CNRS Nantes University UFIP UFIP
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***  TRANSFERASE 04-FEB-04 1S9I  ***

elNémo ID: 21080402425042499

Job options:

ID        	=	 21080402425042499
JOBID     	=	 TRANSFERASE 04-FEB-04 1S9I
USERID    	=	 unknown
PRIVAT    	=	 0

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

DOPROJMODS	=	 0
DORMSD    	=	 0

NRBL      	=	 0
CUTOFF    	=	 0
CAONLY    	=	 0


Input data for this run:


HEADER    TRANSFERASE                             04-FEB-04   1S9I              
TITLE     X-RAY STRUCTURE OF THE HUMAN MITOGEN-ACTIVATED PROTEIN                
TITLE    2 KINASE KINASE 2 (MEK2)IN A COMPLEX WITH LIGAND AND MGATP             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: DUAL SPECIFICITY MITOGEN-ACTIVATED PROTEIN                 
COMPND   3 KINASE KINASE 2;                                                     
COMPND   4 CHAIN: A, B;                                                         
COMPND   5 SYNONYM: MAP KINASE KINASE 2, MAPKK 2, ERK ACTIVATOR                 
COMPND   6 KINASE 2, MAPK/ERK KINASE 2, MEK2;                                   
COMPND   7 EC: 2.7.1.37;                                                        
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: MAP2K2, PRKMK2, MEK2, MKK2;                                    
SOURCE   6 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   9 EXPRESSION_SYSTEM_VECTOR: PLASMID;                                   
SOURCE  10 EXPRESSION_SYSTEM_PLASMID: PET24B                                    
KEYWDS    PROTEIN KINASE-LIGAND-MGATP COMPLEX, PROTEIN-PROTEIN                  
KEYWDS   2 INTERACTIONS, TRANSFERASE                                            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.F.OHREN,H.CHEN,A.PAVLOVSKY,C.WHITEHEAD,C.YAN,P.MCCONNELL,           
AUTHOR   2 A.DELANEY,D.T.DUDLEY,J.SEBOLT-LEOPOLD,C.A.HASEMANN                   
REVDAT   3   24-FEB-09 1S9I    1       VERSN                                    
REVDAT   2   14-DEC-04 1S9I    1       JRNL                                     
REVDAT   1   23-NOV-04 1S9I    0                                                
JRNL        AUTH   J.F.OHREN,H.CHEN,A.PAVLOVSKY,C.WHITEHEAD,E.ZHANG,            
JRNL        AUTH 2 P.KUFFA,C.YAN,P.MCCONNELL,C.SPESSARD,C.BANOTAI,              
JRNL        AUTH 3 W.T.MUELLER,A.DELANEY,C.OMER,J.SEBOLT-LEOPOLD,               
JRNL        AUTH 4 D.T.DUDLEY,I.K.LEUNG,C.FLAMME,J.WARMUS,M.KAUFMAN,            
JRNL        AUTH 5 S.BARRETT,H.TECLE,C.A.HASEMANN                               
JRNL        TITL   STRUCTURES OF HUMAN MAP KINASE KINASE 1 (MEK1) AND           
JRNL        TITL 2 MEK2 DESCRIBE NOVEL NONCOMPETITIVE KINASE                    
JRNL        TITL 3 INHIBITION.                                                  
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  11  1192 2004              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   15543157                                                     
JRNL        DOI    10.1038/NSMB859                                              
REMARK   1                                                                      
REMARK   2                                                                      
REMARK   2 RESOLUTION.    3.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.1.24                                        
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 3.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 14.40                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 15147                          
REMARK   3                                                                      
REMARK   3  FIT TO DATA USED IN REFINEMENT.                                     
REMARK   3   CROSS-VALIDATION METHOD          : THROUGHOUT                      
REMARK   3   FREE R VALUE TEST SET SELECTION  : RANDOM                          
REMARK   3   R VALUE     (WORKING + TEST SET) : 0.294                           
REMARK   3   R VALUE            (WORKING SET) : 0.290                           
REMARK   3   FREE R VALUE                     : 0.364                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 802                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 3.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 3.28                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1055                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : NULL                         
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3350                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 52                           
REMARK   3   BIN FREE R VALUE                    : 0.4820                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 4686                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 126                                     
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 41.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.36000                                             
REMARK   3    B22 (A**2) : -1.36000                                             
REMARK   3    B33 (A**2) : 2.04000                                              
REMARK   3    B12 (A**2) : -0.68000                                             
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.667         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.534         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 30.110        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.850                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.772                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4889 ; 0.007 ; 0.021       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  6601 ; 1.217 ; 1.999       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   588 ; 5.435 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   718 ; 0.072 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  3655 ; 0.002 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  2388 ; 0.195 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   142 ; 0.130 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    30 ; 0.182 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     1 ; 0.049 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2953 ; 0.355 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  4774 ; 0.659 ; 2.000       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1936 ; 0.646 ; 3.000       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1827 ; 1.175 ; 4.500       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : BABINET MODEL WITH MASK                              
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.40                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: MAXIMUM LIKELIHOOD REFINEMENT USING       
REMARK   3  REFMAC 5.1.24                                                       
REMARK   4                                                                      
REMARK   4 1S9I COMPLIES WITH FORMAT V. 3.15, 01-DEC-08                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 11-FEB-04.                  
REMARK 100 THE RCSB ID CODE IS RCSB021536.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 02-AUG-02                          
REMARK 200  TEMPERATURE           (KELVIN) : 100.0                              
REMARK 200  PH                             : 7.00                               
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : APS                                
REMARK 200  BEAMLINE                       : 17-ID                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.000                              
REMARK 200  MONOCHROMATOR                  : SAGITALLY FOCUSED SI(111)          
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARRESEARCH                        
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : CCP4 (TRUNCATE)                    
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 15147                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 3.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 14.400                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.9                               
REMARK 200  DATA REDUNDANCY                : 9.800                              
REMARK 200  R MERGE                    (I) : 0.08800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 25.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 3.20                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 3.28                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 1.0                                
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.36800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 6.000                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: HUMAN MAP2K1                                         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 58.12                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.94                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SODIUM / POTASSIUM PHOSPHATE, DTT,       
REMARK 280  PH 7, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 288K, PH 7.00      
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61 2 2                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+5/6                                            
REMARK 290      11555   -X+Y,Y,-Z+1/2                                           
REMARK 290      12555   X,X-Y,-Z+1/6                                            
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       40.99533            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       81.99067            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       61.49300            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000      102.48833            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       20.49767            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       40.99533            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       81.99067            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000      102.48833            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000       61.49300            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       20.49767            
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 300 REMARK: THE NH2-TRUNCATED MEK2 IS A HOMODIMER IN SOLUTION AND IN     
REMARK 300 THE CRYSTALLOGRAPHIC ASU. MEK2 MAY FORM A FUNCTIONAL DIMER IN        
REMARK 300 VIVO.                                                                
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: 5500 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 28410 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     GLU A    55                                                      
REMARK 465     ALA A    56                                                      
REMARK 465     PHE A    57                                                      
REMARK 465     LEU A    58                                                      
REMARK 465     THR A    59                                                      
REMARK 465     ALA A   224                                                      
REMARK 465     ASN A   225                                                      
REMARK 465     SER A   226                                                      
REMARK 465     PHE A   227                                                      
REMARK 465     GLY A   286                                                      
REMARK 465     GLU A   287                                                      
REMARK 465     GLU A   288                                                      
REMARK 465     GLY A   289                                                      
REMARK 465     GLU A   290                                                      
REMARK 465     PRO A   291                                                      
REMARK 465     HIS A   292                                                      
REMARK 465     SER A   293                                                      
REMARK 465     ILE A   294                                                      
REMARK 465     SER A   295                                                      
REMARK 465     PRO A   296                                                      
REMARK 465     ARG A   297                                                      
REMARK 465     PRO A   298                                                      
REMARK 465     ARG A   299                                                      
REMARK 465     PRO A   300                                                      
REMARK 465     PRO A   301                                                      
REMARK 465     GLY A   302                                                      
REMARK 465     ARG A   303                                                      
REMARK 465     PRO A   304                                                      
REMARK 465     VAL A   305                                                      
REMARK 465     SER A   306                                                      
REMARK 465     GLY A   307                                                      
REMARK 465     HIS A   308                                                      
REMARK 465     GLY A   309                                                      
REMARK 465     MET A   310                                                      
REMARK 465     ASP A   311                                                      
REMARK 465     SER A   312                                                      
REMARK 465     THR A   394                                                      
REMARK 465     PRO A   395                                                      
REMARK 465     THR A   396                                                      
REMARK 465     ARG A   397                                                      
REMARK 465     THR A   398                                                      
REMARK 465     ALA A   399                                                      
REMARK 465     VAL A   400                                                      
REMARK 465     LEU A   401                                                      
REMARK 465     GLU A   402                                                      
REMARK 465     HIS A   403                                                      
REMARK 465     HIS A   404                                                      
REMARK 465     HIS A   405                                                      
REMARK 465     HIS A   406                                                      
REMARK 465     HIS A   407                                                      
REMARK 465     HIS A   408                                                      
REMARK 465     GLU B    55                                                      
REMARK 465     ALA B    56                                                      
REMARK 465     PHE B    57                                                      
REMARK 465     LEU B    58                                                      
REMARK 465     ALA B   224                                                      
REMARK 465     ASN B   225                                                      
REMARK 465     SER B   226                                                      
REMARK 465     PHE B   227                                                      
REMARK 465     VAL B   228                                                      
REMARK 465     GLY B   229                                                      
REMARK 465     PRO B   282                                                      
REMARK 465     VAL B   283                                                      
REMARK 465     VAL B   284                                                      
REMARK 465     ASP B   285                                                      
REMARK 465     GLY B   286                                                      
REMARK 465     GLU B   287                                                      
REMARK 465     GLU B   288                                                      
REMARK 465     GLY B   289                                                      
REMARK 465     GLU B   290                                                      
REMARK 465     PRO B   291                                                      
REMARK 465     HIS B   292                                                      
REMARK 465     SER B   293                                                      
REMARK 465     ILE B   294                                                      
REMARK 465     SER B   295                                                      
REMARK 465     PRO B   296                                                      
REMARK 465     ARG B   297                                                      
REMARK 465     PRO B   298                                                      
REMARK 465     ARG B   299                                                      
REMARK 465     PRO B   300                                                      
REMARK 465     PRO B   301                                                      
REMARK 465     GLY B   302                                                      
REMARK 465     ARG B   303                                                      
REMARK 465     PRO B   304                                                      
REMARK 465     VAL B   305                                                      
REMARK 465     SER B   306                                                      
REMARK 465     GLY B   307                                                      
REMARK 465     HIS B   308                                                      
REMARK 465     GLY B   309                                                      
REMARK 465     MET B   310                                                      
REMARK 465     ASP B   311                                                      
REMARK 465     SER B   312                                                      
REMARK 465     ARG B   313                                                      
REMARK 465     PRO B   314                                                      
REMARK 465     ALA B   315                                                      
REMARK 465     ASN B   390                                                      
REMARK 465     GLN B   391                                                      
REMARK 465     PRO B   392                                                      
REMARK 465     GLY B   393                                                      
REMARK 465     THR B   394                                                      
REMARK 465     PRO B   395                                                      
REMARK 465     THR B   396                                                      
REMARK 465     ARG B   397                                                      
REMARK 465     THR B   398                                                      
REMARK 465     ALA B   399                                                      
REMARK 465     VAL B   400                                                      
REMARK 465     LEU B   401                                                      
REMARK 465     GLU B   402                                                      
REMARK 465     HIS B   403                                                      
REMARK 465     HIS B   404                                                      
REMARK 465     HIS B   405                                                      
REMARK 465     HIS B   406                                                      
REMARK 465     HIS B   407                                                      
REMARK 465     HIS B   408                                                      
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    VAL A  64      -52.53   -126.46                                   
REMARK 500    ILE A  75      -72.93   -104.91                                   
REMARK 500    PRO A  93       34.55    -93.44                                   
REMARK 500    SER A  94      -27.13   -159.75                                   
REMARK 500    GLU A 106      -83.54    -67.19                                   
REMARK 500    LYS A 108       37.16   -141.46                                   
REMARK 500    PRO A 109     -140.55    -95.37                                   
REMARK 500    VAL A 121       -8.08    -57.56                                   
REMARK 500    PRO A 128        5.15    -63.11                                   
REMARK 500    LYS A 163     -102.00    -68.00                                   
REMARK 500    ASP A 194       53.33   -162.57                                   
REMARK 500    ARG A 231      119.99   -174.34                                   
REMARK 500    GLN A 240       21.01    -79.18                                   
REMARK 500    PRO A 282      101.53    -55.37                                   
REMARK 500    VAL A 284     -139.70   -158.79                                   
REMARK 500    VAL A 326      -71.21    -70.36                                   
REMARK 500    ASP A 378       90.35    -69.20                                   
REMARK 500    ASN A 390      108.58    -37.70                                   
REMARK 500    PRO A 392       63.48    -67.95                                   
REMARK 500    LYS B  61       39.89    -88.39                                   
REMARK 500    PRO B 109       75.36    -64.94                                   
REMARK 500    ALA B 110      -53.29   -164.72                                   
REMARK 500    PRO B 128        2.03    -60.93                                   
REMARK 500    ASP B 140       85.35    -64.86                                   
REMARK 500    HIS B 188       -6.28   -140.61                                   
REMARK 500    ARG B 193       14.72    -68.62                                   
REMARK 500    HIS B 243       78.76     58.36                                   
REMARK 500    SER B 245     -148.77   -140.48                                   
REMARK 500    PRO B 340      -30.51    -38.90                                   
REMARK 500    ARG B 388       74.29     58.30                                   
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 A 536  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP A 535   O2G                                                    
REMARK 620 2 ATP A 535   O3B  63.1                                              
REMARK 620 3 ASN A 199   ND2 157.8 112.0                                        
REMARK 620 4 ATP A 535   O1B 100.9  54.3  91.4                                  
REMARK 620 5 ATP A 535   O2A  75.5  97.6 126.3  70.5                            
REMARK 620 6 ASP A 212   OD2 125.9 169.8  61.9 116.2  81.3                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG B 538  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 ATP B 537   O2A                                                    
REMARK 620 2 ASP B 212   OD2  95.3                                              
REMARK 620 3 ATP B 537   O1B  87.3 145.8                                        
REMARK 620 4 ASN B 199   OD1 165.5  73.7  96.7                                  
REMARK 620 5 ATP B 537   O2G  79.9 146.5  67.5 114.5                            
REMARK 620 N                    1     2     3     4                             
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG A 536                  
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MG B 538                  
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP A 535                 
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ATP B 537                 
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5EA A 1001                
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 5EA B 1002                
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1S9J   RELATED DB: PDB                                   
DBREF  1S9I A   55   400  UNP    P36507   MP2K2_HUMAN     55    400             
DBREF  1S9I B   55   400  UNP    P36507   MP2K2_HUMAN     55    400             
SEQADV 1S9I LEU A  401  UNP  P36507              CLONING ARTIFACT               
SEQADV 1S9I GLU A  402  UNP  P36507              CLONING ARTIFACT               
SEQADV 1S9I HIS A  403  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS A  404  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS A  405  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS A  406  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS A  407  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS A  408  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I LEU B  401  UNP  P36507              CLONING ARTIFACT               
SEQADV 1S9I GLU B  402  UNP  P36507              CLONING ARTIFACT               
SEQADV 1S9I HIS B  403  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS B  404  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS B  405  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS B  406  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS B  407  UNP  P36507              EXPRESSION TAG                 
SEQADV 1S9I HIS B  408  UNP  P36507              EXPRESSION TAG                 
SEQRES   1 A  354  GLU ALA PHE LEU THR GLN LYS ALA LYS VAL GLY GLU LEU          
SEQRES   2 A  354  LYS ASP ASP ASP PHE GLU ARG ILE SER GLU LEU GLY ALA          
SEQRES   3 A  354  GLY ASN GLY GLY VAL VAL THR LYS VAL GLN HIS ARG PRO          
SEQRES   4 A  354  SER GLY LEU ILE MET ALA ARG LYS LEU ILE HIS LEU GLU          
SEQRES   5 A  354  ILE LYS PRO ALA ILE ARG ASN GLN ILE ILE ARG GLU LEU          
SEQRES   6 A  354  GLN VAL LEU HIS GLU CYS ASN SER PRO TYR ILE VAL GLY          
SEQRES   7 A  354  PHE TYR GLY ALA PHE TYR SER ASP GLY GLU ILE SER ILE          
SEQRES   8 A  354  CYS MET GLU HIS MET ASP GLY GLY SER LEU ASP GLN VAL          
SEQRES   9 A  354  LEU LYS GLU ALA LYS ARG ILE PRO GLU GLU ILE LEU GLY          
SEQRES  10 A  354  LYS VAL SER ILE ALA VAL LEU ARG GLY LEU ALA TYR LEU          
SEQRES  11 A  354  ARG GLU LYS HIS GLN ILE MET HIS ARG ASP VAL LYS PRO          
SEQRES  12 A  354  SER ASN ILE LEU VAL ASN SER ARG GLY GLU ILE LYS LEU          
SEQRES  13 A  354  CYS ASP PHE GLY VAL SER GLY GLN LEU ILE ASP SER MET          
SEQRES  14 A  354  ALA ASN SER PHE VAL GLY THR ARG SER TYR MET ALA PRO          
SEQRES  15 A  354  GLU ARG LEU GLN GLY THR HIS TYR SER VAL GLN SER ASP          
SEQRES  16 A  354  ILE TRP SER MET GLY LEU SER LEU VAL GLU LEU ALA VAL          
SEQRES  17 A  354  GLY ARG TYR PRO ILE PRO PRO PRO ASP ALA LYS GLU LEU          
SEQRES  18 A  354  GLU ALA ILE PHE GLY ARG PRO VAL VAL ASP GLY GLU GLU          
SEQRES  19 A  354  GLY GLU PRO HIS SER ILE SER PRO ARG PRO ARG PRO PRO          
SEQRES  20 A  354  GLY ARG PRO VAL SER GLY HIS GLY MET ASP SER ARG PRO          
SEQRES  21 A  354  ALA MET ALA ILE PHE GLU LEU LEU ASP TYR ILE VAL ASN          
SEQRES  22 A  354  GLU PRO PRO PRO LYS LEU PRO ASN GLY VAL PHE THR PRO          
SEQRES  23 A  354  ASP PHE GLN GLU PHE VAL ASN LYS CYS LEU ILE LYS ASN          
SEQRES  24 A  354  PRO ALA GLU ARG ALA ASP LEU LYS MET LEU THR ASN HIS          
SEQRES  25 A  354  THR PHE ILE LYS ARG SER GLU VAL GLU GLU VAL ASP PHE          
SEQRES  26 A  354  ALA GLY TRP LEU CYS LYS THR LEU ARG LEU ASN GLN PRO          
SEQRES  27 A  354  GLY THR PRO THR ARG THR ALA VAL LEU GLU HIS HIS HIS          
SEQRES  28 A  354  HIS HIS HIS                                                  
SEQRES   1 B  354  GLU ALA PHE LEU THR GLN LYS ALA LYS VAL GLY GLU LEU          
SEQRES   2 B  354  LYS ASP ASP ASP PHE GLU ARG ILE SER GLU LEU GLY ALA          
SEQRES   3 B  354  GLY ASN GLY GLY VAL VAL THR LYS VAL GLN HIS ARG PRO          
SEQRES   4 B  354  SER GLY LEU ILE MET ALA ARG LYS LEU ILE HIS LEU GLU          
SEQRES   5 B  354  ILE LYS PRO ALA ILE ARG ASN GLN ILE ILE ARG GLU LEU          
SEQRES   6 B  354  GLN VAL LEU HIS GLU CYS ASN SER PRO TYR ILE VAL GLY          
SEQRES   7 B  354  PHE TYR GLY ALA PHE TYR SER ASP GLY GLU ILE SER ILE          
SEQRES   8 B  354  CYS MET GLU HIS MET ASP GLY GLY SER LEU ASP GLN VAL          
SEQRES   9 B  354  LEU LYS GLU ALA LYS ARG ILE PRO GLU GLU ILE LEU GLY          
SEQRES  10 B  354  LYS VAL SER ILE ALA VAL LEU ARG GLY LEU ALA TYR LEU          
SEQRES  11 B  354  ARG GLU LYS HIS GLN ILE MET HIS ARG ASP VAL LYS PRO          
SEQRES  12 B  354  SER ASN ILE LEU VAL ASN SER ARG GLY GLU ILE LYS LEU          
SEQRES  13 B  354  CYS ASP PHE GLY VAL SER GLY GLN LEU ILE ASP SER MET          
SEQRES  14 B  354  ALA ASN SER PHE VAL GLY THR ARG SER TYR MET ALA PRO          
SEQRES  15 B  354  GLU ARG LEU GLN GLY THR HIS TYR SER VAL GLN SER ASP          
SEQRES  16 B  354  ILE TRP SER MET GLY LEU SER LEU VAL GLU LEU ALA VAL          
SEQRES  17 B  354  GLY ARG TYR PRO ILE PRO PRO PRO ASP ALA LYS GLU LEU          
SEQRES  18 B  354  GLU ALA ILE PHE GLY ARG PRO VAL VAL ASP GLY GLU GLU          
SEQRES  19 B  354  GLY GLU PRO HIS SER ILE SER PRO ARG PRO ARG PRO PRO          
SEQRES  20 B  354  GLY ARG PRO VAL SER GLY HIS GLY MET ASP SER ARG PRO          
SEQRES  21 B  354  ALA MET ALA ILE PHE GLU LEU LEU ASP TYR ILE VAL ASN          
SEQRES  22 B  354  GLU PRO PRO PRO LYS LEU PRO ASN GLY VAL PHE THR PRO          
SEQRES  23 B  354  ASP PHE GLN GLU PHE VAL ASN LYS CYS LEU ILE LYS ASN          
SEQRES  24 B  354  PRO ALA GLU ARG ALA ASP LEU LYS MET LEU THR ASN HIS          
SEQRES  25 B  354  THR PHE ILE LYS ARG SER GLU VAL GLU GLU VAL ASP PHE          
SEQRES  26 B  354  ALA GLY TRP LEU CYS LYS THR LEU ARG LEU ASN GLN PRO          
SEQRES  27 B  354  GLY THR PRO THR ARG THR ALA VAL LEU GLU HIS HIS HIS          
SEQRES  28 B  354  HIS HIS HIS                                                  
HET     MG  A 536       1                                                       
HET     MG  B 538       1                                                       
HET    ATP  A 535      31                                                       
HET    ATP  B 537      31                                                       
HET    5EA  A1001      31                                                       
HET    5EA  B1002      31                                                       
HETNAM      MG MAGNESIUM ION                                                    
HETNAM     ATP ADENOSINE-5'-TRIPHOSPHATE                                        
HETNAM     5EA 5-{3,4-DIFLUORO-2-[(2-FLUORO-4-IODOPHENYL)                       
HETNAM   2 5EA  AMINO]PHENYL}-N-(2-MORPHOLIN-4-YLETHYL)-1,3,4-                  
HETNAM   3 5EA  OXADIAZOL-2-AMINE                                               
FORMUL   3   MG    2(MG 2+)                                                     
FORMUL   5  ATP    2(C10 H16 N5 O13 P3)                                         
FORMUL   7  5EA    2(C20 H19 F3 I N5 O2)                                        
HELIX    1   1 LYS A   68  ASP A   70  5                                   3    
HELIX    2   2 PRO A  109  GLN A  120  1                                  12    
HELIX    3   3 VAL A  121  HIS A  123  5                                   3    
HELIX    4   4 LEU A  155  ALA A  162  1                                   8    
HELIX    5   5 PRO A  166  LYS A  187  1                                  22    
HELIX    6   6 LYS A  196  SER A  198  5                                   3    
HELIX    7   7 SER A  216  MET A  223  1                                   8    
HELIX    8   8 ALA A  235  GLN A  240  1                                   6    
HELIX    9   9 SER A  245  GLY A  263  1                                  19    
HELIX   10  10 ASP A  271  GLY A  280  1                                  10    
HELIX   11  11 ALA A  317  GLU A  328  1                                  12    
HELIX   12  12 THR A  339  LEU A  350  1                                  12    
HELIX   13  13 ASP A  359  ASN A  365  1                                   7    
HELIX   14  14 HIS A  366  GLU A  375  1                                  10    
HELIX   15  15 ASP A  378  LEU A  387  1                                  10    
HELIX   16  16 ILE B  111  LEU B  119  1                                   9    
HELIX   17  17 GLN B  120  CYS B  125  5                                   6    
HELIX   18  18 LEU B  155  ALA B  162  1                                   8    
HELIX   19  19 PRO B  166  LYS B  187  1                                  22    
HELIX   20  20 LYS B  196  SER B  198  5                                   3    
HELIX   21  21 SER B  216  SER B  222  1                                   7    
HELIX   22  22 ALA B  235  GLY B  241  1                                   7    
HELIX   23  23 VAL B  246  GLY B  263  1                                  18    
HELIX   24  24 GLU B  274  ILE B  278  5                                   5    
HELIX   25  25 ALA B  317  GLU B  328  1                                  12    
HELIX   26  26 THR B  339  LEU B  350  1                                  12    
HELIX   27  27 ASP B  359  ASN B  365  1                                   7    
HELIX   28  28 HIS B  366  VAL B  374  1                                   9    
HELIX   29  29 ASP B  378  ARG B  388  1                                  11    
SHEET    1   A 5 PHE A  72  ALA A  80  0                                        
SHEET    2   A 5 VAL A  85  HIS A  91 -1  O  LYS A  88   N  SER A  76           
SHEET    3   A 5 ILE A  97  ILE A 103 -1  O  MET A  98   N  VAL A  89           
SHEET    4   A 5 ILE A 143  GLU A 148 -1  O  MET A 147   N  ALA A  99           
SHEET    5   A 5 PHE A 133  TYR A 138 -1  N  GLY A 135   O  CYS A 146           
SHEET    1   B 3 GLY A 153  SER A 154  0                                        
SHEET    2   B 3 ILE A 200  VAL A 202 -1  O  VAL A 202   N  GLY A 153           
SHEET    3   B 3 ILE A 208  LEU A 210 -1  O  LYS A 209   N  LEU A 201           
SHEET    1   C 5 PHE B  72  GLY B  81  0                                        
SHEET    2   C 5 GLY B  84  HIS B  91 -1  O  GLY B  84   N  GLY B  81           
SHEET    3   C 5 ILE B  97  HIS B 104 -1  O  LEU B 102   N  VAL B  85           
SHEET    4   C 5 GLU B 142  GLU B 148 -1  O  ILE B 145   N  LYS B 101           
SHEET    5   C 5 PHE B 133  SER B 139 -1  N  GLY B 135   O  CYS B 146           
SHEET    1   D 3 GLY B 153  SER B 154  0                                        
SHEET    2   D 3 ILE B 200  VAL B 202 -1  O  VAL B 202   N  GLY B 153           
SHEET    3   D 3 ILE B 208  LEU B 210 -1  O  LYS B 209   N  LEU B 201           
LINK        MG    MG A 536                 O2G ATP A 535     1555   1555  2.54  
LINK        MG    MG A 536                 O3B ATP A 535     1555   1555  2.15  
LINK        MG    MG A 536                 ND2 ASN A 199     1555   1555  2.55  
LINK        MG    MG A 536                 O1B ATP A 535     1555   1555  3.02  
LINK        MG    MG A 536                 O2A ATP A 535     1555   1555  2.08  
LINK        MG    MG A 536                 OD2 ASP A 212     1555   1555  2.44  
LINK         O2A ATP B 537                MG    MG B 538     1555   1555  1.91  
LINK        MG    MG B 538                 OD2 ASP B 212     1555   1555  2.55  
LINK        MG    MG B 538                 O1B ATP B 537     1555   1555  2.19  
LINK        MG    MG B 538                 OD1 ASN B 199     1555   1555  2.27  
LINK        MG    MG B 538                 O2G ATP B 537     1555   1555  2.83  
CISPEP   1 VAL A   64    GLY A   65          0        -6.41                     
CISPEP   2 GLY A  280    ARG A  281          0         9.33                     
SITE     1 AC1  3 ASN A 199  ASP A 212  ATP A 535                               
SITE     1 AC2  3 ASN B 199  ASP B 212  ATP B 537                               
SITE     1 AC3 18 LEU A  78  GLY A  81  ASN A  82  VAL A  86                    
SITE     2 AC3 18 ALA A  99  LYS A 101  MET A 147  GLU A 148                    
SITE     3 AC3 18 MET A 150  SER A 154  GLN A 157  ASP A 194                    
SITE     4 AC3 18 LYS A 196  SER A 198  LEU A 201  ASP A 212                    
SITE     5 AC3 18  MG A 536  5EA A1001                                          
SITE     1 AC4 19 LEU B  78  GLY B  79  GLY B  81  ASN B  82                    
SITE     2 AC4 19 GLY B  84  ALA B  99  LYS B 101  MET B 147                    
SITE     3 AC4 19 GLU B 148  MET B 150  SER B 154  GLN B 157                    
SITE     4 AC4 19 LYS B 196  SER B 198  ASN B 199  LEU B 201                    
SITE     5 AC4 19 ASP B 212   MG B 538  5EA B1002                               
SITE     1 AC5 15 ASN A  82  LYS A 101  LEU A 119  LEU A 122                    
SITE     2 AC5 15 VAL A 131  MET A 147  ARG A 193  ASP A 194                    
SITE     3 AC5 15 ASP A 212  PHE A 213  GLY A 214  VAL A 215                    
SITE     4 AC5 15 SER A 216  MET A 223  ATP A 535                               
SITE     1 AC6 12 LYS B 101  LEU B 119  LEU B 122  VAL B 131                    
SITE     2 AC6 12 ASP B 212  PHE B 213  GLY B 214  VAL B 215                    
SITE     3 AC6 12 SER B 216  LEU B 219  MET B 223  ATP B 537                    
CRYST1  161.888  161.888  122.986  90.00  90.00 120.00 P 61 2 2     24          
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      0.006177  0.003566  0.000000        0.00000                         
SCALE2      0.000000  0.007133  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008131        0.00000                         
ATOM      1  N   GLN A  60      58.146  92.598  49.602  1.00 64.67           N  
ATOM      2  CA  GLN A  60      57.474  93.657  50.414  1.00 64.79           C  
ATOM      3  C   GLN A  60      57.028  93.139  51.774  1.00 64.78           C  
ATOM      4  O   GLN A  60      55.940  92.573  51.914  1.00 64.86           O  
ATOM      5  CB  GLN A  60      56.260  94.244  49.674  1.00 64.84           C  
ATOM      6  CG  GLN A  60      55.641  95.503  50.329  1.00 65.18           C  
ATOM      7  CD  GLN A  60      54.578  95.192  51.397  1.00 65.35           C  
ATOM      8  OE1 GLN A  60      53.397  95.041  51.089  1.00 65.09           O  
ATOM      9  NE2 GLN A  60      55.004  95.112  52.650  1.00 65.62           N  
ATOM     10  N   LYS A  61      57.880  93.324  52.771  1.00 64.76           N  
ATOM     11  CA  LYS A  61      57.444  93.311  54.156  1.00 64.72           C  
ATOM     12  C   LYS A  61      58.131  94.484  54.817  1.00 64.94           C  
ATOM     13  O   LYS A  61      58.820  94.335  55.834  1.00 65.01           O  
ATOM     14  CB  LYS A  61      57.764  91.996  54.854  1.00 64.60           C  
ATOM     15  CG  LYS A  61      56.591  91.476  55.678  1.00 64.34           C  
ATOM     16  CD  LYS A  61      56.224  90.042  55.317  1.00 64.08           C  
ATOM     17  CE  LYS A  61      55.478  89.959  53.992  1.00 63.96           C  
ATOM     18  NZ  LYS A  61      56.400  89.659  52.856  1.00 63.84           N  
ATOM     19  N   ALA A  62      57.941  95.650  54.197  1.00 65.05           N  
ATOM     20  CA  ALA A  62      58.546  96.902  54.631  1.00 65.14           C  
ATOM     21  C   ALA A  62      57.936  97.372  55.947  1.00 65.27           C  
ATOM     22  O   ALA A  62      56.752  97.149  56.213  1.00 65.14           O  
ATOM     23  CB  ALA A  62      58.389  97.954  53.555  1.00 65.07           C  
ATOM     24  N   LYS A  63      58.759  98.022  56.764  1.00 65.51           N  
ATOM     25  CA  LYS A  63      58.385  98.371  58.130  1.00 65.90           C  
ATOM     26  C   LYS A  63      58.831  99.784  58.501  1.00 66.29           C  
ATOM     27  O   LYS A  63      59.931 100.215  58.136  1.00 66.30           O  
ATOM     28  CB  LYS A  63      58.956  97.339  59.115  1.00 65.80           C  
ATOM     29  CG  LYS A  63      60.480  97.300  59.221  1.00 65.41           C  
ATOM     30  CD  LYS A  63      61.133  96.794  57.942  1.00 65.40           C  
ATOM     31  CE  LYS A  63      62.208  97.762  57.446  1.00 65.88           C  
ATOM     32  NZ  LYS A  63      61.659  99.009  56.824  1.00 65.58           N  
ATOM     33  N   VAL A  64      57.970 100.508  59.216  1.00 66.65           N  
ATOM     34  CA  VAL A  64      58.305 101.871  59.639  1.00 67.07           C  
ATOM     35  C   VAL A  64      58.172 102.165  61.150  1.00 67.37           C  
ATOM     36  O   VAL A  64      59.126 102.679  61.741  1.00 67.68           O  
ATOM     37  CB  VAL A  64      57.607 102.975  58.796  1.00 67.08           C  
ATOM     38  CG1 VAL A  64      58.429 104.261  58.843  1.00 67.24           C  
ATOM     39  CG2 VAL A  64      57.393 102.527  57.348  1.00 67.14           C  
ATOM     40  N   GLY A  65      57.032 101.883  61.789  1.00 67.46           N  
ATOM     41  CA  GLY A  65      55.800 101.424  61.172  1.00 67.56           C  
ATOM     42  C   GLY A  65      54.597 102.054  61.855  1.00 67.65           C  
ATOM     43  O   GLY A  65      53.449 101.765  61.500  1.00 67.70           O  
ATOM     44  N   GLU A  66      54.868 102.901  62.849  1.00 67.63           N  
ATOM     45  CA  GLU A  66      53.838 103.689  63.518  1.00 67.70           C  
ATOM     46  C   GLU A  66      53.595 104.952  62.702  1.00 67.65           C  
ATOM     47  O   GLU A  66      54.475 105.807  62.588  1.00 67.69           O  
ATOM     48  CB  GLU A  66      54.261 104.032  64.948  1.00 67.77           C  
ATOM     49  CG  GLU A  66      53.109 104.097  65.941  1.00 68.18           C  
ATOM     50  CD  GLU A  66      52.749 102.738  66.522  1.00 68.61           C  
ATOM     51  OE1 GLU A  66      52.194 101.897  65.780  1.00 68.89           O  
ATOM     52  OE2 GLU A  66      53.013 102.513  67.724  1.00 68.46           O  
ATOM     53  N   LEU A  67      52.394 105.059  62.140  1.00 67.59           N  
ATOM     54  CA  LEU A  67      52.108 106.015  61.069  1.00 67.56           C  
ATOM     55  C   LEU A  67      51.530 107.345  61.558  1.00 67.58           C  
ATOM     56  O   LEU A  67      50.493 107.376  62.229  1.00 67.59           O  
ATOM     57  CB  LEU A  67      51.173 105.384  60.027  1.00 67.56           C  
ATOM     58  CG  LEU A  67      51.314 103.891  59.696  1.00 67.54           C  
ATOM     59  CD1 LEU A  67      50.494 103.022  60.654  1.00 67.54           C  
ATOM     60  CD2 LEU A  67      50.911 103.622  58.251  1.00 67.20           C  
ATOM     61  N   LYS A  68      52.212 108.437  61.209  1.00 67.54           N  
ATOM     62  CA  LYS A  68      51.767 109.790  61.546  1.00 67.45           C  
ATOM     63  C   LYS A  68      51.184 110.476  60.316  1.00 67.32           C  
ATOM     64  O   LYS A  68      51.757 110.390  59.226  1.00 67.31           O  
ATOM     65  CB  LYS A  68      52.924 110.629  62.108  1.00 67.47           C  
ATOM     66  CG  LYS A  68      53.585 110.058  63.361  1.00 67.64           C  
ATOM     67  CD  LYS A  68      52.890 110.513  64.641  1.00 67.66           C  
ATOM     68  CE  LYS A  68      52.832 109.388  65.668  1.00 67.79           C  
ATOM     69  NZ  LYS A  68      51.459 108.821  65.798  1.00 67.80           N  
ATOM     70  N   ASP A  69      50.054 111.159  60.499  1.00 67.09           N  
ATOM     71  CA  ASP A  69      49.369 111.859  59.408  1.00 66.92           C  
ATOM     72  C   ASP A  69      50.290 112.818  58.643  1.00 66.86           C  
ATOM     73  O   ASP A  69      50.283 112.839  57.410  1.00 66.80           O  
ATOM     74  CB  ASP A  69      48.136 112.602  59.938  1.00 66.91           C  
ATOM     75  CG  ASP A  69      47.434 113.418  58.863  1.00 66.80           C  
ATOM     76  OD1 ASP A  69      47.665 114.646  58.795  1.00 66.93           O  
ATOM     77  OD2 ASP A  69      46.634 112.921  58.045  1.00 66.57           O  
ATOM     78  N   ASP A  70      51.085 113.593  59.381  1.00 66.82           N  
ATOM     79  CA  ASP A  70      51.989 114.588  58.791  1.00 66.73           C  
ATOM     80  C   ASP A  70      53.249 113.980  58.152  1.00 66.57           C  
ATOM     81  O   ASP A  70      54.049 114.692  57.532  1.00 66.47           O  
ATOM     82  CB  ASP A  70      52.359 115.653  59.830  1.00 66.77           C  
ATOM     83  CG  ASP A  70      51.192 116.570  60.166  1.00 67.09           C  
ATOM     84  OD1 ASP A  70      51.426 117.787  60.339  1.00 67.46           O  
ATOM     85  OD2 ASP A  70      50.010 116.167  60.279  1.00 67.15           O  
ATOM     86  N   ASP A  71      53.409 112.665  58.299  1.00 66.36           N  
ATOM     87  CA  ASP A  71      54.488 111.931  57.641  1.00 66.14           C  
ATOM     88  C   ASP A  71      54.165 111.622  56.171  1.00 65.79           C  
ATOM     89  O   ASP A  71      55.014 111.095  55.444  1.00 65.79           O  
ATOM     90  CB  ASP A  71      54.790 110.632  58.397  1.00 66.27           C  
ATOM     91  CG  ASP A  71      56.032 110.730  59.272  1.00 66.73           C  
ATOM     92  OD1 ASP A  71      56.071 110.039  60.316  1.00 67.36           O  
ATOM     93  OD2 ASP A  71      57.020 111.452  58.996  1.00 66.73           O  
ATOM     94  N   PHE A  72      52.945 111.957  55.742  1.00 65.27           N  
ATOM     95  CA  PHE A  72      52.476 111.652  54.389  1.00 64.70           C  
ATOM     96  C   PHE A  72      52.468 112.860  53.458  1.00 64.43           C  
ATOM     97  O   PHE A  72      52.261 113.994  53.892  1.00 64.29           O  
ATOM     98  CB  PHE A  72      51.086 111.015  54.429  1.00 64.66           C  
ATOM     99  CG  PHE A  72      51.064 109.652  55.049  1.00 64.34           C  
ATOM    100  CD1 PHE A  72      50.638 109.479  56.361  1.00 64.21           C  
ATOM    101  CD2 PHE A  72      51.475 108.538  54.327  1.00 64.17           C  
ATOM    102  CE1 PHE A  72      50.619 108.216  56.948  1.00 64.09           C  
ATOM    103  CE2 PHE A  72      51.458 107.272  54.904  1.00 64.10           C  
ATOM    104  CZ  PHE A  72      51.031 107.111  56.218  1.00 63.97           C  
ATOM    105  N   GLU A  73      52.683 112.590  52.173  1.00 64.17           N  
ATOM    106  CA  GLU A  73      52.770 113.625  51.149  1.00 63.99           C  
ATOM    107  C   GLU A  73      52.065 113.201  49.855  1.00 63.76           C  
ATOM    108  O   GLU A  73      52.474 112.241  49.197  1.00 63.76           O  
ATOM    109  CB  GLU A  73      54.238 113.961  50.870  1.00 64.02           C  
ATOM    110  CG  GLU A  73      54.502 115.416  50.528  1.00 64.29           C  
ATOM    111  CD  GLU A  73      55.728 115.585  49.652  1.00 64.78           C  
ATOM    112  OE1 GLU A  73      55.601 115.446  48.414  1.00 64.67           O  
ATOM    113  OE2 GLU A  73      56.820 115.849  50.203  1.00 65.07           O  
ATOM    114  N   ARG A  74      51.006 113.930  49.506  1.00 63.43           N  
ATOM    115  CA  ARG A  74      50.225 113.691  48.294  1.00 63.11           C  
ATOM    116  C   ARG A  74      51.090 113.782  47.039  1.00 62.74           C  
ATOM    117  O   ARG A  74      51.673 114.827  46.760  1.00 62.67           O  
ATOM    118  CB  ARG A  74      49.099 114.724  48.200  1.00 63.28           C  
ATOM    119  CG  ARG A  74      47.685 114.159  48.172  1.00 63.71           C  
ATOM    120  CD  ARG A  74      46.590 115.226  48.107  1.00 64.46           C  
ATOM    121  NE  ARG A  74      46.589 116.079  49.297  1.00 65.30           N  
ATOM    122  CZ  ARG A  74      45.871 115.849  50.395  1.00 65.86           C  
ATOM    123  NH1 ARG A  74      45.075 114.786  50.475  1.00 65.96           N  
ATOM    124  NH2 ARG A  74      45.951 116.687  51.421  1.00 65.94           N  
ATOM    125  N   ILE A  75      51.177 112.682  46.296  1.00 62.42           N  
ATOM    126  CA  ILE A  75      51.878 112.668  45.012  1.00 62.14           C  
ATOM    127  C   ILE A  75      50.862 112.649  43.875  1.00 61.94           C  
ATOM    128  O   ILE A  75      50.672 113.653  43.187  1.00 61.96           O  
ATOM    129  CB  ILE A  75      52.842 111.457  44.896  1.00 62.18           C  
ATOM    130  CG1 ILE A  75      53.765 111.372  46.113  1.00 62.25           C  
ATOM    131  CG2 ILE A  75      53.658 111.529  43.595  1.00 61.97           C  
ATOM    132  CD1 ILE A  75      54.314 109.982  46.359  1.00 62.46           C  
ATOM    133  N   SER A  76      50.215 111.502  43.687  1.00 61.60           N  
ATOM    134  CA  SER A  76      49.206 111.344  42.649  1.00 61.36           C  
ATOM    135  C   SER A  76      47.884 110.933  43.275  1.00 61.18           C  
ATOM    136  O   SER A  76      47.854 110.400  44.386  1.00 61.12           O  
ATOM    137  CB  SER A  76      49.642 110.296  41.618  1.00 61.38           C  
ATOM    138  OG  SER A  76      51.019 110.415  41.299  1.00 61.46           O  
ATOM    139  N   GLU A  77      46.791 111.206  42.570  1.00 60.97           N  
ATOM    140  CA  GLU A  77      45.495 110.660  42.945  1.00 60.79           C  
ATOM    141  C   GLU A  77      45.346 109.309  42.246  1.00 60.70           C  
ATOM    142  O   GLU A  77      45.733 109.162  41.082  1.00 60.78           O  
ATOM    143  CB  GLU A  77      44.368 111.622  42.562  1.00 60.79           C  
ATOM    144  CG  GLU A  77      43.199 111.658  43.543  1.00 60.56           C  
ATOM    145  CD  GLU A  77      43.485 112.467  44.799  1.00 60.03           C  
ATOM    146  OE1 GLU A  77      44.324 113.392  44.747  1.00 59.85           O  
ATOM    147  OE2 GLU A  77      42.866 112.177  45.844  1.00 59.77           O  
ATOM    148  N   LEU A  78      44.816 108.319  42.959  1.00 60.49           N  
ATOM    149  CA  LEU A  78      44.704 106.967  42.407  1.00 60.36           C  
ATOM    150  C   LEU A  78      43.295 106.616  41.927  1.00 60.18           C  
ATOM    151  O   LEU A  78      43.136 105.830  40.987  1.00 60.18           O  
ATOM    152  CB  LEU A  78      45.213 105.921  43.407  1.00 60.38           C  
ATOM    153  CG  LEU A  78      46.725 105.675  43.401  1.00 60.50           C  
ATOM    154  CD1 LEU A  78      47.156 104.879  44.621  1.00 60.47           C  
ATOM    155  CD2 LEU A  78      47.166 104.971  42.124  1.00 60.96           C  
ATOM    156  N   GLY A  79      42.285 107.201  42.572  1.00 59.89           N  
ATOM    157  CA  GLY A  79      40.894 106.958  42.230  1.00 59.49           C  
ATOM    158  C   GLY A  79      39.984 107.060  43.435  1.00 59.27           C  
ATOM    159  O   GLY A  79      40.453 107.279  44.553  1.00 59.27           O  
ATOM    160  N   ALA A  80      38.682 106.904  43.205  1.00 59.12           N  
ATOM    161  CA  ALA A  80      37.685 106.933  44.276  1.00 59.06           C  
ATOM    162  C   ALA A  80      36.415 106.166  43.901  1.00 59.01           C  
ATOM    163  O   ALA A  80      36.145 105.929  42.720  1.00 59.04           O  
ATOM    164  CB  ALA A  80      37.347 108.376  44.658  1.00 59.08           C  
ATOM    165  N   GLY A  81      35.641 105.781  44.913  1.00 58.93           N  
ATOM    166  CA  GLY A  81      34.383 105.088  44.701  1.00 58.95           C  
ATOM    167  C   GLY A  81      33.891 104.352  45.931  1.00 59.00           C  
ATOM    168  O   GLY A  81      34.689 103.956  46.783  1.00 59.25           O  
ATOM    169  N   ASN A  82      32.573 104.181  46.018  1.00 58.92           N  
ATOM    170  CA  ASN A  82      31.914 103.421  47.086  1.00 58.90           C  
ATOM    171  C   ASN A  82      32.423 103.669  48.506  1.00 58.64           C  
ATOM    172  O   ASN A  82      32.645 102.725  49.270  1.00 58.68           O  
ATOM    173  CB  ASN A  82      31.938 101.919  46.775  1.00 59.08           C  
ATOM    174  CG  ASN A  82      30.581 101.261  46.973  1.00 59.88           C  
ATOM    175  OD1 ASN A  82      30.108 101.099  48.104  1.00 60.54           O  
ATOM    176  ND2 ASN A  82      29.942 100.887  45.867  1.00 60.70           N  
ATOM    177  N   GLY A  83      32.598 104.941  48.852  1.00 58.38           N  
ATOM    178  CA  GLY A  83      33.044 105.328  50.181  1.00 58.05           C  
ATOM    179  C   GLY A  83      34.517 105.052  50.404  1.00 57.74           C  
ATOM    180  O   GLY A  83      34.876 104.185  51.201  1.00 57.75           O  
ATOM    181  N   GLY A  84      35.364 105.793  49.691  1.00 57.44           N  
ATOM    182  CA  GLY A  84      36.807 105.648  49.783  1.00 57.03           C  
ATOM    183  C   GLY A  84      37.522 106.485  48.739  1.00 56.78           C  
ATOM    184  O   GLY A  84      36.995 106.706  47.644  1.00 56.86           O  
ATOM    185  N   VAL A  85      38.717 106.964  49.078  1.00 56.42           N  
ATOM    186  CA  VAL A  85      39.527 107.749  48.145  1.00 56.16           C  
ATOM    187  C   VAL A  85      40.996 107.326  48.201  1.00 55.83           C  
ATOM    188  O   VAL A  85      41.705 107.633  49.163  1.00 55.79           O  
ATOM    189  CB  VAL A  85      39.421 109.286  48.395  1.00 56.31           C  
ATOM    190  CG1 VAL A  85      39.675 110.060  47.100  1.00 56.40           C  
ATOM    191  CG2 VAL A  85      38.073 109.680  49.022  1.00 56.29           C  
ATOM    192  N   VAL A  86      41.446 106.633  47.159  1.00 55.43           N  
ATOM    193  CA  VAL A  86      42.797 106.079  47.121  1.00 55.14           C  
ATOM    194  C   VAL A  86      43.798 107.099  46.589  1.00 55.02           C  
ATOM    195  O   VAL A  86      43.603 107.664  45.515  1.00 55.06           O  
ATOM    196  CB  VAL A  86      42.859 104.784  46.286  1.00 55.07           C  
ATOM    197  CG1 VAL A  86      44.148 104.035  46.557  1.00 55.03           C  
ATOM    198  CG2 VAL A  86      41.662 103.895  46.588  1.00 54.95           C  
ATOM    199  N   THR A  87      44.866 107.324  47.349  1.00 54.91           N  
ATOM    200  CA  THR A  87      45.853 108.347  47.014  1.00 54.85           C  
ATOM    201  C   THR A  87      47.279 107.807  47.032  1.00 54.85           C  
ATOM    202  O   THR A  87      47.648 107.042  47.923  1.00 54.89           O  
ATOM    203  CB  THR A  87      45.743 109.544  47.989  1.00 54.82           C  
ATOM    204  OG1 THR A  87      44.384 109.709  48.415  1.00 54.60           O  
ATOM    205  CG2 THR A  87      46.041 110.844  47.266  1.00 54.73           C  
ATOM    206  N   LYS A  88      48.073 108.212  46.043  1.00 54.87           N  
ATOM    207  CA  LYS A  88      49.506 107.920  46.026  1.00 54.87           C  
ATOM    208  C   LYS A  88      50.214 108.907  46.945  1.00 55.13           C  
ATOM    209  O   LYS A  88      50.200 110.117  46.711  1.00 55.15           O  
