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***  RECEPTOR 24-MAR-11 2YDV  ***

elNémo ID: 21120308463877833

Job options:

ID        	=	 21120308463877833
JOBID     	=	 RECEPTOR 24-MAR-11 2YDV
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    RECEPTOR                                24-MAR-11   2YDV              
TITLE     THERMOSTABILISED HUMAN A2A RECEPTOR WITH NECA BOUND                   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: ADENOSINE RECEPTOR A2A;                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: RESIDUES 1-317;                                            
COMPND   5 SYNONYM: THERMOSTABILISED HUMAN A2A RECEPTOR;                        
COMPND   6 ENGINEERED: YES;                                                     
COMPND   7 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 TISSUE: BRAIN;                                                       
SOURCE   6 EXPRESSION_SYSTEM: TRICHOPLUSIA NI;                                  
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CABBAGE LOOPER;                            
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 7111;                                       
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: HIGH FIVE;                              
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: BACULOVIRUS;                          
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PBACPAK8                                  
KEYWDS    RECEPTOR, G PROTEIN COUPLED RECEPTOR, SEVEN-HELIX RECEPTOR, AGONIST   
KEYWDS   2 BOUND FORM, THERMOSTABILISING POINT MUTATIONS, GPCR, 7TM RECEPTOR    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    G.LEBON,T.WARNE,P.C.EDWARDS,K.BENNETT,C.J.LANGMEAD,A.G.W.LESLIE,      
AUTHOR   2 C.G.TATE                                                             
REVDAT   5   29-JUL-20 2YDV    1       COMPND REMARK HETNAM SITE                
REVDAT   4   03-APR-19 2YDV    1       SOURCE                                   
REVDAT   3   22-JUN-11 2YDV    1       JRNL                                     
REVDAT   2   01-JUN-11 2YDV    1       REMARK                                   
REVDAT   1   18-MAY-11 2YDV    0                                                
JRNL        AUTH   G.LEBON,T.WARNE,P.C.EDWARDS,K.BENNETT,C.J.LANGMEAD,          
JRNL        AUTH 2 A.G.W.LESLIE,C.G.TATE                                        
JRNL        TITL   AGONIST-BOUND ADENOSINE A(2A) RECEPTOR STRUCTURES REVEAL     
JRNL        TITL 2 COMMON FEATURES OF GPCR ACTIVATION.                          
JRNL        REF    NATURE                        V. 474   521 2011              
JRNL        REFN                   ISSN 0028-0836                               
JRNL        PMID   21593763                                                     
JRNL        DOI    10.1038/NATURE10136                                          
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   G.LEBON,K.BENNETT,A.JAZAYERI,C.G.TATE                        
REMARK   1  TITL   THERMOSTABILISATION OF AN AGONIST-BOUND CONFORMATION OF THE  
REMARK   1  TITL 2 HUMAN ADENOSINE A(2A) RECEPTOR.                              
REMARK   1  REF    J.MOL.BIOL.                   V. 409   298 2011              
REMARK   1  REFN                   ISSN 0022-2836                               
REMARK   1  PMID   21501622                                                     
REMARK   1  DOI    10.1016/J.JMB.2011.03.075                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.6.0100                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 2.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 79.52                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.5                           
REMARK   3   NUMBER OF REFLECTIONS             : 17471                          
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) : 0.234                           
REMARK   3   R VALUE            (WORKING SET) : 0.233                           
REMARK   3   FREE R VALUE                     : 0.258                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 947                             
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) : 2.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.67                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1241                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 98.94                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3170                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 68                           
REMARK   3   BIN FREE R VALUE                    : 0.3370                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2454                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 122                                     
REMARK   3   SOLVENT ATOMS            : 27                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 70.50                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 75.15                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -1.16000                                             
REMARK   3    B22 (A**2) : 0.27000                                              
REMARK   3    B33 (A**2) : 0.69000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -1.76000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.374         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.264         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.215         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 9.904         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.938                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2637 ; 0.007 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3586 ; 1.005 ; 1.991       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   313 ; 4.161 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    97 ;38.306 ;22.680       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   403 ;14.763 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;14.996 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   434 ; 0.068 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1869 ; 0.004 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
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 : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS. HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT. U      
REMARK   3  VALUES REFINED INDIVIDUALLY.                                        
REMARK   4                                                                      
REMARK   4 2YDV COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBE ON 24-MAR-11.                  
REMARK 100 THE DEPOSITION ID IS D_1290047810.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 14-NOV-10                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.4                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ESRF                               
REMARK 200  BEAMLINE                       : ID23-2                             
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.8726                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : MARMOSAIC 225 MM CCD               
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : MOSFLM                             
REMARK 200  DATA SCALING SOFTWARE          : SCALA                              
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 17471                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 49.410                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 0.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.400                              
REMARK 200  R MERGE                    (I) : 0.08000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 8.5000                             
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.74                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 99.2                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.57000                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 1.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 3EML                                       
REMARK 200                                                                      
REMARK 200 REMARK: NONE                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 69.30                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.01                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.05 M ADA NAOH, PH 6.4, 23.6% V/V PEG   
REMARK 280  400, 4% V/V 2-PROPANOL.                                             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       38.46800            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       49.77550            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       38.46800            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       49.77550            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 400                                                                      
REMARK 400 COMPOUND                                                             
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, LEU  48 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ALA  54 TO LEU                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, THR  65 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, GLN  89 TO ALA                        
REMARK 400 ENGINEERED RESIDUE IN CHAIN A, ASN 154 TO ALA                        
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET A     1                                                      
REMARK 465     PRO A     2                                                      
REMARK 465     PRO A   215                                                      
REMARK 465     LEU A   216                                                      
REMARK 465     PRO A   217                                                      
REMARK 465     GLY A   218                                                      
REMARK 465     GLU A   219                                                      
REMARK 465     ARG A   220                                                      
REMARK 465     ALA A   221                                                      
REMARK 465     ARG A   222                                                      
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    PHE A 180      -61.69   -107.72                                   
REMARK 500    PRO A 285       45.26   -105.59                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1UPE   RELATED DB: PDB                                   
REMARK 900 MODELING THE ADENOSINE RECEPTORS: COMPARISON OF THE BINDING DOMAINS  
REMARK 900 OF A2A AGONISTS AND ANTAGONISTS                                      
REMARK 900 RELATED ID: 1MMH   RELATED DB: PDB                                   
REMARK 900 MOLECULAR MODEL OF THE HUMAN A2A ADENOSINE RECEPTOR                  
REMARK 900 RELATED ID: 2YDO   RELATED DB: PDB                                   
REMARK 900 THERMOSTABILISED HUMAN A2A RECEPTOR WITH ADENOSINE BOUND             
REMARK 999                                                                      
REMARK 999 SEQUENCE                                                             
REMARK 999 THE CONSTRUCT WAS TRUNCATED AFTER RESIDUE 316 OF THE A2A             
REMARK 999 SEQUENCE. CONSTRUCT CRYSTALLISED CONTAINS                            
REMARK 999 THERMOSTABILISING MUTATIONS L48A, A54L, T65A, Q89A.                  
REMARK 999 REMOVAL OF GLYCOSYLATION SITE BY MUTATION N154A. AT C-               
REMARK 999 TERMINUS,THERE IS A LINKER PLUS TEV CLEAVAGE SEQUENCE                
REMARK 999 AAAENLYFQ.                                                           
DBREF  2YDV A    1   317  UNP    P29274   AA2AR_HUMAN      1    317             
SEQADV 2YDV ALA A   48  UNP  P29274    LEU    48 ENGINEERED MUTATION            
SEQADV 2YDV LEU A   54  UNP  P29274    ALA    54 ENGINEERED MUTATION            
SEQADV 2YDV ALA A   65  UNP  P29274    THR    65 ENGINEERED MUTATION            
SEQADV 2YDV ALA A   89  UNP  P29274    GLN    89 ENGINEERED MUTATION            
SEQADV 2YDV ALA A  154  UNP  P29274    ASN   154 ENGINEERED MUTATION            
SEQADV 2YDV ALA A  318  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV ALA A  319  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV GLU A  320  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV ASN A  321  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV LEU A  322  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV TYR A  323  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV PHE A  324  UNP  P29274              EXPRESSION TAG                 
SEQADV 2YDV GLN A  325  UNP  P29274              EXPRESSION TAG                 
SEQRES   1 A  325  MET PRO ILE MET GLY SER SER VAL TYR ILE THR VAL GLU          
SEQRES   2 A  325  LEU ALA ILE ALA VAL LEU ALA ILE LEU GLY ASN VAL LEU          
SEQRES   3 A  325  VAL CYS TRP ALA VAL TRP LEU ASN SER ASN LEU GLN ASN          
SEQRES   4 A  325  VAL THR ASN TYR PHE VAL VAL SER ALA ALA ALA ALA ASP          
SEQRES   5 A  325  ILE LEU VAL GLY VAL LEU ALA ILE PRO PHE ALA ILE ALA          
SEQRES   6 A  325  ILE SER THR GLY PHE CYS ALA ALA CYS HIS GLY CYS LEU          
SEQRES   7 A  325  PHE ILE ALA CYS PHE VAL LEU VAL LEU THR ALA SER SER          
SEQRES   8 A  325  ILE PHE SER LEU LEU ALA ILE ALA ILE ASP ARG TYR ILE          
SEQRES   9 A  325  ALA ILE ARG ILE PRO LEU ARG TYR ASN GLY LEU VAL THR          
SEQRES  10 A  325  GLY THR ARG ALA LYS GLY ILE ILE ALA ILE CYS TRP VAL          
SEQRES  11 A  325  LEU SER PHE ALA ILE GLY LEU THR PRO MET LEU GLY TRP          
SEQRES  12 A  325  ASN ASN CYS GLY GLN PRO LYS GLU GLY LYS ALA HIS SER          
SEQRES  13 A  325  GLN GLY CYS GLY GLU GLY GLN VAL ALA CYS LEU PHE GLU          
SEQRES  14 A  325  ASP VAL VAL PRO MET ASN TYR MET VAL TYR PHE ASN PHE          
SEQRES  15 A  325  PHE ALA CYS VAL LEU VAL PRO LEU LEU LEU MET LEU GLY          
SEQRES  16 A  325  VAL TYR LEU ARG ILE PHE LEU ALA ALA ARG ARG GLN LEU          
SEQRES  17 A  325  LYS GLN MET GLU SER GLN PRO LEU PRO GLY GLU ARG ALA          
SEQRES  18 A  325  ARG SER THR LEU GLN LYS GLU VAL HIS ALA ALA LYS SER          
SEQRES  19 A  325  LEU ALA ILE ILE VAL GLY LEU PHE ALA LEU CYS TRP LEU          
SEQRES  20 A  325  PRO LEU HIS ILE ILE ASN CYS PHE THR PHE PHE CYS PRO          
SEQRES  21 A  325  ASP CYS SER HIS ALA PRO LEU TRP LEU MET TYR LEU ALA          
SEQRES  22 A  325  ILE VAL LEU SER HIS THR ASN SER VAL VAL ASN PRO PHE          
SEQRES  23 A  325  ILE TYR ALA TYR ARG ILE ARG GLU PHE ARG GLN THR PHE          
SEQRES  24 A  325  ARG LYS ILE ILE ARG SER HIS VAL LEU ARG GLN GLN GLU          
SEQRES  25 A  325  PRO PHE LYS ALA ALA ALA ALA GLU ASN LEU TYR PHE GLN          
HET    NEC  A 400      22                                                       
HET    SOG  A 501      20                                                       
HET    SOG  A 502      20                                                       
HET    SOG  A 503      20                                                       
HET    SOG  A 504      20                                                       
HET    SOG  A 505      20                                                       
HETNAM     NEC N-ETHYL-5'-CARBOXAMIDO ADENOSINE                                 
HETNAM     SOG OCTYL 1-THIO-BETA-D-GLUCOPYRANOSIDE                              
HETSYN     SOG 1-S-OCTYL-BETA-D-THIOGLUCOSIDE                                   
FORMUL   2  NEC    C12 H16 N6 O4                                                
FORMUL   3  SOG    5(C14 H28 O5 S)                                              
FORMUL   8  HOH   *27(H2 O)                                                     
HELIX    1   1 SER A    6  ASN A   34  1                                  29    
HELIX    2   2 VAL A   40  LEU A   58  1                                  19    
HELIX    3   3 LEU A   58  SER A   67  1                                  10    
HELIX    4   4 ALA A   73  ILE A  108  1                                  36    
HELIX    5   5 ARG A  111  VAL A  116  1                                   6    
HELIX    6   6 THR A  117  LEU A  137  1                                  21    
HELIX    7   7 THR A  138  GLY A  142  5                                   5    
HELIX    8   8 LYS A  150  GLN A  157  1                                   8    
HELIX    9   9 LEU A  167  VAL A  172  1                                   6    
HELIX   10  10 PRO A  173  PHE A  180  1                                   8    
HELIX   11  11 PHE A  180  VAL A  186  1                                   7    
HELIX   12  12 VAL A  186  MET A  211  1                                  26    
HELIX   13  13 SER A  223  CYS A  259  1                                  37    
HELIX   14  14 PRO A  266  THR A  279  1                                  14    
HELIX   15  15 THR A  279  ASN A  284  1                                   6    
HELIX   16  16 PRO A  285  ARG A  291  1                                   7    
HELIX   17  17 ILE A  292  LEU A  308  1                                  17    
HELIX   18  18 GLN A  311  PHE A  324  1                                  14    
SHEET    1  AA 2 CYS A  71  ALA A  72  0                                        
SHEET    2  AA 2 VAL A 164  ALA A 165 -1  O  VAL A 164   N  ALA A  72           
SSBOND   1 CYS A   71    CYS A  159                          1555   1555  2.04  
