.219  1.00 20.89           N
ATOM   1804  N   LYS A 240      -4.438 -24.098  43.527  1.00  9.72           N
ATOM   1805  CA  LYS A 240      -4.067 -25.522  43.487  1.00 11.70           C
ATOM   1806  C   LYS A 240      -4.570 -26.154  42.166  1.00 14.88           C
ATOM   1807  O   LYS A 240      -3.873 -26.980  41.564  1.00 15.63           O
ATOM   1808  CB  LYS A 240      -4.668 -26.258  44.704  1.00 11.68           C
ATOM   1809  CG  LYS A 240      -4.362 -27.761  44.799  1.00 19.23           C
ATOM   1810  CD  LYS A 240      -2.860 -28.026  44.835  1.00 30.66           C
ATOM   1811  CE  LYS A 240      -2.358 -28.431  46.218  1.00 30.03           C
ATOM   1812  NZ  LYS A 240      -2.772 -29.814  46.588  1.00 30.15           N
ATOM   1813  N   ASP A 241      -5.765 -25.765  41.716  1.00 15.63           N
ATOM   1814  CA  ASP A 241      -6.318 -26.285  40.456  1.00 14.86           C
ATOM   1815  C   ASP A 241      -5.349 -25.870  39.353  1.00 17.16           C
ATOM   1816  O   ASP A 241      -4.935 -26.687  38.518  1.00 19.19           O
ATOM   1817  CB  ASP A 241      -7.691 -25.658  40.141  1.00 11.02           C
ATOM   1818  CG  ASP A 241      -8.821 -26.192  41.024  1.00 13.88           C
ATOM   1819  OD1 ASP A 241      -8.633 -27.227  41.691  1.00 15.21           O
ATOM   1820  OD2 ASP A 241      -9.916 -25.568  41.037  1.00 14.20           O
ATOM   1821  N   ILE A 242      -4.991 -24.590  39.367  1.00 18.22           N
ATOM   1822  CA  ILE A 242      -4.068 -24.021  38.394  1.00 19.59           C
ATOM   1823  C   ILE A 242      -2.761 -24.824  38.375  1.00 21.67           C
ATOM   1824  O   ILE A 242      -2.359 -25.345  37.337  1.00 21.86           O
ATOM   1825  CB  ILE A 242      -3.774 -22.530  38.723  1.00 18.85           C
ATOM   1826  CG1 ILE A 242      -5.025 -21.677  38.450  1.00 18.15           C
ATOM   1827  CG2 ILE A 242      -2.577 -22.031  37.941  1.00 19.94           C
ATOM   1828  CD1 ILE A 242      -4.874 -20.178  38.734  1.00 15.49           C
ATOM   1829  N   ASP A 243      -2.140 -24.959  39.544  1.00 22.27           N
ATOM   1830  CA  ASP A 243      -0.880 -25.677  39.676  1.00 23.72           C
ATOM   1831  C   ASP A 243      -1.006 -27.103  39.150  1.00 24.30           C
ATOM   1832  O   ASP A 243      -0.081 -27.614  38.520  1.00 25.52           O
ATOM   1833  CB  ASP A 243      -0.422 -25.695  41.148  1.00 25.17           C
ATOM   1834  CG  ASP A 243      -0.184 -24.295  41.723  1.00 25.96           C
ATOM   1835  OD1 ASP A 243      -0.263 -24.142  42.963  1.00 27.32           O
ATOM   1836  OD2 ASP A 243       0.075 -23.346  40.955  1.00 27.51           O
ATOM   1837  N   GLY A 244      -2.159 -27.728  39.393  1.00 22.83           N
ATOM   1838  CA  GLY A 244      -2.405 -29.092  38.944  1.00 20.27           C
ATOM   1839  C   GLY A 244      -2.867 -29.238  37.495  1.00 19.14           C
ATOM   1840  O   GLY A 244      -3.313 -30.324  37.089  1.00 19.10           O
ATOM   1841  N   LYS A 245      -2.788 -28.139  36.737  1.00 17.15           N
ATOM   1842  CA  LYS A 245      -3.155 -28.070  35.322  1.00 16.16           C
ATOM   1843  C   LYS A 245      -4.625 -28.365  34.962  1.00 15.95           C
ATOM   1844  O   LYS A 245      -4.921 -28.783  33.848  1.00 16.94           O
ATOM   1845  CB  LYS A 245      -2.232 -28.964  34.476  1.00 17.51           C
ATOM   1846  CG  LYS A 245      -0.752 -28.830  34.778  1.00 15.01           C
ATOM   1847  CD  LYS A 245      -0.271 -27.391  34.776  1.00 16.16           C
ATOM   1848  CE  LYS A 245       1.240 -27.356  34.970  1.00 35.87           C
ATOM   1849  NZ  LYS A 245       1.770 -25.962  35.074  1.00 54.84           N
ATOM   1850  N   LYS A 246      -5.541 -28.152  35.897  1.00 13.52           N
ATOM   1851  CA  LYS A 246      -6.960 -28.396  35.625  1.00 12.08           C
ATOM   1852  C   LYS A 246      -7.368 -27.377  34.561  1.00 11.85           C
ATOM   1853  O   LYS A 246      -6.995 -26.211  34.661  1.00 12.21           O
ATOM   1854  CB  LYS A 246      -7.771 -28.169  36.901  1.00  7.85           C
ATOM   1855  CG  LYS A 246      -9.267 -28.487  36.778  1.00  8.69           C
ATOM   1856  CD  LYS A 246      -9.920 -28.413  38.174  1.00 11.63           C
ATOM   1857  CE  LYS A 246     -11.387 -28.779  38.129  1.00  9.46           C
ATOM   1858  NZ  LYS A 246     -11.971 -28.819  39.495  1.00 18.03           N
ATOM   1859  N   ASP A 247      -8.111 -27.800  33.543  1.00 11.12           N
ATOM   1860  CA  ASP A 247      -8.513 -26.869  32.497  1.00 10.26           C
ATOM   1861  C   ASP A 247      -9.888 -26.228  32.737  1.00 10.35           C
ATOM   1862  O   ASP A 247     -10.647 -26.634  33.635  1.00 11.76           O
ATOM   1863  CB  ASP A 247      -8.429 -27.526  31.114  1.00 10.48           C
ATOM   1864  CG  ASP A 247      -9.370 -28.730  30.952  1.00 20.01           C
ATOM   1865  OD1 ASP A 247     -10.441 -28.785  31.598  1.00 16.38           O
ATOM   1866  OD2 ASP A 247      -9.030 -29.632  30.157  1.00 27.39           O
ATOM   1867  N   ILE A 248     -10.225 -25.271  31.886  1.00  8.83           N
ATOM   1868  CA  ILE A 248     -11.471 -24.551  31.998  1.00  8.60           C
ATOM   1869  C   ILE A 248     -12.705 -25.433  31.874  1.00  9.52           C
ATOM   1870  O   ILE A 248     -13.622 -25.313  32.677  1.00 11.28           O
ATOM   1871  CB  ILE A 248     -11.487 -23.331  31.030  1.00  8.38           C
ATOM   1872  CG1 ILE A 248     -10.476 -22.293  31.558  1.00  9.36           C
ATOM   1873  CG2 ILE A 248     -12.933 -22.744  30.878  1.00  7.63           C
ATOM   1874  CD1 ILE A 248     -10.492 -20.921  30.853  1.00  5.98           C
ATOM   1875  N   THR A 249     -12.687 -26.383  30.950  1.00  9.98           N
ATOM   1876  CA  THR A 249     -13.825 -27.275  30.768  1.00 11.50           C
ATOM   1877  C   THR A 249     -14.140 -28.040  32.057  1.00  9.97           C
ATOM   1878  O   THR A 249     -15.310 -28.153  32.440  1.00 10.46           O
ATOM   1879  CB  THR A 249     -13.585 -28.270  29.579  1.00 16.91           C
ATOM   1880  OG1 THR A 249     -13.387 -27.524  28.370  1.00 19.36           O
ATOM   1881  CG2 THR A 249     -14.787 -29.217  29.393  1.00 10.32           C
ATOM   1882  N   ALA A 250     -13.111 -28.497  32.778  1.00  8.94           N
ATOM   1883  CA  ALA A 250     -13.358 -29.228  34.008  1.00  9.25           C
ATOM   1884  C   ALA A 250     -13.826 -28.260  35.083  1.00 10.94           C
ATOM   1885  O   ALA A 250     -14.667 -28.618  35.913  1.00 12.10           O
ATOM   1886  CB  ALA A 250     -12.111 -29.979  34.481  1.00  9.44           C
ATOM   1887  N   ALA A 251     -13.327 -27.025  35.068  1.00 10.19           N
ATOM   1888  CA  ALA A 251     -13.756 -26.060  36.101  1.00  9.80           C
ATOM   1889  C   ALA A 251     -15.239 -25.779  35.948  1.00  9.31           C
ATOM   1890  O   ALA A 251     -15.982 -25.635  36.938  1.00  9.42           O
ATOM   1891  CB  ALA A 251     -12.974 -24.745  35.984  1.00  9.44           C
ATOM   1892  N   LEU A 252     -15.661 -25.691  34.692  1.00  7.26           N
ATOM   1893  CA  LEU A 252     -17.053 -25.413  34.349  1.00  7.36           C
ATOM   1894  C   LEU A 252     -17.962 -26.528  34.833  1.00  6.32           C
ATOM   1895  O   LEU A 252     -19.069 -26.276  35.297  1.00  7.64           O
ATOM   1896  CB  LEU A 252     -17.195 -25.267  32.836  1.00  8.91           C
ATOM   1897  CG  LEU A 252     -17.294 -23.874  32.213  1.00 10.67           C
ATOM   1898  CD1 LEU A 252     -16.769 -22.794  33.111  1.00 12.35           C
ATOM   1899  CD2 LEU A 252     -16.614 -23.885  30.855  1.00 10.10           C
ATOM   1900  N   ALA A 253     -17.501 -27.761  34.681  1.00  4.98           N
ATOM   1901  CA  ALA A 253     -18.264 -28.932  35.120  1.00  3.39           C
ATOM   1902  C   ALA A 253     -18.407 -28.859  36.641  1.00  3.52           C
ATOM   1903  O   ALA A 253     -19.490 -29.057  37.214  1.00  2.86           O
ATOM   1904  CB  ALA A 253     -17.496 -30.200  34.732  1.00  3.26           C
ATOM   1905  N   ALA A 254     -17.297 -28.569  37.307  1.00  5.65           N
ATOM   1906  CA  ALA A 254     -17.331 -28.489  38.767  1.00  5.67           C
ATOM   1907  C   ALA A 254     -18.267 -27.398  39.231  1.00  4.98           C
ATOM   1908  O   ALA A 254     -18.966 -27.563  40.219  1.00  4.46           O
ATOM   1909  CB  ALA A 254     -15.934 -28.246  39.325  1.00  5.88           C
ATOM   1910  N   GLU A 255     -18.290 -26.288  38.495  1.00  5.04           N
ATOM   1911  CA  GLU A 255     -19.129 -25.145  38.861  1.00  3.76           C
ATOM   1912  C   GLU A 255     -20.614 -25.480  38.699  1.00  3.77           C
ATOM   1913  O   GLU A 255     -21.439 -25.164  39.559  1.00  5.76           O
ATOM   1914  CB  GLU A 255     -18.745 -23.930  38.016  1.00  1.94           C
ATOM   1915  CG  GLU A 255     -19.736 -22.789  38.099  1.00  3.97           C
ATOM   1916  CD  GLU A 255     -19.450 -21.757  37.038  1.00  6.98           C
ATOM   1917  OE1 GLU A 255     -19.780 -22.052  35.871  1.00  7.92           O
ATOM   1918  OE2 GLU A 255     -18.868 -20.683  37.368  1.00  8.39           O
ATOM   1919  N   ARG A 256     -20.958 -26.116  37.595  1.00  3.14           N
ATOM   1920  CA  ARG A 256     -22.345 -26.490  37.405  1.00  4.76           C
ATOM   1921  C   ARG A 256     -22.794 -27.417  38.556  1.00  5.75           C
ATOM   1922  O   ARG A 256     -23.840 -27.193  39.196  1.00  6.44           O
ATOM   1923  CB  ARG A 256     -22.493 -27.180  36.063  1.00  6.76           C
ATOM   1924  CG  ARG A 256     -23.927 -27.543  35.744  1.00 13.14           C
ATOM   1925  CD  ARG A 256     -23.898 -28.247  34.435  1.00 16.70           C
ATOM   1926  NE  ARG A 256     -25.206 -28.339  33.845  1.00 19.87           N
ATOM   1927  CZ  ARG A 256     -25.426 -28.901  32.668  1.00 14.90           C
ATOM   1928  NH1 ARG A 256     -24.410 -29.411  31.980  1.00 13.76           N
ATOM   1929  NH2 ARG A 256     -26.659 -28.980  32.216  1.00 17.30           N
ATOM   1930  N   LYS A 257     -21.991 -28.440  38.846  1.00  6.32           N
ATOM   1931  CA  LYS A 257     -22.337 -29.362  39.941  1.00  7.49           C
ATOM   1932  C   LYS A 257     -22.501 -28.603  41.275  1.00  7.82           C
ATOM   1933  O   LYS A 257     -23.427 -28.885  42.059  1.00  6.68           O
ATOM   1934  CB  LYS A 257     -21.241 -30.433  40.091  1.00  8.39           C
ATOM   1935  CG  LYS A 257     -21.417 -31.369  41.306  1.00 10.41           C
ATOM   1936  CD  LYS A 257     -22.648 -32.250  41.097  1.00 17.49           C
ATOM   1937  CE  LYS A 257     -22.768 -33.378  42.130  1.00 26.53           C
ATOM   1938  NZ  LYS A 257     -23.906 -34.293  41.760  1.00 25.40           N
ATOM   1939  N   PHE A 258     -21.607 -27.634  41.511  1.00  7.99           N
ATOM   1940  CA  PHE A 258     -21.626 -26.829  42.740  1.00  7.61           C
ATOM   1941  C   PHE A 258     -23.010 -26.209  43.013  1.00  7.70           C
ATOM   1942  O   PHE A 258     -23.590 -26.390  44.086  1.00  7.78           O
ATOM   1943  CB  PHE A 258     -20.552 -25.721  42.678  1.00  7.03           C
ATOM   1944  CG  PHE A 258     -20.545 -24.805  43.890  1.00  7.14           C
ATOM   1945  CD1 PHE A 258     -19.821 -25.154  45.036  1.00  7.75           C
ATOM   1946  CD2 PHE A 258     -21.284 -23.619  43.889  1.00  7.69           C
ATOM   1947  CE1 PHE A 258     -19.824 -24.345  46.173  1.00  8.07           C
ATOM   1948  CE2 PHE A 258     -21.304 -22.790  45.008  1.00  8.02           C
ATOM   1949  CZ  PHE A 258     -20.564 -23.153  46.171  1.00  7.99           C
ATOM   1950  N   PHE A 259     -23.557 -25.509  42.036  1.00  6.52           N
ATOM   1951  CA  PHE A 259     -24.853 -24.865  42.248  1.00  6.50           C
ATOM   1952  C   PHE A 259     -26.010 -25.834  42.334  1.00  6.87           C
ATOM   1953  O   PHE A 259     -26.911 -25.644  43.134  1.00  6.22           O
ATOM   1954  CB  PHE A 259     -25.106 -23.794  41.189  1.00  6.24           C
ATOM   1955  CG  PHE A 259     -24.190 -22.606  41.330  1.00  4.85           C
ATOM   1956  CD1 PHE A 259     -23.213 -22.354  40.385  1.00  4.01           C
ATOM   1957  CD2 PHE A 259     -24.296 -21.765  42.445  1.00  4.52           C
ATOM   1958  CE1 PHE A 259     -22.328 -21.258  40.530  1.00  4.39           C
ATOM   1959  CE2 PHE A 259     -23.430 -20.683  42.608  1.00  4.77           C
ATOM   1960  CZ  PHE A 259     -22.440 -20.426  41.640  1.00  4.76           C