ATOM    210  CB  LYS A  88      50.073 108.001  44.606  1.00 54.71           C  
ATOM    211  CG  LYS A  88      51.425 107.335  44.428  1.00 53.97           C  
ATOM    212  CD  LYS A  88      52.044 107.700  43.092  1.00 53.38           C  
ATOM    213  CE  LYS A  88      51.928 106.560  42.089  1.00 53.31           C  
ATOM    214  NZ  LYS A  88      53.231 106.224  41.440  1.00 52.82           N  
ATOM    215  N   VAL A  89      50.820 108.375  47.997  1.00 55.44           N  
ATOM    216  CA  VAL A  89      51.442 109.190  49.031  1.00 55.74           C  
ATOM    217  C   VAL A  89      52.870 108.719  49.319  1.00 56.09           C  
ATOM    218  O   VAL A  89      53.201 107.558  49.077  1.00 56.22           O  
ATOM    219  CB  VAL A  89      50.603 109.174  50.334  1.00 55.70           C  
ATOM    220  CG1 VAL A  89      49.322 109.982  50.161  1.00 55.68           C  
ATOM    221  CG2 VAL A  89      50.278 107.746  50.762  1.00 55.53           C  
ATOM    222  N   GLN A  90      53.710 109.625  49.821  1.00 56.46           N  
ATOM    223  CA  GLN A  90      55.078 109.287  50.221  1.00 56.77           C  
ATOM    224  C   GLN A  90      55.278 109.432  51.723  1.00 56.82           C  
ATOM    225  O   GLN A  90      54.845 110.416  52.324  1.00 56.85           O  
ATOM    226  CB  GLN A  90      56.099 110.158  49.484  1.00 56.87           C  
ATOM    227  CG  GLN A  90      57.206 109.364  48.783  1.00 57.72           C  
ATOM    228  CD  GLN A  90      58.541 109.373  49.533  1.00 58.85           C  
ATOM    229  OE1 GLN A  90      59.581 109.046  48.954  1.00 58.97           O  
ATOM    230  NE2 GLN A  90      58.514 109.738  50.813  1.00 59.40           N  
ATOM    231  N   HIS A  91      55.940 108.443  52.317  1.00 56.99           N  
ATOM    232  CA  HIS A  91      56.275 108.457  53.741  1.00 57.15           C  
ATOM    233  C   HIS A  91      57.633 109.134  53.976  1.00 57.23           C  
ATOM    234  O   HIS A  91      58.631 108.772  53.349  1.00 57.31           O  
ATOM    235  CB  HIS A  91      56.291 107.028  54.284  1.00 57.12           C  
ATOM    236  CG  HIS A  91      55.878 106.915  55.718  1.00 57.27           C  
ATOM    237  ND1 HIS A  91      56.597 106.188  56.643  1.00 57.16           N  
ATOM    238  CD2 HIS A  91      54.814 107.423  56.385  1.00 57.51           C  
ATOM    239  CE1 HIS A  91      55.998 106.259  57.818  1.00 57.20           C  
ATOM    240  NE2 HIS A  91      54.914 107.002  57.689  1.00 57.55           N  
ATOM    241  N   ARG A  92      57.661 110.113  54.879  1.00 57.22           N  
ATOM    242  CA  ARG A  92      58.883 110.865  55.188  1.00 57.17           C  
ATOM    243  C   ARG A  92      60.023 110.037  55.816  1.00 56.84           C  
ATOM    244  O   ARG A  92      61.157 110.126  55.342  1.00 56.75           O  
ATOM    245  CB  ARG A  92      58.564 112.085  56.065  1.00 57.41           C  
ATOM    246  CG  ARG A  92      59.101 113.405  55.523  1.00 58.11           C  
ATOM    247  CD  ARG A  92      58.296 114.642  55.945  1.00 58.84           C  
ATOM    248  NE  ARG A  92      56.891 114.604  55.520  1.00 59.41           N  
ATOM    249  CZ  ARG A  92      56.454 114.803  54.272  1.00 59.67           C  
ATOM    250  NH1 ARG A  92      57.301 115.052  53.277  1.00 59.54           N  
ATOM    251  NH2 ARG A  92      55.154 114.751  54.017  1.00 59.90           N  
ATOM    252  N   PRO A  93      59.742 109.242  56.860  1.00 56.56           N  
ATOM    253  CA  PRO A  93      60.793 108.493  57.558  1.00 56.21           C  
ATOM    254  C   PRO A  93      60.989 107.066  57.032  1.00 55.86           C  
ATOM    255  O   PRO A  93      61.298 106.161  57.817  1.00 55.92           O  
ATOM    256  CB  PRO A  93      60.279 108.460  59.001  1.00 56.28           C  
ATOM    257  CG  PRO A  93      58.768 108.515  58.878  1.00 56.44           C  
ATOM    258  CD  PRO A  93      58.427 108.987  57.478  1.00 56.58           C  
ATOM    259  N   SER A  94      60.810 106.876  55.726  1.00 55.37           N  
ATOM    260  CA  SER A  94      61.087 105.597  55.071  1.00 54.89           C  
ATOM    261  C   SER A  94      61.282 105.771  53.565  1.00 54.56           C  
ATOM    262  O   SER A  94      61.982 104.981  52.926  1.00 54.51           O  
ATOM    263  CB  SER A  94      59.979 104.574  55.358  1.00 54.93           C  
ATOM    264  OG  SER A  94      58.732 104.987  54.826  1.00 54.86           O  
ATOM    265  N   GLY A  95      60.659 106.809  53.010  1.00 54.19           N  
ATOM    266  CA  GLY A  95      60.727 107.097  51.586  1.00 53.68           C  
ATOM    267  C   GLY A  95      59.957 106.087  50.761  1.00 53.27           C  
ATOM    268  O   GLY A  95      60.287 105.841  49.601  1.00 53.35           O  
ATOM    269  N   LEU A  96      58.925 105.506  51.363  1.00 52.78           N  
ATOM    270  CA  LEU A  96      58.192 104.419  50.738  1.00 52.39           C  
ATOM    271  C   LEU A  96      56.845 104.875  50.207  1.00 52.07           C  
ATOM    272  O   LEU A  96      55.961 105.257  50.976  1.00 52.04           O  
ATOM    273  CB  LEU A  96      58.007 103.266  51.727  1.00 52.45           C  
ATOM    274  CG  LEU A  96      58.755 101.980  51.374  1.00 52.46           C  
ATOM    275  CD1 LEU A  96      59.360 101.366  52.621  1.00 52.15           C  
ATOM    276  CD2 LEU A  96      57.835 100.990  50.666  1.00 52.67           C  
ATOM    277  N   ILE A  97      56.699 104.827  48.886  1.00 51.64           N  
ATOM    278  CA  ILE A  97      55.443 105.180  48.231  1.00 51.26           C  
ATOM    279  C   ILE A  97      54.363 104.156  48.559  1.00 50.87           C  
ATOM    280  O   ILE A  97      54.423 103.017  48.102  1.00 51.03           O  
ATOM    281  CB  ILE A  97      55.631 105.318  46.697  1.00 51.34           C  
ATOM    282  CG1 ILE A  97      56.629 104.280  46.158  1.00 51.78           C  
ATOM    283  CG2 ILE A  97      56.086 106.728  46.344  1.00 51.48           C  
ATOM    284  CD1 ILE A  97      56.311 103.764  44.755  1.00 52.04           C  
ATOM    285  N   MET A  98      53.398 104.556  49.383  1.00 50.36           N  
ATOM    286  CA  MET A  98      52.258 103.700  49.708  1.00 49.87           C  
ATOM    287  C   MET A  98      50.964 104.225  49.097  1.00 49.73           C  
ATOM    288  O   MET A  98      50.932 105.314  48.524  1.00 49.74           O  
ATOM    289  CB  MET A  98      52.084 103.512  51.226  1.00 49.73           C  
ATOM    290  CG  MET A  98      52.865 104.459  52.120  1.00 49.20           C  
ATOM    291  SD  MET A  98      53.532 103.624  53.582  1.00 47.87           S  
ATOM    292  CE  MET A  98      52.296 103.932  54.746  1.00 47.85           C  
ATOM    293  N   ALA A  99      49.907 103.427  49.204  1.00 49.54           N  
ATOM    294  CA  ALA A  99      48.566 103.869  48.859  1.00 49.36           C  
ATOM    295  C   ALA A  99      47.802 104.131  50.144  1.00 49.28           C  
ATOM    296  O   ALA A  99      47.888 103.353  51.098  1.00 49.26           O  
ATOM    297  CB  ALA A  99      47.855 102.828  48.016  1.00 49.37           C  
ATOM    298  N   ARG A 100      47.071 105.239  50.168  1.00 49.16           N  
ATOM    299  CA  ARG A 100      46.280 105.620  51.328  1.00 49.10           C  
ATOM    300  C   ARG A 100      44.825 105.786  50.924  1.00 48.90           C  
ATOM    301  O   ARG A 100      44.523 106.484  49.958  1.00 48.82           O  
ATOM    302  CB  ARG A 100      46.817 106.919  51.935  1.00 49.19           C  
ATOM    303  CG  ARG A 100      46.195 107.287  53.269  1.00 49.68           C  
ATOM    304  CD  ARG A 100      45.516 108.645  53.280  1.00 50.46           C  
ATOM    305  NE  ARG A 100      45.876 109.418  54.467  1.00 51.17           N  
ATOM    306  CZ  ARG A 100      46.929 110.226  54.550  1.00 51.35           C  
ATOM    307  NH1 ARG A 100      47.744 110.386  53.509  1.00 51.23           N  
ATOM    308  NH2 ARG A 100      47.168 110.878  55.679  1.00 51.23           N  
ATOM    309  N   LYS A 101      43.933 105.136  51.663  1.00 48.82           N  
ATOM    310  CA  LYS A 101      42.505 105.233  51.392  1.00 48.87           C  
ATOM    311  C   LYS A 101      41.793 106.089  52.430  1.00 49.14           C  
ATOM    312  O   LYS A 101      41.855 105.819  53.631  1.00 49.06           O  
ATOM    313  CB  LYS A 101      41.856 103.848  51.303  1.00 48.77           C  
ATOM    314  CG  LYS A 101      40.639 103.804  50.388  1.00 48.26           C  
ATOM    315  CD  LYS A 101      39.929 102.469  50.442  1.00 47.38           C  
ATOM    316  CE  LYS A 101      39.906 101.821  49.073  1.00 47.16           C  
ATOM    317  NZ  LYS A 101      38.535 101.772  48.508  1.00 47.43           N  
ATOM    318  N   LEU A 102      41.122 107.129  51.944  1.00 49.49           N  
ATOM    319  CA  LEU A 102      40.313 107.998  52.784  1.00 49.76           C  
ATOM    320  C   LEU A 102      38.875 107.495  52.787  1.00 49.89           C  
ATOM    321  O   LEU A 102      38.111 107.770  51.861  1.00 49.84           O  
ATOM    322  CB  LEU A 102      40.358 109.450  52.274  1.00 49.83           C  
ATOM    323  CG  LEU A 102      41.569 110.389  52.423  1.00 49.80           C  
ATOM    324  CD1 LEU A 102      42.197 110.354  53.820  1.00 50.02           C  
ATOM    325  CD2 LEU A 102      42.614 110.127  51.341  1.00 49.81           C  
ATOM    326  N   ILE A 103      38.517 106.736  53.815  1.00 50.16           N  
ATOM    327  CA  ILE A 103      37.118 106.414  54.052  1.00 50.59           C  
ATOM    328  C   ILE A 103      36.550 107.522  54.929  1.00 51.12           C  
ATOM    329  O   ILE A 103      36.784 107.553  56.143  1.00 51.10           O  
ATOM    330  CB  ILE A 103      36.959 105.026  54.703  1.00 50.50           C  
ATOM    331  CG1 ILE A 103      37.329 103.928  53.705  1.00 50.33           C  
ATOM    332  CG2 ILE A 103      35.528 104.815  55.193  1.00 50.40           C  
ATOM    333  CD1 ILE A 103      38.484 103.079  54.137  1.00 49.93           C  
ATOM    334  N   HIS A 104      35.824 108.444  54.297  1.00 51.76           N  
ATOM    335  CA  HIS A 104      35.284 109.613  54.984  1.00 52.34           C  
ATOM    336  C   HIS A 104      34.042 109.254  55.783  1.00 52.61           C  
ATOM    337  O   HIS A 104      32.926 109.634  55.431  1.00 52.54           O  
ATOM    338  CB  HIS A 104      34.996 110.749  53.999  1.00 52.48           C  
ATOM    339  CG  HIS A 104      35.148 112.114  54.596  1.00 53.05           C  
ATOM    340  ND1 HIS A 104      36.307 112.853  54.479  1.00 53.51           N  
ATOM    341  CD2 HIS A 104      34.291 112.869  55.324  1.00 53.33           C  
ATOM    342  CE1 HIS A 104      36.156 114.006  55.108  1.00 53.62           C  
ATOM    343  NE2 HIS A 104      34.943 114.041  55.629  1.00 53.56           N  
ATOM    344  N   LEU A 105      34.258 108.520  56.869  1.00 53.17           N  
ATOM    345  CA  LEU A 105      33.169 108.025  57.696  1.00 53.73           C  
ATOM    346  C   LEU A 105      32.671 109.064  58.685  1.00 54.10           C  
ATOM    347  O   LEU A 105      33.460 109.713  59.383  1.00 54.16           O  
ATOM    348  CB  LEU A 105      33.578 106.752  58.427  1.00 53.75           C  
ATOM    349  CG  LEU A 105      32.909 105.478  57.915  1.00 54.00           C  
ATOM    350  CD1 LEU A 105      33.661 104.269  58.438  1.00 54.47           C  
ATOM    351  CD2 LEU A 105      31.437 105.423  58.313  1.00 53.73           C  
ATOM    352  N   GLU A 106      31.346 109.190  58.730  1.00 54.46           N  
ATOM    353  CA  GLU A 106      30.645 110.223  59.486  1.00 54.79           C  
ATOM    354  C   GLU A 106      30.808 110.047  60.996  1.00 54.84           C  
ATOM    355  O   GLU A 106      31.685 110.675  61.605  1.00 54.93           O  
ATOM    356  CB  GLU A 106      29.154 110.260  59.106  1.00 54.95           C  
ATOM    357  CG  GLU A 106      28.777 109.507  57.828  1.00 55.49           C  
ATOM    358  CD  GLU A 106      28.538 108.013  58.039  1.00 55.82           C  
ATOM    359  OE1 GLU A 106      28.487 107.556  59.205  1.00 55.90           O  
ATOM    360  OE2 GLU A 106      28.403 107.289  57.026  1.00 55.71           O  
ATOM    361  N   ILE A 107      29.972 109.189  61.586  1.00 54.78           N  
ATOM    362  CA  ILE A 107      29.956 108.965  63.034  1.00 54.73           C  
ATOM    363  C   ILE A 107      31.363 108.720  63.608  1.00 54.61           C  
ATOM    364  O   ILE A 107      32.190 108.026  62.993  1.00 54.59           O  
ATOM    365  CB  ILE A 107      28.932 107.843  63.402  1.00 54.79           C  
ATOM    366  CG1 ILE A 107      28.154 108.213  64.669  1.00 54.87           C  
ATOM    367  CG2 ILE A 107      29.598 106.469  63.529  1.00 54.94           C  
ATOM    368  CD1 ILE A 107      26.787 108.828  64.398  1.00 54.86           C  
ATOM    369  N   LYS A 108      31.627 109.312  64.774  1.00 54.43           N  
ATOM    370  CA  LYS A 108      32.993 109.415  65.303  1.00 54.32           C  
ATOM    371  C   LYS A 108      33.153 109.226  66.840  1.00 54.70           C  
ATOM    372  O   LYS A 108      33.979 109.910  67.464  1.00 54.82           O  
ATOM    373  CB  LYS A 108      33.596 110.761  64.853  1.00 54.03           C  
ATOM    374  CG  LYS A 108      35.127 110.854  64.832  1.00 52.18           C  
ATOM    375  CD  LYS A 108      35.557 112.292  65.158  1.00 49.25           C  
ATOM    376  CE  LYS A 108      37.040 112.404  65.489  1.00 47.29           C  
ATOM    377  NZ  LYS A 108      37.545 113.791  65.262  1.00 45.59           N  
ATOM    378  N   PRO A 109      32.383 108.320  67.457  1.00 54.83           N  
ATOM    379  CA  PRO A 109      32.581 107.994  68.876  1.00 54.96           C  
ATOM    380  C   PRO A 109      33.473 106.752  69.110  1.00 55.03           C  
ATOM    381  O   PRO A 109      34.471 106.557  68.405  1.00 54.98           O  
ATOM    382  CB  PRO A 109      31.145 107.744  69.366  1.00 54.96           C  
ATOM    383  CG  PRO A 109      30.286 107.699  68.092  1.00 54.96           C  
ATOM    384  CD  PRO A 109      31.228 107.588  66.915  1.00 54.80           C  
ATOM    385  N   ALA A 110      33.102 105.933  70.095  1.00 55.03           N  
ATOM    386  CA  ALA A 110      33.826 104.712  70.440  1.00 55.04           C  
ATOM    387  C   ALA A 110      33.708 103.624  69.368  1.00 55.06           C  
ATOM    388  O   ALA A 110      34.398 102.604  69.430  1.00 55.10           O  
ATOM    389  CB  ALA A 110      33.349 104.182  71.792  1.00 55.09           C  
ATOM    390  N   ILE A 111      32.824 103.842  68.398  1.00 55.08           N  
ATOM    391  CA  ILE A 111      32.689 102.946  67.253  1.00 55.06           C  
ATOM    392  C   ILE A 111      33.864 103.146  66.289  1.00 55.02           C  
ATOM    393  O   ILE A 111      34.510 102.177  65.880  1.00 54.98           O  
ATOM    394  CB  ILE A 111      31.298 103.135  66.563  1.00 55.08           C  
ATOM    395  CG1 ILE A 111      30.210 102.318  67.286  1.00 55.23           C  
ATOM    396  CG2 ILE A 111      31.343 102.805  65.066  1.00 55.02           C  
ATOM    397  CD1 ILE A 111      30.560 100.851  67.580  1.00 55.17           C  
ATOM    398  N   ARG A 112      34.152 104.402  65.950  1.00 54.94           N  
ATOM    399  CA  ARG A 112      35.333 104.725  65.152  1.00 54.95           C  
ATOM    400  C   ARG A 112      36.585 104.107  65.794  1.00 54.70           C  
ATOM    401  O   ARG A 112      37.494 103.645  65.097  1.00 54.74           O  
ATOM    402  CB  ARG A 112      35.451 106.246  64.960  1.00 55.12           C  
ATOM    403  CG  ARG A 112      36.807 106.866  65.266  1.00 55.90           C  
ATOM    404  CD  ARG A 112      36.763 107.927  66.357  1.00 57.72           C  
ATOM    405  NE  ARG A 112      37.931 107.856  67.239  1.00 59.28           N  
ATOM    406  CZ  ARG A 112      38.561 108.912  67.755  1.00 59.70           C  
ATOM    407  NH1 ARG A 112      38.143 110.146  67.486  1.00 59.80           N  
ATOM    408  NH2 ARG A 112      39.617 108.734  68.545  1.00 59.62           N  
ATOM    409  N   ASN A 113      36.593 104.072  67.126  1.00 54.35           N  
ATOM    410  CA  ASN A 113      37.672 103.463  67.901  1.00 53.90           C  
ATOM    411  C   ASN A 113      37.700 101.928  67.825  1.00 53.48           C  
ATOM    412  O   ASN A 113      38.748 101.309  68.025  1.00 53.44           O  
ATOM    413  CB  ASN A 113      37.600 103.930  69.362  1.00 53.96           C  
ATOM    414  CG  ASN A 113      38.863 104.650  69.812  1.00 54.00           C  
ATOM    415  OD1 ASN A 113      39.514 104.240  70.772  1.00 53.62           O  
ATOM    416  ND2 ASN A 113      39.211 105.730  69.120  1.00 54.40           N  
ATOM    417  N   GLN A 114      36.548 101.321  67.546  1.00 52.94           N  
ATOM    418  CA  GLN A 114      36.467  99.873  67.361  1.00 52.38           C  
ATOM    419  C   GLN A 114      36.917  99.501  65.954  1.00 51.77           C  
ATOM    420  O   GLN A 114      37.429  98.404  65.735  1.00 51.66           O  
ATOM    421  CB  GLN A 114      35.042  99.364  67.610  1.00 52.51           C  
ATOM    422  CG  GLN A 114      34.928  97.859  67.866  1.00 52.98           C  
ATOM    423  CD  GLN A 114      33.490  97.353  67.774  1.00 54.01           C  
ATOM    424  OE1 GLN A 114      33.111  96.711  66.788  1.00 54.23           O  
ATOM    425  NE2 GLN A 114      32.690  97.641  68.800  1.00 54.38           N  
ATOM    426  N   ILE A 115      36.724 100.423  65.009  1.00 50.98           N  
ATOM    427  CA  ILE A 115      37.065 100.184  63.608  1.00 50.09           C  
ATOM    428  C   ILE A 115      38.565  99.945  63.446  1.00 49.46           C  
ATOM    429  O   ILE A 115      38.974  98.901  62.943  1.00 49.44           O  
ATOM    430  CB  ILE A 115      36.556 101.336  62.695  1.00 50.12           C  
ATOM    431  CG1 ILE A 115      35.031 101.277  62.577  1.00 49.85           C  
ATOM    432  CG2 ILE A 115      37.198 101.263  61.304  1.00 49.99           C  
ATOM    433  CD1 ILE A 115      34.379 102.585  62.185  1.00 49.93           C  
ATOM    434  N   ILE A 116      39.375 100.902  63.890  1.00 48.64           N  
ATOM    435  CA  ILE A 116      40.823 100.770  63.790  1.00 47.97           C  
ATOM    436  C   ILE A 116      41.299  99.552  64.589  1.00 47.53           C  
ATOM    437  O   ILE A 116      42.148  98.791  64.120  1.00 47.35           O  
ATOM    438  CB  ILE A 116      41.525 102.090  64.213  1.00 47.95           C  
ATOM    439  CG1 ILE A 116      41.626 103.038  63.017  1.00 47.86           C  
ATOM    440  CG2 ILE A 116      42.920 101.839  64.770  1.00 47.97           C  
ATOM    441  CD1 ILE A 116      40.914 104.357  63.211  1.00 47.63           C  
ATOM    442  N   ARG A 117      40.714  99.357  65.771  1.00 47.04           N  
ATOM    443  CA  ARG A 117      41.022  98.210  66.624  1.00 46.65           C  
ATOM    444  C   ARG A 117      40.658  96.894  65.954  1.00 46.37           C  
ATOM    445  O   ARG A 117      41.278  95.865  66.223  1.00 46.45           O  
ATOM    446  CB  ARG A 117      40.286  98.315  67.960  1.00 46.68           C  
ATOM    447  CG  ARG A 117      40.992  97.622  69.117  0.50 46.76           C  
ATOM    448  CD  ARG A 117      41.792  98.562  70.016  0.50 46.81           C  
ATOM    449  NE  ARG A 117      40.987  99.095  71.115  0.50 46.46           N  
ATOM    450  CZ  ARG A 117      40.899  98.546  72.322  0.50 46.42           C  
ATOM    451  NH1 ARG A 117      41.569  97.435  72.609  0.50 46.17           N  
ATOM    452  NH2 ARG A 117      40.137  99.110  73.250  0.50 46.50           N  
ATOM    453  N   GLU A 118      39.642  96.936  65.092  1.00 45.97           N  
ATOM    454  CA  GLU A 118      39.201  95.761  64.344  1.00 45.41           C  
ATOM    455  C   GLU A 118      40.052  95.577  63.091  1.00 44.83           C  
ATOM    456  O   GLU A 118      40.304  94.446  62.665  1.00 44.94           O  
ATOM    457  CB  GLU A 118      37.720  95.876  63.972  1.00 45.48           C  
ATOM    458  CG  GLU A 118      36.770  95.110  64.879  1.00 46.11           C  
ATOM    459  CD  GLU A 118      35.447  94.795  64.198  1.00 47.62           C  
ATOM    460  OE1 GLU A 118      35.362  93.756  63.504  1.00 48.52           O  
ATOM    461  OE2 GLU A 118      34.488  95.585  64.351  1.00 47.83           O  
ATOM    462  N   LEU A 119      40.498  96.690  62.512  1.00 43.94           N  
ATOM    463  CA  LEU A 119      41.325  96.660  61.312  1.00 43.16           C  
ATOM    464  C   LEU A 119      42.686  96.010  61.553  1.00 42.75           C  
ATOM    465  O   LEU A 119      43.285  95.475  60.625  1.00 42.79           O  
ATOM    466  CB  LEU A 119      41.516  98.069  60.751  1.00 43.07           C  
ATOM    467  CG  LEU A 119      40.387  98.655  59.902  1.00 42.92           C  
ATOM    468  CD1 LEU A 119      40.583 100.156  59.743  1.00 42.80           C  
ATOM    469  CD2 LEU A 119      40.297  97.981  58.541  1.00 42.54           C  
ATOM    470  N   GLN A 120      43.157  96.048  62.801  1.00 42.18           N  
ATOM    471  CA  GLN A 120      44.512  95.604  63.164  1.00 41.34           C  
ATOM    472  C   GLN A 120      44.850  94.181  62.729  1.00 40.67           C  
ATOM    473  O   GLN A 120      46.007  93.880  62.461  1.00 40.62           O  
ATOM    474  CB  GLN A 120      44.755  95.761  64.670  1.00 41.28           C  
ATOM    475  CG  GLN A 120      44.858  97.202  65.146  1.00 41.43           C  
ATOM    476  CD  GLN A 120      45.935  97.997  64.423  1.00 41.70           C  
ATOM    477  OE1 GLN A 120      47.116  97.659  64.499  1.00 42.07           O  
ATOM    478  NE2 GLN A 120      45.531  99.061  63.730  1.00 41.22           N  
ATOM    479  N   VAL A 121      43.843  93.318  62.651  1.00 39.85           N  
ATOM    480  CA  VAL A 121      44.041  91.943  62.190  1.00 39.33           C  
ATOM    481  C   VAL A 121      44.655  91.857  60.776  1.00 38.77           C  
ATOM    482  O   VAL A 121      45.026  90.776  60.316  1.00 38.72           O  
ATOM    483  CB  VAL A 121      42.727  91.107  62.268  1.00 39.37           C  
ATOM    484  CG1 VAL A 121      42.373  90.786  63.713  1.00 39.65           C  
ATOM    485  CG2 VAL A 121      41.577  91.832  61.607  1.00 39.71           C  
ATOM    486  N   LEU A 122      44.764  93.005  60.108  1.00 38.14           N  
ATOM    487  CA  LEU A 122      45.339  93.110  58.766  1.00 37.43           C  
ATOM    488  C   LEU A 122      46.858  93.022  58.798  1.00 36.93           C  
ATOM    489  O   LEU A 122      47.498  92.834  57.762  1.00 36.81           O  
ATOM    490  CB  LEU A 122      44.944  94.439  58.127  1.00 37.46           C  
ATOM    491  CG  LEU A 122      43.842  94.533  57.080  1.00 37.54           C  
ATOM    492  CD1 LEU A 122      43.247  95.925  57.123  1.00 37.52           C  
ATOM    493  CD2 LEU A 122      44.390  94.245  55.698  1.00 37.93           C  
ATOM    494  N   HIS A 123      47.427  93.190  59.988  1.00 36.47           N  
ATOM    495  CA  HIS A 123      48.861  93.017  60.200  1.00 36.01           C  
ATOM    496  C   HIS A 123      49.193  91.533  60.176  1.00 35.75           C  
ATOM    497  O   HIS A 123      50.269  91.139  59.739  1.00 35.70           O  
ATOM    498  CB  HIS A 123      49.294  93.631  61.532  1.00 35.93           C  
ATOM    499  CG  HIS A 123      49.495  95.115  61.484  1.00 35.70           C  
ATOM    500  ND1 HIS A 123      48.940  95.970  62.411  1.00 35.64           N  
ATOM    501  CD2 HIS A 123      50.196  95.895  60.627  1.00 35.58           C  
ATOM    502  CE1 HIS A 123      49.287  97.212  62.126  1.00 35.68           C  
ATOM    503  NE2 HIS A 123      50.049  97.195  61.048  1.00 35.61           N  
ATOM    504  N   GLU A 124      48.248  90.719  60.634  1.00 35.48           N  
ATOM    505  CA  GLU A 124      48.393  89.274  60.615  1.00 35.39           C  
ATOM    506  C   GLU A 124      47.953  88.679  59.279  1.00 35.13           C  
ATOM    507  O   GLU A 124      48.007  87.462  59.093  1.00 35.38           O  
ATOM    508  CB  GLU A 124      47.611  88.646  61.769  1.00 35.43           C  
ATOM    509  CG  GLU A 124      48.491  87.863  62.736  1.00 36.58           C  
ATOM    510  CD  GLU A 124      48.613  88.513  64.109  1.00 37.63           C  
ATOM    511  OE1 GLU A 124      48.330  87.825  65.119  1.00 38.71           O  
ATOM    512  OE2 GLU A 124      48.999  89.703  64.187  1.00 37.25           O  
ATOM    513  N   CYS A 125      47.529  89.539  58.353  1.00 34.71           N  
ATOM    514  CA  CYS A 125      47.060  89.110  57.038  1.00 34.19           C  
ATOM    515  C   CYS A 125      48.191  89.121  56.029  1.00 33.91           C  
ATOM    516  O   CYS A 125      48.473  90.148  55.416  1.00 34.06           O  
ATOM    517  CB  CYS A 125      45.946  90.026  56.551  1.00 34.09           C  
ATOM    518  SG  CYS A 125      44.305  89.532  57.091  1.00 34.47           S  
ATOM    519  N   ASN A 126      48.841  87.978  55.854  1.00 33.60           N  
ATOM    520  CA  ASN A 126      49.965  87.893  54.927  1.00 33.36           C  
ATOM    521  C   ASN A 126      49.906  86.712  53.967  1.00 32.89           C  
ATOM    522  O   ASN A 126      49.921  85.548  54.375  1.00 32.76           O  
ATOM    523  CB  ASN A 126      51.300  87.944  55.679  1.00 33.57           C  
ATOM    524  CG  ASN A 126      51.473  89.238  56.462  1.00 34.34           C  
ATOM    525  OD1 ASN A 126      51.732  90.309  55.891  1.00 35.03           O  
ATOM    526  ND2 ASN A 126      51.304  89.150  57.776  1.00 34.91           N  
ATOM    527  N   SER A 127      49.826  87.046  52.685  1.00 32.33           N  
ATOM    528  CA  SER A 127      49.789  86.081  51.603  1.00 31.95           C  
ATOM    529  C   SER A 127      50.229  86.818  50.351  1.00 31.69           C  
ATOM    530  O   SER A 127      49.919  88.002  50.206  1.00 31.76           O  
ATOM    531  CB  SER A 127      48.369  85.542  51.418  1.00 32.01           C  
ATOM    532  OG  SER A 127      48.255  84.785  50.224  1.00 31.86           O  
ATOM    533  N   PRO A 128      50.951  86.142  49.453  1.00 31.42           N  
ATOM    534  CA  PRO A 128      51.357  86.747  48.175  1.00 31.22           C  
ATOM    535  C   PRO A 128      50.160  87.107  47.298  1.00 31.09           C  
ATOM    536  O   PRO A 128      50.331  87.546  46.163  1.00 31.17           O  
ATOM    537  CB  PRO A 128      52.181  85.642  47.515  1.00 30.97           C  
ATOM    538  CG  PRO A 128      51.723  84.402  48.159  1.00 31.17           C  
ATOM    539  CD  PRO A 128      51.456  84.764  49.583  1.00 31.36           C  
ATOM    540  N   TYR A 129      48.962  86.929  47.842  1.00 30.96           N  
ATOM    541  CA  TYR A 129      47.733  87.110  47.099  1.00 30.98           C  
ATOM    542  C   TYR A 129      46.823  88.138  47.766  1.00 31.16           C  
ATOM    543  O   TYR A 129      45.702  88.366  47.319  1.00 31.18           O  
ATOM    544  CB  TYR A 129      47.022  85.760  46.956  1.00 31.03           C  
ATOM    545  CG  TYR A 129      47.858  84.692  46.280  1.00 30.71           C  
ATOM    546  CD1 TYR A 129      48.115  83.475  46.908  1.00 30.52           C  
ATOM    547  CD2 TYR A 129      48.396  84.901  45.015  1.00 30.73           C  
ATOM    548  CE1 TYR A 129      48.891  82.492  46.286  1.00 30.53           C  
ATOM    549  CE2 TYR A 129      49.168  83.930  44.387  1.00 31.09           C  
ATOM    550  CZ  TYR A 129      49.412  82.728  45.023  1.00 30.60           C  
ATOM    551  OH  TYR A 129      50.179  81.776  44.384  1.00 30.03           O  
ATOM    552  N   ILE A 130      47.320  88.750  48.839  1.00 31.47           N  
ATOM    553  CA  ILE A 130      46.606  89.793  49.572  1.00 31.65           C  
ATOM    554  C   ILE A 130      47.504  91.016  49.692  1.00 32.03           C  
ATOM    555  O   ILE A 130      48.634  90.917  50.170  1.00 31.90           O  
ATOM    556  CB  ILE A 130      46.196  89.301  50.987  1.00 31.55           C  
ATOM    557  CG1 ILE A 130      45.395  87.990  50.930  1.00 31.68           C  
ATOM    558  CG2 ILE A 130      45.447  90.387  51.742  1.00 31.27           C  
ATOM    559  CD1 ILE A 130      44.051  88.056  50.195  1.00 31.99           C  
ATOM    560  N   VAL A 131      46.986  92.163  49.263  1.00 32.78           N  
ATOM    561  CA  VAL A 131      47.717  93.431  49.289  1.00 33.58           C  
ATOM    562  C   VAL A 131      48.222  93.774  50.693  1.00 34.30           C  
ATOM    563  O   VAL A 131      47.511  93.585  51.682  1.00 34.47           O  
ATOM    564  CB  VAL A 131      46.856  94.596  48.740  1.00 33.39           C  
ATOM    565  CG1 VAL A 131      47.696  95.844  48.549  1.00 33.46           C  
ATOM    566  CG2 VAL A 131      46.222  94.216  47.420  1.00 33.37           C  
ATOM    567  N   GLY A 132      49.456  94.270  50.764  1.00 35.02           N  
ATOM    568  CA  GLY A 132      50.083  94.642  52.020  1.00 36.04           C  
ATOM    569  C   GLY A 132      49.353  95.733  52.779  1.00 36.79           C  
ATOM    570  O   GLY A 132      48.488  96.415  52.228  1.00 36.79           O  
ATOM    571  N   PHE A 133      49.719  95.896  54.048  1.00 37.61           N  
ATOM    572  CA  PHE A 133      49.028  96.801  54.958  1.00 38.46           C  
ATOM    573  C   PHE A 133      50.013  97.393  55.954  1.00 38.97           C  
ATOM    574  O   PHE A 133      50.555  96.679  56.798  1.00 39.07           O  
ATOM    575  CB  PHE A 133      47.914  96.036  55.683  1.00 38.60           C  
ATOM    576  CG  PHE A 133      47.284  96.790  56.821  1.00 39.21           C  
ATOM    577  CD1 PHE A 133      47.552  96.433  58.140  1.00 39.92           C  
ATOM    578  CD2 PHE A 133      46.409  97.840  56.580  1.00 39.74           C  
ATOM    579  CE1 PHE A 133      46.965  97.120  59.205  1.00 39.88           C  
ATOM    580  CE2 PHE A 133      45.820  98.532  57.635  1.00 40.16           C  
ATOM    581  CZ  PHE A 133      46.097  98.166  58.951  1.00 40.02           C  
ATOM    582  N   TYR A 134      50.241  98.700  55.853  1.00 39.74           N  
ATOM    583  CA  TYR A 134      51.169  99.400  56.740  1.00 40.51           C  
ATOM    584  C   TYR A 134      50.541  99.847  58.066  1.00 41.29           C  
ATOM    585  O   TYR A 134      51.250 100.060  59.057  1.00 41.40           O  
ATOM    586  CB  TYR A 134      51.757 100.610  56.033  1.00 40.34           C  
ATOM    587  CG  TYR A 134      52.507 100.289  54.767  1.00 40.35           C  
ATOM    588  CD1 TYR A 134      53.835  99.862  54.807  1.00 40.23           C  
ATOM    589  CD2 TYR A 134      51.897 100.429  53.522  1.00 40.36           C  
ATOM    590  CE1 TYR A 134      54.534  99.576  53.637  1.00 39.98           C  
ATOM    591  CE2 TYR A 134      52.588 100.147  52.347  1.00 40.20           C  
ATOM    592  CZ  TYR A 134      53.903  99.722  52.412  1.00 40.14           C  
ATOM    593  OH  TYR A 134      54.581  99.441  51.250  1.00 40.60           O  
ATOM    594  N   GLY A 135      49.217  99.997  58.076  1.00 42.22           N  
ATOM    595  CA  GLY A 135      48.495 100.444  59.255  1.00 43.35           C  
ATOM    596  C   GLY A 135      47.301 101.324  58.935  1.00 44.12           C  
ATOM    597  O   GLY A 135      47.058 101.660  57.775  1.00 44.08           O  
ATOM    598  N   ALA A 136      46.553 101.689  59.973  1.00 45.03           N  
ATOM    599  CA  ALA A 136      45.363 102.523  59.820  1.00 46.14           C  
ATOM    600  C   ALA A 136      45.150 103.423  61.032  1.00 46.96           C  
ATOM    601  O   ALA A 136      45.436 103.026  62.164  1.00 47.32           O  
ATOM    602  CB  ALA A 136      44.139 101.660  59.583  1.00 46.12           C  
ATOM    603  N   PHE A 137      44.637 104.628  60.796  1.00 47.80           N  
ATOM    604  CA  PHE A 137      44.515 105.619  61.865  1.00 48.62           C  
ATOM    605  C   PHE A 137      43.346 106.567  61.679  1.00 49.39           C  
ATOM    606  O   PHE A 137      42.839 106.722  60.567  1.00 49.52           O  
ATOM    607  CB  PHE A 137      45.808 106.425  61.992  1.00 48.46           C  
ATOM    608  CG  PHE A 137      46.344 106.931  60.683  1.00 48.17           C  
ATOM    609  CD1 PHE A 137      47.141 106.120  59.881  1.00 47.82           C  
ATOM    610  CD2 PHE A 137      46.070 108.226  60.262  1.00 48.09           C  
ATOM    611  CE1 PHE A 137      47.647 106.590  58.677  1.00 47.93           C  
ATOM    612  CE2 PHE A 137      46.575 108.706  59.056  1.00 48.12           C  
ATOM    613  CZ  PHE A 137      47.363 107.886  58.262  1.00 47.98           C  
ATOM    614  N   TYR A 138      42.931 107.196  62.780  1.00 50.40           N  
ATOM    615  CA  TYR A 138      41.900 108.242  62.767  1.00 51.43           C  
ATOM    616  C   TYR A 138      42.519 109.624  62.498  1.00 51.46           C  
ATOM    617  O   TYR A 138      43.485 110.025  63.156  1.00 51.40           O  
ATOM    618  CB  TYR A 138      41.079 108.234  64.076  1.00 51.82           C  
ATOM    619  CG  TYR A 138      41.818 108.757  65.305  1.00 53.51           C  
ATOM    620  CD1 TYR A 138      41.624 110.071  65.757  1.00 54.76           C  
ATOM    621  CD2 TYR A 138      42.707 107.941  66.016  1.00 54.80           C  
ATOM    622  CE1 TYR A 138      42.302 110.560  66.879  1.00 55.70           C  
ATOM    623  CE2 TYR A 138      43.392 108.421  67.140  1.00 55.88           C  
ATOM    624  CZ  TYR A 138      43.184 109.730  67.566  1.00 56.26           C  
ATOM    625  OH  TYR A 138      43.855 110.207  68.676  1.00 56.94           O  
ATOM    626  N   SER A 139      41.962 110.334  61.519  1.00 51.69           N  
ATOM    627  CA  SER A 139      42.487 111.637  61.098  1.00 51.90           C  
ATOM    628  C   SER A 139      41.362 112.589  60.667  1.00 51.94           C  
ATOM    629  O   SER A 139      40.933 112.587  59.503  1.00 51.93           O  
ATOM    630  CB  SER A 139      43.526 111.473  59.977  1.00 51.87           C  
ATOM    631  OG  SER A 139      44.437 112.562  59.963  1.00 51.86           O  
ATOM    632  N   ASP A 140      40.910 113.405  61.621  1.00 51.89           N  
ATOM    633  CA  ASP A 140      39.748 114.287  61.453  1.00 51.83           C  
ATOM    634  C   ASP A 140      38.540 113.484  60.962  1.00 51.55           C  
ATOM    635  O   ASP A 140      38.070 113.670  59.833  1.00 51.45           O  
ATOM    636  CB  ASP A 140      40.046 115.485  60.522  1.00 52.00           C  
ATOM    637  CG  ASP A 140      41.517 115.907  60.537  1.00 52.39           C  
ATOM    638  OD1 ASP A 140      42.044 116.248  59.453  1.00 52.56           O  
ATOM    639  OD2 ASP A 140      42.219 115.933  61.575  1.00 52.97           O  
ATOM    640  N   GLY A 141      38.064 112.577  61.815  1.00 51.25           N  
ATOM    641  CA  GLY A 141      36.952 111.702  61.483  1.00 50.81           C  
ATOM    642  C   GLY A 141      37.341 110.678  60.435  1.00 50.51           C  
ATOM    643  O   GLY A 141      37.488 109.492  60.750  1.00 50.57           O  
ATOM    644  N   GLU A 142      37.521 111.147  59.197  1.00 50.05           N  
ATOM    645  CA  GLU A 142      37.892 110.299  58.053  1.00 49.61           C  
ATOM    646  C   GLU A 142      39.120 109.405  58.295  1.00 48.89           C  
ATOM    647  O   GLU A 142      40.247 109.893  58.416  1.00 48.71           O  
ATOM    648  CB  GLU A 142      38.073 111.134  56.774  1.00 49.74           C  
ATOM    649  CG  GLU A 142      38.825 112.444  56.951  1.00 50.46           C  
ATOM    650  CD  GLU A 142      39.963 112.600  55.963  1.00 51.30           C  
ATOM    651  OE1 GLU A 142      39.695 112.542  54.743  1.00 51.52           O  
ATOM    652  OE2 GLU A 142      41.122 112.782  56.408  1.00 51.60           O  
ATOM    653  N   ILE A 143      38.877 108.095  58.354  1.00 48.07           N  
ATOM    654  CA  ILE A 143      39.918 107.115  58.657  1.00 47.35           C  
ATOM    655  C   ILE A 143      40.848 106.867  57.467  1.00 46.82           C  
ATOM    656  O   ILE A 143      40.465 107.068  56.313  1.00 46.80           O  
ATOM    657  CB  ILE A 143      39.306 105.785  59.187  1.00 47.36           C  
ATOM    658  CG1 ILE A 143      38.731 104.949  58.049  1.00 47.40           C  
ATOM    659  CG2 ILE A 143      38.236 106.047  60.246  1.00 47.34           C  
ATOM    660  CD1 ILE A 143      39.449 103.642  57.860  1.00 47.85           C  
ATOM    661  N   SER A 144      42.071 106.438  57.762  1.00 46.21           N  
ATOM    662  CA  SER A 144      43.080 106.224  56.731  1.00 45.72           C  
ATOM    663  C   SER A 144      43.707 104.836  56.823  1.00 45.35           C  
ATOM    664  O   SER A 144      44.499 104.568  57.732  1.00 45.40           O  
ATOM    665  CB  SER A 144      44.178 107.289  56.814  1.00 45.67           C  
ATOM    666  OG  SER A 144      43.673 108.589  56.568  1.00 45.75           O  
ATOM    667  N   ILE A 145      43.338 103.961  55.886  1.00 44.74           N  
ATOM    668  CA  ILE A 145      44.008 102.673  55.702  1.00 43.94           C  
ATOM    669  C   ILE A 145      45.174 102.856  54.731  1.00 43.45           C  
ATOM    670  O   ILE A 145      44.982 103.220  53.568  1.00 43.32           O  
ATOM    671  CB  ILE A 145      43.026 101.589  55.180  1.00 43.94           C  
ATOM    672  CG1 ILE A 145      41.915 101.319  56.201  1.00 43.97           C  
ATOM    673  CG2 ILE A 145      43.774 100.297  54.853  1.00 43.66           C  
ATOM    674  CD1 ILE A 145      40.757 100.466  55.666  1.00 43.65           C  
ATOM    675  N   CYS A 146      46.384 102.612  55.220  1.00 42.85           N  
ATOM    676  CA  CYS A 146      47.570 102.717  54.384  1.00 42.33           C  
ATOM    677  C   CYS A 146      48.005 101.342  53.904  1.00 41.99           C  
ATOM    678  O   CYS A 146      48.192 100.422  54.701  1.00 41.90           O  
ATOM    679  CB  CYS A 146      48.686 103.422  55.138  1.00 42.35           C  
ATOM    680  SG  CYS A 146      48.278 105.136  55.513  1.00 42.32           S  
ATOM    681  N   MET A 147      48.153 101.211  52.591  1.00 41.57           N  
ATOM    682  CA  MET A 147      48.353  99.906  51.975  1.00 41.23           C  
ATOM    683  C   MET A 147      49.446  99.903  50.906  1.00 40.92           C  
ATOM    684  O   MET A 147      49.848 100.956  50.412  1.00 40.93           O  
ATOM    685  CB  MET A 147      47.025  99.384  51.406  1.00 41.32           C  
ATOM    686  CG  MET A 147      46.572 100.053  50.109  1.00 41.31           C  
ATOM    687  SD  MET A 147      44.927  99.534  49.584  1.00 41.69           S  
ATOM    688  CE  MET A 147      43.947 100.932  50.167  1.00 40.43           C  
ATOM    689  N   GLU A 148      49.907  98.701  50.563  1.00 40.50           N  
ATOM    690  CA  GLU A 148      50.941  98.479  49.554  1.00 40.21           C  
ATOM    691  C   GLU A 148      50.550  99.040  48.183  1.00 39.89           C  
ATOM    692  O   GLU A 148      49.527  98.658  47.616  1.00 39.96           O  
ATOM    693  CB  GLU A 148      51.256  96.976  49.464  1.00 40.32           C  
ATOM    694  CG  GLU A 148      52.035  96.523  48.231  1.00 40.43           C  
ATOM    695  CD  GLU A 148      52.135  95.005  48.091  1.00 40.75           C  
ATOM    696  OE1 GLU A 148      51.325  94.260  48.698  1.00 40.42           O  
ATOM    697  OE2 GLU A 148      53.038  94.549  47.358  1.00 41.21           O  
ATOM    698  N   HIS A 149      51.376  99.940  47.659  1.00 39.40           N  
ATOM    699  CA  HIS A 149      51.134 100.528  46.348  1.00 39.04           C  
ATOM    700  C   HIS A 149      51.426  99.540  45.213  1.00 38.80           C  
ATOM    701  O   HIS A 149      52.580  99.177  44.959  1.00 38.81           O  
ATOM    702  CB  HIS A 149      51.939 101.818  46.176  1.00 39.11           C  
ATOM    703  CG  HIS A 149      52.111 102.235  44.750  1.00 39.09           C  
ATOM    704  ND1 HIS A 149      53.313 102.124  44.085  1.00 39.27           N  
ATOM    705  CD2 HIS A 149      51.230 102.745  43.857  1.00 39.01           C  
ATOM    706  CE1 HIS A 149      53.167 102.559  42.845  1.00 39.57           C  
ATOM    707  NE2 HIS A 149      51.913 102.940  42.681  1.00 39.26           N  
ATOM    708  N   MET A 150      50.359  99.118  44.539  1.00 38.37           N  
ATOM    709  CA  MET A 150      50.440  98.184  43.422  1.00 37.95           C  
ATOM    710  C   MET A 150      50.616  98.930  42.101  1.00 37.64           C  
ATOM    711  O   MET A 150      49.647  99.433  41.519  1.00 37.56           O  
ATOM    712  CB  MET A 150      49.188  97.315  43.382  1.00 38.02           C  
ATOM    713  CG  MET A 150      48.903  96.599  44.688  1.00 38.33           C  
ATOM    714  SD  MET A 150      50.018  95.225  44.962  1.00 39.41           S  
ATOM    715  CE  MET A 150      49.697  94.199  43.515  1.00 39.13           C  
ATOM    716  N   ASP A 151      51.860  98.977  41.628  1.00 37.16           N  
ATOM    717  CA  ASP A 151      52.240  99.820  40.494  1.00 36.59           C  
ATOM    718  C   ASP A 151      51.670  99.385  39.136  1.00 36.19           C  
ATOM    719  O   ASP A 151      51.846 100.079  38.131  1.00 36.39           O  
ATOM    720  CB  ASP A 151      53.766  99.967  40.432  1.00 36.61           C  
ATOM    721  CG  ASP A 151      54.456  98.740  39.865  1.00 36.65           C  
ATOM    722  OD1 ASP A 151      55.397  98.920  39.062  1.00 36.87           O  
ATOM    723  OD2 ASP A 151      54.135  97.567  40.161  1.00 36.25           O  
ATOM    724  N   GLY A 152      50.994  98.243  39.109  1.00 35.55           N  
ATOM    725  CA  GLY A 152      50.343  97.778  37.899  1.00 34.92           C  
ATOM    726  C   GLY A 152      48.893  98.207  37.855  1.00 34.50           C  
ATOM    727  O   GLY A 152      48.231  98.083  36.828  1.00 34.46           O  
ATOM    728  N   GLY A 153      48.400  98.710  38.981  1.00 34.12           N  
ATOM    729  CA  GLY A 153      47.025  99.157  39.083  1.00 33.77           C  
ATOM    730  C   GLY A 153      46.055  98.005  39.209  1.00 33.48           C  
ATOM    731  O   GLY A 153      46.462  96.861  39.374  1.00 33.57           O  
ATOM    732  N   SER A 154      44.766  98.314  39.138  1.00 33.34           N  
ATOM    733  CA  SER A 154      43.722  97.300  39.209  1.00 33.34           C  
ATOM    734  C   SER A 154      43.615  96.564  37.887  1.00 33.39           C  
ATOM    735  O   SER A 154      44.093  97.039  36.862  1.00 33.46           O  
ATOM    736  CB  SER A 154      42.382  97.944  39.547  1.00 33.36           C  
ATOM    737  OG  SER A 154      42.306  99.261  39.024  1.00 33.54           O  
ATOM    738  N   LEU A 155      42.983  95.400  37.909  1.00 33.55           N  
ATOM    739  CA  LEU A 155      42.788  94.628  36.694  1.00 33.76           C  
ATOM    740  C   LEU A 155      41.867  95.362  35.729  1.00 34.10           C  
ATOM    741  O   LEU A 155      41.947  95.178  34.513  1.00 34.18           O  
ATOM    742  CB  LEU A 155      42.225  93.254  37.033  1.00 33.65           C  
ATOM    743  CG  LEU A 155      43.261  92.165  37.272  1.00 33.33           C  
ATOM    744  CD1 LEU A 155      42.573  90.832  37.184  1.00 33.50           C  
ATOM    745  CD2 LEU A 155      44.387  92.250  36.256  1.00 33.20           C  
ATOM    746  N   ASP A 156      40.995  96.192  36.294  1.00 34.53           N  
ATOM    747  CA  ASP A 156      40.123  97.080  35.538  1.00 34.96           C  
ATOM    748  C   ASP A 156      40.938  98.070  34.704  1.00 35.03           C  
ATOM    749  O   ASP A 156      40.553  98.415  33.579  1.00 35.07           O  
ATOM    750  CB  ASP A 156      39.221  97.843  36.503  1.00 35.09           C  
ATOM    751  CG  ASP A 156      37.844  98.078  35.942  1.00 36.28           C  
ATOM    752  OD1 ASP A 156      37.422  99.256  35.907  1.00 37.79           O  
ATOM    753  OD2 ASP A 156      37.112  97.152  35.515  1.00 37.25           O  
ATOM    754  N   GLN A 157      42.063  98.511  35.270  1.00 34.96           N  
ATOM    755  CA  GLN A 157      42.984  99.423  34.607  1.00 34.89           C  
ATOM    756  C   GLN A 157      43.695  98.742  33.454  1.00 34.71           C  
ATOM    757  O   GLN A 157      43.917  99.360  32.417  1.00 34.76           O  
ATOM    758  CB  GLN A 157      44.023  99.945  35.593  1.00 34.94           C  
ATOM    759  CG  GLN A 157      43.931 101.424  35.885  1.00 35.73           C  
ATOM    760  CD  GLN A 157      43.806 101.714  37.375  1.00 37.04           C  
ATOM    761  OE1 GLN A 157      44.615 101.244  38.182  1.00 36.75           O  
ATOM    762  NE2 GLN A 157      42.790 102.495  37.741  1.00 38.02           N  
ATOM    763  N   VAL A 158      44.058  97.474  33.640  1.00 34.62           N  
ATOM    764  CA  VAL A 158      44.754  96.727  32.592  1.00 34.61           C  
ATOM    765  C   VAL A 158      43.805  96.380  31.450  1.00 34.64           C  
ATOM    766  O   VAL A 158      44.225  96.256  30.306  1.00 34.69           O  
ATOM    767  CB  VAL A 158      45.515  95.466  33.115  1.00 34.52           C  
ATOM    768  CG1 VAL A 158      46.044  95.685  34.527  1.00 34.61           C  
ATOM    769  CG2 VAL A 158      44.658  94.217  33.045  1.00 34.67           C  
ATOM    770  N   LEU A 159      42.522  96.243  31.761  1.00 34.77           N  
ATOM    771  CA  LEU A 159      41.524  95.979  30.737  1.00 34.93           C  
ATOM    772  C   LEU A 159      41.391  97.167  29.784  1.00 35.27           C  
ATOM    773  O   LEU A 159      41.062  96.996  28.613  1.00 35.37           O  
ATOM    774  CB  LEU A 159      40.177  95.644  31.380  1.00 34.73           C  
ATOM    775  CG  LEU A 159      39.053  95.128  30.480  1.00 34.36           C  
ATOM    776  CD1 LEU A 159      39.546  94.067  29.499  1.00 34.53           C  
ATOM    777  CD2 LEU A 159      37.912  94.593  31.325  1.00 34.18           C  
ATOM    778  N   LYS A 160      41.651  98.368  30.293  1.00 35.58           N  
ATOM    779  CA  LYS A 160      41.538  99.578  29.488  1.00 35.91           C  
ATOM    780  C   LYS A 160      42.692  99.680  28.501  1.00 36.03           C  
ATOM    781  O   LYS A 160      42.492 100.076  27.355  1.00 36.31           O  
ATOM    782  CB  LYS A 160      41.471 100.827  30.376  1.00 35.98           C  
ATOM    783  CG  LYS A 160      40.309 100.823  31.371  1.00 36.60           C  
ATOM    784  CD  LYS A 160      39.868 102.237  31.747  1.00 37.40           C  
ATOM    785  CE  LYS A 160      39.126 102.251  33.083  1.00 37.68           C  
ATOM    786  NZ  LYS A 160      37.684 101.873  32.951  1.00 37.76           N  
ATOM    787  N   GLU A 161      43.893  99.315  28.946  1.00 36.19           N  
ATOM    788  CA  GLU A 161      45.094  99.410  28.115  1.00 36.37           C  
ATOM    789  C   GLU A 161      45.250  98.193  27.210  1.00 36.27           C  
ATOM    790  O   GLU A 161      45.681  98.313  26.056  1.00 36.42           O  
ATOM    791  CB  GLU A 161      46.342  99.593  28.979  1.00 36.42           C  
ATOM    792  CG  GLU A 161      46.786 101.037  29.122  1.00 37.65           C  
ATOM    793  CD  GLU A 161      47.435 101.575  27.860  1.00 39.59           C  
ATOM    794  OE1 GLU A 161      46.693 102.067  26.973  1.00 40.13           O  
ATOM    795  OE2 GLU A 161      48.686 101.505  27.760  1.00 40.22           O  
ATOM    796  N   ALA A 162      44.904  97.025  27.745  1.00 36.03           N  
ATOM    797  CA  ALA A 162      44.872  95.797  26.964  1.00 35.84           C  
ATOM    798  C   ALA A 162      43.514  95.681  26.297  1.00 35.65           C  
ATOM    799  O   ALA A 162      42.570  96.373  26.676  1.00 35.77           O  
ATOM    800  CB  ALA A 162      45.134  94.591  27.853  1.00 35.95           C  
ATOM    801  N   LYS A 163      43.422  94.816  25.296  1.00 35.27           N  
ATOM    802  CA  LYS A 163      42.170  94.603  24.575  1.00 34.96           C  
ATOM    803  C   LYS A 163      41.149  93.925  25.509  1.00 34.12           C  
ATOM    804  O   LYS A 163      40.515  94.578  26.347  1.00 33.78           O  
ATOM    805  CB  LYS A 163      42.438  93.768  23.304  1.00 35.44           C  
ATOM    806  CG  LYS A 163      43.649  92.802  23.403  1.00 36.38           C  
ATOM    807  CD  LYS A 163      44.631  92.988  22.248  1.00 38.20           C  
ATOM    808  CE  LYS A 163      46.070  93.067  22.748  1.00 39.04           C  
ATOM    809  NZ  LYS A 163      46.983  93.656  21.719  1.00 39.86           N  
ATOM    810  N   ARG A 164      40.978  92.620  25.327  1.00 33.12           N  
ATOM    811  CA  ARG A 164      40.498  91.749  26.378  1.00 32.09           C  
ATOM    812  C   ARG A 164      41.719  90.951  26.805  1.00 31.08           C  
ATOM    813  O   ARG A 164      42.702  90.867  26.066  1.00 30.81           O  
ATOM    814  CB  ARG A 164      39.386  90.821  25.890  1.00 32.29           C  
ATOM    815  CG  ARG A 164      39.174  90.798  24.398  1.00 33.13           C  
ATOM    816  CD  ARG A 164      39.765  89.585  23.717  1.00 35.18           C  
ATOM    817  NE  ARG A 164      39.713  89.713  22.264  1.00 36.57           N  
ATOM    818  CZ  ARG A 164      40.397  88.956  21.419  1.00 37.61           C  
ATOM    819  NH1 ARG A 164      41.202  87.998  21.872  1.00 38.24           N  
ATOM    820  NH2 ARG A 164      40.275  89.156  20.113  1.00 38.10           N  
ATOM    821  N   ILE A 165      41.667  90.384  28.002  1.00 29.90           N  
ATOM    822  CA  ILE A 165      42.795  89.636  28.524  1.00 28.87           C  
ATOM    823  C   ILE A 165      42.773  88.199  27.982  1.00 28.31           C  
ATOM    824  O   ILE A 165      41.710  87.571  27.950  1.00 28.39           O  
ATOM    825  CB  ILE A 165      42.794  89.702  30.065  1.00 28.79           C  
ATOM    826  CG1 ILE A 165      43.019  91.149  30.510  1.00 28.38           C  
ATOM    827  CG2 ILE A 165      43.876  88.814  30.653  1.00 28.71           C  
ATOM    828  CD1 ILE A 165      42.548  91.452  31.896  1.00 28.36           C  
ATOM    829  N   PRO A 166      43.929  87.704  27.521  1.00 27.61           N  
ATOM    830  CA  PRO A 166      44.058  86.325  27.022  1.00 27.06           C  
ATOM    831  C   PRO A 166      43.768  85.283  28.098  1.00 26.62           C  
ATOM    832  O   PRO A 166      44.200  85.435  29.243  1.00 26.82           O  
ATOM    833  CB  PRO A 166      45.523  86.244  26.590  1.00 27.01           C  
ATOM    834  CG  PRO A 166      46.201  87.339  27.322  1.00 27.23           C  
ATOM    835  CD  PRO A 166      45.204  88.439  27.423  1.00 27.56           C  
ATOM    836  N   GLU A 167      43.060  84.224  27.721  1.00 25.97           N  
ATOM    837  CA  GLU A 167      42.498  83.285  28.692  1.00 25.36           C  
ATOM    838  C   GLU A 167      43.533  82.550  29.539  1.00 24.79           C  
ATOM    839  O   GLU A 167      43.198  81.986  30.572  1.00 24.80           O  
ATOM    840  CB  GLU A 167      41.533  82.307  28.008  1.00 25.41           C  
ATOM    841  CG  GLU A 167      42.154  81.017  27.510  1.00 25.75           C  
ATOM    842  CD  GLU A 167      41.351  79.805  27.922  1.00 26.42           C  
ATOM    843  OE1 GLU A 167      40.479  79.377  27.141  1.00 27.45           O  
ATOM    844  OE2 GLU A 167      41.584  79.278  29.027  1.00 26.70           O  
ATOM    845  N   GLU A 168      44.784  82.562  29.101  1.00 24.23           N  
ATOM    846  CA  GLU A 168      45.857  81.940  29.866  1.00 23.81           C  
ATOM    847  C   GLU A 168      46.286  82.846  31.023  1.00 23.12           C  
ATOM    848  O   GLU A 168      46.635  82.360  32.101  1.00 23.09           O  
ATOM    849  CB  GLU A 168      47.045  81.537  28.971  1.00 23.95           C  
ATOM    850  CG  GLU A 168      47.233  82.356  27.692  1.00 25.46           C  
ATOM    851  CD  GLU A 168      46.351  81.916  26.516  1.00 27.45           C  
ATOM    852  OE1 GLU A 168      46.040  82.777  25.660  1.00 27.39           O  
ATOM    853  OE2 GLU A 168      45.970  80.719  26.425  1.00 28.61           O  
ATOM    854  N   ILE A 169      46.230  84.159  30.802  1.00 22.31           N  
ATOM    855  CA  ILE A 169      46.557  85.137  31.841  1.00 21.61           C  
ATOM    856  C   ILE A 169      45.460  85.192  32.902  1.00 21.35           C  
ATOM    857  O   ILE A 169      45.728  85.454  34.079  1.00 21.25           O  
ATOM    858  CB  ILE A 169      46.817  86.542  31.230  1.00 21.45           C  
ATOM    859  CG1 ILE A 169      48.055  86.519  30.321  1.00 21.16           C  
ATOM    860  CG2 ILE A 169      46.941  87.614  32.321  1.00 20.96           C  
ATOM    861  CD1 ILE A 169      49.405  86.479  31.037  1.00 20.71           C  
ATOM    862  N   LEU A 170      44.227  84.929  32.484  1.00 20.92           N  
ATOM    863  CA  LEU A 170      43.115  84.892  33.421  1.00 20.68           C  
ATOM    864  C   LEU A 170      43.221  83.670  34.310  1.00 20.36           C  
ATOM    865  O   LEU A 170      42.782  83.696  35.452  1.00 20.49           O  
ATOM    866  CB  LEU A 170      41.778  84.903  32.688  1.00 20.81           C  
ATOM    867  CG  LEU A 170      41.415  86.211  31.986  1.00 21.08           C  
ATOM    868  CD1 LEU A 170      40.097  86.046  31.242  1.00 21.29           C  
ATOM    869  CD2 LEU A 170      41.365  87.388  32.967  1.00 20.75           C  
ATOM    870  N   GLY A 171      43.813  82.608  33.777  1.00 19.91           N  
ATOM    871  CA  GLY A 171      44.103  81.420  34.552  1.00 19.60           C  
ATOM    872  C   GLY A 171      44.977  81.746  35.745  1.00 19.45           C  
ATOM    873  O   GLY A 171      44.714  81.292  36.863  1.00 19.63           O  
ATOM    874  N   LYS A 172      46.012  82.549  35.508  1.00 19.06           N  
ATOM    875  CA  LYS A 172      46.910  82.976  36.572  1.00 18.61           C  
ATOM    876  C   LYS A 172      46.179  83.901  37.533  1.00 18.34           C  
ATOM    877  O   LYS A 172      46.372  83.821  38.749  1.00 18.49           O  
ATOM    878  CB  LYS A 172      48.153  83.657  36.001  1.00 18.57           C  
ATOM    879  CG  LYS A 172      49.439  82.895  36.258  1.00 18.70           C  
ATOM    880  CD  LYS A 172      50.194  83.458  37.458  1.00 19.44           C  
ATOM    881  CE  LYS A 172      50.928  82.361  38.231  1.00 19.94           C  
ATOM    882  NZ  LYS A 172      52.415  82.437  38.056  1.00 20.18           N  
ATOM    883  N   VAL A 173      45.330  84.767  36.985  1.00 17.84           N  
ATOM    884  CA  VAL A 173      44.489  85.624  37.808  1.00 17.52           C  
ATOM    885  C   VAL A 173      43.569  84.757  38.662  1.00 17.30           C  
ATOM    886  O   VAL A 173      43.465  84.968  39.875  1.00 17.33           O  