SSBOND   2 CYS A   74    CYS A  146                          1555   1555  2.06  
SSBOND   3 CYS A   77    CYS A  166                          1555   1555  2.04  
SSBOND   4 CYS A  259    CYS A  262                          1555   1555  2.04  
CISPEP   1 ASN A  284    PRO A  285          0        -3.44                     
CRYST1   76.936   99.551   79.655  90.00  93.31  90.00 C 1 2 1       4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.012998  0.000000  0.000752        0.00000                         
SCALE2      0.000000  0.010045  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.012575        0.00000                         
ATOM      1  N   ILE A   3      35.343  -2.057 -30.022  1.00119.08           N  
ATOM      2  CA  ILE A   3      36.094  -0.818 -29.646  1.00119.48           C  
ATOM      3  C   ILE A   3      35.911   0.303 -30.683  1.00122.17           C  
ATOM      4  O   ILE A   3      36.033   1.484 -30.348  1.00122.02           O  
ATOM      5  CB  ILE A   3      37.602  -1.118 -29.355  1.00115.05           C  
ATOM      6  CG1 ILE A   3      37.765  -1.870 -28.032  1.00112.85           C  
ATOM      7  CG2 ILE A   3      38.420   0.146 -29.259  1.00112.06           C  
ATOM      8  CD1 ILE A   3      37.807  -3.368 -28.171  1.00115.61           C  
ATOM      9  N   MET A   4      35.590  -0.074 -31.922  1.00124.85           N  
ATOM     10  CA  MET A   4      35.353   0.879 -33.020  1.00126.03           C  
ATOM     11  C   MET A   4      34.579   2.132 -32.580  1.00125.44           C  
ATOM     12  O   MET A   4      35.002   3.257 -32.858  1.00124.33           O  
ATOM     13  CB  MET A   4      34.631   0.186 -34.187  1.00128.04           C  
ATOM     14  CG  MET A   4      34.387   1.081 -35.404  1.00130.93           C  
ATOM     15  SD  MET A   4      33.005   0.535 -36.431  1.00135.21           S  
ATOM     16  CE  MET A   4      32.708   2.005 -37.414  1.00128.05           C  
ATOM     17  N   GLY A   5      33.456   1.925 -31.893  1.00122.53           N  
ATOM     18  CA  GLY A   5      32.622   3.022 -31.402  1.00115.81           C  
ATOM     19  C   GLY A   5      31.273   3.107 -32.093  1.00110.85           C  
ATOM     20  O   GLY A   5      31.035   2.428 -33.093  1.00113.41           O  
ATOM     21  N   SER A   6      30.390   3.945 -31.552  1.00102.04           N  
ATOM     22  CA  SER A   6      29.057   4.148 -32.116  1.00 97.37           C  
ATOM     23  C   SER A   6      28.863   5.600 -32.546  1.00 93.85           C  
ATOM     24  O   SER A   6      28.961   6.512 -31.726  1.00 89.96           O  
ATOM     25  CB  SER A   6      27.977   3.736 -31.109  1.00 96.88           C  
ATOM     26  OG  SER A   6      26.683   4.114 -31.549  1.00 96.19           O  
ATOM     27  N   SER A   7      28.580   5.795 -33.834  1.00 93.76           N  
ATOM     28  CA  SER A   7      28.404   7.126 -34.428  1.00 90.97           C  
ATOM     29  C   SER A   7      27.181   7.847 -33.873  1.00 88.12           C  
ATOM     30  O   SER A   7      27.174   9.077 -33.759  1.00 84.95           O  
ATOM     31  CB  SER A   7      28.286   7.021 -35.952  1.00 92.13           C  
ATOM     32  OG  SER A   7      29.303   6.195 -36.489  1.00 95.35           O  
ATOM     33  N   VAL A   8      26.149   7.072 -33.540  1.00 85.23           N  
ATOM     34  CA  VAL A   8      24.928   7.605 -32.939  1.00 84.97           C  
ATOM     35  C   VAL A   8      25.252   8.241 -31.586  1.00 84.56           C  
ATOM     36  O   VAL A   8      24.803   9.354 -31.291  1.00 82.53           O  
ATOM     37  CB  VAL A   8      23.840   6.511 -32.762  1.00 85.74           C  
ATOM     38  CG1 VAL A   8      22.493   7.144 -32.422  1.00 85.83           C  
ATOM     39  CG2 VAL A   8      23.720   5.648 -34.015  1.00 85.39           C  
ATOM     40  N   TYR A   9      26.042   7.528 -30.779  1.00 81.31           N  
ATOM     41  CA  TYR A   9      26.496   8.035 -29.487  1.00 79.66           C  
ATOM     42  C   TYR A   9      27.306   9.322 -29.645  1.00 80.39           C  
ATOM     43  O   TYR A   9      27.021  10.318 -28.978  1.00 81.77           O  
ATOM     44  CB  TYR A   9      27.300   6.971 -28.718  1.00 78.57           C  
ATOM     45  CG  TYR A   9      28.171   7.550 -27.623  1.00 75.30           C  
ATOM     46  CD1 TYR A   9      27.611   8.013 -26.427  1.00 74.82           C  
ATOM     47  CD2 TYR A   9      29.552   7.652 -27.788  1.00 72.79           C  
ATOM     48  CE1 TYR A   9      28.408   8.559 -25.424  1.00 72.57           C  
ATOM     49  CE2 TYR A   9      30.359   8.196 -26.790  1.00 72.70           C  
ATOM     50  CZ  TYR A   9      29.781   8.648 -25.612  1.00 71.58           C  
ATOM     51  OH  TYR A   9      30.574   9.186 -24.626  1.00 67.51           O  
ATOM     52  N   ILE A  10      28.299   9.291 -30.534  1.00 79.24           N  
ATOM     53  CA  ILE A  10      29.171  10.441 -30.790  1.00 78.81           C  
ATOM     54  C   ILE A  10      28.366  11.697 -31.105  1.00 80.97           C  
ATOM     55  O   ILE A  10      28.637  12.764 -30.551  1.00 83.50           O  
ATOM     56  CB  ILE A  10      30.156  10.183 -31.973  1.00 78.34           C  
ATOM     57  CG1 ILE A  10      30.804   8.788 -31.893  1.00 77.71           C  
ATOM     58  CG2 ILE A  10      31.199  11.300 -32.079  1.00 75.39           C  
ATOM     59  CD1 ILE A  10      31.767   8.564 -30.741  1.00 76.80           C  
ATOM     60  N   THR A  11      27.375  11.561 -31.987  1.00 82.35           N  
ATOM     61  CA  THR A  11      26.623  12.719 -32.486  1.00 81.56           C  
ATOM     62  C   THR A  11      25.632  13.284 -31.453  1.00 77.40           C  
ATOM     63  O   THR A  11      25.514  14.508 -31.307  1.00 72.00           O  
ATOM     64  CB  THR A  11      25.970  12.449 -33.886  1.00 81.90           C  
ATOM     65  OG1 THR A  11      25.413  13.663 -34.403  1.00 83.58           O  
ATOM     66  CG2 THR A  11      24.883  11.382 -33.820  1.00 83.44           C  
ATOM     67  N   VAL A  12      24.947  12.394 -30.731  1.00 76.84           N  
ATOM     68  CA  VAL A  12      24.091  12.792 -29.605  1.00 76.86           C  
ATOM     69  C   VAL A  12      24.933  13.510 -28.548  1.00 74.58           C  
ATOM     70  O   VAL A  12      24.524  14.540 -28.011  1.00 73.17           O  
ATOM     71  CB  VAL A  12      23.350  11.577 -28.973  1.00 78.48           C  
ATOM     72  CG1 VAL A  12      22.704  11.956 -27.640  1.00 74.98           C  
ATOM     73  CG2 VAL A  12      22.298  11.025 -29.931  1.00 78.38           C  
ATOM     74  N   GLU A  13      26.118  12.965 -28.280  1.00 73.93           N  
ATOM     75  CA  GLU A  13      27.067  13.553 -27.340  1.00 77.22           C  
ATOM     76  C   GLU A  13      27.511  14.942 -27.804  1.00 74.99           C  
ATOM     77  O   GLU A  13      27.635  15.863 -26.995  1.00 77.57           O  
ATOM     78  CB  GLU A  13      28.272  12.619 -27.153  1.00 82.01           C  
ATOM     79  CG  GLU A  13      29.205  12.966 -25.993  1.00 85.82           C  
ATOM     80  CD  GLU A  13      28.784  12.369 -24.651  1.00 87.92           C  
ATOM     81  OE1 GLU A  13      27.666  12.657 -24.173  1.00 88.12           O  
ATOM     82  OE2 GLU A  13      29.592  11.625 -24.057  1.00 89.35           O1-
ATOM     83  N   LEU A  14      27.729  15.088 -29.110  1.00 76.98           N  
ATOM     84  CA  LEU A  14      28.067  16.383 -29.708  1.00 75.83           C  
ATOM     85  C   LEU A  14      26.929  17.396 -29.583  1.00 73.54           C  
ATOM     86  O   LEU A  14      27.170  18.577 -29.316  1.00 74.95           O  
ATOM     87  CB  LEU A  14      28.470  16.214 -31.175  1.00 75.33           C  
ATOM     88  CG  LEU A  14      29.891  15.718 -31.454  1.00 74.91           C  
ATOM     89  CD1 LEU A  14      29.950  15.009 -32.802  1.00 75.00           C  
ATOM     90  CD2 LEU A  14      30.912  16.857 -31.380  1.00 69.90           C  
ATOM     91  N   ALA A  15      25.695  16.929 -29.769  1.00 71.33           N  
ATOM     92  CA  ALA A  15      24.511  17.781 -29.621  1.00 72.08           C  
ATOM     93  C   ALA A  15      24.452  18.416 -28.231  1.00 71.22           C  
ATOM     94  O   ALA A  15      24.298  19.637 -28.102  1.00 70.99           O  
ATOM     95  CB  ALA A  15      23.243  16.989 -29.905  1.00 71.96           C  
ATOM     96  N   ILE A  16      24.602  17.577 -27.204  1.00 68.76           N  
ATOM     97  CA  ILE A  16      24.570  18.007 -25.807  1.00 64.90           C  
ATOM     98  C   ILE A  16      25.613  19.081 -25.526  1.00 65.58           C  
ATOM     99  O   ILE A  16      25.315  20.077 -24.859  1.00 62.20           O  
ATOM    100  CB  ILE A  16      24.782  16.816 -24.852  1.00 66.36           C  
ATOM    101  CG1 ILE A  16      23.635  15.817 -24.997  1.00 65.79           C  
ATOM    102  CG2 ILE A  16      24.917  17.293 -23.388  1.00 64.85           C  
ATOM    103  CD1 ILE A  16      23.965  14.449 -24.485  1.00 67.45           C  
ATOM    104  N   ALA A  17      26.825  18.874 -26.044  1.00 67.03           N  
ATOM    105  CA  ALA A  17      27.911  19.848 -25.911  1.00 69.30           C  
ATOM    106  C   ALA A  17      27.499  21.224 -26.425  1.00 71.78           C  
ATOM    107  O   ALA A  17      27.745  22.235 -25.764  1.00 74.31           O  
ATOM    108  CB  ALA A  17      29.164  19.359 -26.628  1.00 70.08           C  
ATOM    109  N   VAL A  18      26.854  21.252 -27.592  1.00 73.44           N  
ATOM    110  CA  VAL A  18      26.378  22.504 -28.179  1.00 72.76           C  
ATOM    111  C   VAL A  18      25.328  23.156 -27.276  1.00 69.59           C  
ATOM    112  O   VAL A  18      25.491  24.314 -26.877  1.00 67.98           O  
ATOM    113  CB  VAL A  18      25.849  22.315 -29.626  1.00 74.50           C  
ATOM    114  CG1 VAL A  18      25.273  23.617 -30.159  1.00 74.07           C  
ATOM    115  CG2 VAL A  18      26.966  21.827 -30.545  1.00 73.60           C  
ATOM    116  N   LEU A  19      24.279  22.407 -26.931  1.00 67.09           N  
ATOM    117  CA  LEU A  19      23.245  22.906 -26.006  1.00 68.40           C  
ATOM    118  C   LEU A  19      23.795  23.366 -24.649  1.00 69.17           C  
ATOM    119  O   LEU A  19      23.298  24.333 -24.075  1.00 70.89           O  
ATOM    120  CB  LEU A  19      22.136  21.871 -25.806  1.00 67.93           C  
ATOM    121  CG  LEU A  19      21.213  21.604 -27.001  1.00 70.03           C  
ATOM    122  CD1 LEU A  19      20.265  20.463 -26.687  1.00 68.31           C  
ATOM    123  CD2 LEU A  19      20.433  22.861 -27.417  1.00 68.69           C  
ATOM    124  N   ALA A  20      24.822  22.678 -24.148  1.00 69.03           N  
ATOM    125  CA  ALA A  20      25.492  23.077 -22.910  1.00 69.05           C  
ATOM    126  C   ALA A  20      26.220  24.416 -23.054  1.00 68.61           C  
ATOM    127  O   ALA A  20      26.115  25.282 -22.180  1.00 67.24           O  
ATOM    128  CB  ALA A  20      26.450  21.989 -22.439  1.00 69.42           C  
ATOM    129  N   ILE A  21      26.947  24.585 -24.159  1.00 67.98           N  
ATOM    130  CA  ILE A  21      27.626  25.853 -24.448  1.00 67.61           C  
ATOM    131  C   ILE A  21      26.625  26.995 -24.699  1.00 66.91           C  
ATOM    132  O   ILE A  21      26.778  28.082 -24.139  1.00 68.31           O  
ATOM    133  CB  ILE A  21      28.645  25.723 -25.615  1.00 68.62           C  
ATOM    134  CG1 ILE A  21      29.734  24.700 -25.257  1.00 65.84           C  
ATOM    135  CG2 ILE A  21      29.282  27.081 -25.935  1.00 66.26           C  
ATOM    136  CD1 ILE A  21      30.373  24.010 -26.456  1.00 64.47           C  
ATOM    137  N   LEU A  22      25.594  26.734 -25.505  1.00 66.77           N  
ATOM    138  CA  LEU A  22      24.589  27.757 -25.850  1.00 67.17           C  
ATOM    139  C   LEU A  22      23.862  28.312 -24.631  1.00 67.47           C  
ATOM    140  O   LEU A  22      23.868  29.527 -24.399  1.00 68.77           O  
ATOM    141  CB  LEU A  22      23.562  27.218 -26.857  1.00 68.20           C  
ATOM    142  CG  LEU A  22      23.989  26.908 -28.299  1.00 70.09           C  
ATOM    143  CD1 LEU A  22      22.829  26.284 -29.065  1.00 67.58           C  
ATOM    144  CD2 LEU A  22      24.521  28.144 -29.024  1.00 69.24           C  
ATOM    145  N   GLY A  23      23.245  27.418 -23.857  1.00 65.17           N  
ATOM    146  CA  GLY A  23      22.485  27.799 -22.670  1.00 63.64           C  
ATOM    147  C   GLY A  23      23.287  28.509 -21.592  1.00 64.96           C  
ATOM    148  O   GLY A  23      22.773  29.396 -20.908  1.00 66.03           O  
ATOM    149  N   ASN A  24      24.552  28.133 -21.442  1.00 64.68           N  
ATOM    150  CA  ASN A  24      25.357  28.657 -20.346  1.00 65.49           C  
ATOM    151  C   ASN A  24      26.136  29.914 -20.676  1.00 66.68           C  
ATOM    152  O   ASN A  24      26.371  30.743 -19.794  1.00 65.69           O  
ATOM    153  CB  ASN A  24      26.238  27.557 -19.753  1.00 66.81           C  
ATOM    154  CG  ASN A  24      25.426  26.530 -18.983  1.00 65.19           C  
ATOM    155  OD1 ASN A  24      24.932  26.807 -17.889  1.00 64.66           O  
ATOM    156  ND2 ASN A  24      25.263  25.350 -19.563  1.00 65.22           N  
ATOM    157  N   VAL A  25      26.522  30.064 -21.944  1.00 69.89           N  
ATOM    158  CA  VAL A  25      26.940  31.370 -22.461  1.00 71.08           C  
ATOM    159  C   VAL A  25      25.766  32.347 -22.315  1.00 70.01           C  
ATOM    160  O   VAL A  25      25.941  33.468 -21.839  1.00 71.01           O  
ATOM    161  CB  VAL A  25      27.432  31.294 -23.930  1.00 71.32           C  
ATOM    162  CG1 VAL A  25      27.437  32.671 -24.581  1.00 71.63           C  
ATOM    163  CG2 VAL A  25      28.822  30.685 -23.992  1.00 71.40           C  
ATOM    164  N   LEU A  26      24.570  31.894 -22.693  1.00 69.17           N  
ATOM    165  CA  LEU A  26      23.345  32.671 -22.515  1.00 73.60           C  
ATOM    166  C   LEU A  26      23.191  33.187 -21.077  1.00 75.48           C  
ATOM    167  O   LEU A  26      22.940  34.381 -20.869  1.00 78.58           O  
ATOM    168  CB  LEU A  26      22.123  31.847 -22.938  1.00 76.80           C  
ATOM    169  CG  LEU A  26      20.892  32.569 -23.501  1.00 79.00           C  
ATOM    170  CD1 LEU A  26      21.203  33.265 -24.831  1.00 78.87           C  
ATOM    171  CD2 LEU A  26      19.736  31.593 -23.675  1.00 75.90           C  
ATOM    172  N   VAL A  27      23.366  32.294 -20.098  1.00 72.10           N  
ATOM    173  CA  VAL A  27      23.299  32.650 -18.674  1.00 68.49           C  
ATOM    174  C   VAL A  27      24.340  33.708 -18.308  1.00 69.85           C  
ATOM    175  O   VAL A  27      24.019  34.697 -17.644  1.00 72.04           O  
ATOM    176  CB  VAL A  27      23.460  31.399 -17.750  1.00 68.70           C  
ATOM    177  CG1 VAL A  27      23.630  31.799 -16.284  1.00 65.89           C  
ATOM    178  CG2 VAL A  27      22.277  30.450 -17.898  1.00 66.93           C  
ATOM    179  N   CYS A  28      25.579  33.499 -18.745  1.00 73.36           N  
ATOM    180  CA  CYS A  28      26.684  34.400 -18.402  1.00 77.35           C  
ATOM    181  C   CYS A  28      26.563  35.753 -19.089  1.00 76.94           C  
ATOM    182  O   CYS A  28      26.797  36.791 -18.463  1.00 74.56           O  
ATOM    183  CB  CYS A  28      28.034  33.761 -18.732  1.00 81.40           C  
ATOM    184  SG  CYS A  28      28.469  32.375 -17.665  1.00 84.61           S  
ATOM    185  N   TRP A  29      26.205  35.726 -20.373  1.00 79.19           N  
ATOM    186  CA  TRP A  29      25.942  36.935 -21.157  1.00 84.57           C  
ATOM    187  C   TRP A  29      24.902  37.806 -20.452  1.00 83.31           C  
ATOM    188  O   TRP A  29      25.078  39.022 -20.328  1.00 82.53           O  
ATOM    189  CB  TRP A  29      25.433  36.561 -22.554  1.00 92.60           C  
ATOM    190  CG  TRP A  29      25.833  37.506 -23.662  1.00 98.21           C  
ATOM    191  CD1 TRP A  29      26.072  38.850 -23.559  1.00 99.54           C  
ATOM    192  CD2 TRP A  29      26.006  37.174 -25.047  1.00101.37           C  
ATOM    193  NE1 TRP A  29      26.401  39.369 -24.789  1.00101.83           N  
ATOM    194  CE2 TRP A  29      26.366  38.364 -25.721  1.00103.06           C  
ATOM    195  CE3 TRP A  29      25.900  35.984 -25.783  1.00102.66           C  
ATOM    196  CZ2 TRP A  29      26.622  38.400 -27.099  1.00102.22           C  
ATOM    197  CZ3 TRP A  29      26.155  36.020 -27.155  1.00104.03           C  
ATOM    198  CH2 TRP A  29      26.511  37.222 -27.796  1.00103.65           C  
ATOM    199  N   ALA A  30      23.834  37.164 -19.976  1.00 81.30           N  
ATOM    200  CA  ALA A  30      22.741  37.844 -19.282  1.00 82.04           C  
ATOM    201  C   ALA A  30      23.182  38.601 -18.028  1.00 80.31           C  
ATOM    202  O   ALA A  30      22.637  39.659 -17.725  1.00 85.60           O  
ATOM    203  CB  ALA A  30      21.626  36.859 -18.951  1.00 84.13           C  
ATOM    204  N   VAL A  31      24.164  38.069 -17.307  1.00 80.70           N  
ATOM    205  CA  VAL A  31      24.663  38.729 -16.091  1.00 84.19           C  
ATOM    206  C   VAL A  31      25.557  39.926 -16.420  1.00 83.57           C  
ATOM    207  O   VAL A  31      25.584  40.911 -15.678  1.00 77.98           O  
ATOM    208  CB  VAL A  31      25.413  37.746 -15.153  1.00 82.38           C  
ATOM    209  CG1 VAL A  31      25.799  38.427 -13.844  1.00 80.22           C  