ATOM   1961  N   LEU A 260     -25.979 -26.884  41.527  1.00  7.71           N
ATOM   1962  CA  LEU A 260     -27.064 -27.858  41.582  1.00  8.61           C
ATOM   1963  C   LEU A 260     -27.068 -28.641  42.906  1.00  9.48           C
ATOM   1964  O   LEU A 260     -28.142 -28.997  43.399  1.00  9.16           O
ATOM   1965  CB  LEU A 260     -26.991 -28.798  40.376  1.00  8.63           C
ATOM   1966  CG  LEU A 260     -27.412 -28.070  39.089  1.00  7.12           C
ATOM   1967  CD1 LEU A 260     -26.846 -28.789  37.902  1.00  8.09           C
ATOM   1968  CD2 LEU A 260     -28.941 -27.987  38.999  1.00  7.34           C
ATOM   1969  N   SER A 261     -25.890 -28.848  43.501  1.00  8.17           N
ATOM   1970  CA  SER A 261     -25.791 -29.583  44.769  1.00  9.43           C
ATOM   1971  C   SER A 261     -25.821 -28.782  46.065  1.00 11.45           C
ATOM   1972  O   SER A 261     -25.924 -29.373  47.150  1.00 13.87           O
ATOM   1973  CB  SER A 261     -24.535 -30.459  44.799  1.00 11.36           C
ATOM   1974  OG  SER A 261     -24.618 -31.455  43.801  1.00 23.69           O
ATOM   1975  N   HIS A 262     -25.675 -27.469  45.990  1.00  8.83           N
ATOM   1976  CA  HIS A 262     -25.684 -26.663  47.208  1.00  8.93           C
ATOM   1977  C   HIS A 262     -27.116 -26.409  47.710  1.00  9.62           C
ATOM   1978  O   HIS A 262     -27.915 -25.791  47.013  1.00 11.67           O
ATOM   1979  CB  HIS A 262     -24.975 -25.337  46.939  1.00  8.43           C
ATOM   1980  CG  HIS A 262     -24.496 -24.658  48.180  1.00  7.62           C
ATOM   1981  ND1 HIS A 262     -25.357 -24.184  49.145  1.00  6.40           N
ATOM   1982  CD2 HIS A 262     -23.242 -24.389  48.621  1.00  7.23           C
ATOM   1983  CE1 HIS A 262     -24.654 -23.648  50.128  1.00  6.37           C
ATOM   1984  NE2 HIS A 262     -23.370 -23.760  49.832  1.00  6.72           N
ATOM   1985  N   PRO A 263     -27.448 -26.845  48.947  1.00 10.77           N
ATOM   1986  CA  PRO A 263     -28.795 -26.647  49.505  1.00 10.37           C
ATOM   1987  C   PRO A 263     -29.248 -25.188  49.454  1.00 11.29           C
ATOM   1988  O   PRO A 263     -30.439 -24.913  49.341  1.00 11.17           O
ATOM   1989  CB  PRO A 263     -28.640 -27.094  50.963  1.00 10.21           C
ATOM   1990  CG  PRO A 263     -27.572 -28.149  50.890  1.00 10.01           C
ATOM   1991  CD  PRO A 263     -26.568 -27.528  49.917  1.00 10.44           C
ATOM   1992  N   SER A 264     -28.305 -24.249  49.558  1.00 10.91           N
ATOM   1993  CA  SER A 264     -28.661 -22.827  49.540  1.00 11.64           C
ATOM   1994  C   SER A 264     -28.828 -22.189  48.164  1.00 11.18           C
ATOM   1995  O   SER A 264     -29.383 -21.088  48.064  1.00 11.94           O
ATOM   1996  CB  SER A 264     -27.618 -22.004  50.297  1.00 10.73           C
ATOM   1997  OG  SER A 264     -27.461 -22.443  51.632  1.00 14.63           O
ATOM   1998  N   TYR A 265     -28.339 -22.851  47.117  1.00  8.49           N
ATOM   1999  CA  TYR A 265     -28.389 -22.255  45.781  1.00  8.34           C
ATOM   2000  C   TYR A 265     -29.104 -23.045  44.685  1.00  9.60           C
ATOM   2001  O   TYR A 265     -29.338 -22.514  43.601  1.00  9.30           O
ATOM   2002  CB  TYR A 265     -26.952 -21.984  45.282  1.00  6.75           C
ATOM   2003  CG  TYR A 265     -26.008 -21.354  46.295  1.00  6.98           C
ATOM   2004  CD1 TYR A 265     -24.678 -21.795  46.413  1.00  7.06           C
ATOM   2005  CD2 TYR A 265     -26.417 -20.281  47.092  1.00  6.32           C
ATOM   2006  CE1 TYR A 265     -23.784 -21.178  47.291  1.00  6.24           C
ATOM   2007  CE2 TYR A 265     -25.530 -19.658  47.979  1.00  4.84           C
ATOM   2008  CZ  TYR A 265     -24.216 -20.108  48.074  1.00  4.71           C
ATOM   2009  OH  TYR A 265     -23.350 -19.481  48.961  1.00  5.38           O
ATOM   2010  N   ARG A 266     -29.409 -24.315  44.939  1.00 12.50           N
ATOM   2011  CA  ARG A 266     -30.031 -25.154  43.916  1.00 11.20           C
ATOM   2012  C   ARG A 266     -31.238 -24.548  43.189  1.00 10.40           C
ATOM   2013  O   ARG A 266     -31.362 -24.674  41.984  1.00 10.36           O
ATOM   2014  CB  ARG A 266     -30.377 -26.530  44.486  1.00 13.55           C
ATOM   2015  CG  ARG A 266     -31.192 -26.480  45.767  1.00 14.68           C
ATOM   2016  CD  ARG A 266     -31.832 -27.826  46.085  1.00 33.84           C
ATOM   2017  NE  ARG A 266     -30.836 -28.868  46.321  1.00 41.08           N
ATOM   2018  CZ  ARG A 266     -30.479 -29.787  45.427  1.00 45.45           C
ATOM   2019  NH1 ARG A 266     -31.038 -29.809  44.223  1.00 58.08           N
ATOM   2020  NH2 ARG A 266     -29.526 -30.657  45.721  1.00 38.39           N
ATOM   2021  N   HIS A 267     -32.067 -23.810  43.903  1.00 10.52           N
ATOM   2022  CA  HIS A 267     -33.253 -23.220  43.294  1.00 12.34           C
ATOM   2023  C   HIS A 267     -32.890 -22.046  42.382  1.00 13.00           C
ATOM   2024  O   HIS A 267     -33.754 -21.513  41.684  1.00 13.51           O
ATOM   2025  CB  HIS A 267     -34.194 -22.714  44.396  1.00 12.47           C
ATOM   2026  CG  HIS A 267     -33.574 -21.653  45.249  1.00 12.46           C
ATOM   2027  ND1 HIS A 267     -32.472 -21.890  46.046  1.00 12.95           N
ATOM   2028  CD2 HIS A 267     -33.887 -20.345  45.417  1.00 12.81           C
ATOM   2029  CE1 HIS A 267     -32.136 -20.776  46.672  1.00 12.94           C
ATOM   2030  NE2 HIS A 267     -32.979 -19.823  46.306  1.00 12.70           N
ATOM   2031  N   LEU A 268     -31.627 -21.616  42.422  1.00 11.26           N
ATOM   2032  CA  LEU A 268     -31.187 -20.488  41.602  1.00  9.84           C
ATOM   2033  C   LEU A 268     -30.178 -20.945  40.540  1.00 10.91           C
ATOM   2034  O   LEU A 268     -29.750 -20.140  39.699  1.00 10.80           O
ATOM   2035  CB  LEU A 268     -30.499 -19.424  42.471  1.00  9.38           C
ATOM   2036  CG  LEU A 268     -31.097 -18.824  43.754  1.00 10.38           C
ATOM   2037  CD1 LEU A 268     -30.060 -17.899  44.406  1.00  8.63           C
ATOM   2038  CD2 LEU A 268     -32.367 -18.034  43.417  1.00 13.33           C
ATOM   2039  N   ALA A 269     -29.919 -22.250  40.472  1.00  9.78           N
ATOM   2040  CA  ALA A 269     -28.889 -22.751  39.547  1.00 10.03           C
ATOM   2041  C   ALA A 269     -28.938 -22.342  38.083  1.00 10.93           C
ATOM   2042  O   ALA A 269     -27.908 -22.041  37.494  1.00 12.79           O
ATOM   2043  CB  ALA A 269     -28.704 -24.282  39.676  1.00  9.46           C
ATOM   2044  N   ASP A 270     -30.135 -22.308  37.513  1.00 10.64           N
ATOM   2045  CA  ASP A 270     -30.330 -21.947  36.109  1.00 10.87           C
ATOM   2046  C   ASP A 270     -29.925 -20.497  35.818  1.00 10.15           C
ATOM   2047  O   ASP A 270     -29.790 -20.096  34.649  1.00 10.40           O
ATOM   2048  CB  ASP A 270     -31.795 -22.179  35.711  1.00 14.10           C
ATOM   2049  CG  ASP A 270     -32.762 -21.298  36.490  1.00 26.59           C
ATOM   2050  OD1 ASP A 270     -32.541 -21.045  37.699  1.00 28.71           O
ATOM   2051  OD2 ASP A 270     -33.763 -20.856  35.886  1.00 33.17           O
ATOM   2052  N   ARG A 271     -29.800 -19.699  36.868  1.00  5.61           N
ATOM   2053  CA  ARG A 271     -29.396 -18.323  36.703  1.00  6.01           C
ATOM   2054  C   ARG A 271     -28.075 -18.086  37.430  1.00  6.44           C
ATOM   2055  O   ARG A 271     -27.789 -16.978  37.905  1.00  6.58           O
ATOM   2056  CB  ARG A 271     -30.497 -17.367  37.189  1.00  6.35           C
ATOM   2057  CG  ARG A 271     -31.692 -17.331  36.196  1.00  8.15           C
ATOM   2058  CD  ARG A 271     -32.824 -16.419  36.675  1.00 21.83           C
ATOM   2059  NE  ARG A 271     -33.356 -16.870  37.959  1.00 46.35           N
ATOM   2060  CZ  ARG A 271     -33.825 -16.063  38.909  1.00 60.83           C
ATOM   2061  NH1 ARG A 271     -33.838 -14.745  38.725  1.00 66.07           N
ATOM   2062  NH2 ARG A 271     -34.263 -16.576  40.056  1.00 57.12           N
HETATM 2063  N   MSE A 272     -27.276 -19.141  37.504  1.00  6.14           N
HETATM 2064  CA  MSE A 272     -25.983 -19.076  38.144  1.00  7.78           C
HETATM 2065  C   MSE A 272     -24.958 -19.670  37.190  1.00  6.82           C
HETATM 2066  O   MSE A 272     -25.309 -20.440  36.280  1.00  7.12           O
HETATM 2067  CB  MSE A 272     -25.990 -19.924  39.424  1.00  9.79           C
HETATM 2068  CG  MSE A 272     -26.820 -19.363  40.579  1.00 12.02           C
HETATM 2069 SE   MSE A 272     -26.008 -17.812  41.451  1.00 14.68          Se
HETATM 2070  CE  MSE A 272     -27.391 -16.450  41.122  1.00 12.73           C
ATOM   2071  N   GLY A 273     -23.694 -19.325  37.405  1.00  4.51           N
ATOM   2072  CA  GLY A 273     -22.640 -19.909  36.594  1.00  4.18           C
ATOM   2073  C   GLY A 273     -22.038 -19.074  35.494  1.00  3.75           C
ATOM   2074  O   GLY A 273     -22.610 -18.088  35.037  1.00  4.59           O
ATOM   2075  N   THR A 274     -20.867 -19.513  35.059  1.00  4.46           N
ATOM   2076  CA  THR A 274     -20.102 -18.846  34.026  1.00  6.58           C
ATOM   2077  C   THR A 274     -20.779 -18.705  32.654  1.00  6.54           C
ATOM   2078  O   THR A 274     -20.799 -17.611  32.090  1.00  6.46           O
ATOM   2079  CB  THR A 274     -18.680 -19.468  33.952  1.00  7.26           C
ATOM   2080  OG1 THR A 274     -17.999 -19.183  35.189  1.00  5.17           O
ATOM   2081  CG2 THR A 274     -17.896 -18.886  32.807  1.00  6.49           C
ATOM   2082  N   PRO A 275     -21.348 -19.790  32.102  1.00  6.18           N
ATOM   2083  CA  PRO A 275     -22.000 -19.616  30.790  1.00  7.59           C
ATOM   2084  C   PRO A 275     -23.200 -18.662  30.889  1.00  8.37           C
ATOM   2085  O   PRO A 275     -23.454 -17.860  29.976  1.00 10.89           O
ATOM   2086  CB  PRO A 275     -22.443 -21.038  30.433  1.00  8.62           C
ATOM   2087  CG  PRO A 275     -21.363 -21.906  31.114  1.00  8.97           C
ATOM   2088  CD  PRO A 275     -21.226 -21.217  32.455  1.00  7.57           C
ATOM   2089  N   TYR A 276     -23.925 -18.719  32.002  1.00  8.11           N
ATOM   2090  CA  TYR A 276     -25.080 -17.817  32.182  1.00  5.66           C
ATOM   2091  C   TYR A 276     -24.590 -16.363  32.290  1.00  4.77           C
ATOM   2092  O   TYR A 276     -25.236 -15.442  31.791  1.00  5.86           O
ATOM   2093  CB  TYR A 276     -25.870 -18.180  33.438  1.00  4.83           C
ATOM   2094  CG  TYR A 276     -27.046 -17.260  33.700  1.00  6.76           C
ATOM   2095  CD1 TYR A 276     -28.181 -17.298  32.893  1.00 10.38           C
ATOM   2096  CD2 TYR A 276     -27.015 -16.338  34.751  1.00  6.70           C
ATOM   2097  CE1 TYR A 276     -29.259 -16.440  33.125  1.00 10.81           C
ATOM   2098  CE2 TYR A 276     -28.081 -15.480  34.991  1.00  5.29           C
ATOM   2099  CZ  TYR A 276     -29.196 -15.535  34.178  1.00  5.88           C
ATOM   2100  OH  TYR A 276     -30.253 -14.702  34.413  1.00 12.17           O
ATOM   2101  N   LEU A 277     -23.524 -16.144  33.056  1.00  3.60           N
ATOM   2102  CA  LEU A 277     -22.959 -14.797  33.184  1.00  3.81           C
ATOM   2103  C   LEU A 277     -22.606 -14.269  31.791  1.00  5.38           C
ATOM   2104  O   LEU A 277     -22.919 -13.120  31.462  1.00  7.16           O
ATOM   2105  CB  LEU A 277     -21.682 -14.802  34.041  1.00  4.35           C
ATOM   2106  CG  LEU A 277     -20.870 -13.511  34.068  1.00  5.13           C
ATOM   2107  CD1 LEU A 277     -21.787 -12.380  34.517  1.00  6.11           C
ATOM   2108  CD2 LEU A 277     -19.626 -13.649  34.949  1.00  4.12           C
ATOM   2109  N   GLN A 278     -21.960 -15.099  30.968  1.00  6.12           N
ATOM   2110  CA  GLN A 278     -21.573 -14.658  29.622  1.00  6.10           C
ATOM   2111  C   GLN A 278     -22.788 -14.353  28.719  1.00  7.63           C
ATOM   2112  O   GLN A 278     -22.785 -13.356  27.971  1.00  7.91           O
ATOM   2113  CB  GLN A 278     -20.587 -15.648  28.990  1.00  9.05           C
ATOM   2114  CG  GLN A 278     -19.234 -15.627  29.728  1.00  5.99           C
ATOM   2115  CD  GLN A 278     -18.300 -16.782  29.396  1.00  9.55           C
ATOM   2116  OE1 GLN A 278     -17.376 -17.080  30.174  1.00 15.05           O
ATOM   2117  NE2 GLN A 278     -18.513 -17.429  28.249  1.00 15.78           N