ATOM    887  CB  VAL A 173      43.672  86.619  36.957  1.00 17.63           C  
ATOM    888  CG1 VAL A 173      42.468  87.135  37.729  1.00 17.45           C  
ATOM    889  CG2 VAL A 173      44.552  87.784  36.513  1.00 17.61           C  
ATOM    890  N   SER A 174      42.943  83.766  38.022  1.00 16.88           N  
ATOM    891  CA  SER A 174      42.005  82.844  38.667  1.00 16.34           C  
ATOM    892  C   SER A 174      42.616  82.055  39.821  1.00 16.13           C  
ATOM    893  O   SER A 174      41.918  81.712  40.783  1.00 15.95           O  
ATOM    894  CB  SER A 174      41.424  81.880  37.640  1.00 16.30           C  
ATOM    895  OG  SER A 174      40.648  82.579  36.689  1.00 15.92           O  
ATOM    896  N   ILE A 175      43.913  81.768  39.720  1.00 15.86           N  
ATOM    897  CA  ILE A 175      44.628  81.098  40.803  1.00 15.57           C  
ATOM    898  C   ILE A 175      44.677  81.999  42.028  1.00 15.25           C  
ATOM    899  O   ILE A 175      44.307  81.570  43.116  1.00 15.45           O  
ATOM    900  CB  ILE A 175      46.045  80.654  40.366  1.00 15.64           C  
ATOM    901  CG1 ILE A 175      45.981  79.298  39.653  1.00 16.04           C  
ATOM    902  CG2 ILE A 175      46.974  80.543  41.558  1.00 15.37           C  
ATOM    903  CD1 ILE A 175      46.771  79.239  38.350  1.00 16.17           C  
ATOM    904  N   ALA A 176      45.098  83.248  41.840  1.00 14.72           N  
ATOM    905  CA  ALA A 176      45.269  84.176  42.952  1.00 14.25           C  
ATOM    906  C   ALA A 176      43.960  84.589  43.627  1.00 14.11           C  
ATOM    907  O   ALA A 176      43.928  84.788  44.840  1.00 14.14           O  
ATOM    908  CB  ALA A 176      46.028  85.384  42.505  1.00 14.26           C  
ATOM    909  N   VAL A 177      42.882  84.725  42.858  1.00 13.85           N  
ATOM    910  CA  VAL A 177      41.596  85.077  43.455  1.00 13.59           C  
ATOM    911  C   VAL A 177      41.137  83.938  44.346  1.00 13.51           C  
ATOM    912  O   VAL A 177      40.776  84.149  45.494  1.00 13.45           O  
ATOM    913  CB  VAL A 177      40.506  85.380  42.416  1.00 13.58           C  
ATOM    914  CG1 VAL A 177      39.274  85.950  43.107  1.00 13.42           C  
ATOM    915  CG2 VAL A 177      41.015  86.350  41.371  1.00 13.79           C  
ATOM    916  N   LEU A 178      41.167  82.726  43.809  1.00 13.51           N  
ATOM    917  CA  LEU A 178      40.824  81.549  44.585  1.00 13.53           C  
ATOM    918  C   LEU A 178      41.739  81.384  45.800  1.00 13.74           C  
ATOM    919  O   LEU A 178      41.265  81.105  46.897  1.00 14.05           O  
ATOM    920  CB  LEU A 178      40.880  80.300  43.712  1.00 13.47           C  
ATOM    921  CG  LEU A 178      39.744  80.120  42.716  1.00 13.06           C  
ATOM    922  CD1 LEU A 178      40.078  79.002  41.747  1.00 13.07           C  
ATOM    923  CD2 LEU A 178      38.460  79.829  43.450  1.00 13.04           C  
ATOM    924  N   ARG A 179      43.040  81.575  45.618  1.00 13.70           N  
ATOM    925  CA  ARG A 179      43.972  81.360  46.716  1.00 13.91           C  
ATOM    926  C   ARG A 179      43.892  82.451  47.774  1.00 13.94           C  
ATOM    927  O   ARG A 179      43.859  82.163  48.971  1.00 14.17           O  
ATOM    928  CB  ARG A 179      45.393  81.183  46.207  1.00 13.79           C  
ATOM    929  CG  ARG A 179      45.712  79.754  45.865  1.00 14.28           C  
ATOM    930  CD  ARG A 179      47.113  79.569  45.365  1.00 15.93           C  
ATOM    931  NE  ARG A 179      47.261  78.389  44.522  1.00 17.10           N  
ATOM    932  CZ  ARG A 179      48.343  78.128  43.802  1.00 17.76           C  
ATOM    933  NH1 ARG A 179      49.374  78.968  43.815  1.00 17.68           N  
ATOM    934  NH2 ARG A 179      48.394  77.030  43.060  1.00 18.52           N  
ATOM    935  N   GLY A 180      43.849  83.699  47.327  1.00 13.84           N  
ATOM    936  CA  GLY A 180      43.594  84.812  48.219  1.00 13.77           C  
ATOM    937  C   GLY A 180      42.247  84.678  48.907  1.00 13.61           C  
ATOM    938  O   GLY A 180      42.152  84.887  50.110  1.00 13.71           O  
ATOM    939  N   LEU A 181      41.214  84.322  48.146  1.00 13.49           N  
ATOM    940  CA  LEU A 181      39.889  84.103  48.705  1.00 13.63           C  
ATOM    941  C   LEU A 181      39.942  83.048  49.802  1.00 14.15           C  
ATOM    942  O   LEU A 181      39.448  83.266  50.916  1.00 14.14           O  
ATOM    943  CB  LEU A 181      38.891  83.694  47.612  1.00 13.41           C  
ATOM    944  CG  LEU A 181      37.672  84.594  47.341  1.00 12.79           C  
ATOM    945  CD1 LEU A 181      37.949  86.079  47.609  1.00 12.08           C  
ATOM    946  CD2 LEU A 181      37.165  84.402  45.931  1.00 10.77           C  
ATOM    947  N   ALA A 182      40.575  81.919  49.487  1.00 14.76           N  
ATOM    948  CA  ALA A 182      40.671  80.790  50.409  1.00 15.18           C  
ATOM    949  C   ALA A 182      41.557  81.077  51.613  1.00 15.53           C  
ATOM    950  O   ALA A 182      41.352  80.496  52.678  1.00 15.65           O  
ATOM    951  CB  ALA A 182      41.162  79.560  49.688  1.00 15.16           C  
ATOM    952  N   TYR A 183      42.541  81.961  51.438  1.00 15.86           N  
ATOM    953  CA  TYR A 183      43.441  82.328  52.523  1.00 16.06           C  
ATOM    954  C   TYR A 183      42.654  83.056  53.597  1.00 16.39           C  
ATOM    955  O   TYR A 183      42.650  82.634  54.754  1.00 16.47           O  
ATOM    956  CB  TYR A 183      44.616  83.178  52.022  1.00 16.04           C  
ATOM    957  CG  TYR A 183      45.411  83.847  53.129  1.00 16.03           C  
ATOM    958  CD1 TYR A 183      46.329  83.127  53.891  1.00 15.47           C  
ATOM    959  CD2 TYR A 183      45.233  85.202  53.417  1.00 16.16           C  
ATOM    960  CE1 TYR A 183      47.046  83.737  54.908  1.00 16.19           C  
ATOM    961  CE2 TYR A 183      45.944  85.822  54.428  1.00 16.38           C  
ATOM    962  CZ  TYR A 183      46.850  85.088  55.174  1.00 16.61           C  
ATOM    963  OH  TYR A 183      47.554  85.709  56.188  1.00 16.51           O  
ATOM    964  N   LEU A 184      41.975  84.133  53.205  1.00 16.80           N  
ATOM    965  CA  LEU A 184      41.137  84.899  54.123  1.00 17.29           C  
ATOM    966  C   LEU A 184      40.057  84.008  54.729  1.00 17.93           C  
ATOM    967  O   LEU A 184      39.713  84.149  55.903  1.00 17.91           O  
ATOM    968  CB  LEU A 184      40.486  86.089  53.416  1.00 17.06           C  
ATOM    969  CG  LEU A 184      41.355  87.014  52.565  1.00 16.92           C  
ATOM    970  CD1 LEU A 184      40.530  87.579  51.435  1.00 16.91           C  
ATOM    971  CD2 LEU A 184      41.954  88.135  53.393  1.00 16.99           C  
ATOM    972  N   ARG A 185      39.532  83.088  53.922  1.00 18.61           N  
ATOM    973  CA  ARG A 185      38.486  82.179  54.372  1.00 19.22           C  
ATOM    974  C   ARG A 185      38.971  81.234  55.461  1.00 19.64           C  
ATOM    975  O   ARG A 185      38.269  81.036  56.451  1.00 19.99           O  
ATOM    976  CB  ARG A 185      37.929  81.360  53.203  1.00 19.28           C  
ATOM    977  CG  ARG A 185      36.402  81.191  53.198  1.00 19.51           C  
ATOM    978  CD  ARG A 185      35.846  80.312  54.308  1.00 19.21           C  
ATOM    979  NE  ARG A 185      35.257  79.065  53.826  1.00 19.06           N  
ATOM    980  CZ  ARG A 185      33.970  78.746  53.947  1.00 19.07           C  
ATOM    981  NH1 ARG A 185      33.113  79.587  54.518  1.00 18.27           N  
ATOM    982  NH2 ARG A 185      33.533  77.577  53.492  1.00 19.45           N  
ATOM    983  N   GLU A 186      40.159  80.656  55.275  1.00 20.02           N  
ATOM    984  CA  GLU A 186      40.625  79.560  56.124  1.00 20.28           C  
ATOM    985  C   GLU A 186      41.484  80.024  57.291  1.00 20.80           C  
ATOM    986  O   GLU A 186      41.202  79.674  58.436  1.00 20.72           O  
ATOM    987  CB  GLU A 186      41.361  78.500  55.301  1.00 20.13           C  
ATOM    988  CG  GLU A 186      40.454  77.562  54.520  0.50 19.94           C  
ATOM    989  CD  GLU A 186      41.025  77.176  53.165  0.50 19.87           C  
ATOM    990  OE1 GLU A 186      42.220  76.818  53.089  0.50 19.91           O  
ATOM    991  OE2 GLU A 186      40.273  77.221  52.171  0.50 19.91           O  
ATOM    992  N   LYS A 187      42.514  80.819  57.004  1.00 21.64           N  
ATOM    993  CA  LYS A 187      43.449  81.291  58.036  1.00 22.54           C  
ATOM    994  C   LYS A 187      42.798  82.294  59.007  1.00 22.93           C  
ATOM    995  O   LYS A 187      42.813  82.096  60.221  1.00 23.05           O  
ATOM    996  CB  LYS A 187      44.737  81.841  57.407  1.00 22.62           C  
ATOM    997  CG  LYS A 187      45.595  80.779  56.684  1.00 23.30           C  
ATOM    998  CD  LYS A 187      46.576  80.053  57.626  1.00 24.73           C  
ATOM    999  CE  LYS A 187      47.936  80.773  57.723  1.00 25.11           C  
ATOM   1000  NZ  LYS A 187      49.114  79.881  57.451  1.00 24.91           N  
ATOM   1001  N   HIS A 188      42.222  83.360  58.470  1.00 23.53           N  
ATOM   1002  CA  HIS A 188      41.270  84.171  59.223  1.00 24.21           C  
ATOM   1003  C   HIS A 188      39.885  83.627  58.906  1.00 24.83           C  
ATOM   1004  O   HIS A 188      39.780  82.600  58.233  1.00 25.15           O  
ATOM   1005  CB  HIS A 188      41.407  85.630  58.829  1.00 24.13           C  
ATOM   1006  CG  HIS A 188      42.827  86.085  58.772  1.00 23.74           C  
ATOM   1007  ND1 HIS A 188      43.534  86.447  59.896  1.00 23.48           N  
ATOM   1008  CD2 HIS A 188      43.688  86.185  57.734  1.00 23.79           C  
ATOM   1009  CE1 HIS A 188      44.763  86.781  59.549  1.00 24.02           C  
ATOM   1010  NE2 HIS A 188      44.883  86.630  58.243  1.00 24.12           N  
ATOM   1011  N   GLN A 189      38.823  84.276  59.376  1.00 25.31           N  
ATOM   1012  CA  GLN A 189      37.485  83.744  59.102  1.00 25.80           C  
ATOM   1013  C   GLN A 189      36.589  84.684  58.306  1.00 26.04           C  
ATOM   1014  O   GLN A 189      35.386  84.433  58.169  1.00 26.13           O  
ATOM   1015  CB  GLN A 189      36.798  83.278  60.387  1.00 25.87           C  
ATOM   1016  CG  GLN A 189      37.254  81.903  60.860  1.00 26.51           C  
ATOM   1017  CD  GLN A 189      38.529  81.965  61.695  1.00 27.76           C  
ATOM   1018  OE1 GLN A 189      39.616  81.624  61.213  1.00 28.18           O  
ATOM   1019  NE2 GLN A 189      38.400  82.405  62.946  1.00 28.10           N  
ATOM   1020  N   ILE A 190      37.185  85.745  57.761  1.00 26.32           N  
ATOM   1021  CA  ILE A 190      36.439  86.715  56.958  1.00 26.57           C  
ATOM   1022  C   ILE A 190      36.356  86.319  55.490  1.00 26.61           C  
ATOM   1023  O   ILE A 190      37.214  85.601  54.976  1.00 26.52           O  
ATOM   1024  CB  ILE A 190      37.032  88.149  57.076  1.00 26.57           C  
ATOM   1025  CG1 ILE A 190      38.490  88.187  56.608  1.00 26.32           C  
ATOM   1026  CG2 ILE A 190      36.836  88.726  58.490  1.00 27.10           C  
ATOM   1027  CD1 ILE A 190      38.648  88.827  55.252  1.00 26.27           C  
ATOM   1028  N   MET A 191      35.309  86.803  54.829  1.00 26.82           N  
ATOM   1029  CA  MET A 191      35.201  86.731  53.378  1.00 26.92           C  
ATOM   1030  C   MET A 191      35.344  88.118  52.769  1.00 26.77           C  
ATOM   1031  O   MET A 191      35.082  89.129  53.423  1.00 26.87           O  
ATOM   1032  CB  MET A 191      33.873  86.102  52.949  1.00 26.98           C  
ATOM   1033  CG  MET A 191      32.638  86.704  53.590  1.00 27.65           C  
ATOM   1034  SD  MET A 191      31.348  85.472  53.900  1.00 29.88           S  
ATOM   1035  CE  MET A 191      30.347  86.358  55.096  1.00 30.39           C  
ATOM   1036  N   HIS A 192      35.790  88.153  51.519  1.00 26.75           N  
ATOM   1037  CA  HIS A 192      35.705  89.352  50.701  1.00 26.60           C  
ATOM   1038  C   HIS A 192      34.232  89.605  50.594  1.00 26.80           C  
ATOM   1039  O   HIS A 192      33.452  88.669  50.714  1.00 27.35           O  
ATOM   1040  CB  HIS A 192      36.250  89.068  49.307  1.00 26.36           C  
ATOM   1041  CG  HIS A 192      36.990  90.214  48.706  1.00 25.46           C  
ATOM   1042  ND1 HIS A 192      36.401  91.437  48.477  1.00 24.94           N  
ATOM   1043  CD2 HIS A 192      38.273  90.329  48.296  1.00 24.75           C  
ATOM   1044  CE1 HIS A 192      37.291  92.257  47.950  1.00 24.89           C  
ATOM   1045  NE2 HIS A 192      38.435  91.609  47.827  1.00 24.63           N  
ATOM   1046  N   ARG A 193      33.821  90.847  50.398  1.00 26.67           N  
ATOM   1047  CA  ARG A 193      32.404  91.098  50.155  1.00 26.57           C  
ATOM   1048  C   ARG A 193      32.274  91.950  48.911  1.00 26.40           C  
ATOM   1049  O   ARG A 193      31.240  92.582  48.666  1.00 26.28           O  
ATOM   1050  CB  ARG A 193      31.756  91.773  51.362  1.00 26.92           C  
ATOM   1051  CG  ARG A 193      32.001  91.071  52.684  1.00 27.34           C  
ATOM   1052  CD  ARG A 193      31.296  91.703  53.855  1.00 29.01           C  
ATOM   1053  NE  ARG A 193      31.036  90.718  54.902  1.00 31.38           N  
ATOM   1054  CZ  ARG A 193      29.824  90.360  55.321  1.00 32.42           C  
ATOM   1055  NH1 ARG A 193      28.733  90.909  54.788  1.00 32.42           N  
ATOM   1056  NH2 ARG A 193      29.705  89.449  56.282  1.00 32.63           N  
ATOM   1057  N   ASP A 194      33.344  91.942  48.120  1.00 26.25           N  
ATOM   1058  CA  ASP A 194      33.512  92.888  47.028  1.00 25.97           C  
ATOM   1059  C   ASP A 194      34.565  92.464  45.997  1.00 25.54           C  
ATOM   1060  O   ASP A 194      35.480  93.227  45.679  1.00 25.44           O  
ATOM   1061  CB  ASP A 194      33.854  94.264  47.596  1.00 25.94           C  
ATOM   1062  CG  ASP A 194      33.400  95.377  46.706  1.00 26.56           C  
ATOM   1063  OD1 ASP A 194      32.334  95.235  46.066  1.00 27.69           O  
ATOM   1064  OD2 ASP A 194      34.050  96.433  46.580  1.00 27.38           O  
ATOM   1065  N   VAL A 195      34.422  91.250  45.473  1.00 25.02           N  
ATOM   1066  CA  VAL A 195      35.271  90.785  44.379  1.00 24.44           C  
ATOM   1067  C   VAL A 195      34.803  91.446  43.077  1.00 24.17           C  
ATOM   1068  O   VAL A 195      33.635  91.340  42.695  1.00 24.12           O  
ATOM   1069  CB  VAL A 195      35.261  89.231  44.259  1.00 24.36           C  
ATOM   1070  CG1 VAL A 195      36.010  88.768  43.027  1.00 24.08           C  
ATOM   1071  CG2 VAL A 195      35.855  88.593  45.496  1.00 24.18           C  
ATOM   1072  N   LYS A 196      35.719  92.151  42.422  1.00 23.72           N  
ATOM   1073  CA  LYS A 196      35.457  92.790  41.137  1.00 23.52           C  
ATOM   1074  C   LYS A 196      36.778  93.294  40.565  1.00 23.22           C  
ATOM   1075  O   LYS A 196      37.689  93.591  41.326  1.00 23.25           O  
ATOM   1076  CB  LYS A 196      34.446  93.934  41.287  1.00 23.63           C  
ATOM   1077  CG  LYS A 196      34.797  94.967  42.344  1.00 24.49           C  
ATOM   1078  CD  LYS A 196      33.561  95.632  42.907  1.00 25.36           C  
ATOM   1079  CE  LYS A 196      33.755  97.135  42.979  1.00 26.12           C  
ATOM   1080  NZ  LYS A 196      32.654  97.780  43.742  1.00 27.00           N  
ATOM   1081  N   PRO A 197      36.893  93.378  39.240  1.00 23.10           N  
ATOM   1082  CA  PRO A 197      38.147  93.762  38.575  1.00 23.25           C  
ATOM   1083  C   PRO A 197      38.954  94.861  39.263  1.00 23.51           C  
ATOM   1084  O   PRO A 197      40.177  94.739  39.363  1.00 23.59           O  
ATOM   1085  CB  PRO A 197      37.672  94.246  37.210  1.00 23.28           C  
ATOM   1086  CG  PRO A 197      36.457  93.424  36.937  1.00 23.30           C  
ATOM   1087  CD  PRO A 197      35.833  93.086  38.261  1.00 23.07           C  
ATOM   1088  N   SER A 198      38.280  95.910  39.733  1.00 23.77           N  
ATOM   1089  CA  SER A 198      38.944  97.045  40.384  1.00 23.73           C  
ATOM   1090  C   SER A 198      39.546  96.709  41.754  1.00 23.64           C  
ATOM   1091  O   SER A 198      40.218  97.547  42.362  1.00 23.88           O  
ATOM   1092  CB  SER A 198      37.969  98.219  40.519  1.00 23.78           C  
ATOM   1093  OG  SER A 198      36.922  97.922  41.435  1.00 23.77           O  
ATOM   1094  N   ASN A 199      39.288  95.495  42.240  1.00 23.36           N  
ATOM   1095  CA  ASN A 199      39.762  95.058  43.551  1.00 23.21           C  
ATOM   1096  C   ASN A 199      40.774  93.930  43.446  1.00 23.16           C  
ATOM   1097  O   ASN A 199      41.226  93.392  44.460  1.00 23.12           O  
ATOM   1098  CB  ASN A 199      38.591  94.643  44.449  1.00 23.13           C  
ATOM   1099  CG  ASN A 199      37.872  95.834  45.070  1.00 22.97           C  
ATOM   1100  OD1 ASN A 199      36.667  95.778  45.314  1.00 22.63           O  
ATOM   1101  ND2 ASN A 199      38.606  96.916  45.329  1.00 22.89           N  
ATOM   1102  N   ILE A 200      41.110  93.576  42.206  1.00 23.11           N  
ATOM   1103  CA  ILE A 200      42.172  92.621  41.918  1.00 22.94           C  
ATOM   1104  C   ILE A 200      43.370  93.402  41.389  1.00 23.36           C  
ATOM   1105  O   ILE A 200      43.400  93.802  40.230  1.00 23.41           O  
ATOM   1106  CB  ILE A 200      41.696  91.538  40.919  1.00 22.55           C  
ATOM   1107  CG1 ILE A 200      40.354  90.946  41.369  1.00 21.67           C  
ATOM   1108  CG2 ILE A 200      42.737  90.438  40.810  1.00 22.54           C  
ATOM   1109  CD1 ILE A 200      39.650  90.083  40.343  1.00 19.87           C  
ATOM   1110  N   LEU A 201      44.348  93.620  42.261  1.00 24.03           N  
ATOM   1111  CA  LEU A 201      45.493  94.482  41.973  1.00 24.93           C  
ATOM   1112  C   LEU A 201      46.721  93.718  41.475  1.00 25.71           C  
ATOM   1113  O   LEU A 201      47.068  92.663  42.015  1.00 25.93           O  
ATOM   1114  CB  LEU A 201      45.863  95.272  43.227  1.00 24.87           C  
ATOM   1115  CG  LEU A 201      45.241  96.647  43.490  1.00 24.74           C  
ATOM   1116  CD1 LEU A 201      43.807  96.750  42.992  1.00 25.09           C  
ATOM   1117  CD2 LEU A 201      45.301  96.955  44.971  1.00 24.31           C  
ATOM   1118  N   VAL A 202      47.381  94.264  40.456  1.00 26.51           N  
ATOM   1119  CA  VAL A 202      48.568  93.638  39.867  1.00 27.41           C  
ATOM   1120  C   VAL A 202      49.803  94.535  39.956  1.00 28.11           C  
ATOM   1121  O   VAL A 202      49.685  95.729  40.224  1.00 28.29           O  
ATOM   1122  CB  VAL A 202      48.332  93.233  38.401  1.00 27.35           C  
ATOM   1123  CG1 VAL A 202      47.174  92.253  38.304  1.00 27.38           C  
ATOM   1124  CG2 VAL A 202      48.094  94.462  37.527  1.00 27.24           C  
ATOM   1125  N   ASN A 203      50.983  93.955  39.737  1.00 28.95           N  
ATOM   1126  CA  ASN A 203      52.240  94.708  39.808  1.00 29.73           C  
ATOM   1127  C   ASN A 203      53.361  94.194  38.889  1.00 30.27           C  
ATOM   1128  O   ASN A 203      53.299  93.069  38.391  1.00 30.19           O  
ATOM   1129  CB  ASN A 203      52.721  94.835  41.267  1.00 29.73           C  
ATOM   1130  CG  ASN A 203      53.292  93.537  41.826  1.00 29.78           C  
ATOM   1131  OD1 ASN A 203      53.655  92.623  41.080  1.00 29.69           O  
ATOM   1132  ND2 ASN A 203      53.385  93.460  43.154  1.00 29.32           N  
ATOM   1133  N   SER A 204      54.382  95.031  38.691  1.00 31.00           N  
ATOM   1134  CA  SER A 204      55.505  94.743  37.792  1.00 31.76           C  
ATOM   1135  C   SER A 204      56.360  93.534  38.209  1.00 32.36           C  
ATOM   1136  O   SER A 204      57.035  92.928  37.369  1.00 32.50           O  
ATOM   1137  CB  SER A 204      56.393  95.977  37.656  1.00 31.65           C  
ATOM   1138  OG  SER A 204      56.860  96.385  38.927  1.00 31.84           O  
ATOM   1139  N   ARG A 205      56.336  93.199  39.499  1.00 32.83           N  
ATOM   1140  CA  ARG A 205      56.945  91.967  39.994  1.00 33.34           C  
ATOM   1141  C   ARG A 205      56.164  90.744  39.498  1.00 33.20           C  
ATOM   1142  O   ARG A 205      56.657  89.615  39.571  1.00 33.53           O  
ATOM   1143  CB  ARG A 205      56.987  91.957  41.528  1.00 33.74           C  
ATOM   1144  CG  ARG A 205      58.222  92.602  42.149  1.00 35.56           C  
ATOM   1145  CD  ARG A 205      58.092  92.912  43.651  1.00 38.47           C  
ATOM   1146  NE  ARG A 205      57.616  94.278  43.918  1.00 40.54           N  
ATOM   1147  CZ  ARG A 205      58.389  95.302  44.294  1.00 41.51           C  
ATOM   1148  NH1 ARG A 205      59.704  95.144  44.453  1.00 41.73           N  
ATOM   1149  NH2 ARG A 205      57.844  96.495  44.511  1.00 41.75           N  
ATOM   1150  N   GLY A 206      54.941  90.969  39.019  1.00 32.85           N  
ATOM   1151  CA  GLY A 206      54.111  89.898  38.495  1.00 32.55           C  
ATOM   1152  C   GLY A 206      53.116  89.318  39.486  1.00 32.34           C  
ATOM   1153  O   GLY A 206      52.569  88.232  39.260  1.00 32.44           O  
ATOM   1154  N   GLU A 207      52.872  90.045  40.576  1.00 32.00           N  
ATOM   1155  CA  GLU A 207      51.967  89.587  41.628  1.00 31.66           C  
ATOM   1156  C   GLU A 207      50.518  89.964  41.345  1.00 31.55           C  
ATOM   1157  O   GLU A 207      50.236  91.032  40.790  1.00 31.50           O  
ATOM   1158  CB  GLU A 207      52.383  90.138  42.995  1.00 31.53           C  
ATOM   1159  CG  GLU A 207      53.860  89.994  43.315  1.00 31.47           C  
ATOM   1160  CD  GLU A 207      54.166  90.291  44.767  1.00 31.67           C  
ATOM   1161  OE1 GLU A 207      54.125  89.343  45.586  1.00 31.29           O  
ATOM   1162  OE2 GLU A 207      54.446  91.470  45.086  1.00 31.56           O  
ATOM   1163  N   ILE A 208      49.606  89.070  41.722  1.00 31.32           N  
ATOM   1164  CA  ILE A 208      48.179  89.356  41.678  1.00 31.06           C  
ATOM   1165  C   ILE A 208      47.635  89.281  43.096  1.00 30.94           C  
ATOM   1166  O   ILE A 208      47.720  88.234  43.732  1.00 30.92           O  
ATOM   1167  CB  ILE A 208      47.446  88.371  40.755  1.00 30.90           C  
ATOM   1168  CG1 ILE A 208      48.001  88.456  39.334  1.00 30.68           C  
ATOM   1169  CG2 ILE A 208      45.955  88.668  40.749  1.00 31.18           C  
ATOM   1170  CD1 ILE A 208      47.741  87.231  38.494  1.00 30.52           C  
ATOM   1171  N   LYS A 209      47.084  90.392  43.583  1.00 30.82           N  
ATOM   1172  CA  LYS A 209      46.645  90.491  44.974  1.00 30.81           C  
ATOM   1173  C   LYS A 209      45.201  90.985  45.154  1.00 30.97           C  
ATOM   1174  O   LYS A 209      44.527  91.331  44.185  1.00 31.06           O  
ATOM   1175  CB  LYS A 209      47.620  91.357  45.767  1.00 30.78           C  
ATOM   1176  CG  LYS A 209      48.901  90.641  46.155  1.00 30.74           C  
ATOM   1177  CD  LYS A 209      50.069  91.600  46.263  1.00 30.14           C  
ATOM   1178  CE  LYS A 209      51.243  90.937  46.943  1.00 30.07           C  
ATOM   1179  NZ  LYS A 209      52.377  91.884  47.080  1.00 30.44           N  
ATOM   1180  N   LEU A 210      44.740  90.999  46.405  1.00 31.12           N  
ATOM   1181  CA  LEU A 210      43.361  91.333  46.755  1.00 31.24           C  
ATOM   1182  C   LEU A 210      43.314  92.366  47.869  1.00 31.60           C  
ATOM   1183  O   LEU A 210      44.059  92.268  48.843  1.00 31.82           O  
ATOM   1184  CB  LEU A 210      42.619  90.088  47.245  1.00 31.03           C  
ATOM   1185  CG  LEU A 210      41.997  89.092  46.273  1.00 30.78           C  
ATOM   1186  CD1 LEU A 210      41.322  87.989  47.064  1.00 30.31           C  
ATOM   1187  CD2 LEU A 210      41.003  89.763  45.344  1.00 30.72           C  
ATOM   1188  N   CYS A 211      42.423  93.342  47.731  1.00 32.02           N  
ATOM   1189  CA  CYS A 211      42.186  94.337  48.773  1.00 32.33           C  
ATOM   1190  C   CYS A 211      40.701  94.625  48.899  1.00 32.51           C  
ATOM   1191  O   CYS A 211      39.881  93.987  48.242  1.00 32.52           O  
ATOM   1192  CB  CYS A 211      42.931  95.625  48.458  1.00 32.31           C  
ATOM   1193  SG  CYS A 211      42.321  96.408  46.963  1.00 33.09           S  
ATOM   1194  N   ASP A 212      40.371  95.596  49.747  1.00 32.94           N  
ATOM   1195  CA  ASP A 212      38.990  96.021  50.013  1.00 33.28           C  
ATOM   1196  C   ASP A 212      38.060  94.894  50.494  1.00 33.44           C  
ATOM   1197  O   ASP A 212      36.835  94.994  50.403  1.00 33.41           O  
ATOM   1198  CB  ASP A 212      38.412  96.811  48.825  1.00 33.27           C  
ATOM   1199  CG  ASP A 212      39.293  97.991  48.425  1.00 33.57           C  
ATOM   1200  OD1 ASP A 212      39.990  98.546  49.300  1.00 33.54           O  
ATOM   1201  OD2 ASP A 212      39.359  98.433  47.258  1.00 34.24           O  
ATOM   1202  N   PHE A 213      38.660  93.833  51.023  1.00 33.82           N  
ATOM   1203  CA  PHE A 213      37.917  92.759  51.669  1.00 34.38           C  
ATOM   1204  C   PHE A 213      37.538  93.207  53.074  1.00 34.98           C  
ATOM   1205  O   PHE A 213      38.252  94.000  53.692  1.00 35.18           O  
ATOM   1206  CB  PHE A 213      38.749  91.471  51.727  1.00 34.21           C  
ATOM   1207  CG  PHE A 213      40.148  91.676  52.218  1.00 33.62           C  
ATOM   1208  CD1 PHE A 213      40.446  91.561  53.568  1.00 33.41           C  
ATOM   1209  CD2 PHE A 213      41.166  91.992  51.330  1.00 33.25           C  
ATOM   1210  CE1 PHE A 213      41.735  91.762  54.029  1.00 33.67           C  
ATOM   1211  CE2 PHE A 213      42.455  92.195  51.778  1.00 33.51           C  
ATOM   1212  CZ  PHE A 213      42.743  92.081  53.133  1.00 33.94           C  
ATOM   1213  N   GLY A 214      36.419  92.694  53.576  1.00 35.61           N  
ATOM   1214  CA  GLY A 214      35.889  93.114  54.861  1.00 36.16           C  
ATOM   1215  C   GLY A 214      36.554  92.492  56.069  1.00 36.69           C  
ATOM   1216  O   GLY A 214      36.077  91.488  56.601  1.00 36.70           O  
ATOM   1217  N   VAL A 215      37.653  93.101  56.505  1.00 37.28           N  
ATOM   1218  CA  VAL A 215      38.362  92.671  57.708  1.00 38.08           C  
ATOM   1219  C   VAL A 215      37.582  93.036  58.970  1.00 38.65           C  
ATOM   1220  O   VAL A 215      37.374  92.192  59.845  1.00 38.79           O  
ATOM   1221  CB  VAL A 215      39.774  93.285  57.795  1.00 38.02           C  
ATOM   1222  CG1 VAL A 215      40.796  92.218  58.137  1.00 38.24           C  
ATOM   1223  CG2 VAL A 215      40.145  93.964  56.495  1.00 38.05           C  
ATOM   1224  N   SER A 216      37.154  94.296  59.046  1.00 39.38           N  
ATOM   1225  CA  SER A 216      36.381  94.816  60.171  1.00 40.04           C  
ATOM   1226  C   SER A 216      34.886  94.756  59.889  1.00 40.66           C  
ATOM   1227  O   SER A 216      34.409  95.327  58.906  1.00 40.75           O  
ATOM   1228  CB  SER A 216      36.781  96.264  60.456  1.00 40.03           C  
ATOM   1229  OG  SER A 216      35.767  96.943  61.179  1.00 40.05           O  
ATOM   1230  N   GLY A 217      34.146  94.075  60.760  1.00 41.40           N  
ATOM   1231  CA  GLY A 217      32.696  94.042  60.665  1.00 42.30           C  
ATOM   1232  C   GLY A 217      32.114  95.439  60.786  1.00 42.93           C  
ATOM   1233  O   GLY A 217      31.210  95.819  60.038  1.00 42.95           O  
ATOM   1234  N   GLN A 218      32.665  96.207  61.724  1.00 43.56           N  
ATOM   1235  CA  GLN A 218      32.208  97.560  62.014  1.00 44.05           C  
ATOM   1236  C   GLN A 218      32.298  98.477  60.798  1.00 44.24           C  
ATOM   1237  O   GLN A 218      31.368  99.239  60.543  1.00 44.44           O  
ATOM   1238  CB  GLN A 218      32.986  98.143  63.205  1.00 44.21           C  
ATOM   1239  CG  GLN A 218      32.304  99.297  63.957  1.00 44.65           C  
ATOM   1240  CD  GLN A 218      30.819  99.079  64.187  1.00 45.17           C  
ATOM   1241  OE1 GLN A 218      29.991  99.635  63.468  1.00 45.56           O  
ATOM   1242  NE2 GLN A 218      30.481  98.276  65.189  1.00 45.39           N  
ATOM   1243  N   LEU A 219      33.401  98.392  60.051  1.00 44.52           N  
ATOM   1244  CA  LEU A 219      33.620  99.250  58.879  1.00 44.83           C  
ATOM   1245  C   LEU A 219      32.588  99.014  57.782  1.00 45.25           C  
ATOM   1246  O   LEU A 219      32.176  99.956  57.108  1.00 45.38           O  
ATOM   1247  CB  LEU A 219      35.030  99.074  58.307  1.00 44.66           C  
ATOM   1248  CG  LEU A 219      35.816 100.335  57.928  1.00 44.27           C  
ATOM   1249  CD1 LEU A 219      37.189  99.969  57.397  1.00 44.17           C  
ATOM   1250  CD2 LEU A 219      35.088 101.194  56.914  1.00 43.97           C  
ATOM   1251  N   ILE A 220      32.179  97.757  57.610  1.00 45.67           N  
ATOM   1252  CA  ILE A 220      31.138  97.401  56.647  1.00 46.06           C  
ATOM   1253  C   ILE A 220      29.791  97.984  57.075  1.00 46.40           C  
ATOM   1254  O   ILE A 220      29.162  98.717  56.306  1.00 46.55           O  
ATOM   1255  CB  ILE A 220      31.076  95.860  56.448  1.00 46.06           C  
ATOM   1256  CG1 ILE A 220      32.128  95.421  55.428  1.00 45.93           C  
ATOM   1257  CG2 ILE A 220      29.687  95.394  56.001  1.00 46.01           C  
ATOM   1258  CD1 ILE A 220      33.033  94.356  55.945  1.00 45.97           C  
ATOM   1259  N   ASP A 221      29.376  97.679  58.307  1.00 46.77           N  
ATOM   1260  CA  ASP A 221      28.126  98.191  58.873  1.00 47.18           C  
ATOM   1261  C   ASP A 221      28.119  99.721  58.922  1.00 47.18           C  
ATOM   1262  O   ASP A 221      27.063 100.346  59.055  1.00 47.31           O  
ATOM   1263  CB  ASP A 221      27.882  97.606  60.273  1.00 47.35           C  
ATOM   1264  CG  ASP A 221      27.410  96.151  60.232  1.00 48.17           C  
ATOM   1265  OD1 ASP A 221      28.206  95.249  60.587  1.00 48.70           O  
ATOM   1266  OD2 ASP A 221      26.260  95.813  59.864  1.00 49.05           O  
ATOM   1267  N   SER A 222      29.304 100.309  58.796  1.00 47.13           N  
ATOM   1268  CA  SER A 222      29.460 101.754  58.797  1.00 47.30           C  
ATOM   1269  C   SER A 222      29.271 102.375  57.416  1.00 47.29           C  
ATOM   1270  O   SER A 222      28.897 103.543  57.310  1.00 47.36           O  
ATOM   1271  CB  SER A 222      30.824 102.136  59.362  1.00 47.34           C  
ATOM   1272  OG  SER A 222      30.746 102.328  60.764  1.00 47.82           O  
ATOM   1273  N   MET A 223      29.540 101.600  56.365  1.00 47.31           N  
ATOM   1274  CA  MET A 223      29.332 102.056  54.987  1.00 47.19           C  
ATOM   1275  C   MET A 223      28.671 100.980  54.132  1.00 47.22           C  
ATOM   1276  O   MET A 223      27.533 100.581  54.393  1.00 47.24           O  
ATOM   1277  CB  MET A 223      30.636 102.544  54.331  1.00 47.08           C  
ATOM   1278  CG  MET A 223      31.934 102.076  54.987  1.00 46.76           C  
ATOM   1279  SD  MET A 223      33.253 101.660  53.814  1.00 45.80           S  
ATOM   1280  CE  MET A 223      32.871  99.937  53.480  1.00 46.31           C  
ATOM   1281  N   VAL A 228      27.195 102.913  45.206  1.00 34.52           N  
ATOM   1282  CA  VAL A 228      26.643 103.404  43.946  1.00 34.51           C  
ATOM   1283  C   VAL A 228      26.569 102.265  42.927  1.00 34.96           C  
ATOM   1284  O   VAL A 228      27.529 101.497  42.770  1.00 35.01           O  
ATOM   1285  CB  VAL A 228      27.452 104.610  43.363  1.00 34.43           C  
ATOM   1286  CG1 VAL A 228      26.710 105.927  43.597  1.00 33.77           C  
ATOM   1287  CG2 VAL A 228      28.890 104.669  43.918  1.00 33.82           C  
ATOM   1288  N   GLY A 229      25.428 102.158  42.244  1.00 35.43           N  
ATOM   1289  CA  GLY A 229      25.166 101.044  41.344  1.00 35.92           C  
ATOM   1290  C   GLY A 229      25.291 101.357  39.862  1.00 36.24           C  
ATOM   1291  O   GLY A 229      24.299 101.261  39.123  1.00 36.44           O  
ATOM   1292  N   THR A 230      26.501 101.728  39.430  1.00 36.26           N  
ATOM   1293  CA  THR A 230      26.812 101.903  38.005  1.00 36.26           C  
ATOM   1294  C   THR A 230      26.736 100.566  37.266  1.00 36.10           C  
ATOM   1295  O   THR A 230      26.338 100.520  36.097  1.00 36.41           O  
ATOM   1296  CB  THR A 230      28.221 102.508  37.809  1.00 36.41           C  
ATOM   1297  OG1 THR A 230      28.796 102.847  39.081  1.00 36.73           O  
ATOM   1298  CG2 THR A 230      28.137 103.842  37.070  1.00 36.82           C  
ATOM   1299  N   ARG A 231      27.142  99.496  37.963  1.00 35.59           N  
ATOM   1300  CA  ARG A 231      27.122  98.114  37.470  1.00 34.83           C  
ATOM   1301  C   ARG A 231      27.527  97.161  38.595  1.00 34.13           C  
ATOM   1302  O   ARG A 231      28.628  97.261  39.127  1.00 34.18           O  
ATOM   1303  CB  ARG A 231      28.042  97.934  36.255  1.00 34.96           C  
ATOM   1304  CG  ARG A 231      29.445  98.509  36.399  1.00 35.69           C  
ATOM   1305  CD  ARG A 231      30.443  97.939  35.403  1.00 36.99           C  
ATOM   1306  NE  ARG A 231      31.813  98.020  35.899  1.00 38.19           N  
ATOM   1307  CZ  ARG A 231      32.799  98.660  35.279  1.00 39.25           C  
ATOM   1308  NH1 ARG A 231      32.575  99.282  34.121  1.00 39.39           N  
ATOM   1309  NH2 ARG A 231      34.016  98.680  35.817  1.00 39.13           N  
ATOM   1310  N   SER A 232      26.638  96.238  38.953  1.00 33.37           N  
ATOM   1311  CA  SER A 232      26.833  95.405  40.138  1.00 32.66           C  
ATOM   1312  C   SER A 232      27.504  94.058  39.899  1.00 32.21           C  
ATOM   1313  O   SER A 232      27.369  93.457  38.834  1.00 32.08           O  
ATOM   1314  CB  SER A 232      25.511  95.190  40.868  1.00 32.63           C  
ATOM   1315  OG  SER A 232      25.752  94.936  42.241  1.00 32.90           O  
ATOM   1316  N   TYR A 233      28.219  93.592  40.921  1.00 31.62           N  
ATOM   1317  CA  TYR A 233      28.842  92.275  40.914  1.00 30.91           C  
ATOM   1318  C   TYR A 233      28.232  91.391  41.990  1.00 30.63           C  
ATOM   1319  O   TYR A 233      28.788  90.341  42.323  1.00 30.64           O  
ATOM   1320  CB  TYR A 233      30.345  92.392  41.141  1.00 30.74           C  
ATOM   1321  CG  TYR A 233      31.068  93.151  40.058  1.00 30.68           C  
ATOM   1322  CD1 TYR A 233      31.664  92.483  38.991  1.00 30.55           C  
ATOM   1323  CD2 TYR A 233      31.162  94.541  40.099  1.00 30.66           C  
ATOM   1324  CE1 TYR A 233      32.335  93.184  37.993  1.00 30.42           C  
ATOM   1325  CE2 TYR A 233      31.827  95.247  39.108  1.00 30.32           C  
ATOM   1326  CZ  TYR A 233      32.410  94.566  38.060  1.00 30.12           C  
ATOM   1327  OH  TYR A 233      33.067  95.274  37.083  1.00 30.07           O  
ATOM   1328  N   MET A 234      27.092  91.819  42.532  1.00 30.17           N  
ATOM   1329  CA  MET A 234      26.433  91.086  43.606  1.00 29.78           C  
ATOM   1330  C   MET A 234      25.686  89.891  43.056  1.00 29.40           C  
ATOM   1331  O   MET A 234      25.085  89.960  41.985  1.00 29.48           O  
ATOM   1332  CB  MET A 234      25.477  91.986  44.371  1.00 29.90           C  
ATOM   1333  CG  MET A 234      26.128  92.827  45.440  1.00 30.71           C  
ATOM   1334  SD  MET A 234      24.882  93.880  46.202  1.00 33.53           S  
ATOM   1335  CE  MET A 234      25.844  95.385  46.558  1.00 33.55           C  
ATOM   1336  N   ALA A 235      25.741  88.791  43.799  1.00 28.96           N  
ATOM   1337  CA  ALA A 235      25.133  87.533  43.392  1.00 28.52           C  
ATOM   1338  C   ALA A 235      23.623  87.632  43.505  1.00 28.26           C  
ATOM   1339  O   ALA A 235      23.128  88.333  44.381  1.00 28.46           O  
ATOM   1340  CB  ALA A 235      25.648  86.420  44.260  1.00 28.56           C  
ATOM   1341  N   PRO A 236      22.891  86.936  42.635  1.00 27.96           N  
ATOM   1342  CA  PRO A 236      21.424  87.004  42.627  1.00 27.83           C  
ATOM   1343  C   PRO A 236      20.838  86.856  44.026  1.00 27.78           C  
ATOM   1344  O   PRO A 236      19.968  87.638  44.410  1.00 27.88           O  
ATOM   1345  CB  PRO A 236      21.007  85.798  41.778  1.00 27.73           C  
ATOM   1346  CG  PRO A 236      22.208  85.350  41.054  1.00 27.82           C  
ATOM   1347  CD  PRO A 236      23.410  86.031  41.600  1.00 27.92           C  
ATOM   1348  N   GLU A 237      21.334  85.876  44.777  1.00 27.67           N  
ATOM   1349  CA  GLU A 237      20.760  85.518  46.065  1.00 27.51           C  
ATOM   1350  C   GLU A 237      21.086  86.527  47.156  1.00 27.60           C  
ATOM   1351  O   GLU A 237      20.374  86.610  48.154  1.00 27.59           O  
ATOM   1352  CB  GLU A 237      21.197  84.105  46.469  1.00 27.45           C  
ATOM   1353  CG  GLU A 237      22.576  84.010  47.116  1.00 27.02           C  
ATOM   1354  CD  GLU A 237      23.721  84.051  46.121  1.00 25.66           C  
ATOM   1355  OE1 GLU A 237      23.469  84.002  44.903  1.00 24.98           O  
ATOM   1356  OE2 GLU A 237      24.886  84.125  46.565  1.00 25.24           O  
ATOM   1357  N   ARG A 238      22.161  87.288  46.969  1.00 27.82           N  
ATOM   1358  CA  ARG A 238      22.515  88.334  47.924  1.00 28.14           C  
ATOM   1359  C   ARG A 238      21.572  89.505  47.751  1.00 28.21           C  
ATOM   1360  O   ARG A 238      21.048  90.030  48.737  1.00 28.53           O  
ATOM   1361  CB  ARG A 238      23.970  88.800  47.776  1.00 28.10           C  
ATOM   1362  CG  ARG A 238      24.655  89.105  49.106  1.00 28.13           C  
ATOM   1363  CD  ARG A 238      24.415  90.514  49.653  1.00 28.69           C  
ATOM   1364  NE  ARG A 238      24.302  90.536  51.118  1.00 28.99           N  
ATOM   1365  CZ  ARG A 238      24.682  91.550  51.904  1.00 28.66           C  
ATOM   1366  NH1 ARG A 238      25.211  92.655  51.390  1.00 28.42           N  
ATOM   1367  NH2 ARG A 238      24.529  91.459  53.217  1.00 28.64           N  
ATOM   1368  N   LEU A 239      21.353  89.902  46.498  1.00 28.12           N  
ATOM   1369  CA  LEU A 239      20.422  90.978  46.185  1.00 28.15           C  
ATOM   1370  C   LEU A 239      19.075  90.701  46.849  1.00 28.45           C  
ATOM   1371  O   LEU A 239      18.435  91.618  47.366  1.00 28.49           O  
ATOM   1372  CB  LEU A 239      20.271  91.162  44.669  1.00 27.95           C  
ATOM   1373  CG  LEU A 239      21.517  91.516  43.841  1.00 26.97           C  
ATOM   1374  CD1 LEU A 239      21.267  91.247  42.378  1.00 25.84           C  
ATOM   1375  CD2 LEU A 239      21.956  92.958  44.037  1.00 26.21           C  
ATOM   1376  N   GLN A 240      18.684  89.425  46.872  1.00 28.75           N  
ATOM   1377  CA  GLN A 240      17.453  88.981  47.532  1.00 29.21           C  
ATOM   1378  C   GLN A 240      17.573  88.846  49.062  1.00 29.51           C  
ATOM   1379  O   GLN A 240      16.784  88.126  49.689  1.00 29.60           O  
ATOM   1380  CB  GLN A 240      16.953  87.667  46.917  1.00 29.14           C  
ATOM   1381  CG  GLN A 240      16.420  87.805  45.498  1.00 29.64           C  
ATOM   1382  CD  GLN A 240      16.245  86.469  44.790  1.00 30.42           C  
ATOM   1383  OE1 GLN A 240      15.263  86.267  44.071  1.00 30.89           O  
ATOM   1384  NE2 GLN A 240      17.194  85.560  44.983  1.00 30.66           N  
ATOM   1385  N   GLY A 241      18.559  89.525  49.651  1.00 29.82           N  
ATOM   1386  CA  GLY A 241      18.674  89.656  51.099  1.00 30.22           C  
ATOM   1387  C   GLY A 241      19.095  88.466  51.961  1.00 30.54           C  
ATOM   1388  O   GLY A 241      19.079  88.580  53.194  1.00 30.86           O  
ATOM   1389  N   THR A 242      19.448  87.332  51.351  1.00 30.45           N  
ATOM   1390  CA  THR A 242      20.060  86.229  52.098  1.00 30.38           C  
ATOM   1391  C   THR A 242      21.523  86.597  52.260  1.00 30.42           C  
ATOM   1392  O   THR A 242      22.162  86.974  51.279  1.00 30.65           O  
ATOM   1393  CB  THR A 242      19.918  84.871  51.360  1.00 30.52           C  
ATOM   1394  OG1 THR A 242      21.028  84.673  50.470  1.00 30.28           O  
ATOM   1395  CG2 THR A 242      18.691  84.845  50.436  1.00 30.39           C  
ATOM   1396  N   HIS A 243      22.062  86.499  53.475  1.00 30.38           N  
ATOM   1397  CA  HIS A 243      23.388  87.080  53.745  1.00 30.32           C  
ATOM   1398  C   HIS A 243      24.550  86.455  52.955  1.00 30.07           C  
ATOM   1399  O   HIS A 243      24.475  85.315  52.489  1.00 29.91           O  
ATOM   1400  CB  HIS A 243      23.709  87.173  55.253  1.00 30.51           C  
ATOM   1401  CG  HIS A 243      24.353  88.473  55.658  1.00 30.30           C  
ATOM   1402  ND1 HIS A 243      25.718  88.623  55.790  1.00 30.06           N  
ATOM   1403  CD2 HIS A 243      23.816  89.679  55.959  1.00 30.16           C  
ATOM   1404  CE1 HIS A 243      25.992  89.863  56.158  1.00 29.57           C  
ATOM   1405  NE2 HIS A 243      24.855  90.525  56.266  1.00 29.58           N  
ATOM   1406  N   TYR A 244      25.607  87.254  52.816  1.00 29.79           N  
ATOM   1407  CA  TYR A 244      26.769  86.977  51.978  1.00 29.41           C  
ATOM   1408  C   TYR A 244      27.506  85.691  52.380  1.00 28.95           C  
ATOM   1409  O   TYR A 244      27.829  85.486  53.553  1.00 29.01           O  
ATOM   1410  CB  TYR A 244      27.704  88.185  52.052  1.00 29.53           C  
ATOM   1411  CG  TYR A 244      28.658  88.347  50.895  1.00 30.47           C  
ATOM   1412  CD1 TYR A 244      28.437  89.313  49.912  1.00 31.25           C  
ATOM   1413  CD2 TYR A 244      29.810  87.565  50.806  1.00 31.08           C  
ATOM   1414  CE1 TYR A 244      29.334  89.474  48.855  1.00 32.04           C  
ATOM   1415  CE2 TYR A 244      30.703  87.711  49.756  1.00 31.46           C  
ATOM   1416  CZ  TYR A 244      30.467  88.663  48.787  1.00 32.12           C  
ATOM   1417  OH  TYR A 244      31.368  88.799  47.754  1.00 32.74           O  
ATOM   1418  N   SER A 245      27.763  84.843  51.384  1.00 28.20           N  
ATOM   1419  CA  SER A 245      28.404  83.540  51.554  1.00 27.33           C  
ATOM   1420  C   SER A 245      29.753  83.497  50.828  1.00 26.79           C  
ATOM   1421  O   SER A 245      30.183  84.487  50.238  1.00 26.82           O  
ATOM   1422  CB  SER A 245      27.473  82.449  51.005  1.00 27.36           C  
ATOM   1423  OG  SER A 245      28.137  81.204  50.863  1.00 27.29           O  
ATOM   1424  N   VAL A 246      30.424  82.350  50.876  1.00 26.03           N  
ATOM   1425  CA  VAL A 246      31.604  82.122  50.044  1.00 25.24           C  
ATOM   1426  C   VAL A 246      31.187  82.157  48.583  1.00 24.74           C  
ATOM   1427  O   VAL A 246      31.858  82.771  47.753  1.00 24.82           O  
ATOM   1428  CB  VAL A 246      32.259  80.749  50.312  1.00 25.24           C  
ATOM   1429  CG1 VAL A 246      33.754  80.908  50.533  1.00 25.21           C  
ATOM   1430  CG2 VAL A 246      31.596  80.035  51.486  1.00 25.23           C  
ATOM   1431  N   GLN A 247      30.057  81.510  48.291  1.00 23.95           N  
ATOM   1432  CA  GLN A 247      29.526  81.382  46.935  1.00 23.07           C  
ATOM   1433  C   GLN A 247      29.249  82.731  46.298  1.00 22.37           C  
ATOM   1434  O   GLN A 247      29.241  82.855  45.071  1.00 22.44           O  
ATOM   1435  CB  GLN A 247      28.243  80.545  46.919  1.00 23.21           C  
ATOM   1436  CG  GLN A 247      27.971  79.730  48.177  1.00 23.75           C  
ATOM   1437  CD  GLN A 247      28.945  78.586  48.355  1.00 24.79           C  
ATOM   1438  OE1 GLN A 247      29.434  78.354  49.465  1.00 25.62           O  
ATOM   1439  NE2 GLN A 247      29.234  77.869  47.268  1.00 24.49           N  
ATOM   1440  N   SER A 248      29.017  83.735  47.137  1.00 21.37           N  
ATOM   1441  CA  SER A 248      28.799  85.089  46.659  1.00 20.44           C  
ATOM   1442  C   SER A 248      30.067  85.692  46.062  1.00 19.82           C  
ATOM   1443  O   SER A 248      30.013  86.320  45.007  1.00 19.68           O  
ATOM   1444  CB  SER A 248      28.233  85.956  47.771  1.00 20.39           C  
ATOM   1445  OG  SER A 248      26.882  85.606  47.992  1.00 20.41           O  
ATOM   1446  N   ASP A 249      31.203  85.483  46.724  1.00 19.09           N  
ATOM   1447  CA  ASP A 249      32.497  85.884  46.179  1.00 18.50           C  
ATOM   1448  C   ASP A 249      32.785  85.143  44.887  1.00 18.09           C  
ATOM   1449  O   ASP A 249      33.300  85.715  43.921  1.00 17.82           O  
ATOM   1450  CB  ASP A 249      33.611  85.597  47.176  1.00 18.50           C  
ATOM   1451  CG  ASP A 249      33.636  86.582  48.318  1.00 18.75           C  
ATOM   1452  OD1 ASP A 249      33.518  87.798  48.063  1.00 18.66           O  
ATOM   1453  OD2 ASP A 249      33.777  86.232  49.507  1.00 19.60           O  
ATOM   1454  N   ILE A 250      32.442  83.858  44.891  1.00 17.73           N  
ATOM   1455  CA  ILE A 250      32.632  82.988  43.742  1.00 17.32           C  
ATOM   1456  C   ILE A 250      31.886  83.548  42.541  1.00 17.46           C  
ATOM   1457  O   ILE A 250      32.441  83.598  41.443  1.00 17.85           O  
ATOM   1458  CB  ILE A 250      32.176  81.551  44.074  1.00 17.07           C  
ATOM   1459  CG1 ILE A 250      33.019  80.994  45.236  1.00 16.66           C  
ATOM   1460  CG2 ILE A 250      32.202  80.678  42.824  1.00 16.84           C  
ATOM   1461  CD1 ILE A 250      33.444  79.548  45.121  1.00 15.83           C  
ATOM   1462  N   TRP A 251      30.644  83.988  42.753  1.00 17.21           N  
ATOM   1463  CA  TRP A 251      29.861  84.599  41.687  1.00 16.92           C  
ATOM   1464  C   TRP A 251      30.530  85.889  41.223  1.00 16.85           C  
ATOM   1465  O   TRP A 251      30.659  86.134  40.029  1.00 16.84           O  
ATOM   1466  CB  TRP A 251      28.419  84.859  42.139  1.00 16.96           C  
ATOM   1467  CG  TRP A 251      27.625  85.711  41.176  1.00 16.69           C  
ATOM   1468  CD1 TRP A 251      27.705  87.065  41.021  1.00 16.78           C  
ATOM   1469  CD2 TRP A 251      26.650  85.263  40.235  1.00 16.28           C  
ATOM   1470  NE1 TRP A 251      26.837  87.488  40.045  1.00 17.01           N  
ATOM   1471  CE2 TRP A 251      26.175  86.400  39.545  1.00 16.72           C  
ATOM   1472  CE3 TRP A 251      26.120  84.012  39.906  1.00 17.00           C  
ATOM   1473  CZ2 TRP A 251      25.199  86.325  38.548  1.00 17.05           C  
ATOM   1474  CZ3 TRP A 251      25.144  83.935  38.913  1.00 17.57           C  
ATOM   1475  CH2 TRP A 251      24.696  85.088  38.247  1.00 17.62           C  
ATOM   1476  N   SER A 252      30.964  86.705  42.172  1.00 16.90           N  
ATOM   1477  CA  SER A 252      31.652  87.946  41.849  1.00 17.14           C  
ATOM   1478  C   SER A 252      32.904  87.675  41.017  1.00 17.26           C  
ATOM   1479  O   SER A 252      33.245  88.463  40.138  1.00 17.31           O  
ATOM   1480  CB  SER A 252      32.012  88.708  43.124  1.00 17.25           C  
ATOM   1481  OG  SER A 252      30.937  89.522  43.565  1.00 17.67           O  
ATOM   1482  N   MET A 253      33.575  86.553  41.291  1.00 17.33           N  
ATOM   1483  CA  MET A 253      34.765  86.154  40.540  1.00 17.10           C  
ATOM   1484  C   MET A 253      34.442  85.762  39.104  1.00 17.13           C  
ATOM   1485  O   MET A 253      35.117  86.199  38.179  1.00 17.04           O  
ATOM   1486  CB  MET A 253      35.506  85.022  41.243  1.00 16.98           C  
ATOM   1487  CG  MET A 253      36.922  84.824  40.713  1.00 16.94           C  
ATOM   1488  SD  MET A 253      37.741  83.317  41.272  1.00 16.09           S  
ATOM   1489  CE  MET A 253      36.619  82.054  40.660  1.00 15.27           C  
ATOM   1490  N   GLY A 254      33.412  84.937  38.934  1.00 17.40           N  
ATOM   1491  CA  GLY A 254      32.942  84.520  37.623  1.00 17.82           C  
ATOM   1492  C   GLY A 254      32.639  85.690  36.703  1.00 18.11           C  
ATOM   1493  O   GLY A 254      33.279  85.849  35.659  1.00 18.19           O  
ATOM   1494  N   LEU A 255      31.669  86.512  37.098  1.00 18.26           N  
ATOM   1495  CA  LEU A 255      31.352  87.745  36.385  1.00 18.54           C  
ATOM   1496  C   LEU A 255      32.603  88.575  36.084  1.00 18.53           C  
ATOM   1497  O   LEU A 255      32.748  89.094  34.976  1.00 18.61           O  
ATOM   1498  CB  LEU A 255      30.353  88.584  37.182  1.00 18.71           C  
ATOM   1499  CG  LEU A 255      29.265  89.286  36.366  1.00 19.25           C  
ATOM   1500  CD1 LEU A 255      28.048  88.380  36.213  1.00 19.70           C  
ATOM   1501  CD2 LEU A 255      28.876  90.608  37.012  1.00 19.48           C  
ATOM   1502  N   SER A 256      33.497  88.687  37.070  1.00 18.45           N  
ATOM   1503  CA  SER A 256      34.778  89.378  36.903  1.00 18.27           C  
ATOM   1504  C   SER A 256      35.612  88.768  35.781  1.00 18.39           C  
ATOM   1505  O   SER A 256      36.192  89.485  34.959  1.00 18.44           O  
ATOM   1506  CB  SER A 256      35.579  89.351  38.199  1.00 18.01           C  
ATOM   1507  OG  SER A 256      34.961  90.145  39.183  1.00 17.57           O  
ATOM   1508  N   LEU A 257      35.668  87.440  35.752  1.00 18.36           N  
ATOM   1509  CA  LEU A 257      36.403  86.742  34.711  1.00 18.34           C  
ATOM   1510  C   LEU A 257      35.782  87.023  33.346  1.00 18.35           C  
ATOM   1511  O   LEU A 257      36.470  87.499  32.441  1.00 18.37           O  
ATOM   1512  CB  LEU A 257      36.480  85.239  35.004  1.00 18.28           C  
ATOM   1513  CG  LEU A 257      37.445  84.846  36.125  1.00 18.01           C  
ATOM   1514  CD1 LEU A 257      37.446  83.349  36.341  1.00 17.73           C  
ATOM   1515  CD2 LEU A 257      38.851  85.343  35.838  1.00 18.10           C  
ATOM   1516  N   VAL A 258      34.481  86.764  33.221  1.00 18.35           N  
ATOM   1517  CA  VAL A 258      33.758  86.982  31.966  1.00 18.51           C  
ATOM   1518  C   VAL A 258      33.932  88.420  31.467  1.00 18.89           C  
ATOM   1519  O   VAL A 258      34.057  88.658  30.261  1.00 18.82           O  
ATOM   1520  CB  VAL A 258      32.260  86.635  32.096  1.00 18.28           C  
ATOM   1521  CG1 VAL A 258      31.528  86.909  30.794  1.00 17.87           C  
ATOM   1522  CG2 VAL A 258      32.085  85.181  32.492  1.00 18.16           C  
ATOM   1523  N   GLU A 259      33.957  89.365  32.405  1.00 19.23           N  
ATOM   1524  CA  GLU A 259      34.220  90.756  32.081  1.00 19.60           C  
ATOM   1525  C   GLU A 259      35.600  90.911  31.445  1.00 19.87           C  
ATOM   1526  O   GLU A 259      35.719  91.447  30.343  1.00 20.06           O  
ATOM   1527  CB  GLU A 259      34.095  91.643  33.320  1.00 19.53           C  
ATOM   1528  CG  GLU A 259      34.187  93.130  33.005  1.00 19.97           C  
ATOM   1529  CD  GLU A 259      33.900  94.018  34.199  1.00 20.29           C  
ATOM   1530  OE1 GLU A 259      34.577  95.064  34.335  1.00 20.42           O  
ATOM   1531  OE2 GLU A 259      32.995  93.677  34.992  1.00 20.04           O  
ATOM   1532  N   LEU A 260      36.635  90.427  32.129  1.00 20.14           N  
ATOM   1533  CA  LEU A 260      38.011  90.573  31.647  1.00 20.30           C  
ATOM   1534  C   LEU A 260      38.273  89.768  30.372  1.00 20.59           C  
ATOM   1535  O   LEU A 260      39.112  90.146  29.543  1.00 20.65           O  
ATOM   1536  CB  LEU A 260      39.009  90.192  32.739  1.00 20.06           C  
ATOM   1537  CG  LEU A 260      38.943  91.043  34.004  1.00 19.82           C  
ATOM   1538  CD1 LEU A 260      39.463  90.248  35.183  1.00 20.15           C  
ATOM   1539  CD2 LEU A 260      39.721  92.339  33.841  1.00 19.60           C  
ATOM   1540  N   ALA A 261      37.543  88.665  30.228  1.00 20.70           N  
ATOM   1541  CA  ALA A 261      37.628  87.821  29.048  1.00 20.82           C  
ATOM   1542  C   ALA A 261      37.043  88.522  27.824  1.00 20.91           C  
ATOM   1543  O   ALA A 261      37.627  88.484  26.742  1.00 20.87           O  
ATOM   1544  CB  ALA A 261      36.916  86.488  29.300  1.00 20.80           C  
ATOM   1545  N   VAL A 262      35.898  89.172  28.012  1.00 21.06           N  
ATOM   1546  CA  VAL A 262      35.134  89.745  26.904  1.00 21.27           C  
ATOM   1547  C   VAL A 262      35.434  91.235  26.651  1.00 21.51           C  
ATOM   1548  O   VAL A 262      35.237  91.742  25.542  1.00 21.59           O  
ATOM   1549  CB  VAL A 262      33.617  89.483  27.091  1.00 21.17           C  
ATOM   1550  CG1 VAL A 262      32.785  90.284  26.100  1.00 21.04           C  
ATOM   1551  CG2 VAL A 262      33.328  87.995  26.953  1.00 20.75           C  
ATOM   1552  N   GLY A 263      35.920  91.931  27.670  1.00 21.67           N  
ATOM   1553  CA  GLY A 263      36.317  93.316  27.500  1.00 22.16           C  
ATOM   1554  C   GLY A 263      35.312  94.339  27.999  1.00 22.39           C  
ATOM   1555  O   GLY A 263      35.588  95.542  27.988  1.00 22.46           O  
ATOM   1556  N   ARG A 264      34.150  93.869  28.435  1.00 22.57           N  
ATOM   1557  CA  ARG A 264      33.158  94.758  29.022  1.00 22.86           C  
ATOM   1558  C   ARG A 264      32.292  94.060  30.057  1.00 22.94           C  
ATOM   1559  O   ARG A 264      32.225  92.830  30.105  1.00 22.80           O  
ATOM   1560  CB  ARG A 264      32.291  95.407  27.934  1.00 23.03           C  
ATOM   1561  CG  ARG A 264      31.149  94.548  27.405  1.00 23.07           C  
ATOM   1562  CD  ARG A 264      30.270  95.264  26.391  1.00 23.28           C  
ATOM   1563  NE  ARG A 264      29.220  94.400  25.864  1.00 23.77           N  