ATOM    210  CG2 VAL A  31      24.552  36.526 -14.866  1.00 85.17           C  
ATOM    211  N   TRP A  32      26.277  39.838 -17.535  1.00 89.62           N  
ATOM    212  CA  TRP A  32      27.183  40.906 -17.950  1.00 93.83           C  
ATOM    213  C   TRP A  32      26.420  42.140 -18.439  1.00 92.73           C  
ATOM    214  O   TRP A  32      26.762  43.266 -18.075  1.00 92.49           O  
ATOM    215  CB  TRP A  32      28.171  40.402 -19.009  1.00101.44           C  
ATOM    216  CG  TRP A  32      29.148  41.445 -19.487  1.00107.95           C  
ATOM    217  CD1 TRP A  32      29.919  42.267 -18.713  1.00109.19           C  
ATOM    218  CD2 TRP A  32      29.467  41.762 -20.850  1.00111.32           C  
ATOM    219  NE1 TRP A  32      30.689  43.083 -19.508  1.00112.26           N  
ATOM    220  CE2 TRP A  32      30.434  42.793 -20.823  1.00113.47           C  
ATOM    221  CE3 TRP A  32      29.028  41.277 -22.091  1.00112.43           C  
ATOM    222  CZ2 TRP A  32      30.971  43.351 -21.992  1.00115.29           C  
ATOM    223  CZ3 TRP A  32      29.563  41.833 -23.254  1.00114.45           C  
ATOM    224  CH2 TRP A  32      30.524  42.859 -23.193  1.00115.24           C  
ATOM    225  N   LEU A  33      25.383  41.917 -19.248  1.00 92.45           N  
ATOM    226  CA  LEU A  33      24.540  43.001 -19.760  1.00 91.63           C  
ATOM    227  C   LEU A  33      23.687  43.624 -18.655  1.00 94.54           C  
ATOM    228  O   LEU A  33      23.873  44.790 -18.296  1.00 98.65           O  
ATOM    229  CB  LEU A  33      23.639  42.505 -20.900  1.00 88.19           C  
ATOM    230  CG  LEU A  33      24.273  42.053 -22.221  1.00 88.48           C  
ATOM    231  CD1 LEU A  33      23.210  41.461 -23.128  1.00 87.77           C  
ATOM    232  CD2 LEU A  33      25.005  43.192 -22.927  1.00 86.92           C  
ATOM    233  N   ASN A  34      22.762  42.831 -18.118  1.00 92.87           N  
ATOM    234  CA  ASN A  34      21.827  43.284 -17.094  1.00 89.46           C  
ATOM    235  C   ASN A  34      22.518  43.617 -15.771  1.00 89.16           C  
ATOM    236  O   ASN A  34      23.224  42.788 -15.200  1.00 96.53           O  
ATOM    237  CB  ASN A  34      20.733  42.231 -16.889  1.00 85.38           C  
ATOM    238  CG  ASN A  34      19.614  42.708 -15.982  1.00 81.93           C  
ATOM    239  OD1 ASN A  34      19.787  43.627 -15.181  1.00 74.53           O  
ATOM    240  ND2 ASN A  34      18.454  42.072 -16.102  1.00 82.01           N  
ATOM    241  N   SER A  35      22.293  44.837 -15.294  1.00 89.85           N  
ATOM    242  CA  SER A  35      22.904  45.328 -14.062  1.00 88.64           C  
ATOM    243  C   SER A  35      22.161  44.865 -12.803  1.00 88.15           C  
ATOM    244  O   SER A  35      22.735  44.854 -11.711  1.00 86.36           O  
ATOM    245  CB  SER A  35      22.997  46.856 -14.096  1.00 89.76           C  
ATOM    246  OG  SER A  35      23.570  47.362 -12.903  1.00 95.29           O  
ATOM    247  N   ASN A  36      20.890  44.494 -12.960  1.00 88.49           N  
ATOM    248  CA  ASN A  36      20.080  43.951 -11.862  1.00 88.84           C  
ATOM    249  C   ASN A  36      20.548  42.554 -11.459  1.00 91.73           C  
ATOM    250  O   ASN A  36      20.379  42.132 -10.310  1.00 92.32           O  
ATOM    251  CB  ASN A  36      18.597  43.887 -12.252  1.00 88.52           C  
ATOM    252  CG  ASN A  36      18.002  45.254 -12.551  1.00 87.72           C  
ATOM    253  OD1 ASN A  36      17.999  46.148 -11.703  1.00 82.98           O  
ATOM    254  ND2 ASN A  36      17.478  45.413 -13.761  1.00 85.70           N  
ATOM    255  N   LEU A  37      21.133  41.847 -12.421  1.00 88.47           N  
ATOM    256  CA  LEU A  37      21.619  40.494 -12.210  1.00 84.84           C  
ATOM    257  C   LEU A  37      23.009  40.467 -11.564  1.00 84.35           C  
ATOM    258  O   LEU A  37      23.520  39.398 -11.229  1.00 84.13           O  
ATOM    259  CB  LEU A  37      21.615  39.720 -13.537  1.00 81.68           C  
ATOM    260  CG  LEU A  37      20.255  39.475 -14.201  1.00 78.58           C  
ATOM    261  CD1 LEU A  37      20.401  38.688 -15.493  1.00 75.90           C  
ATOM    262  CD2 LEU A  37      19.304  38.756 -13.258  1.00 80.52           C  
ATOM    263  N   GLN A  38      23.606  41.642 -11.374  1.00 83.23           N  
ATOM    264  CA  GLN A  38      24.973  41.738 -10.855  1.00 82.77           C  
ATOM    265  C   GLN A  38      25.040  41.855  -9.332  1.00 82.85           C  
ATOM    266  O   GLN A  38      25.518  42.856  -8.795  1.00 88.43           O  
ATOM    267  CB  GLN A  38      25.740  42.877 -11.544  1.00 78.52           C  
ATOM    268  CG  GLN A  38      26.147  42.541 -12.979  1.00 77.64           C  
ATOM    269  CD  GLN A  38      26.647  43.734 -13.775  1.00 78.08           C  
ATOM    270  OE1 GLN A  38      27.127  44.720 -13.216  1.00 80.73           O  
ATOM    271  NE2 GLN A  38      26.543  43.641 -15.098  1.00 77.25           N  
ATOM    272  N   ASN A  39      24.554  40.823  -8.646  1.00 81.50           N  
ATOM    273  CA  ASN A  39      24.686  40.718  -7.192  1.00 81.54           C  
ATOM    274  C   ASN A  39      25.285  39.372  -6.754  1.00 79.96           C  
ATOM    275  O   ASN A  39      25.387  38.439  -7.557  1.00 76.57           O  
ATOM    276  CB  ASN A  39      23.348  40.995  -6.489  1.00 81.14           C  
ATOM    277  CG  ASN A  39      22.326  39.900  -6.721  1.00 83.83           C  
ATOM    278  OD1 ASN A  39      21.821  39.727  -7.832  1.00 84.73           O  
ATOM    279  ND2 ASN A  39      22.012  39.155  -5.667  1.00 84.43           N  
ATOM    280  N   VAL A  40      25.665  39.290  -5.478  1.00 81.61           N  
ATOM    281  CA  VAL A  40      26.411  38.148  -4.917  1.00 83.04           C  
ATOM    282  C   VAL A  40      25.788  36.776  -5.217  1.00 81.23           C  
ATOM    283  O   VAL A  40      26.491  35.856  -5.635  1.00 81.12           O  
ATOM    284  CB  VAL A  40      26.643  38.316  -3.387  1.00 84.44           C  
ATOM    285  CG1 VAL A  40      27.349  37.098  -2.801  1.00 86.79           C  
ATOM    286  CG2 VAL A  40      27.446  39.587  -3.100  1.00 85.03           C  
ATOM    287  N   THR A  41      24.477  36.657  -5.014  1.00 76.95           N  
ATOM    288  CA  THR A  41      23.732  35.416  -5.264  1.00 74.08           C  
ATOM    289  C   THR A  41      24.034  34.790  -6.632  1.00 71.34           C  
ATOM    290  O   THR A  41      24.009  33.567  -6.780  1.00 72.05           O  
ATOM    291  CB  THR A  41      22.200  35.656  -5.121  1.00 74.62           C  
ATOM    292  OG1 THR A  41      21.921  36.163  -3.810  1.00 75.78           O  
ATOM    293  CG2 THR A  41      21.393  34.370  -5.344  1.00 69.66           C  
ATOM    294  N   ASN A  42      24.327  35.632  -7.619  1.00 71.50           N  
ATOM    295  CA  ASN A  42      24.519  35.171  -8.992  1.00 73.09           C  
ATOM    296  C   ASN A  42      25.943  34.734  -9.325  1.00 70.79           C  
ATOM    297  O   ASN A  42      26.173  34.091 -10.348  1.00 66.84           O  
ATOM    298  CB  ASN A  42      23.991  36.206  -9.982  1.00 77.64           C  
ATOM    299  CG  ASN A  42      22.482  36.356  -9.902  1.00 83.66           C  
ATOM    300  OD1 ASN A  42      21.739  35.442 -10.262  1.00 85.81           O  
ATOM    301  ND2 ASN A  42      22.021  37.505  -9.413  1.00 83.72           N  
ATOM    302  N   TYR A  43      26.891  35.036  -8.462  1.00 74.33           N  
ATOM    303  CA  TYR A  43      28.259  34.510  -8.550  1.00 75.85           C  
ATOM    304  C   TYR A  43      28.237  32.986  -8.561  1.00 71.68           C  
ATOM    305  O   TYR A  43      28.984  32.358  -9.311  1.00 72.30           O  
ATOM    306  CB  TYR A  43      29.113  34.998  -7.375  1.00 82.05           C  
ATOM    307  CG  TYR A  43      29.364  36.493  -7.339  1.00 93.03           C  
ATOM    308  CD1 TYR A  43      28.771  37.356  -8.273  1.00 97.38           C  
ATOM    309  CD2 TYR A  43      30.172  37.051  -6.350  1.00 95.13           C  
ATOM    310  CE1 TYR A  43      28.994  38.723  -8.233  1.00100.09           C  
ATOM    311  CE2 TYR A  43      30.396  38.419  -6.298  1.00100.16           C  
ATOM    312  CZ  TYR A  43      29.807  39.249  -7.241  1.00102.90           C  
ATOM    313  OH  TYR A  43      30.031  40.608  -7.196  1.00106.70           O  
ATOM    314  N   PHE A  44      27.316  32.425  -7.723  1.00 64.85           N  
ATOM    315  CA  PHE A  44      27.145  30.977  -7.677  1.00 62.84           C  
ATOM    316  C   PHE A  44      26.527  30.423  -8.962  1.00 64.42           C  
ATOM    317  O   PHE A  44      26.854  29.312  -9.388  1.00 68.42           O  
ATOM    318  CB  PHE A  44      26.321  30.563  -6.455  1.00 60.30           C  
ATOM    319  CG  PHE A  44      26.906  31.017  -5.141  1.00 58.73           C  
ATOM    320  CD1 PHE A  44      28.097  30.472  -4.664  1.00 57.58           C  
ATOM    321  CD2 PHE A  44      26.265  31.994  -4.381  1.00 59.87           C  
ATOM    322  CE1 PHE A  44      28.641  30.890  -3.446  1.00 60.19           C  
ATOM    323  CE2 PHE A  44      26.801  32.426  -3.159  1.00 61.00           C  
ATOM    324  CZ  PHE A  44      27.989  31.869  -2.689  1.00 61.47           C  
ATOM    325  N   VAL A  45      25.646  31.204  -9.581  1.00 64.09           N  
ATOM    326  CA  VAL A  45      25.031  30.826 -10.859  1.00 60.28           C  
ATOM    327  C   VAL A  45      26.036  30.946 -12.012  1.00 58.43           C  
ATOM    328  O   VAL A  45      26.071  30.087 -12.904  1.00 56.76           O  
ATOM    329  CB  VAL A  45      23.732  31.644 -11.136  1.00 61.03           C  
ATOM    330  CG1 VAL A  45      23.138  31.311 -12.497  1.00 58.45           C  
ATOM    331  CG2 VAL A  45      22.698  31.387 -10.040  1.00 59.30           C  
ATOM    332  N   VAL A  46      26.860  31.996 -11.978  1.00 58.60           N  
ATOM    333  CA  VAL A  46      27.890  32.218 -13.003  1.00 60.81           C  
ATOM    334  C   VAL A  46      28.965  31.129 -12.959  1.00 60.70           C  
ATOM    335  O   VAL A  46      29.380  30.624 -14.008  1.00 61.41           O  
ATOM    336  CB  VAL A  46      28.535  33.633 -12.904  1.00 64.78           C  
ATOM    337  CG1 VAL A  46      29.676  33.794 -13.922  1.00 65.10           C  
ATOM    338  CG2 VAL A  46      27.489  34.723 -13.131  1.00 65.48           C  
ATOM    339  N   SER A  47      29.393  30.765 -11.748  1.00 59.34           N  
ATOM    340  CA  SER A  47      30.351  29.675 -11.544  1.00 59.41           C  
ATOM    341  C   SER A  47      29.855  28.391 -12.184  1.00 58.57           C  
ATOM    342  O   SER A  47      30.573  27.763 -12.970  1.00 57.00           O  
ATOM    343  CB  SER A  47      30.590  29.419 -10.054  1.00 62.06           C  
ATOM    344  OG  SER A  47      31.004  30.593  -9.383  1.00 65.07           O  
ATOM    345  N   ALA A  48      28.618  28.022 -11.849  1.00 56.03           N  
ATOM    346  CA  ALA A  48      28.012  26.792 -12.338  1.00 56.61           C  
ATOM    347  C   ALA A  48      27.912  26.797 -13.857  1.00 58.57           C  
ATOM    348  O   ALA A  48      28.246  25.805 -14.517  1.00 56.81           O  
ATOM    349  CB  ALA A  48      26.651  26.582 -11.700  1.00 53.55           C  
ATOM    350  N   ALA A  49      27.473  27.928 -14.402  1.00 62.41           N  
ATOM    351  CA  ALA A  49      27.362  28.104 -15.846  1.00 62.78           C  
ATOM    352  C   ALA A  49      28.730  28.030 -16.529  1.00 59.67           C  
ATOM    353  O   ALA A  49      28.856  27.415 -17.590  1.00 58.34           O  
ATOM    354  CB  ALA A  49      26.647  29.414 -16.177  1.00 65.55           C  
ATOM    355  N   ALA A  50      29.745  28.644 -15.915  1.00 57.32           N  
ATOM    356  CA  ALA A  50      31.128  28.561 -16.418  1.00 59.69           C  
ATOM    357  C   ALA A  50      31.627  27.113 -16.507  1.00 61.93           C  
ATOM    358  O   ALA A  50      32.117  26.682 -17.555  1.00 66.03           O  
ATOM    359  CB  ALA A  50      32.066  29.401 -15.560  1.00 58.79           C  
ATOM    360  N   ALA A  51      31.473  26.369 -15.409  1.00 61.51           N  
ATOM    361  CA  ALA A  51      31.838  24.949 -15.337  1.00 58.07           C  
ATOM    362  C   ALA A  51      31.131  24.084 -16.382  1.00 58.58           C  
ATOM    363  O   ALA A  51      31.740  23.174 -16.949  1.00 60.69           O  
ATOM    364  CB  ALA A  51      31.585  24.407 -13.932  1.00 58.44           C  
ATOM    365  N   ASP A  52      29.855  24.369 -16.639  1.00 61.10           N  
ATOM    366  CA  ASP A  52      29.087  23.641 -17.655  1.00 64.75           C  
ATOM    367  C   ASP A  52      29.602  23.902 -19.071  1.00 65.58           C  
ATOM    368  O   ASP A  52      29.552  23.016 -19.933  1.00 61.04           O  
ATOM    369  CB  ASP A  52      27.603  23.993 -17.576  1.00 68.85           C  
ATOM    370  CG  ASP A  52      26.924  23.425 -16.341  1.00 74.53           C  
ATOM    371  OD1 ASP A  52      27.271  22.305 -15.897  1.00 76.63           O  
ATOM    372  OD2 ASP A  52      26.022  24.108 -15.819  1.00 76.06           O1-
ATOM    373  N   ILE A  53      30.084  25.126 -19.301  1.00 66.39           N  
ATOM    374  CA  ILE A  53      30.733  25.476 -20.560  1.00 64.79           C  
ATOM    375  C   ILE A  53      31.961  24.588 -20.748  1.00 63.88           C  
ATOM    376  O   ILE A  53      32.080  23.909 -21.769  1.00 63.01           O  
ATOM    377  CB  ILE A  53      31.099  26.983 -20.634  1.00 65.55           C  
ATOM    378  CG1 ILE A  53      29.827  27.835 -20.752  1.00 63.52           C  
ATOM    379  CG2 ILE A  53      32.029  27.257 -21.819  1.00 63.24           C  
ATOM    380  CD1 ILE A  53      29.972  29.252 -20.239  1.00 60.65           C  
ATOM    381  N   LEU A  54      32.844  24.561 -19.749  1.00 63.33           N  
ATOM    382  CA  LEU A  54      34.031  23.698 -19.802  1.00 63.06           C  
ATOM    383  C   LEU A  54      33.685  22.219 -20.028  1.00 60.63           C  
ATOM    384  O   LEU A  54      34.464  21.492 -20.642  1.00 59.99           O  
ATOM    385  CB  LEU A  54      34.911  23.871 -18.556  1.00 64.70           C  
ATOM    386  CG  LEU A  54      35.622  25.217 -18.326  1.00 68.13           C  
ATOM    387  CD1 LEU A  54      36.421  25.209 -17.021  1.00 66.92           C  
ATOM    388  CD2 LEU A  54      36.535  25.592 -19.496  1.00 69.37           C  
ATOM    389  N   VAL A  55      32.521  21.785 -19.544  1.00 57.31           N  
ATOM    390  CA  VAL A  55      32.038  20.424 -19.800  1.00 58.15           C  
ATOM    391  C   VAL A  55      31.733  20.221 -21.287  1.00 60.92           C  
ATOM    392  O   VAL A  55      32.028  19.161 -21.856  1.00 60.44           O  
ATOM    393  CB  VAL A  55      30.786  20.075 -18.931  1.00 59.41           C  
ATOM    394  CG1 VAL A  55      30.107  18.787 -19.408  1.00 54.84           C  
ATOM    395  CG2 VAL A  55      31.161  19.963 -17.455  1.00 57.30           C  
ATOM    396  N   GLY A  56      31.143  21.247 -21.904  1.00 66.06           N  
ATOM    397  CA  GLY A  56      30.795  21.231 -23.324  1.00 61.34           C  
ATOM    398  C   GLY A  56      32.013  21.371 -24.215  1.00 62.36           C  
ATOM    399  O   GLY A  56      32.148  20.656 -25.209  1.00 64.60           O  
ATOM    400  N   VAL A  57      32.902  22.292 -23.856  1.00 62.18           N  
ATOM    401  CA  VAL A  57      34.099  22.558 -24.649  1.00 66.36           C  
ATOM    402  C   VAL A  57      35.161  21.462 -24.481  1.00 70.36           C  
ATOM    403  O   VAL A  57      35.655  20.917 -25.473  1.00 71.05           O  
ATOM    404  CB  VAL A  57      34.711  23.943 -24.322  1.00 66.42           C  
ATOM    405  CG1 VAL A  57      35.919  24.222 -25.212  1.00 66.99           C  
ATOM    406  CG2 VAL A  57      33.673  25.040 -24.491  1.00 66.37           C  
ATOM    407  N   LEU A  58      35.503  21.143 -23.232  1.00 70.28           N  
ATOM    408  CA  LEU A  58      36.620  20.236 -22.939  1.00 67.01           C  
ATOM    409  C   LEU A  58      36.197  18.808 -22.576  1.00 66.12           C  
ATOM    410  O   LEU A  58      36.690  17.853 -23.173  1.00 67.33           O  
ATOM    411  CB  LEU A  58      37.517  20.821 -21.839  1.00 64.02           C  
ATOM    412  CG  LEU A  58      38.169  22.192 -22.048  1.00 65.00           C  
ATOM    413  CD1 LEU A  58      38.647  22.755 -20.722  1.00 64.71           C  
ATOM    414  CD2 LEU A  58      39.322  22.134 -23.048  1.00 66.27           C  
ATOM    415  N   ALA A  59      35.280  18.668 -21.616  1.00 64.84           N  
ATOM    416  CA  ALA A  59      34.959  17.358 -21.036  1.00 62.67           C  
ATOM    417  C   ALA A  59      34.290  16.385 -21.996  1.00 62.37           C  
ATOM    418  O   ALA A  59      34.684  15.219 -22.058  1.00 63.19           O  
ATOM    419  CB  ALA A  59      34.139  17.505 -19.757  1.00 62.51           C  
ATOM    420  N   ILE A  60      33.285  16.851 -22.735  1.00 62.74           N  
ATOM    421  CA  ILE A  60      32.582  15.989 -23.697  1.00 64.11           C  
ATOM    422  C   ILE A  60      33.463  15.544 -24.885  1.00 64.95           C  
ATOM    423  O   ILE A  60      33.445  14.363 -25.250  1.00 64.60           O  
ATOM    424  CB  ILE A  60      31.231  16.595 -24.174  1.00 66.47           C  
ATOM    425  CG1 ILE A  60      30.219  16.619 -23.020  1.00 67.64           C  
ATOM    426  CG2 ILE A  60      30.674  15.807 -25.355  1.00 64.10           C  
ATOM    427  CD1 ILE A  60      28.860  17.250 -23.360  1.00 63.75           C  