ATOM   2118  N   LYS A 279     -23.841 -15.160  28.844  1.00  7.74           N
ATOM   2119  CA  LYS A 279     -25.072 -14.946  28.081  1.00  7.99           C
ATOM   2120  C   LYS A 279     -25.685 -13.590  28.483  1.00  8.88           C
ATOM   2121  O   LYS A 279     -26.058 -12.765  27.625  1.00  9.74           O
ATOM   2122  CB  LYS A 279     -26.086 -16.056  28.387  1.00  9.28           C
ATOM   2123  CG  LYS A 279     -27.422 -15.909  27.631  1.00 12.54           C
ATOM   2124  CD  LYS A 279     -28.308 -17.166  27.797  1.00 25.09           C
ATOM   2125  CE  LYS A 279     -28.708 -17.425  29.257  1.00 39.82           C
ATOM   2126  NZ  LYS A 279     -29.372 -18.773  29.518  1.00 38.23           N
ATOM   2127  N   VAL A 280     -25.775 -13.369  29.792  1.00  7.01           N
ATOM   2128  CA  VAL A 280     -26.337 -12.135  30.329  1.00  7.56           C
ATOM   2129  C   VAL A 280     -25.550 -10.886  29.945  1.00  7.36           C
ATOM   2130  O   VAL A 280     -26.135  -9.900  29.494  1.00  5.64           O
ATOM   2131  CB  VAL A 280     -26.488 -12.215  31.881  1.00  7.03           C
ATOM   2132  CG1 VAL A 280     -26.777 -10.820  32.477  1.00  6.47           C
ATOM   2133  CG2 VAL A 280     -27.625 -13.182  32.215  1.00  6.57           C
ATOM   2134  N   LEU A 281     -24.225 -10.926  30.090  1.00  9.28           N
ATOM   2135  CA  LEU A 281     -23.416  -9.758  29.750  1.00 10.03           C
ATOM   2136  C   LEU A 281     -23.589  -9.397  28.291  1.00 11.84           C
ATOM   2137  O   LEU A 281     -23.767  -8.221  27.959  1.00 12.17           O
ATOM   2138  CB  LEU A 281     -21.931  -9.996  30.060  1.00 11.04           C
ATOM   2139  CG  LEU A 281     -21.601  -9.868  31.544  1.00 11.36           C
ATOM   2140  CD1 LEU A 281     -20.226 -10.470  31.824  1.00 14.14           C
ATOM   2141  CD2 LEU A 281     -21.612  -8.388  31.895  1.00  9.99           C
ATOM   2142  N   ASN A 282     -23.620 -10.418  27.429  1.00 13.10           N
ATOM   2143  CA  ASN A 282     -23.780 -10.212  25.995  1.00 10.21           C
ATOM   2144  C   ASN A 282     -25.128  -9.582  25.689  1.00  9.65           C
ATOM   2145  O   ASN A 282     -25.226  -8.672  24.853  1.00 11.79           O
ATOM   2146  CB  ASN A 282     -23.630 -11.538  25.233  1.00  8.49           C
ATOM   2147  CG  ASN A 282     -23.804 -11.369  23.733  1.00 12.28           C
ATOM   2148  OD1 ASN A 282     -24.808 -11.803  23.162  1.00 15.06           O
ATOM   2149  ND2 ASN A 282     -22.854 -10.701  23.100  1.00 10.09           N
ATOM   2150  N   GLN A 283     -26.170 -10.047  26.362  1.00  8.74           N
ATOM   2151  CA  GLN A 283     -27.496  -9.474  26.129  1.00  9.84           C
ATOM   2152  C   GLN A 283     -27.535  -8.023  26.624  1.00 10.70           C
ATOM   2153  O   GLN A 283     -28.058  -7.143  25.945  1.00 13.08           O
ATOM   2154  CB  GLN A 283     -28.585 -10.293  26.826  1.00  9.35           C
ATOM   2155  CG  GLN A 283     -30.001  -9.823  26.500  1.00 29.21           C
ATOM   2156  CD  GLN A 283     -30.335  -9.927  25.014  1.00 45.30           C
ATOM   2157  OE1 GLN A 283     -30.637 -11.010  24.511  1.00 59.27           O
ATOM   2158  NE2 GLN A 283     -30.282  -8.796  24.306  1.00 31.86           N
ATOM   2159  N   GLN A 284     -26.968  -7.771  27.798  1.00  9.87           N
ATOM   2160  CA  GLN A 284     -26.954  -6.406  28.344  1.00  8.99           C
ATOM   2161  C   GLN A 284     -26.165  -5.473  27.440  1.00  8.69           C
ATOM   2162  O   GLN A 284     -26.564  -4.320  27.225  1.00  9.82           O
ATOM   2163  CB  GLN A 284     -26.334  -6.369  29.742  1.00 10.12           C
ATOM   2164  CG  GLN A 284     -27.086  -7.144  30.803  1.00 13.93           C
ATOM   2165  CD  GLN A 284     -28.514  -6.660  30.966  1.00 21.73           C
ATOM   2166  OE1 GLN A 284     -29.468  -7.444  30.830  1.00 21.48           O
ATOM   2167  NE2 GLN A 284     -28.676  -5.378  31.276  1.00 23.05           N
ATOM   2168  N   LEU A 285     -25.040  -5.950  26.912  1.00  8.17           N
ATOM   2169  CA  LEU A 285     -24.222  -5.097  26.052  1.00  9.96           C
ATOM   2170  C   LEU A 285     -24.968  -4.805  24.751  1.00 11.75           C
ATOM   2171  O   LEU A 285     -24.983  -3.678  24.265  1.00 11.92           O
ATOM   2172  CB  LEU A 285     -22.875  -5.745  25.752  1.00  9.72           C
ATOM   2173  CG  LEU A 285     -21.937  -4.835  24.954  1.00 10.62           C
ATOM   2174  CD1 LEU A 285     -21.650  -3.572  25.748  1.00 11.38           C
ATOM   2175  CD2 LEU A 285     -20.637  -5.580  24.629  1.00 12.11           C
ATOM   2176  N   THR A 286     -25.564  -5.841  24.178  1.00 12.67           N
ATOM   2177  CA  THR A 286     -26.333  -5.679  22.949  1.00 12.05           C
ATOM   2178  C   THR A 286     -27.432  -4.632  23.164  1.00  9.80           C
ATOM   2179  O   THR A 286     -27.622  -3.737  22.339  1.00 11.55           O
ATOM   2180  CB  THR A 286     -26.922  -7.025  22.520  1.00 15.98           C
ATOM   2181  OG1 THR A 286     -25.838  -7.913  22.223  1.00 20.82           O
ATOM   2182  CG2 THR A 286     -27.802  -6.876  21.285  1.00 19.82           C
ATOM   2183  N   ASN A 287     -28.138  -4.749  24.279  1.00  8.77           N
ATOM   2184  CA  ASN A 287     -29.197  -3.809  24.628  1.00 12.07           C
ATOM   2185  C   ASN A 287     -28.617  -2.399  24.724  1.00 15.58           C
ATOM   2186  O   ASN A 287     -29.162  -1.444  24.150  1.00 16.53           O
ATOM   2187  CB  ASN A 287     -29.819  -4.189  25.986  1.00  8.11           C
ATOM   2188  CG  ASN A 287     -30.749  -5.391  25.896  1.00 20.98           C
ATOM   2189  OD1 ASN A 287     -31.314  -5.824  26.899  1.00 27.28           O
ATOM   2190  ND2 ASN A 287     -30.902  -5.939  24.706  1.00 17.43           N
ATOM   2191  N   HIS A 288     -27.487  -2.277  25.416  1.00 14.80           N
ATOM   2192  CA  HIS A 288     -26.859  -0.979  25.588  1.00 15.31           C
ATOM   2193  C   HIS A 288     -26.442  -0.346  24.257  1.00 14.32           C
ATOM   2194  O   HIS A 288     -26.674   0.841  24.029  1.00 15.42           O
ATOM   2195  CB  HIS A 288     -25.650  -1.088  26.524  1.00 17.18           C
ATOM   2196  CG  HIS A 288     -25.221   0.230  27.093  1.00 19.48           C
ATOM   2197  ND1 HIS A 288     -25.832   0.800  28.190  1.00 19.93           N
ATOM   2198  CD2 HIS A 288     -24.266   1.106  26.700  1.00 20.58           C
ATOM   2199  CE1 HIS A 288     -25.269   1.965  28.452  1.00 20.40           C
ATOM   2200  NE2 HIS A 288     -24.316   2.175  27.563  1.00 20.15           N
ATOM   2201  N   ILE A 289     -25.856  -1.142  23.370  1.00 13.55           N
ATOM   2202  CA  ILE A 289     -25.397  -0.657  22.075  1.00 14.32           C
ATOM   2203  C   ILE A 289     -26.579  -0.206  21.204  1.00 15.68           C
ATOM   2204  O   ILE A 289     -26.527   0.857  20.582  1.00 14.95           O
ATOM   2205  CB  ILE A 289     -24.592  -1.744  21.310  1.00 14.20           C
ATOM   2206  CG1 ILE A 289     -23.245  -2.011  21.996  1.00 11.68           C
ATOM   2207  CG2 ILE A 289     -24.353  -1.302  19.859  1.00 15.38           C
ATOM   2208  CD1 ILE A 289     -22.470  -3.177  21.368  1.00 11.08           C
ATOM   2209  N   ARG A 290     -27.631  -1.021  21.139  1.00 16.78           N
ATOM   2210  CA  ARG A 290     -28.801  -0.654  20.339  1.00 18.18           C
ATOM   2211  C   ARG A 290     -29.290   0.734  20.738  1.00 21.41           C
ATOM   2212  O   ARG A 290     -29.638   1.548  19.882  1.00 22.03           O
ATOM   2213  CB  ARG A 290     -29.937  -1.676  20.508  1.00 15.38           C
ATOM   2214  CG  ARG A 290     -31.313  -1.147  20.093  1.00 28.05           C
ATOM   2215  CD  ARG A 290     -32.342  -2.279  19.931  1.00 42.23           C
ATOM   2216  NE  ARG A 290     -32.131  -3.030  18.691  1.00 55.42           N
ATOM   2217  CZ  ARG A 290     -32.843  -4.094  18.315  1.00 56.82           C
ATOM   2218  NH1 ARG A 290     -33.825  -4.560  19.082  1.00 57.54           N
ATOM   2219  NH2 ARG A 290     -32.587  -4.682  17.152  1.00 47.58           N
ATOM   2220  N   ASP A 291     -29.285   0.998  22.040  1.00 24.10           N
ATOM   2221  CA  ASP A 291     -29.727   2.271  22.586  1.00 25.11           C
ATOM   2222  C   ASP A 291     -28.769   3.441  22.354  1.00 24.64           C
ATOM   2223  O   ASP A 291     -29.208   4.583  22.185  1.00 25.28           O
ATOM   2224  CB  ASP A 291     -29.935   2.143  24.098  1.00 30.74           C
ATOM   2225  CG  ASP A 291     -31.138   1.289  24.468  1.00 46.13           C
ATOM   2226  OD1 ASP A 291     -31.427   1.227  25.683  1.00 50.32           O
ATOM   2227  OD2 ASP A 291     -31.787   0.686  23.575  1.00 49.88           O
ATOM   2228  N   THR A 292     -27.467   3.171  22.403  1.00 22.94           N
ATOM   2229  CA  THR A 292     -26.480   4.230  22.254  1.00 20.04           C
ATOM   2230  C   THR A 292     -25.975   4.478  20.849  1.00 16.81           C
ATOM   2231  O   THR A 292     -25.201   5.411  20.628  1.00 17.04           O
ATOM   2232  CB  THR A 292     -25.269   3.982  23.174  1.00 19.48           C
ATOM   2233  OG1 THR A 292     -24.711   2.687  22.901  1.00 19.63           O
ATOM   2234  CG2 THR A 292     -25.695   4.063  24.638  1.00 18.77           C
ATOM   2235  N   LEU A 293     -26.418   3.658  19.904  1.00 16.37           N
ATOM   2236  CA  LEU A 293     -25.982   3.771  18.518  1.00 16.66           C
ATOM   2237  C   LEU A 293     -26.129   5.149  17.878  1.00 16.31           C
ATOM   2238  O   LEU A 293     -25.191   5.640  17.226  1.00 15.24           O
ATOM   2239  CB  LEU A 293     -26.689   2.741  17.646  1.00 17.96           C
ATOM   2240  CG  LEU A 293     -25.829   1.688  16.953  1.00 19.69           C
ATOM   2241  CD1 LEU A 293     -26.669   1.086  15.848  1.00 22.16           C
ATOM   2242  CD2 LEU A 293     -24.567   2.292  16.363  1.00 20.76           C
ATOM   2243  N   PRO A 294     -27.329   5.758  17.977  1.00 15.70           N
ATOM   2244  CA  PRO A 294     -27.457   7.084  17.359  1.00 15.27           C
ATOM   2245  C   PRO A 294     -26.431   8.071  17.912  1.00 14.86           C
ATOM   2246  O   PRO A 294     -25.860   8.866  17.162  1.00 14.86           O
ATOM   2247  CB  PRO A 294     -28.889   7.486  17.714  1.00 14.88           C
ATOM   2248  CG  PRO A 294     -29.595   6.172  17.723  1.00 15.02           C
ATOM   2249  CD  PRO A 294     -28.629   5.316  18.520  1.00 14.83           C
ATOM   2250  N   GLY A 295     -26.172   7.997  19.219  1.00 13.51           N
ATOM   2251  CA  GLY A 295     -25.205   8.897  19.816  1.00 11.60           C
ATOM   2252  C   GLY A 295     -23.794   8.573  19.332  1.00 12.12           C
ATOM   2253  O   GLY A 295     -22.966   9.469  19.124  1.00 13.04           O
ATOM   2254  N   LEU A 296     -23.496   7.287  19.196  1.00 11.48           N
ATOM   2255  CA  LEU A 296     -22.182   6.888  18.706  1.00 12.40           C
ATOM   2256  C   LEU A 296     -22.000   7.433  17.279  1.00 12.27           C
ATOM   2257  O   LEU A 296     -20.929   7.940  16.920  1.00 12.01           O
ATOM   2258  CB  LEU A 296     -22.050   5.372  18.707  1.00 12.81           C
ATOM   2259  CG  LEU A 296     -20.747   4.891  18.070  1.00 15.29           C
ATOM   2260  CD1 LEU A 296     -19.520   5.545  18.751  1.00 15.04           C
ATOM   2261  CD2 LEU A 296     -20.706   3.368  18.175  1.00 14.87           C
ATOM   2262  N   ARG A 297     -23.050   7.342  16.471  1.00 12.23           N
ATOM   2263  CA  ARG A 297     -22.977   7.861  15.099  1.00 11.61           C
ATOM   2264  C   ARG A 297     -22.621   9.362  15.139  1.00  9.86           C
ATOM   2265  O   ARG A 297     -21.688   9.812  14.464  1.00  8.38           O
ATOM   2266  CB  ARG A 297     -24.315   7.634  14.378  1.00 14.06           C
ATOM   2267  CG  ARG A 297     -24.425   8.291  13.006  1.00 13.41           C
ATOM   2268  CD  ARG A 297     -25.831   8.079  12.442  1.00 20.93           C
ATOM   2269  NE  ARG A 297     -26.161   9.012  11.369  1.00 40.02           N
ATOM   2270  CZ  ARG A 297     -26.677  10.228  11.549  1.00 51.60           C
ATOM   2271  NH1 ARG A 297     -26.935  10.684  12.770  1.00 43.40           N
ATOM   2272  NH2 ARG A 297     -26.913  11.008  10.496  1.00 58.04           N
ATOM   2273  N   ASN A 298     -23.350  10.129  15.950  1.00  9.56           N
ATOM   2274  CA  ASN A 298     -23.075  11.571  16.078  1.00  6.92           C
ATOM   2275  C   ASN A 298     -21.615  11.831  16.529  1.00  8.34           C