ATOM   1564  CZ  ARG A 264      28.078  94.137  26.489  1.00 24.63           C  
ATOM   1565  NH1 ARG A 264      27.815  94.669  27.678  1.00 24.79           N  
ATOM   1566  NH2 ARG A 264      27.187  93.338  25.925  1.00 24.81           N  
ATOM   1567  N   TYR A 265      31.645  94.866  30.891  1.00 23.13           N  
ATOM   1568  CA  TYR A 265      30.677  94.370  31.850  1.00 23.31           C  
ATOM   1569  C   TYR A 265      29.635  93.589  31.067  1.00 23.94           C  
ATOM   1570  O   TYR A 265      29.034  94.126  30.141  1.00 24.03           O  
ATOM   1571  CB  TYR A 265      30.044  95.535  32.611  1.00 23.01           C  
ATOM   1572  CG  TYR A 265      29.116  95.115  33.718  1.00 21.59           C  
ATOM   1573  CD1 TYR A 265      29.598  94.455  34.846  1.00 20.90           C  
ATOM   1574  CD2 TYR A 265      27.758  95.378  33.641  1.00 20.12           C  
ATOM   1575  CE1 TYR A 265      28.745  94.066  35.864  1.00 19.98           C  
ATOM   1576  CE2 TYR A 265      26.902  95.002  34.653  1.00 19.36           C  
ATOM   1577  CZ  TYR A 265      27.399  94.345  35.761  1.00 19.37           C  
ATOM   1578  OH  TYR A 265      26.545  93.963  36.765  1.00 18.78           O  
ATOM   1579  N   PRO A 266      29.450  92.318  31.411  1.00 24.58           N  
ATOM   1580  CA  PRO A 266      28.664  91.405  30.580  1.00 25.36           C  
ATOM   1581  C   PRO A 266      27.162  91.418  30.839  1.00 26.35           C  
ATOM   1582  O   PRO A 266      26.452  90.784  30.048  1.00 26.50           O  
ATOM   1583  CB  PRO A 266      29.227  90.028  30.952  1.00 25.26           C  
ATOM   1584  CG  PRO A 266      30.232  90.274  32.059  1.00 24.89           C  
ATOM   1585  CD  PRO A 266      29.980  91.639  32.601  1.00 24.63           C  
ATOM   1586  N   ILE A 267      26.686  92.096  31.889  1.00 27.30           N  
ATOM   1587  CA  ILE A 267      25.311  91.865  32.357  1.00 28.22           C  
ATOM   1588  C   ILE A 267      24.222  92.178  31.340  1.00 29.16           C  
ATOM   1589  O   ILE A 267      23.278  91.399  31.224  1.00 29.65           O  
ATOM   1590  CB  ILE A 267      25.031  92.475  33.733  1.00 28.09           C  
ATOM   1591  CG1 ILE A 267      25.571  91.546  34.824  1.00 27.92           C  
ATOM   1592  CG2 ILE A 267      23.535  92.715  33.935  1.00 27.98           C  
ATOM   1593  CD1 ILE A 267      25.176  90.102  34.664  1.00 27.67           C  
ATOM   1594  N   PRO A 268      24.323  93.285  30.606  1.00 29.84           N  
ATOM   1595  CA  PRO A 268      23.689  93.325  29.285  1.00 30.33           C  
ATOM   1596  C   PRO A 268      24.581  92.484  28.352  1.00 31.07           C  
ATOM   1597  O   PRO A 268      25.654  92.945  27.958  1.00 31.07           O  
ATOM   1598  CB  PRO A 268      23.701  94.817  28.925  1.00 30.25           C  
ATOM   1599  CG  PRO A 268      24.115  95.533  30.187  1.00 30.03           C  
ATOM   1600  CD  PRO A 268      24.964  94.567  30.954  1.00 29.74           C  
ATOM   1601  N   PRO A 269      24.176  91.248  28.053  1.00 31.76           N  
ATOM   1602  CA  PRO A 269      25.030  90.306  27.316  1.00 32.30           C  
ATOM   1603  C   PRO A 269      25.220  90.692  25.855  1.00 32.98           C  
ATOM   1604  O   PRO A 269      24.269  91.160  25.226  1.00 32.94           O  
ATOM   1605  CB  PRO A 269      24.259  88.986  27.409  1.00 32.27           C  
ATOM   1606  CG  PRO A 269      23.254  89.204  28.480  1.00 32.12           C  
ATOM   1607  CD  PRO A 269      22.872  90.647  28.378  1.00 31.86           C  
ATOM   1608  N   PRO A 270      26.435  90.510  25.336  1.00 33.70           N  
ATOM   1609  CA  PRO A 270      26.738  90.816  23.935  1.00 34.35           C  
ATOM   1610  C   PRO A 270      25.993  89.910  22.964  1.00 35.05           C  
ATOM   1611  O   PRO A 270      26.071  88.679  23.067  1.00 34.87           O  
ATOM   1612  CB  PRO A 270      28.252  90.594  23.844  1.00 34.30           C  
ATOM   1613  CG  PRO A 270      28.574  89.688  24.964  1.00 34.01           C  
ATOM   1614  CD  PRO A 270      27.624  90.030  26.059  1.00 33.83           C  
ATOM   1615  N   ASP A 271      25.258  90.538  22.049  1.00 35.98           N  
ATOM   1616  CA  ASP A 271      24.529  89.830  21.004  1.00 36.91           C  
ATOM   1617  C   ASP A 271      25.511  89.409  19.917  1.00 37.54           C  
ATOM   1618  O   ASP A 271      26.553  90.053  19.731  1.00 37.62           O  
ATOM   1619  CB  ASP A 271      23.414  90.715  20.434  1.00 36.88           C  
ATOM   1620  CG  ASP A 271      23.834  91.455  19.170  1.00 37.42           C  
ATOM   1621  OD1 ASP A 271      24.710  92.349  19.256  1.00 36.92           O  
ATOM   1622  OD2 ASP A 271      23.338  91.204  18.045  1.00 38.29           O  
ATOM   1623  N   ALA A 272      25.171  88.336  19.203  1.00 38.20           N  
ATOM   1624  CA  ALA A 272      26.052  87.739  18.201  1.00 38.69           C  
ATOM   1625  C   ALA A 272      26.825  88.778  17.391  1.00 39.15           C  
ATOM   1626  O   ALA A 272      28.042  88.667  17.235  1.00 39.16           O  
ATOM   1627  CB  ALA A 272      25.266  86.820  17.288  1.00 38.59           C  
ATOM   1628  N   LYS A 273      26.117  89.794  16.905  1.00 39.86           N  
ATOM   1629  CA  LYS A 273      26.726  90.855  16.109  1.00 40.80           C  
ATOM   1630  C   LYS A 273      27.891  91.519  16.844  1.00 41.53           C  
ATOM   1631  O   LYS A 273      28.961  91.707  16.263  1.00 41.68           O  
ATOM   1632  CB  LYS A 273      25.676  91.895  15.692  1.00 40.76           C  
ATOM   1633  CG  LYS A 273      26.175  92.950  14.705  1.00 40.61           C  
ATOM   1634  CD  LYS A 273      25.036  93.490  13.858  1.00 40.70           C  
ATOM   1635  CE  LYS A 273      24.774  94.959  14.142  1.00 41.02           C  
ATOM   1636  NZ  LYS A 273      23.784  95.547  13.191  1.00 41.31           N  
ATOM   1637  N   GLU A 274      27.679  91.859  18.117  1.00 42.40           N  
ATOM   1638  CA  GLU A 274      28.699  92.534  18.927  1.00 43.20           C  
ATOM   1639  C   GLU A 274      29.904  91.645  19.194  1.00 43.63           C  
ATOM   1640  O   GLU A 274      31.035  92.134  19.243  1.00 43.84           O  
ATOM   1641  CB  GLU A 274      28.121  93.024  20.256  1.00 43.28           C  
ATOM   1642  CG  GLU A 274      28.972  94.082  20.948  1.00 43.84           C  
ATOM   1643  CD  GLU A 274      28.534  94.356  22.378  1.00 45.18           C  
ATOM   1644  OE1 GLU A 274      27.346  94.121  22.709  1.00 45.28           O  
ATOM   1645  OE2 GLU A 274      29.384  94.816  23.176  1.00 45.81           O  
ATOM   1646  N   LEU A 275      29.654  90.348  19.370  1.00 44.09           N  
ATOM   1647  CA  LEU A 275      30.718  89.371  19.599  1.00 44.47           C  
ATOM   1648  C   LEU A 275      31.626  89.230  18.373  1.00 45.03           C  
ATOM   1649  O   LEU A 275      32.825  88.974  18.504  1.00 44.99           O  
ATOM   1650  CB  LEU A 275      30.130  88.017  19.998  1.00 44.27           C  
ATOM   1651  CG  LEU A 275      29.413  87.919  21.347  1.00 43.61           C  
ATOM   1652  CD1 LEU A 275      28.350  86.832  21.304  1.00 42.69           C  
ATOM   1653  CD2 LEU A 275      30.407  87.657  22.463  1.00 42.98           C  
ATOM   1654  N   GLU A 276      31.047  89.409  17.186  1.00 45.77           N  
ATOM   1655  CA  GLU A 276      31.810  89.422  15.941  1.00 46.53           C  
ATOM   1656  C   GLU A 276      32.777  90.610  15.888  1.00 46.85           C  
ATOM   1657  O   GLU A 276      33.805  90.552  15.219  1.00 46.95           O  
ATOM   1658  CB  GLU A 276      30.869  89.426  14.729  1.00 46.57           C  
ATOM   1659  CG  GLU A 276      31.481  88.837  13.465  1.00 47.40           C  
ATOM   1660  CD  GLU A 276      30.458  88.578  12.374  1.00 48.66           C  
ATOM   1661  OE1 GLU A 276      29.984  87.426  12.253  1.00 48.93           O  
ATOM   1662  OE2 GLU A 276      30.130  89.527  11.629  1.00 49.39           O  
ATOM   1663  N   ALA A 277      32.446  91.682  16.600  1.00 47.38           N  
ATOM   1664  CA  ALA A 277      33.310  92.857  16.655  1.00 47.98           C  
ATOM   1665  C   ALA A 277      34.389  92.730  17.728  1.00 48.46           C  
ATOM   1666  O   ALA A 277      35.332  93.524  17.758  1.00 48.57           O  
ATOM   1667  CB  ALA A 277      32.486  94.114  16.872  1.00 47.99           C  
ATOM   1668  N   ILE A 278      34.248  91.733  18.602  1.00 49.03           N  
ATOM   1669  CA  ILE A 278      35.200  91.518  19.693  1.00 49.49           C  
ATOM   1670  C   ILE A 278      36.328  90.564  19.292  1.00 49.93           C  
ATOM   1671  O   ILE A 278      37.502  90.889  19.468  1.00 50.01           O  
ATOM   1672  CB  ILE A 278      34.480  91.049  20.979  1.00 49.41           C  
ATOM   1673  CG1 ILE A 278      33.403  92.061  21.378  1.00 49.19           C  
ATOM   1674  CG2 ILE A 278      35.477  90.891  22.121  1.00 49.58           C  
ATOM   1675  CD1 ILE A 278      32.374  91.529  22.354  1.00 49.58           C  
ATOM   1676  N   PHE A 279      35.966  89.393  18.769  1.00 50.53           N  
ATOM   1677  CA  PHE A 279      36.927  88.457  18.178  1.00 51.19           C  
ATOM   1678  C   PHE A 279      36.299  87.752  16.975  1.00 52.07           C  
ATOM   1679  O   PHE A 279      36.026  86.548  17.021  1.00 52.20           O  
ATOM   1680  CB  PHE A 279      37.452  87.417  19.191  1.00 50.98           C  
ATOM   1681  CG  PHE A 279      36.731  87.401  20.524  1.00 50.26           C  
ATOM   1682  CD1 PHE A 279      35.344  87.307  20.600  1.00 49.46           C  
ATOM   1683  CD2 PHE A 279      37.458  87.439  21.710  1.00 49.29           C  
ATOM   1684  CE1 PHE A 279      34.700  87.285  21.832  1.00 48.79           C  
ATOM   1685  CE2 PHE A 279      36.823  87.415  22.940  1.00 48.65           C  
ATOM   1686  CZ  PHE A 279      35.442  87.337  23.002  1.00 48.65           C  
ATOM   1687  N   GLY A 280      36.076  88.508  15.900  1.00 52.96           N  
ATOM   1688  CA  GLY A 280      35.347  88.012  14.741  1.00 54.04           C  
ATOM   1689  C   GLY A 280      36.133  87.068  13.850  1.00 54.83           C  
ATOM   1690  O   GLY A 280      37.298  87.335  13.550  1.00 54.94           O  
ATOM   1691  N   ARG A 281      35.492  85.992  13.384  1.00 55.57           N  
ATOM   1692  CA  ARG A 281      34.042  85.804  13.532  1.00 56.39           C  
ATOM   1693  C   ARG A 281      33.533  84.542  14.287  1.00 56.85           C  
ATOM   1694  O   ARG A 281      32.323  84.270  14.246  1.00 56.77           O  
ATOM   1695  CB  ARG A 281      33.350  85.955  12.156  1.00 56.47           C  
ATOM   1696  CG  ARG A 281      33.143  84.663  11.350  1.00 57.12           C  
ATOM   1697  CD  ARG A 281      34.329  84.238  10.490  1.00 57.93           C  
ATOM   1698  NE  ARG A 281      34.780  82.889  10.833  1.00 58.50           N  
ATOM   1699  CZ  ARG A 281      36.046  82.548  11.070  1.00 59.07           C  
ATOM   1700  NH1 ARG A 281      37.022  83.453  10.998  1.00 58.97           N  
ATOM   1701  NH2 ARG A 281      36.340  81.289  11.378  1.00 59.02           N  
ATOM   1702  N   PRO A 282      34.409  83.781  14.969  1.00 57.37           N  
ATOM   1703  CA  PRO A 282      33.942  82.673  15.828  1.00 57.61           C  
ATOM   1704  C   PRO A 282      32.924  83.167  16.870  1.00 57.84           C  
ATOM   1705  O   PRO A 282      33.306  83.771  17.879  1.00 57.99           O  
ATOM   1706  CB  PRO A 282      35.230  82.179  16.514  1.00 57.55           C  
ATOM   1707  CG  PRO A 282      36.345  82.610  15.622  1.00 57.47           C  
ATOM   1708  CD  PRO A 282      35.885  83.885  14.976  1.00 57.34           C  
ATOM   1709  N   VAL A 283      31.640  82.924  16.612  1.00 58.01           N  
ATOM   1710  CA  VAL A 283      30.572  83.537  17.402  1.00 58.17           C  
ATOM   1711  C   VAL A 283      29.365  82.621  17.596  1.00 58.33           C  
ATOM   1712  O   VAL A 283      28.721  82.203  16.629  1.00 58.34           O  
ATOM   1713  CB  VAL A 283      30.119  84.887  16.769  1.00 58.17           C  
ATOM   1714  CG1 VAL A 283      28.742  85.310  17.261  1.00 58.17           C  
ATOM   1715  CG2 VAL A 283      31.135  85.979  17.048  1.00 58.23           C  
ATOM   1716  N   VAL A 284      29.089  82.301  18.858  1.00 58.61           N  
ATOM   1717  CA  VAL A 284      27.831  81.669  19.275  1.00 59.00           C  
ATOM   1718  C   VAL A 284      27.592  81.909  20.780  1.00 59.20           C  
ATOM   1719  O   VAL A 284      27.849  83.011  21.280  1.00 59.22           O  
ATOM   1720  CB  VAL A 284      27.721  80.146  18.891  1.00 59.05           C  
ATOM   1721  CG1 VAL A 284      26.773  79.957  17.720  1.00 58.80           C  
ATOM   1722  CG2 VAL A 284      29.085  79.523  18.587  1.00 59.17           C  
ATOM   1723  N   ASP A 285      27.103  80.896  21.495  1.00 59.39           N  
ATOM   1724  CA  ASP A 285      26.797  81.037  22.921  1.00 59.47           C  
ATOM   1725  C   ASP A 285      27.740  80.217  23.807  1.00 59.39           C  
ATOM   1726  O   ASP A 285      27.307  79.398  24.623  1.00 59.27           O  
ATOM   1727  CB  ASP A 285      25.329  80.679  23.194  1.00 59.58           C  
ATOM   1728  CG  ASP A 285      24.357  81.648  22.537  1.00 59.76           C  
ATOM   1729  OD1 ASP A 285      24.304  82.823  22.962  1.00 59.89           O  
ATOM   1730  OD2 ASP A 285      23.611  81.320  21.589  1.00 60.07           O  
ATOM   1731  N   ARG A 313      25.800 100.324  22.314  1.00 43.49           N  
ATOM   1732  CA  ARG A 313      24.481 100.949  22.415  1.00 43.41           C  
ATOM   1733  C   ARG A 313      24.232 101.551  23.836  1.00 43.59           C  
ATOM   1734  O   ARG A 313      25.156 102.169  24.378  1.00 43.75           O  
ATOM   1735  CB  ARG A 313      23.388  99.982  21.910  1.00 43.31           C  
ATOM   1736  CG  ARG A 313      22.881 100.298  20.483  1.00 42.26           C  
ATOM   1737  CD  ARG A 313      23.079  99.160  19.474  1.00 40.34           C  
ATOM   1738  NE  ARG A 313      22.012  99.105  18.465  1.00 39.10           N  
ATOM   1739  CZ  ARG A 313      22.055  99.694  17.262  1.00 38.21           C  
ATOM   1740  NH1 ARG A 313      23.119 100.411  16.885  1.00 36.99           N  
ATOM   1741  NH2 ARG A 313      21.022  99.565  16.429  1.00 37.06           N  
ATOM   1742  N   PRO A 314      23.042 101.409  24.445  1.00 43.61           N  
ATOM   1743  CA  PRO A 314      22.786 102.034  25.758  1.00 43.55           C  
ATOM   1744  C   PRO A 314      23.194 101.194  26.990  1.00 43.38           C  
ATOM   1745  O   PRO A 314      23.460  99.990  26.873  1.00 43.52           O  
ATOM   1746  CB  PRO A 314      21.264 102.263  25.746  1.00 43.63           C  
ATOM   1747  CG  PRO A 314      20.742 101.550  24.494  1.00 43.69           C  
ATOM   1748  CD  PRO A 314      21.848 100.685  23.970  1.00 43.63           C  
ATOM   1749  N   ALA A 315      23.237 101.832  28.160  1.00 42.90           N  
ATOM   1750  CA  ALA A 315      23.653 101.157  29.389  1.00 42.47           C  
ATOM   1751  C   ALA A 315      22.524 101.113  30.414  1.00 42.08           C  
ATOM   1752  O   ALA A 315      22.053 102.160  30.869  1.00 42.34           O  
ATOM   1753  CB  ALA A 315      24.890 101.830  29.978  1.00 42.52           C  
ATOM   1754  N   MET A 316      22.121  99.892  30.776  1.00 41.31           N  
ATOM   1755  CA  MET A 316      20.965  99.607  31.643  1.00 40.45           C  
ATOM   1756  C   MET A 316      20.798 100.528  32.850  1.00 39.86           C  
ATOM   1757  O   MET A 316      21.781 100.913  33.492  1.00 39.88           O  
ATOM   1758  CB  MET A 316      21.033  98.156  32.138  1.00 40.48           C  
ATOM   1759  CG  MET A 316      20.563  97.107  31.138  1.00 40.40           C  
ATOM   1760  SD  MET A 316      20.001  95.600  31.959  1.00 40.52           S  
ATOM   1761  CE  MET A 316      19.011  94.855  30.674  1.00 41.02           C  
ATOM   1762  N   ALA A 317      19.549 100.847  33.183  1.00 39.15           N  
ATOM   1763  CA  ALA A 317      19.238 101.615  34.392  1.00 38.48           C  
ATOM   1764  C   ALA A 317      19.402 100.760  35.654  1.00 37.96           C  
ATOM   1765  O   ALA A 317      19.516  99.534  35.573  1.00 37.92           O  
ATOM   1766  CB  ALA A 317      17.838 102.192  34.312  1.00 38.54           C  
ATOM   1767  N   ILE A 318      19.401 101.412  36.814  1.00 37.20           N  
ATOM   1768  CA  ILE A 318      19.752 100.756  38.076  1.00 36.43           C  
ATOM   1769  C   ILE A 318      18.913  99.519  38.369  1.00 35.81           C  
ATOM   1770  O   ILE A 318      19.461  98.425  38.514  1.00 35.64           O  
ATOM   1771  CB  ILE A 318      19.714 101.745  39.267  1.00 36.53           C  
ATOM   1772  CG1 ILE A 318      20.429 103.060  38.914  1.00 36.85           C  
ATOM   1773  CG2 ILE A 318      20.372 101.114  40.491  1.00 36.24           C  
ATOM   1774  CD1 ILE A 318      19.508 104.187  38.449  1.00 36.98           C  
ATOM   1775  N   PHE A 319      17.594  99.689  38.450  1.00 35.12           N  
ATOM   1776  CA  PHE A 319      16.699  98.556  38.704  1.00 34.41           C  
ATOM   1777  C   PHE A 319      16.797  97.526  37.577  1.00 34.08           C  
ATOM   1778  O   PHE A 319      17.100  96.357  37.819  1.00 33.97           O  
ATOM   1779  CB  PHE A 319      15.251  99.019  38.922  1.00 34.21           C  
ATOM   1780  CG  PHE A 319      14.327  97.930  39.390  1.00 33.24           C  
ATOM   1781  CD1 PHE A 319      14.490  97.347  40.643  1.00 32.55           C  
ATOM   1782  CD2 PHE A 319      13.293  97.486  38.576  1.00 32.43           C  
ATOM   1783  CE1 PHE A 319      13.641  96.335  41.076  1.00 32.29           C  
ATOM   1784  CE2 PHE A 319      12.435  96.477  39.000  1.00 32.24           C  
ATOM   1785  CZ  PHE A 319      12.609  95.898  40.251  1.00 32.20           C  
ATOM   1786  N   GLU A 320      16.570  97.986  36.351  1.00 33.62           N  
ATOM   1787  CA  GLU A 320      16.755  97.188  35.144  1.00 33.37           C  
ATOM   1788  C   GLU A 320      17.924  96.208  35.243  1.00 32.79           C  
ATOM   1789  O   GLU A 320      17.809  95.053  34.838  1.00 32.76           O  
ATOM   1790  CB  GLU A 320      16.973  98.127  33.958  1.00 33.58           C  
ATOM   1791  CG  GLU A 320      16.488  97.600  32.617  1.00 34.63           C  
ATOM   1792  CD  GLU A 320      17.148  98.311  31.450  1.00 36.22           C  
ATOM   1793  OE1 GLU A 320      17.416  97.647  30.424  1.00 37.29           O  
ATOM   1794  OE2 GLU A 320      17.404  99.534  31.554  1.00 36.67           O  
ATOM   1795  N   LEU A 321      19.040  96.682  35.789  1.00 32.23           N  
ATOM   1796  CA  LEU A 321      20.269  95.906  35.883  1.00 31.65           C  
ATOM   1797  C   LEU A 321      20.130  94.766  36.867  1.00 31.26           C  
ATOM   1798  O   LEU A 321      20.301  93.607  36.508  1.00 31.07           O  
ATOM   1799  CB  LEU A 321      21.423  96.812  36.318  1.00 31.75           C  
ATOM   1800  CG  LEU A 321      22.878  96.521  35.934  1.00 31.66           C  
ATOM   1801  CD1 LEU A 321      23.457  95.358  36.722  1.00 30.89           C  
ATOM   1802  CD2 LEU A 321      23.023  96.304  34.430  1.00 32.17           C  
ATOM   1803  N   LEU A 322      19.828  95.110  38.112  1.00 31.02           N  
ATOM   1804  CA  LEU A 322      19.721  94.134  39.189  1.00 30.73           C  
ATOM   1805  C   LEU A 322      18.624  93.118  38.887  1.00 30.69           C  
ATOM   1806  O   LEU A 322      18.829  91.918  39.041  1.00 30.69           O  
ATOM   1807  CB  LEU A 322      19.456  94.841  40.520  1.00 30.59           C  
ATOM   1808  CG  LEU A 322      20.636  95.328  41.374  1.00 30.35           C  
ATOM   1809  CD1 LEU A 322      21.767  95.972  40.574  1.00 29.46           C  
ATOM   1810  CD2 LEU A 322      20.129  96.291  42.426  1.00 30.02           C  
ATOM   1811  N   ASP A 323      17.472  93.613  38.430  1.00 30.67           N  
ATOM   1812  CA  ASP A 323      16.329  92.776  38.070  1.00 30.48           C  
ATOM   1813  C   ASP A 323      16.707  91.810  36.960  1.00 30.10           C  
ATOM   1814  O   ASP A 323      16.104  90.746  36.820  1.00 30.14           O  
ATOM   1815  CB  ASP A 323      15.143  93.648  37.638  1.00 30.78           C  
ATOM   1816  CG  ASP A 323      13.860  92.848  37.438  1.00 31.77           C  
ATOM   1817  OD1 ASP A 323      13.319  92.298  38.426  1.00 32.98           O  
ATOM   1818  OD2 ASP A 323      13.314  92.722  36.322  1.00 32.89           O  
ATOM   1819  N   TYR A 324      17.708  92.191  36.173  1.00 29.64           N  
ATOM   1820  CA  TYR A 324      18.251  91.305  35.164  1.00 29.20           C  
ATOM   1821  C   TYR A 324      19.099  90.232  35.843  1.00 28.73           C  
ATOM   1822  O   TYR A 324      18.851  89.041  35.660  1.00 28.55           O  
ATOM   1823  CB  TYR A 324      19.059  92.084  34.121  1.00 29.40           C  
ATOM   1824  CG  TYR A 324      19.327  91.282  32.875  1.00 30.22           C  
ATOM   1825  CD1 TYR A 324      18.516  91.414  31.753  1.00 31.07           C  
ATOM   1826  CD2 TYR A 324      20.380  90.369  32.826  1.00 30.74           C  
ATOM   1827  CE1 TYR A 324      18.749  90.662  30.612  1.00 31.30           C  
ATOM   1828  CE2 TYR A 324      20.619  89.617  31.695  1.00 30.95           C  
ATOM   1829  CZ  TYR A 324      19.804  89.768  30.595  1.00 31.30           C  
ATOM   1830  OH  TYR A 324      20.048  89.018  29.475  1.00 32.87           O  
ATOM   1831  N   ILE A 325      20.074  90.666  36.644  1.00 28.26           N  
ATOM   1832  CA  ILE A 325      20.974  89.764  37.370  1.00 27.73           C  
ATOM   1833  C   ILE A 325      20.215  88.688  38.138  1.00 27.66           C  
ATOM   1834  O   ILE A 325      20.603  87.525  38.116  1.00 27.85           O  
ATOM   1835  CB  ILE A 325      21.902  90.549  38.323  1.00 27.55           C  
ATOM   1836  CG1 ILE A 325      22.887  91.409  37.532  1.00 27.18           C  
ATOM   1837  CG2 ILE A 325      22.663  89.604  39.240  1.00 27.63           C  
ATOM   1838  CD1 ILE A 325      23.713  92.330  38.393  1.00 26.79           C  
ATOM   1839  N   VAL A 326      19.132  89.071  38.807  1.00 27.58           N  
ATOM   1840  CA  VAL A 326      18.310  88.100  39.524  1.00 27.49           C  
ATOM   1841  C   VAL A 326      17.549  87.200  38.550  1.00 27.57           C  
ATOM   1842  O   VAL A 326      17.885  86.026  38.400  1.00 27.50           O  
ATOM   1843  CB  VAL A 326      17.308  88.761  40.515  1.00 27.34           C  
ATOM   1844  CG1 VAL A 326      16.657  87.705  41.393  1.00 27.10           C  
ATOM   1845  CG2 VAL A 326      17.991  89.787  41.382  1.00 27.23           C  
ATOM   1846  N   ASN A 327      16.551  87.766  37.876  1.00 27.66           N  
ATOM   1847  CA  ASN A 327      15.548  86.981  37.158  1.00 27.83           C  
ATOM   1848  C   ASN A 327      15.999  86.339  35.849  1.00 28.02           C  
ATOM   1849  O   ASN A 327      15.510  85.268  35.488  1.00 28.16           O  
ATOM   1850  CB  ASN A 327      14.283  87.808  36.931  1.00 27.84           C  
ATOM   1851  CG  ASN A 327      13.728  88.398  38.223  1.00 28.07           C  
ATOM   1852  OD1 ASN A 327      13.420  89.591  38.289  1.00 27.99           O  
ATOM   1853  ND2 ASN A 327      13.595  87.564  39.252  1.00 27.68           N  
ATOM   1854  N   GLU A 328      16.926  86.989  35.146  1.00 28.20           N  
ATOM   1855  CA  GLU A 328      17.403  86.503  33.847  1.00 28.11           C  
ATOM   1856  C   GLU A 328      18.596  85.561  33.992  1.00 28.03           C  
ATOM   1857  O   GLU A 328      19.328  85.644  34.978  1.00 28.05           O  
ATOM   1858  CB  GLU A 328      17.756  87.670  32.918  1.00 28.02           C  
ATOM   1859  CG  GLU A 328      16.584  88.547  32.507  1.00 28.71           C  
ATOM   1860  CD  GLU A 328      15.348  87.770  32.078  1.00 30.15           C  
ATOM   1861  OE1 GLU A 328      15.472  86.769  31.335  1.00 30.85           O  
ATOM   1862  OE2 GLU A 328      14.236  88.174  32.481  1.00 30.93           O  
ATOM   1863  N   PRO A 329      18.783  84.664  33.019  1.00 28.03           N  
ATOM   1864  CA  PRO A 329      19.904  83.715  33.027  1.00 27.90           C  
ATOM   1865  C   PRO A 329      21.283  84.374  33.138  1.00 27.71           C  
ATOM   1866  O   PRO A 329      21.461  85.475  32.614  1.00 27.65           O  
ATOM   1867  CB  PRO A 329      19.762  82.994  31.678  1.00 27.95           C  
ATOM   1868  CG  PRO A 329      18.866  83.848  30.867  1.00 28.08           C  
ATOM   1869  CD  PRO A 329      17.918  84.462  31.842  1.00 28.19           C  
ATOM   1870  N   PRO A 330      22.230  83.708  33.809  1.00 27.63           N  
ATOM   1871  CA  PRO A 330      23.588  84.236  33.995  1.00 27.53           C  
ATOM   1872  C   PRO A 330      24.364  84.342  32.691  1.00 27.48           C  
ATOM   1873  O   PRO A 330      24.077  83.596  31.754  1.00 27.48           O  
ATOM   1874  CB  PRO A 330      24.247  83.182  34.889  1.00 27.46           C  
ATOM   1875  CG  PRO A 330      23.484  81.942  34.635  1.00 27.45           C  
ATOM   1876  CD  PRO A 330      22.072  82.389  34.451  1.00 27.67           C  
ATOM   1877  N   PRO A 331      25.345  85.236  32.641  1.00 27.53           N  
ATOM   1878  CA  PRO A 331      26.172  85.405  31.441  1.00 27.68           C  
ATOM   1879  C   PRO A 331      27.053  84.186  31.213  1.00 27.87           C  
ATOM   1880  O   PRO A 331      27.312  83.417  32.145  1.00 27.91           O  
ATOM   1881  CB  PRO A 331      27.034  86.622  31.779  1.00 27.76           C  
ATOM   1882  CG  PRO A 331      27.096  86.630  33.269  1.00 27.58           C  
ATOM   1883  CD  PRO A 331      25.758  86.140  33.730  1.00 27.49           C  
ATOM   1884  N   LYS A 332      27.505  84.016  29.978  1.00 28.08           N  
ATOM   1885  CA  LYS A 332      28.291  82.854  29.600  1.00 28.34           C  
ATOM   1886  C   LYS A 332      29.464  83.257  28.723  1.00 28.39           C  
ATOM   1887  O   LYS A 332      29.459  84.322  28.106  1.00 28.49           O  
ATOM   1888  CB  LYS A 332      27.408  81.833  28.876  1.00 28.35           C  
ATOM   1889  CG  LYS A 332      26.622  80.935  29.819  1.00 29.39           C  
ATOM   1890  CD  LYS A 332      25.544  80.150  29.092  1.00 31.21           C  
ATOM   1891  CE  LYS A 332      25.389  78.744  29.676  1.00 32.18           C  
ATOM   1892  NZ  LYS A 332      25.933  77.682  28.765  1.00 32.81           N  
ATOM   1893  N   LEU A 333      30.479  82.406  28.685  1.00 28.57           N  
ATOM   1894  CA  LEU A 333      31.571  82.581  27.748  1.00 28.67           C  
ATOM   1895  C   LEU A 333      31.113  82.153  26.349  1.00 29.00           C  
ATOM   1896  O   LEU A 333      30.445  81.123  26.201  1.00 28.83           O  
ATOM   1897  CB  LEU A 333      32.791  81.776  28.203  1.00 28.51           C  
ATOM   1898  CG  LEU A 333      34.036  82.575  28.602  1.00 27.94           C  
ATOM   1899  CD1 LEU A 333      33.679  83.936  29.183  1.00 27.42           C  
ATOM   1900  CD2 LEU A 333      34.892  81.792  29.577  1.00 27.23           C  
ATOM   1901  N   PRO A 334      31.442  82.955  25.335  1.00 29.39           N  
ATOM   1902  CA  PRO A 334      31.160  82.600  23.939  1.00 29.72           C  
ATOM   1903  C   PRO A 334      31.862  81.307  23.525  1.00 30.10           C  
ATOM   1904  O   PRO A 334      32.946  80.997  24.036  1.00 30.30           O  
ATOM   1905  CB  PRO A 334      31.736  83.783  23.152  1.00 29.66           C  
ATOM   1906  CG  PRO A 334      32.696  84.421  24.069  1.00 29.43           C  
ATOM   1907  CD  PRO A 334      32.097  84.271  25.436  1.00 29.49           C  
ATOM   1908  N   ASN A 335      31.245  80.569  22.608  1.00 30.29           N  
ATOM   1909  CA  ASN A 335      31.786  79.297  22.154  1.00 30.51           C  
ATOM   1910  C   ASN A 335      32.952  79.436  21.165  1.00 30.36           C  
ATOM   1911  O   ASN A 335      33.153  80.499  20.560  1.00 30.40           O  
ATOM   1912  CB  ASN A 335      30.670  78.457  21.535  1.00 30.81           C  
ATOM   1913  CG  ASN A 335      30.388  77.187  22.318  1.00 31.96           C  
ATOM   1914  OD1 ASN A 335      29.234  76.897  22.666  1.00 32.60           O  
ATOM   1915  ND2 ASN A 335      31.442  76.412  22.594  1.00 33.25           N  
ATOM   1916  N   GLY A 336      33.721  78.356  21.020  1.00 30.07           N  
ATOM   1917  CA  GLY A 336      34.767  78.254  20.014  1.00 29.61           C  
ATOM   1918  C   GLY A 336      35.891  79.276  20.089  1.00 29.32           C  
ATOM   1919  O   GLY A 336      36.697  79.382  19.158  1.00 29.54           O  
ATOM   1920  N   VAL A 337      35.949  80.030  21.183  1.00 28.71           N  
ATOM   1921  CA  VAL A 337      37.026  80.994  21.379  1.00 28.15           C  
ATOM   1922  C   VAL A 337      37.883  80.650  22.607  1.00 27.75           C  
ATOM   1923  O   VAL A 337      39.109  80.591  22.509  1.00 27.89           O  
ATOM   1924  CB  VAL A 337      36.511  82.471  21.354  1.00 28.17           C  
ATOM   1925  CG1 VAL A 337      35.104  82.580  21.917  1.00 28.27           C  
ATOM   1926  CG2 VAL A 337      37.474  83.424  22.064  1.00 28.22           C  
ATOM   1927  N   PHE A 338      37.243  80.400  23.746  1.00 27.16           N  
ATOM   1928  CA  PHE A 338      37.955  79.945  24.941  1.00 26.50           C  
ATOM   1929  C   PHE A 338      37.754  78.442  25.137  1.00 26.36           C  
ATOM   1930  O   PHE A 338      36.733  77.889  24.712  1.00 26.44           O  
ATOM   1931  CB  PHE A 338      37.488  80.707  26.181  1.00 26.31           C  
ATOM   1932  CG  PHE A 338      37.378  82.191  25.981  1.00 25.64           C  
ATOM   1933  CD1 PHE A 338      38.486  83.014  26.155  1.00 25.36           C  
ATOM   1934  CD2 PHE A 338      36.165  82.771  25.630  1.00 24.74           C  
ATOM   1935  CE1 PHE A 338      38.388  84.396  25.977  1.00 24.61           C  
ATOM   1936  CE2 PHE A 338      36.060  84.144  25.449  1.00 24.21           C  
ATOM   1937  CZ  PHE A 338      37.172  84.958  25.623  1.00 24.09           C  
ATOM   1938  N   THR A 339      38.723  77.792  25.785  1.00 26.05           N  
ATOM   1939  CA  THR A 339      38.699  76.341  26.010  1.00 25.81           C  
ATOM   1940  C   THR A 339      37.426  75.878  26.709  1.00 25.76           C  
ATOM   1941  O   THR A 339      36.916  76.588  27.574  1.00 25.87           O  
ATOM   1942  CB  THR A 339      39.911  75.892  26.849  1.00 25.80           C  
ATOM   1943  OG1 THR A 339      40.724  77.021  27.193  1.00 25.46           O  
ATOM   1944  CG2 THR A 339      40.833  75.018  26.024  1.00 25.82           C  
ATOM   1945  N   PRO A 340      36.913  74.698  26.345  1.00 25.68           N  
ATOM   1946  CA  PRO A 340      35.736  74.127  27.015  1.00 25.75           C  
ATOM   1947  C   PRO A 340      35.897  74.062  28.535  1.00 25.88           C  
ATOM   1948  O   PRO A 340      34.908  74.123  29.273  1.00 26.04           O  
ATOM   1949  CB  PRO A 340      35.652  72.715  26.429  1.00 25.57           C  
ATOM   1950  CG  PRO A 340      36.273  72.834  25.096  1.00 25.48           C  
ATOM   1951  CD  PRO A 340      37.390  73.827  25.256  1.00 25.69           C  
ATOM   1952  N   ASP A 341      37.139  73.957  28.991  1.00 25.88           N  
ATOM   1953  CA  ASP A 341      37.419  73.899  30.413  1.00 25.93           C  
ATOM   1954  C   ASP A 341      37.206  75.250  31.079  1.00 25.63           C  
ATOM   1955  O   ASP A 341      36.521  75.328  32.097  1.00 25.78           O  
ATOM   1956  CB  ASP A 341      38.825  73.351  30.659  1.00 26.33           C  
ATOM   1957  CG  ASP A 341      38.870  71.823  30.626  1.00 27.06           C  
ATOM   1958  OD1 ASP A 341      39.987  71.265  30.589  1.00 27.70           O  
ATOM   1959  OD2 ASP A 341      37.846  71.099  30.639  1.00 27.78           O  
ATOM   1960  N   PHE A 342      37.771  76.311  30.497  1.00 25.26           N  
ATOM   1961  CA  PHE A 342      37.522  77.683  30.958  1.00 24.69           C  
ATOM   1962  C   PHE A 342      36.028  77.961  30.989  1.00 24.47           C  
ATOM   1963  O   PHE A 342      35.520  78.570  31.932  1.00 24.43           O  
ATOM   1964  CB  PHE A 342      38.212  78.702  30.048  1.00 24.52           C  
ATOM   1965  CG  PHE A 342      38.317  80.090  30.639  1.00 24.31           C  
ATOM   1966  CD1 PHE A 342      38.251  80.301  32.009  1.00 23.93           C  
ATOM   1967  CD2 PHE A 342      38.496  81.193  29.811  1.00 24.38           C  
ATOM   1968  CE1 PHE A 342      38.361  81.585  32.543  1.00 23.61           C  
ATOM   1969  CE2 PHE A 342      38.606  82.480  30.341  1.00 23.84           C  
ATOM   1970  CZ  PHE A 342      38.539  82.671  31.708  1.00 23.33           C  
ATOM   1971  N   GLN A 343      35.335  77.492  29.955  1.00 24.22           N  
ATOM   1972  CA  GLN A 343      33.897  77.655  29.844  1.00 24.07           C  
ATOM   1973  C   GLN A 343      33.189  77.038  31.043  1.00 23.96           C  
ATOM   1974  O   GLN A 343      32.394  77.716  31.691  1.00 24.11           O  
ATOM   1975  CB  GLN A 343      33.380  77.073  28.526  1.00 24.06           C  
ATOM   1976  CG  GLN A 343      33.650  77.962  27.321  1.00 24.40           C  
ATOM   1977  CD  GLN A 343      33.067  77.414  26.027  1.00 25.42           C  
ATOM   1978  OE1 GLN A 343      33.809  76.966  25.145  1.00 25.75           O  
ATOM   1979  NE2 GLN A 343      31.740  77.463  25.901  1.00 25.25           N  
ATOM   1980  N   GLU A 344      33.500  75.779  31.357  1.00 23.75           N  
ATOM   1981  CA  GLU A 344      32.848  75.081  32.470  1.00 23.72           C  
ATOM   1982  C   GLU A 344      33.231  75.667  33.827  1.00 23.10           C  
ATOM   1983  O   GLU A 344      32.393  75.743  34.722  1.00 23.17           O  
ATOM   1984  CB  GLU A 344      33.112  73.566  32.423  1.00 24.14           C  
ATOM   1985  CG  GLU A 344      32.159  72.677  33.240  1.00 26.56           C  
ATOM   1986  CD  GLU A 344      30.682  73.126  33.236  1.00 30.30           C  
ATOM   1987  OE1 GLU A 344      30.138  73.419  34.338  1.00 30.73           O  
ATOM   1988  OE2 GLU A 344      30.046  73.171  32.144  1.00 31.47           O  
ATOM   1989  N   PHE A 345      34.481  76.104  33.964  1.00 22.45           N  
ATOM   1990  CA  PHE A 345      34.936  76.790  35.170  1.00 21.85           C  
ATOM   1991  C   PHE A 345      34.051  77.998  35.505  1.00 22.00           C  
ATOM   1992  O   PHE A 345      33.421  78.029  36.570  1.00 21.99           O  
ATOM   1993  CB  PHE A 345      36.399  77.217  35.027  1.00 21.55           C  
ATOM   1994  CG  PHE A 345      36.978  77.855  36.266  1.00 20.46           C  
ATOM   1995  CD1 PHE A 345      37.404  77.078  37.334  1.00 19.34           C  
ATOM   1996  CD2 PHE A 345      37.114  79.234  36.356  1.00 19.56           C  
ATOM   1997  CE1 PHE A 345      37.945  77.664  38.472  1.00 18.78           C  
ATOM   1998  CE2 PHE A 345      37.656  79.825  37.495  1.00 18.96           C  
ATOM   1999  CZ  PHE A 345      38.073  79.037  38.552  1.00 18.25           C  
ATOM   2000  N   VAL A 346      33.991  78.973  34.593  1.00 21.95           N  
ATOM   2001  CA  VAL A 346      33.219  80.205  34.825  1.00 21.90           C  
ATOM   2002  C   VAL A 346      31.715  79.957  34.978  1.00 21.67           C  
ATOM   2003  O   VAL A 346      31.018  80.715  35.654  1.00 21.72           O  
ATOM   2004  CB  VAL A 346      33.481  81.318  33.752  1.00 21.89           C  
ATOM   2005  CG1 VAL A 346      34.967  81.474  33.472  1.00 21.90           C  
ATOM   2006  CG2 VAL A 346      32.710  81.054  32.470  1.00 22.03           C  
ATOM   2007  N   ASN A 347      31.228  78.893  34.351  1.00 21.35           N  
ATOM   2008  CA  ASN A 347      29.824  78.543  34.430  1.00 21.16           C  
ATOM   2009  C   ASN A 347      29.475  77.979  35.792  1.00 21.13           C  
ATOM   2010  O   ASN A 347      28.398  78.253  36.331  1.00 21.11           O  
ATOM   2011  CB  ASN A 347      29.464  77.564  33.322  1.00 21.15           C  
ATOM   2012  CG  ASN A 347      29.191  78.257  32.009  1.00 20.84           C  
ATOM   2013  OD1 ASN A 347      29.794  79.281  31.695  1.00 20.77           O  
ATOM   2014  ND2 ASN A 347      28.273  77.706  31.234  1.00 21.20           N  
ATOM   2015  N   LYS A 348      30.399  77.203  36.350  1.00 21.10           N  
ATOM   2016  CA  LYS A 348      30.257  76.704  37.710  1.00 21.12           C  
ATOM   2017  C   LYS A 348      30.313  77.859  38.699  1.00 21.09           C  
ATOM   2018  O   LYS A 348      29.721  77.796  39.773  1.00 21.16           O  
ATOM   2019  CB  LYS A 348      31.325  75.663  38.025  1.00 21.11           C  
ATOM   2020  CG  LYS A 348      30.771  74.251  38.128  1.00 21.42           C  
ATOM   2021  CD  LYS A 348      31.800  73.219  37.692  1.00 22.28           C  
ATOM   2022  CE  LYS A 348      31.321  71.801  37.969  1.00 23.42           C  
ATOM   2023  NZ  LYS A 348      30.192  71.393  37.084  1.00 24.27           N  
ATOM   2024  N   CYS A 349      31.010  78.922  38.312  1.00 21.03           N  
ATOM   2025  CA  CYS A 349      31.074  80.138  39.107  1.00 20.97           C  
ATOM   2026  C   CYS A 349      29.788  80.947  39.042  1.00 21.06           C  
ATOM   2027  O   CYS A 349      29.461  81.672  39.981  1.00 21.18           O  
ATOM   2028  CB  CYS A 349      32.221  81.010  38.628  1.00 20.85           C  
ATOM   2029  SG  CYS A 349      33.800  80.478  39.275  1.00 20.99           S  
ATOM   2030  N   LEU A 350      29.072  80.843  37.927  1.00 20.98           N  
ATOM   2031  CA  LEU A 350      27.915  81.693  37.705  1.00 20.84           C  
ATOM   2032  C   LEU A 350      26.600  80.921  37.723  1.00 21.20           C  
ATOM   2033  O   LEU A 350      25.707  81.194  36.925  1.00 21.82           O  
ATOM   2034  CB  LEU A 350      28.065  82.475  36.396  1.00 20.38           C  
ATOM   2035  CG  LEU A 350      29.099  83.593  36.363  1.00 19.89           C  
ATOM   2036  CD1 LEU A 350      29.398  83.961  34.933  1.00 19.67           C  
ATOM   2037  CD2 LEU A 350      28.624  84.809  37.135  1.00 19.93           C  
ATOM   2038  N   ILE A 351      26.467  79.957  38.624  1.00 21.14           N  
ATOM   2039  CA  ILE A 351      25.187  79.284  38.770  1.00 21.27           C  
ATOM   2040  C   ILE A 351      24.360  80.132  39.717  1.00 21.58           C  
ATOM   2041  O   ILE A 351      24.823  80.465  40.803  1.00 21.79           O  
ATOM   2042  CB  ILE A 351      25.369  77.842  39.281  1.00 21.20           C  
ATOM   2043  CG1 ILE A 351      25.872  76.948  38.148  1.00 21.16           C  
ATOM   2044  CG2 ILE A 351      24.070  77.279  39.835  1.00 20.97           C  
ATOM   2045  CD1 ILE A 351      26.994  76.034  38.551  1.00 21.01           C  
ATOM   2046  N   LYS A 352      23.149  80.497  39.293  1.00 21.90           N  
ATOM   2047  CA  LYS A 352      22.288  81.390  40.070  1.00 22.11           C  
ATOM   2048  C   LYS A 352      21.950  80.834  41.456  1.00 22.21           C  
ATOM   2049  O   LYS A 352      21.931  81.578  42.440  1.00 22.39           O  
ATOM   2050  CB  LYS A 352      21.016  81.738  39.295  1.00 22.15           C  
ATOM   2051  CG  LYS A 352      21.250  82.661  38.099  1.00 22.62           C  
ATOM   2052  CD  LYS A 352      20.143  83.698  37.953  1.00 22.94           C  
ATOM   2053  CE  LYS A 352      19.001  83.184  37.091  1.00 23.24           C  
ATOM   2054  NZ  LYS A 352      17.685  83.298  37.780  1.00 23.15           N  
ATOM   2055  N   ASN A 353      21.693  79.531  41.528  1.00 22.19           N  
ATOM   2056  CA  ASN A 353      21.515  78.848  42.806  1.00 22.32           C  
ATOM   2057  C   ASN A 353      22.857  78.769  43.544  1.00 22.61           C  
ATOM   2058  O   ASN A 353      23.775  78.073  43.089  1.00 22.76           O  
ATOM   2059  CB  ASN A 353      20.925  77.453  42.569  1.00 22.18           C  
ATOM   2060  CG  ASN A 353      20.691  76.667  43.855  1.00 22.17           C  
ATOM   2061  OD1 ASN A 353      20.371  75.477  43.801  1.00 22.48           O  
ATOM   2062  ND2 ASN A 353      20.837  77.318  45.008  1.00 21.79           N  
ATOM   2063  N   PRO A 354      22.976  79.482  44.669  1.00 22.71           N  
ATOM   2064  CA  PRO A 354      24.241  79.560  45.411  1.00 22.89           C  
ATOM   2065  C   PRO A 354      24.660  78.215  45.986  1.00 23.22           C  
ATOM   2066  O   PRO A 354      25.855  77.963  46.144  1.00 23.34           O  
ATOM   2067  CB  PRO A 354      23.915  80.533  46.542  1.00 22.75           C  
ATOM   2068  CG  PRO A 354      22.460  80.424  46.706  1.00 22.66           C  
ATOM   2069  CD  PRO A 354      21.919  80.265  45.327  1.00 22.64           C  
ATOM   2070  N   ALA A 355      23.677  77.369  46.287  1.00 23.49           N  
ATOM   2071  CA  ALA A 355      23.924  76.047  46.844  1.00 23.71           C  
ATOM   2072  C   ALA A 355      24.402  75.075  45.776  1.00 23.89           C  
ATOM   2073  O   ALA A 355      25.025  74.063  46.087  1.00 24.07           O  
ATOM   2074  CB  ALA A 355      22.673  75.527  47.495  1.00 23.78           C  
ATOM   2075  N   GLU A 356      24.097  75.391  44.520  1.00 24.16           N  
ATOM   2076  CA  GLU A 356      24.470  74.564  43.369  1.00 24.28           C  
ATOM   2077  C   GLU A 356      25.760  75.074  42.726  1.00 24.01           C  
ATOM   2078  O   GLU A 356      26.438  74.347  41.993  1.00 23.89           O  
ATOM   2079  CB  GLU A 356      23.346  74.570  42.339  1.00 24.34           C  
ATOM   2080  CG  GLU A 356      22.621  73.254  42.174  1.00 25.16           C  
ATOM   2081  CD  GLU A 356      22.093  73.092  40.763  1.00 27.45           C  
ATOM   2082  OE1 GLU A 356      22.700  72.318  39.992  1.00 28.96           O  
ATOM   2083  OE2 GLU A 356      21.085  73.749  40.415  1.00 28.07           O  
ATOM   2084  N   ARG A 357      26.074  76.336  43.002  1.00 23.67           N  
ATOM   2085  CA  ARG A 357      27.317  76.954  42.577  1.00 23.43           C  
ATOM   2086  C   ARG A 357      28.510  76.166  43.091  1.00 23.39           C  
ATOM   2087  O   ARG A 357      28.454  75.578  44.172  1.00 23.47           O  
ATOM   2088  CB  ARG A 357      27.383  78.372  43.130  1.00 23.37           C  
ATOM   2089  CG  ARG A 357      28.371  79.276  42.442  1.00 23.26           C  
ATOM   2090  CD  ARG A 357      27.814  80.650  42.161  1.00 24.54           C  
ATOM   2091  NE  ARG A 357      27.411  81.347  43.382  1.00 25.11           N  
ATOM   2092  CZ  ARG A 357      26.263  82.001  43.547  1.00 25.09           C  
ATOM   2093  NH1 ARG A 357      25.362  82.069  42.574  1.00 24.11           N  
ATOM   2094  NH2 ARG A 357      26.016  82.597  44.704  1.00 25.70           N  
ATOM   2095  N   ALA A 358      29.584  76.162  42.308  1.00 23.30           N  
ATOM   2096  CA  ALA A 358      30.854  75.585  42.717  1.00 23.22           C  
ATOM   2097  C   ALA A 358      31.350  76.260  43.982  1.00 23.43           C  
ATOM   2098  O   ALA A 358      31.160  77.458  44.169  1.00 23.42           O  
ATOM   2099  CB  ALA A 358      31.869  75.755  41.622  1.00 23.08           C  
ATOM   2100  N   ASP A 359      31.973  75.481  44.857  1.00 23.73           N  
ATOM   2101  CA  ASP A 359      32.597  76.024  46.049  1.00 24.02           C  
ATOM   2102  C   ASP A 359      34.085  76.056  45.801  1.00 23.95           C  
ATOM   2103  O   ASP A 359      34.541  75.586  44.761  1.00 23.86           O  
ATOM   2104  CB  ASP A 359      32.274  75.166  47.268  1.00 24.33           C  
ATOM   2105  CG  ASP A 359      33.181  73.970  47.383  1.00 25.32           C  
ATOM   2106  OD1 ASP A 359      33.036  73.027  46.570  1.00 26.07           O  
ATOM   2107  OD2 ASP A 359      34.081  73.899  48.247  1.00 26.76           O  
ATOM   2108  N   LEU A 360      34.833  76.596  46.762  1.00 24.14           N  
ATOM   2109  CA  LEU A 360      36.275  76.804  46.628  1.00 24.23           C  
ATOM   2110  C   LEU A 360      37.056  75.539  46.268  1.00 24.31           C  
ATOM   2111  O   LEU A 360      38.035  75.606  45.524  1.00 24.04           O  
ATOM   2112  CB  LEU A 360      36.836  77.442  47.902  1.00 24.23           C  
ATOM   2113  CG  LEU A 360      37.372  78.879  47.839  1.00 24.16           C  
ATOM   2114  CD1 LEU A 360      36.641  79.730  46.815  1.00 24.07           C  
ATOM   2115  CD2 LEU A 360      37.289  79.534  49.207  1.00 24.28           C  
ATOM   2116  N   LYS A 361      36.605  74.396  46.783  1.00 24.64           N  
ATOM   2117  CA  LYS A 361      37.267  73.112  46.546  1.00 25.20           C  
ATOM   2118  C   LYS A 361      37.098  72.613  45.121  1.00 25.39           C  
ATOM   2119  O   LYS A 361      38.062  72.172  44.508  1.00 25.42           O  
ATOM   2120  CB  LYS A 361      36.766  72.050  47.526  1.00 25.39           C  
ATOM   2121  CG  LYS A 361      37.666  70.829  47.637  1.00 25.88           C  
ATOM   2122  CD  LYS A 361      37.374  70.045  48.903  1.00 26.93           C  
ATOM   2123  CE  LYS A 361      36.982  68.618  48.575  1.00 27.91           C  
ATOM   2124  NZ  LYS A 361      37.732  67.624  49.399  1.00 28.89           N  
ATOM   2125  N   MET A 362      35.870  72.672  44.610  1.00 25.89           N  
ATOM   2126  CA  MET A 362      35.579  72.322  43.219  1.00 26.45           C  
ATOM   2127  C   MET A 362      36.454  73.132  42.253  1.00 26.33           C  
ATOM   2128  O   MET A 362      37.062  72.583  41.329  1.00 26.18           O  
ATOM   2129  CB  MET A 362      34.094  72.564  42.900  1.00 26.71           C  
ATOM   2130  CG  MET A 362      33.171  71.384  43.165  1.00 28.04           C  
ATOM   2131  SD  MET A 362      31.710  71.825  44.165  1.00 31.33           S  
ATOM   2132  CE  MET A 362      30.824  70.215  44.240  1.00 31.07           C  
ATOM   2133  N   LEU A 363      36.516  74.437  42.493  1.00 26.37           N  
ATOM   2134  CA  LEU A 363      37.219  75.358  41.615  1.00 26.50           C  
ATOM   2135  C   LEU A 363      38.732  75.170  41.644  1.00 26.60           C  
ATOM   2136  O   LEU A 363      39.379  75.217  40.595  1.00 26.62           O  
ATOM   2137  CB  LEU A 363      36.847  76.809  41.940  1.00 26.54           C  
ATOM   2138  CG  LEU A 363      35.396  77.261  41.721  1.00 26.45           C  
ATOM   2139  CD1 LEU A 363      35.261  78.727  42.077  1.00 26.06           C  
ATOM   2140  CD2 LEU A 363      34.920  77.017  40.293  1.00 26.15           C  
ATOM   2141  N   THR A 364      39.297  74.959  42.832  1.00 26.64           N  
ATOM   2142  CA  THR A 364      40.742  74.771  42.948  1.00 26.77           C  
ATOM   2143  C   THR A 364      41.177  73.470  42.289  1.00 26.63           C  
ATOM   2144  O   THR A 364      42.257  73.396  41.711  1.00 26.80           O  
ATOM   2145  CB  THR A 364      41.208  74.826  44.410  1.00 26.80           C  
ATOM   2146  OG1 THR A 364      40.739  76.036  45.011  1.00 27.69           O  
ATOM   2147  CG2 THR A 364      42.716  74.998  44.483  1.00 27.12           C  
ATOM   2148  N   ASN A 365      40.323  72.458  42.356  1.00 26.48           N  
ATOM   2149  CA  ASN A 365      40.624  71.179  41.735  1.00 26.47           C  
ATOM   2150  C   ASN A 365      40.152  71.065  40.292  1.00 26.36           C  
ATOM   2151  O   ASN A 365      40.300  70.012  39.672  1.00 26.45           O  
ATOM   2152  CB  ASN A 365      40.053  70.043  42.572  1.00 26.56           C  
ATOM   2153  CG  ASN A 365      40.994  69.617  43.663  1.00 27.45           C  
ATOM   2154  OD1 ASN A 365      40.941  70.133  44.783  1.00 28.13           O  
ATOM   2155  ND2 ASN A 365      41.891  68.684  43.340  1.00 28.58           N  
ATOM   2156  N   HIS A 366      39.583  72.143  39.760  1.00 26.18           N  
ATOM   2157  CA  HIS A 366      39.098  72.139  38.385  1.00 25.86           C  
ATOM   2158  C   HIS A 366      40.263  72.007  37.425  1.00 25.84           C  
ATOM   2159  O   HIS A 366      41.347  72.541  37.659  1.00 25.72           O  
ATOM   2160  CB  HIS A 366      38.283  73.395  38.068  1.00 25.78           C  
ATOM   2161  CG  HIS A 366      37.506  73.300  36.792  1.00 25.42           C  
ATOM   2162  ND1 HIS A 366      36.221  72.806  36.737  1.00 25.70           N  
ATOM   2163  CD2 HIS A 366      37.836  73.624  35.521  1.00 25.34           C  
ATOM   2164  CE1 HIS A 366      35.791  72.832  35.488  1.00 25.26           C  
ATOM   2165  NE2 HIS A 366      36.753  73.324  34.731  1.00 25.47           N  
ATOM   2166  N   THR A 367      40.027  71.280  36.344  1.00 26.00           N  
ATOM   2167  CA  THR A 367      41.047  71.046  35.336  1.00 26.25           C  
ATOM   2168  C   THR A 367      41.552  72.344  34.686  1.00 26.24           C  
ATOM   2169  O   THR A 367      42.683  72.385  34.208  1.00 26.40           O  
ATOM   2170  CB  THR A 367      40.560  70.009  34.283  1.00 26.29           C  
ATOM   2171  OG1 THR A 367      40.953  70.421  32.968  1.00 26.74           O  
ATOM   2172  CG2 THR A 367      39.032  69.970  34.204  1.00 26.69           C  
ATOM   2173  N   PHE A 368      40.729  73.395  34.682  1.00 26.20           N  
ATOM   2174  CA  PHE A 368      41.148  74.706  34.174  1.00 26.13           C  
ATOM   2175  C   PHE A 368      42.242  75.297  35.058  1.00 26.26           C  
ATOM   2176  O   PHE A 368      43.165  75.938  34.564  1.00 25.99           O  
ATOM   2177  CB  PHE A 368      39.956  75.675  34.049  1.00 25.99           C  
ATOM   2178  CG  PHE A 368      40.354  77.134  33.901  1.00 25.87           C  
ATOM   2179  CD1 PHE A 368      40.152  78.035  34.946  1.00 25.38           C  
ATOM   2180  CD2 PHE A 368      40.934  77.603  32.719  1.00 25.83           C  
ATOM   2181  CE1 PHE A 368      40.520  79.373  34.819  1.00 24.94           C  
ATOM   2182  CE2 PHE A 368      41.309  78.940  32.583  1.00 24.93           C  
ATOM   2183  CZ  PHE A 368      41.101  79.824  33.635  1.00 25.25           C  
ATOM   2184  N   ILE A 369      42.126  75.066  36.362  1.00 26.73           N  
ATOM   2185  CA  ILE A 369      43.091  75.566  37.340  1.00 27.20           C  
ATOM   2186  C   ILE A 369      44.309  74.654  37.406  1.00 27.58           C  
ATOM   2187  O   ILE A 369      45.430  75.125  37.584  1.00 27.47           O  
ATOM   2188  CB  ILE A 369      42.423  75.740  38.740  1.00 27.16           C  
ATOM   2189  CG1 ILE A 369      41.414  76.897  38.723  1.00 26.80           C  
ATOM   2190  CG2 ILE A 369      43.467  75.944  39.843  1.00 27.24           C  
ATOM   2191  CD1 ILE A 369      42.018  78.276  38.455  1.00 26.84           C  
ATOM   2192  N   LYS A 370      44.082  73.352  37.256  1.00 28.27           N  
ATOM   2193  CA  LYS A 370      45.172  72.388  37.171  1.00 29.08           C  
ATOM   2194  C   LYS A 370      46.058  72.692  35.962  1.00 29.50           C  
ATOM   2195  O   LYS A 370      47.271  72.840  36.107  1.00 29.69           O  
ATOM   2196  CB  LYS A 370      44.631  70.964  37.083  1.00 29.16           C  
ATOM   2197  CG  LYS A 370      44.070  70.411  38.383  1.00 29.84           C  
ATOM   2198  CD  LYS A 370      43.113  69.258  38.090  1.00 31.13           C  
ATOM   2199  CE  LYS A 370      43.101  68.223  39.208  1.00 32.12           C  
ATOM   2200  NZ  LYS A 370      41.888  67.347  39.148  1.00 32.58           N  
ATOM   2201  N   ARG A 371      45.440  72.799  34.784  1.00 30.07           N  
ATOM   2202  CA  ARG A 371      46.123  73.151  33.538  1.00 30.71           C  
ATOM   2203  C   ARG A 371      46.863  74.474  33.661  1.00 31.20           C  
ATOM   2204  O   ARG A 371      47.968  74.617  33.153  1.00 31.25           O  
ATOM   2205  CB  ARG A 371      45.111  73.229  32.391  1.00 30.74           C  
ATOM   2206  CG  ARG A 371      45.702  73.313  30.987  1.00 31.35           C  
ATOM   2207  CD  ARG A 371      44.692  73.725  29.909  1.00 32.55           C  
ATOM   2208  NE  ARG A 371      44.425  75.168  29.935  1.00 34.15           N  
ATOM   2209  CZ  ARG A 371      43.227  75.738  29.761  1.00 34.38           C  
ATOM   2210  NH1 ARG A 371      42.141  75.003  29.539  1.00 34.68           N  
ATOM   2211  NH2 ARG A 371      43.115  77.057  29.812  1.00 34.09           N  
ATOM   2212  N   SER A 372      46.248  75.430  34.351  1.00 32.01           N  
ATOM   2213  CA  SER A 372      46.789  76.780  34.484  1.00 32.69           C  
ATOM   2214  C   SER A 372      48.015  76.811  35.375  1.00 33.28           C  
ATOM   2215  O   SER A 372      48.820  77.735  35.302  1.00 33.47           O  
ATOM   2216  CB  SER A 372      45.728  77.734  35.045  1.00 32.61           C  
ATOM   2217  OG  SER A 372      44.690  77.970  34.111  1.00 32.42           O  
ATOM   2218  N   GLU A 373      48.145  75.808  36.231  1.00 34.14           N  
ATOM   2219  CA  GLU A 373      49.260  75.760  37.157  1.00 35.11           C  
ATOM   2220  C   GLU A 373      50.522  75.282  36.446  1.00 35.77           C  
ATOM   2221  O   GLU A 373      51.585  75.902  36.570  1.00 36.00           O  
ATOM   2222  CB  GLU A 373      48.931  74.858  38.337  1.00 35.09           C  
ATOM   2223  CG  GLU A 373      48.153  75.539  39.447  1.00 35.55           C  
ATOM   2224  CD  GLU A 373      47.898  74.601  40.608  1.00 36.53           C  
ATOM   2225  OE1 GLU A 373      46.965  73.774  40.513  1.00 36.96           O  
ATOM   2226  OE2 GLU A 373      48.646  74.676  41.608  1.00 37.06           O  
ATOM   2227  N   VAL A 374      50.396  74.192  35.690  1.00 36.47           N  
ATOM   2228  CA  VAL A 374      51.540  73.606  34.991  1.00 37.11           C  
ATOM   2229  C   VAL A 374      52.043  74.475  33.840  1.00 37.73           C  
ATOM   2230  O   VAL A 374      53.250  74.573  33.626  1.00 37.85           O  
ATOM   2231  CB  VAL A 374      51.282  72.148  34.501  1.00 36.96           C  
ATOM   2232  CG1 VAL A 374      51.421  71.173  35.654  1.00 37.33           C  
ATOM   2233  CG2 VAL A 374      49.927  72.004  33.846  1.00 36.61           C  
ATOM   2234  N   GLU A 375      51.129  75.110  33.108  1.00 38.52           N  
ATOM   2235  CA  GLU A 375      51.535  75.908  31.952  1.00 39.32           C  
ATOM   2236  C   GLU A 375      52.043  77.278  32.373  1.00 39.80           C  
ATOM   2237  O   GLU A 375      51.371  78.293  32.198  1.00 40.06           O  
ATOM   2238  CB  GLU A 375      50.445  75.969  30.856  1.00 39.34           C  
ATOM   2239  CG  GLU A 375      49.168  76.730  31.185  1.00 39.41           C  
ATOM   2240  CD  GLU A 375      48.077  76.520  30.149  1.00 39.65           C  