ATOM    428  N   PRO A  61      34.240  16.477 -25.486  1.00 66.34           N  
ATOM    429  CA  PRO A  61      35.176  16.034 -26.531  1.00 69.25           C  
ATOM    430  C   PRO A  61      36.154  14.968 -26.028  1.00 68.27           C  
ATOM    431  O   PRO A  61      36.380  13.972 -26.720  1.00 68.11           O  
ATOM    432  CB  PRO A  61      35.922  17.321 -26.901  1.00 68.70           C  
ATOM    433  CG  PRO A  61      34.952  18.393 -26.613  1.00 67.54           C  
ATOM    434  CD  PRO A  61      34.221  17.948 -25.374  1.00 65.94           C  
ATOM    435  N   PHE A  62      36.702  15.170 -24.828  1.00 67.19           N  
ATOM    436  CA  PHE A  62      37.559  14.172 -24.178  1.00 65.93           C  
ATOM    437  C   PHE A  62      36.833  12.844 -23.940  1.00 65.92           C  
ATOM    438  O   PHE A  62      37.422  11.775 -24.101  1.00 66.26           O  
ATOM    439  CB  PHE A  62      38.104  14.695 -22.847  1.00 65.34           C  
ATOM    440  CG  PHE A  62      39.121  15.796 -22.980  1.00 67.34           C  
ATOM    441  CD1 PHE A  62      39.758  16.050 -24.191  1.00 67.13           C  
ATOM    442  CD2 PHE A  62      39.468  16.562 -21.872  1.00 70.24           C  
ATOM    443  CE1 PHE A  62      40.699  17.068 -24.302  1.00 68.77           C  
ATOM    444  CE2 PHE A  62      40.417  17.581 -21.974  1.00 72.47           C  
ATOM    445  CZ  PHE A  62      41.034  17.832 -23.193  1.00 69.12           C  
ATOM    446  N   ALA A  63      35.558  12.920 -23.565  1.00 63.08           N  
ATOM    447  CA  ALA A  63      34.757  11.730 -23.306  1.00 64.40           C  
ATOM    448  C   ALA A  63      34.517  10.932 -24.582  1.00 66.55           C  
ATOM    449  O   ALA A  63      34.509   9.704 -24.550  1.00 66.75           O  
ATOM    450  CB  ALA A  63      33.432  12.105 -22.647  1.00 63.11           C  
ATOM    451  N   ILE A  64      34.321  11.637 -25.697  1.00 70.70           N  
ATOM    452  CA  ILE A  64      34.150  11.001 -27.009  1.00 70.70           C  
ATOM    453  C   ILE A  64      35.388  10.179 -27.379  1.00 70.11           C  
ATOM    454  O   ILE A  64      35.276   9.020 -27.788  1.00 67.25           O  
ATOM    455  CB  ILE A  64      33.822  12.037 -28.127  1.00 71.28           C  
ATOM    456  CG1 ILE A  64      32.385  12.550 -27.976  1.00 72.05           C  
ATOM    457  CG2 ILE A  64      34.002  11.420 -29.519  1.00 71.39           C  
ATOM    458  CD1 ILE A  64      32.015  13.686 -28.917  1.00 71.37           C  
ATOM    459  N   ALA A  65      36.560  10.789 -27.218  1.00 71.01           N  
ATOM    460  CA  ALA A  65      37.834  10.134 -27.505  1.00 72.56           C  
ATOM    461  C   ALA A  65      37.989   8.820 -26.735  1.00 74.01           C  
ATOM    462  O   ALA A  65      38.302   7.781 -27.322  1.00 73.71           O  
ATOM    463  CB  ALA A  65      38.991  11.084 -27.201  1.00 71.49           C  
ATOM    464  N   ILE A  66      37.732   8.873 -25.427  1.00 74.33           N  
ATOM    465  CA  ILE A  66      37.874   7.717 -24.534  1.00 73.92           C  
ATOM    466  C   ILE A  66      36.944   6.552 -24.899  1.00 74.38           C  
ATOM    467  O   ILE A  66      37.188   5.413 -24.496  1.00 75.82           O  
ATOM    468  CB  ILE A  66      37.673   8.122 -23.040  1.00 76.38           C  
ATOM    469  CG1 ILE A  66      38.635   9.245 -22.627  1.00 77.60           C  
ATOM    470  CG2 ILE A  66      37.850   6.936 -22.115  1.00 79.76           C  
ATOM    471  CD1 ILE A  66      40.104   8.986 -22.928  1.00 75.88           C  
ATOM    472  N   SER A  67      35.892   6.833 -25.667  1.00 74.53           N  
ATOM    473  CA  SER A  67      34.946   5.793 -26.085  1.00 74.68           C  
ATOM    474  C   SER A  67      35.429   5.003 -27.306  1.00 74.45           C  
ATOM    475  O   SER A  67      34.902   3.927 -27.599  1.00 71.78           O  
ATOM    476  CB  SER A  67      33.558   6.385 -26.345  1.00 74.32           C  
ATOM    477  OG  SER A  67      33.552   7.202 -27.502  1.00 75.85           O  
ATOM    478  N   THR A  68      36.441   5.535 -27.993  1.00 75.19           N  
ATOM    479  CA  THR A  68      36.916   4.969 -29.260  1.00 77.23           C  
ATOM    480  C   THR A  68      37.993   3.909 -29.087  1.00 80.14           C  
ATOM    481  O   THR A  68      38.272   3.152 -30.014  1.00 84.91           O  
ATOM    482  CB  THR A  68      37.475   6.053 -30.213  1.00 75.97           C  
ATOM    483  OG1 THR A  68      38.690   6.593 -29.676  1.00 74.03           O  
ATOM    484  CG2 THR A  68      36.455   7.171 -30.442  1.00 75.84           C  
ATOM    485  N   GLY A  69      38.608   3.872 -27.910  1.00 84.38           N  
ATOM    486  CA  GLY A  69      39.691   2.931 -27.636  1.00 84.28           C  
ATOM    487  C   GLY A  69      40.856   3.099 -28.590  1.00 84.59           C  
ATOM    488  O   GLY A  69      41.382   2.117 -29.117  1.00 87.87           O  
ATOM    489  N   PHE A  70      41.246   4.352 -28.815  1.00 80.34           N  
ATOM    490  CA  PHE A  70      42.388   4.675 -29.664  1.00 80.17           C  
ATOM    491  C   PHE A  70      43.700   4.274 -28.989  1.00 81.16           C  
ATOM    492  O   PHE A  70      43.737   4.063 -27.776  1.00 81.98           O  
ATOM    493  CB  PHE A  70      42.385   6.167 -30.035  1.00 74.85           C  
ATOM    494  CG  PHE A  70      42.535   7.095 -28.860  1.00 70.77           C  
ATOM    495  CD1 PHE A  70      41.422   7.500 -28.128  1.00 70.85           C  
ATOM    496  CD2 PHE A  70      43.786   7.578 -28.495  1.00 68.36           C  
ATOM    497  CE1 PHE A  70      41.553   8.363 -27.041  1.00 67.40           C  
ATOM    498  CE2 PHE A  70      43.929   8.440 -27.412  1.00 69.35           C  
ATOM    499  CZ  PHE A  70      42.809   8.833 -26.682  1.00 67.83           C  
ATOM    500  N   CYS A  71      44.769   4.173 -29.778  1.00 85.46           N  
ATOM    501  CA  CYS A  71      46.083   3.775 -29.264  1.00 85.17           C  
ATOM    502  C   CYS A  71      46.823   4.938 -28.614  1.00 80.92           C  
ATOM    503  O   CYS A  71      47.006   5.990 -29.232  1.00 82.22           O  
ATOM    504  CB  CYS A  71      46.940   3.167 -30.377  1.00 87.57           C  
ATOM    505  SG  CYS A  71      46.267   1.648 -31.065  1.00 98.35           S  
ATOM    506  N   ALA A  72      47.242   4.735 -27.365  1.00 76.02           N  
ATOM    507  CA  ALA A  72      47.996   5.740 -26.613  1.00 74.58           C  
ATOM    508  C   ALA A  72      48.702   5.141 -25.400  1.00 71.71           C  
ATOM    509  O   ALA A  72      48.383   4.033 -24.964  1.00 72.11           O  
ATOM    510  CB  ALA A  72      47.075   6.882 -26.173  1.00 76.30           C  
ATOM    511  N   ALA A  73      49.661   5.888 -24.861  1.00 70.82           N  
ATOM    512  CA  ALA A  73      50.286   5.555 -23.586  1.00 73.09           C  
ATOM    513  C   ALA A  73      49.237   5.533 -22.469  1.00 73.50           C  
ATOM    514  O   ALA A  73      48.446   6.472 -22.335  1.00 73.48           O  
ATOM    515  CB  ALA A  73      51.384   6.559 -23.264  1.00 70.33           C  
ATOM    516  N   CYS A  74      49.241   4.463 -21.676  1.00 74.64           N  
ATOM    517  CA  CYS A  74      48.285   4.284 -20.579  1.00 75.65           C  
ATOM    518  C   CYS A  74      48.107   5.542 -19.724  1.00 77.01           C  
ATOM    519  O   CYS A  74      46.979   5.911 -19.385  1.00 78.75           O  
ATOM    520  CB  CYS A  74      48.699   3.111 -19.686  1.00 73.39           C  
ATOM    521  SG  CYS A  74      47.387   2.526 -18.567  1.00 85.03           S  
ATOM    522  N   HIS A  75      49.217   6.196 -19.386  1.00 76.00           N  
ATOM    523  CA  HIS A  75      49.194   7.351 -18.489  1.00 75.54           C  
ATOM    524  C   HIS A  75      48.680   8.622 -19.151  1.00 74.36           C  
ATOM    525  O   HIS A  75      48.224   9.540 -18.464  1.00 70.91           O  
ATOM    526  CB  HIS A  75      50.564   7.569 -17.849  1.00 76.31           C  
ATOM    527  CG  HIS A  75      50.891   6.558 -16.797  1.00 79.93           C  
ATOM    528  ND1 HIS A  75      51.503   5.357 -17.085  1.00 80.90           N  
ATOM    529  CD2 HIS A  75      50.664   6.556 -15.462  1.00 79.28           C  
ATOM    530  CE1 HIS A  75      51.652   4.664 -15.969  1.00 79.77           C  
ATOM    531  NE2 HIS A  75      51.153   5.370 -14.970  1.00 80.52           N  
ATOM    532  N   GLY A  76      48.757   8.668 -20.480  1.00 71.71           N  
ATOM    533  CA  GLY A  76      48.130   9.733 -21.251  1.00 70.62           C  
ATOM    534  C   GLY A  76      46.627   9.516 -21.285  1.00 70.72           C  
ATOM    535  O   GLY A  76      45.844  10.467 -21.206  1.00 70.09           O  
ATOM    536  N   CYS A  77      46.234   8.251 -21.390  1.00 68.69           N  
ATOM    537  CA  CYS A  77      44.832   7.870 -21.394  1.00 70.40           C  
ATOM    538  C   CYS A  77      44.186   8.138 -20.039  1.00 70.15           C  
ATOM    539  O   CYS A  77      43.038   8.586 -19.964  1.00 70.46           O  
ATOM    540  CB  CYS A  77      44.681   6.399 -21.765  1.00 74.60           C  
ATOM    541  SG  CYS A  77      42.963   5.887 -21.900  1.00 86.64           S  
ATOM    542  N   LEU A  78      44.932   7.874 -18.972  1.00 68.07           N  
ATOM    543  CA  LEU A  78      44.433   8.085 -17.618  1.00 66.97           C  
ATOM    544  C   LEU A  78      44.217   9.571 -17.324  1.00 67.61           C  
ATOM    545  O   LEU A  78      43.266   9.937 -16.626  1.00 67.94           O  
ATOM    546  CB  LEU A  78      45.379   7.455 -16.590  1.00 63.80           C  
ATOM    547  CG  LEU A  78      44.978   7.516 -15.111  1.00 61.61           C  
ATOM    548  CD1 LEU A  78      43.766   6.653 -14.798  1.00 60.09           C  
ATOM    549  CD2 LEU A  78      46.156   7.149 -14.227  1.00 60.73           C  
ATOM    550  N   PHE A  79      45.096  10.412 -17.867  1.00 66.19           N  
ATOM    551  CA  PHE A  79      45.042  11.860 -17.649  1.00 70.82           C  
ATOM    552  C   PHE A  79      43.805  12.502 -18.289  1.00 70.02           C  
ATOM    553  O   PHE A  79      43.222  13.434 -17.733  1.00 69.78           O  
ATOM    554  CB  PHE A  79      46.326  12.530 -18.158  1.00 72.74           C  
ATOM    555  CG  PHE A  79      46.481  13.961 -17.721  1.00 74.68           C  
ATOM    556  CD1 PHE A  79      47.038  14.268 -16.482  1.00 77.66           C  
ATOM    557  CD2 PHE A  79      46.074  15.005 -18.550  1.00 77.63           C  
ATOM    558  CE1 PHE A  79      47.183  15.595 -16.068  1.00 78.72           C  
ATOM    559  CE2 PHE A  79      46.214  16.337 -18.148  1.00 79.27           C  
ATOM    560  CZ  PHE A  79      46.771  16.630 -16.903  1.00 79.14           C  
ATOM    561  N   ILE A  80      43.415  11.994 -19.454  1.00 66.92           N  
ATOM    562  CA  ILE A  80      42.216  12.461 -20.141  1.00 67.25           C  
ATOM    563  C   ILE A  80      40.949  12.039 -19.378  1.00 65.63           C  
ATOM    564  O   ILE A  80      40.022  12.837 -19.213  1.00 64.73           O  
ATOM    565  CB  ILE A  80      42.180  11.958 -21.608  1.00 67.81           C  
ATOM    566  CG1 ILE A  80      43.388  12.492 -22.384  1.00 67.59           C  
ATOM    567  CG2 ILE A  80      40.889  12.377 -22.301  1.00 67.09           C  
ATOM    568  CD1 ILE A  80      43.777  11.643 -23.589  1.00 70.26           C  
ATOM    569  N   ALA A  81      40.919  10.792 -18.912  1.00 62.39           N  
ATOM    570  CA  ALA A  81      39.802  10.290 -18.116  1.00 59.79           C  
ATOM    571  C   ALA A  81      39.689  11.066 -16.804  1.00 60.09           C  
ATOM    572  O   ALA A  81      38.588  11.365 -16.336  1.00 58.31           O  
ATOM    573  CB  ALA A  81      39.961   8.804 -17.853  1.00 56.90           C  
ATOM    574  N   CYS A  82      40.839  11.413 -16.233  1.00 59.58           N  
ATOM    575  CA  CYS A  82      40.884  12.197 -15.007  1.00 59.33           C  
ATOM    576  C   CYS A  82      40.384  13.608 -15.222  1.00 59.77           C  
ATOM    577  O   CYS A  82      39.796  14.208 -14.319  1.00 60.70           O  
ATOM    578  CB  CYS A  82      42.300  12.222 -14.435  1.00 59.60           C  
ATOM    579  SG  CYS A  82      42.672  10.768 -13.436  1.00 58.99           S  
ATOM    580  N   PHE A  83      40.621  14.136 -16.419  1.00 63.39           N  
ATOM    581  CA  PHE A  83      40.204  15.489 -16.743  1.00 64.18           C  
ATOM    582  C   PHE A  83      38.695  15.559 -16.973  1.00 61.88           C  
ATOM    583  O   PHE A  83      38.066  16.568 -16.664  1.00 65.21           O  
ATOM    584  CB  PHE A  83      40.996  16.044 -17.928  1.00 69.80           C  
ATOM    585  CG  PHE A  83      41.359  17.497 -17.779  1.00 79.96           C  
ATOM    586  CD1 PHE A  83      42.135  17.927 -16.698  1.00 84.02           C  
ATOM    587  CD2 PHE A  83      40.926  18.438 -18.710  1.00 84.17           C  
ATOM    588  CE1 PHE A  83      42.470  19.274 -16.545  1.00 86.96           C  
ATOM    589  CE2 PHE A  83      41.260  19.789 -18.573  1.00 87.71           C  
ATOM    590  CZ  PHE A  83      42.032  20.208 -17.487  1.00 89.85           C  
ATOM    591  N   VAL A  84      38.114  14.478 -17.488  1.00 58.46           N  
ATOM    592  CA  VAL A  84      36.658  14.365 -17.583  1.00 57.78           C  
ATOM    593  C   VAL A  84      36.033  14.385 -16.179  1.00 56.76           C  
ATOM    594  O   VAL A  84      34.999  15.025 -15.962  1.00 55.14           O  
ATOM    595  CB  VAL A  84      36.216  13.094 -18.366  1.00 57.19           C  
ATOM    596  CG1 VAL A  84      34.709  12.926 -18.325  1.00 57.61           C  
ATOM    597  CG2 VAL A  84      36.673  13.165 -19.814  1.00 56.60           C  
ATOM    598  N   LEU A  85      36.684  13.701 -15.237  1.00 54.12           N  
ATOM    599  CA  LEU A  85      36.205  13.582 -13.864  1.00 50.68           C  
ATOM    600  C   LEU A  85      36.245  14.906 -13.101  1.00 51.35           C  
ATOM    601  O   LEU A  85      35.264  15.274 -12.451  1.00 49.16           O  
ATOM    602  CB  LEU A  85      36.986  12.495 -13.114  1.00 49.09           C  
ATOM    603  CG  LEU A  85      36.693  11.035 -13.498  1.00 48.81           C  
ATOM    604  CD1 LEU A  85      37.834  10.107 -13.086  1.00 46.02           C  
ATOM    605  CD2 LEU A  85      35.348  10.541 -12.935  1.00 47.33           C  
ATOM    606  N   VAL A  86      37.370  15.618 -13.192  1.00 50.36           N  
ATOM    607  CA  VAL A  86      37.535  16.928 -12.542  1.00 49.78           C  
ATOM    608  C   VAL A  86      36.486  17.953 -12.997  1.00 49.46           C  
ATOM    609  O   VAL A  86      35.883  18.639 -12.166  1.00 49.25           O  
ATOM    610  CB  VAL A  86      38.962  17.516 -12.778  1.00 50.53           C  
ATOM    611  CG1 VAL A  86      39.061  18.974 -12.295  1.00 47.57           C  
ATOM    612  CG2 VAL A  86      40.018  16.662 -12.095  1.00 49.86           C  
ATOM    613  N   LEU A  87      36.283  18.050 -14.311  1.00 49.60           N  
ATOM    614  CA  LEU A  87      35.411  19.074 -14.897  1.00 50.51           C  
ATOM    615  C   LEU A  87      33.931  18.819 -14.616  1.00 52.46           C  
ATOM    616  O   LEU A  87      33.176  19.758 -14.320  1.00 52.43           O  
ATOM    617  CB  LEU A  87      35.656  19.218 -16.407  1.00 49.01           C  
ATOM    618  CG  LEU A  87      37.024  19.718 -16.897  1.00 48.53           C  
ATOM    619  CD1 LEU A  87      37.084  19.660 -18.416  1.00 48.16           C  
ATOM    620  CD2 LEU A  87      37.355  21.126 -16.395  1.00 46.93           C  
ATOM    621  N   THR A  88      33.519  17.556 -14.702  1.00 49.46           N  
ATOM    622  CA  THR A  88      32.162  17.190 -14.326  1.00 51.91           C  
ATOM    623  C   THR A  88      31.935  17.366 -12.819  1.00 51.96           C  
ATOM    624  O   THR A  88      30.827  17.701 -12.390  1.00 53.55           O  
ATOM    625  CB  THR A  88      31.786  15.760 -14.780  1.00 53.68           C  
ATOM    626  OG1 THR A  88      32.632  14.796 -14.138  1.00 56.09           O  
ATOM    627  CG2 THR A  88      31.916  15.629 -16.297  1.00 52.59           C  
ATOM    628  N   ALA A  89      32.987  17.162 -12.029  1.00 51.02           N  
ATOM    629  CA  ALA A  89      32.910  17.329 -10.578  1.00 52.15           C  
ATOM    630  C   ALA A  89      32.672  18.785 -10.200  1.00 52.40           C  
ATOM    631  O   ALA A  89      31.819  19.074  -9.351  1.00 51.45           O  
ATOM    632  CB  ALA A  89      34.173  16.793  -9.894  1.00 52.04           C  
ATOM    633  N   SER A  90      33.421  19.689 -10.839  1.00 52.14           N  
ATOM    634  CA  SER A  90      33.271  21.134 -10.630  1.00 53.25           C  
ATOM    635  C   SER A  90      31.847  21.581 -10.945  1.00 50.51           C  
ATOM    636  O   SER A  90      31.262  22.379 -10.218  1.00 52.89           O  
ATOM    637  CB  SER A  90      34.279  21.917 -11.479  1.00 53.68           C  
ATOM    638  OG  SER A  90      34.012  21.763 -12.868  1.00 54.78           O  
ATOM    639  N   SER A  91      31.303  21.039 -12.025  1.00 49.64           N  
ATOM    640  CA  SER A  91      29.909  21.247 -12.409  1.00 51.14           C  
ATOM    641  C   SER A  91      28.938  20.870 -11.277  1.00 49.20           C  
ATOM    642  O   SER A  91      28.027  21.630 -10.960  1.00 48.81           O  
ATOM    643  CB  SER A  91      29.605  20.443 -13.683  1.00 51.40           C  
ATOM    644  OG  SER A  91      28.213  20.288 -13.884  1.00 56.13           O  