ATOM   2276  O   ASN A 298     -20.963  12.727  16.012  1.00  7.41           O
ATOM   2277  CB  ASN A 298     -24.006  12.223  17.107  1.00 11.49           C
ATOM   2278  CG  ASN A 298     -25.470  12.265  16.669  1.00 15.49           C
ATOM   2279  OD1 ASN A 298     -26.369  12.252  17.509  1.00 19.16           O
ATOM   2280  ND2 ASN A 298     -25.709  12.375  15.379  1.00 10.27           N
ATOM   2281  N   LYS A 299     -21.099  11.046  17.482  1.00  8.14           N
ATOM   2282  CA  LYS A 299     -19.728  11.258  17.970  1.00  9.92           C
ATOM   2283  C   LYS A 299     -18.688  10.962  16.900  1.00 11.58           C
ATOM   2284  O   LYS A 299     -17.713  11.711  16.736  1.00 12.65           O
ATOM   2285  CB  LYS A 299     -19.428  10.408  19.217  1.00 14.48           C
ATOM   2286  CG  LYS A 299     -20.236  10.797  20.458  1.00 17.64           C
ATOM   2287  CD  LYS A 299     -19.810   9.976  21.682  1.00 32.52           C
ATOM   2288  CE  LYS A 299     -20.432  10.494  22.996  1.00 37.53           C
ATOM   2289  NZ  LYS A 299     -21.880  10.189  23.154  1.00 36.79           N
ATOM   2290  N   LEU A 300     -18.908   9.880  16.161  1.00 10.42           N
ATOM   2291  CA  LEU A 300     -17.985   9.504  15.100  1.00 10.59           C
ATOM   2292  C   LEU A 300     -18.006  10.541  13.968  1.00 10.24           C
ATOM   2293  O   LEU A 300     -16.958  10.907  13.438  1.00 12.02           O
ATOM   2294  CB  LEU A 300     -18.293   8.087  14.596  1.00 10.82           C
ATOM   2295  CG  LEU A 300     -18.149   6.994  15.663  1.00 11.32           C
ATOM   2296  CD1 LEU A 300     -18.183   5.629  14.994  1.00 12.60           C
ATOM   2297  CD2 LEU A 300     -16.824   7.144  16.430  1.00 12.54           C
ATOM   2298  N   GLN A 301     -19.183  11.065  13.647  1.00 10.25           N
ATOM   2299  CA  GLN A 301     -19.299  12.086  12.604  1.00  9.88           C
ATOM   2300  C   GLN A 301     -18.441  13.298  12.994  1.00 10.08           C
ATOM   2301  O   GLN A 301     -17.746  13.882  12.145  1.00  9.05           O
ATOM   2302  CB  GLN A 301     -20.760  12.529  12.451  1.00  9.37           C
ATOM   2303  CG  GLN A 301     -21.629  11.569  11.678  1.00 17.31           C
ATOM   2304  CD  GLN A 301     -23.115  11.901  11.771  1.00 37.04           C
ATOM   2305  OE1 GLN A 301     -23.560  12.646  12.659  1.00 47.12           O
ATOM   2306  NE2 GLN A 301     -23.896  11.315  10.877  1.00 36.09           N
ATOM   2307  N   SER A 302     -18.543  13.690  14.271  1.00  9.71           N
ATOM   2308  CA  SER A 302     -17.795  14.811  14.833  1.00  9.75           C
ATOM   2309  C   SER A 302     -16.280  14.525  14.771  1.00  9.39           C
ATOM   2310  O   SER A 302     -15.488  15.374  14.331  1.00 10.34           O
ATOM   2311  CB  SER A 302     -18.248  15.041  16.290  1.00 14.64           C
ATOM   2312  OG  SER A 302     -17.730  16.243  16.847  1.00 18.38           O
ATOM   2313  N   GLN A 303     -15.868  13.345  15.226  1.00 10.21           N
ATOM   2314  CA  GLN A 303     -14.458  12.966  15.182  1.00 10.59           C
ATOM   2315  C   GLN A 303     -13.930  13.004  13.731  1.00 11.37           C
ATOM   2316  O   GLN A 303     -12.788  13.399  13.503  1.00 12.10           O
ATOM   2317  CB  GLN A 303     -14.247  11.572  15.771  1.00 14.48           C
ATOM   2318  CG  GLN A 303     -14.353  11.489  17.299  1.00 27.01           C
ATOM   2319  CD  GLN A 303     -13.327  12.360  18.009  1.00 33.66           C
ATOM   2320  OE1 GLN A 303     -13.682  13.299  18.716  1.00 40.68           O
ATOM   2321  NE2 GLN A 303     -12.051  12.055  17.821  1.00 29.18           N
ATOM   2322  N   LEU A 304     -14.751  12.585  12.761  1.00 11.00           N
ATOM   2323  CA  LEU A 304     -14.335  12.602  11.352  1.00 10.55           C
ATOM   2324  C   LEU A 304     -13.984  14.049  10.954  1.00 12.04           C
ATOM   2325  O   LEU A 304     -12.875  14.311  10.457  1.00 13.42           O
ATOM   2326  CB  LEU A 304     -15.452  12.066  10.444  1.00 10.60           C
ATOM   2327  CG  LEU A 304     -15.115  11.939   8.940  1.00 10.97           C
ATOM   2328  CD1 LEU A 304     -14.004  10.922   8.714  1.00  9.15           C
ATOM   2329  CD2 LEU A 304     -16.361  11.543   8.130  1.00 10.69           C
ATOM   2330  N   LEU A 305     -14.898  14.986  11.229  1.00 13.49           N
ATOM   2331  CA  LEU A 305     -14.667  16.396  10.922  1.00 15.18           C
ATOM   2332  C   LEU A 305     -13.403  16.904  11.618  1.00 15.97           C
ATOM   2333  O   LEU A 305     -12.603  17.621  11.017  1.00 16.40           O
ATOM   2334  CB  LEU A 305     -15.858  17.269  11.339  1.00 15.85           C
ATOM   2335  CG  LEU A 305     -17.136  17.179  10.506  1.00 17.54           C
ATOM   2336  CD1 LEU A 305     -18.176  18.177  11.048  1.00 18.19           C
ATOM   2337  CD2 LEU A 305     -16.805  17.488   9.048  1.00 19.93           C
ATOM   2338  N   SER A 306     -13.212  16.480  12.865  1.00 16.39           N
ATOM   2339  CA  SER A 306     -12.061  16.881  13.656  1.00 16.53           C
ATOM   2340  C   SER A 306     -10.766  16.399  13.014  1.00 16.75           C
ATOM   2341  O   SER A 306      -9.834  17.184  12.839  1.00 17.76           O
ATOM   2342  CB  SER A 306     -12.190  16.341  15.092  1.00 16.09           C
ATOM   2343  OG  SER A 306     -11.048  16.658  15.869  1.00 22.20           O
ATOM   2344  N   ILE A 307     -10.718  15.117  12.647  1.00 15.23           N
ATOM   2345  CA  ILE A 307      -9.530  14.529  12.022  1.00 14.16           C
ATOM   2346  C   ILE A 307      -9.208  15.165  10.658  1.00 14.37           C
ATOM   2347  O   ILE A 307      -8.032  15.399  10.334  1.00 15.25           O
ATOM   2348  CB  ILE A 307      -9.683  13.003  11.859  1.00 14.71           C
ATOM   2349  CG1 ILE A 307      -9.964  12.338  13.216  1.00 22.74           C
ATOM   2350  CG2 ILE A 307      -8.442  12.424  11.205  1.00 14.82           C
ATOM   2351  CD1 ILE A 307      -8.808  12.362  14.235  1.00 27.73           C
ATOM   2352  N   GLU A 308     -10.235  15.456   9.862  1.00 13.28           N
ATOM   2353  CA  GLU A 308     -10.013  16.089   8.562  1.00 13.22           C
ATOM   2354  C   GLU A 308      -9.314  17.434   8.754  1.00 15.19           C
ATOM   2355  O   GLU A 308      -8.349  17.758   8.036  1.00 14.15           O
ATOM   2356  CB  GLU A 308     -11.317  16.299   7.793  1.00  8.82           C
ATOM   2357  CG  GLU A 308     -11.881  15.021   7.179  1.00 16.13           C
ATOM   2358  CD  GLU A 308     -13.105  15.274   6.308  1.00 35.14           C
ATOM   2359  OE1 GLU A 308     -14.124  14.581   6.499  1.00 29.26           O
ATOM   2360  OE2 GLU A 308     -13.048  16.165   5.433  1.00 54.89           O
ATOM   2361  N   LYS A 309      -9.799  18.211   9.723  1.00 16.40           N
ATOM   2362  CA  LYS A 309      -9.199  19.515  10.014  1.00 17.26           C
ATOM   2363  C   LYS A 309      -7.763  19.360  10.512  1.00 16.94           C
ATOM   2364  O   LYS A 309      -6.897  20.174  10.192  1.00 15.59           O
ATOM   2365  CB  LYS A 309     -10.026  20.263  11.067  1.00 22.33           C
ATOM   2366  CG  LYS A 309      -9.445  21.633  11.436  1.00 32.57           C
ATOM   2367  CD  LYS A 309     -10.252  22.327  12.529  1.00 43.36           C
ATOM   2368  CE  LYS A 309     -11.556  22.902  11.994  1.00 52.13           C
ATOM   2369  NZ  LYS A 309     -11.351  24.135  11.174  1.00 55.27           N
ATOM   2370  N   GLU A 310      -7.522  18.320  11.311  1.00 18.52           N
ATOM   2371  CA  GLU A 310      -6.197  18.053  11.883  1.00 18.24           C
ATOM   2372  C   GLU A 310      -5.192  17.783  10.754  1.00 17.76           C
ATOM   2373  O   GLU A 310      -4.067  18.305  10.743  1.00 16.63           O
ATOM   2374  CB  GLU A 310      -6.287  16.854  12.827  1.00 21.91           C
ATOM   2375  CG  GLU A 310      -5.314  16.856  13.986  1.00 27.85           C
ATOM   2376  CD  GLU A 310      -5.561  15.706  14.956  1.00 35.87           C
ATOM   2377  OE1 GLU A 310      -6.733  15.470  15.327  1.00 41.09           O
ATOM   2378  OE2 GLU A 310      -4.583  15.036  15.351  1.00 38.15           O
ATOM   2379  N   VAL A 311      -5.628  16.993   9.784  1.00 17.32           N
ATOM   2380  CA  VAL A 311      -4.799  16.672   8.641  1.00 16.67           C
ATOM   2381  C   VAL A 311      -4.494  17.958   7.839  1.00 17.21           C
ATOM   2382  O   VAL A 311      -3.387  18.128   7.324  1.00 18.06           O
ATOM   2383  CB  VAL A 311      -5.513  15.668   7.717  1.00 16.38           C
ATOM   2384  CG1 VAL A 311      -4.752  15.577   6.393  1.00 16.51           C
ATOM   2385  CG2 VAL A 311      -5.582  14.292   8.390  1.00 15.70           C
ATOM   2386  N   GLU A 312      -5.477  18.841   7.703  1.00 17.01           N
ATOM   2387  CA  GLU A 312      -5.241  20.091   6.968  1.00 18.42           C
ATOM   2388  C   GLU A 312      -4.278  20.988   7.743  1.00 19.76           C
ATOM   2389  O   GLU A 312      -3.392  21.615   7.161  1.00 21.42           O
ATOM   2390  CB  GLU A 312      -6.549  20.832   6.703  1.00 21.59           C
ATOM   2391  CG  GLU A 312      -7.440  20.097   5.707  1.00 49.71           C
ATOM   2392  CD  GLU A 312      -8.656  20.892   5.232  1.00 66.27           C
ATOM   2393  OE1 GLU A 312      -8.598  22.148   5.174  1.00 55.84           O
ATOM   2394  OE2 GLU A 312      -9.671  20.239   4.889  1.00 70.02           O
ATOM   2395  N   GLU A 313      -4.428  21.010   9.068  1.00 17.98           N
ATOM   2396  CA  GLU A 313      -3.566  21.822   9.908  1.00 17.40           C
ATOM   2397  C   GLU A 313      -2.137  21.301   9.973  1.00 17.44           C
ATOM   2398  O   GLU A 313      -1.185  22.086  10.020  1.00 19.54           O
ATOM   2399  CB  GLU A 313      -4.186  21.998  11.303  1.00 18.88           C
ATOM   2400  CG  GLU A 313      -4.910  23.347  11.446  1.00 30.85           C
ATOM   2401  CD  GLU A 313      -6.118  23.322  12.393  1.00 48.44           C
ATOM   2402  OE1 GLU A 313      -6.100  22.577  13.403  1.00 46.65           O
ATOM   2403  OE2 GLU A 313      -7.088  24.070  12.122  1.00 44.84           O
ATOM   2404  N   TYR A 314      -1.967  19.988   9.913  1.00 18.53           N
ATOM   2405  CA  TYR A 314      -0.625  19.416   9.967  1.00 19.18           C
ATOM   2406  C   TYR A 314       0.142  19.814   8.718  1.00 20.40           C
ATOM   2407  O   TYR A 314       1.352  20.026   8.754  1.00 20.45           O
ATOM   2408  CB  TYR A 314      -0.671  17.892  10.072  1.00 17.75           C
ATOM   2409  CG  TYR A 314       0.684  17.296  10.377  1.00 17.55           C
ATOM   2410  CD1 TYR A 314       1.464  16.721   9.364  1.00 18.49           C
ATOM   2411  CD2 TYR A 314       1.192  17.311  11.676  1.00 16.30           C
ATOM   2412  CE1 TYR A 314       2.717  16.177   9.640  1.00 17.38           C
ATOM   2413  CE2 TYR A 314       2.437  16.769  11.964  1.00 16.10           C
ATOM   2414  CZ  TYR A 314       3.199  16.204  10.939  1.00 18.74           C
ATOM   2415  OH  TYR A 314       4.440  15.659  11.218  1.00 23.96           O
ATOM   2416  N   LYS A 315      -0.588  19.904   7.615  1.00 22.65           N
ATOM   2417  CA  LYS A 315      -0.025  20.291   6.329  1.00 25.50           C
ATOM   2418  C   LYS A 315       0.661  21.649   6.460  1.00 25.62           C
ATOM   2419  O   LYS A 315       1.696  21.898   5.835  1.00 26.41           O
ATOM   2420  CB  LYS A 315      -1.153  20.359   5.304  1.00 34.87           C
ATOM   2421  CG  LYS A 315      -0.737  20.549   3.865  1.00 43.60           C
ATOM   2422  CD  LYS A 315      -1.980  20.542   2.973  1.00 47.58           C
ATOM   2423  CE  LYS A 315      -2.890  19.338   3.265  1.00 46.40           C
ATOM   2424  NZ  LYS A 315      -2.226  18.011   3.060  1.00 39.67           N
ATOM   2425  N   ASN A 316       0.097  22.513   7.298  1.00 24.59           N
ATOM   2426  CA  ASN A 316       0.662  23.839   7.514  1.00 24.14           C
ATOM   2427  C   ASN A 316       1.847  23.768   8.488  1.00 23.96           C
ATOM   2428  O   ASN A 316       2.841  24.467   8.306  1.00 25.61           O
ATOM   2429  CB  ASN A 316      -0.406  24.814   8.039  1.00 23.03           C
ATOM   2430  CG  ASN A 316      -1.594  24.948   7.095  1.00 26.33           C
ATOM   2431  OD1 ASN A 316      -1.441  24.919   5.874  1.00 25.90           O
ATOM   2432  ND2 ASN A 316      -2.792  25.063   7.662  1.00 35.01           N