ATOM   2241  OE1 GLU A 375      47.385  77.502  29.811  1.00 40.42           O  
ATOM   2242  OE2 GLU A 375      47.904  75.376  29.673  1.00 39.28           O  
ATOM   2243  N   GLU A 376      53.244  77.289  32.937  1.00 40.47           N  
ATOM   2244  CA  GLU A 376      53.883  78.524  33.370  1.00 41.25           C  
ATOM   2245  C   GLU A 376      53.990  79.530  32.223  1.00 41.43           C  
ATOM   2246  O   GLU A 376      54.594  79.260  31.178  1.00 41.31           O  
ATOM   2247  CB  GLU A 376      55.252  78.239  34.004  1.00 41.45           C  
ATOM   2248  CG  GLU A 376      55.481  78.915  35.356  1.00 42.54           C  
ATOM   2249  CD  GLU A 376      54.271  78.865  36.286  1.00 43.61           C  
ATOM   2250  OE1 GLU A 376      53.959  77.771  36.815  1.00 43.73           O  
ATOM   2251  OE2 GLU A 376      53.638  79.927  36.494  1.00 43.74           O  
ATOM   2252  N   VAL A 377      53.355  80.679  32.434  1.00 41.79           N  
ATOM   2253  CA  VAL A 377      53.322  81.764  31.461  1.00 42.05           C  
ATOM   2254  C   VAL A 377      53.828  83.048  32.109  1.00 42.38           C  
ATOM   2255  O   VAL A 377      53.512  83.337  33.270  1.00 42.57           O  
ATOM   2256  CB  VAL A 377      51.904  81.975  30.869  1.00 41.91           C  
ATOM   2257  CG1 VAL A 377      51.618  80.926  29.811  1.00 42.15           C  
ATOM   2258  CG2 VAL A 377      50.829  81.949  31.951  1.00 41.52           C  
ATOM   2259  N   ASP A 378      54.622  83.805  31.356  1.00 42.64           N  
ATOM   2260  CA  ASP A 378      55.235  85.029  31.857  1.00 42.93           C  
ATOM   2261  C   ASP A 378      54.189  86.116  32.082  1.00 43.20           C  
ATOM   2262  O   ASP A 378      53.886  86.891  31.169  1.00 43.41           O  
ATOM   2263  CB  ASP A 378      56.308  85.519  30.880  1.00 42.96           C  
ATOM   2264  CG  ASP A 378      57.250  86.536  31.497  1.00 42.86           C  
ATOM   2265  OD1 ASP A 378      57.160  86.787  32.718  1.00 42.73           O  
ATOM   2266  OD2 ASP A 378      58.120  87.135  30.830  1.00 42.93           O  
ATOM   2267  N   PHE A 379      53.635  86.158  33.295  1.00 43.40           N  
ATOM   2268  CA  PHE A 379      52.654  87.181  33.662  1.00 43.51           C  
ATOM   2269  C   PHE A 379      53.301  88.557  33.793  1.00 43.77           C  
ATOM   2270  O   PHE A 379      52.687  89.565  33.446  1.00 43.83           O  
ATOM   2271  CB  PHE A 379      51.913  86.824  34.957  1.00 43.43           C  
ATOM   2272  CG  PHE A 379      50.931  87.880  35.402  1.00 42.80           C  
ATOM   2273  CD1 PHE A 379      51.289  88.823  36.354  1.00 42.42           C  
ATOM   2274  CD2 PHE A 379      49.657  87.939  34.850  1.00 42.36           C  
ATOM   2275  CE1 PHE A 379      50.390  89.807  36.755  1.00 42.45           C  
ATOM   2276  CE2 PHE A 379      48.754  88.917  35.246  1.00 42.21           C  
ATOM   2277  CZ  PHE A 379      49.122  89.853  36.199  1.00 42.20           C  
ATOM   2278  N   ALA A 380      54.532  88.587  34.299  1.00 44.04           N  
ATOM   2279  CA  ALA A 380      55.285  89.830  34.437  1.00 44.40           C  
ATOM   2280  C   ALA A 380      55.624  90.423  33.072  1.00 44.65           C  
ATOM   2281  O   ALA A 380      55.541  91.640  32.876  1.00 44.54           O  
ATOM   2282  CB  ALA A 380      56.549  89.601  35.252  1.00 44.43           C  
ATOM   2283  N   GLY A 381      55.995  89.550  32.136  1.00 45.00           N  
ATOM   2284  CA  GLY A 381      56.330  89.947  30.780  1.00 45.48           C  
ATOM   2285  C   GLY A 381      55.129  90.492  30.039  1.00 45.80           C  
ATOM   2286  O   GLY A 381      55.221  91.525  29.371  1.00 45.84           O  
ATOM   2287  N   TRP A 382      54.001  89.797  30.167  1.00 46.12           N  
ATOM   2288  CA  TRP A 382      52.748  90.235  29.565  1.00 46.45           C  
ATOM   2289  C   TRP A 382      52.238  91.519  30.215  1.00 46.91           C  
ATOM   2290  O   TRP A 382      51.905  92.478  29.516  1.00 47.03           O  
ATOM   2291  CB  TRP A 382      51.686  89.140  29.652  1.00 46.25           C  
ATOM   2292  CG  TRP A 382      50.370  89.569  29.102  1.00 45.71           C  
ATOM   2293  CD1 TRP A 382      49.961  89.482  27.809  1.00 45.47           C  
ATOM   2294  CD2 TRP A 382      49.291  90.172  29.824  1.00 45.45           C  
ATOM   2295  NE1 TRP A 382      48.690  89.985  27.677  1.00 45.55           N  
ATOM   2296  CE2 TRP A 382      48.254  90.416  28.901  1.00 45.42           C  
ATOM   2297  CE3 TRP A 382      49.090  90.528  31.166  1.00 45.57           C  
ATOM   2298  CZ2 TRP A 382      47.036  91.000  29.273  1.00 45.57           C  
ATOM   2299  CZ3 TRP A 382      47.882  91.113  31.534  1.00 45.45           C  
ATOM   2300  CH2 TRP A 382      46.871  91.341  30.590  1.00 45.47           C  
ATOM   2301  N   LEU A 383      52.177  91.527  31.547  1.00 47.40           N  
ATOM   2302  CA  LEU A 383      51.690  92.684  32.291  1.00 47.96           C  
ATOM   2303  C   LEU A 383      52.468  93.931  31.915  1.00 48.63           C  
ATOM   2304  O   LEU A 383      51.873  94.960  31.609  1.00 48.70           O  
ATOM   2305  CB  LEU A 383      51.769  92.440  33.801  1.00 47.77           C  
ATOM   2306  CG  LEU A 383      50.902  93.251  34.769  1.00 47.25           C  
ATOM   2307  CD1 LEU A 383      51.742  94.306  35.470  1.00 46.49           C  
ATOM   2308  CD2 LEU A 383      49.690  93.879  34.088  1.00 46.84           C  
ATOM   2309  N   CYS A 384      53.793  93.820  31.911  1.00 49.51           N  
ATOM   2310  CA  CYS A 384      54.669  94.949  31.614  1.00 50.49           C  
ATOM   2311  C   CYS A 384      54.635  95.404  30.152  1.00 51.04           C  
ATOM   2312  O   CYS A 384      54.680  96.605  29.882  1.00 51.14           O  
ATOM   2313  CB  CYS A 384      56.101  94.631  32.030  1.00 50.47           C  
ATOM   2314  SG  CYS A 384      56.360  94.654  33.818  1.00 51.27           S  
ATOM   2315  N   LYS A 385      54.553  94.455  29.221  1.00 51.76           N  
ATOM   2316  CA  LYS A 385      54.589  94.782  27.793  1.00 52.54           C  
ATOM   2317  C   LYS A 385      53.303  95.421  27.259  1.00 52.93           C  
ATOM   2318  O   LYS A 385      53.352  96.238  26.342  1.00 53.00           O  
ATOM   2319  CB  LYS A 385      54.971  93.561  26.951  1.00 52.70           C  
ATOM   2320  CG  LYS A 385      56.325  93.690  26.240  1.00 53.22           C  
ATOM   2321  CD  LYS A 385      56.176  94.279  24.836  1.00 53.88           C  
ATOM   2322  CE  LYS A 385      56.564  93.270  23.758  1.00 54.29           C  
ATOM   2323  NZ  LYS A 385      55.373  92.627  23.129  1.00 54.30           N  
ATOM   2324  N   THR A 386      52.161  95.043  27.825  1.00 53.54           N  
ATOM   2325  CA  THR A 386      50.879  95.627  27.420  1.00 54.14           C  
ATOM   2326  C   THR A 386      50.551  96.914  28.194  1.00 54.62           C  
ATOM   2327  O   THR A 386      49.599  97.629  27.853  1.00 54.70           O  
ATOM   2328  CB  THR A 386      49.726  94.600  27.557  1.00 54.07           C  
ATOM   2329  OG1 THR A 386      49.616  94.177  28.920  1.00 53.89           O  
ATOM   2330  CG2 THR A 386      50.049  93.311  26.800  1.00 54.00           C  
ATOM   2331  N   LEU A 387      51.347  97.204  29.225  1.00 55.10           N  
ATOM   2332  CA  LEU A 387      51.154  98.390  30.060  1.00 55.55           C  
ATOM   2333  C   LEU A 387      52.310  99.382  29.944  1.00 56.19           C  
ATOM   2334  O   LEU A 387      52.307 100.419  30.619  1.00 56.22           O  
ATOM   2335  CB  LEU A 387      50.975  97.980  31.524  1.00 55.30           C  
ATOM   2336  CG  LEU A 387      49.619  98.213  32.188  1.00 54.80           C  
ATOM   2337  CD1 LEU A 387      48.606  97.195  31.724  1.00 54.43           C  
ATOM   2338  CD2 LEU A 387      49.768  98.147  33.691  1.00 54.55           C  
ATOM   2339  N   ARG A 388      53.285  99.056  29.088  1.00 56.95           N  
ATOM   2340  CA  ARG A 388      54.510  99.848  28.909  1.00 57.67           C  
ATOM   2341  C   ARG A 388      55.151 100.190  30.261  1.00 58.12           C  
ATOM   2342  O   ARG A 388      55.513 101.344  30.522  1.00 58.21           O  
ATOM   2343  CB  ARG A 388      54.228 101.115  28.088  1.00 57.71           C  
ATOM   2344  CG  ARG A 388      54.152 100.890  26.582  1.00 58.40           C  
ATOM   2345  CD  ARG A 388      55.388 101.365  25.818  1.00 59.72           C  
ATOM   2346  NE  ARG A 388      55.055 101.982  24.532  1.00 60.44           N  
ATOM   2347  CZ  ARG A 388      55.498 103.171  24.119  1.00 60.95           C  
ATOM   2348  NH1 ARG A 388      56.303 103.900  24.888  1.00 60.64           N  
ATOM   2349  NH2 ARG A 388      55.130 103.635  22.927  1.00 61.05           N  
ATOM   2350  N   LEU A 389      55.286  99.171  31.110  1.00 58.67           N  
ATOM   2351  CA  LEU A 389      55.682  99.347  32.507  1.00 59.26           C  
ATOM   2352  C   LEU A 389      56.978  98.606  32.861  1.00 59.82           C  
ATOM   2353  O   LEU A 389      57.423  98.642  34.014  1.00 59.92           O  
ATOM   2354  CB  LEU A 389      54.535  98.902  33.431  1.00 59.18           C  
ATOM   2355  CG  LEU A 389      54.567  99.216  34.935  1.00 59.01           C  
ATOM   2356  CD1 LEU A 389      54.160 100.660  35.228  1.00 59.10           C  
ATOM   2357  CD2 LEU A 389      53.683  98.242  35.699  1.00 58.35           C  
ATOM   2358  N   ASN A 390      57.585  97.956  31.867  1.00 60.44           N  
ATOM   2359  CA  ASN A 390      58.790  97.139  32.076  1.00 61.09           C  
ATOM   2360  C   ASN A 390      59.792  97.703  33.092  1.00 61.46           C  
ATOM   2361  O   ASN A 390      60.455  98.715  32.845  1.00 61.61           O  
ATOM   2362  CB  ASN A 390      59.483  96.795  30.741  1.00 61.11           C  
ATOM   2363  CG  ASN A 390      59.793  98.022  29.896  1.00 61.17           C  
ATOM   2364  OD1 ASN A 390      60.901  98.565  29.944  1.00 61.07           O  
ATOM   2365  ND2 ASN A 390      58.816  98.457  29.106  1.00 61.45           N  
ATOM   2366  N   GLN A 391      59.867  97.047  34.248  1.00 61.85           N  
ATOM   2367  CA  GLN A 391      60.822  97.406  35.296  1.00 62.23           C  
ATOM   2368  C   GLN A 391      61.494  96.134  35.842  1.00 62.50           C  
ATOM   2369  O   GLN A 391      60.935  95.035  35.709  1.00 62.48           O  
ATOM   2370  CB  GLN A 391      60.131  98.204  36.414  1.00 62.19           C  
ATOM   2371  CG  GLN A 391      59.762  99.644  36.029  1.00 62.13           C  
ATOM   2372  CD  GLN A 391      60.720 100.698  36.579  1.00 62.00           C  
ATOM   2373  OE1 GLN A 391      61.845 100.386  36.975  1.00 61.87           O  
ATOM   2374  NE2 GLN A 391      60.272 101.950  36.596  1.00 61.69           N  
ATOM   2375  N   PRO A 392      62.686  96.272  36.436  1.00 62.76           N  
ATOM   2376  CA  PRO A 392      63.422  95.118  36.981  1.00 62.97           C  
ATOM   2377  C   PRO A 392      62.732  94.495  38.202  1.00 63.09           C  
ATOM   2378  O   PRO A 392      63.294  94.492  39.304  1.00 63.16           O  
ATOM   2379  CB  PRO A 392      64.787  95.716  37.373  1.00 62.97           C  
ATOM   2380  CG  PRO A 392      64.846  97.057  36.716  1.00 62.92           C  
ATOM   2381  CD  PRO A 392      63.432  97.531  36.624  1.00 62.78           C  
ATOM   2382  N   GLY A 393      61.529  93.964  37.993  1.00 63.13           N  
ATOM   2383  CA  GLY A 393      60.708  93.459  39.078  1.00 63.22           C  
ATOM   2384  C   GLY A 393      59.898  94.568  39.726  1.00 63.30           C  
ATOM   2385  O   GLY A 393      60.443  95.580  40.177  1.00 63.29           O  
TER    2386      GLY A 393                                                      
ATOM   2387  N   THR B  59      20.901 138.531  46.345  1.00 57.81           N  
ATOM   2388  CA  THR B  59      21.661 139.706  45.825  1.00 57.87           C  
ATOM   2389  C   THR B  59      23.015 139.278  45.244  1.00 57.96           C  
ATOM   2390  O   THR B  59      23.406 138.111  45.360  1.00 57.99           O  
ATOM   2391  CB  THR B  59      21.829 140.788  46.917  1.00 57.84           C  
ATOM   2392  OG1 THR B  59      22.658 140.288  47.971  1.00 57.82           O  
ATOM   2393  CG2 THR B  59      20.499 141.076  47.609  1.00 57.83           C  
ATOM   2394  N   GLN B  60      23.730 140.224  44.631  1.00 57.97           N  
ATOM   2395  CA  GLN B  60      24.856 139.876  43.766  1.00 57.99           C  
ATOM   2396  C   GLN B  60      26.255 140.140  44.315  1.00 58.25           C  
ATOM   2397  O   GLN B  60      26.540 141.198  44.891  1.00 58.34           O  
ATOM   2398  CB  GLN B  60      24.683 140.480  42.372  1.00 57.88           C  
ATOM   2399  CG  GLN B  60      23.341 140.136  41.708  1.00 57.50           C  
ATOM   2400  CD  GLN B  60      23.179 138.657  41.390  1.00 56.51           C  
ATOM   2401  OE1 GLN B  60      22.992 137.842  42.292  1.00 56.34           O  
ATOM   2402  NE2 GLN B  60      23.235 138.313  40.108  1.00 55.99           N  
ATOM   2403  N   LYS B  61      27.118 139.153  44.076  1.00 58.34           N  
ATOM   2404  CA  LYS B  61      28.446 139.032  44.668  1.00 58.22           C  
ATOM   2405  C   LYS B  61      29.548 139.744  43.877  1.00 58.51           C  
ATOM   2406  O   LYS B  61      30.663 139.229  43.746  1.00 58.39           O  
ATOM   2407  CB  LYS B  61      28.782 137.544  44.807  1.00 58.01           C  
ATOM   2408  CG  LYS B  61      29.140 136.827  43.493  1.00 57.47           C  
ATOM   2409  CD  LYS B  61      27.960 136.087  42.873  1.00 56.50           C  
ATOM   2410  CE  LYS B  61      28.019 136.114  41.350  1.00 55.74           C  
ATOM   2411  NZ  LYS B  61      28.582 134.863  40.779  1.00 54.65           N  
ATOM   2412  N   ALA B  62      29.241 140.929  43.356  1.00 58.95           N  
ATOM   2413  CA  ALA B  62      30.231 141.729  42.633  1.00 59.37           C  
ATOM   2414  C   ALA B  62      31.414 142.085  43.537  1.00 59.63           C  
ATOM   2415  O   ALA B  62      32.505 142.402  43.057  1.00 59.61           O  
ATOM   2416  CB  ALA B  62      29.593 142.983  42.081  1.00 59.31           C  
ATOM   2417  N   LYS B  63      31.168 142.015  44.845  1.00 60.01           N  
ATOM   2418  CA  LYS B  63      32.154 142.281  45.891  1.00 60.34           C  
ATOM   2419  C   LYS B  63      33.430 141.441  45.761  1.00 60.63           C  
ATOM   2420  O   LYS B  63      34.515 141.895  46.124  1.00 60.59           O  
ATOM   2421  CB  LYS B  63      31.517 142.073  47.273  1.00 60.32           C  
ATOM   2422  CG  LYS B  63      30.230 141.237  47.266  1.00 60.40           C  
ATOM   2423  CD  LYS B  63      29.227 141.731  48.299  1.00 60.77           C  
ATOM   2424  CE  LYS B  63      28.122 142.561  47.653  1.00 61.10           C  
ATOM   2425  NZ  LYS B  63      28.007 143.916  48.270  1.00 60.62           N  
ATOM   2426  N   VAL B  64      33.290 140.223  45.242  1.00 61.15           N  
ATOM   2427  CA  VAL B  64      34.428 139.326  45.024  1.00 61.68           C  
ATOM   2428  C   VAL B  64      34.738 139.132  43.533  1.00 62.08           C  
ATOM   2429  O   VAL B  64      34.195 139.833  42.670  1.00 62.15           O  
ATOM   2430  CB  VAL B  64      34.219 137.936  45.708  1.00 61.62           C  
ATOM   2431  CG1 VAL B  64      34.071 138.086  47.212  1.00 61.76           C  
ATOM   2432  CG2 VAL B  64      33.018 137.195  45.117  1.00 61.64           C  
ATOM   2433  N   GLY B  65      35.621 138.177  43.247  1.00 62.55           N  
ATOM   2434  CA  GLY B  65      35.928 137.769  41.888  1.00 63.05           C  
ATOM   2435  C   GLY B  65      36.543 136.385  41.852  1.00 63.41           C  
ATOM   2436  O   GLY B  65      36.027 135.455  42.485  1.00 63.50           O  
ATOM   2437  N   GLU B  66      37.650 136.254  41.120  1.00 63.71           N  
ATOM   2438  CA  GLU B  66      38.348 134.976  40.968  1.00 63.98           C  
ATOM   2439  C   GLU B  66      38.804 134.446  42.322  1.00 64.16           C  
ATOM   2440  O   GLU B  66      39.244 135.208  43.186  1.00 64.13           O  
ATOM   2441  CB  GLU B  66      39.541 135.102  40.007  1.00 64.00           C  
ATOM   2442  CG  GLU B  66      39.180 135.600  38.608  1.00 64.09           C  
ATOM   2443  CD  GLU B  66      39.551 134.626  37.498  1.00 63.92           C  
ATOM   2444  OE1 GLU B  66      39.064 133.471  37.508  1.00 63.78           O  
ATOM   2445  OE2 GLU B  66      40.325 135.025  36.601  1.00 63.82           O  
ATOM   2446  N   LEU B  67      38.680 133.139  42.504  1.00 64.53           N  
ATOM   2447  CA  LEU B  67      39.008 132.519  43.781  1.00 64.97           C  
ATOM   2448  C   LEU B  67      40.083 131.455  43.631  1.00 65.40           C  
ATOM   2449  O   LEU B  67      40.001 130.585  42.759  1.00 65.46           O  
ATOM   2450  CB  LEU B  67      37.762 131.920  44.445  1.00 64.82           C  
ATOM   2451  CG  LEU B  67      36.453 131.861  43.656  1.00 64.59           C  
ATOM   2452  CD1 LEU B  67      36.462 130.688  42.680  1.00 64.53           C  
ATOM   2453  CD2 LEU B  67      35.268 131.776  44.607  1.00 64.14           C  
ATOM   2454  N   LYS B  68      41.097 131.554  44.485  1.00 65.88           N  
ATOM   2455  CA  LYS B  68      42.123 130.528  44.610  1.00 66.28           C  
ATOM   2456  C   LYS B  68      41.943 129.814  45.950  1.00 66.51           C  
ATOM   2457  O   LYS B  68      41.014 130.124  46.707  1.00 66.54           O  
ATOM   2458  CB  LYS B  68      43.518 131.150  44.496  1.00 66.35           C  
ATOM   2459  CG  LYS B  68      44.104 131.113  43.090  1.00 66.62           C  
ATOM   2460  CD  LYS B  68      44.402 132.514  42.572  1.00 66.97           C  
ATOM   2461  CE  LYS B  68      43.421 132.924  41.482  1.00 67.18           C  
ATOM   2462  NZ  LYS B  68      44.032 133.856  40.486  1.00 67.35           N  
ATOM   2463  N   ASP B  69      42.828 128.864  46.243  1.00 66.78           N  
ATOM   2464  CA  ASP B  69      42.701 128.037  47.441  1.00 67.12           C  
ATOM   2465  C   ASP B  69      43.012 128.769  48.754  1.00 67.22           C  
ATOM   2466  O   ASP B  69      42.262 128.652  49.734  1.00 67.18           O  
ATOM   2467  CB  ASP B  69      43.571 126.784  47.312  1.00 67.21           C  
ATOM   2468  CG  ASP B  69      43.407 125.841  48.487  1.00 67.54           C  
ATOM   2469  OD1 ASP B  69      42.416 125.077  48.503  1.00 67.75           O  
ATOM   2470  OD2 ASP B  69      44.215 125.803  49.443  1.00 68.03           O  
ATOM   2471  N   ASP B  70      44.110 129.524  48.758  1.00 67.35           N  
ATOM   2472  CA  ASP B  70      44.640 130.156  49.969  1.00 67.55           C  
ATOM   2473  C   ASP B  70      43.705 131.192  50.592  1.00 67.50           C  
ATOM   2474  O   ASP B  70      43.673 131.346  51.818  1.00 67.46           O  
ATOM   2475  CB  ASP B  70      46.002 130.793  49.683  1.00 67.67           C  
ATOM   2476  CG  ASP B  70      46.864 129.933  48.783  1.00 68.25           C  
ATOM   2477  OD1 ASP B  70      47.833 129.327  49.291  1.00 69.14           O  
ATOM   2478  OD2 ASP B  70      46.642 129.797  47.560  1.00 68.46           O  
ATOM   2479  N   ASP B  71      42.945 131.883  49.741  1.00 67.40           N  
ATOM   2480  CA  ASP B  71      42.040 132.956  50.163  1.00 67.29           C  
ATOM   2481  C   ASP B  71      40.986 132.513  51.184  1.00 67.11           C  
ATOM   2482  O   ASP B  71      40.351 133.350  51.830  1.00 67.06           O  
ATOM   2483  CB  ASP B  71      41.359 133.582  48.941  1.00 67.36           C  
ATOM   2484  CG  ASP B  71      42.272 134.537  48.186  1.00 67.74           C  
ATOM   2485  OD1 ASP B  71      42.857 134.125  47.158  1.00 67.74           O  
ATOM   2486  OD2 ASP B  71      42.461 135.720  48.544  1.00 68.09           O  
ATOM   2487  N   PHE B  72      40.819 131.201  51.333  1.00 66.90           N  
ATOM   2488  CA  PHE B  72      39.812 130.643  52.230  1.00 66.79           C  
ATOM   2489  C   PHE B  72      40.372 130.190  53.580  1.00 66.80           C  
ATOM   2490  O   PHE B  72      41.525 129.761  53.675  1.00 66.99           O  
ATOM   2491  CB  PHE B  72      39.086 129.485  51.547  1.00 66.79           C  
ATOM   2492  CG  PHE B  72      38.273 129.900  50.356  1.00 66.27           C  
ATOM   2493  CD1 PHE B  72      38.607 129.452  49.082  1.00 65.86           C  
ATOM   2494  CD2 PHE B  72      37.175 130.739  50.508  1.00 65.55           C  
ATOM   2495  CE1 PHE B  72      37.858 129.830  47.979  1.00 65.50           C  
ATOM   2496  CE2 PHE B  72      36.424 131.124  49.415  1.00 65.39           C  
ATOM   2497  CZ  PHE B  72      36.764 130.669  48.146  1.00 65.51           C  
ATOM   2498  N   GLU B  73      39.536 130.284  54.614  1.00 66.61           N  
ATOM   2499  CA  GLU B  73      39.906 129.908  55.976  1.00 66.54           C  
ATOM   2500  C   GLU B  73      38.731 129.181  56.638  1.00 66.47           C  
ATOM   2501  O   GLU B  73      37.620 129.708  56.682  1.00 66.55           O  
ATOM   2502  CB  GLU B  73      40.311 131.158  56.775  1.00 66.59           C  
ATOM   2503  CG  GLU B  73      40.601 130.933  58.254  1.00 66.77           C  
ATOM   2504  CD  GLU B  73      40.018 132.025  59.141  1.00 66.86           C  
ATOM   2505  OE1 GLU B  73      38.821 131.935  59.494  1.00 66.54           O  
ATOM   2506  OE2 GLU B  73      40.757 132.974  59.491  1.00 66.92           O  
ATOM   2507  N   ARG B  74      38.982 127.975  57.145  1.00 66.33           N  
ATOM   2508  CA  ARG B  74      37.929 127.132  57.720  1.00 66.23           C  
ATOM   2509  C   ARG B  74      37.333 127.719  59.003  1.00 66.08           C  
ATOM   2510  O   ARG B  74      38.067 128.100  59.915  1.00 66.18           O  
ATOM   2511  CB  ARG B  74      38.461 125.723  57.989  1.00 66.31           C  
ATOM   2512  CG  ARG B  74      38.700 124.890  56.741  1.00 66.56           C  
ATOM   2513  CD  ARG B  74      38.231 123.443  56.866  1.00 67.16           C  
ATOM   2514  NE  ARG B  74      39.346 122.495  56.864  1.00 67.74           N  
ATOM   2515  CZ  ARG B  74      39.932 122.008  55.770  1.00 68.13           C  
ATOM   2516  NH1 ARG B  74      39.521 122.370  54.559  1.00 68.15           N  
ATOM   2517  NH2 ARG B  74      40.939 121.153  55.888  1.00 68.29           N  
ATOM   2518  N   ILE B  75      36.004 127.786  59.061  1.00 65.90           N  
ATOM   2519  CA  ILE B  75      35.288 128.319  60.228  1.00 65.74           C  
ATOM   2520  C   ILE B  75      34.511 127.219  60.960  1.00 65.67           C  
ATOM   2521  O   ILE B  75      34.494 127.179  62.196  1.00 65.70           O  
ATOM   2522  CB  ILE B  75      34.340 129.489  59.819  1.00 65.74           C  
ATOM   2523  CG1 ILE B  75      35.144 130.686  59.297  1.00 65.74           C  
ATOM   2524  CG2 ILE B  75      33.448 129.924  60.990  1.00 65.82           C  
ATOM   2525  CD1 ILE B  75      34.330 131.676  58.477  1.00 65.41           C  
ATOM   2526  N   SER B  76      33.871 126.337  60.191  1.00 65.52           N  
ATOM   2527  CA  SER B  76      33.076 125.235  60.738  1.00 65.36           C  
ATOM   2528  C   SER B  76      32.920 124.077  59.745  1.00 65.29           C  
ATOM   2529  O   SER B  76      33.327 124.174  58.584  1.00 65.27           O  
ATOM   2530  CB  SER B  76      31.699 125.736  61.193  1.00 65.38           C  
ATOM   2531  OG  SER B  76      31.212 124.977  62.287  1.00 65.30           O  
ATOM   2532  N   GLU B  77      32.336 122.981  60.222  1.00 65.22           N  
ATOM   2533  CA  GLU B  77      32.066 121.805  59.404  1.00 65.11           C  
ATOM   2534  C   GLU B  77      30.563 121.700  59.188  1.00 64.92           C  
ATOM   2535  O   GLU B  77      29.794 121.685  60.152  1.00 64.96           O  
ATOM   2536  CB  GLU B  77      32.598 120.544  60.096  1.00 65.24           C  
ATOM   2537  CG  GLU B  77      33.116 119.462  59.154  1.00 65.47           C  
ATOM   2538  CD  GLU B  77      34.482 119.778  58.557  1.00 65.53           C  
ATOM   2539  OE1 GLU B  77      35.269 120.525  59.181  1.00 65.28           O  
ATOM   2540  OE2 GLU B  77      34.767 119.273  57.449  1.00 65.71           O  
ATOM   2541  N   LEU B  78      30.148 121.636  57.927  1.00 64.66           N  
ATOM   2542  CA  LEU B  78      28.727 121.670  57.593  1.00 64.46           C  
ATOM   2543  C   LEU B  78      28.130 120.288  57.317  1.00 64.33           C  
ATOM   2544  O   LEU B  78      27.056 119.961  57.834  1.00 64.23           O  
ATOM   2545  CB  LEU B  78      28.463 122.624  56.419  1.00 64.49           C  
ATOM   2546  CG  LEU B  78      28.350 124.117  56.746  1.00 64.43           C  
ATOM   2547  CD1 LEU B  78      28.641 124.952  55.514  1.00 64.40           C  
ATOM   2548  CD2 LEU B  78      26.978 124.466  57.316  1.00 64.74           C  
ATOM   2549  N   GLY B  79      28.820 119.487  56.506  1.00 64.15           N  
ATOM   2550  CA  GLY B  79      28.334 118.161  56.165  1.00 64.04           C  
ATOM   2551  C   GLY B  79      29.210 117.354  55.227  1.00 64.02           C  
ATOM   2552  O   GLY B  79      30.168 117.868  54.635  1.00 63.94           O  
ATOM   2553  N   ALA B  80      28.868 116.072  55.104  1.00 63.95           N  
ATOM   2554  CA  ALA B  80      29.549 115.151  54.200  1.00 63.90           C  
ATOM   2555  C   ALA B  80      28.529 114.271  53.482  1.00 63.86           C  
ATOM   2556  O   ALA B  80      27.501 113.904  54.058  1.00 63.88           O  
ATOM   2557  CB  ALA B  80      30.550 114.294  54.966  1.00 63.88           C  
ATOM   2558  N   GLY B  81      28.818 113.943  52.224  1.00 63.78           N  
ATOM   2559  CA  GLY B  81      27.962 113.081  51.427  1.00 63.73           C  
ATOM   2560  C   GLY B  81      28.739 112.125  50.540  1.00 63.81           C  
ATOM   2561  O   GLY B  81      29.945 111.931  50.724  1.00 63.83           O  
ATOM   2562  N   ASN B  82      28.039 111.524  49.577  1.00 63.83           N  
ATOM   2563  CA  ASN B  82      28.639 110.598  48.617  1.00 63.78           C  
ATOM   2564  C   ASN B  82      29.557 111.296  47.619  1.00 63.84           C  
ATOM   2565  O   ASN B  82      29.139 111.655  46.512  1.00 63.91           O  
ATOM   2566  CB  ASN B  82      27.553 109.821  47.879  1.00 63.69           C  
ATOM   2567  CG  ASN B  82      26.904 108.778  48.747  1.00 63.84           C  
ATOM   2568  OD1 ASN B  82      27.502 107.745  49.047  1.00 64.19           O  
ATOM   2569  ND2 ASN B  82      25.672 109.043  49.167  1.00 64.08           N  
ATOM   2570  N   GLY B  83      30.813 111.475  48.022  1.00 63.86           N  
ATOM   2571  CA  GLY B  83      31.790 112.196  47.226  1.00 63.85           C  
ATOM   2572  C   GLY B  83      31.618 113.693  47.393  1.00 63.81           C  
ATOM   2573  O   GLY B  83      31.324 114.397  46.422  1.00 63.86           O  
ATOM   2574  N   GLY B  84      31.789 114.174  48.625  1.00 63.68           N  
ATOM   2575  CA  GLY B  84      31.612 115.583  48.927  1.00 63.59           C  
ATOM   2576  C   GLY B  84      31.627 115.968  50.397  1.00 63.53           C  
ATOM   2577  O   GLY B  84      30.869 115.421  51.202  1.00 63.45           O  
ATOM   2578  N   VAL B  85      32.501 116.916  50.738  1.00 63.43           N  
ATOM   2579  CA  VAL B  85      32.525 117.538  52.063  1.00 63.30           C  
ATOM   2580  C   VAL B  85      32.287 119.043  51.925  1.00 63.28           C  
ATOM   2581  O   VAL B  85      32.940 119.712  51.119  1.00 63.30           O  
ATOM   2582  CB  VAL B  85      33.866 117.320  52.810  1.00 63.25           C  
ATOM   2583  CG1 VAL B  85      33.640 117.310  54.317  1.00 63.26           C  
ATOM   2584  CG2 VAL B  85      34.561 116.044  52.358  1.00 63.12           C  
ATOM   2585  N   VAL B  86      31.349 119.565  52.711  1.00 63.17           N  
ATOM   2586  CA  VAL B  86      31.004 120.986  52.671  1.00 63.10           C  
ATOM   2587  C   VAL B  86      31.409 121.677  53.975  1.00 63.05           C  
ATOM   2588  O   VAL B  86      31.190 121.143  55.067  1.00 63.09           O  
ATOM   2589  CB  VAL B  86      29.493 121.216  52.382  1.00 63.11           C  
ATOM   2590  CG1 VAL B  86      29.240 122.647  51.935  1.00 63.13           C  
ATOM   2591  CG2 VAL B  86      28.975 120.238  51.328  1.00 63.07           C  
ATOM   2592  N   THR B  87      31.992 122.867  53.852  1.00 62.93           N  
ATOM   2593  CA  THR B  87      32.540 123.583  55.000  1.00 62.83           C  
ATOM   2594  C   THR B  87      32.249 125.073  54.962  1.00 62.81           C  
ATOM   2595  O   THR B  87      32.308 125.698  53.904  1.00 62.87           O  
ATOM   2596  CB  THR B  87      34.060 123.373  55.078  1.00 62.81           C  
ATOM   2597  OG1 THR B  87      34.549 122.903  53.814  1.00 62.78           O  
ATOM   2598  CG2 THR B  87      34.384 122.241  56.024  1.00 62.91           C  
ATOM   2599  N   LYS B  88      31.942 125.633  56.128  1.00 62.80           N  
ATOM   2600  CA  LYS B  88      31.794 127.073  56.288  1.00 62.86           C  
ATOM   2601  C   LYS B  88      33.178 127.707  56.212  1.00 62.99           C  
ATOM   2602  O   LYS B  88      34.068 127.351  56.984  1.00 63.05           O  
ATOM   2603  CB  LYS B  88      31.130 127.390  57.631  1.00 62.81           C  
ATOM   2604  CG  LYS B  88      30.326 128.683  57.653  1.00 62.86           C  
ATOM   2605  CD  LYS B  88      30.230 129.255  59.061  1.00 62.74           C  
ATOM   2606  CE  LYS B  88      28.883 128.952  59.702  1.00 62.81           C  
ATOM   2607  NZ  LYS B  88      28.325 130.131  60.434  1.00 63.09           N  
ATOM   2608  N   VAL B  89      33.366 128.617  55.259  1.00 63.18           N  
ATOM   2609  CA  VAL B  89      34.652 129.297  55.075  1.00 63.40           C  
ATOM   2610  C   VAL B  89      34.476 130.800  54.845  1.00 63.61           C  
ATOM   2611  O   VAL B  89      33.378 131.262  54.532  1.00 63.76           O  
ATOM   2612  CB  VAL B  89      35.501 128.689  53.912  1.00 63.39           C  
ATOM   2613  CG1 VAL B  89      35.808 127.210  54.152  1.00 63.46           C  
ATOM   2614  CG2 VAL B  89      34.831 128.903  52.558  1.00 63.32           C  
ATOM   2615  N   GLN B  90      35.564 131.552  55.011  1.00 63.76           N  
ATOM   2616  CA  GLN B  90      35.575 132.988  54.749  1.00 63.85           C  
ATOM   2617  C   GLN B  90      36.530 133.297  53.608  1.00 63.93           C  
ATOM   2618  O   GLN B  90      37.603 132.694  53.512  1.00 63.94           O  
ATOM   2619  CB  GLN B  90      35.994 133.766  56.000  1.00 63.82           C  
ATOM   2620  CG  GLN B  90      35.658 135.254  55.957  1.00 64.12           C  
ATOM   2621  CD  GLN B  90      35.380 135.836  57.333  1.00 64.48           C  
ATOM   2622  OE1 GLN B  90      34.284 135.670  57.875  1.00 64.55           O  
ATOM   2623  NE2 GLN B  90      36.368 136.520  57.900  1.00 64.50           N  
ATOM   2624  N   HIS B  91      36.130 134.227  52.743  1.00 63.96           N  
ATOM   2625  CA  HIS B  91      37.002 134.718  51.683  1.00 64.00           C  
ATOM   2626  C   HIS B  91      37.891 135.842  52.215  1.00 64.16           C  
ATOM   2627  O   HIS B  91      37.446 136.667  53.015  1.00 64.21           O  
ATOM   2628  CB  HIS B  91      36.179 135.198  50.489  1.00 63.85           C  
ATOM   2629  CG  HIS B  91      36.919 135.154  49.188  1.00 63.92           C  
ATOM   2630  ND1 HIS B  91      36.754 136.107  48.206  1.00 64.01           N  
ATOM   2631  CD2 HIS B  91      37.830 134.274  48.708  1.00 63.79           C  
ATOM   2632  CE1 HIS B  91      37.529 135.814  47.176  1.00 63.92           C  
ATOM   2633  NE2 HIS B  91      38.195 134.708  47.456  1.00 63.62           N  
ATOM   2634  N   ARG B  92      39.151 135.858  51.785  1.00 64.40           N  
ATOM   2635  CA  ARG B  92      40.096 136.901  52.191  1.00 64.63           C  
ATOM   2636  C   ARG B  92      39.661 138.299  51.715  1.00 64.57           C  
ATOM   2637  O   ARG B  92      39.381 139.158  52.554  1.00 64.60           O  
ATOM   2638  CB  ARG B  92      41.536 136.571  51.741  1.00 64.75           C  
ATOM   2639  CG  ARG B  92      42.643 137.375  52.450  1.00 65.38           C  
ATOM   2640  CD  ARG B  92      43.176 138.578  51.650  1.00 66.38           C  
ATOM   2641  NE  ARG B  92      44.423 139.135  52.193  1.00 67.11           N  
ATOM   2642  CZ  ARG B  92      44.501 140.184  53.018  1.00 67.37           C  
ATOM   2643  NH1 ARG B  92      43.401 140.811  53.425  1.00 67.39           N  
ATOM   2644  NH2 ARG B  92      45.687 140.607  53.444  1.00 67.06           N  
ATOM   2645  N   PRO B  93      39.576 138.522  50.395  1.00 64.54           N  
ATOM   2646  CA  PRO B  93      39.315 139.865  49.852  1.00 64.48           C  
ATOM   2647  C   PRO B  93      38.057 140.511  50.421  1.00 64.34           C  
ATOM   2648  O   PRO B  93      38.086 141.699  50.751  1.00 64.42           O  
ATOM   2649  CB  PRO B  93      39.143 139.614  48.350  1.00 64.51           C  
ATOM   2650  CG  PRO B  93      39.897 138.365  48.091  1.00 64.70           C  
ATOM   2651  CD  PRO B  93      39.705 137.523  49.316  1.00 64.57           C  
ATOM   2652  N   SER B  94      36.981 139.739  50.533  1.00 64.10           N  
ATOM   2653  CA  SER B  94      35.735 140.235  51.098  1.00 63.95           C  
ATOM   2654  C   SER B  94      35.267 139.287  52.180  1.00 63.77           C  
ATOM   2655  O   SER B  94      35.172 138.081  51.954  1.00 63.84           O  
ATOM   2656  CB  SER B  94      34.663 140.376  50.016  1.00 64.00           C  
ATOM   2657  OG  SER B  94      35.145 141.122  48.911  1.00 63.99           O  
ATOM   2658  N   GLY B  95      34.973 139.840  53.353  1.00 63.61           N  
ATOM   2659  CA  GLY B  95      34.605 139.046  54.514  1.00 63.48           C  
ATOM   2660  C   GLY B  95      33.256 138.363  54.388  1.00 63.29           C  
ATOM   2661  O   GLY B  95      32.342 138.618  55.178  1.00 63.39           O  
ATOM   2662  N   LEU B  96      33.140 137.485  53.396  1.00 62.99           N  
ATOM   2663  CA  LEU B  96      31.888 136.794  53.119  1.00 62.65           C  
ATOM   2664  C   LEU B  96      31.952 135.339  53.554  1.00 62.41           C  
ATOM   2665  O   LEU B  96      32.855 134.593  53.153  1.00 62.41           O  
ATOM   2666  CB  LEU B  96      31.544 136.880  51.630  1.00 62.62           C  
ATOM   2667  CG  LEU B  96      30.865 138.162  51.152  1.00 62.57           C  
ATOM   2668  CD1 LEU B  96      31.195 138.399  49.690  1.00 62.57           C  
ATOM   2669  CD2 LEU B  96      29.355 138.105  51.371  1.00 62.54           C  
ATOM   2670  N   ILE B  97      30.996 134.944  54.386  1.00 62.00           N  
ATOM   2671  CA  ILE B  97      30.850 133.546  54.754  1.00 61.66           C  
ATOM   2672  C   ILE B  97      30.165 132.804  53.609  1.00 61.49           C  
ATOM   2673  O   ILE B  97      29.003 133.066  53.289  1.00 61.57           O  
ATOM   2674  CB  ILE B  97      30.058 133.382  56.070  1.00 61.63           C  
ATOM   2675  CG1 ILE B  97      29.792 134.735  56.735  1.00 61.55           C  
ATOM   2676  CG2 ILE B  97      30.795 132.448  57.012  1.00 61.66           C  
ATOM   2677  CD1 ILE B  97      28.320 135.050  56.901  1.00 61.32           C  
ATOM   2678  N   MET B  98      30.909 131.903  52.976  1.00 61.19           N  
ATOM   2679  CA  MET B  98      30.380 131.068  51.903  1.00 60.89           C  
ATOM   2680  C   MET B  98      30.672 129.597  52.172  1.00 60.85           C  
ATOM   2681  O   MET B  98      31.734 129.257  52.687  1.00 61.01           O  
ATOM   2682  CB  MET B  98      30.962 131.485  50.549  1.00 60.79           C  
ATOM   2683  CG  MET B  98      32.440 131.833  50.550  1.00 60.18           C  
ATOM   2684  SD  MET B  98      32.781 133.229  49.463  1.00 59.82           S  
ATOM   2685  CE  MET B  98      33.445 132.408  48.037  1.00 59.40           C  
ATOM   2686  N   ALA B  99      29.729 128.726  51.827  1.00 60.67           N  
ATOM   2687  CA  ALA B  99      29.931 127.291  51.986  1.00 60.53           C  
ATOM   2688  C   ALA B  99      30.819 126.735  50.875  1.00 60.50           C  
ATOM   2689  O   ALA B  99      30.618 127.031  49.694  1.00 60.48           O  
ATOM   2690  CB  ALA B  99      28.606 126.568  52.023  1.00 60.54           C  
ATOM   2691  N   ARG B 100      31.801 125.931  51.272  1.00 60.48           N  
ATOM   2692  CA  ARG B 100      32.773 125.362  50.348  1.00 60.45           C  
ATOM   2693  C   ARG B 100      32.506 123.885  50.122  1.00 60.38           C  
ATOM   2694  O   ARG B 100      32.508 123.099  51.067  1.00 60.30           O  
ATOM   2695  CB  ARG B 100      34.188 125.549  50.896  1.00 60.53           C  
ATOM   2696  CG  ARG B 100      35.233 125.795  49.828  1.00 60.71           C  
ATOM   2697  CD  ARG B 100      36.383 124.811  49.846  1.00 60.62           C  
ATOM   2698  NE  ARG B 100      37.467 125.261  48.979  1.00 61.09           N  
ATOM   2699  CZ  ARG B 100      38.753 124.997  49.175  1.00 61.64           C  
ATOM   2700  NH1 ARG B 100      39.140 124.267  50.215  1.00 61.98           N  
ATOM   2701  NH2 ARG B 100      39.659 125.460  48.323  1.00 61.54           N  
ATOM   2702  N   LYS B 101      32.282 123.512  48.866  1.00 60.46           N  
ATOM   2703  CA  LYS B 101      32.022 122.119  48.526  1.00 60.58           C  
ATOM   2704  C   LYS B 101      33.232 121.449  47.891  1.00 60.73           C  
ATOM   2705  O   LYS B 101      33.531 121.652  46.714  1.00 60.60           O  
ATOM   2706  CB  LYS B 101      30.790 121.979  47.630  1.00 60.55           C  
ATOM   2707  CG  LYS B 101      30.180 120.589  47.672  1.00 60.58           C  
ATOM   2708  CD  LYS B 101      28.664 120.628  47.574  1.00 60.65           C  
ATOM   2709  CE  LYS B 101      28.088 119.252  47.275  1.00 60.25           C  
ATOM   2710  NZ  LYS B 101      28.691 118.656  46.051  1.00 60.04           N  
ATOM   2711  N   LEU B 102      33.918 120.651  48.703  1.00 61.11           N  
ATOM   2712  CA  LEU B 102      35.050 119.849  48.270  1.00 61.48           C  
ATOM   2713  C   LEU B 102      34.529 118.580  47.626  1.00 61.79           C  
ATOM   2714  O   LEU B 102      33.790 117.826  48.257  1.00 61.87           O  
ATOM   2715  CB  LEU B 102      35.916 119.461  49.475  1.00 61.44           C  
ATOM   2716  CG  LEU B 102      36.783 120.465  50.244  1.00 61.49           C  
ATOM   2717  CD1 LEU B 102      37.629 121.316  49.305  1.00 61.73           C  
ATOM   2718  CD2 LEU B 102      35.956 121.336  51.191  1.00 61.33           C  
ATOM   2719  N   ILE B 103      34.906 118.346  46.373  1.00 62.22           N  
ATOM   2720  CA  ILE B 103      34.588 117.087  45.706  1.00 62.70           C  
ATOM   2721  C   ILE B 103      35.878 116.340  45.354  1.00 63.09           C  
ATOM   2722  O   ILE B 103      36.571 116.677  44.385  1.00 63.05           O  
ATOM   2723  CB  ILE B 103      33.665 117.316  44.478  1.00 62.69           C  
ATOM   2724  CG1 ILE B 103      32.250 117.664  44.946  1.00 62.87           C  
ATOM   2725  CG2 ILE B 103      33.592 116.075  43.594  1.00 62.70           C  
ATOM   2726  CD1 ILE B 103      31.834 119.086  44.642  1.00 63.48           C  
ATOM   2727  N   HIS B 104      36.191 115.339  46.178  1.00 63.62           N  
ATOM   2728  CA  HIS B 104      37.403 114.525  46.044  1.00 64.10           C  
ATOM   2729  C   HIS B 104      37.285 113.559  44.869  1.00 64.25           C  
ATOM   2730  O   HIS B 104      36.429 112.668  44.868  1.00 64.31           O  
ATOM   2731  CB  HIS B 104      37.689 113.761  47.343  1.00 64.18           C  
ATOM   2732  CG  HIS B 104      36.463 113.431  48.140  1.00 64.72           C  
ATOM   2733  ND1 HIS B 104      36.162 114.050  49.335  1.00 65.21           N  
ATOM   2734  CD2 HIS B 104      35.463 112.544  47.914  1.00 65.09           C  
ATOM   2735  CE1 HIS B 104      35.030 113.559  49.810  1.00 65.41           C  
ATOM   2736  NE2 HIS B 104      34.587 112.643  48.968  1.00 65.43           N  
ATOM   2737  N   LEU B 105      38.147 113.745  43.871  1.00 64.42           N  
ATOM   2738  CA  LEU B 105      37.994 113.060  42.592  1.00 64.61           C  
ATOM   2739  C   LEU B 105      39.316 112.782  41.877  1.00 64.74           C  
ATOM   2740  O   LEU B 105      40.349 113.385  42.184  1.00 64.68           O  
ATOM   2741  CB  LEU B 105      37.058 113.863  41.677  1.00 64.61           C  
ATOM   2742  CG  LEU B 105      35.948 113.103  40.941  1.00 64.76           C  
ATOM   2743  CD1 LEU B 105      34.756 112.809  41.853  1.00 64.74           C  
ATOM   2744  CD2 LEU B 105      35.504 113.881  39.704  1.00 64.83           C  
ATOM   2745  N   GLU B 106      39.258 111.862  40.917  1.00 64.93           N  
ATOM   2746  CA  GLU B 106      40.412 111.498  40.105  1.00 65.04           C  
ATOM   2747  C   GLU B 106      40.079 111.517  38.609  1.00 65.04           C  
ATOM   2748  O   GLU B 106      39.400 110.620  38.094  1.00 64.97           O  
ATOM   2749  CB  GLU B 106      40.943 110.125  40.521  1.00 65.07           C  
ATOM   2750  CG  GLU B 106      42.344 109.812  40.012  1.00 65.16           C  
ATOM   2751  CD  GLU B 106      42.401 108.579  39.126  1.00 65.15           C  
ATOM   2752  OE1 GLU B 106      43.469 108.341  38.521  1.00 65.13           O  
ATOM   2753  OE2 GLU B 106      41.389 107.848  39.035  1.00 65.20           O  
ATOM   2754  N   ILE B 107      40.559 112.551  37.923  1.00 65.04           N  
ATOM   2755  CA  ILE B 107      40.398 112.661  36.476  1.00 65.04           C  
ATOM   2756  C   ILE B 107      41.584 113.369  35.817  1.00 64.90           C  
ATOM   2757  O   ILE B 107      42.186 114.281  36.404  1.00 64.86           O  
ATOM   2758  CB  ILE B 107      39.014 113.310  36.103  1.00 65.19           C  
ATOM   2759  CG1 ILE B 107      38.133 112.322  35.308  1.00 65.26           C  
ATOM   2760  CG2 ILE B 107      39.168 114.680  35.404  1.00 65.12           C  
ATOM   2761  CD1 ILE B 107      38.819 111.594  34.144  1.00 65.06           C  
ATOM   2762  N   LYS B 108      41.900 112.929  34.598  1.00 64.69           N  
ATOM   2763  CA  LYS B 108      43.023 113.433  33.804  1.00 64.34           C  
ATOM   2764  C   LYS B 108      43.098 114.967  33.776  1.00 64.91           C  
ATOM   2765  O   LYS B 108      42.058 115.632  33.741  1.00 64.93           O  
ATOM   2766  CB  LYS B 108      42.918 112.887  32.372  1.00 63.82           C  
ATOM   2767  CG  LYS B 108      44.252 112.500  31.725  1.00 61.14           C  
ATOM   2768  CD  LYS B 108      44.064 112.125  30.250  1.00 56.72           C  
ATOM   2769  CE  LYS B 108      45.145 112.737  29.352  1.00 53.95           C  
ATOM   2770  NZ  LYS B 108      44.848 112.544  27.895  1.00 51.36           N  
ATOM   2771  N   PRO B 109      44.314 115.527  33.823  1.00 65.38           N  
ATOM   2772  CA  PRO B 109      44.520 116.953  33.528  1.00 65.73           C  
ATOM   2773  C   PRO B 109      44.183 117.272  32.064  1.00 66.03           C  
ATOM   2774  O   PRO B 109      45.076 117.459  31.227  1.00 66.10           O  
ATOM   2775  CB  PRO B 109      46.013 117.173  33.827  1.00 65.68           C  
ATOM   2776  CG  PRO B 109      46.629 115.827  33.742  1.00 65.67           C  
ATOM   2777  CD  PRO B 109      45.574 114.860  34.204  1.00 65.51           C  
ATOM   2778  N   ALA B 110      42.880 117.319  31.781  1.00 66.35           N  
ATOM   2779  CA  ALA B 110      42.343 117.544  30.439  1.00 66.61           C  
ATOM   2780  C   ALA B 110      40.861 117.914  30.513  1.00 66.73           C  
ATOM   2781  O   ALA B 110      40.444 118.942  29.965  1.00 66.76           O  
ATOM   2782  CB  ALA B 110      42.544 116.303  29.557  1.00 66.67           C  
ATOM   2783  N   ILE B 111      40.075 117.076  31.193  1.00 66.82           N  
ATOM   2784  CA  ILE B 111      38.633 117.308  31.341  1.00 66.90           C  
ATOM   2785  C   ILE B 111      38.229 117.857  32.716  1.00 66.85           C  
ATOM   2786  O   ILE B 111      37.059 118.170  32.945  1.00 66.77           O  
ATOM   2787  CB  ILE B 111      37.796 116.044  30.966  1.00 66.93           C  
ATOM   2788  CG1 ILE B 111      38.132 114.856  31.874  1.00 66.82           C  
ATOM   2789  CG2 ILE B 111      37.965 115.697  29.481  1.00 67.17           C  
ATOM   2790  CD1 ILE B 111      36.918 114.042  32.268  1.00 66.98           C  
ATOM   2791  N   ARG B 112      39.203 117.968  33.619  1.00 66.82           N  
ATOM   2792  CA  ARG B 112      39.009 118.652  34.899  1.00 66.76           C  
ATOM   2793  C   ARG B 112      38.763 120.137  34.641  1.00 66.48           C  
ATOM   2794  O   ARG B 112      38.015 120.791  35.370  1.00 66.43           O  
ATOM   2795  CB  ARG B 112      40.214 118.450  35.830  1.00 66.91           C  
ATOM   2796  CG  ARG B 112      41.577 118.718  35.184  1.00 67.55           C  
ATOM   2797  CD  ARG B 112      42.465 119.714  35.933  1.00 68.48           C  
ATOM   2798  NE  ARG B 112      41.822 121.013  36.150  1.00 69.11           N  
ATOM   2799  CZ  ARG B 112      41.959 122.076  35.359  1.00 69.61           C  
ATOM   2800  NH1 ARG B 112      42.715 122.021  34.269  1.00 69.81           N  
ATOM   2801  NH2 ARG B 112      41.331 123.205  35.659  1.00 70.07           N  
ATOM   2802  N   ASN B 113      39.409 120.653  33.598  1.00 66.20           N  
ATOM   2803  CA  ASN B 113      39.097 121.970  33.063  1.00 66.01           C  
ATOM   2804  C   ASN B 113      37.694 121.947  32.465  1.00 65.67           C  
ATOM   2805  O   ASN B 113      36.888 122.841  32.732  1.00 65.73           O  
ATOM   2806  CB  ASN B 113      40.123 122.383  32.000  1.00 66.14           C  
ATOM   2807  CG  ASN B 113      40.611 123.814  32.177  1.00 66.53           C  
ATOM   2808  OD1 ASN B 113      41.664 124.054  32.774  1.00 67.18           O  
ATOM   2809  ND2 ASN B 113      39.851 124.772  31.650  1.00 66.58           N  
ATOM   2810  N   GLN B 114      37.410 120.905  31.680  1.00 65.10           N  
ATOM   2811  CA  GLN B 114      36.107 120.726  31.033  1.00 64.46           C  
ATOM   2812  C   GLN B 114      34.968 120.576  32.041  1.00 63.87           C  
ATOM   2813  O   GLN B 114      33.828 120.929  31.745  1.00 63.83           O  
ATOM   2814  CB  GLN B 114      36.131 119.524  30.084  1.00 64.55           C  
ATOM   2815  CG  GLN B 114      35.967 119.879  28.608  1.00 64.66           C  
ATOM   2816  CD  GLN B 114      34.521 120.142  28.215  1.00 64.67           C  
ATOM   2817  OE1 GLN B 114      34.222 121.154  27.575  1.00 64.93           O  
ATOM   2818  NE2 GLN B 114      33.624 119.234  28.591  1.00 64.32           N  
ATOM   2819  N   ILE B 115      35.283 120.048  33.222  1.00 63.12           N  
ATOM   2820  CA  ILE B 115      34.318 119.967  34.315  1.00 62.38           C  
ATOM   2821  C   ILE B 115      34.103 121.347  34.939  1.00 61.83           C  
ATOM   2822  O   ILE B 115      32.974 121.717  35.258  1.00 61.80           O  
ATOM   2823  CB  ILE B 115      34.748 118.895  35.357  1.00 62.39           C  
ATOM   2824  CG1 ILE B 115      33.998 117.588  35.097  1.00 62.40           C  
ATOM   2825  CG2 ILE B 115      34.508 119.359  36.796  1.00 62.28           C  
ATOM   2826  CD1 ILE B 115      34.892 116.430  34.729  1.00 62.51           C  
ATOM   2827  N   ILE B 116      35.185 122.107  35.086  1.00 61.15           N  
ATOM   2828  CA  ILE B 116      35.109 123.477  35.582  1.00 60.55           C  
ATOM   2829  C   ILE B 116      34.371 124.362  34.571  1.00 60.15           C  
ATOM   2830  O   ILE B 116      33.517 125.167  34.949  1.00 60.08           O  
ATOM   2831  CB  ILE B 116      36.533 124.011  35.921  1.00 60.57           C  
ATOM   2832  CG1 ILE B 116      36.755 124.017  37.436  1.00 60.55           C  
ATOM   2833  CG2 ILE B 116      36.781 125.406  35.349  1.00 60.62           C  
ATOM   2834  CD1 ILE B 116      37.862 123.097  37.884  1.00 60.35           C  
ATOM   2835  N   ARG B 117      34.690 124.176  33.290  1.00 59.61           N  
ATOM   2836  CA  ARG B 117      34.083 124.929  32.193  1.00 59.02           C  
ATOM   2837  C   ARG B 117      32.565 124.775  32.165  1.00 58.54           C  
ATOM   2838  O   ARG B 117      31.840 125.755  31.979  1.00 58.55           O  
ATOM   2839  CB  ARG B 117      34.669 124.477  30.852  1.00 59.06           C  
ATOM   2840  CG  ARG B 117      35.845 125.309  30.362  0.50 59.15           C  
ATOM   2841  CD  ARG B 117      37.097 124.503  30.024  0.50 59.22           C  
ATOM   2842  NE  ARG B 117      36.868 123.484  28.999  0.50 59.30           N  
ATOM   2843  CZ  ARG B 117      37.209 123.611  27.720  0.50 59.48           C  
ATOM   2844  NH1 ARG B 117      37.798 124.719  27.284  0.50 59.44           N  
ATOM   2845  NH2 ARG B 117      36.958 122.624  26.868  0.50 59.48           N  
ATOM   2846  N   GLU B 118      32.095 123.543  32.355  1.00 57.93           N  
ATOM   2847  CA  GLU B 118      30.665 123.238  32.337  1.00 57.24           C  
ATOM   2848  C   GLU B 118      29.975 123.723  33.611  1.00 56.61           C  
ATOM   2849  O   GLU B 118      28.777 124.013  33.602  1.00 56.52           O  
ATOM   2850  CB  GLU B 118      30.426 121.740  32.102  1.00 57.24           C  
ATOM   2851  CG  GLU B 118      30.764 121.288  30.683  1.00 57.57           C  
ATOM   2852  CD  GLU B 118      30.148 119.949  30.302  1.00 58.23           C  
ATOM   2853  OE1 GLU B 118      30.192 119.007  31.126  1.00 58.26           O  
ATOM   2854  OE2 GLU B 118      29.625 119.835  29.168  1.00 58.29           O  
ATOM   2855  N   LEU B 119      30.749 123.830  34.690  1.00 55.84           N  
ATOM   2856  CA  LEU B 119      30.257 124.349  35.965  1.00 55.16           C  
ATOM   2857  C   LEU B 119      30.152 125.877  35.974  1.00 54.73           C  
ATOM   2858  O   LEU B 119      29.597 126.459  36.911  1.00 54.73           O  
ATOM   2859  CB  LEU B 119      31.159 123.894  37.118  1.00 55.06           C  
ATOM   2860  CG  LEU B 119      30.869 122.555  37.795  1.00 54.81           C  
ATOM   2861  CD1 LEU B 119      32.132 122.029  38.454  1.00 55.13           C  
ATOM   2862  CD2 LEU B 119      29.772 122.692  38.821  1.00 54.61           C  
ATOM   2863  N   GLN B 120      30.684 126.519  34.936  1.00 54.08           N  
ATOM   2864  CA  GLN B 120      30.719 127.980  34.873  1.00 53.41           C  
ATOM   2865  C   GLN B 120      29.357 128.595  34.535  1.00 52.91           C  
ATOM   2866  O   GLN B 120      29.135 129.787  34.769  1.00 52.92           O  
ATOM   2867  CB  GLN B 120      31.800 128.468  33.893  1.00 53.45           C  
ATOM   2868  CG  GLN B 120      33.250 128.206  34.335  1.00 53.26           C  
ATOM   2869  CD  GLN B 120      33.567 128.727  35.732  1.00 53.04           C  
ATOM   2870  OE1 GLN B 120      33.731 129.931  35.928  1.00 53.21           O  
ATOM   2871  NE2 GLN B 120      33.659 127.821  36.700  1.00 52.48           N  
ATOM   2872  N   VAL B 121      28.449 127.781  33.999  1.00 52.13           N  
ATOM   2873  CA  VAL B 121      27.095 128.237  33.678  1.00 51.37           C  
ATOM   2874  C   VAL B 121      26.265 128.475  34.941  1.00 50.77           C  
ATOM   2875  O   VAL B 121      25.160 129.013  34.880  1.00 50.71           O  
ATOM   2876  CB  VAL B 121      26.346 127.267  32.711  1.00 51.44           C  
ATOM   2877  CG1 VAL B 121      27.140 127.055  31.427  1.00 51.52           C  
ATOM   2878  CG2 VAL B 121      26.024 125.934  33.385  1.00 51.51           C  
ATOM   2879  N   LEU B 122      26.807 128.068  36.084  1.00 50.09           N  
ATOM   2880  CA  LEU B 122      26.156 128.296  37.365  1.00 49.55           C  
ATOM   2881  C   LEU B 122      26.163 129.783  37.685  1.00 49.18           C  
ATOM   2882  O   LEU B 122      25.273 130.287  38.373  1.00 49.21           O  
ATOM   2883  CB  LEU B 122      26.858 127.511  38.470  1.00 49.53           C  
ATOM   2884  CG  LEU B 122      26.251 126.177  38.902  1.00 49.39           C  
ATOM   2885  CD1 LEU B 122      27.341 125.277  39.432  1.00 49.26           C  
ATOM   2886  CD2 LEU B 122      25.170 126.382  39.952  1.00 49.22           C  
ATOM   2887  N   HIS B 123      27.175 130.476  37.169  1.00 48.67           N  
ATOM   2888  CA  HIS B 123      27.259 131.928  37.251  1.00 48.19           C  
ATOM   2889  C   HIS B 123      26.062 132.571  36.552  1.00 47.85           C  
ATOM   2890  O   HIS B 123      25.637 133.671  36.920  1.00 47.82           O  
ATOM   2891  CB  HIS B 123      28.559 132.418  36.609  1.00 48.25           C  
ATOM   2892  CG  HIS B 123      29.746 132.376  37.522  1.00 48.21           C  
ATOM   2893  ND1 HIS B 123      31.008 132.037  37.083  1.00 48.02           N  
ATOM   2894  CD2 HIS B 123      29.867 132.641  38.845  1.00 48.26           C  
ATOM   2895  CE1 HIS B 123      31.854 132.090  38.096  1.00 48.17           C  
ATOM   2896  NE2 HIS B 123      31.187 132.453  39.177  1.00 48.30           N  
ATOM   2897  N   GLU B 124      25.532 131.873  35.546  1.00 47.35           N  
ATOM   2898  CA  GLU B 124      24.356 132.315  34.801  1.00 46.98           C  
ATOM   2899  C   GLU B 124      23.039 131.928  35.495  1.00 46.58           C  
ATOM   2900  O   GLU B 124      21.958 132.375  35.087  1.00 46.67           O  
ATOM   2901  CB  GLU B 124      24.389 131.765  33.372  1.00 47.00           C  
ATOM   2902  CG  GLU B 124      25.290 132.540  32.423  1.00 47.71           C  
ATOM   2903  CD  GLU B 124      26.182 131.633  31.588  1.00 48.97           C  
ATOM   2904  OE1 GLU B 124      25.709 131.107  30.553  1.00 49.48           O  
ATOM   2905  OE2 GLU B 124      27.361 131.445  31.963  1.00 49.43           O  
ATOM   2906  N   CYS B 125      23.135 131.109  36.542  1.00 45.86           N  
ATOM   2907  CA  CYS B 125      21.964 130.699  37.313  1.00 45.10           C  
ATOM   2908  C   CYS B 125      21.709 131.646  38.478  1.00 44.85           C  
ATOM   2909  O   CYS B 125      22.403 131.595  39.497  1.00 45.07           O  
ATOM   2910  CB  CYS B 125      22.128 129.268  37.824  1.00 45.01           C  
ATOM   2911  SG  CYS B 125      22.011 128.026  36.532  1.00 43.89           S  
ATOM   2912  N   ASN B 126      20.714 132.514  38.316  1.00 44.30           N  
ATOM   2913  CA  ASN B 126      20.332 133.464  39.357  1.00 43.73           C  
ATOM   2914  C   ASN B 126      18.819 133.516  39.579  1.00 43.16           C  
ATOM   2915  O   ASN B 126      18.064 134.024  38.743  1.00 42.99           O  
ATOM   2916  CB  ASN B 126      20.884 134.871  39.062  1.00 43.92           C  
ATOM   2917  CG  ASN B 126      22.287 134.847  38.452  1.00 44.23           C  