ATOM    645  N   ILE A  92      29.149  19.701 -10.673  1.00 48.99           N  
ATOM    646  CA  ILE A  92      28.328  19.218  -9.560  1.00 46.91           C  
ATOM    647  C   ILE A  92      28.472  20.091  -8.313  1.00 45.78           C  
ATOM    648  O   ILE A  92      27.480  20.464  -7.695  1.00 44.87           O  
ATOM    649  CB  ILE A  92      28.668  17.744  -9.207  1.00 46.84           C  
ATOM    650  CG1 ILE A  92      28.226  16.800 -10.334  1.00 45.72           C  
ATOM    651  CG2 ILE A  92      28.025  17.339  -7.887  1.00 46.79           C  
ATOM    652  CD1 ILE A  92      28.822  15.402 -10.238  1.00 46.86           C  
ATOM    653  N   PHE A  93      29.708  20.422  -7.953  1.00 48.28           N  
ATOM    654  CA  PHE A  93      29.975  21.166  -6.721  1.00 49.40           C  
ATOM    655  C   PHE A  93      29.515  22.608  -6.784  1.00 50.21           C  
ATOM    656  O   PHE A  93      29.012  23.144  -5.792  1.00 50.25           O  
ATOM    657  CB  PHE A  93      31.457  21.098  -6.345  1.00 50.49           C  
ATOM    658  CG  PHE A  93      31.893  19.754  -5.842  1.00 50.34           C  
ATOM    659  CD1 PHE A  93      31.211  19.131  -4.803  1.00 50.99           C  
ATOM    660  CD2 PHE A  93      32.982  19.107  -6.412  1.00 50.82           C  
ATOM    661  CE1 PHE A  93      31.615  17.887  -4.336  1.00 52.29           C  
ATOM    662  CE2 PHE A  93      33.394  17.862  -5.953  1.00 50.50           C  
ATOM    663  CZ  PHE A  93      32.707  17.250  -4.916  1.00 51.63           C  
ATOM    664  N   SER A  94      29.693  23.243  -7.940  1.00 49.51           N  
ATOM    665  CA  SER A  94      29.225  24.614  -8.112  1.00 51.65           C  
ATOM    666  C   SER A  94      27.687  24.676  -8.161  1.00 51.78           C  
ATOM    667  O   SER A  94      27.092  25.705  -7.840  1.00 52.97           O  
ATOM    668  CB  SER A  94      29.862  25.263  -9.344  1.00 50.46           C  
ATOM    669  OG  SER A  94      29.462  24.592 -10.520  1.00 55.21           O  
ATOM    670  N   LEU A  95      27.055  23.572  -8.557  1.00 49.84           N  
ATOM    671  CA  LEU A  95      25.606  23.449  -8.483  1.00 51.74           C  
ATOM    672  C   LEU A  95      25.149  23.318  -7.030  1.00 55.34           C  
ATOM    673  O   LEU A  95      24.136  23.908  -6.639  1.00 59.58           O  
ATOM    674  CB  LEU A  95      25.109  22.266  -9.316  1.00 51.50           C  
ATOM    675  CG  LEU A  95      23.589  22.076  -9.384  1.00 54.73           C  
ATOM    676  CD1 LEU A  95      22.908  23.249 -10.111  1.00 55.16           C  
ATOM    677  CD2 LEU A  95      23.236  20.742 -10.038  1.00 52.36           C  
ATOM    678  N   LEU A  96      25.904  22.555  -6.239  1.00 52.29           N  
ATOM    679  CA  LEU A  96      25.678  22.458  -4.799  1.00 51.24           C  
ATOM    680  C   LEU A  96      25.749  23.826  -4.104  1.00 53.23           C  
ATOM    681  O   LEU A  96      24.943  24.120  -3.210  1.00 54.94           O  
ATOM    682  CB  LEU A  96      26.680  21.479  -4.164  1.00 49.75           C  
ATOM    683  CG  LEU A  96      26.652  21.240  -2.647  1.00 49.07           C  
ATOM    684  CD1 LEU A  96      25.337  20.596  -2.205  1.00 49.44           C  
ATOM    685  CD2 LEU A  96      27.832  20.387  -2.197  1.00 48.57           C  
ATOM    686  N   ALA A  97      26.710  24.656  -4.513  1.00 53.44           N  
ATOM    687  CA  ALA A  97      26.887  25.990  -3.924  1.00 55.09           C  
ATOM    688  C   ALA A  97      25.619  26.838  -4.037  1.00 53.99           C  
ATOM    689  O   ALA A  97      25.278  27.579  -3.116  1.00 54.65           O  
ATOM    690  CB  ALA A  97      28.074  26.712  -4.551  1.00 54.72           C  
ATOM    691  N   ILE A  98      24.921  26.715  -5.163  1.00 54.02           N  
ATOM    692  CA  ILE A  98      23.639  27.392  -5.353  1.00 54.72           C  
ATOM    693  C   ILE A  98      22.633  26.957  -4.280  1.00 55.09           C  
ATOM    694  O   ILE A  98      21.986  27.799  -3.658  1.00 55.80           O  
ATOM    695  CB  ILE A  98      23.087  27.185  -6.785  1.00 53.78           C  
ATOM    696  CG1 ILE A  98      24.047  27.814  -7.803  1.00 52.33           C  
ATOM    697  CG2 ILE A  98      21.685  27.790  -6.926  1.00 53.05           C  
ATOM    698  CD1 ILE A  98      23.867  27.327  -9.230  1.00 52.81           C  
ATOM    699  N   ALA A  99      22.543  25.650  -4.043  1.00 56.48           N  
ATOM    700  CA  ALA A  99      21.637  25.091  -3.037  1.00 56.83           C  
ATOM    701  C   ALA A  99      21.945  25.532  -1.601  1.00 58.48           C  
ATOM    702  O   ALA A  99      21.025  25.840  -0.843  1.00 59.67           O  
ATOM    703  CB  ALA A  99      21.606  23.577  -3.133  1.00 56.05           C  
ATOM    704  N   ILE A 100      23.225  25.558  -1.230  1.00 60.26           N  
ATOM    705  CA  ILE A 100      23.640  26.006   0.108  1.00 60.26           C  
ATOM    706  C   ILE A 100      23.335  27.496   0.294  1.00 62.82           C  
ATOM    707  O   ILE A 100      22.914  27.932   1.375  1.00 61.73           O  
ATOM    708  CB  ILE A 100      25.138  25.710   0.372  1.00 61.58           C  
ATOM    709  CG1 ILE A 100      25.371  24.198   0.488  1.00 61.35           C  
ATOM    710  CG2 ILE A 100      25.619  26.408   1.644  1.00 63.80           C  
ATOM    711  CD1 ILE A 100      26.844  23.780   0.466  1.00 60.58           C  
ATOM    712  N   ASP A 101      23.539  28.262  -0.777  1.00 63.85           N  
ATOM    713  CA  ASP A 101      23.214  29.684  -0.813  1.00 65.58           C  
ATOM    714  C   ASP A 101      21.725  29.934  -0.546  1.00 66.45           C  
ATOM    715  O   ASP A 101      21.373  30.736   0.321  1.00 66.88           O  
ATOM    716  CB  ASP A 101      23.621  30.278  -2.161  1.00 65.83           C  
ATOM    717  CG  ASP A 101      23.258  31.740  -2.285  1.00 69.20           C  
ATOM    718  OD1 ASP A 101      23.831  32.559  -1.537  1.00 69.51           O  
ATOM    719  OD2 ASP A 101      22.400  32.069  -3.133  1.00 71.68           O1-
ATOM    720  N   ARG A 102      20.866  29.238  -1.292  1.00 66.98           N  
ATOM    721  CA  ARG A 102      19.413  29.332  -1.121  1.00 68.04           C  
ATOM    722  C   ARG A 102      18.964  28.846   0.254  1.00 70.55           C  
ATOM    723  O   ARG A 102      17.973  29.331   0.789  1.00 72.61           O  
ATOM    724  CB  ARG A 102      18.672  28.554  -2.217  1.00 65.03           C  
ATOM    725  CG  ARG A 102      18.902  29.054  -3.648  1.00 68.79           C  
ATOM    726  CD  ARG A 102      18.302  30.429  -3.898  1.00 68.32           C  
ATOM    727  NE  ARG A 102      19.146  31.507  -3.388  1.00 70.11           N  
ATOM    728  CZ  ARG A 102      18.687  32.652  -2.890  1.00 70.70           C  
ATOM    729  NH1 ARG A 102      17.382  32.882  -2.818  1.00 71.64           N  
ATOM    730  NH2 ARG A 102      19.538  33.567  -2.452  1.00 71.29           N  
ATOM    731  N   TYR A 103      19.699  27.888   0.813  1.00 72.04           N  
ATOM    732  CA  TYR A 103      19.444  27.396   2.157  1.00 75.18           C  
ATOM    733  C   TYR A 103      19.616  28.518   3.183  1.00 78.48           C  
ATOM    734  O   TYR A 103      18.702  28.798   3.958  1.00 80.67           O  
ATOM    735  CB  TYR A 103      20.366  26.218   2.472  1.00 76.54           C  
ATOM    736  CG  TYR A 103      20.161  25.611   3.838  1.00 80.24           C  
ATOM    737  CD1 TYR A 103      18.983  24.937   4.152  1.00 81.30           C  
ATOM    738  CD2 TYR A 103      21.146  25.708   4.820  1.00 82.70           C  
ATOM    739  CE1 TYR A 103      18.788  24.374   5.409  1.00 84.55           C  
ATOM    740  CE2 TYR A 103      20.962  25.144   6.082  1.00 85.56           C  
ATOM    741  CZ  TYR A 103      19.778  24.481   6.367  1.00 85.61           C  
ATOM    742  OH  TYR A 103      19.579  23.921   7.607  1.00 91.87           O  
ATOM    743  N   ILE A 104      20.780  29.166   3.162  1.00 80.35           N  
ATOM    744  CA  ILE A 104      21.079  30.288   4.055  1.00 78.54           C  
ATOM    745  C   ILE A 104      20.084  31.433   3.848  1.00 80.07           C  
ATOM    746  O   ILE A 104      19.586  32.011   4.816  1.00 80.30           O  
ATOM    747  CB  ILE A 104      22.536  30.795   3.866  1.00 77.22           C  
ATOM    748  CG1 ILE A 104      23.534  29.653   4.078  1.00 75.18           C  
ATOM    749  CG2 ILE A 104      22.848  31.953   4.822  1.00 77.08           C  
ATOM    750  CD1 ILE A 104      24.853  29.840   3.357  1.00 74.67           C  
ATOM    751  N   ALA A 105      19.786  31.735   2.586  1.00 80.12           N  
ATOM    752  CA  ALA A 105      18.882  32.831   2.230  1.00 82.16           C  
ATOM    753  C   ALA A 105      17.474  32.671   2.801  1.00 87.83           C  
ATOM    754  O   ALA A 105      16.860  33.653   3.224  1.00 94.37           O  
ATOM    755  CB  ALA A 105      18.822  33.003   0.723  1.00 76.25           C  
ATOM    756  N   ILE A 106      16.969  31.439   2.807  1.00 91.01           N  
ATOM    757  CA  ILE A 106      15.612  31.160   3.276  1.00 92.57           C  
ATOM    758  C   ILE A 106      15.562  30.946   4.790  1.00 96.59           C  
ATOM    759  O   ILE A 106      14.643  31.428   5.454  1.00100.70           O  
ATOM    760  CB  ILE A 106      14.949  29.981   2.485  1.00 92.11           C  
ATOM    761  CG1 ILE A 106      14.198  30.504   1.252  1.00 90.65           C  
ATOM    762  CG2 ILE A 106      13.974  29.183   3.355  1.00 91.22           C  
ATOM    763  CD1 ILE A 106      15.064  30.772   0.027  1.00 86.80           C  
ATOM    764  N   ARG A 107      16.557  30.250   5.334  1.00 98.81           N  
ATOM    765  CA  ARG A 107      16.568  29.940   6.763  1.00103.95           C  
ATOM    766  C   ARG A 107      17.042  31.096   7.644  1.00107.85           C  
ATOM    767  O   ARG A 107      16.446  31.361   8.689  1.00110.22           O  
ATOM    768  CB  ARG A 107      17.368  28.663   7.051  1.00107.94           C  
ATOM    769  CG  ARG A 107      16.821  27.397   6.369  1.00113.47           C  
ATOM    770  CD  ARG A 107      15.389  27.042   6.799  1.00116.50           C  
ATOM    771  NE  ARG A 107      15.326  26.491   8.153  1.00118.83           N  
ATOM    772  CZ  ARG A 107      14.288  25.826   8.656  1.00116.67           C  
ATOM    773  NH1 ARG A 107      13.202  25.610   7.923  1.00114.83           N  
ATOM    774  NH2 ARG A 107      14.339  25.369   9.900  1.00116.76           N  
ATOM    775  N   ILE A 108      18.102  31.786   7.220  1.00109.43           N  
ATOM    776  CA  ILE A 108      18.621  32.955   7.947  1.00105.19           C  
ATOM    777  C   ILE A 108      18.603  34.193   7.035  1.00103.59           C  
ATOM    778  O   ILE A 108      19.657  34.639   6.569  1.00107.35           O  
ATOM    779  CB  ILE A 108      20.060  32.711   8.490  1.00106.85           C  
ATOM    780  CG1 ILE A 108      20.207  31.288   9.047  1.00110.42           C  
ATOM    781  CG2 ILE A 108      20.424  33.756   9.550  1.00105.33           C  
ATOM    782  CD1 ILE A 108      21.616  30.719   8.947  1.00110.42           C  
ATOM    783  N   PRO A 109      17.403  34.756   6.778  1.00101.20           N  
ATOM    784  CA  PRO A 109      17.279  35.819   5.777  1.00100.23           C  
ATOM    785  C   PRO A 109      17.830  37.160   6.250  1.00100.91           C  
ATOM    786  O   PRO A 109      18.153  38.018   5.424  1.00100.96           O  
ATOM    787  CB  PRO A 109      15.761  35.920   5.547  1.00 98.27           C  
ATOM    788  CG  PRO A 109      15.140  34.801   6.347  1.00 95.82           C  
ATOM    789  CD  PRO A 109      16.111  34.488   7.430  1.00 99.28           C  
ATOM    790  N   LEU A 110      17.939  37.328   7.566  1.00102.00           N  
ATOM    791  CA  LEU A 110      18.435  38.565   8.165  1.00103.80           C  
ATOM    792  C   LEU A 110      19.930  38.777   7.908  1.00104.00           C  
ATOM    793  O   LEU A 110      20.317  39.741   7.244  1.00104.78           O  
ATOM    794  CB  LEU A 110      18.134  38.593   9.672  1.00107.93           C  
ATOM    795  CG  LEU A 110      16.675  38.698  10.140  1.00107.46           C  
ATOM    796  CD1 LEU A 110      16.543  38.289  11.602  1.00103.12           C  
ATOM    797  CD2 LEU A 110      16.108  40.101   9.920  1.00105.30           C  
ATOM    798  N   ARG A 111      20.760  37.868   8.420  1.00104.57           N  
ATOM    799  CA  ARG A 111      22.218  37.995   8.304  1.00102.98           C  
ATOM    800  C   ARG A 111      22.800  37.588   6.948  1.00 97.21           C  
ATOM    801  O   ARG A 111      23.981  37.826   6.688  1.00 96.80           O  
ATOM    802  CB  ARG A 111      22.930  37.246   9.438  1.00106.19           C  
ATOM    803  CG  ARG A 111      23.364  38.152  10.583  1.00113.08           C  
ATOM    804  CD  ARG A 111      24.423  37.493  11.459  1.00115.34           C  
ATOM    805  NE  ARG A 111      23.846  36.535  12.402  1.00115.30           N  
ATOM    806  CZ  ARG A 111      23.431  36.840  13.629  1.00116.50           C  
ATOM    807  NH1 ARG A 111      23.519  38.085  14.082  1.00117.09           N  
ATOM    808  NH2 ARG A 111      22.923  35.894  14.407  1.00117.58           N  
ATOM    809  N   TYR A 112      21.971  36.993   6.090  1.00 90.20           N  
ATOM    810  CA  TYR A 112      22.402  36.545   4.763  1.00 89.37           C  
ATOM    811  C   TYR A 112      23.275  37.557   4.018  1.00 90.48           C  
ATOM    812  O   TYR A 112      24.299  37.189   3.441  1.00 95.29           O  
ATOM    813  CB  TYR A 112      21.197  36.166   3.891  1.00 85.12           C  
ATOM    814  CG  TYR A 112      21.565  35.845   2.455  1.00 81.89           C  
ATOM    815  CD1 TYR A 112      22.017  34.573   2.100  1.00 82.61           C  
ATOM    816  CD2 TYR A 112      21.475  36.815   1.455  1.00 80.33           C  
ATOM    817  CE1 TYR A 112      22.359  34.271   0.786  1.00 79.31           C  
ATOM    818  CE2 TYR A 112      21.821  36.524   0.138  1.00 79.11           C  
ATOM    819  CZ  TYR A 112      22.261  35.249  -0.187  1.00 79.18           C  
ATOM    820  OH  TYR A 112      22.602  34.949  -1.483  1.00 78.51           O  
ATOM    821  N   ASN A 113      22.861  38.821   4.027  1.00 89.98           N  
ATOM    822  CA  ASN A 113      23.551  39.870   3.275  1.00 90.11           C  
ATOM    823  C   ASN A 113      24.889  40.276   3.890  1.00 89.53           C  
ATOM    824  O   ASN A 113      25.771  40.783   3.193  1.00 86.53           O  
ATOM    825  CB  ASN A 113      22.633  41.079   3.079  1.00 90.13           C  
ATOM    826  CG  ASN A 113      21.398  40.740   2.257  1.00 93.26           C  
ATOM    827  OD1 ASN A 113      20.309  40.554   2.800  1.00 94.09           O  
ATOM    828  ND2 ASN A 113      21.570  40.634   0.944  1.00 94.13           N  
ATOM    829  N   GLY A 114      25.031  40.041   5.193  1.00 89.55           N  
ATOM    830  CA  GLY A 114      26.290  40.270   5.899  1.00 89.36           C  
ATOM    831  C   GLY A 114      27.197  39.050   5.893  1.00 89.35           C  
ATOM    832  O   GLY A 114      28.420  39.181   5.956  1.00 91.15           O  
ATOM    833  N   LEU A 115      26.594  37.863   5.815  1.00 87.22           N  
ATOM    834  CA  LEU A 115      27.330  36.598   5.806  1.00 83.79           C  
ATOM    835  C   LEU A 115      27.828  36.208   4.408  1.00 80.17           C  
ATOM    836  O   LEU A 115      29.014  35.934   4.223  1.00 80.34           O  
ATOM    837  CB  LEU A 115      26.470  35.472   6.393  1.00 83.87           C  
ATOM    838  CG  LEU A 115      27.210  34.245   6.933  1.00 84.84           C  
ATOM    839  CD1 LEU A 115      27.766  34.512   8.331  1.00 84.84           C  
ATOM    840  CD2 LEU A 115      26.288  33.043   6.951  1.00 84.03           C  
ATOM    841  N   VAL A 116      26.923  36.182   3.434  1.00 75.89           N  
ATOM    842  CA  VAL A 116      27.272  35.789   2.069  1.00 74.56           C  
ATOM    843  C   VAL A 116      27.696  37.005   1.240  1.00 75.50           C  
ATOM    844  O   VAL A 116      26.908  37.556   0.465  1.00 74.56           O  
ATOM    845  CB  VAL A 116      26.122  35.001   1.378  1.00 72.04           C  
ATOM    846  CG1 VAL A 116      26.545  34.515  -0.009  1.00 69.15           C  
ATOM    847  CG2 VAL A 116      25.693  33.821   2.238  1.00 69.08           C  
ATOM    848  N   THR A 117      28.952  37.414   1.419  1.00 77.28           N  
ATOM    849  CA  THR A 117      29.524  38.554   0.696  1.00 76.61           C  
ATOM    850  C   THR A 117      30.190  38.112  -0.607  1.00 77.83           C  
ATOM    851  O   THR A 117      30.387  36.918  -0.834  1.00 82.90           O  
ATOM    852  CB  THR A 117      30.562  39.306   1.552  1.00 75.68           C  
ATOM    853  OG1 THR A 117      31.719  38.482   1.736  1.00 77.33           O  
ATOM    854  CG2 THR A 117      29.982  39.679   2.912  1.00 76.60           C  
ATOM    855  N   GLY A 118      30.543  39.082  -1.450  1.00 77.78           N  
ATOM    856  CA  GLY A 118      31.215  38.817  -2.723  1.00 76.67           C  
ATOM    857  C   GLY A 118      32.557  38.121  -2.579  1.00 78.69           C  
ATOM    858  O   GLY A 118      32.933  37.306  -3.424  1.00 84.42           O  
ATOM    859  N   THR A 119      33.278  38.445  -1.508  1.00 75.44           N  
ATOM    860  CA  THR A 119      34.577  37.836  -1.215  1.00 76.72           C  
ATOM    861  C   THR A 119      34.427  36.393  -0.718  1.00 76.27           C  
ATOM    862  O   THR A 119      35.149  35.499  -1.165  1.00 73.17           O  