ATOM   2433  N   PHE A 317       1.751  22.897   9.493  1.00 22.77           N
ATOM   2434  CA  PHE A 317       2.809  22.737  10.502  1.00 21.22           C
ATOM   2435  C   PHE A 317       4.074  22.163   9.855  1.00 22.30           C
ATOM   2436  O   PHE A 317       5.200  22.528  10.216  1.00 22.10           O
ATOM   2437  CB  PHE A 317       2.324  21.821  11.640  1.00 19.82           C
ATOM   2438  CG  PHE A 317       3.335  21.621  12.749  1.00 18.75           C
ATOM   2439  CD1 PHE A 317       3.822  22.713  13.480  1.00 17.42           C
ATOM   2440  CD2 PHE A 317       3.811  20.348  13.054  1.00 18.25           C
ATOM   2441  CE1 PHE A 317       4.760  22.537  14.488  1.00 15.47           C
ATOM   2442  CE2 PHE A 317       4.761  20.151  14.068  1.00 16.46           C
ATOM   2443  CZ  PHE A 317       5.237  21.259  14.789  1.00 15.53           C
ATOM   2444  N   ARG A 318       3.874  21.263   8.899  1.00 23.22           N
ATOM   2445  CA  ARG A 318       4.977  20.632   8.195  1.00 30.20           C
ATOM   2446  C   ARG A 318       4.720  20.718   6.694  1.00 36.45           C
ATOM   2447  O   ARG A 318       4.351  19.717   6.066  1.00 37.06           O
ATOM   2448  CB  ARG A 318       5.124  19.163   8.624  1.00 30.09           C
ATOM   2449  CG  ARG A 318       5.614  18.960  10.073  1.00 28.98           C
ATOM   2450  CD  ARG A 318       7.095  19.283  10.181  1.00 37.21           C
ATOM   2451  NE  ARG A 318       7.591  19.247  11.555  1.00 42.59           N
ATOM   2452  CZ  ARG A 318       7.689  20.314  12.349  1.00 34.59           C
ATOM   2453  NH1 ARG A 318       7.314  21.518  11.909  1.00 18.97           N
ATOM   2454  NH2 ARG A 318       8.205  20.183  13.570  1.00 18.12           N
ATOM   2455  N   PRO A 319       4.896  21.918   6.096  1.00 39.09           N
ATOM   2456  CA  PRO A 319       4.679  22.103   4.647  1.00 41.41           C
ATOM   2457  C   PRO A 319       5.398  20.994   3.882  1.00 45.44           C
ATOM   2458  O   PRO A 319       5.097  20.712   2.720  1.00 47.17           O
ATOM   2459  CB  PRO A 319       5.266  23.492   4.369  1.00 40.28           C
ATOM   2460  CG  PRO A 319       6.122  23.798   5.597  1.00 39.50           C
ATOM   2461  CD  PRO A 319       5.370  23.159   6.724  1.00 38.72           C
ATOM   2462  N   ASP A 320       6.343  20.367   4.579  1.00 49.98           N
ATOM   2463  CA  ASP A 320       7.103  19.220   4.108  1.00 52.37           C
ATOM   2464  C   ASP A 320       8.119  19.431   3.020  1.00 53.92           C
ATOM   2465  O   ASP A 320       8.264  20.515   2.456  1.00 53.18           O
ATOM   2466  CB  ASP A 320       6.151  18.091   3.672  1.00 51.81           C
ATOM   2467  CG  ASP A 320       5.814  17.132   4.795  1.00 55.69           C
ATOM   2468  OD1 ASP A 320       6.752  16.642   5.465  1.00 59.39           O
ATOM   2469  OD2 ASP A 320       4.611  16.846   4.993  1.00 55.08           O
ATOM   2470  N   LYS A 321       8.884  18.364   2.813  1.00 56.73           N
ATOM   2471  CA  LYS A 321       9.879  18.274   1.757  1.00 58.62           C
ATOM   2472  C   LYS A 321       9.132  17.319   0.800  1.00 59.61           C
ATOM   2473  O   LYS A 321       9.738  16.566   0.027  1.00 58.79           O
ATOM   2474  CB  LYS A 321      11.160  17.614   2.288  1.00 59.51           C
ATOM   2475  CG  LYS A 321      12.436  18.027   1.546  1.00 63.04           C
ATOM   2476  CD  LYS A 321      12.910  19.423   1.966  1.00 56.27           C
ATOM   2477  CE  LYS A 321      14.107  19.928   1.148  1.00 49.15           C
ATOM   2478  NZ  LYS A 321      13.695  20.556  -0.141  1.00 45.19           N
ATOM   2479  N   HIS A 322       7.800  17.342   0.933  1.00 60.36           N
ATOM   2480  CA  HIS A 322       6.844  16.537   0.179  1.00 60.37           C
ATOM   2481  C   HIS A 322       7.071  15.031   0.198  1.00 60.60           C
ATOM   2482  O   HIS A 322       6.769  14.322  -0.766  1.00 60.83           O
ATOM   2483  CB  HIS A 322       6.662  17.107  -1.226  1.00 60.40           C
ATOM   2484  CG  HIS A 322       6.118  18.503  -1.219  1.00 60.98           C
ATOM   2485  ND1 HIS A 322       5.244  18.950  -0.248  1.00 60.96           N
ATOM   2486  CD2 HIS A 322       6.364  19.567  -2.023  1.00 61.00           C
ATOM   2487  CE1 HIS A 322       4.978  20.229  -0.451  1.00 60.61           C
ATOM   2488  NE2 HIS A 322       5.645  20.627  -1.521  1.00 61.15           N
ATOM   2489  N   GLY A 323       7.567  14.555   1.338  1.00 60.31           N
ATOM   2490  CA  GLY A 323       7.807  13.136   1.524  1.00 60.43           C
ATOM   2491  C   GLY A 323       6.640  12.564   2.312  1.00 60.21           C
ATOM   2492  O   GLY A 323       5.479  12.907   2.034  1.00 60.57           O
ATOM   2493  N   THR A 324       6.933  11.749   3.325  1.00 58.19           N
ATOM   2494  CA  THR A 324       5.879  11.159   4.142  1.00 54.87           C
ATOM   2495  C   THR A 324       6.345  10.852   5.568  1.00 51.51           C
ATOM   2496  O   THR A 324       7.327  10.120   5.775  1.00 52.66           O
ATOM   2497  CB  THR A 324       5.298   9.879   3.483  1.00 52.94           C
ATOM   2498  OG1 THR A 324       4.685  10.222   2.229  1.00 45.64           O
ATOM   2499  CG2 THR A 324       4.247   9.223   4.407  1.00 55.68           C
ATOM   2500  N   ASP A 325       5.669  11.453   6.548  1.00 47.54           N
ATOM   2501  CA  ASP A 325       6.009  11.224   7.942  1.00 43.40           C
ATOM   2502  C   ASP A 325       4.931  10.454   8.693  1.00 38.27           C
ATOM   2503  O   ASP A 325       3.743  10.530   8.367  1.00 36.00           O
ATOM   2504  CB  ASP A 325       6.369  12.534   8.672  1.00 47.14           C
ATOM   2505  CG  ASP A 325       5.254  13.571   8.647  1.00 46.84           C
ATOM   2506  OD1 ASP A 325       4.158  13.288   8.135  1.00 47.80           O
ATOM   2507  OD2 ASP A 325       5.492  14.692   9.147  1.00 45.94           O
ATOM   2508  N   SER A 326       5.366   9.734   9.719  1.00 33.62           N
ATOM   2509  CA  SER A 326       4.492   8.917  10.553  1.00 28.35           C
ATOM   2510  C   SER A 326       3.207   9.603  11.013  1.00 23.65           C
ATOM   2511  O   SER A 326       2.165   8.974  11.052  1.00 22.75           O
ATOM   2512  CB  SER A 326       5.264   8.428  11.777  1.00 27.31           C
ATOM   2513  OG  SER A 326       6.425   7.714  11.390  1.00 33.43           O
ATOM   2514  N   ARG A 327       3.284  10.887  11.360  1.00 21.18           N
ATOM   2515  CA  ARG A 327       2.112  11.607  11.849  1.00 18.47           C
ATOM   2516  C   ARG A 327       0.934  11.594  10.889  1.00 19.42           C
ATOM   2517  O   ARG A 327      -0.206  11.405  11.306  1.00 18.99           O
ATOM   2518  CB  ARG A 327       2.472  13.042  12.214  1.00 18.95           C
ATOM   2519  CG  ARG A 327       3.398  13.161  13.418  1.00 29.25           C
ATOM   2520  CD  ARG A 327       2.643  13.178  14.733  1.00 23.31           C
ATOM   2521  NE  ARG A 327       1.797  14.357  14.825  1.00 27.69           N
ATOM   2522  CZ  ARG A 327       0.470  14.312  14.900  1.00 40.41           C
ATOM   2523  NH1 ARG A 327      -0.159  13.143  14.911  1.00 42.67           N
ATOM   2524  NH2 ARG A 327      -0.232  15.437  14.889  1.00 39.67           N
ATOM   2525  N   VAL A 328       1.205  11.775   9.600  1.00 21.82           N
ATOM   2526  CA  VAL A 328       0.135  11.783   8.616  1.00 22.65           C
ATOM   2527  C   VAL A 328      -0.440  10.381   8.480  1.00 19.73           C
ATOM   2528  O   VAL A 328      -1.657  10.210   8.432  1.00 18.84           O
ATOM   2529  CB  VAL A 328       0.603  12.358   7.241  1.00 25.27           C
ATOM   2530  CG1 VAL A 328       1.590  11.421   6.568  1.00 25.86           C
ATOM   2531  CG2 VAL A 328      -0.597  12.629   6.339  1.00 25.53           C
ATOM   2532  N   ASP A 726       0.424   9.369   8.493  1.00 18.25           N
ATOM   2533  CA  ASP A 726      -0.061   7.998   8.385  1.00 17.89           C
ATOM   2534  C   ASP A 726      -0.970   7.696   9.568  1.00 16.71           C
ATOM   2535  O   ASP A 726      -2.075   7.164   9.394  1.00 16.64           O
ATOM   2536  CB  ASP A 726       1.095   7.002   8.316  1.00 22.02           C
ATOM   2537  CG  ASP A 726       1.848   7.057   6.976  1.00 32.78           C
ATOM   2538  OD1 ASP A 726       1.303   7.599   5.986  1.00 34.86           O
ATOM   2539  OD2 ASP A 726       2.986   6.549   6.913  1.00 32.71           O
ATOM   2540  N   GLU A 727      -0.543   8.115  10.762  1.00 15.74           N
ATOM   2541  CA  GLU A 727      -1.336   7.897  11.970  1.00 14.03           C
ATOM   2542  C   GLU A 727      -2.700   8.566  11.816  1.00 12.08           C
ATOM   2543  O   GLU A 727      -3.758   7.973  12.111  1.00 12.10           O
ATOM   2544  CB  GLU A 727      -0.592   8.469  13.192  1.00 16.17           C
ATOM   2545  CG  GLU A 727       0.552   7.588  13.663  1.00 17.13           C
ATOM   2546  CD  GLU A 727       1.550   8.300  14.569  1.00 18.81           C
ATOM   2547  OE1 GLU A 727       2.661   7.757  14.713  1.00 34.21           O
ATOM   2548  OE2 GLU A 727       1.225   9.362  15.154  1.00 19.60           O
HETATM 2549  N   MSE A 728      -2.678   9.815  11.372  1.00 10.60           N
HETATM 2550  CA  MSE A 728      -3.928  10.545  11.188  1.00 11.55           C
HETATM 2551  C   MSE A 728      -4.828   9.936  10.112  1.00 12.31           C
HETATM 2552  O   MSE A 728      -6.034   9.849  10.307  1.00 12.16           O
HETATM 2553  CB  MSE A 728      -3.674  12.037  10.908  1.00  9.90           C
HETATM 2554  CG  MSE A 728      -3.223  12.828  12.148  1.00  9.44           C
HETATM 2555 SE   MSE A 728      -2.920  14.606  11.782  1.00  7.08          Se
HETATM 2556  CE  MSE A 728      -1.468  14.436  10.957  1.00  8.21           C
ATOM   2557  N   LEU A 729      -4.249   9.493   8.996  1.00 12.11           N
ATOM   2558  CA  LEU A 729      -5.052   8.899   7.935  1.00 11.78           C
ATOM   2559  C   LEU A 729      -5.641   7.572   8.387  1.00 11.17           C
ATOM   2560  O   LEU A 729      -6.738   7.214   7.976  1.00 11.82           O
ATOM   2561  CB  LEU A 729      -4.249   8.723   6.637  1.00 12.85           C
ATOM   2562  CG  LEU A 729      -3.936  10.000   5.835  1.00 13.08           C
ATOM   2563  CD1 LEU A 729      -3.467   9.619   4.447  1.00 14.04           C
ATOM   2564  CD2 LEU A 729      -5.190  10.873   5.716  1.00 13.23           C
ATOM   2565  N   ARG A 730      -4.947   6.877   9.284  1.00 10.51           N
ATOM   2566  CA  ARG A 730      -5.444   5.604   9.802  1.00 10.02           C
ATOM   2567  C   ARG A 730      -6.735   5.852  10.589  1.00  9.24           C
ATOM   2568  O   ARG A 730      -7.740   5.154  10.393  1.00 10.39           O
ATOM   2569  CB  ARG A 730      -4.411   4.932  10.699  1.00 10.91           C
ATOM   2570  CG  ARG A 730      -4.814   3.526  11.170  1.00  8.35           C
ATOM   2571  CD  ARG A 730      -3.768   2.979  12.141  1.00 11.02           C
ATOM   2572  NE  ARG A 730      -4.141   1.675  12.694  1.00 15.78           N
ATOM   2573  CZ  ARG A 730      -3.340   0.938  13.454  1.00 14.85           C
ATOM   2574  NH1 ARG A 730      -2.122   1.375  13.748  1.00 13.28           N
ATOM   2575  NH2 ARG A 730      -3.748  -0.239  13.913  1.00 19.95           N
HETATM 2576  N   MSE A 731      -6.738   6.881  11.427  1.00  8.13           N
HETATM 2577  CA  MSE A 731      -7.948   7.196  12.185  1.00  8.49           C
HETATM 2578  C   MSE A 731      -9.051   7.624  11.219  1.00  8.83           C
HETATM 2579  O   MSE A 731     -10.212   7.231  11.360  1.00  9.89           O
HETATM 2580  CB  MSE A 731      -7.696   8.317  13.213  1.00  6.36           C
HETATM 2581  CG  MSE A 731      -6.793   7.919  14.411  1.00  4.82           C
HETATM 2582 SE   MSE A 731      -6.660   9.254  15.664  1.00  1.42          Se
HETATM 2583  CE  MSE A 731      -5.500  10.288  14.792  1.00  1.97           C
ATOM   2584  N   TYR A 732      -8.685   8.471  10.262  1.00  8.97           N
ATOM   2585  CA  TYR A 732      -9.622   8.972   9.266  1.00  9.25           C
ATOM   2586  C   TYR A 732     -10.346   7.827   8.520  1.00  9.24           C
ATOM   2587  O   TYR A 732     -11.582   7.776   8.469  1.00  8.49           O
ATOM   2588  CB  TYR A 732      -8.861   9.879   8.279  1.00 10.17           C
ATOM   2589  CG  TYR A 732      -9.636  10.221   7.010  1.00 11.21           C
ATOM   2590  CD1 TYR A 732     -10.641  11.189   7.016  1.00  9.02           C