ATOM   2918  OD1 ASN B 126      23.247 134.382  39.076  1.00 44.64           O  
ATOM   2919  ND2 ASN B 126      22.407 135.358  37.229  1.00 44.43           N  
ATOM   2920  N   SER B 127      18.394 132.974  40.714  1.00 42.53           N  
ATOM   2921  CA  SER B 127      17.005 133.016  41.153  1.00 42.01           C  
ATOM   2922  C   SER B 127      16.974 132.926  42.677  1.00 41.71           C  
ATOM   2923  O   SER B 127      17.786 132.212  43.267  1.00 41.94           O  
ATOM   2924  CB  SER B 127      16.217 131.854  40.538  1.00 42.07           C  
ATOM   2925  OG  SER B 127      14.960 131.674  41.173  1.00 41.98           O  
ATOM   2926  N   PRO B 128      16.059 133.644  43.326  1.00 41.25           N  
ATOM   2927  CA  PRO B 128      15.905 133.555  44.783  1.00 41.00           C  
ATOM   2928  C   PRO B 128      15.534 132.163  45.298  1.00 40.70           C  
ATOM   2929  O   PRO B 128      15.357 131.999  46.503  1.00 40.66           O  
ATOM   2930  CB  PRO B 128      14.784 134.559  45.080  1.00 40.92           C  
ATOM   2931  CG  PRO B 128      14.088 134.743  43.806  1.00 40.97           C  
ATOM   2932  CD  PRO B 128      15.132 134.626  42.744  1.00 41.36           C  
ATOM   2933  N   TYR B 129      15.432 131.186  44.400  1.00 40.57           N  
ATOM   2934  CA  TYR B 129      15.122 129.803  44.764  1.00 40.44           C  
ATOM   2935  C   TYR B 129      16.242 128.849  44.384  1.00 40.31           C  
ATOM   2936  O   TYR B 129      16.219 127.682  44.757  1.00 40.18           O  
ATOM   2937  CB  TYR B 129      13.826 129.345  44.094  1.00 40.52           C  
ATOM   2938  CG  TYR B 129      12.654 130.260  44.322  1.00 40.57           C  
ATOM   2939  CD1 TYR B 129      12.055 130.928  43.260  1.00 40.52           C  
ATOM   2940  CD2 TYR B 129      12.144 130.458  45.602  1.00 40.84           C  
ATOM   2941  CE1 TYR B 129      10.973 131.770  43.468  1.00 41.09           C  
ATOM   2942  CE2 TYR B 129      11.069 131.300  45.820  1.00 41.17           C  
ATOM   2943  CZ  TYR B 129      10.487 131.950  44.751  1.00 41.33           C  
ATOM   2944  OH  TYR B 129       9.416 132.780  44.971  1.00 42.45           O  
ATOM   2945  N   ILE B 130      17.200 129.339  43.608  1.00 40.29           N  
ATOM   2946  CA  ILE B 130      18.397 128.577  43.307  1.00 40.46           C  
ATOM   2947  C   ILE B 130      19.499 129.140  44.183  1.00 40.76           C  
ATOM   2948  O   ILE B 130      19.647 130.356  44.288  1.00 40.95           O  
ATOM   2949  CB  ILE B 130      18.756 128.685  41.808  1.00 40.34           C  
ATOM   2950  CG1 ILE B 130      17.774 127.881  40.937  1.00 40.41           C  
ATOM   2951  CG2 ILE B 130      20.204 128.273  41.549  1.00 40.25           C  
ATOM   2952  CD1 ILE B 130      17.461 126.461  41.406  1.00 40.35           C  
ATOM   2953  N   VAL B 131      20.252 128.252  44.828  1.00 41.05           N  
ATOM   2954  CA  VAL B 131      21.339 128.646  45.721  1.00 41.23           C  
ATOM   2955  C   VAL B 131      22.392 129.440  44.950  1.00 41.45           C  
ATOM   2956  O   VAL B 131      22.757 129.083  43.830  1.00 41.36           O  
ATOM   2957  CB  VAL B 131      21.962 127.411  46.430  1.00 41.22           C  
ATOM   2958  CG1 VAL B 131      23.355 127.708  46.969  1.00 41.30           C  
ATOM   2959  CG2 VAL B 131      21.063 126.938  47.554  1.00 41.04           C  
ATOM   2960  N   GLY B 132      22.850 130.533  45.551  1.00 41.81           N  
ATOM   2961  CA  GLY B 132      23.850 131.384  44.938  1.00 42.41           C  
ATOM   2962  C   GLY B 132      25.158 130.652  44.753  1.00 42.79           C  
ATOM   2963  O   GLY B 132      25.594 129.935  45.645  1.00 42.74           O  
ATOM   2964  N   PHE B 133      25.775 130.838  43.590  1.00 43.27           N  
ATOM   2965  CA  PHE B 133      27.043 130.204  43.261  1.00 43.73           C  
ATOM   2966  C   PHE B 133      28.136 131.263  43.134  1.00 44.20           C  
ATOM   2967  O   PHE B 133      28.073 132.110  42.248  1.00 44.34           O  
ATOM   2968  CB  PHE B 133      26.884 129.412  41.961  1.00 43.60           C  
ATOM   2969  CG  PHE B 133      28.176 128.928  41.368  1.00 43.56           C  
ATOM   2970  CD1 PHE B 133      28.725 129.564  40.258  1.00 43.54           C  
ATOM   2971  CD2 PHE B 133      28.832 127.821  41.898  1.00 43.50           C  
ATOM   2972  CE1 PHE B 133      29.915 129.115  39.692  1.00 43.32           C  
ATOM   2973  CE2 PHE B 133      30.024 127.367  41.341  1.00 43.42           C  
ATOM   2974  CZ  PHE B 133      30.564 128.015  40.234  1.00 43.40           C  
ATOM   2975  N   TYR B 134      29.127 131.218  44.024  1.00 44.92           N  
ATOM   2976  CA  TYR B 134      30.247 132.167  43.991  1.00 45.65           C  
ATOM   2977  C   TYR B 134      31.288 131.803  42.936  1.00 46.22           C  
ATOM   2978  O   TYR B 134      31.560 132.593  42.032  1.00 46.19           O  
ATOM   2979  CB  TYR B 134      30.918 132.293  45.362  1.00 45.55           C  
ATOM   2980  CG  TYR B 134      30.142 133.116  46.367  1.00 45.72           C  
ATOM   2981  CD1 TYR B 134      30.117 134.507  46.289  1.00 45.55           C  
ATOM   2982  CD2 TYR B 134      29.440 132.503  47.405  1.00 45.76           C  
ATOM   2983  CE1 TYR B 134      29.405 135.267  47.216  1.00 45.51           C  
ATOM   2984  CE2 TYR B 134      28.727 133.256  48.338  1.00 45.67           C  
ATOM   2985  CZ  TYR B 134      28.713 134.637  48.233  1.00 45.75           C  
ATOM   2986  OH  TYR B 134      28.012 135.392  49.147  1.00 46.20           O  
ATOM   2987  N   GLY B 135      31.872 130.613  43.052  1.00 47.07           N  
ATOM   2988  CA  GLY B 135      32.882 130.182  42.103  1.00 48.16           C  
ATOM   2989  C   GLY B 135      33.388 128.768  42.284  1.00 48.92           C  
ATOM   2990  O   GLY B 135      33.234 128.169  43.351  1.00 48.76           O  
ATOM   2991  N   ALA B 136      34.004 128.250  41.221  1.00 49.92           N  
ATOM   2992  CA  ALA B 136      34.522 126.883  41.179  1.00 51.02           C  
ATOM   2993  C   ALA B 136      35.899 126.812  40.522  1.00 51.82           C  
ATOM   2994  O   ALA B 136      36.163 127.495  39.528  1.00 51.96           O  
ATOM   2995  CB  ALA B 136      33.545 125.960  40.461  1.00 50.88           C  
ATOM   2996  N   PHE B 137      36.762 125.964  41.081  1.00 52.86           N  
ATOM   2997  CA  PHE B 137      38.155 125.849  40.646  1.00 53.79           C  
ATOM   2998  C   PHE B 137      38.744 124.460  40.904  1.00 54.53           C  
ATOM   2999  O   PHE B 137      38.139 123.641  41.607  1.00 54.58           O  
ATOM   3000  CB  PHE B 137      39.019 126.920  41.331  1.00 53.66           C  
ATOM   3001  CG  PHE B 137      38.967 126.883  42.836  1.00 53.41           C  
ATOM   3002  CD1 PHE B 137      37.891 127.431  43.525  1.00 53.11           C  
ATOM   3003  CD2 PHE B 137      40.006 126.317  43.565  1.00 53.47           C  
ATOM   3004  CE1 PHE B 137      37.844 127.409  44.912  1.00 53.07           C  
ATOM   3005  CE2 PHE B 137      39.967 126.289  44.957  1.00 53.46           C  
ATOM   3006  CZ  PHE B 137      38.884 126.839  45.629  1.00 53.22           C  
ATOM   3007  N   TYR B 138      39.919 124.208  40.321  1.00 55.40           N  
ATOM   3008  CA  TYR B 138      40.670 122.975  40.559  1.00 56.23           C  
ATOM   3009  C   TYR B 138      41.726 123.180  41.641  1.00 56.63           C  
ATOM   3010  O   TYR B 138      42.561 124.086  41.549  1.00 56.67           O  
ATOM   3011  CB  TYR B 138      41.333 122.472  39.271  1.00 56.32           C  
ATOM   3012  CG  TYR B 138      41.930 121.076  39.380  1.00 56.97           C  
ATOM   3013  CD1 TYR B 138      43.289 120.892  39.652  1.00 57.18           C  
ATOM   3014  CD2 TYR B 138      41.135 119.938  39.204  1.00 57.47           C  
ATOM   3015  CE1 TYR B 138      43.838 119.607  39.749  1.00 57.36           C  
ATOM   3016  CE2 TYR B 138      41.676 118.651  39.298  1.00 57.45           C  
ATOM   3017  CZ  TYR B 138      43.025 118.494  39.570  1.00 57.38           C  
ATOM   3018  OH  TYR B 138      43.558 117.226  39.663  1.00 57.33           O  
ATOM   3019  N   SER B 139      41.673 122.334  42.665  1.00 57.23           N  
ATOM   3020  CA  SER B 139      42.669 122.339  43.734  1.00 57.92           C  
ATOM   3021  C   SER B 139      43.448 121.024  43.732  1.00 58.23           C  
ATOM   3022  O   SER B 139      42.979 120.018  43.179  1.00 58.33           O  
ATOM   3023  CB  SER B 139      42.007 122.573  45.099  1.00 57.98           C  
ATOM   3024  OG  SER B 139      42.804 123.418  45.916  1.00 58.15           O  
ATOM   3025  N   ASP B 140      44.637 121.043  44.342  1.00 58.52           N  
ATOM   3026  CA  ASP B 140      45.511 119.870  44.398  1.00 58.79           C  
ATOM   3027  C   ASP B 140      44.862 118.748  45.213  1.00 58.74           C  
ATOM   3028  O   ASP B 140      45.097 118.615  46.420  1.00 58.70           O  
ATOM   3029  CB  ASP B 140      46.896 120.238  44.960  1.00 58.99           C  
ATOM   3030  CG  ASP B 140      48.015 120.124  43.914  1.00 59.51           C  
ATOM   3031  OD1 ASP B 140      48.028 119.140  43.136  1.00 59.86           O  
ATOM   3032  OD2 ASP B 140      48.932 120.972  43.802  1.00 60.00           O  
ATOM   3033  N   GLY B 141      44.031 117.959  44.533  1.00 58.69           N  
ATOM   3034  CA  GLY B 141      43.306 116.867  45.157  1.00 58.68           C  
ATOM   3035  C   GLY B 141      41.819 116.844  44.851  1.00 58.68           C  
ATOM   3036  O   GLY B 141      41.245 115.768  44.657  1.00 58.75           O  
ATOM   3037  N   GLU B 142      41.196 118.024  44.805  1.00 58.59           N  
ATOM   3038  CA  GLU B 142      39.736 118.137  44.687  1.00 58.41           C  
ATOM   3039  C   GLU B 142      39.278 119.366  43.897  1.00 58.02           C  
ATOM   3040  O   GLU B 142      40.042 120.320  43.729  1.00 58.01           O  
ATOM   3041  CB  GLU B 142      39.084 118.144  46.080  1.00 58.53           C  
ATOM   3042  CG  GLU B 142      39.799 119.005  47.120  1.00 59.32           C  
ATOM   3043  CD  GLU B 142      40.086 118.261  48.421  1.00 60.40           C  
ATOM   3044  OE1 GLU B 142      40.365 117.036  48.374  1.00 60.65           O  
ATOM   3045  OE2 GLU B 142      40.038 118.906  49.498  1.00 60.53           O  
ATOM   3046  N   ILE B 143      38.034 119.325  43.404  1.00 57.50           N  
ATOM   3047  CA  ILE B 143      37.387 120.501  42.807  1.00 56.82           C  
ATOM   3048  C   ILE B 143      36.416 121.129  43.798  1.00 56.40           C  
ATOM   3049  O   ILE B 143      35.525 120.464  44.334  1.00 56.28           O  
ATOM   3050  CB  ILE B 143      36.681 120.202  41.435  1.00 56.79           C  
ATOM   3051  CG1 ILE B 143      35.610 119.114  41.560  1.00 56.56           C  
ATOM   3052  CG2 ILE B 143      37.698 119.864  40.351  1.00 56.76           C  
ATOM   3053  CD1 ILE B 143      34.330 119.447  40.821  1.00 56.39           C  
ATOM   3054  N   SER B 144      36.611 122.416  44.049  1.00 55.89           N  
ATOM   3055  CA  SER B 144      35.789 123.128  45.007  1.00 55.44           C  
ATOM   3056  C   SER B 144      34.667 123.866  44.310  1.00 55.09           C  
ATOM   3057  O   SER B 144      34.831 124.353  43.191  1.00 55.13           O  
ATOM   3058  CB  SER B 144      36.635 124.113  45.808  1.00 55.47           C  
ATOM   3059  OG  SER B 144      37.172 123.497  46.961  1.00 55.50           O  
ATOM   3060  N   ILE B 145      33.520 123.927  44.973  1.00 54.57           N  
ATOM   3061  CA  ILE B 145      32.434 124.792  44.546  1.00 54.05           C  
ATOM   3062  C   ILE B 145      32.038 125.641  45.748  1.00 53.69           C  
ATOM   3063  O   ILE B 145      31.578 125.132  46.772  1.00 53.73           O  
ATOM   3064  CB  ILE B 145      31.249 123.968  43.962  1.00 54.08           C  
ATOM   3065  CG1 ILE B 145      31.559 123.543  42.522  1.00 54.11           C  
ATOM   3066  CG2 ILE B 145      29.954 124.767  43.975  1.00 53.93           C  
ATOM   3067  CD1 ILE B 145      31.372 122.063  42.247  1.00 54.16           C  
ATOM   3068  N   CYS B 146      32.261 126.940  45.627  1.00 53.20           N  
ATOM   3069  CA  CYS B 146      31.929 127.860  46.697  1.00 52.83           C  
ATOM   3070  C   CYS B 146      30.583 128.494  46.397  1.00 52.27           C  
ATOM   3071  O   CYS B 146      30.386 129.078  45.335  1.00 52.22           O  
ATOM   3072  CB  CYS B 146      33.021 128.917  46.842  1.00 53.01           C  
ATOM   3073  SG  CYS B 146      34.674 128.307  46.432  1.00 53.77           S  
ATOM   3074  N   MET B 147      29.654 128.359  47.334  1.00 51.66           N  
ATOM   3075  CA  MET B 147      28.287 128.809  47.124  1.00 51.20           C  
ATOM   3076  C   MET B 147      27.767 129.644  48.295  1.00 50.80           C  
ATOM   3077  O   MET B 147      28.383 129.684  49.359  1.00 50.73           O  
ATOM   3078  CB  MET B 147      27.372 127.603  46.851  1.00 51.32           C  
ATOM   3079  CG  MET B 147      27.103 126.709  48.057  1.00 51.59           C  
ATOM   3080  SD  MET B 147      26.242 125.180  47.643  1.00 52.05           S  
ATOM   3081  CE  MET B 147      27.297 123.984  48.430  1.00 51.94           C  
ATOM   3082  N   GLU B 148      26.638 130.315  48.079  1.00 50.33           N  
ATOM   3083  CA  GLU B 148      25.964 131.096  49.114  1.00 49.88           C  
ATOM   3084  C   GLU B 148      25.812 130.253  50.377  1.00 49.59           C  
ATOM   3085  O   GLU B 148      25.368 129.106  50.307  1.00 49.68           O  
ATOM   3086  CB  GLU B 148      24.587 131.547  48.611  1.00 49.88           C  
ATOM   3087  CG  GLU B 148      24.038 132.807  49.265  1.00 49.62           C  
ATOM   3088  CD  GLU B 148      22.531 132.760  49.482  1.00 49.35           C  
ATOM   3089  OE1 GLU B 148      22.081 133.153  50.581  1.00 49.50           O  
ATOM   3090  OE2 GLU B 148      21.794 132.341  48.558  1.00 48.67           O  
ATOM   3091  N   HIS B 149      26.197 130.811  51.523  1.00 49.11           N  
ATOM   3092  CA  HIS B 149      26.093 130.078  52.781  1.00 48.61           C  
ATOM   3093  C   HIS B 149      24.690 130.156  53.363  1.00 48.26           C  
ATOM   3094  O   HIS B 149      24.240 131.222  53.783  1.00 48.21           O  
ATOM   3095  CB  HIS B 149      27.120 130.558  53.808  1.00 48.60           C  
ATOM   3096  CG  HIS B 149      26.912 129.981  55.174  1.00 48.72           C  
ATOM   3097  ND1 HIS B 149      26.463 130.732  56.239  1.00 48.67           N  
ATOM   3098  CD2 HIS B 149      27.066 128.719  55.642  1.00 48.90           C  
ATOM   3099  CE1 HIS B 149      26.362 129.960  57.307  1.00 48.63           C  
ATOM   3100  NE2 HIS B 149      26.721 128.734  56.972  1.00 48.59           N  
ATOM   3101  N   MET B 150      24.013 129.012  53.387  1.00 47.94           N  
ATOM   3102  CA  MET B 150      22.676 128.908  53.962  1.00 47.68           C  
ATOM   3103  C   MET B 150      22.762 128.452  55.416  1.00 47.57           C  
ATOM   3104  O   MET B 150      23.115 127.306  55.707  1.00 47.49           O  
ATOM   3105  CB  MET B 150      21.793 127.967  53.133  1.00 47.61           C  
ATOM   3106  CG  MET B 150      21.686 128.340  51.646  1.00 47.55           C  
ATOM   3107  SD  MET B 150      20.759 129.864  51.276  1.00 46.70           S  
ATOM   3108  CE  MET B 150      19.081 129.331  51.586  1.00 46.47           C  
ATOM   3109  N   ASP B 151      22.434 129.373  56.318  1.00 47.47           N  
ATOM   3110  CA  ASP B 151      22.574 129.172  57.762  1.00 47.31           C  
ATOM   3111  C   ASP B 151      21.500 128.273  58.392  1.00 47.16           C  
ATOM   3112  O   ASP B 151      21.624 127.868  59.553  1.00 47.23           O  
ATOM   3113  CB  ASP B 151      22.627 130.528  58.480  1.00 47.39           C  
ATOM   3114  CG  ASP B 151      21.440 131.418  58.147  1.00 47.48           C  
ATOM   3115  OD1 ASP B 151      20.428 131.355  58.877  1.00 47.31           O  
ATOM   3116  OD2 ASP B 151      21.433 132.209  57.179  1.00 47.73           O  
ATOM   3117  N   GLY B 152      20.451 127.965  57.633  1.00 46.90           N  
ATOM   3118  CA  GLY B 152      19.442 127.019  58.074  1.00 46.70           C  
ATOM   3119  C   GLY B 152      19.785 125.594  57.671  1.00 46.57           C  
ATOM   3120  O   GLY B 152      19.074 124.649  58.021  1.00 46.52           O  
ATOM   3121  N   GLY B 153      20.879 125.443  56.928  1.00 46.42           N  
ATOM   3122  CA  GLY B 153      21.322 124.147  56.454  1.00 46.41           C  
ATOM   3123  C   GLY B 153      20.318 123.474  55.537  1.00 46.40           C  
ATOM   3124  O   GLY B 153      19.709 124.120  54.685  1.00 46.40           O  
ATOM   3125  N   SER B 154      20.139 122.172  55.726  1.00 46.35           N  
ATOM   3126  CA  SER B 154      19.258 121.386  54.877  1.00 46.32           C  
ATOM   3127  C   SER B 154      17.902 121.153  55.525  1.00 46.30           C  
ATOM   3128  O   SER B 154      17.739 121.346  56.730  1.00 46.40           O  
ATOM   3129  CB  SER B 154      19.919 120.061  54.533  1.00 46.31           C  
ATOM   3130  OG  SER B 154      20.782 120.221  53.422  1.00 46.67           O  
ATOM   3131  N   LEU B 155      16.930 120.740  54.717  1.00 46.26           N  
ATOM   3132  CA  LEU B 155      15.568 120.547  55.195  1.00 46.27           C  
ATOM   3133  C   LEU B 155      15.416 119.310  56.076  1.00 46.53           C  
ATOM   3134  O   LEU B 155      14.548 119.271  56.945  1.00 46.62           O  
ATOM   3135  CB  LEU B 155      14.586 120.496  54.026  1.00 46.10           C  
ATOM   3136  CG  LEU B 155      13.761 121.746  53.717  1.00 45.57           C  
ATOM   3137  CD1 LEU B 155      12.534 121.354  52.916  1.00 45.37           C  
ATOM   3138  CD2 LEU B 155      13.349 122.499  54.972  1.00 44.94           C  
ATOM   3139  N   ASP B 156      16.254 118.302  55.852  1.00 46.79           N  
ATOM   3140  CA  ASP B 156      16.260 117.123  56.719  1.00 47.06           C  
ATOM   3141  C   ASP B 156      17.017 117.434  58.002  1.00 47.19           C  
ATOM   3142  O   ASP B 156      16.734 116.855  59.052  1.00 47.18           O  
ATOM   3143  CB  ASP B 156      16.872 115.911  56.019  1.00 47.01           C  
ATOM   3144  CG  ASP B 156      18.315 116.128  55.642  1.00 47.06           C  
ATOM   3145  OD1 ASP B 156      19.106 115.168  55.735  1.00 47.54           O  
ATOM   3146  OD2 ASP B 156      18.750 117.230  55.249  1.00 47.08           O  
ATOM   3147  N   GLN B 157      17.978 118.352  57.904  1.00 47.37           N  
ATOM   3148  CA  GLN B 157      18.675 118.863  59.079  1.00 47.63           C  
ATOM   3149  C   GLN B 157      17.650 119.448  60.039  1.00 47.64           C  
ATOM   3150  O   GLN B 157      17.604 119.070  61.209  1.00 47.75           O  
ATOM   3151  CB  GLN B 157      19.707 119.925  58.696  1.00 47.63           C  
ATOM   3152  CG  GLN B 157      20.986 119.376  58.080  1.00 48.16           C  
ATOM   3153  CD  GLN B 157      22.195 120.276  58.322  1.00 49.12           C  
ATOM   3154  OE1 GLN B 157      22.060 121.500  58.423  1.00 49.43           O  
ATOM   3155  NE2 GLN B 157      23.377 119.671  58.413  1.00 49.34           N  
ATOM   3156  N   VAL B 158      16.810 120.345  59.529  1.00 47.67           N  
ATOM   3157  CA  VAL B 158      15.772 120.964  60.347  1.00 47.78           C  
ATOM   3158  C   VAL B 158      14.690 119.952  60.722  1.00 47.87           C  
ATOM   3159  O   VAL B 158      14.014 120.109  61.742  1.00 47.88           O  
ATOM   3160  CB  VAL B 158      15.159 122.244  59.693  1.00 47.78           C  
ATOM   3161  CG1 VAL B 158      16.252 123.190  59.219  1.00 47.76           C  
ATOM   3162  CG2 VAL B 158      14.227 121.902  58.549  1.00 47.71           C  
ATOM   3163  N   LEU B 159      14.542 118.912  59.902  1.00 47.87           N  
ATOM   3164  CA  LEU B 159      13.627 117.822  60.219  1.00 48.01           C  
ATOM   3165  C   LEU B 159      14.213 116.969  61.334  1.00 48.20           C  
ATOM   3166  O   LEU B 159      13.475 116.361  62.117  1.00 48.28           O  
ATOM   3167  CB  LEU B 159      13.327 116.963  58.989  1.00 47.87           C  
ATOM   3168  CG  LEU B 159      12.635 115.613  59.218  1.00 47.82           C  
ATOM   3169  CD1 LEU B 159      11.184 115.768  59.673  1.00 47.16           C  
ATOM   3170  CD2 LEU B 159      12.722 114.765  57.963  1.00 48.60           C  
ATOM   3171  N   LYS B 160      15.541 116.928  61.406  1.00 48.31           N  
ATOM   3172  CA  LYS B 160      16.208 116.199  62.474  1.00 48.45           C  
ATOM   3173  C   LYS B 160      15.887 116.825  63.828  1.00 48.36           C  
ATOM   3174  O   LYS B 160      15.712 116.110  64.815  1.00 48.45           O  
ATOM   3175  CB  LYS B 160      17.717 116.116  62.237  1.00 48.55           C  
ATOM   3176  CG  LYS B 160      18.148 114.832  61.529  1.00 49.17           C  
ATOM   3177  CD  LYS B 160      19.220 114.074  62.317  1.00 50.15           C  
ATOM   3178  CE  LYS B 160      18.634 112.881  63.074  1.00 50.48           C  
ATOM   3179  NZ  LYS B 160      18.828 111.595  62.342  1.00 50.72           N  
ATOM   3180  N   GLU B 161      15.781 118.155  63.861  1.00 48.14           N  
ATOM   3181  CA  GLU B 161      15.396 118.873  65.075  1.00 47.95           C  
ATOM   3182  C   GLU B 161      13.882 118.828  65.286  1.00 47.74           C  
ATOM   3183  O   GLU B 161      13.409 118.192  66.228  1.00 47.85           O  
ATOM   3184  CB  GLU B 161      15.896 120.316  65.047  1.00 47.97           C  
ATOM   3185  CG  GLU B 161      17.315 120.468  64.526  1.00 48.50           C  
ATOM   3186  CD  GLU B 161      18.329 120.694  65.630  1.00 49.42           C  
ATOM   3187  OE1 GLU B 161      19.472 120.206  65.488  1.00 49.64           O  
ATOM   3188  OE2 GLU B 161      17.990 121.363  66.634  1.00 49.88           O  
ATOM   3189  N   ALA B 162      13.129 119.492  64.411  1.00 47.42           N  
ATOM   3190  CA  ALA B 162      11.668 119.463  64.472  1.00 47.12           C  
ATOM   3191  C   ALA B 162      11.160 118.113  63.988  1.00 46.94           C  
ATOM   3192  O   ALA B 162      11.327 117.766  62.819  1.00 47.01           O  
ATOM   3193  CB  ALA B 162      11.076 120.583  63.642  1.00 47.13           C  
ATOM   3194  N   LYS B 163      10.539 117.360  64.893  1.00 46.69           N  
ATOM   3195  CA  LYS B 163      10.137 115.974  64.636  1.00 46.42           C  
ATOM   3196  C   LYS B 163       9.408 115.776  63.293  1.00 45.95           C  
ATOM   3197  O   LYS B 163       9.712 114.841  62.546  1.00 46.08           O  
ATOM   3198  CB  LYS B 163       9.309 115.428  65.810  1.00 46.69           C  
ATOM   3199  CG  LYS B 163      10.137 115.082  67.060  1.00 47.15           C  
ATOM   3200  CD  LYS B 163       9.373 114.157  68.016  1.00 47.96           C  
ATOM   3201  CE  LYS B 163       9.572 114.562  69.478  1.00 48.20           C  
ATOM   3202  NZ  LYS B 163       8.327 114.393  70.292  1.00 48.30           N  
ATOM   3203  N   ARG B 164       8.454 116.658  63.003  1.00 45.23           N  
ATOM   3204  CA  ARG B 164       7.828 116.742  61.685  1.00 44.50           C  
ATOM   3205  C   ARG B 164       7.801 118.206  61.240  1.00 43.72           C  
ATOM   3206  O   ARG B 164       8.078 119.103  62.038  1.00 43.76           O  
ATOM   3207  CB  ARG B 164       6.416 116.144  61.713  1.00 44.68           C  
ATOM   3208  CG  ARG B 164       5.401 116.931  62.538  1.00 45.84           C  
ATOM   3209  CD  ARG B 164       4.409 116.061  63.299  1.00 47.95           C  
ATOM   3210  NE  ARG B 164       4.010 116.651  64.581  1.00 49.76           N  
ATOM   3211  CZ  ARG B 164       4.702 116.553  65.721  1.00 50.75           C  
ATOM   3212  NH1 ARG B 164       5.852 115.881  65.769  1.00 50.84           N  
ATOM   3213  NH2 ARG B 164       4.239 117.133  66.825  1.00 50.99           N  
ATOM   3214  N   ILE B 165       7.478 118.452  59.973  1.00 42.77           N  
ATOM   3215  CA  ILE B 165       7.343 119.827  59.480  1.00 41.81           C  
ATOM   3216  C   ILE B 165       5.893 120.144  59.077  1.00 41.08           C  
ATOM   3217  O   ILE B 165       5.279 119.389  58.328  1.00 40.99           O  
ATOM   3218  CB  ILE B 165       8.360 120.116  58.348  1.00 41.76           C  
ATOM   3219  CG1 ILE B 165       9.756 120.309  58.953  1.00 41.62           C  
ATOM   3220  CG2 ILE B 165       7.960 121.355  57.565  1.00 41.81           C  
ATOM   3221  CD1 ILE B 165      10.889 120.292  57.955  1.00 41.36           C  
ATOM   3222  N   PRO B 166       5.349 121.249  59.591  1.00 40.44           N  
ATOM   3223  CA  PRO B 166       3.923 121.553  59.436  1.00 39.90           C  
ATOM   3224  C   PRO B 166       3.557 122.015  58.031  1.00 39.29           C  
ATOM   3225  O   PRO B 166       4.384 122.626  57.339  1.00 39.18           O  
ATOM   3226  CB  PRO B 166       3.697 122.685  60.443  1.00 39.96           C  
ATOM   3227  CG  PRO B 166       4.938 122.709  61.281  1.00 40.24           C  
ATOM   3228  CD  PRO B 166       6.038 122.298  60.361  1.00 40.46           C  
ATOM   3229  N   GLU B 167       2.314 121.727  57.642  1.00 38.46           N  
ATOM   3230  CA  GLU B 167       1.801 121.987  56.299  1.00 37.67           C  
ATOM   3231  C   GLU B 167       2.093 123.395  55.818  1.00 37.37           C  
ATOM   3232  O   GLU B 167       2.642 123.574  54.735  1.00 37.30           O  
ATOM   3233  CB  GLU B 167       0.301 121.720  56.243  1.00 37.50           C  
ATOM   3234  CG  GLU B 167      -0.315 121.918  54.872  1.00 36.98           C  
ATOM   3235  CD  GLU B 167      -1.748 121.436  54.809  1.00 37.10           C  
ATOM   3236  OE1 GLU B 167      -2.164 120.682  55.719  1.00 37.06           O  
ATOM   3237  OE2 GLU B 167      -2.463 121.814  53.852  1.00 36.80           O  
ATOM   3238  N   GLU B 168       1.731 124.386  56.630  1.00 37.04           N  
ATOM   3239  CA  GLU B 168       1.981 125.794  56.311  1.00 36.75           C  
ATOM   3240  C   GLU B 168       3.396 125.988  55.774  1.00 36.08           C  
ATOM   3241  O   GLU B 168       3.589 126.639  54.746  1.00 36.16           O  
ATOM   3242  CB  GLU B 168       1.740 126.712  57.525  1.00 37.00           C  
ATOM   3243  CG  GLU B 168       1.261 126.019  58.800  1.00 38.24           C  
ATOM   3244  CD  GLU B 168       1.612 126.792  60.067  1.00 39.66           C  
ATOM   3245  OE1 GLU B 168       1.026 127.879  60.291  1.00 40.14           O  
ATOM   3246  OE2 GLU B 168       2.470 126.309  60.844  1.00 39.76           O  
ATOM   3247  N   ILE B 169       4.371 125.403  56.462  1.00 35.20           N  
ATOM   3248  CA  ILE B 169       5.759 125.481  56.037  1.00 34.48           C  
ATOM   3249  C   ILE B 169       5.941 124.683  54.755  1.00 33.83           C  
ATOM   3250  O   ILE B 169       6.585 125.150  53.812  1.00 33.82           O  
ATOM   3251  CB  ILE B 169       6.717 124.963  57.145  1.00 34.65           C  
ATOM   3252  CG1 ILE B 169       6.423 125.639  58.496  1.00 34.95           C  
ATOM   3253  CG2 ILE B 169       8.195 125.100  56.715  1.00 34.37           C  
ATOM   3254  CD1 ILE B 169       7.010 127.047  58.673  1.00 35.26           C  
ATOM   3255  N   LEU B 170       5.359 123.488  54.717  1.00 32.89           N  
ATOM   3256  CA  LEU B 170       5.506 122.615  53.558  1.00 31.94           C  
ATOM   3257  C   LEU B 170       4.928 123.245  52.293  1.00 31.40           C  
ATOM   3258  O   LEU B 170       5.442 123.017  51.195  1.00 31.40           O  
ATOM   3259  CB  LEU B 170       4.911 121.232  53.831  1.00 31.84           C  
ATOM   3260  CG  LEU B 170       5.825 120.283  54.615  1.00 31.39           C  
ATOM   3261  CD1 LEU B 170       5.387 118.846  54.429  1.00 31.00           C  
ATOM   3262  CD2 LEU B 170       7.299 120.441  54.236  1.00 30.61           C  
ATOM   3263  N   GLY B 171       3.878 124.047  52.460  1.00 30.64           N  
ATOM   3264  CA  GLY B 171       3.345 124.865  51.385  1.00 29.83           C  
ATOM   3265  C   GLY B 171       4.370 125.854  50.857  1.00 29.31           C  
ATOM   3266  O   GLY B 171       4.540 125.991  49.650  1.00 29.17           O  
ATOM   3267  N   LYS B 172       5.064 126.532  51.765  1.00 28.92           N  
ATOM   3268  CA  LYS B 172       6.107 127.482  51.393  1.00 28.69           C  
ATOM   3269  C   LYS B 172       7.290 126.773  50.733  1.00 28.41           C  
ATOM   3270  O   LYS B 172       7.963 127.340  49.871  1.00 28.35           O  
ATOM   3271  CB  LYS B 172       6.573 128.276  52.617  1.00 28.80           C  
ATOM   3272  CG  LYS B 172       6.179 129.749  52.608  1.00 29.42           C  
ATOM   3273  CD  LYS B 172       7.243 130.615  53.295  1.00 30.93           C  
ATOM   3274  CE  LYS B 172       7.804 131.722  52.381  1.00 31.31           C  
ATOM   3275  NZ  LYS B 172       9.191 132.136  52.774  1.00 30.87           N  
ATOM   3276  N   VAL B 173       7.536 125.531  51.141  1.00 28.13           N  
ATOM   3277  CA  VAL B 173       8.592 124.713  50.545  1.00 27.83           C  
ATOM   3278  C   VAL B 173       8.219 124.300  49.120  1.00 27.54           C  
ATOM   3279  O   VAL B 173       9.005 124.492  48.187  1.00 27.41           O  
ATOM   3280  CB  VAL B 173       8.887 123.456  51.394  1.00 27.83           C  
ATOM   3281  CG1 VAL B 173       9.868 122.536  50.679  1.00 27.79           C  
ATOM   3282  CG2 VAL B 173       9.428 123.847  52.752  1.00 27.96           C  
ATOM   3283  N   SER B 174       7.016 123.739  48.973  1.00 27.08           N  
ATOM   3284  CA  SER B 174       6.491 123.299  47.686  1.00 26.71           C  
ATOM   3285  C   SER B 174       6.586 124.395  46.639  1.00 26.63           C  
ATOM   3286  O   SER B 174       7.055 124.153  45.523  1.00 26.71           O  
ATOM   3287  CB  SER B 174       5.042 122.846  47.828  1.00 26.64           C  
ATOM   3288  OG  SER B 174       4.931 121.829  48.798  1.00 26.37           O  
ATOM   3289  N   ILE B 175       6.142 125.594  47.006  1.00 26.37           N  
ATOM   3290  CA  ILE B 175       6.293 126.768  46.158  1.00 26.27           C  
ATOM   3291  C   ILE B 175       7.757 126.904  45.733  1.00 26.29           C  
ATOM   3292  O   ILE B 175       8.083 126.743  44.561  1.00 26.40           O  
ATOM   3293  CB  ILE B 175       5.802 128.049  46.892  1.00 26.21           C  
ATOM   3294  CG1 ILE B 175       4.277 128.054  47.019  1.00 25.96           C  
ATOM   3295  CG2 ILE B 175       6.272 129.310  46.171  1.00 26.33           C  
ATOM   3296  CD1 ILE B 175       3.757 128.881  48.177  1.00 25.27           C  
ATOM   3297  N   ALA B 176       8.636 127.147  46.699  1.00 26.31           N  
ATOM   3298  CA  ALA B 176      10.037 127.443  46.421  1.00 26.36           C  
ATOM   3299  C   ALA B 176      10.733 126.389  45.563  1.00 26.33           C  
ATOM   3300  O   ALA B 176      11.653 126.712  44.814  1.00 26.27           O  
ATOM   3301  CB  ALA B 176      10.795 127.664  47.717  1.00 26.49           C  
ATOM   3302  N   VAL B 177      10.294 125.138  45.676  1.00 26.46           N  
ATOM   3303  CA  VAL B 177      10.827 124.058  44.845  1.00 26.58           C  
ATOM   3304  C   VAL B 177      10.221 124.135  43.453  1.00 26.55           C  
ATOM   3305  O   VAL B 177      10.950 124.153  42.461  1.00 26.60           O  
ATOM   3306  CB  VAL B 177      10.582 122.652  45.459  1.00 26.67           C  
ATOM   3307  CG1 VAL B 177      10.793 121.550  44.420  1.00 26.59           C  
ATOM   3308  CG2 VAL B 177      11.489 122.429  46.652  1.00 26.68           C  
ATOM   3309  N   LEU B 178       8.891 124.191  43.386  1.00 26.46           N  
ATOM   3310  CA  LEU B 178       8.194 124.275  42.108  1.00 26.54           C  
ATOM   3311  C   LEU B 178       8.732 125.416  41.246  1.00 26.69           C  
ATOM   3312  O   LEU B 178       8.902 125.264  40.038  1.00 26.62           O  
ATOM   3313  CB  LEU B 178       6.685 124.414  42.318  1.00 26.36           C  
ATOM   3314  CG  LEU B 178       5.914 123.109  42.539  1.00 26.45           C  
ATOM   3315  CD1 LEU B 178       4.455 123.392  42.841  1.00 26.53           C  
ATOM   3316  CD2 LEU B 178       6.039 122.158  41.349  1.00 26.20           C  
ATOM   3317  N   ARG B 179       9.015 126.550  41.879  1.00 26.90           N  
ATOM   3318  CA  ARG B 179       9.536 127.708  41.170  1.00 27.25           C  
ATOM   3319  C   ARG B 179      10.984 127.467  40.779  1.00 27.06           C  
ATOM   3320  O   ARG B 179      11.375 127.722  39.635  1.00 27.02           O  
ATOM   3321  CB  ARG B 179       9.406 128.978  42.012  1.00 27.42           C  
ATOM   3322  CG  ARG B 179       7.989 129.294  42.460  1.00 29.12           C  
ATOM   3323  CD  ARG B 179       7.297 130.417  41.685  1.00 32.17           C  
ATOM   3324  NE  ARG B 179       6.019 130.801  42.297  1.00 33.32           N  
ATOM   3325  CZ  ARG B 179       5.893 131.635  43.327  1.00 33.34           C  
ATOM   3326  NH1 ARG B 179       6.967 132.195  43.880  1.00 33.08           N  
ATOM   3327  NH2 ARG B 179       4.688 131.910  43.808  1.00 33.09           N  
ATOM   3328  N   GLY B 180      11.768 126.970  41.732  1.00 26.92           N  
ATOM   3329  CA  GLY B 180      13.158 126.627  41.494  1.00 26.90           C  
ATOM   3330  C   GLY B 180      13.304 125.646  40.347  1.00 26.95           C  
ATOM   3331  O   GLY B 180      14.162 125.828  39.482  1.00 26.92           O  
ATOM   3332  N   LEU B 181      12.460 124.613  40.347  1.00 26.96           N  
ATOM   3333  CA  LEU B 181      12.388 123.639  39.262  1.00 26.94           C  
ATOM   3334  C   LEU B 181      12.104 124.330  37.940  1.00 27.15           C  
ATOM   3335  O   LEU B 181      12.808 124.110  36.955  1.00 27.08           O  
ATOM   3336  CB  LEU B 181      11.292 122.613  39.544  1.00 26.75           C  
ATOM   3337  CG  LEU B 181      11.701 121.192  39.925  1.00 26.92           C  
ATOM   3338  CD1 LEU B 181      12.972 121.170  40.751  1.00 27.03           C  
ATOM   3339  CD2 LEU B 181      10.577 120.515  40.683  1.00 27.20           C  
ATOM   3340  N   ALA B 182      11.078 125.183  37.944  1.00 27.57           N  
ATOM   3341  CA  ALA B 182      10.637 125.923  36.763  1.00 27.71           C  
ATOM   3342  C   ALA B 182      11.730 126.827  36.229  1.00 27.95           C  
ATOM   3343  O   ALA B 182      11.855 126.998  35.023  1.00 27.90           O  
ATOM   3344  CB  ALA B 182       9.395 126.730  37.076  1.00 27.58           C  
ATOM   3345  N   TYR B 183      12.521 127.398  37.134  1.00 28.47           N  
ATOM   3346  CA  TYR B 183      13.612 128.283  36.742  1.00 28.88           C  
ATOM   3347  C   TYR B 183      14.606 127.563  35.844  1.00 29.11           C  
ATOM   3348  O   TYR B 183      14.840 127.994  34.723  1.00 29.29           O  
ATOM   3349  CB  TYR B 183      14.325 128.898  37.959  1.00 28.90           C  
ATOM   3350  CG  TYR B 183      15.519 129.733  37.564  1.00 28.94           C  
ATOM   3351  CD1 TYR B 183      15.352 131.025  37.059  1.00 29.58           C  
ATOM   3352  CD2 TYR B 183      16.809 129.220  37.654  1.00 28.66           C  
ATOM   3353  CE1 TYR B 183      16.443 131.789  36.668  1.00 29.78           C  
ATOM   3354  CE2 TYR B 183      17.904 129.970  37.270  1.00 29.27           C  
ATOM   3355  CZ  TYR B 183      17.714 131.251  36.776  1.00 30.24           C  
ATOM   3356  OH  TYR B 183      18.801 131.997  36.392  1.00 31.92           O  
ATOM   3357  N   LEU B 184      15.167 126.461  36.335  1.00 29.53           N  
ATOM   3358  CA  LEU B 184      16.172 125.696  35.593  1.00 29.98           C  
ATOM   3359  C   LEU B 184      15.633 125.137  34.273  1.00 30.53           C  
ATOM   3360  O   LEU B 184      16.396 124.903  33.335  1.00 30.57           O  
ATOM   3361  CB  LEU B 184      16.740 124.561  36.456  1.00 29.75           C  
ATOM   3362  CG  LEU B 184      17.185 124.851  37.894  1.00 29.19           C  
ATOM   3363  CD1 LEU B 184      17.123 123.581  38.718  1.00 28.52           C  
ATOM   3364  CD2 LEU B 184      18.581 125.459  37.949  1.00 28.43           C  
ATOM   3365  N   ARG B 185      14.317 124.933  34.216  1.00 31.31           N  
ATOM   3366  CA  ARG B 185      13.644 124.374  33.042  1.00 32.03           C  
ATOM   3367  C   ARG B 185      13.382 125.448  32.005  1.00 32.22           C  
ATOM   3368  O   ARG B 185      13.685 125.267  30.826  1.00 32.44           O  
ATOM   3369  CB  ARG B 185      12.321 123.711  33.446  1.00 32.17           C  
ATOM   3370  CG  ARG B 185      11.832 122.639  32.484  1.00 33.40           C  
ATOM   3371  CD  ARG B 185      10.410 122.126  32.776  1.00 35.78           C  
ATOM   3372  NE  ARG B 185       9.378 122.834  32.007  1.00 36.56           N  
ATOM   3373  CZ  ARG B 185       8.996 122.509  30.774  1.00 36.65           C  
ATOM   3374  NH1 ARG B 185       9.552 121.476  30.143  1.00 35.98           N  
ATOM   3375  NH2 ARG B 185       8.054 123.227  30.168  1.00 36.60           N  
ATOM   3376  N   GLU B 186      12.808 126.561  32.454  1.00 32.50           N  
ATOM   3377  CA  GLU B 186      12.492 127.677  31.578  1.00 32.64           C  
ATOM   3378  C   GLU B 186      13.763 128.389  31.129  1.00 32.89           C  
ATOM   3379  O   GLU B 186      13.958 128.605  29.937  1.00 33.19           O  
ATOM   3380  CB  GLU B 186      11.537 128.658  32.268  1.00 32.55           C  
ATOM   3381  CG  GLU B 186      10.068 128.251  32.231  0.50 32.50           C  
ATOM   3382  CD  GLU B 186       9.203 129.032  33.211  0.50 32.37           C  
ATOM   3383  OE1 GLU B 186       9.167 130.279  33.133  0.50 32.39           O  
ATOM   3384  OE2 GLU B 186       8.546 128.398  34.061  0.50 32.37           O  
ATOM   3385  N   LYS B 187      14.638 128.714  32.078  1.00 33.13           N  
ATOM   3386  CA  LYS B 187      15.758 129.622  31.817  1.00 33.42           C  
ATOM   3387  C   LYS B 187      17.089 128.947  31.471  1.00 33.55           C  
ATOM   3388  O   LYS B 187      18.025 129.619  31.036  1.00 33.82           O  
ATOM   3389  CB  LYS B 187      15.950 130.598  32.988  1.00 33.46           C  
ATOM   3390  CG  LYS B 187      14.677 131.338  33.421  1.00 33.98           C  
ATOM   3391  CD  LYS B 187      14.878 132.854  33.488  1.00 34.77           C  
ATOM   3392  CE  LYS B 187      13.914 133.501  34.484  1.00 35.14           C  
ATOM   3393  NZ  LYS B 187      14.452 134.760  35.095  1.00 35.37           N  
ATOM   3394  N   HIS B 188      17.177 127.631  31.652  1.00 33.67           N  
ATOM   3395  CA  HIS B 188      18.437 126.915  31.429  1.00 33.76           C  
ATOM   3396  C   HIS B 188      18.279 125.542  30.755  1.00 33.99           C  
ATOM   3397  O   HIS B 188      19.269 124.898  30.404  1.00 34.03           O  
ATOM   3398  CB  HIS B 188      19.211 126.791  32.748  1.00 33.74           C  
ATOM   3399  CG  HIS B 188      19.663 128.106  33.306  1.00 33.44           C  
ATOM   3400  ND1 HIS B 188      20.817 128.735  32.890  1.00 33.13           N  
ATOM   3401  CD2 HIS B 188      19.106 128.919  34.235  1.00 32.95           C  
ATOM   3402  CE1 HIS B 188      20.955 129.874  33.545  1.00 32.85           C  
ATOM   3403  NE2 HIS B 188      19.930 130.010  34.367  1.00 32.56           N  
ATOM   3404  N   GLN B 189      17.033 125.111  30.574  1.00 34.36           N  
ATOM   3405  CA  GLN B 189      16.703 123.858  29.892  1.00 34.71           C  
ATOM   3406  C   GLN B 189      17.318 122.643  30.569  1.00 34.82           C  
ATOM   3407  O   GLN B 189      17.809 121.741  29.890  1.00 35.14           O  
ATOM   3408  CB  GLN B 189      17.145 123.903  28.425  1.00 34.79           C  
ATOM   3409  CG  GLN B 189      16.141 124.533  27.483  1.00 35.95           C  
ATOM   3410  CD  GLN B 189      16.565 125.916  27.004  1.00 37.43           C  
ATOM   3411  OE1 GLN B 189      17.738 126.295  27.118  1.00 38.21           O  
ATOM   3412  NE2 GLN B 189      15.612 126.671  26.464  1.00 37.59           N  
ATOM   3413  N   ILE B 190      17.308 122.616  31.899  1.00 34.90           N  
ATOM   3414  CA  ILE B 190      17.883 121.486  32.634  1.00 34.90           C  
ATOM   3415  C   ILE B 190      17.090 121.099  33.868  1.00 34.81           C  
ATOM   3416  O   ILE B 190      16.606 121.961  34.598  1.00 34.71           O  
ATOM   3417  CB  ILE B 190      19.360 121.739  33.018  1.00 34.92           C  
ATOM   3418  CG1 ILE B 190      19.548 123.138  33.602  1.00 34.97           C  
ATOM   3419  CG2 ILE B 190      20.282 121.496  31.821  1.00 35.34           C  
ATOM   3420  CD1 ILE B 190      20.062 123.115  35.011  1.00 35.57           C  
ATOM   3421  N   MET B 191      16.972 119.793  34.091  1.00 34.86           N  
ATOM   3422  CA  MET B 191      16.277 119.262  35.259  1.00 35.01           C  
ATOM   3423  C   MET B 191      17.195 119.092  36.478  1.00 35.02           C  
ATOM   3424  O   MET B 191      18.411 118.952  36.348  1.00 35.01           O  
ATOM   3425  CB  MET B 191      15.533 117.958  34.918  1.00 35.03           C  
ATOM   3426  CG  MET B 191      16.409 116.759  34.556  1.00 35.27           C  
ATOM   3427  SD  MET B 191      15.429 115.356  33.952  1.00 35.04           S  
ATOM   3428  CE  MET B 191      15.720 114.178  35.228  1.00 36.06           C  
ATOM   3429  N   HIS B 192      16.590 119.128  37.660  1.00 35.17           N  
ATOM   3430  CA  HIS B 192      17.308 119.004  38.919  1.00 35.48           C  
ATOM   3431  C   HIS B 192      17.325 117.536  39.327  1.00 35.75           C  
ATOM   3432  O   HIS B 192      16.553 117.122  40.195  1.00 36.18           O  
ATOM   3433  CB  HIS B 192      16.593 119.833  39.991  1.00 35.46           C  
ATOM   3434  CG  HIS B 192      17.381 120.014  41.249  1.00 35.10           C  
ATOM   3435  ND1 HIS B 192      18.135 119.007  41.808  1.00 34.90           N  
ATOM   3436  CD2 HIS B 192      17.532 121.089  42.057  1.00 35.29           C  
ATOM   3437  CE1 HIS B 192      18.718 119.453  42.904  1.00 35.22           C  
ATOM   3438  NE2 HIS B 192      18.370 120.714  43.078  1.00 35.27           N  
ATOM   3439  N   ARG B 193      18.212 116.749  38.725  1.00 35.71           N  
ATOM   3440  CA  ARG B 193      18.093 115.287  38.808  1.00 35.73           C  
ATOM   3441  C   ARG B 193      18.349 114.675  40.196  1.00 35.31           C  
ATOM   3442  O   ARG B 193      18.517 113.458  40.324  1.00 35.22           O  
ATOM   3443  CB  ARG B 193      18.931 114.590  37.720  1.00 35.88           C  
ATOM   3444  CG  ARG B 193      20.027 115.435  37.101  1.00 37.23           C  
ATOM   3445  CD  ARG B 193      20.282 115.146  35.631  1.00 39.45           C  
ATOM   3446  NE  ARG B 193      20.629 113.746  35.395  1.00 41.12           N  
ATOM   3447  CZ  ARG B 193      19.949 112.930  34.597  1.00 42.08           C  
ATOM   3448  NH1 ARG B 193      18.878 113.370  33.943  1.00 42.78           N  
ATOM   3449  NH2 ARG B 193      20.342 111.672  34.444  1.00 42.03           N  
ATOM   3450  N   ASP B 194      18.350 115.517  41.228  1.00 34.84           N  
ATOM   3451  CA  ASP B 194      18.599 115.071  42.592  1.00 34.42           C  
ATOM   3452  C   ASP B 194      17.871 115.940  43.608  1.00 34.25           C  
ATOM   3453  O   ASP B 194      18.498 116.633  44.412  1.00 34.23           O  
ATOM   3454  CB  ASP B 194      20.103 115.068  42.875  1.00 34.48           C  
ATOM   3455  CG  ASP B 194      20.457 114.320  44.139  1.00 34.46           C  
ATOM   3456  OD1 ASP B 194      21.281 114.838  44.923  1.00 34.60           O  
ATOM   3457  OD2 ASP B 194      19.966 113.213  44.434  1.00 34.94           O  
ATOM   3458  N   VAL B 195      16.544 115.909  43.567  1.00 34.06           N  
ATOM   3459  CA  VAL B 195      15.747 116.627  44.555  1.00 33.91           C  
ATOM   3460  C   VAL B 195      15.524 115.731  45.769  1.00 34.03           C  
ATOM   3461  O   VAL B 195      15.077 114.589  45.635  1.00 34.16           O  
ATOM   3462  CB  VAL B 195      14.405 117.131  43.967  1.00 33.78           C  
ATOM   3463  CG1 VAL B 195      13.463 117.613  45.062  1.00 33.20           C  
ATOM   3464  CG2 VAL B 195      14.658 118.248  42.973  1.00 33.76           C  
ATOM   3465  N   LYS B 196      15.874 116.249  46.943  1.00 33.99           N  
ATOM   3466  CA  LYS B 196      15.628 115.578  48.219  1.00 34.01           C  
ATOM   3467  C   LYS B 196      15.794 116.588  49.351  1.00 34.07           C  
ATOM   3468  O   LYS B 196      16.353 117.662  49.133  1.00 34.08           O  
ATOM   3469  CB  LYS B 196      16.569 114.381  48.418  1.00 34.11           C  
ATOM   3470  CG  LYS B 196      18.035 114.631  48.112  1.00 33.86           C  
ATOM   3471  CD  LYS B 196      18.700 113.347  47.665  1.00 33.41           C  
ATOM   3472  CE  LYS B 196      20.069 113.190  48.292  1.00 33.48           C  
ATOM   3473  NZ  LYS B 196      21.142 113.611  47.354  1.00 33.35           N  
ATOM   3474  N   PRO B 197      15.316 116.259  50.552  1.00 34.10           N  
ATOM   3475  CA  PRO B 197      15.400 117.181  51.693  1.00 34.16           C  
ATOM   3476  C   PRO B 197      16.799 117.732  51.945  1.00 34.31           C  
ATOM   3477  O   PRO B 197      16.916 118.883  52.353  1.00 34.33           O  
ATOM   3478  CB  PRO B 197      14.946 116.318  52.863  1.00 34.14           C  
ATOM   3479  CG  PRO B 197      14.021 115.346  52.244  1.00 34.09           C  
ATOM   3480  CD  PRO B 197      14.640 115.003  50.921  1.00 34.04           C  
ATOM   3481  N   SER B 198      17.832 116.934  51.687  1.00 34.66           N  
ATOM   3482  CA  SER B 198      19.226 117.363  51.867  1.00 34.83           C  
ATOM   3483  C   SER B 198      19.686 118.341  50.786  1.00 34.84           C  
ATOM   3484  O   SER B 198      20.762 118.931  50.889  1.00 34.91           O  
ATOM   3485  CB  SER B 198      20.169 116.154  51.911  1.00 34.84           C  
ATOM   3486  OG  SER B 198      19.861 115.211  50.893  1.00 35.23           O  
ATOM   3487  N   ASN B 199      18.870 118.506  49.754  1.00 34.88           N  
ATOM   3488  CA  ASN B 199      19.209 119.395  48.654  1.00 35.05           C  
ATOM   3489  C   ASN B 199      18.289 120.607  48.570  1.00 35.11           C  
ATOM   3490  O   ASN B 199      18.289 121.334  47.575  1.00 35.08           O  
ATOM   3491  CB  ASN B 199      19.219 118.623  47.335  1.00 35.15           C  
ATOM   3492  CG  ASN B 199      20.535 117.926  47.081  1.00 35.04           C  
ATOM   3493  OD1 ASN B 199      21.449 117.974  47.906  1.00 34.95           O  
ATOM   3494  ND2 ASN B 199      20.642 117.273  45.931  1.00 35.18           N  
ATOM   3495  N   ILE B 200      17.499 120.805  49.619  1.00 35.27           N  
ATOM   3496  CA  ILE B 200      16.699 122.012  49.770  1.00 35.46           C  
ATOM   3497  C   ILE B 200      17.257 122.789  50.959  1.00 35.79           C  
ATOM   3498  O   ILE B 200      17.099 122.390  52.115  1.00 35.82           O  
ATOM   3499  CB  ILE B 200      15.195 121.681  49.949  1.00 35.30           C  
ATOM   3500  CG1 ILE B 200      14.678 120.851  48.772  1.00 35.07           C  
ATOM   3501  CG2 ILE B 200      14.378 122.951  50.071  1.00 35.04           C  
ATOM   3502  CD1 ILE B 200      13.663 119.786  49.163  1.00 34.80           C  
ATOM   3503  N   LEU B 201      17.924 123.895  50.656  1.00 36.19           N  
ATOM   3504  CA  LEU B 201      18.633 124.676  51.654  1.00 36.89           C  
ATOM   3505  C   LEU B 201      17.819 125.886  52.119  1.00 37.38           C  
ATOM   3506  O   LEU B 201      17.265 126.619  51.296  1.00 37.72           O  
ATOM   3507  CB  LEU B 201      19.981 125.116  51.082  1.00 36.86           C  
ATOM   3508  CG  LEU B 201      21.146 124.111  51.068  1.00 37.04           C  
ATOM   3509  CD1 LEU B 201      20.770 122.757  50.469  1.00 37.03           C  
ATOM   3510  CD2 LEU B 201      22.342 124.692  50.334  1.00 36.48           C  
ATOM   3511  N   VAL B 202      17.744 126.085  53.436  1.00 37.71           N  
ATOM   3512  CA  VAL B 202      16.997 127.206  54.017  1.00 38.05           C  
ATOM   3513  C   VAL B 202      17.914 128.196  54.747  1.00 38.53           C  
ATOM   3514  O   VAL B 202      19.073 127.881  55.009  1.00 38.68           O  
ATOM   3515  CB  VAL B 202      15.891 126.717  54.979  1.00 37.87           C  
ATOM   3516  CG1 VAL B 202      14.891 125.847  54.245  1.00 37.71           C  
ATOM   3517  CG2 VAL B 202      16.486 125.967  56.151  1.00 37.75           C  
ATOM   3518  N   ASN B 203      17.406 129.392  55.050  1.00 39.07           N  
ATOM   3519  CA  ASN B 203      18.129 130.340  55.918  1.00 39.62           C  
ATOM   3520  C   ASN B 203      17.250 131.280  56.763  1.00 39.95           C  
ATOM   3521  O   ASN B 203      16.044 131.413  56.520  1.00 39.97           O  
ATOM   3522  CB  ASN B 203      19.212 131.124  55.149  1.00 39.56           C  
ATOM   3523  CG  ASN B 203      18.646 132.047  54.086  1.00 39.73           C  
ATOM   3524  OD1 ASN B 203      17.462 132.396  54.099  1.00 39.95           O  
ATOM   3525  ND2 ASN B 203      19.504 132.456  53.153  1.00 39.44           N  
ATOM   3526  N   SER B 204      17.877 131.925  57.748  1.00 40.31           N  
ATOM   3527  CA  SER B 204      17.196 132.813  58.695  1.00 40.75           C  
ATOM   3528  C   SER B 204      16.485 134.012  58.042  1.00 41.08           C  
ATOM   3529  O   SER B 204      15.640 134.658  58.671  1.00 41.14           O  
ATOM   3530  CB  SER B 204      18.186 133.310  59.750  1.00 40.71           C  
ATOM   3531  OG  SER B 204      19.358 133.819  59.133  1.00 40.76           O  
ATOM   3532  N   ARG B 205      16.837 134.307  56.790  1.00 41.31           N  
ATOM   3533  CA  ARG B 205      16.168 135.346  56.009  1.00 41.41           C  
ATOM   3534  C   ARG B 205      14.750 134.913  55.594  1.00 41.35           C  
ATOM   3535  O   ARG B 205      13.942 135.743  55.173  1.00 41.49           O  
ATOM   3536  CB  ARG B 205      17.015 135.727  54.784  1.00 41.52           C  
ATOM   3537  CG  ARG B 205      18.199 136.651  55.097  1.00 42.17           C  
ATOM   3538  CD  ARG B 205      19.394 136.529  54.137  1.00 43.29           C  
ATOM   3539  NE  ARG B 205      20.665 136.904  54.772  1.00 44.50           N  
ATOM   3540  CZ  ARG B 205      21.879 136.774  54.218  1.00 45.41           C  
ATOM   3541  NH1 ARG B 205      22.961 137.150  54.900  1.00 45.34           N  
ATOM   3542  NH2 ARG B 205      22.023 136.273  52.990  1.00 45.36           N  
ATOM   3543  N   GLY B 206      14.454 133.620  55.729  1.00 41.21           N  
ATOM   3544  CA  GLY B 206      13.138 133.079  55.417  1.00 41.05           C  
ATOM   3545  C   GLY B 206      13.080 132.404  54.057  1.00 41.00           C  
ATOM   3546  O   GLY B 206      12.001 132.018  53.589  1.00 40.85           O  
ATOM   3547  N   GLU B 207      14.250 132.260  53.434  1.00 40.90           N  
ATOM   3548  CA  GLU B 207      14.368 131.739  52.076  1.00 40.84           C  
ATOM   3549  C   GLU B 207      14.528 130.232  52.034  1.00 40.79           C  
ATOM   3550  O   GLU B 207      15.256 129.650  52.840  1.00 41.01           O  
ATOM   3551  CB  GLU B 207      15.562 132.368  51.371  1.00 40.78           C  
ATOM   3552  CG  GLU B 207      15.294 133.752  50.825  1.00 41.45           C  
ATOM   3553  CD  GLU B 207      16.570 134.488  50.500  1.00 42.13           C  
ATOM   3554  OE1 GLU B 207      16.790 134.793  49.307  1.00 42.81           O  
ATOM   3555  OE2 GLU B 207      17.350 134.757  51.439  1.00 42.24           O  
ATOM   3556  N   ILE B 208      13.847 129.615  51.074  1.00 40.53           N  
ATOM   3557  CA  ILE B 208      13.985 128.200  50.789  1.00 40.21           C  
ATOM   3558  C   ILE B 208      14.565 128.094  49.390  1.00 40.27           C  
ATOM   3559  O   ILE B 208      13.961 128.572  48.431  1.00 40.31           O  
ATOM   3560  CB  ILE B 208      12.616 127.517  50.853  1.00 40.04           C  
ATOM   3561  CG1 ILE B 208      12.013 127.656  52.247  1.00 39.76           C  
ATOM   3562  CG2 ILE B 208      12.733 126.055  50.482  1.00 40.46           C  
ATOM   3563  CD1 ILE B 208      10.513 127.497  52.281  1.00 39.80           C  
ATOM   3564  N   LYS B 209      15.734 127.473  49.272  1.00 40.34           N  
ATOM   3565  CA  LYS B 209      16.437 127.408  47.993  1.00 40.59           C  
ATOM   3566  C   LYS B 209      16.886 125.999  47.596  1.00 40.83           C  
ATOM   3567  O   LYS B 209      17.212 125.184  48.451  1.00 40.92           O  
ATOM   3568  CB  LYS B 209      17.638 128.350  48.007  1.00 40.51           C  
ATOM   3569  CG  LYS B 209      17.284 129.816  47.919  1.00 40.49           C  
ATOM   3570  CD  LYS B 209      18.482 130.636  47.489  1.00 40.74           C  
ATOM   3571  CE  LYS B 209      18.391 132.063  48.002  1.00 40.82           C  
ATOM   3572  NZ  LYS B 209      18.867 133.027  46.971  1.00 41.54           N  
ATOM   3573  N   LEU B 210      16.907 125.732  46.292  1.00 41.20           N  
ATOM   3574  CA  LEU B 210      17.344 124.449  45.756  1.00 41.61           C  
ATOM   3575  C   LEU B 210      18.842 124.426  45.533  1.00 42.09           C  
ATOM   3576  O   LEU B 210      19.440 125.445  45.201  1.00 42.00           O  
ATOM   3577  CB  LEU B 210      16.642 124.147  44.435  1.00 41.53           C  
ATOM   3578  CG  LEU B 210      15.205 123.629  44.465  1.00 41.50           C  
ATOM   3579  CD1 LEU B 210      14.732 123.404  43.044  1.00 41.50           C  
ATOM   3580  CD2 LEU B 210      15.068 122.354  45.283  1.00 41.54           C  
ATOM   3581  N   CYS B 211      19.430 123.241  45.686  1.00 42.88           N  
ATOM   3582  CA  CYS B 211      20.876 123.051  45.619  1.00 43.71           C  
ATOM   3583  C   CYS B 211      21.234 121.776  44.867  1.00 44.28           C  
ATOM   3584  O   CYS B 211      20.390 120.902  44.703  1.00 44.39           O  
ATOM   3585  CB  CYS B 211      21.444 122.973  47.035  1.00 43.60           C  
ATOM   3586  SG  CYS B 211      23.244 123.029  47.133  1.00 44.03           S  
ATOM   3587  N   ASP B 212      22.489 121.687  44.418  1.00 45.08           N  
ATOM   3588  CA  ASP B 212      23.082 120.466  43.839  1.00 45.83           C  
ATOM   3589  C   ASP B 212      22.335 119.882  42.640  1.00 46.28           C  
ATOM   3590  O   ASP B 212      21.880 118.737  42.683  1.00 46.34           O  
ATOM   3591  CB  ASP B 212      23.273 119.371  44.905  1.00 45.88           C  
ATOM   3592  CG  ASP B 212      24.077 119.839  46.098  1.00 46.30           C  
ATOM   3593  OD1 ASP B 212      25.212 120.325  45.908  1.00 47.20           O  
ATOM   3594  OD2 ASP B 212      23.657 119.746  47.273  1.00 46.70           O  