ATOM    863  CB  THR A 119      35.394  38.711  -0.223  1.00 78.58           C  
ATOM    864  OG1 THR A 119      36.090  39.723  -0.958  1.00 78.92           O  
ATOM    865  CG2 THR A 119      36.411  37.891   0.568  1.00 78.46           C  
ATOM    866  N   ARG A 120      33.480  36.175   0.193  1.00 75.55           N  
ATOM    867  CA  ARG A 120      33.175  34.835   0.689  1.00 71.50           C  
ATOM    868  C   ARG A 120      32.613  33.912  -0.392  1.00 69.13           C  
ATOM    869  O   ARG A 120      32.849  32.708  -0.357  1.00 65.76           O  
ATOM    870  CB  ARG A 120      32.248  34.901   1.904  1.00 71.98           C  
ATOM    871  CG  ARG A 120      33.008  34.821   3.215  1.00 75.24           C  
ATOM    872  CD  ARG A 120      32.144  35.059   4.431  1.00 75.80           C  
ATOM    873  NE  ARG A 120      32.294  36.421   4.935  1.00 81.55           N  
ATOM    874  CZ  ARG A 120      32.073  36.789   6.195  1.00 84.02           C  
ATOM    875  NH1 ARG A 120      31.693  35.897   7.104  1.00 85.35           N  
ATOM    876  NH2 ARG A 120      32.242  38.054   6.551  1.00 84.13           N  
ATOM    877  N   ALA A 121      31.891  34.484  -1.355  1.00 70.05           N  
ATOM    878  CA  ALA A 121      31.373  33.728  -2.500  1.00 69.33           C  
ATOM    879  C   ALA A 121      32.500  33.179  -3.374  1.00 67.01           C  
ATOM    880  O   ALA A 121      32.385  32.087  -3.926  1.00 65.06           O  
ATOM    881  CB  ALA A 121      30.424  34.585  -3.331  1.00 68.56           C  
ATOM    882  N   LYS A 122      33.584  33.941  -3.494  1.00 69.47           N  
ATOM    883  CA  LYS A 122      34.759  33.505  -4.259  1.00 69.11           C  
ATOM    884  C   LYS A 122      35.552  32.447  -3.490  1.00 65.01           C  
ATOM    885  O   LYS A 122      36.160  31.560  -4.090  1.00 61.20           O  
ATOM    886  CB  LYS A 122      35.651  34.694  -4.609  1.00 71.60           C  
ATOM    887  CG  LYS A 122      35.059  35.634  -5.643  1.00 74.52           C  
ATOM    888  CD  LYS A 122      35.875  36.901  -5.736  1.00 75.23           C  
ATOM    889  CE  LYS A 122      35.215  37.911  -6.642  1.00 78.75           C  
ATOM    890  NZ  LYS A 122      35.617  39.289  -6.258  1.00 81.44           N  
ATOM    891  N   GLY A 123      35.534  32.553  -2.162  1.00 62.01           N  
ATOM    892  CA  GLY A 123      36.048  31.506  -1.291  1.00 62.37           C  
ATOM    893  C   GLY A 123      35.387  30.176  -1.615  1.00 63.87           C  
ATOM    894  O   GLY A 123      36.074  29.195  -1.916  1.00 65.07           O  
ATOM    895  N   ILE A 124      34.052  30.156  -1.578  1.00 62.06           N  
ATOM    896  CA  ILE A 124      33.271  28.955  -1.882  1.00 59.07           C  
ATOM    897  C   ILE A 124      33.563  28.422  -3.289  1.00 57.44           C  
ATOM    898  O   ILE A 124      33.756  27.216  -3.466  1.00 56.39           O  
ATOM    899  CB  ILE A 124      31.743  29.169  -1.648  1.00 58.28           C  
ATOM    900  CG1 ILE A 124      31.385  28.947  -0.179  1.00 59.52           C  
ATOM    901  CG2 ILE A 124      30.919  28.187  -2.454  1.00 58.65           C  
ATOM    902  CD1 ILE A 124      31.432  30.186   0.679  1.00 60.82           C  
ATOM    903  N   ILE A 125      33.611  29.319  -4.274  1.00 55.89           N  
ATOM    904  CA  ILE A 125      33.943  28.941  -5.653  1.00 55.26           C  
ATOM    905  C   ILE A 125      35.286  28.202  -5.732  1.00 55.98           C  
ATOM    906  O   ILE A 125      35.377  27.144  -6.363  1.00 56.10           O  
ATOM    907  CB  ILE A 125      33.970  30.170  -6.593  1.00 57.12           C  
ATOM    908  CG1 ILE A 125      32.575  30.796  -6.696  1.00 59.74           C  
ATOM    909  CG2 ILE A 125      34.521  29.796  -7.989  1.00 55.96           C  
ATOM    910  CD1 ILE A 125      32.565  32.227  -7.246  1.00 60.29           C  
ATOM    911  N   ALA A 126      36.314  28.769  -5.092  1.00 53.86           N  
ATOM    912  CA  ALA A 126      37.654  28.176  -5.055  1.00 53.44           C  
ATOM    913  C   ALA A 126      37.646  26.782  -4.415  1.00 53.71           C  
ATOM    914  O   ALA A 126      38.230  25.842  -4.962  1.00 55.03           O  
ATOM    915  CB  ALA A 126      38.629  29.098  -4.330  1.00 51.78           C  
ATOM    916  N   ILE A 127      36.970  26.662  -3.272  1.00 50.20           N  
ATOM    917  CA  ILE A 127      36.742  25.379  -2.615  1.00 51.30           C  
ATOM    918  C   ILE A 127      36.128  24.342  -3.575  1.00 53.26           C  
ATOM    919  O   ILE A 127      36.560  23.187  -3.592  1.00 56.84           O  
ATOM    920  CB  ILE A 127      35.886  25.544  -1.324  1.00 49.77           C  
ATOM    921  CG1 ILE A 127      36.701  26.265  -0.244  1.00 49.79           C  
ATOM    922  CG2 ILE A 127      35.399  24.196  -0.809  1.00 47.50           C  
ATOM    923  CD1 ILE A 127      35.883  26.920   0.875  1.00 48.76           C  
ATOM    924  N   CYS A 128      35.152  24.756  -4.383  1.00 51.62           N  
ATOM    925  CA  CYS A 128      34.540  23.858  -5.374  1.00 54.72           C  
ATOM    926  C   CYS A 128      35.569  23.271  -6.329  1.00 54.92           C  
ATOM    927  O   CYS A 128      35.496  22.091  -6.690  1.00 54.16           O  
ATOM    928  CB  CYS A 128      33.446  24.572  -6.179  1.00 53.84           C  
ATOM    929  SG  CYS A 128      31.900  24.794  -5.284  1.00 57.20           S  
ATOM    930  N   TRP A 129      36.526  24.104  -6.725  1.00 55.85           N  
ATOM    931  CA  TRP A 129      37.570  23.693  -7.651  1.00 58.35           C  
ATOM    932  C   TRP A 129      38.712  22.919  -6.999  1.00 58.23           C  
ATOM    933  O   TRP A 129      39.315  22.064  -7.641  1.00 60.47           O  
ATOM    934  CB  TRP A 129      38.096  24.893  -8.424  1.00 58.26           C  
ATOM    935  CG  TRP A 129      37.213  25.237  -9.575  1.00 55.85           C  
ATOM    936  CD1 TRP A 129      36.235  26.191  -9.607  1.00 55.57           C  
ATOM    937  CD2 TRP A 129      37.210  24.614 -10.862  1.00 56.79           C  
ATOM    938  NE1 TRP A 129      35.632  26.209 -10.842  1.00 54.52           N  
ATOM    939  CE2 TRP A 129      36.210  25.252 -11.632  1.00 54.44           C  
ATOM    940  CE3 TRP A 129      37.961  23.581 -11.445  1.00 57.42           C  
ATOM    941  CZ2 TRP A 129      35.943  24.895 -12.954  1.00 54.91           C  
ATOM    942  CZ3 TRP A 129      37.691  23.223 -12.763  1.00 57.36           C  
ATOM    943  CH2 TRP A 129      36.690  23.884 -13.503  1.00 56.82           C  
ATOM    944  N   VAL A 130      39.005  23.211  -5.736  1.00 57.22           N  
ATOM    945  CA  VAL A 130      40.012  22.445  -5.001  1.00 57.58           C  
ATOM    946  C   VAL A 130      39.533  20.999  -4.851  1.00 58.07           C  
ATOM    947  O   VAL A 130      40.268  20.065  -5.185  1.00 59.55           O  
ATOM    948  CB  VAL A 130      40.347  23.076  -3.624  1.00 58.29           C  
ATOM    949  CG1 VAL A 130      41.123  22.093  -2.734  1.00 55.99           C  
ATOM    950  CG2 VAL A 130      41.129  24.373  -3.807  1.00 55.20           C  
ATOM    951  N   LEU A 131      38.296  20.831  -4.381  1.00 54.71           N  
ATOM    952  CA  LEU A 131      37.684  19.513  -4.237  1.00 54.26           C  
ATOM    953  C   LEU A 131      37.596  18.746  -5.562  1.00 55.44           C  
ATOM    954  O   LEU A 131      37.730  17.527  -5.582  1.00 55.52           O  
ATOM    955  CB  LEU A 131      36.295  19.623  -3.597  1.00 56.48           C  
ATOM    956  CG  LEU A 131      36.110  19.589  -2.066  1.00 60.02           C  
ATOM    957  CD1 LEU A 131      36.551  18.250  -1.476  1.00 59.23           C  
ATOM    958  CD2 LEU A 131      36.810  20.733  -1.336  1.00 60.16           C  
ATOM    959  N   SER A 132      37.380  19.460  -6.664  1.00 55.90           N  
ATOM    960  CA  SER A 132      37.288  18.832  -7.981  1.00 55.70           C  
ATOM    961  C   SER A 132      38.615  18.230  -8.429  1.00 54.17           C  
ATOM    962  O   SER A 132      38.644  17.104  -8.921  1.00 52.60           O  
ATOM    963  CB  SER A 132      36.775  19.826  -9.024  1.00 60.39           C  
ATOM    964  OG  SER A 132      35.500  20.313  -8.649  1.00 64.38           O  
ATOM    965  N   PHE A 133      39.703  18.984  -8.251  1.00 55.36           N  
ATOM    966  CA  PHE A 133      41.051  18.529  -8.605  1.00 55.00           C  
ATOM    967  C   PHE A 133      41.506  17.386  -7.706  1.00 54.04           C  
ATOM    968  O   PHE A 133      41.934  16.343  -8.191  1.00 52.84           O  
ATOM    969  CB  PHE A 133      42.062  19.687  -8.554  1.00 57.99           C  
ATOM    970  CG  PHE A 133      42.077  20.547  -9.798  1.00 60.22           C  
ATOM    971  CD1 PHE A 133      42.614  20.066 -10.990  1.00 62.24           C  
ATOM    972  CD2 PHE A 133      41.554  21.837  -9.777  1.00 60.55           C  
ATOM    973  CE1 PHE A 133      42.625  20.860 -12.147  1.00 62.96           C  
ATOM    974  CE2 PHE A 133      41.563  22.641 -10.928  1.00 61.45           C  
ATOM    975  CZ  PHE A 133      42.099  22.149 -12.112  1.00 62.27           C  
ATOM    976  N   ALA A 134      41.391  17.581  -6.394  1.00 55.65           N  
ATOM    977  CA  ALA A 134      41.778  16.566  -5.421  1.00 54.42           C  
ATOM    978  C   ALA A 134      41.131  15.206  -5.707  1.00 56.43           C  
ATOM    979  O   ALA A 134      41.775  14.166  -5.553  1.00 57.52           O  
ATOM    980  CB  ALA A 134      41.441  17.027  -4.023  1.00 54.27           C  
ATOM    981  N   ILE A 135      39.868  15.220  -6.132  1.00 53.45           N  
ATOM    982  CA  ILE A 135      39.102  13.990  -6.316  1.00 51.99           C  
ATOM    983  C   ILE A 135      39.312  13.380  -7.704  1.00 51.78           C  
ATOM    984  O   ILE A 135      39.559  12.181  -7.833  1.00 50.26           O  
ATOM    985  CB  ILE A 135      37.592  14.212  -6.014  1.00 53.15           C  
ATOM    986  CG1 ILE A 135      37.398  14.471  -4.514  1.00 54.29           C  
ATOM    987  CG2 ILE A 135      36.747  13.004  -6.466  1.00 52.07           C  
ATOM    988  CD1 ILE A 135      36.092  15.155  -4.142  1.00 54.54           C  
ATOM    989  N   GLY A 136      39.217  14.213  -8.734  1.00 49.84           N  
ATOM    990  CA  GLY A 136      39.348  13.754 -10.102  1.00 47.57           C  
ATOM    991  C   GLY A 136      40.764  13.399 -10.491  1.00 48.95           C  
ATOM    992  O   GLY A 136      40.961  12.625 -11.426  1.00 53.70           O  
ATOM    993  N   LEU A 137      41.746  13.965  -9.790  1.00 47.56           N  
ATOM    994  CA  LEU A 137      43.157  13.650 -10.037  1.00 51.00           C  
ATOM    995  C   LEU A 137      43.704  12.540  -9.133  1.00 53.64           C  
ATOM    996  O   LEU A 137      44.849  12.111  -9.314  1.00 52.85           O  
ATOM    997  CB  LEU A 137      44.053  14.893  -9.902  1.00 49.45           C  
ATOM    998  CG  LEU A 137      43.971  16.038 -10.918  1.00 50.80           C  
ATOM    999  CD1 LEU A 137      45.025  17.089 -10.576  1.00 50.78           C  
ATOM   1000  CD2 LEU A 137      44.128  15.561 -12.366  1.00 49.41           C  
ATOM   1001  N   THR A 138      42.902  12.092  -8.163  1.00 51.99           N  
ATOM   1002  CA  THR A 138      43.310  11.021  -7.244  1.00 53.85           C  
ATOM   1003  C   THR A 138      43.908   9.799  -7.970  1.00 56.32           C  
ATOM   1004  O   THR A 138      44.934   9.271  -7.525  1.00 55.30           O  
ATOM   1005  CB  THR A 138      42.164  10.618  -6.258  1.00 54.93           C  
ATOM   1006  OG1 THR A 138      42.084  11.584  -5.207  1.00 55.00           O  
ATOM   1007  CG2 THR A 138      42.404   9.251  -5.624  1.00 54.81           C  
ATOM   1008  N   PRO A 139      43.293   9.363  -9.098  1.00 57.37           N  
ATOM   1009  CA  PRO A 139      43.887   8.254  -9.853  1.00 59.37           C  
ATOM   1010  C   PRO A 139      45.309   8.501 -10.372  1.00 61.42           C  
ATOM   1011  O   PRO A 139      46.045   7.544 -10.601  1.00 66.31           O  
ATOM   1012  CB  PRO A 139      42.911   8.069 -11.019  1.00 56.41           C  
ATOM   1013  CG  PRO A 139      41.612   8.531 -10.472  1.00 55.76           C  
ATOM   1014  CD  PRO A 139      41.971   9.726  -9.648  1.00 55.18           C  
ATOM   1015  N   MET A 140      45.690   9.764 -10.549  1.00 64.78           N  
ATOM   1016  CA  MET A 140      47.047  10.120 -10.980  1.00 68.52           C  
ATOM   1017  C   MET A 140      48.115   9.693  -9.977  1.00 69.02           C  
ATOM   1018  O   MET A 140      49.229   9.350 -10.361  1.00 70.39           O  
ATOM   1019  CB  MET A 140      47.162  11.627 -11.204  1.00 71.65           C  
ATOM   1020  CG  MET A 140      46.335  12.177 -12.351  1.00 76.78           C  
ATOM   1021  SD  MET A 140      46.998  11.709 -13.955  1.00 84.77           S  
ATOM   1022  CE  MET A 140      45.882  10.408 -14.385  1.00 79.10           C  
ATOM   1023  N   LEU A 141      47.758   9.716  -8.696  1.00 70.85           N  
ATOM   1024  CA  LEU A 141      48.683   9.416  -7.603  1.00 71.40           C  
ATOM   1025  C   LEU A 141      49.059   7.939  -7.496  1.00 70.60           C  
ATOM   1026  O   LEU A 141      49.931   7.580  -6.704  1.00 74.68           O  
ATOM   1027  CB  LEU A 141      48.100   9.885  -6.261  1.00 72.17           C  
ATOM   1028  CG  LEU A 141      47.638  11.336  -6.108  1.00 74.38           C  
ATOM   1029  CD1 LEU A 141      46.965  11.524  -4.753  1.00 75.26           C  
ATOM   1030  CD2 LEU A 141      48.789  12.323  -6.292  1.00 73.15           C  
ATOM   1031  N   GLY A 142      48.400   7.084  -8.270  1.00 67.49           N  
ATOM   1032  CA  GLY A 142      48.711   5.660  -8.245  1.00 64.86           C  
ATOM   1033  C   GLY A 142      47.504   4.748  -8.202  1.00 63.62           C  
ATOM   1034  O   GLY A 142      47.613   3.564  -8.529  1.00 64.11           O  
ATOM   1035  N   TRP A 143      46.356   5.288  -7.793  1.00 59.99           N  
ATOM   1036  CA  TRP A 143      45.111   4.522  -7.774  1.00 58.52           C  
ATOM   1037  C   TRP A 143      44.545   4.374  -9.201  1.00 60.81           C  
ATOM   1038  O   TRP A 143      43.541   5.000  -9.564  1.00 59.74           O  
ATOM   1039  CB  TRP A 143      44.090   5.172  -6.834  1.00 53.99           C  
ATOM   1040  CG  TRP A 143      42.991   4.242  -6.390  1.00 52.27           C  
ATOM   1041  CD1 TRP A 143      42.792   2.954  -6.796  1.00 51.20           C  
ATOM   1042  CD2 TRP A 143      41.926   4.542  -5.477  1.00 50.42           C  
ATOM   1043  NE1 TRP A 143      41.684   2.427  -6.183  1.00 50.03           N  
ATOM   1044  CE2 TRP A 143      41.130   3.379  -5.370  1.00 50.90           C  
ATOM   1045  CE3 TRP A 143      41.571   5.675  -4.731  1.00 49.41           C  
ATOM   1046  CZ2 TRP A 143      39.998   3.316  -4.543  1.00 50.83           C  
ATOM   1047  CZ3 TRP A 143      40.445   5.614  -3.910  1.00 47.14           C  
ATOM   1048  CH2 TRP A 143      39.672   4.444  -3.825  1.00 49.06           C  
ATOM   1049  N   ASN A 144      45.207   3.546 -10.008  1.00 61.16           N  
ATOM   1050  CA  ASN A 144      44.820   3.346 -11.406  1.00 61.34           C  
ATOM   1051  C   ASN A 144      45.144   1.941 -11.904  1.00 61.73           C  
ATOM   1052  O   ASN A 144      45.786   1.164 -11.196  1.00 61.67           O  
ATOM   1053  CB  ASN A 144      45.463   4.405 -12.300  1.00 60.75           C  
ATOM   1054  CG  ASN A 144      46.973   4.409 -12.203  1.00 60.69           C  
ATOM   1055  OD1 ASN A 144      47.638   3.542 -12.758  1.00 60.92           O  
ATOM   1056  ND2 ASN A 144      47.522   5.395 -11.503  1.00 60.01           N  
ATOM   1057  N   ASN A 145      44.691   1.621 -13.117  1.00 61.86           N  
ATOM   1058  CA  ASN A 145      44.847   0.278 -13.682  1.00 60.74           C  
ATOM   1059  C   ASN A 145      46.034   0.152 -14.624  1.00 63.09           C  
ATOM   1060  O   ASN A 145      46.202  -0.878 -15.279  1.00 61.12           O  
ATOM   1061  CB  ASN A 145      43.577  -0.149 -14.415  1.00 57.82           C  
ATOM   1062  CG  ASN A 145      42.454  -0.533 -13.480  1.00 58.51           C  
ATOM   1063  OD1 ASN A 145      42.658  -0.743 -12.281  1.00 62.24           O  
ATOM   1064  ND2 ASN A 145      41.250  -0.635 -14.028  1.00 55.48           N  
ATOM   1065  N   CYS A 146      46.860   1.194 -14.678  1.00 67.52           N  
ATOM   1066  CA  CYS A 146      47.971   1.258 -15.632  1.00 72.96           C  
ATOM   1067  C   CYS A 146      49.114   0.280 -15.367  1.00 75.86           C  
ATOM   1068  O   CYS A 146      49.921   0.006 -16.260  1.00 79.35           O  
ATOM   1069  CB  CYS A 146      48.501   2.686 -15.750  1.00 76.33           C  
ATOM   1070  SG  CYS A 146      47.534   3.691 -16.881  1.00 79.49           S  
ATOM   1071  N   GLY A 147      49.176  -0.245 -14.145  1.00 79.31           N  
ATOM   1072  CA  GLY A 147      50.141  -1.280 -13.796  1.00 79.01           C  
ATOM   1073  C   GLY A 147      49.829  -2.596 -14.483  1.00 80.65           C  
ATOM   1074  O   GLY A 147      50.716  -3.429 -14.666  1.00 86.62           O  
ATOM   1075  N   GLN A 148      48.566  -2.775 -14.870  1.00 79.64           N  
ATOM   1076  CA  GLN A 148      48.090  -4.027 -15.461  1.00 78.28           C  
ATOM   1077  C   GLN A 148      47.465  -3.824 -16.850  1.00 74.58           C  
ATOM   1078  O   GLN A 148      46.261  -4.034 -17.021  1.00 68.47           O  
ATOM   1079  CB  GLN A 148      47.084  -4.715 -14.521  1.00 80.69           C  
ATOM   1080  CG  GLN A 148      47.653  -5.152 -13.165  1.00 88.75           C  