ATOM   2591  CD2 TYR A 732      -9.355   9.566   5.810  1.00 11.99           C
ATOM   2592  CE1 TYR A 732     -11.347  11.500   5.845  1.00 12.36           C
ATOM   2593  CE2 TYR A 732     -10.051   9.861   4.641  1.00 12.21           C
ATOM   2594  CZ  TYR A 732     -11.034  10.825   4.658  1.00 13.71           C
ATOM   2595  OH  TYR A 732     -11.673  11.145   3.474  1.00 19.03           O
ATOM   2596  N   HIS A 733      -9.587   6.873   8.011  1.00 10.68           N
ATOM   2597  CA  HIS A 733     -10.200   5.766   7.275  1.00 13.30           C
ATOM   2598  C   HIS A 733     -11.079   4.918   8.181  1.00 14.73           C
ATOM   2599  O   HIS A 733     -12.174   4.522   7.784  1.00 16.04           O
ATOM   2600  CB  HIS A 733      -9.131   4.889   6.605  1.00 14.14           C
ATOM   2601  CG  HIS A 733      -8.408   5.579   5.490  1.00 15.86           C
ATOM   2602  ND1 HIS A 733      -9.072   6.155   4.426  1.00 16.83           N
ATOM   2603  CD2 HIS A 733      -7.094   5.863   5.312  1.00 16.63           C
ATOM   2604  CE1 HIS A 733      -8.203   6.782   3.651  1.00 16.59           C
ATOM   2605  NE2 HIS A 733      -6.997   6.621   4.167  1.00 17.28           N
ATOM   2606  N   ALA A 734     -10.594   4.643   9.396  1.00 14.26           N
ATOM   2607  CA  ALA A 734     -11.351   3.832  10.342  1.00 12.84           C
ATOM   2608  C   ALA A 734     -12.683   4.500  10.663  1.00 12.36           C
ATOM   2609  O   ALA A 734     -13.720   3.829  10.729  1.00 12.84           O
ATOM   2610  CB  ALA A 734     -10.529   3.587  11.630  1.00 11.93           C
ATOM   2611  N   LEU A 735     -12.670   5.817  10.829  1.00 10.42           N
ATOM   2612  CA  LEU A 735     -13.902   6.544  11.117  1.00 11.00           C
ATOM   2613  C   LEU A 735     -14.880   6.450   9.933  1.00 13.92           C
ATOM   2614  O   LEU A 735     -16.062   6.134  10.109  1.00 15.17           O
ATOM   2615  CB  LEU A 735     -13.592   8.007  11.433  1.00  9.97           C
ATOM   2616  CG  LEU A 735     -13.079   8.216  12.866  1.00  8.47           C
ATOM   2617  CD1 LEU A 735     -12.272   9.503  12.984  1.00  8.75           C
ATOM   2618  CD2 LEU A 735     -14.268   8.240  13.816  1.00  5.64           C
ATOM   2619  N   LYS A 736     -14.385   6.733   8.734  1.00 16.59           N
ATOM   2620  CA  LYS A 736     -15.222   6.657   7.542  1.00 18.85           C
ATOM   2621  C   LYS A 736     -15.832   5.265   7.358  1.00 19.19           C
ATOM   2622  O   LYS A 736     -17.037   5.136   7.132  1.00 20.02           O
ATOM   2623  CB  LYS A 736     -14.405   7.033   6.310  1.00 20.51           C
ATOM   2624  CG  LYS A 736     -14.548   8.475   5.902  1.00 23.98           C
ATOM   2625  CD  LYS A 736     -13.595   8.822   4.771  1.00 35.66           C
ATOM   2626  CE  LYS A 736     -13.786   7.954   3.535  1.00 40.69           C
ATOM   2627  NZ  LYS A 736     -15.134   8.131   2.909  1.00 48.65           N
ATOM   2628  N   GLU A 737     -15.009   4.225   7.465  1.00 19.35           N
ATOM   2629  CA  GLU A 737     -15.501   2.852   7.311  1.00 19.18           C
ATOM   2630  C   GLU A 737     -16.524   2.506   8.382  1.00 19.94           C
ATOM   2631  O   GLU A 737     -17.563   1.903   8.092  1.00 20.65           O
ATOM   2632  CB  GLU A 737     -14.350   1.860   7.354  1.00 18.95           C
ATOM   2633  CG  GLU A 737     -13.467   1.927   6.120  1.00 25.93           C
ATOM   2634  CD  GLU A 737     -12.322   0.940   6.169  1.00 43.64           C
ATOM   2635  OE1 GLU A 737     -11.167   1.360   5.949  1.00 46.06           O
ATOM   2636  OE2 GLU A 737     -12.580  -0.258   6.420  1.00 55.91           O
ATOM   2637  N   ALA A 738     -16.247   2.901   9.622  1.00 20.19           N
ATOM   2638  CA  ALA A 738     -17.181   2.630  10.709  1.00 20.59           C
ATOM   2639  C   ALA A 738     -18.535   3.300  10.427  1.00 21.95           C
ATOM   2640  O   ALA A 738     -19.588   2.663  10.541  1.00 21.66           O
ATOM   2641  CB  ALA A 738     -16.611   3.120  12.025  1.00 20.49           C
ATOM   2642  N   LEU A 739     -18.503   4.570  10.027  1.00 25.62           N
ATOM   2643  CA  LEU A 739     -19.723   5.323   9.735  1.00 27.02           C
ATOM   2644  C   LEU A 739     -20.528   4.731   8.581  1.00 29.43           C
ATOM   2645  O   LEU A 739     -21.757   4.856   8.542  1.00 29.91           O
ATOM   2646  CB  LEU A 739     -19.393   6.790   9.453  1.00 26.50           C
ATOM   2647  CG  LEU A 739     -19.071   7.644  10.683  1.00 25.10           C
ATOM   2648  CD1 LEU A 739     -18.310   8.898  10.275  1.00 25.06           C
ATOM   2649  CD2 LEU A 739     -20.367   8.009  11.401  1.00 23.77           C
ATOM   2650  N   SER A 740     -19.837   4.085   7.645  1.00 33.07           N
ATOM   2651  CA  SER A 740     -20.503   3.469   6.504  1.00 35.67           C
ATOM   2652  C   SER A 740     -21.428   2.354   6.987  1.00 36.38           C
ATOM   2653  O   SER A 740     -22.548   2.212   6.501  1.00 36.87           O
ATOM   2654  CB  SER A 740     -19.468   2.907   5.522  1.00 40.07           C
ATOM   2655  OG  SER A 740     -18.631   3.939   5.021  1.00 45.13           O
ATOM   2656  N   ILE A 741     -20.962   1.581   7.959  1.00 36.41           N
ATOM   2657  CA  ILE A 741     -21.744   0.483   8.503  1.00 37.89           C
ATOM   2658  C   ILE A 741     -22.874   1.000   9.384  1.00 38.25           C
ATOM   2659  O   ILE A 741     -23.977   0.454   9.366  1.00 37.27           O
ATOM   2660  CB  ILE A 741     -20.855  -0.491   9.292  1.00 39.73           C
ATOM   2661  CG1 ILE A 741     -19.925  -1.231   8.332  1.00 45.23           C
ATOM   2662  CG2 ILE A 741     -21.706  -1.513  10.040  1.00 40.40           C
ATOM   2663  CD1 ILE A 741     -20.606  -2.354   7.569  1.00 49.87           C
ATOM   2664  N   ILE A 742     -22.591   2.041  10.167  1.00 39.97           N
ATOM   2665  CA  ILE A 742     -23.597   2.649  11.036  1.00 41.18           C
ATOM   2666  C   ILE A 742     -24.478   3.541  10.147  1.00 43.57           C
ATOM   2667  O   ILE A 742     -24.527   4.763  10.326  1.00 44.82           O
ATOM   2668  CB  ILE A 742     -22.924   3.507  12.141  1.00 40.19           C
ATOM   2669  CG1 ILE A 742     -21.902   2.670  12.908  1.00 39.75           C
ATOM   2670  CG2 ILE A 742     -23.960   4.009  13.136  1.00 40.57           C
ATOM   2671  CD1 ILE A 742     -21.177   3.444  13.983  1.00 40.67           C
ATOM   2672  N   GLY A 743     -25.150   2.921   9.176  1.00 45.66           N
ATOM   2673  CA  GLY A 743     -25.997   3.647   8.240  1.00 47.12           C
ATOM   2674  C   GLY A 743     -26.909   4.679   8.870  1.00 49.13           C
ATOM   2675  O   GLY A 743     -28.009   4.354   9.317  1.00 50.63           O
TER    2676      GLY A 743
HETATM 2677  PB  GDP A1744      -7.655 -10.725  39.831  1.00  3.96           P
HETATM 2678  O1B GDP A1744      -7.646 -10.666  38.356  1.00  3.81           O
HETATM 2679  O2B GDP A1744      -8.706  -9.999  40.542  1.00  3.95           O
HETATM 2680  O3B GDP A1744      -6.439 -10.268  40.561  1.00  4.05           O
HETATM 2681  O3A GDP A1744      -8.074 -12.208  40.288  1.00  4.71           O
HETATM 2682  PA  GDP A1744      -7.351 -13.487  39.647  1.00  5.53           P
HETATM 2683  O1A GDP A1744      -8.256 -13.886  38.551  1.00  5.97           O
HETATM 2684  O2A GDP A1744      -5.911 -13.313  39.365  1.00  5.88           O
HETATM 2685  O5' GDP A1744      -7.435 -14.658  40.725  1.00  5.52           O
HETATM 2686  C5' GDP A1744      -6.907 -14.444  42.027  1.00  5.56           C
HETATM 2687  C4' GDP A1744      -6.715 -15.747  42.743  1.00  5.44           C
HETATM 2688  O4' GDP A1744      -7.999 -16.236  43.215  1.00  5.47           O
HETATM 2689  C3' GDP A1744      -6.093 -16.869  41.923  1.00  5.50           C
HETATM 2690  O3' GDP A1744      -5.237 -17.624  42.773  1.00  5.58           O
HETATM 2691  C2' GDP A1744      -7.313 -17.684  41.485  1.00  5.39           C
HETATM 2692  O2' GDP A1744      -7.002 -19.058  41.305  1.00  5.40           O
HETATM 2693  C1' GDP A1744      -8.237 -17.523  42.691  1.00  5.05           C
HETATM 2694  N9  GDP A1744      -9.661 -17.606  42.391  1.00  4.21           N
HETATM 2695  C8  GDP A1744     -10.382 -16.788  41.541  1.00  3.97           C
HETATM 2696  N7  GDP A1744     -11.655 -17.089  41.509  1.00  3.97           N
HETATM 2697  C5  GDP A1744     -11.778 -18.167  42.378  1.00  4.22           C
HETATM 2698  C6  GDP A1744     -12.919 -18.930  42.740  1.00  4.10           C
HETATM 2699  O6  GDP A1744     -14.083 -18.787  42.377  1.00  4.06           O
HETATM 2700  N1  GDP A1744     -12.594 -19.954  43.618  1.00  3.89           N
HETATM 2701  C2  GDP A1744     -11.335 -20.216  44.097  1.00  3.74           C
HETATM 2702  N2  GDP A1744     -11.215 -21.283  44.907  1.00  3.84           N
HETATM 2703  N3  GDP A1744     -10.268 -19.497  43.789  1.00  4.00           N
HETATM 2704  C4  GDP A1744     -10.558 -18.502  42.924  1.00  4.09           C
HETATM 2705 AL   ALF A1745      -5.297  -8.619  40.342  1.00 14.96          Al
HETATM 2706  F1  ALF A1745      -3.835  -9.613  39.966  1.00 15.40           F
HETATM 2707  F2  ALF A1745      -6.722  -7.593  40.814  1.00 14.99           F
HETATM 2708  F3  ALF A1745      -4.837  -8.773  42.057  1.00 15.59           F
HETATM 2709  F4  ALF A1745      -5.699  -8.588  38.601  1.00 15.28           F
HETATM 2710 MG   MG  A1746      -6.251  -9.724  37.200  1.00  5.68          Mg
HETATM 2711 NA   NA  A1747      -4.141 -11.129  42.200  1.00  8.57          Na
HETATM 2712  O   HOH A2001     -23.303  -7.812   9.649  1.00 25.52           O
HETATM 2713  O   HOH A2002     -16.481 -10.164  12.693  1.00 40.15           O
HETATM 2714  O   HOH A2003     -18.337  -5.885   9.396  1.00 29.50           O
HETATM 2715  O   HOH A2004     -13.566  -2.721  20.327  1.00 11.68           O
HETATM 2716  O   HOH A2005     -14.160  -7.277  19.665  1.00 37.98           O
HETATM 2717  O   HOH A2006     -11.789  -6.928  14.448  1.00 23.00           O
HETATM 2718  O   HOH A2007      -8.088   2.257  26.024  1.00  8.42           O
HETATM 2719  O   HOH A2008      -7.104   0.836  12.192  1.00 12.05           O
HETATM 2720  O   HOH A2009     -10.899   9.282  29.048  1.00 18.94           O
HETATM 2721  O   HOH A2010      -7.120   4.060  28.126  1.00 19.46           O
HETATM 2722  O   HOH A2011      -6.738   9.329  29.461  1.00 41.38           O
HETATM 2723  O   HOH A2012     -16.323  10.028  27.728  1.00 26.92           O
HETATM 2724  O   HOH A2013     -11.525   3.317  23.110  1.00  1.00           O
HETATM 2725  O   HOH A2014      -7.369  -1.162  20.557  1.00 17.27           O
HETATM 2726  O   HOH A2015      -3.294   5.814  14.295  1.00 10.72           O
HETATM 2727  O   HOH A2016      -6.036   1.357  24.372  1.00 26.40           O
HETATM 2728  O   HOH A2017      -3.466   2.465  23.929  1.00 34.72           O
HETATM 2729  O   HOH A2018       1.427 -13.725  47.335  1.00 26.97           O
HETATM 2730  O   HOH A2019      -1.137  11.294  20.009  1.00 17.60           O
HETATM 2731  O   HOH A2020       0.596   6.572  22.675  1.00 41.82           O
HETATM 2732  O   HOH A2021      -2.264   8.485  26.241  1.00 21.30           O
HETATM 2733  O   HOH A2022      -4.936   5.639  25.349  1.00 31.22           O
HETATM 2734  O   HOH A2023     -12.375  11.019  27.587  1.00 25.71           O
HETATM 2735  O   HOH A2024      -7.189   7.264  27.130  1.00 16.07           O
HETATM 2736  O   HOH A2025      -6.289   9.187  25.386  1.00 19.95           O
HETATM 2737  O   HOH A2026     -16.534  10.576  23.450  1.00 32.54           O
HETATM 2738  O   HOH A2027      -7.552  14.165  24.225  1.00 31.91           O
HETATM 2739  O   HOH A2028      -6.792  13.574  21.785  1.00 47.70           O
HETATM 2740  O   HOH A2029     -16.252  10.133  20.960  1.00 43.58           O
HETATM 2741  O   HOH A2030       2.997 -12.061  38.534  1.00 37.39           O
HETATM 2742  O   HOH A2031     -14.727   9.695  25.541  1.00 20.11           O
HETATM 2743  O   HOH A2032     -18.805   9.253  27.970  1.00 21.98           O
HETATM 2744  O   HOH A2033     -16.732   7.681  20.298  1.00 11.32           O
HETATM 2745  O   HOH A2034     -16.281   3.528  26.442  1.00  7.79           O
HETATM 2746  O   HOH A2035     -13.908   4.156  24.497  1.00 10.42           O
HETATM 2747  O   HOH A2036     -16.134  -1.352  20.980  1.00 21.05           O
HETATM 2748  O   HOH A2037     -14.478   2.739  28.493  1.00 11.24           O