ATOM   3595  N   PHE B 213      22.217 120.661  41.572  1.00 46.93           N  
ATOM   3596  CA  PHE B 213      21.601 120.176  40.339  1.00 47.56           C  
ATOM   3597  C   PHE B 213      22.675 119.940  39.287  1.00 48.25           C  
ATOM   3598  O   PHE B 213      23.708 120.612  39.282  1.00 48.19           O  
ATOM   3599  CB  PHE B 213      20.527 121.147  39.825  1.00 47.37           C  
ATOM   3600  CG  PHE B 213      20.877 122.591  40.014  1.00 46.73           C  
ATOM   3601  CD1 PHE B 213      21.621 123.267  39.057  1.00 46.16           C  
ATOM   3602  CD2 PHE B 213      20.474 123.273  41.154  1.00 46.17           C  
ATOM   3603  CE1 PHE B 213      21.956 124.593  39.233  1.00 45.97           C  
ATOM   3604  CE2 PHE B 213      20.807 124.604  41.336  1.00 46.01           C  
ATOM   3605  CZ  PHE B 213      21.550 125.263  40.374  1.00 45.95           C  
ATOM   3606  N   GLY B 214      22.424 118.982  38.400  1.00 49.20           N  
ATOM   3607  CA  GLY B 214      23.398 118.581  37.403  1.00 50.37           C  
ATOM   3608  C   GLY B 214      23.488 119.514  36.215  1.00 51.19           C  
ATOM   3609  O   GLY B 214      22.960 119.206  35.143  1.00 51.24           O  
ATOM   3610  N   VAL B 215      24.153 120.654  36.402  1.00 52.08           N  
ATOM   3611  CA  VAL B 215      24.397 121.575  35.295  1.00 53.23           C  
ATOM   3612  C   VAL B 215      25.468 120.999  34.393  1.00 54.02           C  
ATOM   3613  O   VAL B 215      25.419 121.166  33.172  1.00 54.19           O  
ATOM   3614  CB  VAL B 215      24.834 123.000  35.747  1.00 53.22           C  
ATOM   3615  CG1 VAL B 215      23.625 123.837  36.150  1.00 53.22           C  
ATOM   3616  CG2 VAL B 215      25.878 122.952  36.861  1.00 53.13           C  
ATOM   3617  N   SER B 216      26.426 120.315  35.014  1.00 54.96           N  
ATOM   3618  CA  SER B 216      27.562 119.743  34.312  1.00 56.02           C  
ATOM   3619  C   SER B 216      27.296 118.288  33.953  1.00 56.78           C  
ATOM   3620  O   SER B 216      27.240 117.423  34.833  1.00 56.98           O  
ATOM   3621  CB  SER B 216      28.827 119.865  35.168  1.00 55.94           C  
ATOM   3622  OG  SER B 216      29.821 118.945  34.750  1.00 56.03           O  
ATOM   3623  N   GLY B 217      27.134 118.029  32.657  1.00 57.66           N  
ATOM   3624  CA  GLY B 217      26.941 116.680  32.150  1.00 58.87           C  
ATOM   3625  C   GLY B 217      28.102 115.747  32.460  1.00 59.76           C  
ATOM   3626  O   GLY B 217      27.889 114.574  32.773  1.00 59.83           O  
ATOM   3627  N   GLN B 218      29.325 116.274  32.386  1.00 60.59           N  
ATOM   3628  CA  GLN B 218      30.536 115.482  32.611  1.00 61.43           C  
ATOM   3629  C   GLN B 218      30.963 115.399  34.085  1.00 61.99           C  
ATOM   3630  O   GLN B 218      31.936 114.717  34.412  1.00 62.08           O  
ATOM   3631  CB  GLN B 218      31.689 115.991  31.731  1.00 61.44           C  
ATOM   3632  CG  GLN B 218      32.378 114.911  30.880  1.00 61.62           C  
ATOM   3633  CD  GLN B 218      31.468 114.298  29.814  1.00 61.98           C  
ATOM   3634  OE1 GLN B 218      31.283 113.080  29.782  1.00 61.94           O  
ATOM   3635  NE2 GLN B 218      30.911 115.136  28.941  1.00 61.79           N  
ATOM   3636  N   LEU B 219      30.245 116.095  34.966  1.00 62.71           N  
ATOM   3637  CA  LEU B 219      30.401 115.890  36.407  1.00 63.48           C  
ATOM   3638  C   LEU B 219      29.649 114.626  36.805  1.00 63.98           C  
ATOM   3639  O   LEU B 219      30.132 113.827  37.614  1.00 64.00           O  
ATOM   3640  CB  LEU B 219      29.855 117.075  37.204  1.00 63.48           C  
ATOM   3641  CG  LEU B 219      30.644 117.536  38.434  1.00 63.77           C  
ATOM   3642  CD1 LEU B 219      30.184 118.924  38.845  1.00 64.18           C  
ATOM   3643  CD2 LEU B 219      30.513 116.572  39.607  1.00 63.57           C  
ATOM   3644  N   ILE B 220      28.455 114.472  36.230  1.00 64.59           N  
ATOM   3645  CA  ILE B 220      27.619 113.287  36.405  1.00 65.13           C  
ATOM   3646  C   ILE B 220      28.376 112.024  35.975  1.00 65.55           C  
ATOM   3647  O   ILE B 220      28.442 111.042  36.729  1.00 65.65           O  
ATOM   3648  CB  ILE B 220      26.301 113.444  35.596  1.00 65.08           C  
ATOM   3649  CG1 ILE B 220      25.536 114.694  36.051  1.00 65.11           C  
ATOM   3650  CG2 ILE B 220      25.435 112.185  35.704  1.00 65.04           C  
ATOM   3651  CD1 ILE B 220      24.712 115.355  34.955  1.00 65.32           C  
ATOM   3652  N   ASP B 221      28.956 112.075  34.773  1.00 65.94           N  
ATOM   3653  CA  ASP B 221      29.713 110.961  34.201  1.00 66.29           C  
ATOM   3654  C   ASP B 221      30.944 110.609  35.033  1.00 66.37           C  
ATOM   3655  O   ASP B 221      31.274 109.432  35.186  1.00 66.45           O  
ATOM   3656  CB  ASP B 221      30.116 111.269  32.753  1.00 66.41           C  
ATOM   3657  CG  ASP B 221      29.048 110.854  31.740  1.00 67.11           C  
ATOM   3658  OD1 ASP B 221      28.040 110.227  32.144  1.00 67.68           O  
ATOM   3659  OD2 ASP B 221      29.133 111.114  30.516  1.00 67.60           O  
ATOM   3660  N   SER B 222      31.602 111.633  35.578  1.00 66.49           N  
ATOM   3661  CA  SER B 222      32.776 111.448  36.433  1.00 66.65           C  
ATOM   3662  C   SER B 222      32.412 111.025  37.864  1.00 66.71           C  
ATOM   3663  O   SER B 222      33.292 110.896  38.725  1.00 66.73           O  
ATOM   3664  CB  SER B 222      33.630 112.720  36.451  1.00 66.70           C  
ATOM   3665  OG  SER B 222      35.012 112.406  36.524  1.00 66.91           O  
ATOM   3666  N   MET B 223      31.119 110.812  38.106  1.00 66.68           N  
ATOM   3667  CA  MET B 223      30.635 110.311  39.390  1.00 66.70           C  
ATOM   3668  C   MET B 223      29.764 109.075  39.190  1.00 66.69           C  
ATOM   3669  O   MET B 223      29.808 108.435  38.137  1.00 66.66           O  
ATOM   3670  CB  MET B 223      29.848 111.390  40.135  1.00 66.73           C  
ATOM   3671  CG  MET B 223      30.699 112.528  40.692  1.00 66.83           C  
ATOM   3672  SD  MET B 223      29.773 113.727  41.696  1.00 67.11           S  
ATOM   3673  CE  MET B 223      28.245 113.921  40.742  1.00 66.89           C  
ATOM   3674  N   THR B 230      20.731 104.058  52.127  1.00 41.24           N  
ATOM   3675  CA  THR B 230      19.572 103.650  52.927  1.00 41.32           C  
ATOM   3676  C   THR B 230      18.244 104.161  52.350  1.00 41.07           C  
ATOM   3677  O   THR B 230      17.218 103.481  52.460  1.00 41.51           O  
ATOM   3678  CB  THR B 230      19.713 104.082  54.427  1.00 41.43           C  
ATOM   3679  OG1 THR B 230      20.754 105.059  54.580  1.00 41.77           O  
ATOM   3680  CG2 THR B 230      20.192 102.918  55.283  1.00 41.58           C  
ATOM   3681  N   ARG B 231      18.270 105.352  51.747  1.00 40.35           N  
ATOM   3682  CA  ARG B 231      17.090 105.962  51.130  1.00 39.52           C  
ATOM   3683  C   ARG B 231      17.275 106.148  49.616  1.00 38.91           C  
ATOM   3684  O   ARG B 231      18.404 106.206  49.116  1.00 38.97           O  
ATOM   3685  CB  ARG B 231      16.796 107.322  51.771  1.00 39.62           C  
ATOM   3686  CG  ARG B 231      16.525 107.302  53.265  1.00 40.22           C  
ATOM   3687  CD  ARG B 231      16.904 108.600  53.975  1.00 41.63           C  
ATOM   3688  NE  ARG B 231      15.803 109.127  54.785  1.00 42.77           N  
ATOM   3689  CZ  ARG B 231      15.869 109.380  56.093  1.00 43.33           C  
ATOM   3690  NH1 ARG B 231      16.989 109.158  56.772  1.00 43.44           N  
ATOM   3691  NH2 ARG B 231      14.805 109.860  56.728  1.00 43.44           N  
ATOM   3692  N   SER B 232      16.164 106.242  48.889  1.00 37.95           N  
ATOM   3693  CA  SER B 232      16.198 106.597  47.474  1.00 36.92           C  
ATOM   3694  C   SER B 232      14.999 107.448  47.128  1.00 36.27           C  
ATOM   3695  O   SER B 232      13.876 107.121  47.493  1.00 36.18           O  
ATOM   3696  CB  SER B 232      16.218 105.356  46.589  1.00 36.94           C  
ATOM   3697  OG  SER B 232      16.520 105.708  45.250  1.00 36.99           O  
ATOM   3698  N   TYR B 233      15.243 108.541  46.417  1.00 35.59           N  
ATOM   3699  CA  TYR B 233      14.173 109.457  46.040  1.00 34.92           C  
ATOM   3700  C   TYR B 233      13.873 109.411  44.544  1.00 34.94           C  
ATOM   3701  O   TYR B 233      12.996 110.126  44.053  1.00 34.75           O  
ATOM   3702  CB  TYR B 233      14.516 110.876  46.491  1.00 34.54           C  
ATOM   3703  CG  TYR B 233      14.672 110.995  47.982  1.00 33.09           C  
ATOM   3704  CD1 TYR B 233      13.560 111.098  48.810  1.00 31.99           C  
ATOM   3705  CD2 TYR B 233      15.929 110.985  48.568  1.00 32.02           C  
ATOM   3706  CE1 TYR B 233      13.695 111.198  50.182  1.00 31.00           C  
ATOM   3707  CE2 TYR B 233      16.074 111.089  49.939  1.00 31.31           C  
ATOM   3708  CZ  TYR B 233      14.954 111.194  50.737  1.00 30.85           C  
ATOM   3709  OH  TYR B 233      15.098 111.298  52.097  1.00 31.01           O  
ATOM   3710  N   MET B 234      14.600 108.552  43.834  1.00 34.96           N  
ATOM   3711  CA  MET B 234      14.459 108.412  42.392  1.00 35.15           C  
ATOM   3712  C   MET B 234      13.094 107.880  41.981  1.00 35.10           C  
ATOM   3713  O   MET B 234      12.454 107.135  42.726  1.00 35.15           O  
ATOM   3714  CB  MET B 234      15.548 107.511  41.845  1.00 35.23           C  
ATOM   3715  CG  MET B 234      16.652 108.265  41.158  1.00 36.04           C  
ATOM   3716  SD  MET B 234      17.561 107.141  40.112  1.00 38.50           S  
ATOM   3717  CE  MET B 234      18.831 106.549  41.270  1.00 38.23           C  
ATOM   3718  N   ALA B 235      12.669 108.271  40.783  1.00 35.04           N  
ATOM   3719  CA  ALA B 235      11.340 107.973  40.276  1.00 35.01           C  
ATOM   3720  C   ALA B 235      11.278 106.586  39.644  1.00 35.13           C  
ATOM   3721  O   ALA B 235      12.300 106.066  39.201  1.00 35.02           O  
ATOM   3722  CB  ALA B 235      10.928 109.033  39.273  1.00 35.01           C  
ATOM   3723  N   PRO B 236      10.087 105.985  39.607  1.00 35.34           N  
ATOM   3724  CA  PRO B 236       9.898 104.690  38.948  1.00 35.45           C  
ATOM   3725  C   PRO B 236      10.553 104.655  37.579  1.00 35.61           C  
ATOM   3726  O   PRO B 236      11.335 103.750  37.332  1.00 35.71           O  
ATOM   3727  CB  PRO B 236       8.378 104.592  38.811  1.00 35.40           C  
ATOM   3728  CG  PRO B 236       7.865 105.341  39.971  1.00 35.34           C  
ATOM   3729  CD  PRO B 236       8.828 106.473  40.202  1.00 35.37           C  
ATOM   3730  N   GLU B 237      10.264 105.638  36.730  1.00 35.97           N  
ATOM   3731  CA  GLU B 237      10.762 105.654  35.353  1.00 36.26           C  
ATOM   3732  C   GLU B 237      12.279 105.757  35.271  1.00 36.44           C  
ATOM   3733  O   GLU B 237      12.881 105.366  34.273  1.00 36.59           O  
ATOM   3734  CB  GLU B 237      10.106 106.782  34.548  1.00 36.26           C  
ATOM   3735  CG  GLU B 237      10.592 108.180  34.898  1.00 36.45           C  
ATOM   3736  CD  GLU B 237       9.662 108.917  35.846  1.00 37.03           C  
ATOM   3737  OE1 GLU B 237       8.962 108.255  36.658  1.00 35.86           O  
ATOM   3738  OE2 GLU B 237       9.641 110.173  35.777  1.00 37.35           O  
ATOM   3739  N   ARG B 238      12.891 106.286  36.322  1.00 36.75           N  
ATOM   3740  CA  ARG B 238      14.335 106.453  36.353  1.00 37.15           C  
ATOM   3741  C   ARG B 238      15.041 105.156  36.709  1.00 37.67           C  
ATOM   3742  O   ARG B 238      16.204 104.956  36.353  1.00 37.81           O  
ATOM   3743  CB  ARG B 238      14.721 107.547  37.338  1.00 36.94           C  
ATOM   3744  CG  ARG B 238      15.421 108.707  36.693  1.00 36.14           C  
ATOM   3745  CD  ARG B 238      16.170 109.560  37.671  1.00 35.01           C  
ATOM   3746  NE  ARG B 238      17.551 109.776  37.266  1.00 33.62           N  
ATOM   3747  CZ  ARG B 238      18.312 110.747  37.736  1.00 33.16           C  
ATOM   3748  NH1 ARG B 238      17.833 111.594  38.635  1.00 32.56           N  
ATOM   3749  NH2 ARG B 238      19.559 110.870  37.312  1.00 33.68           N  
ATOM   3750  N   LEU B 239      14.332 104.283  37.416  1.00 38.30           N  
ATOM   3751  CA  LEU B 239      14.876 103.000  37.832  1.00 38.98           C  
ATOM   3752  C   LEU B 239      14.554 101.932  36.804  1.00 39.70           C  
ATOM   3753  O   LEU B 239      15.403 101.109  36.481  1.00 39.95           O  
ATOM   3754  CB  LEU B 239      14.336 102.588  39.209  1.00 38.80           C  
ATOM   3755  CG  LEU B 239      14.424 103.546  40.406  1.00 38.44           C  
ATOM   3756  CD1 LEU B 239      13.460 103.099  41.499  1.00 37.62           C  
ATOM   3757  CD2 LEU B 239      15.850 103.681  40.952  1.00 37.72           C  
ATOM   3758  N   GLN B 240      13.330 101.964  36.285  1.00 40.79           N  
ATOM   3759  CA  GLN B 240      12.816 100.939  35.372  1.00 41.91           C  
ATOM   3760  C   GLN B 240      13.572 100.848  34.045  1.00 42.62           C  
ATOM   3761  O   GLN B 240      13.698  99.758  33.473  1.00 42.77           O  
ATOM   3762  CB  GLN B 240      11.327 101.163  35.104  1.00 41.92           C  
ATOM   3763  CG  GLN B 240      10.421 100.543  36.144  1.00 42.68           C  
ATOM   3764  CD  GLN B 240       9.773  99.256  35.662  1.00 44.54           C  
ATOM   3765  OE1 GLN B 240      10.451  98.235  35.483  1.00 45.33           O  
ATOM   3766  NE2 GLN B 240       8.457  99.295  35.454  1.00 45.03           N  
ATOM   3767  N   GLY B 241      14.065 101.988  33.560  1.00 43.36           N  
ATOM   3768  CA  GLY B 241      14.816 102.032  32.316  1.00 44.33           C  
ATOM   3769  C   GLY B 241      14.739 103.364  31.597  1.00 45.03           C  
ATOM   3770  O   GLY B 241      15.312 104.360  32.053  1.00 45.10           O  
ATOM   3771  N   THR B 242      14.016 103.369  30.476  1.00 45.72           N  
ATOM   3772  CA  THR B 242      13.907 104.531  29.582  1.00 46.31           C  
ATOM   3773  C   THR B 242      12.787 105.508  29.964  1.00 46.42           C  
ATOM   3774  O   THR B 242      12.111 105.322  30.978  1.00 46.31           O  
ATOM   3775  CB  THR B 242      13.719 104.060  28.112  1.00 46.49           C  
ATOM   3776  OG1 THR B 242      13.221 102.711  28.092  1.00 46.63           O  
ATOM   3777  CG2 THR B 242      15.076 103.974  27.390  1.00 46.55           C  
ATOM   3778  N   HIS B 243      12.612 106.542  29.135  1.00 46.78           N  
ATOM   3779  CA  HIS B 243      11.582 107.582  29.308  1.00 47.09           C  
ATOM   3780  C   HIS B 243      11.700 108.322  30.653  1.00 46.68           C  
ATOM   3781  O   HIS B 243      10.947 108.031  31.588  1.00 46.81           O  
ATOM   3782  CB  HIS B 243      10.159 106.995  29.130  1.00 47.43           C  
ATOM   3783  CG  HIS B 243       9.475 107.394  27.851  1.00 48.60           C  
ATOM   3784  ND1 HIS B 243       9.444 108.694  27.386  1.00 49.34           N  
ATOM   3785  CD2 HIS B 243       8.771 106.659  26.954  1.00 49.25           C  
ATOM   3786  CE1 HIS B 243       8.765 108.738  26.252  1.00 49.49           C  
ATOM   3787  NE2 HIS B 243       8.345 107.517  25.969  1.00 49.57           N  
ATOM   3788  N   TYR B 244      12.638 109.267  30.746  1.00 46.10           N  
ATOM   3789  CA  TYR B 244      12.821 110.052  31.975  1.00 45.64           C  
ATOM   3790  C   TYR B 244      13.136 111.529  31.738  1.00 44.92           C  
ATOM   3791  O   TYR B 244      14.106 111.872  31.061  1.00 45.10           O  
ATOM   3792  CB  TYR B 244      13.862 109.399  32.901  1.00 45.94           C  
ATOM   3793  CG  TYR B 244      15.318 109.692  32.580  1.00 47.12           C  
ATOM   3794  CD1 TYR B 244      16.139 110.341  33.509  1.00 47.89           C  
ATOM   3795  CD2 TYR B 244      15.883 109.304  31.357  1.00 48.36           C  
ATOM   3796  CE1 TYR B 244      17.486 110.608  33.230  1.00 48.63           C  
ATOM   3797  CE2 TYR B 244      17.230 109.571  31.062  1.00 49.24           C  
ATOM   3798  CZ  TYR B 244      18.027 110.222  32.003  1.00 49.36           C  
ATOM   3799  OH  TYR B 244      19.355 110.479  31.715  1.00 49.15           O  
ATOM   3800  N   SER B 245      12.309 112.400  32.310  1.00 43.95           N  
ATOM   3801  CA  SER B 245      12.445 113.842  32.117  1.00 42.87           C  
ATOM   3802  C   SER B 245      12.178 114.636  33.401  1.00 42.05           C  
ATOM   3803  O   SER B 245      12.444 114.161  34.505  1.00 41.90           O  
ATOM   3804  CB  SER B 245      11.507 114.304  30.999  1.00 42.97           C  
ATOM   3805  OG  SER B 245      10.150 114.162  31.392  1.00 43.03           O  
ATOM   3806  N   VAL B 246      11.652 115.849  33.240  1.00 41.02           N  
ATOM   3807  CA  VAL B 246      11.328 116.732  34.361  1.00 39.94           C  
ATOM   3808  C   VAL B 246      10.148 116.215  35.208  1.00 39.09           C  
ATOM   3809  O   VAL B 246       9.811 116.797  36.238  1.00 39.00           O  
ATOM   3810  CB  VAL B 246      11.099 118.202  33.873  1.00 40.02           C  
ATOM   3811  CG1 VAL B 246       9.886 118.304  32.948  1.00 39.90           C  
ATOM   3812  CG2 VAL B 246      10.992 119.181  35.055  1.00 40.07           C  
ATOM   3813  N   GLN B 247       9.534 115.117  34.775  1.00 38.01           N  
ATOM   3814  CA  GLN B 247       8.492 114.466  35.562  1.00 37.13           C  
ATOM   3815  C   GLN B 247       9.095 113.711  36.752  1.00 36.59           C  
ATOM   3816  O   GLN B 247       8.427 113.487  37.766  1.00 36.53           O  
ATOM   3817  CB  GLN B 247       7.663 113.515  34.694  1.00 37.07           C  
ATOM   3818  CG  GLN B 247       6.670 114.188  33.747  1.00 36.92           C  
ATOM   3819  CD  GLN B 247       6.029 115.439  34.321  1.00 37.27           C  
ATOM   3820  OE1 GLN B 247       5.330 115.383  35.336  1.00 37.46           O  
ATOM   3821  NE2 GLN B 247       6.262 116.572  33.669  1.00 37.49           N  
ATOM   3822  N   SER B 248      10.364 113.334  36.618  1.00 35.71           N  
ATOM   3823  CA  SER B 248      11.090 112.626  37.666  1.00 34.84           C  
ATOM   3824  C   SER B 248      11.265 113.457  38.929  1.00 34.06           C  
ATOM   3825  O   SER B 248      11.177 112.934  40.041  1.00 34.09           O  
ATOM   3826  CB  SER B 248      12.455 112.184  37.149  1.00 34.89           C  
ATOM   3827  OG  SER B 248      12.298 111.398  35.983  1.00 35.46           O  
ATOM   3828  N   ASP B 249      11.512 114.750  38.756  1.00 33.01           N  
ATOM   3829  CA  ASP B 249      11.749 115.628  39.893  1.00 32.14           C  
ATOM   3830  C   ASP B 249      10.451 115.901  40.655  1.00 31.75           C  
ATOM   3831  O   ASP B 249      10.479 116.154  41.864  1.00 31.76           O  
ATOM   3832  CB  ASP B 249      12.432 116.930  39.453  1.00 32.05           C  
ATOM   3833  CG  ASP B 249      13.869 116.717  38.969  1.00 31.53           C  
ATOM   3834  OD1 ASP B 249      14.549 115.773  39.432  1.00 30.45           O  
ATOM   3835  OD2 ASP B 249      14.409 117.458  38.123  1.00 31.12           O  
ATOM   3836  N   ILE B 250       9.321 115.835  39.947  1.00 31.01           N  
ATOM   3837  CA  ILE B 250       8.009 115.948  40.574  1.00 30.25           C  
ATOM   3838  C   ILE B 250       7.876 114.834  41.611  1.00 29.80           C  
ATOM   3839  O   ILE B 250       7.586 115.110  42.780  1.00 29.90           O  
ATOM   3840  CB  ILE B 250       6.864 115.882  39.521  1.00 30.31           C  
ATOM   3841  CG1 ILE B 250       7.011 116.985  38.457  1.00 30.36           C  
ATOM   3842  CG2 ILE B 250       5.491 115.946  40.191  1.00 30.40           C  
ATOM   3843  CD1 ILE B 250       6.609 118.382  38.898  1.00 29.76           C  
ATOM   3844  N   TRP B 251       8.121 113.590  41.185  1.00 29.07           N  
ATOM   3845  CA  TRP B 251       8.129 112.426  42.081  1.00 28.25           C  
ATOM   3846  C   TRP B 251       9.045 112.684  43.278  1.00 27.82           C  
ATOM   3847  O   TRP B 251       8.627 112.554  44.434  1.00 27.79           O  
ATOM   3848  CB  TRP B 251       8.544 111.147  41.329  1.00 28.09           C  
ATOM   3849  CG  TRP B 251       8.738 109.941  42.216  1.00 27.89           C  
ATOM   3850  CD1 TRP B 251       9.859 109.619  42.928  1.00 28.05           C  
ATOM   3851  CD2 TRP B 251       7.786 108.906  42.490  1.00 27.74           C  
ATOM   3852  NE1 TRP B 251       9.664 108.452  43.628  1.00 27.77           N  
ATOM   3853  CE2 TRP B 251       8.400 107.992  43.379  1.00 27.61           C  
ATOM   3854  CE3 TRP B 251       6.471 108.654  42.077  1.00 28.20           C  
ATOM   3855  CZ2 TRP B 251       7.749 106.852  43.858  1.00 27.79           C  
ATOM   3856  CZ3 TRP B 251       5.819 107.520  42.559  1.00 28.32           C  
ATOM   3857  CH2 TRP B 251       6.462 106.635  43.440  1.00 28.31           C  
ATOM   3858  N   SER B 252      10.283 113.070  42.984  1.00 27.15           N  
ATOM   3859  CA  SER B 252      11.266 113.387  44.007  1.00 26.63           C  
ATOM   3860  C   SER B 252      10.683 114.344  45.041  1.00 26.24           C  
ATOM   3861  O   SER B 252      10.646 114.030  46.232  1.00 26.08           O  
ATOM   3862  CB  SER B 252      12.521 113.986  43.369  1.00 26.70           C  
ATOM   3863  OG  SER B 252      13.173 113.047  42.528  1.00 26.91           O  
ATOM   3864  N   MET B 253      10.204 115.493  44.566  1.00 25.81           N  
ATOM   3865  CA  MET B 253       9.643 116.535  45.423  1.00 25.25           C  
ATOM   3866  C   MET B 253       8.473 115.997  46.219  1.00 25.17           C  
ATOM   3867  O   MET B 253       8.344 116.284  47.404  1.00 25.06           O  
ATOM   3868  CB  MET B 253       9.204 117.738  44.584  1.00 25.21           C  
ATOM   3869  CG  MET B 253       8.474 118.841  45.355  1.00 24.18           C  
ATOM   3870  SD  MET B 253       7.430 119.859  44.289  1.00 21.68           S  
ATOM   3871  CE  MET B 253       6.023 118.852  44.097  1.00 20.74           C  
ATOM   3872  N   GLY B 254       7.630 115.210  45.560  1.00 25.23           N  
ATOM   3873  CA  GLY B 254       6.472 114.613  46.199  1.00 25.46           C  
ATOM   3874  C   GLY B 254       6.848 113.786  47.410  1.00 25.54           C  
ATOM   3875  O   GLY B 254       6.365 114.041  48.514  1.00 25.57           O  
ATOM   3876  N   LEU B 255       7.726 112.808  47.199  1.00 25.54           N  
ATOM   3877  CA  LEU B 255       8.204 111.952  48.274  1.00 25.57           C  
ATOM   3878  C   LEU B 255       8.851 112.770  49.386  1.00 25.72           C  
ATOM   3879  O   LEU B 255       8.510 112.609  50.554  1.00 25.71           O  
ATOM   3880  CB  LEU B 255       9.189 110.915  47.734  1.00 25.59           C  
ATOM   3881  CG  LEU B 255       9.183 109.550  48.428  1.00 25.15           C  
ATOM   3882  CD1 LEU B 255       8.386 108.534  47.633  1.00 25.08           C  
ATOM   3883  CD2 LEU B 255      10.593 109.064  48.635  1.00 24.63           C  
ATOM   3884  N   SER B 256       9.767 113.657  49.005  1.00 25.98           N  
ATOM   3885  CA  SER B 256      10.445 114.556  49.935  1.00 26.34           C  
ATOM   3886  C   SER B 256       9.483 115.321  50.854  1.00 26.74           C  
ATOM   3887  O   SER B 256       9.768 115.515  52.035  1.00 26.84           O  
ATOM   3888  CB  SER B 256      11.319 115.547  49.162  1.00 26.33           C  
ATOM   3889  OG  SER B 256      12.300 114.884  48.379  1.00 26.09           O  
ATOM   3890  N   LEU B 257       8.349 115.753  50.307  1.00 27.16           N  
ATOM   3891  CA  LEU B 257       7.327 116.430  51.098  1.00 27.59           C  
ATOM   3892  C   LEU B 257       6.664 115.459  52.060  1.00 27.96           C  
ATOM   3893  O   LEU B 257       6.516 115.765  53.236  1.00 28.12           O  
ATOM   3894  CB  LEU B 257       6.273 117.086  50.199  1.00 27.64           C  
ATOM   3895  CG  LEU B 257       6.678 118.333  49.406  1.00 27.35           C  
ATOM   3896  CD1 LEU B 257       5.665 118.613  48.301  1.00 26.70           C  
ATOM   3897  CD2 LEU B 257       6.850 119.540  50.314  1.00 26.78           C  
ATOM   3898  N   VAL B 258       6.284 114.288  51.553  1.00 28.50           N  
ATOM   3899  CA  VAL B 258       5.688 113.222  52.365  1.00 29.10           C  
ATOM   3900  C   VAL B 258       6.621 112.764  53.494  1.00 29.61           C  
ATOM   3901  O   VAL B 258       6.158 112.369  54.560  1.00 29.66           O  
ATOM   3902  CB  VAL B 258       5.270 112.011  51.493  1.00 29.02           C  
ATOM   3903  CG1 VAL B 258       4.616 110.921  52.334  1.00 29.06           C  
ATOM   3904  CG2 VAL B 258       4.318 112.449  50.396  1.00 28.90           C  
ATOM   3905  N   GLU B 259       7.929 112.824  53.252  1.00 30.31           N  
ATOM   3906  CA  GLU B 259       8.927 112.538  54.276  1.00 30.99           C  
ATOM   3907  C   GLU B 259       8.821 113.551  55.407  1.00 31.66           C  
ATOM   3908  O   GLU B 259       8.576 113.175  56.548  1.00 31.86           O  
ATOM   3909  CB  GLU B 259      10.338 112.549  53.677  1.00 30.95           C  
ATOM   3910  CG  GLU B 259      11.476 112.617  54.692  1.00 30.58           C  
ATOM   3911  CD  GLU B 259      12.784 112.070  54.149  1.00 29.99           C  
ATOM   3912  OE1 GLU B 259      13.861 112.529  54.584  1.00 29.44           O  
ATOM   3913  OE2 GLU B 259      12.739 111.176  53.282  1.00 30.14           O  
ATOM   3914  N   LEU B 260       8.985 114.832  55.082  1.00 32.54           N  
ATOM   3915  CA  LEU B 260       8.938 115.899  56.087  1.00 33.46           C  
ATOM   3916  C   LEU B 260       7.561 116.006  56.754  1.00 34.06           C  
ATOM   3917  O   LEU B 260       7.439 116.485  57.881  1.00 34.13           O  
ATOM   3918  CB  LEU B 260       9.349 117.246  55.482  1.00 33.33           C  
ATOM   3919  CG  LEU B 260      10.659 117.298  54.689  1.00 33.47           C  
ATOM   3920  CD1 LEU B 260      10.538 118.252  53.517  1.00 33.53           C  
ATOM   3921  CD2 LEU B 260      11.839 117.689  55.569  1.00 33.60           C  
ATOM   3922  N   ALA B 261       6.534 115.544  56.052  1.00 34.86           N  
ATOM   3923  CA  ALA B 261       5.185 115.542  56.583  1.00 35.79           C  
ATOM   3924  C   ALA B 261       5.053 114.521  57.709  1.00 36.60           C  
ATOM   3925  O   ALA B 261       4.739 114.878  58.850  1.00 36.90           O  
ATOM   3926  CB  ALA B 261       4.190 115.252  55.477  1.00 35.59           C  
ATOM   3927  N   VAL B 262       5.311 113.256  57.381  1.00 37.46           N  
ATOM   3928  CA  VAL B 262       5.132 112.149  58.313  1.00 38.13           C  
ATOM   3929  C   VAL B 262       6.230 112.143  59.372  1.00 38.86           C  
ATOM   3930  O   VAL B 262       5.949 111.964  60.557  1.00 39.25           O  
ATOM   3931  CB  VAL B 262       5.066 110.787  57.586  1.00 38.00           C  
ATOM   3932  CG1 VAL B 262       4.785 109.663  58.569  1.00 38.28           C  
ATOM   3933  CG2 VAL B 262       3.995 110.802  56.498  1.00 37.82           C  
ATOM   3934  N   GLY B 263       7.473 112.353  58.951  1.00 39.55           N  
ATOM   3935  CA  GLY B 263       8.578 112.444  59.890  1.00 40.51           C  
ATOM   3936  C   GLY B 263       9.796 111.638  59.489  1.00 41.29           C  
ATOM   3937  O   GLY B 263      10.922 111.998  59.847  1.00 41.48           O  
ATOM   3938  N   ARG B 264       9.575 110.548  58.753  1.00 41.89           N  
ATOM   3939  CA  ARG B 264      10.673 109.733  58.228  1.00 42.52           C  
ATOM   3940  C   ARG B 264      10.504 109.393  56.743  1.00 42.78           C  
ATOM   3941  O   ARG B 264       9.457 109.666  56.143  1.00 42.83           O  
ATOM   3942  CB  ARG B 264      10.840 108.453  59.053  1.00 42.65           C  
ATOM   3943  CG  ARG B 264       9.601 107.573  59.102  1.00 43.31           C  
ATOM   3944  CD  ARG B 264       9.889 106.113  59.369  1.00 44.46           C  
ATOM   3945  NE  ARG B 264       8.778 105.267  58.939  1.00 45.35           N  
ATOM   3946  CZ  ARG B 264       8.810 104.460  57.884  1.00 45.96           C  
ATOM   3947  NH1 ARG B 264       9.904 104.373  57.136  1.00 46.27           N  
ATOM   3948  NH2 ARG B 264       7.746 103.731  57.577  1.00 46.26           N  
ATOM   3949  N   TYR B 265      11.549 108.806  56.162  1.00 43.10           N  
ATOM   3950  CA  TYR B 265      11.516 108.306  54.792  1.00 43.51           C  
ATOM   3951  C   TYR B 265      10.340 107.332  54.617  1.00 44.11           C  
ATOM   3952  O   TYR B 265      10.325 106.262  55.216  1.00 44.13           O  
ATOM   3953  CB  TYR B 265      12.853 107.640  54.445  1.00 43.27           C  
ATOM   3954  CG  TYR B 265      12.908 107.058  53.058  1.00 42.72           C  
ATOM   3955  CD1 TYR B 265      13.163 107.865  51.951  1.00 42.29           C  
ATOM   3956  CD2 TYR B 265      12.696 105.698  52.848  1.00 42.33           C  
ATOM   3957  CE1 TYR B 265      13.207 107.331  50.674  1.00 41.74           C  
ATOM   3958  CE2 TYR B 265      12.745 105.157  51.581  1.00 41.67           C  
ATOM   3959  CZ  TYR B 265      12.995 105.978  50.501  1.00 41.51           C  
ATOM   3960  OH  TYR B 265      13.033 105.441  49.246  1.00 41.47           O  
ATOM   3961  N   PRO B 266       9.356 107.711  53.805  1.00 44.80           N  
ATOM   3962  CA  PRO B 266       8.054 107.039  53.798  1.00 45.49           C  
ATOM   3963  C   PRO B 266       7.872 105.908  52.780  1.00 46.24           C  
ATOM   3964  O   PRO B 266       6.728 105.504  52.564  1.00 46.23           O  
ATOM   3965  CB  PRO B 266       7.111 108.184  53.444  1.00 45.47           C  
ATOM   3966  CG  PRO B 266       7.931 109.047  52.507  1.00 45.12           C  
ATOM   3967  CD  PRO B 266       9.390 108.821  52.837  1.00 44.82           C  
ATOM   3968  N   ILE B 267       8.944 105.404  52.175  1.00 47.22           N  
ATOM   3969  CA  ILE B 267       8.782 104.397  51.119  1.00 48.25           C  
ATOM   3970  C   ILE B 267       8.375 103.001  51.602  1.00 48.97           C  
ATOM   3971  O   ILE B 267       7.697 102.281  50.865  1.00 49.22           O  
ATOM   3972  CB  ILE B 267       9.974 104.379  50.127  1.00 48.29           C  
ATOM   3973  CG1 ILE B 267       9.564 105.018  48.792  1.00 48.01           C  
ATOM   3974  CG2 ILE B 267      10.524 102.959  49.922  1.00 48.66           C  
ATOM   3975  CD1 ILE B 267       8.193 104.586  48.271  1.00 47.37           C  
ATOM   3976  N   PRO B 268       8.790 102.593  52.804  1.00 49.59           N  
ATOM   3977  CA  PRO B 268       7.980 101.637  53.560  1.00 50.08           C  
ATOM   3978  C   PRO B 268       6.842 102.470  54.165  1.00 50.82           C  
ATOM   3979  O   PRO B 268       7.082 103.161  55.162  1.00 50.87           O  
ATOM   3980  CB  PRO B 268       8.940 101.125  54.639  1.00 49.95           C  
ATOM   3981  CG  PRO B 268      10.286 101.692  54.290  1.00 49.68           C  
ATOM   3982  CD  PRO B 268      10.036 102.938  53.512  1.00 49.53           C  
ATOM   3983  N   PRO B 269       5.651 102.454  53.553  1.00 51.36           N  
ATOM   3984  CA  PRO B 269       4.555 103.332  53.975  1.00 51.82           C  
ATOM   3985  C   PRO B 269       4.081 102.976  55.379  1.00 52.45           C  
ATOM   3986  O   PRO B 269       3.663 101.837  55.591  1.00 52.44           O  
ATOM   3987  CB  PRO B 269       3.460 103.048  52.937  1.00 51.78           C  
ATOM   3988  CG  PRO B 269       4.176 102.431  51.789  1.00 51.43           C  
ATOM   3989  CD  PRO B 269       5.242 101.596  52.427  1.00 51.40           C  
ATOM   3990  N   PRO B 270       4.169 103.927  56.313  1.00 53.12           N  
ATOM   3991  CA  PRO B 270       3.819 103.690  57.719  1.00 53.72           C  
ATOM   3992  C   PRO B 270       2.446 103.055  57.904  1.00 54.46           C  
ATOM   3993  O   PRO B 270       1.474 103.444  57.249  1.00 54.29           O  
ATOM   3994  CB  PRO B 270       3.852 105.093  58.326  1.00 53.68           C  
ATOM   3995  CG  PRO B 270       4.820 105.838  57.484  1.00 53.45           C  
ATOM   3996  CD  PRO B 270       4.626 105.312  56.090  1.00 53.21           C  
ATOM   3997  N   ASP B 271       2.394 102.073  58.800  1.00 55.51           N  
ATOM   3998  CA  ASP B 271       1.214 101.236  59.006  1.00 56.59           C  
ATOM   3999  C   ASP B 271       0.123 101.932  59.822  1.00 57.14           C  
ATOM   4000  O   ASP B 271       0.223 103.121  60.131  1.00 57.07           O  
ATOM   4001  CB  ASP B 271       1.613  99.896  59.655  1.00 56.66           C  
ATOM   4002  CG  ASP B 271       2.411 100.076  60.949  1.00 57.29           C  
ATOM   4003  OD1 ASP B 271       1.814 100.443  61.988  1.00 57.77           O  
ATOM   4004  OD2 ASP B 271       3.642  99.867  61.021  1.00 57.60           O  
ATOM   4005  N   ALA B 272      -0.912 101.168  60.169  1.00 58.02           N  
ATOM   4006  CA  ALA B 272      -2.051 101.665  60.939  1.00 58.92           C  
ATOM   4007  C   ALA B 272      -1.672 102.307  62.282  1.00 59.50           C  
ATOM   4008  O   ALA B 272      -2.390 103.186  62.768  1.00 59.56           O  
ATOM   4009  CB  ALA B 272      -3.077 100.546  61.149  1.00 58.89           C  
ATOM   4010  N   LYS B 273      -0.552 101.874  62.868  1.00 60.20           N  
ATOM   4011  CA  LYS B 273      -0.115 102.374  64.179  1.00 60.91           C  
ATOM   4012  C   LYS B 273       1.296 102.983  64.189  1.00 61.24           C  
ATOM   4013  O   LYS B 273       1.776 103.436  65.234  1.00 61.20           O  
ATOM   4014  CB  LYS B 273      -0.246 101.274  65.252  1.00 60.95           C  
ATOM   4015  CG  LYS B 273       0.861 100.215  65.228  1.00 61.48           C  
ATOM   4016  CD  LYS B 273       0.489  98.979  66.044  1.00 61.81           C  
ATOM   4017  CE  LYS B 273       1.586  97.920  65.974  1.00 61.72           C  
ATOM   4018  NZ  LYS B 273       1.580  97.190  64.672  1.00 61.65           N  
ATOM   4019  N   GLU B 274       1.951 102.996  63.029  1.00 61.75           N  
ATOM   4020  CA  GLU B 274       3.303 103.546  62.914  1.00 62.29           C  
ATOM   4021  C   GLU B 274       3.336 105.043  63.226  1.00 62.53           C  
ATOM   4022  O   GLU B 274       4.129 105.497  64.055  1.00 62.45           O  
ATOM   4023  CB  GLU B 274       3.884 103.276  61.521  1.00 62.26           C  
ATOM   4024  CG  GLU B 274       5.256 102.622  61.545  1.00 62.82           C  
ATOM   4025  CD  GLU B 274       6.171 103.105  60.433  1.00 63.33           C  
ATOM   4026  OE1 GLU B 274       6.299 102.384  59.416  1.00 63.55           O  
ATOM   4027  OE2 GLU B 274       6.772 104.194  60.581  1.00 63.11           O  
ATOM   4028  N   LEU B 275       2.452 105.791  62.568  1.00 62.96           N  
ATOM   4029  CA  LEU B 275       2.360 107.242  62.720  1.00 63.38           C  
ATOM   4030  C   LEU B 275       1.715 107.644  64.049  1.00 63.73           C  
ATOM   4031  O   LEU B 275       1.766 108.813  64.443  1.00 63.79           O  
ATOM   4032  CB  LEU B 275       1.578 107.865  61.551  1.00 63.37           C  
ATOM   4033  CG  LEU B 275       1.216 107.031  60.316  1.00 63.27           C  
ATOM   4034  CD1 LEU B 275      -0.219 106.522  60.387  1.00 62.92           C  
ATOM   4035  CD2 LEU B 275       1.432 107.837  59.043  1.00 63.45           C  
ATOM   4036  N   GLU B 276       1.112 106.668  64.728  1.00 64.10           N  
ATOM   4037  CA  GLU B 276       0.442 106.881  66.012  1.00 64.37           C  
ATOM   4038  C   GLU B 276       1.393 107.393  67.101  1.00 64.59           C  
ATOM   4039  O   GLU B 276       0.955 108.002  68.078  1.00 64.54           O  
ATOM   4040  CB  GLU B 276      -0.246 105.589  66.458  1.00 64.37           C  
ATOM   4041  CG  GLU B 276      -1.479 105.783  67.324  1.00 64.39           C  
ATOM   4042  CD  GLU B 276      -1.361 105.072  68.658  1.00 64.71           C  
ATOM   4043  OE1 GLU B 276      -1.093 103.847  68.669  1.00 64.95           O  
ATOM   4044  OE2 GLU B 276      -1.531 105.741  69.700  1.00 65.09           O  
ATOM   4045  N   ALA B 277       2.692 107.151  66.920  1.00 64.96           N  
ATOM   4046  CA  ALA B 277       3.725 107.706  67.795  1.00 65.35           C  
ATOM   4047  C   ALA B 277       3.876 109.220  67.599  1.00 65.71           C  
ATOM   4048  O   ALA B 277       4.818 109.834  68.114  1.00 65.79           O  
ATOM   4049  CB  ALA B 277       5.053 106.997  67.563  1.00 65.26           C  
ATOM   4050  N   ILE B 278       2.947 109.807  66.840  1.00 66.12           N  
ATOM   4051  CA  ILE B 278       2.899 111.253  66.599  1.00 66.38           C  
ATOM   4052  C   ILE B 278       1.508 111.867  66.876  1.00 66.77           C  
ATOM   4053  O   ILE B 278       1.418 113.029  67.284  1.00 66.84           O  
ATOM   4054  CB  ILE B 278       3.380 111.611  65.157  1.00 66.21           C  
ATOM   4055  CG1 ILE B 278       4.448 110.625  64.640  1.00 65.94           C  
ATOM   4056  CG2 ILE B 278       3.864 113.051  65.101  1.00 66.16           C  
ATOM   4057  CD1 ILE B 278       5.880 110.892  65.105  1.00 65.44           C  
ATOM   4058  N   PHE B 279       0.439 111.092  66.656  1.00 67.16           N  
ATOM   4059  CA  PHE B 279      -0.944 111.553  66.885  1.00 67.47           C  
ATOM   4060  C   PHE B 279      -1.924 110.423  67.274  1.00 67.50           C  
ATOM   4061  O   PHE B 279      -1.589 109.241  67.187  1.00 67.49           O  
ATOM   4062  CB  PHE B 279      -1.467 112.330  65.661  1.00 67.59           C  
ATOM   4063  CG  PHE B 279      -2.331 113.528  66.008  1.00 68.05           C  
ATOM   4064  CD1 PHE B 279      -1.762 114.701  66.506  1.00 68.22           C  
ATOM   4065  CD2 PHE B 279      -3.716 113.486  65.818  1.00 68.27           C  
ATOM   4066  CE1 PHE B 279      -2.559 115.808  66.816  1.00 68.46           C  
ATOM   4067  CE2 PHE B 279      -4.521 114.588  66.125  1.00 68.15           C  
ATOM   4068  CZ  PHE B 279      -3.942 115.750  66.624  1.00 68.37           C  
ATOM   4069  N   GLY B 280      -3.132 110.806  67.692  1.00 67.59           N  
ATOM   4070  CA  GLY B 280      -4.136 109.881  68.197  1.00 67.62           C  
ATOM   4071  C   GLY B 280      -4.731 108.921  67.184  1.00 67.69           C  
ATOM   4072  O   GLY B 280      -4.577 107.710  67.322  1.00 67.70           O  
ATOM   4073  N   ARG B 281      -5.417 109.457  66.176  1.00 67.88           N  
ATOM   4074  CA  ARG B 281      -6.103 108.634  65.170  1.00 68.08           C  
ATOM   4075  C   ARG B 281      -5.140 107.960  64.191  1.00 68.06           C  
ATOM   4076  O   ARG B 281      -5.158 106.737  64.033  1.00 67.98           O  
ATOM   4077  CB  ARG B 281      -7.146 109.460  64.403  1.00 68.11           C  
ATOM   4078  CG  ARG B 281      -8.588 108.968  64.564  1.00 68.42           C  
ATOM   4079  CD  ARG B 281      -9.250 109.374  65.886  1.00 69.03           C  
ATOM   4080  NE  ARG B 281     -10.715 109.393  65.815  1.00 69.00           N  
ATOM   4081  CZ  ARG B 281     -11.529 109.138  66.840  1.00 68.67           C  
ATOM   4082  NH1 ARG B 281     -11.036 108.832  68.038  1.00 68.28           N  
ATOM   4083  NH2 ARG B 281     -12.845 109.188  66.667  1.00 68.40           N  
ATOM   4084  N   MET B 316      14.082  97.058  53.520  1.00 52.50           N  
ATOM   4085  CA  MET B 316      15.356  97.230  54.215  1.00 52.62           C  
ATOM   4086  C   MET B 316      16.559  96.980  53.288  1.00 52.38           C  
ATOM   4087  O   MET B 316      17.568  97.695  53.360  1.00 52.42           O  
ATOM   4088  CB  MET B 316      15.421  96.328  55.454  1.00 52.72           C  
ATOM   4089  CG  MET B 316      15.282  97.081  56.778  1.00 53.88           C  
ATOM   4090  SD  MET B 316      14.550  96.075  58.114  1.00 56.41           S  
ATOM   4091  CE  MET B 316      14.220  97.330  59.389  1.00 55.28           C  
ATOM   4092  N   ALA B 317      16.443  95.964  52.428  1.00 51.97           N  
ATOM   4093  CA  ALA B 317      17.467  95.647  51.428  1.00 51.36           C  
ATOM   4094  C   ALA B 317      17.401  96.641  50.273  1.00 50.93           C  
ATOM   4095  O   ALA B 317      16.354  97.248  50.038  1.00 51.00           O  
ATOM   4096  CB  ALA B 317      17.287  94.224  50.916  1.00 51.37           C  
ATOM   4097  N   ILE B 318      18.513  96.803  49.557  1.00 50.24           N  
ATOM   4098  CA  ILE B 318      18.595  97.785  48.471  1.00 49.56           C  
ATOM   4099  C   ILE B 318      17.831  97.380  47.207  1.00 49.00           C  
ATOM   4100  O   ILE B 318      17.344  98.236  46.471  1.00 48.95           O  
ATOM   4101  CB  ILE B 318      20.060  98.149  48.130  1.00 49.67           C  
ATOM   4102  CG1 ILE B 318      21.055  97.275  48.910  1.00 49.94           C  
ATOM   4103  CG2 ILE B 318      20.299  99.636  48.397  1.00 49.75           C  
ATOM   4104  CD1 ILE B 318      22.394  97.031  48.188  1.00 50.14           C  
ATOM   4105  N   PHE B 319      17.729  96.079  46.961  1.00 48.29           N  
ATOM   4106  CA  PHE B 319      16.946  95.581  45.837  1.00 47.55           C  
ATOM   4107  C   PHE B 319      15.479  95.567  46.210  1.00 47.32           C  
ATOM   4108  O   PHE B 319      14.624  95.852  45.376  1.00 47.41           O  
ATOM   4109  CB  PHE B 319      17.404  94.174  45.433  1.00 47.45           C  
ATOM   4110  CG  PHE B 319      16.657  93.596  44.258  1.00 46.11           C  
ATOM   4111  CD1 PHE B 319      16.893  94.057  42.970  1.00 44.99           C  
ATOM   4112  CD2 PHE B 319      15.732  92.577  44.443  1.00 44.97           C  
ATOM   4113  CE1 PHE B 319      16.211  93.520  41.889  1.00 44.52           C  
ATOM   4114  CE2 PHE B 319      15.047  92.032  43.365  1.00 44.50           C  
ATOM   4115  CZ  PHE B 319      15.287  92.505  42.087  1.00 44.15           C  
ATOM   4116  N   GLU B 320      15.204  95.230  47.469  1.00 47.01           N  
ATOM   4117  CA  GLU B 320      13.845  95.191  48.011  1.00 46.75           C  
ATOM   4118  C   GLU B 320      13.188  96.563  47.925  1.00 46.41           C  
ATOM   4119  O   GLU B 320      12.019  96.685  47.543  1.00 46.28           O  
ATOM   4120  CB  GLU B 320      13.877  94.721  49.466  1.00 46.83           C  
ATOM   4121  CG  GLU B 320      12.946  93.561  49.769  1.00 47.06           C  
ATOM   4122  CD  GLU B 320      11.887  93.925  50.788  1.00 47.28           C  
ATOM   4123  OE1 GLU B 320      10.702  94.037  50.402  1.00 47.13           O  
ATOM   4124  OE2 GLU B 320      12.244  94.101  51.974  1.00 47.46           O  
ATOM   4125  N   LEU B 321      13.969  97.579  48.290  1.00 46.05           N  
ATOM   4126  CA  LEU B 321      13.603  98.983  48.165  1.00 45.61           C  
ATOM   4127  C   LEU B 321      13.206  99.308  46.737  1.00 45.34           C  
ATOM   4128  O   LEU B 321      12.057  99.654  46.469  1.00 45.45           O  
ATOM   4129  CB  LEU B 321      14.786  99.857  48.574  1.00 45.52           C  
ATOM   4130  CG  LEU B 321      14.551 101.104  49.421  1.00 45.78           C  
ATOM   4131  CD1 LEU B 321      14.461 102.329  48.535  1.00 46.05           C  
ATOM   4132  CD2 LEU B 321      13.316 100.977  50.305  1.00 46.06           C  
ATOM   4133  N   LEU B 322      14.160  99.173  45.823  1.00 44.96           N  
ATOM   4134  CA  LEU B 322      13.935  99.460  44.413  1.00 44.63           C  
ATOM   4135  C   LEU B 322      12.717  98.721  43.871  1.00 44.51           C  
ATOM   4136  O   LEU B 322      12.008  99.242  43.014  1.00 44.45           O  
ATOM   4137  CB  LEU B 322      15.181  99.115  43.600  1.00 44.60           C  
ATOM   4138  CG  LEU B 322      16.137 100.251  43.213  1.00 44.51           C  
ATOM   4139  CD1 LEU B 322      16.793 100.934  44.422  1.00 44.06           C  
ATOM   4140  CD2 LEU B 322      17.200  99.719  42.266  1.00 44.40           C  
ATOM   4141  N   ASP B 323      12.472  97.517  44.387  1.00 44.43           N  
ATOM   4142  CA  ASP B 323      11.309  96.729  43.989  1.00 44.39           C  
ATOM   4143  C   ASP B 323      10.022  97.386  44.467  1.00 44.17           C  
ATOM   4144  O   ASP B 323       9.031  97.420  43.732  1.00 44.17           O  
ATOM   4145  CB  ASP B 323      11.397  95.289  44.513  1.00 44.58           C  
ATOM   4146  CG  ASP B 323      10.385  94.355  43.845  1.00 45.23           C  
ATOM   4147  OD1 ASP B 323      10.778  93.612  42.919  1.00 46.02           O  
ATOM   4148  OD2 ASP B 323       9.177  94.291  44.176  1.00 45.75           O  
ATOM   4149  N   TYR B 324      10.042  97.907  45.693  1.00 43.86           N  
ATOM   4150  CA  TYR B 324       8.865  98.551  46.271  1.00 43.56           C  
ATOM   4151  C   TYR B 324       8.467  99.797  45.484  1.00 43.07           C  
ATOM   4152  O   TYR B 324       7.312  99.936  45.081  1.00 43.06           O  
ATOM   4153  CB  TYR B 324       9.090  98.895  47.745  1.00 43.76           C  
ATOM   4154  CG  TYR B 324       7.827  98.855  48.579  1.00 44.58           C  
ATOM   4155  CD1 TYR B 324       7.468  97.703  49.279  1.00 45.29           C  
ATOM   4156  CD2 TYR B 324       6.989  99.968  48.669  1.00 45.21           C  
ATOM   4157  CE1 TYR B 324       6.307  97.660  50.046  1.00 45.78           C  
ATOM   4158  CE2 TYR B 324       5.825  99.935  49.432  1.00 45.39           C  
ATOM   4159  CZ  TYR B 324       5.491  98.780  50.119  1.00 45.78           C  
ATOM   4160  OH  TYR B 324       4.340  98.735  50.877  1.00 46.11           O  
ATOM   4161  N   ILE B 325       9.435 100.683  45.255  1.00 42.39           N  
ATOM   4162  CA  ILE B 325       9.209 101.912  44.502  1.00 41.69           C  
ATOM   4163  C   ILE B 325       8.609 101.616  43.128  1.00 41.58           C  
ATOM   4164  O   ILE B 325       7.642 102.258  42.718  1.00 41.76           O  
ATOM   4165  CB  ILE B 325      10.524 102.714  44.366  1.00 41.45           C  
ATOM   4166  CG1 ILE B 325      11.034 103.138  45.743  1.00 40.87           C  
ATOM   4167  CG2 ILE B 325      10.326 103.932  43.474  1.00 41.24           C  
ATOM   4168  CD1 ILE B 325      12.499 103.482  45.770  1.00 40.44           C  
ATOM   4169  N   VAL B 326       9.173 100.627  42.439  1.00 41.28           N  
ATOM   4170  CA  VAL B 326       8.797 100.312  41.061  1.00 40.98           C  
ATOM   4171  C   VAL B 326       7.458  99.574  40.954  1.00 40.93           C  
ATOM   4172  O   VAL B 326       6.665  99.854  40.050  1.00 41.01           O  
ATOM   4173  CB  VAL B 326       9.917  99.499  40.354  1.00 40.92           C  
ATOM   4174  CG1 VAL B 326       9.394  98.783  39.114  1.00 40.85           C  
ATOM   4175  CG2 VAL B 326      11.097 100.397  40.001  1.00 40.78           C  
ATOM   4176  N   ASN B 327       7.210  98.645  41.880  1.00 40.72           N  
ATOM   4177  CA  ASN B 327       6.107  97.692  41.742  1.00 40.47           C  
ATOM   4178  C   ASN B 327       4.975  97.812  42.765  1.00 40.20           C  
ATOM   4179  O   ASN B 327       3.896  97.251  42.564  1.00 40.25           O  
ATOM   4180  CB  ASN B 327       6.646  96.256  41.721  1.00 40.59           C  
ATOM   4181  CG  ASN B 327       7.475  95.958  40.478  1.00 40.92           C  
ATOM   4182  OD1 ASN B 327       8.683  95.738  40.567  1.00 41.17           O  
ATOM   4183  ND2 ASN B 327       6.825  95.944  39.314  1.00 41.13           N  
ATOM   4184  N   GLU B 328       5.214  98.543  43.848  1.00 39.79           N  
ATOM   4185  CA  GLU B 328       4.197  98.728  44.880  1.00 39.42           C  
ATOM   4186  C   GLU B 328       3.650 100.167  44.915  1.00 39.01           C  
ATOM   4187  O   GLU B 328       4.348 101.106  44.513  1.00 39.08           O  
ATOM   4188  CB  GLU B 328       4.754  98.308  46.248  1.00 39.48           C  
ATOM   4189  CG  GLU B 328       4.133  97.042  46.839  1.00 40.28           C  
ATOM   4190  CD  GLU B 328       3.673  96.032  45.790  1.00 41.09           C  
ATOM   4191  OE1 GLU B 328       2.443  95.905  45.569  1.00 41.02           O  
ATOM   4192  OE2 GLU B 328       4.541  95.355  45.193  1.00 41.67           O  
ATOM   4193  N   PRO B 329       2.403 100.336  45.370  1.00 38.47           N  
ATOM   4194  CA  PRO B 329       1.791 101.659  45.531  1.00 37.98           C  
ATOM   4195  C   PRO B 329       2.683 102.689  46.226  1.00 37.51           C  
ATOM   4196  O   PRO B 329       3.491 102.330  47.087  1.00 37.65           O  
ATOM   4197  CB  PRO B 329       0.566 101.365  46.407  1.00 37.96           C  
ATOM   4198  CG  PRO B 329       0.746  99.966  46.870  1.00 38.11           C  
ATOM   4199  CD  PRO B 329       1.451  99.279  45.747  1.00 38.53           C  
ATOM   4200  N   PRO B 330       2.523 103.959  45.862  1.00 36.98           N  
ATOM   4201  CA  PRO B 330       3.311 105.039  46.457  1.00 36.53           C  
ATOM   4202  C   PRO B 330       2.777 105.420  47.835  1.00 36.11           C  
ATOM   4203  O   PRO B 330       1.624 105.117  48.145  1.00 36.03           O  
ATOM   4204  CB  PRO B 330       3.111 106.198  45.472  1.00 36.57           C  
ATOM   4205  CG  PRO B 330       2.305 105.638  44.332  1.00 36.67           C  
ATOM   4206  CD  PRO B 330       1.567 104.471  44.864  1.00 36.98           C  
ATOM   4207  N   PRO B 331       3.600 106.072  48.650  1.00 35.83           N  
ATOM   4208  CA  PRO B 331       3.150 106.575  49.951  1.00 35.78           C  
ATOM   4209  C   PRO B 331       2.090 107.672  49.814  1.00 35.81           C  
ATOM   4210  O   PRO B 331       2.084 108.426  48.835  1.00 35.80           O  
ATOM   4211  CB  PRO B 331       4.428 107.151  50.563  1.00 35.74           C  
ATOM   4212  CG  PRO B 331       5.296 107.451  49.395  1.00 35.78           C  
ATOM   4213  CD  PRO B 331       5.019 106.377  48.401  1.00 35.74           C  
ATOM   4214  N   LYS B 332       1.196 107.736  50.795  1.00 35.73           N  
ATOM   4215  CA  LYS B 332       0.147 108.741  50.847  1.00 35.61           C  
ATOM   4216  C   LYS B 332       0.262 109.472  52.167  1.00 35.51           C  
ATOM   4217  O   LYS B 332       0.825 108.943  53.121  1.00 35.70           O  
ATOM   4218  CB  LYS B 332      -1.226 108.077  50.751  1.00 35.62           C  
ATOM   4219  CG  LYS B 332      -1.781 107.983  49.337  1.00 36.38           C  
ATOM   4220  CD  LYS B 332      -3.257 107.595  49.344  1.00 37.77           C  
ATOM   4221  CE  LYS B 332      -3.659 106.852  48.066  1.00 38.67           C  
ATOM   4222  NZ  LYS B 332      -4.579 105.695  48.341  1.00 39.22           N  
ATOM   4223  N   LEU B 333      -0.261 110.693  52.221  1.00 35.42           N  
ATOM   4224  CA  LEU B 333      -0.381 111.411  53.484  1.00 35.06           C  
ATOM   4225  C   LEU B 333      -1.644 110.928  54.190  1.00 35.05           C  
ATOM   4226  O   LEU B 333      -2.705 110.863  53.566  1.00 35.14           O  
ATOM   4227  CB  LEU B 333      -0.442 112.919  53.241  1.00 34.98           C  
ATOM   4228  CG  LEU B 333       0.863 113.630  52.887  1.00 34.38           C  
ATOM   4229  CD1 LEU B 333       0.680 115.136  52.909  1.00 34.25           C  
ATOM   4230  CD2 LEU B 333       1.964 113.228  53.831  1.00 34.42           C  
ATOM   4231  N   PRO B 334      -1.538 110.575  55.471  1.00 35.02           N  
ATOM   4232  CA  PRO B 334      -2.691 110.061  56.227  1.00 35.04           C  
ATOM   4233  C   PRO B 334      -3.796 111.110  56.326  1.00 35.09           C  
ATOM   4234  O   PRO B 334      -3.519 112.257  56.694  1.00 34.99           O  
ATOM   4235  CB  PRO B 334      -2.101 109.754  57.610  1.00 35.09           C  
ATOM   4236  CG  PRO B 334      -0.847 110.574  57.698  1.00 35.02           C  
ATOM   4237  CD  PRO B 334      -0.317 110.642  56.295  1.00 35.11           C  
ATOM   4238  N   ASN B 335      -5.027 110.732  55.984  1.00 35.22           N  
ATOM   4239  CA  ASN B 335      -6.114 111.709  55.917  1.00 35.47           C  
ATOM   4240  C   ASN B 335      -6.670 112.084  57.282  1.00 35.42           C  
ATOM   4241  O   ASN B 335      -7.803 111.746  57.622  1.00 35.57           O  
ATOM   4242  CB  ASN B 335      -7.226 111.274  54.952  1.00 35.62           C  
ATOM   4243  CG  ASN B 335      -7.840 109.947  55.320  1.00 36.37           C  
ATOM   4244  OD1 ASN B 335      -7.240 108.899  55.102  1.00 38.31           O  
ATOM   4245  ND2 ASN B 335      -9.050 109.981  55.873  1.00 36.73           N  
ATOM   4246  N   GLY B 336      -5.860 112.799  58.055  1.00 35.38           N  
ATOM   4247  CA  GLY B 336      -6.257 113.236  59.378  1.00 35.24           C  
ATOM   4248  C   GLY B 336      -5.787 114.641  59.664  1.00 35.09           C  
ATOM   4249  O   GLY B 336      -6.580 115.586  59.661  1.00 34.97           O  
ATOM   4250  N   VAL B 337      -4.487 114.773  59.902  1.00 34.95           N  
ATOM   4251  CA  VAL B 337      -3.899 116.054  60.283  1.00 34.92           C  
ATOM   4252  C   VAL B 337      -3.626 117.002  59.092  1.00 34.77           C  
ATOM   4253  O   VAL B 337      -3.532 118.226  59.278  1.00 34.87           O  
ATOM   4254  CB  VAL B 337      -2.634 115.849  61.166  1.00 35.00           C  
ATOM   4255  CG1 VAL B 337      -1.355 115.764  60.321  1.00 34.95           C  
ATOM   4256  CG2 VAL B 337      -2.537 116.933  62.230  1.00 34.90           C  
ATOM   4257  N   PHE B 338      -3.515 116.439  57.886  1.00 34.31           N  
ATOM   4258  CA  PHE B 338      -3.244 117.225  56.680  1.00 33.83           C  
ATOM   4259  C   PHE B 338      -4.520 117.485  55.890  1.00 33.64           C  
ATOM   4260  O   PHE B 338      -5.441 116.659  55.886  1.00 33.68           O  
ATOM   4261  CB  PHE B 338      -2.200 116.542  55.791  1.00 33.76           C  
ATOM   4262  CG  PHE B 338      -0.946 116.142  56.518  1.00 33.64           C  
ATOM   4263  CD1 PHE B 338      -0.084 117.106  57.039  1.00 33.49           C  
ATOM   4264  CD2 PHE B 338      -0.624 114.799  56.682  1.00 33.53           C  
ATOM   4265  CE1 PHE B 338       1.081 116.738  57.716  1.00 33.03           C  
ATOM   4266  CE2 PHE B 338       0.536 114.421  57.355  1.00 33.45           C  
ATOM   4267  CZ  PHE B 338       1.390 115.396  57.874  1.00 33.28           C  
ATOM   4268  N   THR B 339      -4.559 118.634  55.222  1.00 33.26           N  
ATOM   4269  CA  THR B 339      -5.749 119.093  54.515  1.00 32.96           C  
ATOM   4270  C   THR B 339      -5.950 118.364  53.198  1.00 32.76           C  
ATOM   4271  O   THR B 339      -4.979 118.110  52.484  1.00 32.84           O  