ATOM   1081  CD  GLN A 148      47.831  -3.996 -12.183  1.00 93.93           C  
ATOM   1082  OE1 GLN A 148      46.902  -3.220 -11.937  1.00 95.06           O  
ATOM   1083  NE2 GLN A 148      49.029  -3.881 -11.616  1.00 94.18           N  
ATOM   1084  N   PRO A 149      48.286  -3.437 -17.853  1.00 75.79           N  
ATOM   1085  CA  PRO A 149      47.784  -3.171 -19.208  1.00 74.98           C  
ATOM   1086  C   PRO A 149      47.249  -4.431 -19.874  1.00 76.02           C  
ATOM   1087  O   PRO A 149      47.619  -5.540 -19.488  1.00 79.19           O  
ATOM   1088  CB  PRO A 149      49.028  -2.683 -19.967  1.00 74.86           C  
ATOM   1089  CG  PRO A 149      50.082  -2.441 -18.927  1.00 76.55           C  
ATOM   1090  CD  PRO A 149      49.757  -3.363 -17.804  1.00 76.72           C  
ATOM   1091  N   LYS A 150      46.386  -4.259 -20.868  1.00 78.26           N  
ATOM   1092  CA  LYS A 150      45.796  -5.393 -21.573  1.00 79.10           C  
ATOM   1093  C   LYS A 150      46.393  -5.542 -22.968  1.00 80.99           C  
ATOM   1094  O   LYS A 150      46.037  -4.803 -23.888  1.00 76.33           O  
ATOM   1095  CB  LYS A 150      44.272  -5.265 -21.609  1.00 76.15           C  
ATOM   1096  CG  LYS A 150      43.665  -5.312 -20.221  1.00 74.26           C  
ATOM   1097  CD  LYS A 150      42.179  -5.068 -20.222  1.00 72.90           C  
ATOM   1098  CE  LYS A 150      41.657  -5.094 -18.799  1.00 68.44           C  
ATOM   1099  NZ  LYS A 150      40.188  -4.955 -18.761  1.00 68.05           N  
ATOM   1100  N   GLU A 151      47.319  -6.493 -23.096  1.00 85.79           N  
ATOM   1101  CA  GLU A 151      48.058  -6.735 -24.337  1.00 87.87           C  
ATOM   1102  C   GLU A 151      47.201  -7.357 -25.434  1.00 83.76           C  
ATOM   1103  O   GLU A 151      47.329  -6.991 -26.603  1.00 84.03           O  
ATOM   1104  CB  GLU A 151      49.292  -7.609 -24.073  1.00 96.79           C  
ATOM   1105  CG  GLU A 151      50.594  -6.833 -23.869  1.00101.89           C  
ATOM   1106  CD  GLU A 151      50.656  -6.095 -22.541  1.00106.16           C  
ATOM   1107  OE1 GLU A 151      50.183  -6.646 -21.523  1.00112.10           O  
ATOM   1108  OE2 GLU A 151      51.190  -4.965 -22.516  1.00103.73           O  
ATOM   1109  N   GLY A 152      46.337  -8.295 -25.050  1.00 83.53           N  
ATOM   1110  CA  GLY A 152      45.438  -8.974 -25.989  1.00 85.79           C  
ATOM   1111  C   GLY A 152      44.506  -8.024 -26.718  1.00 86.05           C  
ATOM   1112  O   GLY A 152      44.276  -8.168 -27.920  1.00 88.95           O  
ATOM   1113  N   LYS A 153      43.977  -7.050 -25.981  1.00 84.83           N  
ATOM   1114  CA  LYS A 153      43.111  -6.010 -26.532  1.00 82.42           C  
ATOM   1115  C   LYS A 153      43.923  -4.956 -27.294  1.00 83.34           C  
ATOM   1116  O   LYS A 153      43.467  -4.432 -28.316  1.00 82.75           O  
ATOM   1117  CB  LYS A 153      42.276  -5.372 -25.412  1.00 79.34           C  
ATOM   1118  CG  LYS A 153      41.427  -4.173 -25.828  1.00 78.25           C  
ATOM   1119  CD  LYS A 153      40.078  -4.141 -25.119  1.00 77.22           C  
ATOM   1120  CE  LYS A 153      40.214  -4.032 -23.610  1.00 77.89           C  
ATOM   1121  NZ  LYS A 153      38.900  -3.844 -22.943  1.00 76.84           N  
ATOM   1122  N   ALA A 154      45.121  -4.655 -26.792  1.00 81.19           N  
ATOM   1123  CA  ALA A 154      46.027  -3.708 -27.440  1.00 83.34           C  
ATOM   1124  C   ALA A 154      46.489  -4.227 -28.800  1.00 87.55           C  
ATOM   1125  O   ALA A 154      46.655  -3.450 -29.744  1.00 87.66           O  
ATOM   1126  CB  ALA A 154      47.223  -3.415 -26.548  1.00 77.89           C  
ATOM   1127  N   HIS A 155      46.687  -5.542 -28.887  1.00 90.77           N  
ATOM   1128  CA  HIS A 155      47.082  -6.195 -30.130  1.00 94.70           C  
ATOM   1129  C   HIS A 155      45.967  -6.130 -31.173  1.00 96.98           C  
ATOM   1130  O   HIS A 155      46.213  -5.760 -32.323  1.00101.21           O  
ATOM   1131  CB  HIS A 155      47.499  -7.649 -29.875  1.00 96.27           C  
ATOM   1132  CG  HIS A 155      47.978  -8.366 -31.100  1.00 98.63           C  
ATOM   1133  ND1 HIS A 155      49.116  -7.994 -31.785  1.00 98.12           N  
ATOM   1134  CD2 HIS A 155      47.474  -9.436 -31.760  1.00 97.24           C  
ATOM   1135  CE1 HIS A 155      49.291  -8.802 -32.815  1.00 98.14           C  
ATOM   1136  NE2 HIS A 155      48.309  -9.686 -32.822  1.00 97.82           N  
ATOM   1137  N   SER A 156      44.749  -6.480 -30.759  1.00 96.02           N  
ATOM   1138  CA  SER A 156      43.576  -6.458 -31.639  1.00 95.96           C  
ATOM   1139  C   SER A 156      43.327  -5.096 -32.297  1.00 97.92           C  
ATOM   1140  O   SER A 156      42.834  -5.031 -33.423  1.00102.16           O  
ATOM   1141  CB  SER A 156      42.330  -6.912 -30.879  1.00 95.25           C  
ATOM   1142  OG  SER A 156      42.453  -8.262 -30.465  1.00 95.03           O  
ATOM   1143  N   GLN A 157      43.677  -4.019 -31.595  1.00 97.51           N  
ATOM   1144  CA  GLN A 157      43.532  -2.656 -32.116  1.00 95.39           C  
ATOM   1145  C   GLN A 157      44.749  -2.207 -32.930  1.00 96.62           C  
ATOM   1146  O   GLN A 157      44.776  -1.089 -33.452  1.00 97.41           O  
ATOM   1147  CB  GLN A 157      43.269  -1.662 -30.974  1.00 93.53           C  
ATOM   1148  CG  GLN A 157      41.928  -1.838 -30.272  1.00 89.00           C  
ATOM   1149  CD  GLN A 157      40.745  -1.622 -31.193  1.00 87.27           C  
ATOM   1150  OE1 GLN A 157      40.589  -0.550 -31.783  1.00 86.37           O  
ATOM   1151  NE2 GLN A 157      39.895  -2.638 -31.312  1.00 84.37           N  
ATOM   1152  N   GLY A 158      45.748  -3.081 -33.031  1.00 97.32           N  
ATOM   1153  CA  GLY A 158      46.975  -2.789 -33.767  1.00 98.66           C  
ATOM   1154  C   GLY A 158      47.799  -1.667 -33.165  1.00 99.79           C  
ATOM   1155  O   GLY A 158      48.376  -0.858 -33.894  1.00 99.99           O  
ATOM   1156  N   CYS A 159      47.849  -1.614 -31.835  1.00 99.48           N  
ATOM   1157  CA  CYS A 159      48.652  -0.616 -31.131  1.00100.24           C  
ATOM   1158  C   CYS A 159      50.111  -1.050 -31.078  1.00 99.20           C  
ATOM   1159  O   CYS A 159      50.409  -2.233 -30.897  1.00 96.37           O  
ATOM   1160  CB  CYS A 159      48.128  -0.384 -29.706  1.00102.86           C  
ATOM   1161  SG  CYS A 159      46.435   0.292 -29.550  1.00108.74           S  
ATOM   1162  N   GLY A 160      51.014  -0.086 -31.235  1.00 99.79           N  
ATOM   1163  CA  GLY A 160      52.449  -0.338 -31.118  1.00101.31           C  
ATOM   1164  C   GLY A 160      52.826  -0.714 -29.699  1.00104.23           C  
ATOM   1165  O   GLY A 160      52.035  -0.528 -28.772  1.00107.04           O  
ATOM   1166  N   GLU A 161      54.034  -1.246 -29.527  1.00105.51           N  
ATOM   1167  CA  GLU A 161      54.495  -1.690 -28.210  1.00106.67           C  
ATOM   1168  C   GLU A 161      54.561  -0.536 -27.212  1.00104.60           C  
ATOM   1169  O   GLU A 161      55.032   0.556 -27.541  1.00106.34           O  
ATOM   1170  CB  GLU A 161      55.837  -2.430 -28.304  1.00110.14           C  
ATOM   1171  CG  GLU A 161      56.950  -1.681 -29.036  1.00113.74           C  
ATOM   1172  CD  GLU A 161      58.132  -2.571 -29.400  1.00115.65           C  
ATOM   1173  OE1 GLU A 161      58.285  -3.660 -28.800  1.00112.62           O  
ATOM   1174  OE2 GLU A 161      58.912  -2.176 -30.292  1.00117.35           O  
ATOM   1175  N   GLY A 162      54.067  -0.784 -26.002  1.00 98.73           N  
ATOM   1176  CA  GLY A 162      53.979   0.249 -24.972  1.00 97.08           C  
ATOM   1177  C   GLY A 162      52.750   1.131 -25.118  1.00 94.26           C  
ATOM   1178  O   GLY A 162      52.714   2.249 -24.598  1.00 95.25           O  
ATOM   1179  N   GLN A 163      51.747   0.630 -25.836  1.00 90.28           N  
ATOM   1180  CA  GLN A 163      50.481   1.338 -26.011  1.00 88.04           C  
ATOM   1181  C   GLN A 163      49.293   0.427 -25.722  1.00 86.77           C  
ATOM   1182  O   GLN A 163      49.374  -0.795 -25.885  1.00 86.85           O  
ATOM   1183  CB  GLN A 163      50.359   1.912 -27.423  1.00 87.55           C  
ATOM   1184  CG  GLN A 163      51.283   3.083 -27.714  1.00 87.41           C  
ATOM   1185  CD  GLN A 163      50.970   3.753 -29.040  1.00 87.65           C  
ATOM   1186  OE1 GLN A 163      50.776   3.087 -30.060  1.00 85.28           O  
ATOM   1187  NE2 GLN A 163      50.918   5.081 -29.031  1.00 85.81           N  
ATOM   1188  N   VAL A 164      48.193   1.037 -25.289  1.00 81.76           N  
ATOM   1189  CA  VAL A 164      46.967   0.311 -24.966  1.00 78.40           C  
ATOM   1190  C   VAL A 164      45.756   0.985 -25.600  1.00 74.54           C  
ATOM   1191  O   VAL A 164      45.810   2.170 -25.947  1.00 73.11           O  
ATOM   1192  CB  VAL A 164      46.743   0.190 -23.428  1.00 79.95           C  
ATOM   1193  CG1 VAL A 164      47.835  -0.656 -22.787  1.00 79.59           C  
ATOM   1194  CG2 VAL A 164      46.656   1.571 -22.762  1.00 78.01           C  
ATOM   1195  N   ALA A 165      44.674   0.222 -25.750  1.00 69.46           N  
ATOM   1196  CA  ALA A 165      43.388   0.767 -26.173  1.00 69.83           C  
ATOM   1197  C   ALA A 165      42.834   1.686 -25.081  1.00 71.51           C  
ATOM   1198  O   ALA A 165      42.522   1.243 -23.973  1.00 72.63           O  
ATOM   1199  CB  ALA A 165      42.411  -0.361 -26.480  1.00 67.49           C  
ATOM   1200  N   CYS A 166      42.730   2.972 -25.395  1.00 73.37           N  
ATOM   1201  CA  CYS A 166      42.307   3.966 -24.418  1.00 75.34           C  
ATOM   1202  C   CYS A 166      40.807   3.892 -24.105  1.00 76.91           C  
ATOM   1203  O   CYS A 166      39.992   4.545 -24.760  1.00 75.55           O  
ATOM   1204  CB  CYS A 166      42.703   5.368 -24.886  1.00 77.92           C  
ATOM   1205  SG  CYS A 166      42.385   6.679 -23.688  1.00 86.21           S  
ATOM   1206  N   LEU A 167      40.459   3.078 -23.108  1.00 76.60           N  
ATOM   1207  CA  LEU A 167      39.091   2.990 -22.596  1.00 74.26           C  
ATOM   1208  C   LEU A 167      39.027   3.427 -21.132  1.00 74.37           C  
ATOM   1209  O   LEU A 167      39.982   3.223 -20.373  1.00 73.48           O  
ATOM   1210  CB  LEU A 167      38.539   1.567 -22.722  1.00 75.42           C  
ATOM   1211  CG  LEU A 167      38.083   0.930 -24.046  1.00 76.63           C  
ATOM   1212  CD1 LEU A 167      37.443   1.929 -25.014  1.00 77.22           C  
ATOM   1213  CD2 LEU A 167      39.216   0.166 -24.712  1.00 76.75           C  
ATOM   1214  N   PHE A 168      37.889   4.005 -20.741  1.00 71.36           N  
ATOM   1215  CA  PHE A 168      37.687   4.528 -19.384  1.00 64.83           C  
ATOM   1216  C   PHE A 168      37.847   3.438 -18.333  1.00 62.05           C  
ATOM   1217  O   PHE A 168      38.642   3.581 -17.400  1.00 62.37           O  
ATOM   1218  CB  PHE A 168      36.312   5.201 -19.257  1.00 61.31           C  
ATOM   1219  CG  PHE A 168      36.092   5.909 -17.945  1.00 57.43           C  
ATOM   1220  CD1 PHE A 168      36.452   7.246 -17.793  1.00 55.66           C  
ATOM   1221  CD2 PHE A 168      35.520   5.240 -16.860  1.00 54.08           C  
ATOM   1222  CE1 PHE A 168      36.252   7.911 -16.577  1.00 55.64           C  
ATOM   1223  CE2 PHE A 168      35.315   5.894 -15.639  1.00 53.47           C  
ATOM   1224  CZ  PHE A 168      35.682   7.231 -15.497  1.00 54.92           C  
ATOM   1225  N   GLU A 169      37.103   2.349 -18.506  1.00 60.14           N  
ATOM   1226  CA  GLU A 169      37.113   1.223 -17.566  1.00 60.28           C  
ATOM   1227  C   GLU A 169      38.410   0.417 -17.593  1.00 62.20           C  
ATOM   1228  O   GLU A 169      38.552  -0.552 -16.852  1.00 67.05           O  
ATOM   1229  CB  GLU A 169      35.914   0.298 -17.814  1.00 56.41           C  
ATOM   1230  CG  GLU A 169      34.569   0.931 -17.494  1.00 59.16           C  
ATOM   1231  CD  GLU A 169      33.417  -0.062 -17.525  1.00 63.52           C  
ATOM   1232  OE1 GLU A 169      33.671  -1.286 -17.518  1.00 63.27           O  
ATOM   1233  OE2 GLU A 169      32.250   0.385 -17.550  1.00 66.26           O1-
ATOM   1234  N   ASP A 170      39.351   0.815 -18.445  1.00 66.42           N  
ATOM   1235  CA  ASP A 170      40.652   0.152 -18.517  1.00 67.33           C  
ATOM   1236  C   ASP A 170      41.763   0.903 -17.780  1.00 63.99           C  
ATOM   1237  O   ASP A 170      42.787   0.318 -17.444  1.00 67.96           O  
ATOM   1238  CB  ASP A 170      41.041  -0.118 -19.974  1.00 69.24           C  
ATOM   1239  CG  ASP A 170      40.234  -1.251 -20.594  1.00 74.33           C  
ATOM   1240  OD1 ASP A 170      39.450  -1.908 -19.870  1.00 76.05           O  
ATOM   1241  OD2 ASP A 170      40.383  -1.489 -21.810  1.00 75.30           O1-
ATOM   1242  N   VAL A 171      41.559   2.192 -17.533  1.00 61.39           N  
ATOM   1243  CA  VAL A 171      42.534   2.996 -16.792  1.00 60.98           C  
ATOM   1244  C   VAL A 171      42.007   3.440 -15.415  1.00 60.08           C  
ATOM   1245  O   VAL A 171      42.770   3.503 -14.452  1.00 62.35           O  
ATOM   1246  CB  VAL A 171      43.042   4.220 -17.618  1.00 61.70           C  
ATOM   1247  CG1 VAL A 171      43.830   3.752 -18.838  1.00 63.34           C  
ATOM   1248  CG2 VAL A 171      41.887   5.133 -18.042  1.00 58.23           C  
ATOM   1249  N   VAL A 172      40.711   3.735 -15.326  1.00 55.26           N  
ATOM   1250  CA  VAL A 172      40.101   4.167 -14.069  1.00 56.10           C  
ATOM   1251  C   VAL A 172      39.499   2.960 -13.341  1.00 55.10           C  
ATOM   1252  O   VAL A 172      38.612   2.296 -13.877  1.00 56.93           O  
ATOM   1253  CB  VAL A 172      39.016   5.267 -14.286  1.00 53.42           C  
ATOM   1254  CG1 VAL A 172      38.366   5.650 -12.967  1.00 50.29           C  
ATOM   1255  CG2 VAL A 172      39.623   6.499 -14.942  1.00 53.03           C  
ATOM   1256  N   PRO A 173      39.976   2.678 -12.115  1.00 54.12           N  
ATOM   1257  CA  PRO A 173      39.502   1.502 -11.378  1.00 52.17           C  
ATOM   1258  C   PRO A 173      38.061   1.641 -10.917  1.00 50.94           C  
ATOM   1259  O   PRO A 173      37.613   2.740 -10.596  1.00 51.81           O  
ATOM   1260  CB  PRO A 173      40.441   1.435 -10.161  1.00 52.75           C  
ATOM   1261  CG  PRO A 173      41.614   2.309 -10.510  1.00 54.08           C  
ATOM   1262  CD  PRO A 173      41.038   3.392 -11.382  1.00 55.13           C  
ATOM   1263  N   MET A 174      37.344   0.524 -10.889  1.00 53.97           N  
ATOM   1264  CA  MET A 174      35.960   0.514 -10.440  1.00 55.60           C  
ATOM   1265  C   MET A 174      35.779   0.771  -8.934  1.00 55.17           C  
ATOM   1266  O   MET A 174      34.740   1.289  -8.519  1.00 55.55           O  
ATOM   1267  CB  MET A 174      35.256  -0.782 -10.850  1.00 57.20           C  
ATOM   1268  CG  MET A 174      34.671  -0.783 -12.263  1.00 64.48           C  
ATOM   1269  SD  MET A 174      33.542   0.578 -12.681  1.00 69.57           S  
ATOM   1270  CE  MET A 174      32.624   0.727 -11.164  1.00 65.83           C  
ATOM   1271  N   ASN A 175      36.765   0.412  -8.114  1.00 53.39           N  
ATOM   1272  CA  ASN A 175      36.636   0.676  -6.678  1.00 52.24           C  
ATOM   1273  C   ASN A 175      36.756   2.161  -6.363  1.00 50.39           C  
ATOM   1274  O   ASN A 175      36.009   2.680  -5.526  1.00 47.28           O  
ATOM   1275  CB  ASN A 175      37.569  -0.193  -5.817  1.00 52.60           C  
ATOM   1276  CG  ASN A 175      39.020  -0.107  -6.234  1.00 54.47           C  
ATOM   1277  OD1 ASN A 175      39.375   0.594  -7.183  1.00 60.74           O  
ATOM   1278  ND2 ASN A 175      39.874  -0.830  -5.522  1.00 54.05           N  
ATOM   1279  N   TYR A 176      37.670   2.838  -7.063  1.00 48.81           N  
ATOM   1280  CA  TYR A 176      37.737   4.301  -7.049  1.00 49.32           C  
ATOM   1281  C   TYR A 176      36.390   4.947  -7.408  1.00 48.51           C  
ATOM   1282  O   TYR A 176      35.922   5.855  -6.716  1.00 48.02           O  
ATOM   1283  CB  TYR A 176      38.826   4.832  -7.996  1.00 50.46           C  
ATOM   1284  CG  TYR A 176      38.661   6.313  -8.253  1.00 49.88           C  
ATOM   1285  CD1 TYR A 176      39.108   7.260  -7.325  1.00 48.93           C  
ATOM   1286  CD2 TYR A 176      38.006   6.768  -9.396  1.00 50.11           C  
ATOM   1287  CE1 TYR A 176      38.925   8.621  -7.549  1.00 49.80           C  
ATOM   1288  CE2 TYR A 176      37.815   8.123  -9.624  1.00 50.72           C  
ATOM   1289  CZ  TYR A 176      38.272   9.039  -8.700  1.00 48.83           C  
ATOM   1290  OH  TYR A 176      38.077  10.370  -8.938  1.00 49.66           O  
ATOM   1291  N   MET A 177      35.783   4.473  -8.493  1.00 48.49           N  
ATOM   1292  CA  MET A 177      34.496   4.988  -8.955  1.00 49.05           C  
ATOM   1293  C   MET A 177      33.376   4.766  -7.949  1.00 47.97           C  
ATOM   1294  O   MET A 177      32.562   5.658  -7.712  1.00 48.73           O  
ATOM   1295  CB  MET A 177      34.117   4.376 -10.315  1.00 51.12           C  
ATOM   1296  CG  MET A 177      34.864   4.975 -11.534  1.00 49.90           C  
ATOM   1297  SD  MET A 177      34.854   6.786 -11.607  1.00 50.90           S  