HETATM 2749  O   HOH A2038     -10.750   2.057  25.727  1.00  7.33           O
HETATM 2750  O   HOH A2039     -12.747  -7.374  46.282  1.00 46.81           O
HETATM 2751  O   HOH A2040      -0.722  -4.576  45.728  1.00  6.37           O
HETATM 2752  O   HOH A2041       0.020  -7.050  46.761  1.00 15.75           O
HETATM 2753  O   HOH A2042     -10.715  -9.092  46.634  1.00 13.41           O
HETATM 2754  O   HOH A2043       7.076 -11.885  38.949  1.00 45.94           O
HETATM 2755  O   HOH A2044     -16.910 -15.540  32.958  1.00  8.68           O
HETATM 2756  O   HOH A2045       2.204 -11.148  47.795  1.00 30.99           O
HETATM 2757  O   HOH A2046     -10.223 -18.681  34.514  1.00 14.76           O
HETATM 2758  O   HOH A2047      -4.325 -18.228  32.918  1.00 11.11           O
HETATM 2759  O   HOH A2048     -13.245 -21.569  34.752  1.00 10.94           O
HETATM 2760  O   HOH A2049     -15.748 -20.788  29.504  1.00 23.43           O
HETATM 2761  O   HOH A2050     -16.399 -16.964  35.302  1.00  6.88           O
HETATM 2762  O   HOH A2051     -16.009 -19.283  24.987  1.00 29.28           O
HETATM 2763  O   HOH A2052     -17.140 -15.389  24.731  1.00 12.27           O
HETATM 2764  O   HOH A2053     -11.716 -22.112  23.760  1.00 35.38           O
HETATM 2765  O   HOH A2054     -12.682 -24.349  27.262  1.00 32.58           O
HETATM 2766  O   HOH A2055      -5.896 -25.803  29.642  1.00 31.21           O
HETATM 2767  O   HOH A2056      -4.676 -21.991  34.467  1.00 28.67           O
HETATM 2768  O   HOH A2057      -5.528 -23.456  27.877  1.00 18.81           O
HETATM 2769  O   HOH A2058      -0.650 -16.572  35.457  1.00 15.38           O
HETATM 2770  O   HOH A2059       0.987 -15.137  37.172  1.00 22.60           O
HETATM 2771  O   HOH A2060      -1.124 -18.495  38.515  1.00 23.76           O
HETATM 2772  O   HOH A2061      -6.509 -15.078  46.126  1.00 24.94           O
HETATM 2773  O   HOH A2062       0.318 -15.277  42.651  1.00 27.13           O
HETATM 2774  O   HOH A2063      -4.815 -16.559  48.333  1.00 45.36           O
HETATM 2775  O   HOH A2064     -10.091   2.172  45.742  1.00 27.62           O
HETATM 2776  O   HOH A2065      -2.858   8.134  49.977  1.00 33.30           O
HETATM 2777  O   HOH A2066       1.681   6.386  36.080  1.00 33.93           O
HETATM 2778  O   HOH A2067       3.240  -9.556  39.344  1.00 17.13           O
HETATM 2779  O   HOH A2068     -12.410  10.596  40.039  1.00 25.16           O
HETATM 2780  O   HOH A2069      -0.773  -9.454  34.040  1.00  7.17           O
HETATM 2781  O   HOH A2070       1.402 -10.314  35.246  1.00 15.51           O
HETATM 2782  O   HOH A2071      -4.151  -6.909  40.160  1.00 15.10           O
HETATM 2783  O   HOH A2072      -3.413 -10.353  34.273  1.00  4.19           O
HETATM 2784  O   HOH A2073     -26.506   3.767  31.232  1.00 41.69           O
HETATM 2785  O   HOH A2074     -25.836   6.527  27.814  1.00 29.49           O
HETATM 2786  O   HOH A2075      -3.151  -6.714  31.835  1.00  5.06           O
HETATM 2787  O   HOH A2076      -7.390  -3.869  21.994  1.00 16.60           O
HETATM 2788  O   HOH A2077      -6.595  -4.905  19.610  1.00 14.46           O
HETATM 2789  O   HOH A2078     -13.111   9.186  50.605  1.00 17.53           O
HETATM 2790  O   HOH A2079     -15.362 -13.830  11.562  1.00 47.45           O
HETATM 2791  O   HOH A2080     -14.275 -23.476  13.264  1.00 33.01           O
HETATM 2792  O   HOH A2081      -5.958 -22.399  16.008  1.00 33.23           O
HETATM 2793  O   HOH A2082     -14.681 -25.678  41.600  1.00 10.24           O
HETATM 2794  O   HOH A2083      -4.370  -6.396  18.606  1.00 14.33           O
HETATM 2795  O   HOH A2084      -6.004 -10.763  11.942  1.00 21.24           O
HETATM 2796  O   HOH A2085      -0.676  -6.787  15.515  1.00 19.43           O
HETATM 2797  O   HOH A2086       0.670  -9.908  17.675  1.00 12.30           O
HETATM 2798  O   HOH A2087       0.849   0.064  17.682  1.00 27.03           O
HETATM 2799  O   HOH A2088      -0.426  -3.976  23.040  1.00 11.58           O
HETATM 2800  O   HOH A2089     -29.153  -0.911  49.374  1.00 38.05           O
HETATM 2801  O   HOH A2090      -0.066  -8.969  13.785  1.00 27.61           O
HETATM 2802  O   HOH A2091       3.261 -14.893  13.202  1.00 30.41           O
HETATM 2803  O   HOH A2092      -7.515 -28.220  46.510  1.00 36.88           O
HETATM 2804  O   HOH A2093      -7.530 -32.023  40.842  1.00 34.78           O
HETATM 2805  O   HOH A2094       3.178 -24.167  20.904  1.00 42.84           O
HETATM 2806  O   HOH A2095       3.477 -23.926  25.292  1.00 23.60           O
HETATM 2807  O   HOH A2096      -1.976 -29.104  30.550  1.00 27.29           O
HETATM 2808  O   HOH A2097     -14.111 -31.940  31.991  1.00 12.55           O
HETATM 2809  O   HOH A2098      -7.823 -32.088  35.943  1.00 24.98           O
HETATM 2810  O   HOH A2099       5.668 -21.630  30.118  1.00 47.22           O
HETATM 2811  O   HOH A2100     -13.647 -33.037  34.499  1.00 19.94           O
HETATM 2812  O   HOH A2101       5.337 -15.067  24.345  1.00 15.07           O
HETATM 2813  O   HOH A2102     -16.826 -26.672  43.599  1.00 20.19           O
HETATM 2814  O   HOH A2103     -20.022 -29.352  44.865  1.00 13.35           O
HETATM 2815  O   HOH A2104     -23.320 -23.651  34.610  1.00 13.03           O
HETATM 2816  O   HOH A2105     -27.537 -25.799  35.910  1.00 21.84           O
HETATM 2817  O   HOH A2106       5.138 -17.321  33.877  1.00 39.10           O
HETATM 2818  O   HOH A2107     -22.900 -27.382  50.095  1.00 37.79           O
HETATM 2819  O   HOH A2108       8.117 -10.104  24.664  1.00 47.85           O
HETATM 2820  O   HOH A2109       2.185 -12.772  36.224  1.00 15.29           O
HETATM 2821  O   HOH A2110       9.763  -7.909  29.707  1.00 14.58           O
HETATM 2822  O   HOH A2111     -25.519 -19.849  27.357  1.00 18.19           O
HETATM 2823  O   HOH A2112     -22.541 -17.015  25.314  1.00 20.82           O
HETATM 2824  O   HOH A2113     -20.890 -20.487  27.014  1.00 24.82           O
HETATM 2825  O   HOH A2114       7.072  -7.042  25.331  1.00 18.47           O
HETATM 2826  O   HOH A2115       1.718  -2.263  25.247  1.00 29.65           O
HETATM 2827  O   HOH A2116     -24.963 -15.883  24.214  1.00 23.61           O
HETATM 2828  O   HOH A2117      -0.809  -6.797  33.580  1.00  6.43           O
HETATM 2829  O   HOH A2118       8.580 -11.384  32.067  1.00 31.95           O
HETATM 2830  O   HOH A2119       6.343  -9.351  37.583  1.00 39.30           O
HETATM 2831  O   HOH A2120     -32.995 -10.339  30.333  1.00 39.91           O
HETATM 2832  O   HOH A2121      10.357  -0.726  33.049  1.00 38.81           O
HETATM 2833  O   HOH A2122     -28.710  10.009  21.491  1.00 33.11           O
HETATM 2834  O   HOH A2123     -28.753   7.520  13.518  1.00 28.17           O
HETATM 2835  O   HOH A2124     -20.604  16.245  10.088  1.00 38.65           O
HETATM 2836  O   HOH A2125       2.058  -8.866  45.762  1.00  1.60           O
HETATM 2837  O   HOH A2126       2.606  -9.939  43.173  1.00 29.08           O
HETATM 2838  O   HOH A2127      -0.213  20.105  13.216  1.00 18.90           O
HETATM 2839  O   HOH A2128       2.954   2.027  40.605  1.00 18.73           O
HETATM 2840  O   HOH A2129       3.650   4.020  32.424  1.00 25.64           O
HETATM 2841  O   HOH A2130      -5.638   3.812  30.273  1.00 13.43           O
HETATM 2842  O   HOH A2131      -0.850  -1.138  22.235  1.00 18.71           O
HETATM 2843  O   HOH A2132     -11.420  -8.733  12.321  1.00 26.85           O
HETATM 2844  O   HOH A2133     -20.568 -15.644  19.165  1.00 24.96           O
HETATM 2845  O   HOH A2134     -21.905 -12.068  19.109  1.00 36.26           O
HETATM 2846  O   HOH A2135     -17.425 -12.132  14.114  1.00 22.19           O
HETATM 2847  O   HOH A2136     -17.739  -4.498  22.810  1.00 10.19           O
HETATM 2848  O   HOH A2137     -16.267  -5.623  20.330  1.00 40.77           O
HETATM 2849  O   HOH A2138      -4.640  -9.096  32.073  1.00  8.39           O
HETATM 2850  O   HOH A2139      -7.532  -8.138  36.880  1.00  5.95           O
HETATM 2851  O   HOH A2140     -10.471  -3.527  38.912  1.00  6.34           O
HETATM 2852  O   HOH A2141      -4.333  -5.066  42.164  1.00  7.12           O
HETATM 2853  O   HOH A2142      -4.132   3.811  50.770  1.00 10.38           O
HETATM 2854  O   HOH A2143      -1.253  -2.092  47.292  1.00  7.21           O
HETATM 2855  O   HOH A2144      -2.510   4.097  48.715  1.00 15.41           O
HETATM 2856  O   HOH A2145      -0.089   5.024  51.969  1.00 28.47           O
HETATM 2857  O   HOH A2146      -0.247   9.701  41.310  1.00 42.58           O
HETATM 2858  O   HOH A2147      -7.412   1.248  44.848  1.00 10.61           O
HETATM 2859  O   HOH A2148     -10.099   4.827  46.944  1.00 17.71           O
HETATM 2860  O   HOH A2149      -4.621   7.095  47.726  1.00 23.45           O
HETATM 2861  O   HOH A2150      -0.385   5.716  37.721  1.00 18.60           O
HETATM 2862  O   HOH A2151      -3.119   5.361  37.123  1.00 12.68           O
HETATM 2863  O   HOH A2152      -7.628  -0.294  38.079  1.00 24.37           O
HETATM 2864  O   HOH A2153      -9.175   7.986  42.120  1.00 28.80           O
HETATM 2865  O   HOH A2154      -3.170   8.830  38.724  1.00 39.29           O
HETATM 2866  O   HOH A2155      -4.551   6.924  35.551  1.00 28.18           O
HETATM 2867  O   HOH A2156      -9.966   9.533  39.478  1.00 19.32           O
HETATM 2868  O   HOH A2157      -7.553  12.458  38.827  1.00 39.38           O
HETATM 2869  O   HOH A2158      -6.832   4.507  32.681  1.00 26.20           O
HETATM 2870  O   HOH A2159     -12.712   8.843  30.961  1.00 17.10           O
HETATM 2871  O   HOH A2160     -11.952  10.684  33.093  1.00 23.57           O
HETATM 2872  O   HOH A2161      -9.792   4.701  29.153  1.00  7.38           O
HETATM 2873  O   HOH A2162      -9.849   7.042  27.595  1.00 18.16           O
HETATM 2874  O   HOH A2163     -11.932   3.713  27.517  1.00 14.11           O
HETATM 2875  O   HOH A2164     -24.578   5.251  29.900  1.00 18.95           O
HETATM 2876  O   HOH A2165     -24.215   6.850  25.580  1.00 28.24           O
HETATM 2877  O   HOH A2166     -23.026   6.743  22.259  1.00 20.51           O
HETATM 2878  O   HOH A2167     -20.341  -7.829  42.950  1.00 10.79           O
HETATM 2879  O   HOH A2168     -14.595  -5.896  44.788  1.00  7.54           O
HETATM 2880  O   HOH A2169     -20.559 -13.088  50.730  1.00 22.35           O
HETATM 2881  O   HOH A2170     -17.935 -14.112  53.531  1.00 21.81           O
HETATM 2882  O   HOH A2171     -12.464 -12.172  54.024  1.00 13.76           O
HETATM 2883  O   HOH A2172     -11.644 -12.437  49.859  1.00  8.10           O
HETATM 2884  O   HOH A2173      -9.859 -15.765  48.827  1.00  8.34           O
HETATM 2885  O   HOH A2174     -12.203  -9.328  53.325  1.00 17.01           O
HETATM 2886  O   HOH A2175     -20.355 -13.088  54.039  1.00 19.61           O
HETATM 2887  O   HOH A2176     -16.987  -8.335  49.258  1.00 24.22           O
HETATM 2888  O   HOH A2177     -17.136 -12.652  55.899  1.00 26.52           O
HETATM 2889  O   HOH A2178     -15.679 -10.237  55.591  1.00 12.12           O
HETATM 2890  O   HOH A2179     -22.053 -10.862  52.139  1.00 22.61           O
HETATM 2891  O   HOH A2180     -22.336  -7.367  53.990  1.00  7.50           O
HETATM 2892  O   HOH A2181     -10.849  -5.598  48.750  1.00 29.73           O
HETATM 2893  O   HOH A2182     -14.391   1.353  45.677  1.00  8.96           O
HETATM 2894  O   HOH A2183     -12.103   0.979  47.118  1.00 18.69           O
HETATM 2895  O   HOH A2184      -9.053  -3.251  48.481  1.00 13.45           O
HETATM 2896  O   HOH A2185     -14.949   7.639  49.216  1.00 14.63           O
HETATM 2897  O   HOH A2186     -20.744   4.500  46.409  1.00  8.26           O
HETATM 2898  O   HOH A2187     -12.687   5.015  47.252  1.00 29.67           O
HETATM 2899  O   HOH A2188     -22.249   6.546  45.384  1.00 42.83           O
HETATM 2900  O   HOH A2189     -26.555   0.437  41.900  1.00 27.98           O
HETATM 2901  O   HOH A2190     -14.584   7.582  46.585  1.00 15.10           O
HETATM 2902  O   HOH A2191     -21.907   9.431  38.620  1.00 36.08           O
HETATM 2903  O   HOH A2192     -14.369   3.988  45.166  1.00 16.31           O
HETATM 2904  O   HOH A2193     -17.932   9.472  40.050  1.00 34.89           O
HETATM 2905  O   HOH A2194     -23.578   8.580  36.142  1.00 30.95           O