ATOM   4272  CB  THR B 339      -5.651 120.594  54.242  1.00 33.00           C  
ATOM   4273  OG1 THR B 339      -4.730 121.194  55.161  1.00 32.66           O  
ATOM   4274  CG2 THR B 339      -6.965 121.267  54.575  1.00 33.40           C  
ATOM   4275  N   PRO B 340      -7.203 118.032  52.874  1.00 32.56           N  
ATOM   4276  CA  PRO B 340      -7.552 117.432  51.579  1.00 32.47           C  
ATOM   4277  C   PRO B 340      -6.784 118.010  50.389  1.00 32.45           C  
ATOM   4278  O   PRO B 340      -6.545 117.286  49.424  1.00 32.77           O  
ATOM   4279  CB  PRO B 340      -9.040 117.759  51.435  1.00 32.37           C  
ATOM   4280  CG  PRO B 340      -9.549 117.836  52.827  1.00 32.46           C  
ATOM   4281  CD  PRO B 340      -8.390 118.174  53.735  1.00 32.51           C  
ATOM   4282  N   ASP B 341      -6.403 119.283  50.451  1.00 32.19           N  
ATOM   4283  CA  ASP B 341      -5.706 119.916  49.334  1.00 31.78           C  
ATOM   4284  C   ASP B 341      -4.208 119.606  49.297  1.00 31.49           C  
ATOM   4285  O   ASP B 341      -3.632 119.466  48.218  1.00 31.29           O  
ATOM   4286  CB  ASP B 341      -5.991 121.413  49.303  1.00 31.79           C  
ATOM   4287  CG  ASP B 341      -7.432 121.708  48.963  1.00 31.80           C  
ATOM   4288  OD1 ASP B 341      -8.121 122.355  49.777  1.00 32.25           O  
ATOM   4289  OD2 ASP B 341      -7.967 121.305  47.909  1.00 32.18           O  
ATOM   4290  N   PHE B 342      -3.586 119.499  50.470  1.00 31.26           N  
ATOM   4291  CA  PHE B 342      -2.208 119.023  50.560  1.00 31.03           C  
ATOM   4292  C   PHE B 342      -2.157 117.540  50.235  1.00 30.90           C  
ATOM   4293  O   PHE B 342      -1.265 117.069  49.521  1.00 30.98           O  
ATOM   4294  CB  PHE B 342      -1.626 119.252  51.948  1.00 30.89           C  
ATOM   4295  CG  PHE B 342      -0.141 119.039  52.022  1.00 30.91           C  
ATOM   4296  CD1 PHE B 342       0.637 119.012  50.867  1.00 31.12           C  
ATOM   4297  CD2 PHE B 342       0.484 118.870  53.245  1.00 30.98           C  
ATOM   4298  CE1 PHE B 342       2.006 118.821  50.932  1.00 31.32           C  
ATOM   4299  CE2 PHE B 342       1.855 118.681  53.319  1.00 31.11           C  
ATOM   4300  CZ  PHE B 342       2.617 118.657  52.159  1.00 31.42           C  
ATOM   4301  N   GLN B 343      -3.124 116.818  50.787  1.00 30.59           N  
ATOM   4302  CA  GLN B 343      -3.364 115.422  50.470  1.00 30.34           C  
ATOM   4303  C   GLN B 343      -3.308 115.197  48.958  1.00 29.85           C  
ATOM   4304  O   GLN B 343      -2.548 114.361  48.474  1.00 29.66           O  
ATOM   4305  CB  GLN B 343      -4.738 115.039  51.019  1.00 30.52           C  
ATOM   4306  CG  GLN B 343      -5.193 113.632  50.732  1.00 31.35           C  
ATOM   4307  CD  GLN B 343      -5.801 112.993  51.952  1.00 32.29           C  
ATOM   4308  OE1 GLN B 343      -5.077 112.522  52.828  1.00 32.30           O  
ATOM   4309  NE2 GLN B 343      -7.133 112.987  52.027  1.00 32.85           N  
ATOM   4310  N   GLU B 344      -4.109 115.975  48.230  1.00 29.40           N  
ATOM   4311  CA  GLU B 344      -4.251 115.854  46.784  1.00 28.84           C  
ATOM   4312  C   GLU B 344      -2.981 116.252  46.053  1.00 28.30           C  
ATOM   4313  O   GLU B 344      -2.633 115.643  45.041  1.00 28.18           O  
ATOM   4314  CB  GLU B 344      -5.402 116.727  46.302  1.00 28.89           C  
ATOM   4315  CG  GLU B 344      -6.494 115.972  45.582  1.00 29.72           C  
ATOM   4316  CD  GLU B 344      -7.664 116.869  45.238  1.00 31.24           C  
ATOM   4317  OE1 GLU B 344      -8.586 117.004  46.083  1.00 31.50           O  
ATOM   4318  OE2 GLU B 344      -7.650 117.443  44.125  1.00 31.61           O  
ATOM   4319  N   PHE B 345      -2.303 117.278  46.568  1.00 27.63           N  
ATOM   4320  CA  PHE B 345      -1.068 117.769  45.974  1.00 27.03           C  
ATOM   4321  C   PHE B 345      -0.021 116.657  45.835  1.00 27.18           C  
ATOM   4322  O   PHE B 345       0.409 116.335  44.719  1.00 27.21           O  
ATOM   4323  CB  PHE B 345      -0.508 118.931  46.789  1.00 26.67           C  
ATOM   4324  CG  PHE B 345       0.672 119.595  46.154  1.00 25.52           C  
ATOM   4325  CD1 PHE B 345       0.507 120.431  45.062  1.00 24.45           C  
ATOM   4326  CD2 PHE B 345       1.950 119.377  46.643  1.00 24.77           C  
ATOM   4327  CE1 PHE B 345       1.601 121.039  44.468  1.00 24.44           C  
ATOM   4328  CE2 PHE B 345       3.048 119.983  46.057  1.00 24.44           C  
ATOM   4329  CZ  PHE B 345       2.874 120.816  44.966  1.00 24.21           C  
ATOM   4330  N   VAL B 346       0.366 116.060  46.963  1.00 26.96           N  
ATOM   4331  CA  VAL B 346       1.373 115.001  46.969  1.00 26.85           C  
ATOM   4332  C   VAL B 346       0.914 113.754  46.215  1.00 26.84           C  
ATOM   4333  O   VAL B 346       1.719 113.087  45.564  1.00 26.88           O  
ATOM   4334  CB  VAL B 346       1.818 114.617  48.397  1.00 26.83           C  
ATOM   4335  CG1 VAL B 346       2.494 115.792  49.088  1.00 26.79           C  
ATOM   4336  CG2 VAL B 346       0.645 114.099  49.221  1.00 27.19           C  
ATOM   4337  N   ASN B 347      -0.379 113.452  46.300  1.00 26.88           N  
ATOM   4338  CA  ASN B 347      -0.954 112.320  45.584  1.00 26.98           C  
ATOM   4339  C   ASN B 347      -0.875 112.523  44.082  1.00 26.99           C  
ATOM   4340  O   ASN B 347      -0.946 111.563  43.318  1.00 27.16           O  
ATOM   4341  CB  ASN B 347      -2.404 112.097  46.000  1.00 27.03           C  
ATOM   4342  CG  ASN B 347      -2.530 111.214  47.221  1.00 27.58           C  
ATOM   4343  OD1 ASN B 347      -1.915 111.470  48.262  1.00 28.41           O  
ATOM   4344  ND2 ASN B 347      -3.338 110.168  47.106  1.00 28.12           N  
ATOM   4345  N   LYS B 348      -0.728 113.779  43.667  1.00 26.97           N  
ATOM   4346  CA  LYS B 348      -0.559 114.108  42.258  1.00 26.94           C  
ATOM   4347  C   LYS B 348       0.912 114.042  41.854  1.00 26.96           C  
ATOM   4348  O   LYS B 348       1.229 113.838  40.679  1.00 26.97           O  
ATOM   4349  CB  LYS B 348      -1.153 115.483  41.946  1.00 26.92           C  
ATOM   4350  CG  LYS B 348      -2.649 115.461  41.661  1.00 26.74           C  
ATOM   4351  CD  LYS B 348      -3.042 116.627  40.782  1.00 26.83           C  
ATOM   4352  CE  LYS B 348      -4.525 116.945  40.880  1.00 26.75           C  
ATOM   4353  NZ  LYS B 348      -4.823 118.223  40.160  1.00 26.89           N  
ATOM   4354  N   CYS B 349       1.801 114.212  42.831  1.00 26.92           N  
ATOM   4355  CA  CYS B 349       3.242 114.127  42.594  1.00 26.97           C  
ATOM   4356  C   CYS B 349       3.764 112.702  42.613  1.00 27.09           C  
ATOM   4357  O   CYS B 349       4.873 112.445  42.150  1.00 27.08           O  
ATOM   4358  CB  CYS B 349       4.015 114.920  43.639  1.00 26.82           C  
ATOM   4359  SG  CYS B 349       3.442 116.596  43.856  1.00 26.95           S  
ATOM   4360  N   LEU B 350       2.983 111.782  43.171  1.00 27.18           N  
ATOM   4361  CA  LEU B 350       3.443 110.410  43.331  1.00 27.23           C  
ATOM   4362  C   LEU B 350       2.600 109.402  42.565  1.00 27.37           C  
ATOM   4363  O   LEU B 350       2.337 108.310  43.054  1.00 27.60           O  
ATOM   4364  CB  LEU B 350       3.534 110.041  44.815  1.00 27.20           C  
ATOM   4365  CG  LEU B 350       4.504 110.852  45.683  1.00 27.30           C  
ATOM   4366  CD1 LEU B 350       4.159 110.671  47.146  1.00 27.34           C  
ATOM   4367  CD2 LEU B 350       5.967 110.483  45.427  1.00 27.00           C  
ATOM   4368  N   ILE B 351       2.172 109.776  41.364  1.00 27.54           N  
ATOM   4369  CA  ILE B 351       1.555 108.830  40.443  1.00 27.75           C  
ATOM   4370  C   ILE B 351       2.691 108.211  39.649  1.00 28.06           C  
ATOM   4371  O   ILE B 351       3.498 108.931  39.060  1.00 28.12           O  
ATOM   4372  CB  ILE B 351       0.567 109.543  39.504  1.00 27.64           C  
ATOM   4373  CG1 ILE B 351      -0.650 110.047  40.279  1.00 27.32           C  
ATOM   4374  CG2 ILE B 351       0.129 108.619  38.380  1.00 27.84           C  
ATOM   4375  CD1 ILE B 351      -1.191 111.359  39.758  1.00 27.18           C  
ATOM   4376  N   LYS B 352       2.755 106.882  39.635  1.00 28.48           N  
ATOM   4377  CA  LYS B 352       3.900 106.166  39.056  1.00 28.84           C  
ATOM   4378  C   LYS B 352       4.140 106.463  37.578  1.00 28.83           C  
ATOM   4379  O   LYS B 352       5.253 106.806  37.193  1.00 28.78           O  
ATOM   4380  CB  LYS B 352       3.788 104.659  39.298  1.00 29.06           C  
ATOM   4381  CG  LYS B 352       4.349 104.217  40.648  1.00 29.31           C  
ATOM   4382  CD  LYS B 352       4.678 102.736  40.651  1.00 29.86           C  
ATOM   4383  CE  LYS B 352       3.581 101.940  41.335  1.00 30.42           C  
ATOM   4384  NZ  LYS B 352       4.073 100.613  41.772  1.00 30.52           N  
ATOM   4385  N   ASN B 353       3.099 106.324  36.761  1.00 29.03           N  
ATOM   4386  CA  ASN B 353       3.159 106.726  35.360  1.00 29.27           C  
ATOM   4387  C   ASN B 353       3.481 108.222  35.257  1.00 29.57           C  
ATOM   4388  O   ASN B 353       2.682 109.055  35.687  1.00 29.86           O  
ATOM   4389  CB  ASN B 353       1.824 106.428  34.670  1.00 29.11           C  
ATOM   4390  CG  ASN B 353       1.914 106.461  33.147  1.00 28.77           C  
ATOM   4391  OD1 ASN B 353       1.158 105.767  32.473  1.00 29.32           O  
ATOM   4392  ND2 ASN B 353       2.821 107.270  32.602  1.00 27.34           N  
ATOM   4393  N   PRO B 354       4.641 108.568  34.700  1.00 29.73           N  
ATOM   4394  CA  PRO B 354       5.043 109.976  34.593  1.00 29.83           C  
ATOM   4395  C   PRO B 354       4.031 110.818  33.815  1.00 29.88           C  
ATOM   4396  O   PRO B 354       3.821 111.977  34.169  1.00 29.95           O  
ATOM   4397  CB  PRO B 354       6.382 109.908  33.851  1.00 29.79           C  
ATOM   4398  CG  PRO B 354       6.387 108.576  33.189  1.00 29.99           C  
ATOM   4399  CD  PRO B 354       5.655 107.666  34.127  1.00 29.88           C  
ATOM   4400  N   ALA B 355       3.409 110.240  32.790  1.00 30.04           N  
ATOM   4401  CA  ALA B 355       2.429 110.960  31.977  1.00 30.18           C  
ATOM   4402  C   ALA B 355       1.197 111.313  32.793  1.00 30.19           C  
ATOM   4403  O   ALA B 355       0.705 112.442  32.717  1.00 30.54           O  
ATOM   4404  CB  ALA B 355       2.039 110.154  30.750  1.00 30.26           C  
ATOM   4405  N   GLU B 356       0.713 110.345  33.571  1.00 29.93           N  
ATOM   4406  CA  GLU B 356      -0.441 110.538  34.443  1.00 29.76           C  
ATOM   4407  C   GLU B 356      -0.111 111.531  35.562  1.00 29.42           C  
ATOM   4408  O   GLU B 356      -0.931 112.376  35.924  1.00 29.27           O  
ATOM   4409  CB  GLU B 356      -0.917 109.192  35.008  1.00 29.84           C  
ATOM   4410  CG  GLU B 356      -2.095 108.585  34.254  1.00 30.88           C  
ATOM   4411  CD  GLU B 356      -2.113 107.061  34.274  1.00 32.55           C  
ATOM   4412  OE1 GLU B 356      -2.664 106.481  35.243  1.00 33.09           O  
ATOM   4413  OE2 GLU B 356      -1.590 106.440  33.314  1.00 32.60           O  
ATOM   4414  N   ARG B 357       1.106 111.434  36.085  1.00 29.19           N  
ATOM   4415  CA  ARG B 357       1.595 112.340  37.118  1.00 28.85           C  
ATOM   4416  C   ARG B 357       1.426 113.791  36.702  1.00 28.86           C  
ATOM   4417  O   ARG B 357       1.637 114.140  35.536  1.00 28.94           O  
ATOM   4418  CB  ARG B 357       3.067 112.057  37.396  1.00 28.65           C  
ATOM   4419  CG  ARG B 357       3.620 112.749  38.612  1.00 28.04           C  
ATOM   4420  CD  ARG B 357       4.694 111.959  39.301  1.00 27.47           C  
ATOM   4421  NE  ARG B 357       5.892 111.831  38.478  1.00 26.91           N  
ATOM   4422  CZ  ARG B 357       6.490 110.683  38.186  1.00 26.34           C  
ATOM   4423  NH1 ARG B 357       6.014 109.533  38.644  1.00 25.78           N  
ATOM   4424  NH2 ARG B 357       7.575 110.688  37.429  1.00 26.48           N  
ATOM   4425  N   ALA B 358       1.046 114.627  37.663  1.00 28.85           N  
ATOM   4426  CA  ALA B 358       0.888 116.058  37.430  1.00 28.84           C  
ATOM   4427  C   ALA B 358       2.212 116.679  37.014  1.00 28.84           C  
ATOM   4428  O   ALA B 358       3.277 116.212  37.420  1.00 29.11           O  
ATOM   4429  CB  ALA B 358       0.355 116.733  38.677  1.00 28.84           C  
ATOM   4430  N   ASP B 359       2.152 117.721  36.194  1.00 28.78           N  
ATOM   4431  CA  ASP B 359       3.365 118.409  35.779  1.00 28.89           C  
ATOM   4432  C   ASP B 359       3.480 119.798  36.403  1.00 28.94           C  
ATOM   4433  O   ASP B 359       2.575 120.249  37.097  1.00 28.96           O  
ATOM   4434  CB  ASP B 359       3.472 118.450  34.253  1.00 29.02           C  
ATOM   4435  CG  ASP B 359       2.732 119.611  33.643  1.00 29.32           C  
ATOM   4436  OD1 ASP B 359       1.493 119.675  33.790  1.00 29.49           O  
ATOM   4437  OD2 ASP B 359       3.316 120.506  32.995  1.00 30.32           O  
ATOM   4438  N   LEU B 360       4.607 120.458  36.154  1.00 29.15           N  
ATOM   4439  CA  LEU B 360       4.943 121.740  36.769  1.00 29.19           C  
ATOM   4440  C   LEU B 360       3.800 122.744  36.810  1.00 29.47           C  
ATOM   4441  O   LEU B 360       3.516 123.303  37.867  1.00 29.51           O  
ATOM   4442  CB  LEU B 360       6.147 122.355  36.063  1.00 29.13           C  
ATOM   4443  CG  LEU B 360       7.353 122.787  36.893  1.00 28.82           C  
ATOM   4444  CD1 LEU B 360       7.654 121.804  38.001  1.00 29.13           C  
ATOM   4445  CD2 LEU B 360       8.558 122.943  35.987  1.00 29.20           C  
ATOM   4446  N   LYS B 361       3.146 122.963  35.670  1.00 29.87           N  
ATOM   4447  CA  LYS B 361       2.066 123.947  35.578  1.00 30.32           C  
ATOM   4448  C   LYS B 361       0.835 123.529  36.366  1.00 30.47           C  
ATOM   4449  O   LYS B 361       0.264 124.339  37.096  1.00 30.41           O  
ATOM   4450  CB  LYS B 361       1.692 124.237  34.122  1.00 30.51           C  
ATOM   4451  CG  LYS B 361       1.576 125.728  33.801  1.00 31.13           C  
ATOM   4452  CD  LYS B 361       1.556 125.979  32.294  1.00 32.27           C  
ATOM   4453  CE  LYS B 361       2.814 126.716  31.823  1.00 32.82           C  
ATOM   4454  NZ  LYS B 361       2.526 128.125  31.410  1.00 33.64           N  
ATOM   4455  N   MET B 362       0.436 122.267  36.226  1.00 30.82           N  
ATOM   4456  CA  MET B 362      -0.709 121.736  36.970  1.00 31.32           C  
ATOM   4457  C   MET B 362      -0.543 121.934  38.482  1.00 30.98           C  
ATOM   4458  O   MET B 362      -1.490 122.286  39.182  1.00 30.94           O  
ATOM   4459  CB  MET B 362      -0.950 120.257  36.633  1.00 31.63           C  
ATOM   4460  CG  MET B 362      -1.503 120.008  35.218  1.00 33.70           C  
ATOM   4461  SD  MET B 362      -1.612 118.233  34.760  1.00 38.26           S  
ATOM   4462  CE  MET B 362      -1.598 118.321  32.936  1.00 37.20           C  
ATOM   4463  N   LEU B 363       0.675 121.728  38.966  1.00 30.92           N  
ATOM   4464  CA  LEU B 363       0.990 121.870  40.378  1.00 30.91           C  
ATOM   4465  C   LEU B 363       1.058 123.333  40.791  1.00 31.16           C  
ATOM   4466  O   LEU B 363       0.544 123.716  41.845  1.00 31.02           O  
ATOM   4467  CB  LEU B 363       2.327 121.196  40.687  1.00 30.76           C  
ATOM   4468  CG  LEU B 363       2.420 119.680  40.574  1.00 30.07           C  
ATOM   4469  CD1 LEU B 363       3.770 119.252  41.077  1.00 29.73           C  
ATOM   4470  CD2 LEU B 363       1.313 118.995  41.357  1.00 29.28           C  
ATOM   4471  N   THR B 364       1.701 124.145  39.953  1.00 31.47           N  
ATOM   4472  CA  THR B 364       1.922 125.556  40.257  1.00 31.60           C  
ATOM   4473  C   THR B 364       0.616 126.351  40.326  1.00 31.69           C  
ATOM   4474  O   THR B 364       0.572 127.432  40.910  1.00 31.89           O  
ATOM   4475  CB  THR B 364       2.935 126.176  39.271  1.00 31.39           C  
ATOM   4476  OG1 THR B 364       3.619 127.248  39.918  1.00 31.98           O  
ATOM   4477  CG2 THR B 364       2.244 126.866  38.108  1.00 31.52           C  
ATOM   4478  N   ASN B 365      -0.439 125.794  39.738  1.00 31.77           N  
ATOM   4479  CA  ASN B 365      -1.765 126.384  39.786  1.00 31.91           C  
ATOM   4480  C   ASN B 365      -2.729 125.505  40.563  1.00 31.92           C  
ATOM   4481  O   ASN B 365      -3.945 125.659  40.453  1.00 32.04           O  
ATOM   4482  CB  ASN B 365      -2.291 126.626  38.373  1.00 32.07           C  
ATOM   4483  CG  ASN B 365      -1.383 127.531  37.560  1.00 32.95           C  
ATOM   4484  OD1 ASN B 365      -0.746 127.086  36.602  1.00 33.97           O  
ATOM   4485  ND2 ASN B 365      -1.318 128.810  37.936  1.00 33.26           N  
ATOM   4486  N   HIS B 366      -2.180 124.575  41.341  1.00 31.95           N  
ATOM   4487  CA  HIS B 366      -2.987 123.724  42.211  1.00 31.82           C  
ATOM   4488  C   HIS B 366      -3.466 124.564  43.382  1.00 31.71           C  
ATOM   4489  O   HIS B 366      -2.757 125.463  43.837  1.00 31.60           O  
ATOM   4490  CB  HIS B 366      -2.184 122.516  42.701  1.00 31.78           C  
ATOM   4491  CG  HIS B 366      -2.998 121.505  43.445  1.00 31.76           C  
ATOM   4492  ND1 HIS B 366      -3.473 120.352  42.856  1.00 32.29           N  
ATOM   4493  CD2 HIS B 366      -3.417 121.469  44.731  1.00 31.40           C  
ATOM   4494  CE1 HIS B 366      -4.152 119.652  43.747  1.00 31.91           C  
ATOM   4495  NE2 HIS B 366      -4.133 120.308  44.893  1.00 31.54           N  
ATOM   4496  N   THR B 367      -4.670 124.265  43.858  1.00 31.71           N  
ATOM   4497  CA  THR B 367      -5.321 125.059  44.898  1.00 31.73           C  
ATOM   4498  C   THR B 367      -4.491 125.163  46.182  1.00 31.89           C  
ATOM   4499  O   THR B 367      -4.486 126.204  46.835  1.00 31.89           O  
ATOM   4500  CB  THR B 367      -6.763 124.550  45.177  1.00 31.52           C  
ATOM   4501  OG1 THR B 367      -6.910 124.233  46.563  1.00 31.37           O  
ATOM   4502  CG2 THR B 367      -7.024 123.222  44.480  1.00 31.49           C  
ATOM   4503  N   PHE B 368      -3.783 124.088  46.516  1.00 32.24           N  
ATOM   4504  CA  PHE B 368      -2.884 124.054  47.668  1.00 32.65           C  
ATOM   4505  C   PHE B 368      -1.774 125.103  47.545  1.00 33.06           C  
ATOM   4506  O   PHE B 368      -1.486 125.822  48.501  1.00 33.09           O  
ATOM   4507  CB  PHE B 368      -2.302 122.640  47.846  1.00 32.55           C  
ATOM   4508  CG  PHE B 368      -1.135 122.564  48.794  1.00 32.35           C  
ATOM   4509  CD1 PHE B 368       0.165 122.467  48.309  1.00 32.45           C  
ATOM   4510  CD2 PHE B 368      -1.333 122.574  50.170  1.00 32.29           C  
ATOM   4511  CE1 PHE B 368       1.252 122.394  49.184  1.00 32.39           C  
ATOM   4512  CE2 PHE B 368      -0.253 122.505  51.048  1.00 32.24           C  
ATOM   4513  CZ  PHE B 368       1.040 122.415  50.553  1.00 31.98           C  
ATOM   4514  N   ILE B 369      -1.168 125.188  46.362  1.00 33.55           N  
ATOM   4515  CA  ILE B 369      -0.113 126.158  46.088  1.00 34.03           C  
ATOM   4516  C   ILE B 369      -0.638 127.591  46.168  1.00 34.55           C  
ATOM   4517  O   ILE B 369       0.004 128.459  46.765  1.00 34.59           O  
ATOM   4518  CB  ILE B 369       0.529 125.871  44.710  1.00 33.86           C  
ATOM   4519  CG1 ILE B 369       1.494 124.687  44.800  1.00 34.07           C  
ATOM   4520  CG2 ILE B 369       1.254 127.087  44.166  1.00 34.09           C  
ATOM   4521  CD1 ILE B 369       2.583 124.812  45.865  1.00 34.20           C  
ATOM   4522  N   LYS B 370      -1.809 127.823  45.575  1.00 35.27           N  
ATOM   4523  CA  LYS B 370      -2.424 129.147  45.545  1.00 35.92           C  
ATOM   4524  C   LYS B 370      -2.743 129.605  46.953  1.00 36.45           C  
ATOM   4525  O   LYS B 370      -2.436 130.740  47.326  1.00 36.63           O  
ATOM   4526  CB  LYS B 370      -3.696 129.136  44.701  1.00 35.83           C  
ATOM   4527  CG  LYS B 370      -3.447 129.246  43.210  1.00 36.25           C  
ATOM   4528  CD  LYS B 370      -4.217 128.180  42.458  1.00 37.08           C  
ATOM   4529  CE  LYS B 370      -5.518 128.719  41.884  1.00 37.76           C  
ATOM   4530  NZ  LYS B 370      -6.095 127.784  40.874  1.00 38.48           N  
ATOM   4531  N   ARG B 371      -3.351 128.705  47.725  1.00 37.05           N  
ATOM   4532  CA  ARG B 371      -3.682 128.942  49.126  1.00 37.75           C  
ATOM   4533  C   ARG B 371      -2.420 129.222  49.947  1.00 38.34           C  
ATOM   4534  O   ARG B 371      -2.423 130.055  50.856  1.00 38.43           O  
ATOM   4535  CB  ARG B 371      -4.442 127.734  49.682  1.00 37.71           C  
ATOM   4536  CG  ARG B 371      -4.865 127.827  51.138  1.00 37.63           C  
ATOM   4537  CD  ARG B 371      -4.876 126.492  51.851  1.00 37.40           C  
ATOM   4538  NE  ARG B 371      -3.523 126.050  52.167  1.00 37.62           N  
ATOM   4539  CZ  ARG B 371      -3.225 124.921  52.800  1.00 38.02           C  
ATOM   4540  NH1 ARG B 371      -4.187 124.095  53.201  1.00 37.86           N  
ATOM   4541  NH2 ARG B 371      -1.955 124.620  53.037  1.00 37.66           N  
ATOM   4542  N   SER B 372      -1.338 128.530  49.607  1.00 39.07           N  
ATOM   4543  CA  SER B 372      -0.070 128.704  50.296  1.00 39.71           C  
ATOM   4544  C   SER B 372       0.591 130.010  49.890  1.00 40.27           C  
ATOM   4545  O   SER B 372       1.322 130.608  50.677  1.00 40.43           O  
ATOM   4546  CB  SER B 372       0.860 127.525  50.004  1.00 39.65           C  
ATOM   4547  OG  SER B 372       0.299 126.305  50.461  1.00 39.59           O  
ATOM   4548  N   GLU B 373       0.318 130.450  48.665  1.00 41.07           N  
ATOM   4549  CA  GLU B 373       0.971 131.624  48.091  1.00 42.00           C  
ATOM   4550  C   GLU B 373       0.595 132.924  48.799  1.00 42.48           C  
ATOM   4551  O   GLU B 373       1.392 133.864  48.860  1.00 42.44           O  
ATOM   4552  CB  GLU B 373       0.650 131.732  46.601  1.00 42.11           C  
ATOM   4553  CG  GLU B 373       1.692 131.104  45.689  1.00 42.83           C  
ATOM   4554  CD  GLU B 373       1.275 131.111  44.227  1.00 44.05           C  
ATOM   4555  OE1 GLU B 373       0.056 131.106  43.946  1.00 44.86           O  
ATOM   4556  OE2 GLU B 373       2.168 131.119  43.351  1.00 44.64           O  
ATOM   4557  N   VAL B 374      -0.621 132.970  49.332  1.00 43.21           N  
ATOM   4558  CA  VAL B 374      -1.121 134.176  49.986  1.00 43.99           C  
ATOM   4559  C   VAL B 374      -1.118 134.061  51.508  1.00 44.57           C  
ATOM   4560  O   VAL B 374      -1.452 135.017  52.213  1.00 44.69           O  
ATOM   4561  CB  VAL B 374      -2.534 134.549  49.489  1.00 43.86           C  
ATOM   4562  CG1 VAL B 374      -2.524 134.751  47.985  1.00 43.98           C  
ATOM   4563  CG2 VAL B 374      -3.544 133.489  49.891  1.00 43.89           C  
ATOM   4564  N   GLU B 375      -0.742 132.886  52.004  1.00 45.37           N  
ATOM   4565  CA  GLU B 375      -0.697 132.647  53.438  1.00 46.11           C  
ATOM   4566  C   GLU B 375       0.447 133.418  54.084  1.00 46.87           C  
ATOM   4567  O   GLU B 375       1.506 133.622  53.474  1.00 46.85           O  
ATOM   4568  CB  GLU B 375      -0.602 131.152  53.749  1.00 45.88           C  
ATOM   4569  CG  GLU B 375      -1.873 130.594  54.367  1.00 45.67           C  
ATOM   4570  CD  GLU B 375      -1.908 129.079  54.401  1.00 45.49           C  
ATOM   4571  OE1 GLU B 375      -1.191 128.488  55.237  1.00 45.79           O  
ATOM   4572  OE2 GLU B 375      -2.658 128.478  53.600  1.00 45.05           O  
ATOM   4573  N   GLU B 376       0.192 133.870  55.311  1.00 47.83           N  
ATOM   4574  CA  GLU B 376       1.151 134.629  56.112  1.00 48.68           C  
ATOM   4575  C   GLU B 376       1.771 133.706  57.159  1.00 48.99           C  
ATOM   4576  O   GLU B 376       1.097 133.268  58.102  1.00 49.12           O  
ATOM   4577  CB  GLU B 376       0.478 135.841  56.782  1.00 48.85           C  
ATOM   4578  CG  GLU B 376      -1.051 135.823  56.794  1.00 49.95           C  
ATOM   4579  CD  GLU B 376      -1.633 134.992  57.934  1.00 51.55           C  
ATOM   4580  OE1 GLU B 376      -1.932 135.579  59.004  1.00 52.16           O  
ATOM   4581  OE2 GLU B 376      -1.798 133.756  57.760  1.00 51.60           O  
ATOM   4582  N   VAL B 377       3.050 133.393  56.970  1.00 49.37           N  
ATOM   4583  CA  VAL B 377       3.769 132.482  57.858  1.00 49.76           C  
ATOM   4584  C   VAL B 377       5.154 133.034  58.193  1.00 50.06           C  
ATOM   4585  O   VAL B 377       5.959 133.318  57.292  1.00 50.20           O  
ATOM   4586  CB  VAL B 377       3.922 131.062  57.244  1.00 49.80           C  
ATOM   4587  CG1 VAL B 377       4.190 130.027  58.339  1.00 49.82           C  
ATOM   4588  CG2 VAL B 377       2.699 130.672  56.405  1.00 49.69           C  
ATOM   4589  N   ASP B 378       5.427 133.181  59.488  1.00 50.25           N  
ATOM   4590  CA  ASP B 378       6.737 133.627  59.948  1.00 50.50           C  
ATOM   4591  C   ASP B 378       7.736 132.474  59.842  1.00 50.62           C  
ATOM   4592  O   ASP B 378       8.222 131.973  60.858  1.00 50.72           O  
ATOM   4593  CB  ASP B 378       6.655 134.156  61.388  1.00 50.49           C  
ATOM   4594  CG  ASP B 378       7.697 135.234  61.685  1.00 50.89           C  
ATOM   4595  OD1 ASP B 378       8.888 135.030  61.363  1.00 50.98           O  
ATOM   4596  OD2 ASP B 378       7.418 136.319  62.244  1.00 51.31           O  
ATOM   4597  N   PHE B 379       8.033 132.053  58.611  1.00 50.72           N  
ATOM   4598  CA  PHE B 379       8.904 130.900  58.382  1.00 50.87           C  
ATOM   4599  C   PHE B 379      10.325 131.128  58.905  1.00 51.12           C  
ATOM   4600  O   PHE B 379      10.951 130.212  59.445  1.00 51.09           O  
ATOM   4601  CB  PHE B 379       8.932 130.505  56.902  1.00 50.76           C  
ATOM   4602  CG  PHE B 379      10.049 129.557  56.551  1.00 50.37           C  
ATOM   4603  CD1 PHE B 379      11.189 130.016  55.899  1.00 50.34           C  
ATOM   4604  CD2 PHE B 379       9.969 128.213  56.888  1.00 49.99           C  
ATOM   4605  CE1 PHE B 379      12.232 129.148  55.578  1.00 50.12           C  
ATOM   4606  CE2 PHE B 379      11.004 127.339  56.574  1.00 50.26           C  
ATOM   4607  CZ  PHE B 379      12.138 127.807  55.916  1.00 50.05           C  
ATOM   4608  N   ALA B 380      10.826 132.348  58.734  1.00 51.44           N  
ATOM   4609  CA  ALA B 380      12.094 132.747  59.328  1.00 51.81           C  
ATOM   4610  C   ALA B 380      12.032 132.606  60.853  1.00 52.14           C  
ATOM   4611  O   ALA B 380      13.019 132.226  61.492  1.00 52.13           O  
ATOM   4612  CB  ALA B 380      12.431 134.171  58.935  1.00 51.80           C  
ATOM   4613  N   GLY B 381      10.859 132.902  61.419  1.00 52.50           N  
ATOM   4614  CA  GLY B 381      10.621 132.809  62.851  1.00 52.89           C  
ATOM   4615  C   GLY B 381      10.549 131.381  63.352  1.00 53.14           C  
ATOM   4616  O   GLY B 381      11.218 131.027  64.323  1.00 53.22           O  
ATOM   4617  N   TRP B 382       9.737 130.562  62.688  1.00 53.41           N  
ATOM   4618  CA  TRP B 382       9.644 129.141  63.005  1.00 53.71           C  
ATOM   4619  C   TRP B 382      11.016 128.478  62.917  1.00 53.90           C  
ATOM   4620  O   TRP B 382      11.341 127.601  63.719  1.00 53.96           O  
ATOM   4621  CB  TRP B 382       8.649 128.438  62.076  1.00 53.72           C  
ATOM   4622  CG  TRP B 382       8.616 126.949  62.254  1.00 53.90           C  
ATOM   4623  CD1 TRP B 382       7.795 126.236  63.086  1.00 53.87           C  
ATOM   4624  CD2 TRP B 382       9.447 125.986  61.593  1.00 54.22           C  
ATOM   4625  NE1 TRP B 382       8.063 124.892  62.979  1.00 54.07           N  
ATOM   4626  CE2 TRP B 382       9.073 124.709  62.071  1.00 54.05           C  
ATOM   4627  CE3 TRP B 382      10.473 126.071  60.636  1.00 54.17           C  
ATOM   4628  CZ2 TRP B 382       9.684 123.533  61.628  1.00 53.86           C  
ATOM   4629  CZ3 TRP B 382      11.082 124.901  60.199  1.00 53.97           C  
ATOM   4630  CH2 TRP B 382      10.684 123.650  60.695  1.00 54.11           C  
ATOM   4631  N   LEU B 383      11.813 128.903  61.941  1.00 54.18           N  
ATOM   4632  CA  LEU B 383      13.156 128.373  61.768  1.00 54.55           C  
ATOM   4633  C   LEU B 383      14.013 128.646  62.998  1.00 54.95           C  
ATOM   4634  O   LEU B 383      14.591 127.724  63.574  1.00 55.09           O  
ATOM   4635  CB  LEU B 383      13.815 128.960  60.519  1.00 54.41           C  
ATOM   4636  CG  LEU B 383      14.218 127.983  59.414  1.00 54.12           C  
ATOM   4637  CD1 LEU B 383      14.828 128.740  58.259  1.00 54.08           C  
ATOM   4638  CD2 LEU B 383      15.190 126.936  59.923  1.00 54.12           C  
ATOM   4639  N   CYS B 384      14.069 129.911  63.407  1.00 55.39           N  
ATOM   4640  CA  CYS B 384      14.882 130.322  64.550  1.00 55.82           C  
ATOM   4641  C   CYS B 384      14.349 129.782  65.877  1.00 55.95           C  
ATOM   4642  O   CYS B 384      15.118 129.572  66.816  1.00 55.97           O  
ATOM   4643  CB  CYS B 384      15.007 131.847  64.595  1.00 55.82           C  
ATOM   4644  SG  CYS B 384      16.128 132.514  63.341  1.00 56.32           S  
ATOM   4645  N   LYS B 385      13.040 129.547  65.942  1.00 56.26           N  
ATOM   4646  CA  LYS B 385      12.408 128.951  67.121  1.00 56.59           C  
ATOM   4647  C   LYS B 385      12.896 127.517  67.371  1.00 57.61           C  
ATOM   4648  O   LYS B 385      12.871 127.034  68.512  1.00 57.77           O  
ATOM   4649  CB  LYS B 385      10.874 129.000  67.004  1.00 56.14           C  
ATOM   4650  CG  LYS B 385      10.176 127.634  66.919  1.00 53.69           C  
ATOM   4651  CD  LYS B 385       8.672 127.748  67.135  1.00 49.87           C  
ATOM   4652  CE  LYS B 385       7.972 126.420  66.854  1.00 47.51           C  
ATOM   4653  NZ  LYS B 385       6.610 126.631  66.271  1.00 45.68           N  
ATOM   4654  N   THR B 386      13.337 126.848  66.305  1.00 58.59           N  
ATOM   4655  CA  THR B 386      13.841 125.480  66.404  1.00 59.57           C  
ATOM   4656  C   THR B 386      15.368 125.413  66.313  1.00 60.24           C  
ATOM   4657  O   THR B 386      16.022 124.934  67.242  1.00 60.47           O  
ATOM   4658  CB  THR B 386      13.175 124.562  65.354  1.00 59.50           C  
ATOM   4659  OG1 THR B 386      12.651 125.353  64.281  1.00 59.62           O  
ATOM   4660  CG2 THR B 386      11.935 123.903  65.941  1.00 59.59           C  
ATOM   4661  N   LEU B 387      15.930 125.911  65.213  1.00 61.01           N  
ATOM   4662  CA  LEU B 387      17.375 125.848  64.981  1.00 61.83           C  
ATOM   4663  C   LEU B 387      18.228 126.683  65.950  1.00 62.42           C  
ATOM   4664  O   LEU B 387      19.429 126.431  66.087  1.00 62.55           O  
ATOM   4665  CB  LEU B 387      17.704 126.230  63.534  1.00 61.83           C  
ATOM   4666  CG  LEU B 387      18.452 125.194  62.687  1.00 61.95           C  
ATOM   4667  CD1 LEU B 387      18.234 125.470  61.214  1.00 61.68           C  
ATOM   4668  CD2 LEU B 387      19.948 125.163  63.007  1.00 62.13           C  
ATOM   4669  N   ARG B 388      17.608 127.666  66.609  1.00 63.14           N  
ATOM   4670  CA  ARG B 388      18.277 128.536  67.590  1.00 63.80           C  
ATOM   4671  C   ARG B 388      19.483 129.312  67.027  1.00 64.16           C  
ATOM   4672  O   ARG B 388      20.640 128.973  67.312  1.00 64.31           O  
ATOM   4673  CB  ARG B 388      18.690 127.742  68.840  1.00 63.84           C  
ATOM   4674  CG  ARG B 388      17.583 127.526  69.862  1.00 64.50           C  
ATOM   4675  CD  ARG B 388      18.009 127.765  71.315  1.00 65.42           C  
ATOM   4676  NE  ARG B 388      18.959 126.765  71.813  1.00 66.07           N  
ATOM   4677  CZ  ARG B 388      18.721 125.926  72.822  1.00 66.69           C  
ATOM   4678  NH1 ARG B 388      17.553 125.944  73.457  1.00 66.95           N  
ATOM   4679  NH2 ARG B 388      19.656 125.058  73.198  1.00 66.93           N  
ATOM   4680  N   LEU B 389      19.206 130.343  66.225  1.00 64.54           N  
ATOM   4681  CA  LEU B 389      20.238 131.283  65.762  1.00 64.83           C  
ATOM   4682  C   LEU B 389      19.665 132.677  65.498  1.00 64.95           C  
ATOM   4683  O   LEU B 389      20.379 133.679  65.576  1.00 65.07           O  
ATOM   4684  CB  LEU B 389      20.969 130.764  64.514  1.00 64.89           C  
ATOM   4685  CG  LEU B 389      22.449 131.173  64.414  1.00 65.15           C  
ATOM   4686  CD1 LEU B 389      23.348 129.974  64.098  1.00 65.33           C  
ATOM   4687  CD2 LEU B 389      22.658 132.297  63.399  1.00 65.12           C  
TER    4688      LEU B 389                                                      
HETATM 4689 MG    MG A 536      37.543  99.185  45.819  1.00 18.85          MG  
HETATM 4690 MG    MG B 538      23.616 117.406  48.291  1.00 32.28          MG  
HETATM 4691  PG  ATP A 535      35.026 100.266  45.255  1.00 48.91           P  
HETATM 4692  O1G ATP A 535      34.287  98.987  45.544  1.00 48.93           O  
HETATM 4693  O2G ATP A 535      35.726 100.846  46.458  1.00 49.34           O  
HETATM 4694  O3G ATP A 535      34.225 101.255  44.449  1.00 49.22           O  
HETATM 4695  PB  ATP A 535      36.986 100.842  43.343  1.00 48.15           P  
HETATM 4696  O1B ATP A 535      38.341 100.231  43.096  1.00 48.79           O  
HETATM 4697  O2B ATP A 535      36.100 101.221  42.183  1.00 48.44           O  
HETATM 4698  O3B ATP A 535      36.193  99.792  44.267  1.00 48.59           O  
HETATM 4699  PA  ATP A 535      38.398 102.300  45.290  1.00 47.75           P  
HETATM 4700  O1A ATP A 535      38.197 103.581  46.058  1.00 47.81           O  
HETATM 4701  O2A ATP A 535      38.547 100.998  46.036  1.00 48.02           O  
HETATM 4702  O3A ATP A 535      37.162 102.145  44.267  1.00 47.98           O  
HETATM 4703  O5' ATP A 535      39.689 102.459  44.344  1.00 47.58           O  
HETATM 4704  C5' ATP A 535      39.697 103.312  43.204  1.00 47.69           C  
HETATM 4705  C4' ATP A 535      40.953 103.058  42.377  1.00 47.83           C  
HETATM 4706  O4' ATP A 535      42.124 103.163  43.190  1.00 47.59           O  
HETATM 4707  C3' ATP A 535      40.986 101.669  41.756  1.00 47.99           C  
HETATM 4708  O3' ATP A 535      40.512 101.708  40.419  1.00 48.54           O  
HETATM 4709  C2' ATP A 535      42.439 101.244  41.811  1.00 47.83           C  
HETATM 4710  O2' ATP A 535      43.025 101.353  40.526  1.00 48.01           O  
HETATM 4711  C1' ATP A 535      43.119 102.240  42.738  1.00 47.56           C  
HETATM 4712  N9  ATP A 535      43.760 101.540  43.883  1.00 47.03           N  
HETATM 4713  C8  ATP A 535      43.142 101.056  44.979  1.00 46.77           C  
HETATM 4714  N7  ATP A 535      44.026 100.476  45.828  1.00 46.38           N  
HETATM 4715  C5  ATP A 535      45.237 100.583  45.274  1.00 46.55           C  
HETATM 4716  C6  ATP A 535      46.620 100.181  45.635  1.00 46.53           C  
HETATM 4717  N6  ATP A 535      46.872  99.531  46.795  1.00 46.58           N  
HETATM 4718  N1  ATP A 535      47.607 100.478  44.778  1.00 46.40           N  
HETATM 4719  C2  ATP A 535      47.369 101.124  43.618  1.00 46.46           C  
HETATM 4720  N3  ATP A 535      46.142 101.517  43.226  1.00 46.43           N  
HETATM 4721  C4  ATP A 535      45.064 101.284  43.990  1.00 46.66           C  
HETATM 4722  PG  ATP B 537      24.357 113.382  48.717  1.00 52.42           P  
HETATM 4723  O1G ATP B 537      23.398 112.286  48.322  1.00 52.68           O  
HETATM 4724  O2G ATP B 537      24.193 114.659  47.922  1.00 52.76           O  
HETATM 4725  O3G ATP B 537      25.770 112.898  48.865  1.00 52.50           O  
HETATM 4726  PB  ATP B 537      24.127 115.227  50.817  1.00 51.04           P  
HETATM 4727  O1B ATP B 537      23.252 116.222  50.096  1.00 51.17           O  
HETATM 4728  O2B ATP B 537      24.040 115.129  52.320  1.00 51.16           O  
HETATM 4729  O3B ATP B 537      23.862 113.762  50.198  1.00 51.70           O  
HETATM 4730  PA  ATP B 537      26.244 116.909  49.964  1.00 50.61           P  
HETATM 4731  O1A ATP B 537      27.745 116.799  49.865  1.00 50.78           O  
HETATM 4732  O2A ATP B 537      25.466 117.387  48.762  1.00 50.80           O  
HETATM 4733  O3A ATP B 537      25.669 115.473  50.413  1.00 50.94           O  
HETATM 4734  O5' ATP B 537      25.894 117.842  51.226  1.00 50.42           O  
HETATM 4735  C5' ATP B 537      26.440 117.558  52.510  1.00 50.41           C  
HETATM 4736  C4' ATP B 537      25.666 118.286  53.602  1.00 50.77           C  
HETATM 4737  O4' ATP B 537      26.193 119.601  53.782  1.00 50.93           O  
HETATM 4738  C3' ATP B 537      24.187 118.442  53.296  1.00 50.95           C  
HETATM 4739  O3' ATP B 537      23.440 117.426  53.945  1.00 51.18           O  
HETATM 4740  C2' ATP B 537      23.828 119.820  53.817  1.00 51.18           C  
HETATM 4741  O2' ATP B 537      23.165 119.733  55.068  1.00 51.41           O  
HETATM 4742  C1' ATP B 537      25.147 120.549  54.005  1.00 51.23           C  
HETATM 4743  N9  ATP B 537      25.263 121.659  53.025  1.00 51.57           N  
HETATM 4744  C8  ATP B 537      25.473 121.521  51.702  1.00 51.74           C  
HETATM 4745  N7  ATP B 537      25.533 122.726  51.083  1.00 51.74           N  
HETATM 4746  C5  ATP B 537      25.361 123.664  52.014  1.00 51.63           C  
HETATM 4747  C6  ATP B 537      25.315 125.145  52.034  1.00 51.66           C  
HETATM 4748  N6  ATP B 537      25.471 125.857  50.892  1.00 51.58           N  
HETATM 4749  N1  ATP B 537      25.112 125.750  53.215  1.00 51.66           N  
HETATM 4750  C2  ATP B 537      24.954 125.043  54.354  1.00 51.71           C  
HETATM 4751  N3  ATP B 537      24.986 123.696  54.407  1.00 51.72           N  
HETATM 4752  C4  ATP B 537      25.181 122.965  53.300  1.00 51.64           C  
HETATM 4753  I1  5EA A1001      44.732  95.182  52.218  1.00 38.21           I  
HETATM 4754  C23 5EA A1001      42.905  96.152  52.526  1.00 34.76           C  
HETATM 4755  C21 5EA A1001      41.829  95.448  53.070  1.00 34.09           C  
HETATM 4756  C16 5EA A1001      40.593  96.062  53.282  1.00 32.98           C  
HETATM 4757  C19 5EA A1001      42.779  97.497  52.182  1.00 33.94           C  
HETATM 4758  C15 5EA A1001      41.566  98.150  52.382  1.00 32.96           C  
HETATM 4759  F20 5EA A1001      41.433  99.446  52.057  1.00 32.87           F  
HETATM 4760  C10 5EA A1001      40.413  97.410  52.962  1.00 32.52           C  
HETATM 4761  N5  5EA A1001      39.243  98.084  53.142  1.00 31.15           N  
HETATM 4762  C2  5EA A1001      38.138  97.658  53.808  1.00 29.92           C  
HETATM 4763  C6  5EA A1001      38.212  96.949  55.115  1.00 29.46           C  
HETATM 4764  F1  5EA A1001      39.387  96.673  55.699  1.00 29.95           F  
HETATM 4765  C11 5EA A1001      36.953  96.529  55.777  1.00 29.05           C  
HETATM 4766  F17 5EA A1001      36.990  95.880  56.952  1.00 28.76           F  
HETATM 4767  C9  5EA A1001      35.730  96.809  55.182  1.00 29.17           C  
HETATM 4768  C4  5EA A1001      35.650  97.482  53.964  1.00 29.42           C  
HETATM 4769  C1  5EA A1001      36.774  97.915  53.260  1.00 29.71           C  
HETATM 4770  C3  5EA A1001      36.539  98.635  51.960  1.00 30.06           C  
HETATM 4771  O7  5EA A1001      35.219  98.753  51.363  1.00 30.26           O  
HETATM 4772  C13 5EA A1001      35.598  99.520  50.191  1.00 30.73           C  
HETATM 4773  N14 5EA A1001      36.907  99.776  50.166  1.00 30.23           N  
HETATM 4774  N8  5EA A1001      37.468  99.251  51.223  1.00 30.01           N  
HETATM 4775  N18 5EA A1001      34.716  99.912  49.269  1.00 31.40           N  
HETATM 4776  C22 5EA A1001      33.617  99.062  48.839  1.00 32.21           C  
HETATM 4777  C24 5EA A1001      32.340  99.264  49.660  1.00 33.27           C  
HETATM 4778  N26 5EA A1001      31.487  98.100  49.415  1.00 33.97           N  
HETATM 4779  C27 5EA A1001      30.790  98.043  48.128  1.00 34.13           C  
HETATM 4780  C29 5EA A1001      29.914  96.809  47.916  1.00 34.38           C  
HETATM 4781  O31 5EA A1001      29.824  95.814  48.945  1.00 34.70           O  
HETATM 4782  C30 5EA A1001      30.517  95.904  50.198  1.00 34.47           C  
HETATM 4783  C28 5EA A1001      31.413  97.110  50.489  1.00 34.21           C  
HETATM 4784  I1  5EA B1002      24.149 126.256  43.539  1.00 46.30           I  
HETATM 4785  C23 5EA B1002      25.033 124.395  43.189  1.00 41.49           C  
HETATM 4786  C21 5EA B1002      24.750 123.692  42.016  1.00 40.25           C  
HETATM 4787  C16 5EA B1002      25.329 122.448  41.766  1.00 38.54           C  
HETATM 4788  C19 5EA B1002      25.903 123.874  44.144  1.00 40.35           C  
HETATM 4789  C15 5EA B1002      26.505 122.638  43.931  1.00 38.73           C  
HETATM 4790  F20 5EA B1002      27.345 122.140  44.849  1.00 38.86           F  
HETATM 4791  C10 5EA B1002      26.214 121.877  42.685  1.00 37.74           C  
HETATM 4792  N5  5EA B1002      26.825 120.671  42.503  1.00 35.64           N  
HETATM 4793  C2  5EA B1002      26.732 119.857  41.417  1.00 33.93           C  
HETATM 4794  C6  5EA B1002      26.752 120.373  40.017  1.00 33.47           C  
HETATM 4795  F1  5EA B1002      26.849 121.689  39.759  1.00 33.13           F  
HETATM 4796  C11 5EA B1002      26.646 119.401  38.892  1.00 33.32           C  
HETATM 4797  F17 5EA B1002      26.651 119.826  37.612  1.00 33.67           F  
HETATM 4798  C9  5EA B1002      26.546 118.039  39.160  1.00 33.03           C  
HETATM 4799  C4  5EA B1002      26.536 117.552  40.465  1.00 33.07           C  
HETATM 4800  C1  5EA B1002      26.621 118.377  41.586  1.00 33.41           C  
HETATM 4801  C3  5EA B1002      26.612 117.713  42.935  1.00 33.60           C  
HETATM 4802  O7  5EA B1002      26.664 116.270  43.094  1.00 33.65           O  
HETATM 4803  C13 5EA B1002      26.649 116.222  44.545  1.00 33.71           C  
HETATM 4804  N14 5EA B1002      26.599 117.441  45.078  1.00 33.57           N  
HETATM 4805  N8  5EA B1002      26.584 118.330  44.119  1.00 33.79           N  
HETATM 4806  N18 5EA B1002      26.678 115.081  45.235  1.00 33.91           N  
HETATM 4807  C22 5EA B1002      26.528 113.781  44.597  1.00 33.74           C  
HETATM 4808  C24 5EA B1002      25.081 113.507  44.186  1.00 33.85           C  
HETATM 4809  N26 5EA B1002      25.057 112.213  43.513  1.00 34.19           N  
HETATM 4810  C27 5EA B1002      24.852 111.037  44.358  1.00 34.32           C  
HETATM 4811  C29 5EA B1002      24.831 109.700  43.616  1.00 34.33           C  
HETATM 4812  O31 5EA B1002      24.997 109.671  42.193  1.00 34.60           O  
HETATM 4813  C30 5EA B1002      25.189 110.845  41.393  1.00 34.42           C  
HETATM 4814  C28 5EA B1002      25.224 112.222  42.060  1.00 34.40           C  
CONECT 1101 4689                                                                
CONECT 1201 4689                                                                
CONECT 3493 4690                                                                
CONECT 3594 4690                                                                
CONECT 4689 1101 1201 4693 4696                                                 
CONECT 4689 4698 4701                                                           
CONECT 4690 3493 3594 4724 4727                                                 
CONECT 4690 4732                                                                
CONECT 4691 4692 4693 4694 4698                                                 
CONECT 4692 4691                                                                
CONECT 4693 4689 4691                                                           
CONECT 4694 4691                                                                
CONECT 4695 4696 4697 4698 4702                                                 
CONECT 4696 4689 4695                                                           
CONECT 4697 4695                                                                
CONECT 4698 4689 4691 4695                                                      
CONECT 4699 4700 4701 4702 4703                                                 
CONECT 4700 4699                                                                
CONECT 4701 4689 4699                                                           
CONECT 4702 4695 4699                                                           
CONECT 4703 4699 4704                                                           
CONECT 4704 4703 4705                                                           
CONECT 4705 4704 4706 4707                                                      
CONECT 4706 4705 4711                                                           
CONECT 4707 4705 4708 4709                                                      
CONECT 4708 4707                                                                
CONECT 4709 4707 4710 4711                                                      
CONECT 4710 4709                                                                
CONECT 4711 4706 4709 4712                                                      
CONECT 4712 4711 4713 4721                                                      
CONECT 4713 4712 4714                                                           
CONECT 4714 4713 4715                                                           
CONECT 4715 4714 4716 4721                                                      
CONECT 4716 4715 4717 4718                                                      
CONECT 4717 4716                                                                
CONECT 4718 4716 4719                                                           
CONECT 4719 4718 4720                                                           
CONECT 4720 4719 4721                                                           
CONECT 4721 4712 4715 4720                                                      
CONECT 4722 4723 4724 4725 4729                                                 
CONECT 4723 4722                                                                
CONECT 4724 4690 4722                                                           
CONECT 4725 4722                                                                
CONECT 4726 4727 4728 4729 4733                                                 
CONECT 4727 4690 4726                                                           
CONECT 4728 4726                                                                
CONECT 4729 4722 4726                                                           
CONECT 4730 4731 4732 4733 4734                                                 
CONECT 4731 4730                                                                
CONECT 4732 4690 4730                                                           
CONECT 4733 4726 4730                                                           
CONECT 4734 4730 4735                                                           
CONECT 4735 4734 4736                                                           
CONECT 4736 4735 4737 4738                                                      
CONECT 4737 4736 4742                                                           
CONECT 4738 4736 4739 4740                                                      
CONECT 4739 4738                                                                
CONECT 4740 4738 4741 4742                                                      
CONECT 4741 4740                                                                
CONECT 4742 4737 4740 4743                                                      
CONECT 4743 4742 4744 4752                                                      
CONECT 4744 4743 4745                                                           
CONECT 4745 4744 4746                                                           
CONECT 4746 4745 4747 4752                                                      
CONECT 4747 4746 4748 4749                                                      
CONECT 4748 4747                                                                
CONECT 4749 4747 4750                                                           
CONECT 4750 4749 4751                                                           
CONECT 4751 4750 4752                                                           
CONECT 4752 4743 4746 4751                                                      
CONECT 4753 4754                                                                
CONECT 4754 4753 4755 4757                                                      
CONECT 4755 4754 4756                                                           
CONECT 4756 4755 4760                                                           
CONECT 4757 4754 4758                                                           
CONECT 4758 4757 4759 4760                                                      
CONECT 4759 4758                                                                
CONECT 4760 4756 4758 4761                                                      
CONECT 4761 4760 4762                                                           
CONECT 4762 4761 4763 4769                                                      
CONECT 4763 4762 4764 4765                                                      
CONECT 4764 4763                                                                
CONECT 4765 4763 4766 4767                                                      
CONECT 4766 4765                                                                
CONECT 4767 4765 4768                                                           
CONECT 4768 4767 4769                                                           
CONECT 4769 4762 4768 4770                                                      
CONECT 4770 4769 4771 4774                                                      
CONECT 4771 4770 4772                                                           
CONECT 4772 4771 4773 4775                                                      
CONECT 4773 4772 4774                                                           
CONECT 4774 4770 4773                                                           
CONECT 4775 4772 4776                                                           
CONECT 4776 4775 4777                                                           
CONECT 4777 4776 4778                                                           
CONECT 4778 4777 4779 4783                                                      
CONECT 4779 4778 4780                                                           
CONECT 4780 4779 4781                                                           
CONECT 4781 4780 4782                                                           
CONECT 4782 4781 4783                                                           
CONECT 4783 4778 4782                                                           
CONECT 4784 4785                                                                
CONECT 4785 4784 4786 4788                                                      
CONECT 4786 4785 4787                                                           
CONECT 4787 4786 4791                                                           
CONECT 4788 4785 4789                                                           
CONECT 4789 4788 4790 4791                                                      
CONECT 4790 4789                                                                
CONECT 4791 4787 4789 4792                                                      
CONECT 4792 4791 4793                                                           
CONECT 4793 4792 4794 4800                                                      
CONECT 4794 4793 4795 4796                                                      
CONECT 4795 4794                                                                
CONECT 4796 4794 4797 4798                                                      
CONECT 4797 4796                                                                
CONECT 4798 4796 4799                                                           
CONECT 4799 4798 4800                                                           
CONECT 4800 4793 4799 4801                                                      
CONECT 4801 4800 4802 4805                                                      
CONECT 4802 4801 4803                                                           
CONECT 4803 4802 4804 4806                                                      
CONECT 4804 4803 4805                                                           
CONECT 4805 4801 4804                                                           
CONECT 4806 4803 4807                                                           
CONECT 4807 4806 4808                                                           
CONECT 4808 4807 4809                                                           
CONECT 4809 4808 4810 4814                                                      
CONECT 4810 4809 4811                                                           
CONECT 4811 4810 4812                                                           
CONECT 4812 4811 4813                                                           
CONECT 4813 4812 4814                                                           
CONECT 4814 4809 4813                                                           
MASTER      485    0    6   29   16    0   19    6 4812    2  132   56          
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.