HETATM 2906  O   HOH A2195     -19.725   8.117  35.263  1.00 20.22           O
HETATM 2907  O   HOH A2196     -23.990   0.751  40.121  1.00 10.50           O
HETATM 2908  O   HOH A2197     -26.804   5.546  36.993  1.00 21.92           O
HETATM 2909  O   HOH A2198     -25.553   4.984  33.896  1.00 31.00           O
HETATM 2910  O   HOH A2199     -26.886   3.738  44.735  1.00 23.88           O
HETATM 2911  O   HOH A2200     -32.059   1.215  39.814  1.00 45.33           O
HETATM 2912  O   HOH A2201     -23.193   6.876  33.841  1.00 28.61           O
HETATM 2913  O   HOH A2202     -10.430 -12.183  47.432  1.00 21.73           O
HETATM 2914  O   HOH A2203      -8.670 -17.411  45.883  1.00 45.43           O
HETATM 2915  O   HOH A2204     -18.237 -23.220  50.049  1.00 38.55           O
HETATM 2916  O   HOH A2205     -13.328 -24.506  50.964  1.00 44.95           O
HETATM 2917  O   HOH A2206     -12.748 -23.776  42.761  1.00  7.65           O
HETATM 2918  O   HOH A2207     -12.727 -25.379  46.246  1.00 22.84           O
HETATM 2919  O   HOH A2208     -12.171 -18.272  52.148  1.00 10.72           O
HETATM 2920  O   HOH A2209     -12.569 -22.364  52.442  1.00 25.91           O
HETATM 2921  O   HOH A2210     -19.240 -23.289  52.864  1.00 17.98           O
HETATM 2922  O   HOH A2211     -15.045 -23.278  57.858  1.00  8.45           O
HETATM 2923  O   HOH A2212     -16.796 -16.788  54.290  1.00  1.00           O
HETATM 2924  O   HOH A2213     -18.343 -16.872  58.768  1.00 13.10           O
HETATM 2925  O   HOH A2214     -17.419 -30.664  57.770  1.00 36.39           O
HETATM 2926  O   HOH A2215     -21.292 -24.707  55.110  1.00 34.36           O
HETATM 2927  O   HOH A2216     -21.392 -22.226  51.583  1.00 13.17           O
HETATM 2928  O   HOH A2217     -25.216 -22.645  55.217  1.00 23.95           O
HETATM 2929  O   HOH A2218     -24.654 -17.074  55.990  1.00 14.52           O
HETATM 2930  O   HOH A2219     -29.387 -19.681  53.361  1.00 18.53           O
HETATM 2931  O   HOH A2220     -23.103 -13.331  52.343  1.00 37.40           O
HETATM 2932  O   HOH A2221     -27.273 -15.587  53.000  1.00 21.81           O
HETATM 2933  O   HOH A2222     -33.217 -21.429  50.242  1.00 19.07           O
HETATM 2934  O   HOH A2223     -32.746 -14.033  50.999  1.00 34.59           O
HETATM 2935  O   HOH A2224     -25.692 -13.441  52.037  1.00 18.78           O
HETATM 2936  O   HOH A2225     -27.788  -8.676  46.874  1.00 15.63           O
HETATM 2937  O   HOH A2226     -30.264 -14.485  40.814  1.00 28.36           O
HETATM 2938  O   HOH A2227     -35.027 -16.734  44.910  1.00 33.99           O
HETATM 2939  O   HOH A2228     -34.256  -7.396  44.956  1.00 28.05           O
HETATM 2940  O   HOH A2229     -33.813  -5.952  49.829  1.00 29.47           O
HETATM 2941  O   HOH A2230     -29.666  -3.339  51.281  1.00 14.22           O
HETATM 2942  O   HOH A2231     -29.827  -1.059  46.319  1.00 23.91           O
HETATM 2943  O   HOH A2232     -28.861  -0.755  41.084  1.00  9.17           O
HETATM 2944  O   HOH A2233     -30.509  -8.223  34.809  1.00 34.13           O
HETATM 2945  O   HOH A2234     -27.474  -3.160  38.324  1.00 10.23           O
HETATM 2946  O   HOH A2235     -32.287  -5.827  33.794  1.00 35.93           O
HETATM 2947  O   HOH A2236     -29.733 -11.363  40.994  1.00 27.93           O
HETATM 2948  O   HOH A2237     -28.683 -14.471  38.719  1.00 11.77           O
HETATM 2949  O   HOH A2238     -15.772 -21.703  36.165  1.00 26.40           O
HETATM 2950  O   HOH A2239      -9.411 -18.984  38.707  1.00 15.97           O
HETATM 2951  O   HOH A2240     -11.063 -20.694  36.117  1.00  5.95           O
HETATM 2952  O   HOH A2241      -9.016 -26.170  45.529  1.00 10.43           O
HETATM 2953  O   HOH A2242      -2.514 -17.523  44.230  1.00 21.79           O
HETATM 2954  O   HOH A2243     -12.231 -25.860  39.484  1.00 14.73           O
HETATM 2955  O   HOH A2244     -11.376 -26.396  43.771  1.00 15.61           O
HETATM 2956  O   HOH A2245      -6.870 -28.737  43.039  1.00 31.81           O
HETATM 2957  O   HOH A2246      -3.002 -33.057  37.394  1.00 31.44           O
HETATM 2958  O   HOH A2247      -4.354 -27.289  31.209  1.00 45.02           O
HETATM 2959  O   HOH A2248     -13.309 -27.942  41.882  1.00 18.29           O
HETATM 2960  O   HOH A2249      -4.447 -25.024  34.900  1.00 43.54           O
HETATM 2961  O   HOH A2250     -10.427 -29.489  41.612  1.00 18.09           O
HETATM 2962  O   HOH A2251     -13.615 -31.288  39.613  1.00 41.56           O
HETATM 2963  O   HOH A2252      -8.329 -30.554  33.459  1.00 23.75           O
HETATM 2964  O   HOH A2253     -11.759 -31.088  31.038  1.00 17.72           O
HETATM 2965  O   HOH A2254      -8.228 -24.262  30.085  1.00 14.93           O
HETATM 2966  O   HOH A2255     -15.759 -25.900  27.707  1.00 23.85           O
HETATM 2967  O   HOH A2256     -10.880 -26.486  28.766  1.00 28.67           O
HETATM 2968  O   HOH A2257     -17.586 -28.872  31.274  1.00  7.83           O
HETATM 2969  O   HOH A2258     -14.167 -30.941  37.048  1.00 24.36           O
HETATM 2970  O   HOH A2259     -15.024 -24.516  39.124  1.00  9.97           O
HETATM 2971  O   HOH A2260     -21.053 -25.706  32.352  1.00 13.42           O
HETATM 2972  O   HOH A2261     -18.505 -28.833  42.487  1.00 19.68           O
HETATM 2973  O   HOH A2262     -20.527 -24.178  34.498  1.00  3.45           O
HETATM 2974  O   HOH A2263     -25.705 -25.493  37.899  1.00 16.49           O
HETATM 2975  O   HOH A2264     -22.433 -27.773  46.219  1.00 17.79           O
HETATM 2976  O   HOH A2265     -27.453 -31.155  48.710  1.00 10.24           O
HETATM 2977  O   HOH A2266     -23.653 -29.698  48.274  1.00 34.12           O
HETATM 2978  O   HOH A2267     -25.887 -32.255  41.664  1.00 25.32           O
HETATM 2979  O   HOH A2268      -1.101   3.166   9.116  1.00 36.79           O
HETATM 2980  O   HOH A2269     -32.397 -26.136  50.694  1.00 39.77           O
HETATM 2981  O   HOH A2270       1.216   3.852  14.698  1.00 28.90           O
HETATM 2982  O   HOH A2271     -21.110 -20.856  49.190  1.00  4.97           O
HETATM 2983  O   HOH A2272     -33.731 -30.171  46.534  1.00 31.31           O
HETATM 2984  O   HOH A2273     -29.951 -30.111  48.510  1.00 28.10           O
HETATM 2985  O   HOH A2274     -34.283 -19.510  39.580  1.00 41.03           O
HETATM 2986  O   HOH A2275     -28.589 -21.838  32.944  1.00 15.45           O
HETATM 2987  O   HOH A2276     -31.566 -19.227  32.641  1.00 28.82           O
HETATM 2988  O   HOH A2277     -33.880 -21.250  32.948  1.00 27.05           O
HETATM 2989  O   HOH A2278     -32.381 -12.025  37.236  1.00 36.74           O
HETATM 2990  O   HOH A2279     -24.234 -21.107  33.915  1.00  5.23           O
HETATM 2991  O   HOH A2280     -24.482 -23.202  37.147  1.00 14.54           O
HETATM 2992  O   HOH A2281     -23.130 -18.760  27.422  1.00 16.68           O
HETATM 2993  O   HOH A2282     -29.883 -12.935  36.735  1.00 20.65           O
HETATM 2994  O   HOH A2283     -26.075 -21.464  31.836  1.00 18.44           O
HETATM 2995  O   HOH A2284     -32.076 -14.463  32.448  1.00 31.17           O
HETATM 2996  O   HOH A2285     -19.442 -16.947  25.805  1.00 24.39           O
HETATM 2997  O   HOH A2286     -18.319 -20.638  29.183  1.00 25.70           O
HETATM 2998  O   HOH A2287     -26.417 -13.453  24.930  1.00 18.74           O
HETATM 2999  O   HOH A2288     -30.432 -13.538  26.751  1.00 24.09           O
HETATM 3000  O   HOH A2289     -30.735  -4.347  29.526  1.00  9.38           O
HETATM 3001  O   HOH A2290     -26.823  -3.332  31.805  1.00 19.54           O
HETATM 3002  O   HOH A2291     -28.214  -2.750  28.800  1.00 19.55           O
HETATM 3003  O   HOH A2292     -30.072 -10.378  30.339  1.00 10.13           O
HETATM 3004  O   HOH A2293     -32.165  -6.335  31.079  1.00 23.25           O
HETATM 3005  O   HOH A2294     -33.386  -7.647  26.970  1.00 27.53           O
HETATM 3006  O   HOH A2295     -26.815  -0.916  30.148  1.00 21.26           O
HETATM 3007  O   HOH A2296     -28.503   1.609  28.151  1.00 34.51           O
HETATM 3008  O   HOH A2297     -32.336  -1.560  25.288  1.00 27.85           O
HETATM 3009  O   HOH A2298     -27.925   7.302  21.621  1.00 22.45           O
HETATM 3010  O   HOH A2299     -27.635   9.686  15.119  1.00 24.83           O
HETATM 3011  O   HOH A2300     -21.899  14.920  14.832  1.00 26.32           O
HETATM 3012  O   HOH A2301     -22.770  10.845  26.464  1.00 34.45           O
HETATM 3013  O   HOH A2302     -25.346  10.895  22.736  1.00 23.22           O
HETATM 3014  O   HOH A2303     -18.579  14.393   9.550  1.00 25.76           O
HETATM 3015  O   HOH A2304     -20.337  16.537  13.428  1.00 21.63           O
HETATM 3016  O   HOH A2305     -15.725  18.110  15.053  1.00 31.90           O
HETATM 3017  O   HOH A2306     -13.319  19.079   8.858  1.00 27.96           O
HETATM 3018  O   HOH A2307      -9.201  19.200  14.887  1.00 29.25           O
HETATM 3019  O   HOH A2308      -2.997  12.942  16.311  1.00 29.40           O
HETATM 3020  O   HOH A2309      -2.755  19.034  13.219  1.00 16.49           O
HETATM 3021  O   HOH A2310      -0.861  24.207  11.981  1.00 17.64           O
HETATM 3022  O   HOH A2311      -4.099  20.588  14.871  1.00 27.58           O
HETATM 3023  O   HOH A2312       5.780  15.953  14.319  1.00 21.55           O
HETATM 3024  O   HOH A2313      -2.778  25.640  10.908  1.00 19.32           O
HETATM 3025  O   HOH A2314       6.444  25.014  10.041  1.00 24.91           O
HETATM 3026  O   HOH A2315       8.253  17.093  13.341  1.00 35.21           O
HETATM 3027  O   HOH A2316       8.138  20.771   6.490  1.00 16.03           O
HETATM 3028  O   HOH A2317       5.604  13.964   4.777  1.00 38.96           O
HETATM 3029  O   HOH A2318      -2.476  17.114  15.096  1.00 32.92           O
HETATM 3030  O   HOH A2319       1.116  18.253  14.841  1.00 17.00           O
HETATM 3031  O   HOH A2320      -2.431   5.142   7.357  1.00 29.01           O
HETATM 3032  O   HOH A2321      -1.370   6.305   5.060  1.00 44.47           O
HETATM 3033  O   HOH A2322      -0.113   4.545  11.159  1.00 21.71           O
HETATM 3034  O   HOH A2323      -2.104  -2.539  13.907  1.00 41.36           O
HETATM 3035  O   HOH A2324      -1.241   4.195  13.810  1.00 11.06           O
HETATM 3036  O   HOH A2325      -0.541  -0.181  15.438  1.00 33.70           O
HETATM 3037  O   HOH A2326     -13.575  12.846   3.451  1.00 23.08           O
HETATM 3038  O   HOH A2327     -11.744   4.425   3.845  1.00 19.44           O
HETATM 3039  O   HOH A2328     -13.358   1.100  11.066  1.00 17.33           O
HETATM 3040  O   HOH A2329     -18.782   6.983   5.589  1.00 20.71           O
HETATM 3041  O   HOH A2330     -14.664   5.013   3.332  1.00 26.16           O
HETATM 3042  O   HOH A2331      -5.139 -11.379  37.724  1.00  5.62           O
HETATM 3043  O   HOH A2332      -5.948 -18.029  45.244  1.00 20.39           O
CONECT    3    4    2    9
CONECT  266 2711
CONECT  290 2710
CONECT  410 2711
CONECT  420 2711
CONECT  441 2710
CONECT 1034 1040 1035 1033
CONECT 1032 1030 1033
CONECT 1186 1187 1185 1192
CONECT 1184 1185 1178
CONECT 1202 1201 1208 1203
CONECT 1200 1201 1194
CONECT 1568 1569 1567 1574
CONECT 1566 1560 1567
CONECT 2065 2071 2064 2066
CONECT 2063 2054 2064
CONECT 2551 2552 2550 2557
CONECT 2549 2550 2542
CONECT 2578 2584 2579 2577
CONECT 2576 2577 2567
CONECT 2693 2688 2691 2694
CONECT 2701 2700 2702 2703
CONECT 2691 2689 2693 2692
CONECT 2689 2687 2691 2690
CONECT 2704 2703 2694 2697
CONECT 2687 2689 2688 2686
CONECT 2697 2704 2696 2698
CONECT 2686 2685 2687
CONECT 2698 2700 2697 2699
CONECT 2695 2694 2696
CONECT 2700 2701 2698
CONECT 2702 2701
CONECT 2703 2701 2704
CONECT 2696 2695 2697
CONECT 2694 2704 2693 2695
CONECT 2683 2682
CONECT 2678 2677
CONECT 2678 2710
CONECT 2692 2691
CONECT 2684 2682
CONECT 2679 2677
CONECT 2690 2689
CONECT 2681 2677 2682
CONECT 2680 2677
CONECT 2680 2711 2705
CONECT 2688 2687 2693
CONECT 2685 2686 2682
CONECT 2699 2698
CONECT 2682 2683 2681 2685 2684
CONECT 2677 2681 2678 2680 2679
CONECT 2705 2709 2707 2708 2706
CONECT 2705 2710 2711 2680 2782
CONECT 2706 2705
CONECT 2706 2711
CONECT 2707 2705
CONECT 2708 2705
CONECT 2708 2711
CONECT 2709 2705
CONECT 2709 2710
CONECT 2710  441 2705 2709 2678
CONECT 2710 2850 3042  290
CONECT 2711  410  420 2705 2706
CONECT 2711 2708 2680  266
CONECT 2782 2705
CONECT 2850 2710
CONECT 3042 2710
END



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