ATOM   1298  CE  MET A 177      33.093   7.119 -11.775  1.00 49.55           C  
ATOM   1299  N   VAL A 178      33.354   3.581  -7.350  1.00 48.76           N  
ATOM   1300  CA  VAL A 178      32.275   3.174  -6.459  1.00 50.71           C  
ATOM   1301  C   VAL A 178      32.455   3.712  -5.037  1.00 53.42           C  
ATOM   1302  O   VAL A 178      31.512   4.257  -4.463  1.00 53.21           O  
ATOM   1303  CB  VAL A 178      32.106   1.627  -6.455  1.00 51.55           C  
ATOM   1304  CG1 VAL A 178      31.263   1.148  -5.270  1.00 50.97           C  
ATOM   1305  CG2 VAL A 178      31.506   1.158  -7.772  1.00 48.27           C  
ATOM   1306  N   TYR A 179      33.663   3.577  -4.490  1.00 57.02           N  
ATOM   1307  CA  TYR A 179      33.926   3.911  -3.082  1.00 58.94           C  
ATOM   1308  C   TYR A 179      34.230   5.376  -2.825  1.00 60.22           C  
ATOM   1309  O   TYR A 179      33.898   5.904  -1.761  1.00 60.55           O  
ATOM   1310  CB  TYR A 179      35.064   3.055  -2.512  1.00 58.96           C  
ATOM   1311  CG  TYR A 179      34.694   1.610  -2.279  1.00 60.63           C  
ATOM   1312  CD1 TYR A 179      33.489   1.268  -1.660  1.00 63.29           C  
ATOM   1313  CD2 TYR A 179      35.542   0.581  -2.682  1.00 60.95           C  
ATOM   1314  CE1 TYR A 179      33.139  -0.066  -1.448  1.00 65.23           C  
ATOM   1315  CE2 TYR A 179      35.203  -0.753  -2.472  1.00 64.10           C  
ATOM   1316  CZ  TYR A 179      34.001  -1.067  -1.857  1.00 65.14           C  
ATOM   1317  OH  TYR A 179      33.665  -2.381  -1.646  1.00 69.87           O  
ATOM   1318  N   PHE A 180      34.871   6.028  -3.788  1.00 59.75           N  
ATOM   1319  CA  PHE A 180      35.280   7.412  -3.612  1.00 59.04           C  
ATOM   1320  C   PHE A 180      34.416   8.360  -4.456  1.00 59.27           C  
ATOM   1321  O   PHE A 180      33.704   9.199  -3.900  1.00 58.87           O  
ATOM   1322  CB  PHE A 180      36.788   7.559  -3.887  1.00 58.71           C  
ATOM   1323  CG  PHE A 180      37.370   8.906  -3.512  1.00 58.84           C  
ATOM   1324  CD1 PHE A 180      36.764   9.720  -2.553  1.00 60.14           C  
ATOM   1325  CD2 PHE A 180      38.552   9.342  -4.104  1.00 58.37           C  
ATOM   1326  CE1 PHE A 180      37.316  10.964  -2.211  1.00 58.97           C  
ATOM   1327  CE2 PHE A 180      39.115  10.572  -3.765  1.00 59.30           C  
ATOM   1328  CZ  PHE A 180      38.492  11.387  -2.815  1.00 59.23           C  
ATOM   1329  N   ASN A 181      34.451   8.199  -5.779  1.00 57.68           N  
ATOM   1330  CA  ASN A 181      33.774   9.119  -6.704  1.00 56.53           C  
ATOM   1331  C   ASN A 181      32.243   9.176  -6.569  1.00 57.29           C  
ATOM   1332  O   ASN A 181      31.664  10.259  -6.505  1.00 57.28           O  
ATOM   1333  CB  ASN A 181      34.177   8.817  -8.150  1.00 55.48           C  
ATOM   1334  CG  ASN A 181      33.949   9.992  -9.075  1.00 52.27           C  
ATOM   1335  OD1 ASN A 181      32.826  10.258  -9.479  1.00 52.98           O  
ATOM   1336  ND2 ASN A 181      35.022  10.694  -9.424  1.00 51.51           N  
ATOM   1337  N   PHE A 182      31.593   8.018  -6.521  1.00 56.26           N  
ATOM   1338  CA  PHE A 182      30.139   7.963  -6.333  1.00 56.61           C  
ATOM   1339  C   PHE A 182      29.675   8.640  -5.023  1.00 57.20           C  
ATOM   1340  O   PHE A 182      28.709   9.407  -5.028  1.00 57.48           O  
ATOM   1341  CB  PHE A 182      29.650   6.508  -6.443  1.00 54.35           C  
ATOM   1342  CG  PHE A 182      28.193   6.309  -6.117  1.00 54.73           C  
ATOM   1343  CD1 PHE A 182      27.210   7.120  -6.677  1.00 56.10           C  
ATOM   1344  CD2 PHE A 182      27.802   5.276  -5.268  1.00 56.27           C  
ATOM   1345  CE1 PHE A 182      25.861   6.921  -6.380  1.00 56.27           C  
ATOM   1346  CE2 PHE A 182      26.461   5.066  -4.964  1.00 56.55           C  
ATOM   1347  CZ  PHE A 182      25.486   5.891  -5.521  1.00 58.60           C  
ATOM   1348  N   PHE A 183      30.368   8.372  -3.917  1.00 56.75           N  
ATOM   1349  CA  PHE A 183      29.985   8.937  -2.619  1.00 57.56           C  
ATOM   1350  C   PHE A 183      30.305  10.429  -2.492  1.00 55.21           C  
ATOM   1351  O   PHE A 183      29.458  11.215  -2.060  1.00 52.24           O  
ATOM   1352  CB  PHE A 183      30.608   8.139  -1.462  1.00 59.59           C  
ATOM   1353  CG  PHE A 183      29.961   6.795  -1.235  1.00 63.92           C  
ATOM   1354  CD1 PHE A 183      28.774   6.688  -0.508  1.00 64.41           C  
ATOM   1355  CD2 PHE A 183      30.536   5.634  -1.750  1.00 64.92           C  
ATOM   1356  CE1 PHE A 183      28.170   5.443  -0.301  1.00 65.80           C  
ATOM   1357  CE2 PHE A 183      29.938   4.382  -1.550  1.00 65.99           C  
ATOM   1358  CZ  PHE A 183      28.755   4.286  -0.828  1.00 64.85           C  
ATOM   1359  N   ALA A 184      31.517  10.812  -2.882  1.00 53.48           N  
ATOM   1360  CA  ALA A 184      31.954  12.202  -2.791  1.00 54.48           C  
ATOM   1361  C   ALA A 184      31.233  13.119  -3.777  1.00 54.75           C  
ATOM   1362  O   ALA A 184      30.854  14.239  -3.423  1.00 57.80           O  
ATOM   1363  CB  ALA A 184      33.465  12.304  -2.988  1.00 54.09           C  
ATOM   1364  N   CYS A 185      31.047  12.642  -5.006  1.00 52.81           N  
ATOM   1365  CA  CYS A 185      30.593  13.498  -6.102  1.00 53.04           C  
ATOM   1366  C   CYS A 185      29.100  13.437  -6.382  1.00 51.93           C  
ATOM   1367  O   CYS A 185      28.528  14.400  -6.890  1.00 52.94           O  
ATOM   1368  CB  CYS A 185      31.368  13.194  -7.388  1.00 52.99           C  
ATOM   1369  SG  CYS A 185      33.120  13.605  -7.295  1.00 59.64           S  
ATOM   1370  N   VAL A 186      28.471  12.311  -6.071  1.00 49.63           N  
ATOM   1371  CA  VAL A 186      27.076  12.129  -6.438  1.00 49.34           C  
ATOM   1372  C   VAL A 186      26.164  12.001  -5.218  1.00 50.06           C  
ATOM   1373  O   VAL A 186      25.237  12.798  -5.053  1.00 48.35           O  
ATOM   1374  CB  VAL A 186      26.889  10.945  -7.421  1.00 48.57           C  
ATOM   1375  CG1 VAL A 186      25.401  10.724  -7.754  1.00 45.18           C  
ATOM   1376  CG2 VAL A 186      27.712  11.175  -8.692  1.00 47.93           C  
ATOM   1377  N   LEU A 187      26.426  11.012  -4.369  1.00 48.95           N  
ATOM   1378  CA  LEU A 187      25.523  10.736  -3.253  1.00 49.37           C  
ATOM   1379  C   LEU A 187      25.484  11.840  -2.199  1.00 48.15           C  
ATOM   1380  O   LEU A 187      24.398  12.274  -1.807  1.00 49.02           O  
ATOM   1381  CB  LEU A 187      25.829   9.389  -2.607  1.00 50.94           C  
ATOM   1382  CG  LEU A 187      24.628   8.795  -1.879  1.00 55.27           C  
ATOM   1383  CD1 LEU A 187      23.666   8.155  -2.880  1.00 57.90           C  
ATOM   1384  CD2 LEU A 187      25.079   7.787  -0.830  1.00 56.43           C  
ATOM   1385  N   VAL A 188      26.649  12.303  -1.746  1.00 47.44           N  
ATOM   1386  CA  VAL A 188      26.683  13.380  -0.744  1.00 47.95           C  
ATOM   1387  C   VAL A 188      26.003  14.667  -1.259  1.00 47.63           C  
ATOM   1388  O   VAL A 188      25.019  15.108  -0.665  1.00 48.79           O  
ATOM   1389  CB  VAL A 188      28.102  13.608  -0.140  1.00 48.88           C  
ATOM   1390  CG1 VAL A 188      28.205  14.960   0.566  1.00 49.94           C  
ATOM   1391  CG2 VAL A 188      28.444  12.482   0.831  1.00 48.09           C  
ATOM   1392  N   PRO A 189      26.492  15.251  -2.375  1.00 48.37           N  
ATOM   1393  CA  PRO A 189      25.800  16.415  -2.928  1.00 48.20           C  
ATOM   1394  C   PRO A 189      24.284  16.225  -3.081  1.00 49.49           C  
ATOM   1395  O   PRO A 189      23.522  17.115  -2.694  1.00 48.95           O  
ATOM   1396  CB  PRO A 189      26.467  16.589  -4.293  1.00 47.88           C  
ATOM   1397  CG  PRO A 189      27.852  16.120  -4.068  1.00 48.56           C  
ATOM   1398  CD  PRO A 189      27.720  14.948  -3.139  1.00 49.16           C  
ATOM   1399  N   LEU A 190      23.860  15.078  -3.617  1.00 49.37           N  
ATOM   1400  CA  LEU A 190      22.438  14.776  -3.798  1.00 50.51           C  
ATOM   1401  C   LEU A 190      21.677  14.798  -2.479  1.00 52.70           C  
ATOM   1402  O   LEU A 190      20.612  15.411  -2.385  1.00 54.95           O  
ATOM   1403  CB  LEU A 190      22.234  13.430  -4.505  1.00 49.63           C  
ATOM   1404  CG  LEU A 190      20.813  12.855  -4.614  1.00 49.41           C  
ATOM   1405  CD1 LEU A 190      19.883  13.745  -5.443  1.00 48.72           C  
ATOM   1406  CD2 LEU A 190      20.838  11.443  -5.181  1.00 48.03           C  
ATOM   1407  N   LEU A 191      22.226  14.138  -1.465  1.00 53.71           N  
ATOM   1408  CA  LEU A 191      21.598  14.130  -0.148  1.00 54.66           C  
ATOM   1409  C   LEU A 191      21.557  15.513   0.489  1.00 54.78           C  
ATOM   1410  O   LEU A 191      20.557  15.878   1.110  1.00 56.46           O  
ATOM   1411  CB  LEU A 191      22.275  13.123   0.783  1.00 55.33           C  
ATOM   1412  CG  LEU A 191      22.037  11.636   0.493  1.00 55.27           C  
ATOM   1413  CD1 LEU A 191      22.702  10.794   1.577  1.00 58.10           C  
ATOM   1414  CD2 LEU A 191      20.550  11.287   0.373  1.00 52.03           C  
ATOM   1415  N   LEU A 192      22.631  16.284   0.323  1.00 54.60           N  
ATOM   1416  CA  LEU A 192      22.664  17.665   0.816  1.00 55.28           C  
ATOM   1417  C   LEU A 192      21.620  18.555   0.129  1.00 55.72           C  
ATOM   1418  O   LEU A 192      20.943  19.345   0.787  1.00 55.06           O  
ATOM   1419  CB  LEU A 192      24.069  18.275   0.692  1.00 52.25           C  
ATOM   1420  CG  LEU A 192      25.139  17.782   1.674  1.00 53.90           C  
ATOM   1421  CD1 LEU A 192      26.538  18.297   1.293  1.00 50.67           C  
ATOM   1422  CD2 LEU A 192      24.788  18.154   3.125  1.00 51.82           C  
ATOM   1423  N   MET A 193      21.490  18.420  -1.189  1.00 56.55           N  
ATOM   1424  CA  MET A 193      20.535  19.225  -1.945  1.00 57.27           C  
ATOM   1425  C   MET A 193      19.096  18.805  -1.643  1.00 57.08           C  
ATOM   1426  O   MET A 193      18.206  19.652  -1.551  1.00 55.78           O  
ATOM   1427  CB  MET A 193      20.815  19.148  -3.447  1.00 55.93           C  
ATOM   1428  CG  MET A 193      22.050  19.907  -3.903  1.00 55.07           C  
ATOM   1429  SD  MET A 193      22.241  19.981  -5.701  1.00 54.87           S  
ATOM   1430  CE  MET A 193      22.305  18.247  -6.168  1.00 51.11           C  
ATOM   1431  N   LEU A 194      18.877  17.498  -1.496  1.00 56.95           N  
ATOM   1432  CA  LEU A 194      17.573  16.971  -1.099  1.00 58.55           C  
ATOM   1433  C   LEU A 194      17.180  17.482   0.294  1.00 59.39           C  
ATOM   1434  O   LEU A 194      16.013  17.809   0.535  1.00 62.19           O  
ATOM   1435  CB  LEU A 194      17.556  15.436  -1.151  1.00 57.45           C  
ATOM   1436  CG  LEU A 194      16.243  14.707  -0.816  1.00 59.44           C  
ATOM   1437  CD1 LEU A 194      15.112  15.082  -1.772  1.00 59.27           C  
ATOM   1438  CD2 LEU A 194      16.444  13.197  -0.800  1.00 59.26           C  
ATOM   1439  N   GLY A 195      18.163  17.563   1.189  1.00 57.26           N  
ATOM   1440  CA  GLY A 195      17.962  18.088   2.537  1.00 58.18           C  
ATOM   1441  C   GLY A 195      17.645  19.571   2.549  1.00 61.33           C  
ATOM   1442  O   GLY A 195      16.879  20.043   3.394  1.00 64.83           O  
ATOM   1443  N   VAL A 196      18.243  20.309   1.615  1.00 62.07           N  
ATOM   1444  CA  VAL A 196      17.971  21.736   1.457  1.00 59.95           C  
ATOM   1445  C   VAL A 196      16.545  21.954   0.947  1.00 59.96           C  
ATOM   1446  O   VAL A 196      15.836  22.836   1.429  1.00 64.26           O  
ATOM   1447  CB  VAL A 196      19.002  22.414   0.527  1.00 59.00           C  
ATOM   1448  CG1 VAL A 196      18.511  23.782   0.065  1.00 58.95           C  
ATOM   1449  CG2 VAL A 196      20.340  22.561   1.238  1.00 59.04           C  
ATOM   1450  N   TYR A 197      16.131  21.139  -0.017  1.00 58.01           N  
ATOM   1451  CA  TYR A 197      14.781  21.201  -0.550  1.00 59.35           C  
ATOM   1452  C   TYR A 197      13.734  20.891   0.527  1.00 60.94           C  
ATOM   1453  O   TYR A 197      12.708  21.570   0.617  1.00 60.69           O  
ATOM   1454  CB  TYR A 197      14.627  20.264  -1.757  1.00 58.99           C  
ATOM   1455  CG  TYR A 197      13.191  19.914  -2.060  1.00 58.43           C  
ATOM   1456  CD1 TYR A 197      12.341  20.836  -2.663  1.00 58.69           C  
ATOM   1457  CD2 TYR A 197      12.676  18.665  -1.720  1.00 62.06           C  
ATOM   1458  CE1 TYR A 197      11.013  20.521  -2.925  1.00 59.94           C  
ATOM   1459  CE2 TYR A 197      11.350  18.340  -1.981  1.00 63.64           C  
ATOM   1460  CZ  TYR A 197      10.529  19.273  -2.583  1.00 61.52           C  
ATOM   1461  OH  TYR A 197       9.222  18.956  -2.838  1.00 64.32           O  
ATOM   1462  N   LEU A 198      14.002  19.881   1.350  1.00 62.23           N  
ATOM   1463  CA  LEU A 198      13.057  19.473   2.389  1.00 64.92           C  
ATOM   1464  C   LEU A 198      12.876  20.529   3.484  1.00 67.88           C  
ATOM   1465  O   LEU A 198      11.810  20.617   4.098  1.00 68.92           O  
ATOM   1466  CB  LEU A 198      13.441  18.109   2.976  1.00 64.52           C  
ATOM   1467  CG  LEU A 198      13.294  16.908   2.023  1.00 66.16           C  
ATOM   1468  CD1 LEU A 198      13.986  15.671   2.570  1.00 67.73           C  
ATOM   1469  CD2 LEU A 198      11.833  16.597   1.682  1.00 65.59           C  
ATOM   1470  N   ARG A 199      13.906  21.343   3.701  1.00 69.68           N  
ATOM   1471  CA  ARG A 199      13.834  22.435   4.670  1.00 72.22           C  
ATOM   1472  C   ARG A 199      13.091  23.653   4.127  1.00 70.86           C  
ATOM   1473  O   ARG A 199      12.416  24.355   4.885  1.00 70.05           O  
ATOM   1474  CB  ARG A 199      15.232  22.826   5.167  1.00 77.81           C  
ATOM   1475  CG  ARG A 199      15.828  21.838   6.172  1.00 84.91           C  
ATOM   1476  CD  ARG A 199      15.115  21.922   7.519  1.00 90.63           C  
ATOM   1477  NE  ARG A 199      15.045  20.629   8.199  1.00 92.15           N  
ATOM   1478  CZ  ARG A 199      14.272  20.372   9.253  1.00 95.20           C  
ATOM   1479  NH1 ARG A 199      13.489  21.318   9.762  1.00 93.78           N  
ATOM   1480  NH2 ARG A 199      14.277  19.163   9.802  1.00 97.20           N  
ATOM   1481  N   ILE A 200      13.220  23.905   2.824  1.00 66.06           N  
ATOM   1482  CA  ILE A 200      12.473  24.989   2.177  1.00 64.51           C  
ATOM   1483  C   ILE A 200      10.988  24.615   2.053  1.00 65.50           C  
ATOM   1484  O   ILE A 200      10.107  25.464   2.226  1.00 66.24           O  
ATOM   1485  CB  ILE A 200      13.083  25.393   0.805  1.00 60.77           C  
ATOM   1486  CG1 ILE A 200      14.492  25.966   1.012  1.00 60.90           C  
ATOM   1487  CG2 ILE A 200      12.199  26.421   0.090  1.00 57.63           C  
ATOM   1488  CD1 ILE A 200      15.217  26.376  -0.261  1.00 58.68           C  
ATOM   1489  N   PHE A 201      10.727  23.341   1.774  1.00 63.27           N  
ATOM   1490  CA  PHE A 201       9.367  22.825   1.700  1.00 65.59           C  
ATOM   1491  C   PHE A 201       8.645  22.951   3.047  1.00 67.31           C  
ATOM   1492  O   PHE A 201       7.491  23.387   3.097  1.00 66.36           O  
ATOM   1493  CB  PHE A 201       9.374  21.368   1.220  1.00 66.66           C  
ATOM   1494  CG  PHE A 201       8.005  20.779   1.036  1.00 69.49           C  
ATOM   1495  CD1 PHE A 201       7.314  20.952  -0.161  1.00 70.73           C  
ATOM   1496  CD2 PHE A 201       7.404  20.043   2.056  1.00 71.87           C  
ATOM   1497  CE1 PHE A 201       6.040  20.407  -0.337  1.00 69.79           C  
ATOM   1498  CE2 PHE A 201       6.128  19.497   1.889  1.00 72.30           C  
ATOM   1499  CZ  PHE A 201       5.449  19.681   0.689  1.00 68.83           C  
ATOM   1500  N   LEU A 202       9.334  22.569   4.125  1.00 67.35           N  
ATOM   1501  CA  LEU A 202       8.793  22.643   5.482  1.00 68.30           C  
ATOM   1502  C   LEU A 202       8.519  24.077   5.939  1.00 69.42           C  
ATOM   1503  O   LEU A 202       7.608  24.317   6.731  1.00 72.73           O  
ATOM   1504  CB  LEU A 202       9.723  21.936   6.474  1.00 70.80           C  
ATOM   1505  CG  LEU A 202       9.398  20.508   6.940  1.00 74.55           C  
ATOM   1506  CD1 LEU A 202       8.090  20.481   7.728  1.00 76.47           C  
ATOM   1507  CD2 LEU A 202       9.361  19.490   5.796  1.00 76.02           C  
ATOM   1508  N   ALA A 203       9.310  25.020   5.434  1.00 67.56           N  
ATOM   1509  CA  ALA A 203       9.081  26.437   5.681  1.00 68.11           C  
ATOM   1510  C   ALA A 203       7.781  26.886   5.018  1.00 69.89           C  
ATOM   1511  O   ALA A 203       7.013  27.654   5.603  1.00 70.42           O  
ATOM   1512  CB  ALA A 203      10.251  27.265   5.175  1.00 64.95           C  
ATOM   1513  N   ALA A 204       7.545  26.397   3.800  1.00 68.21           N  
ATOM   1514  CA  ALA A 204       6.315  26.686   3.067  1.00 68.98           C  
ATOM   1515  C   ALA A 204       5.095  26.072   3.757  1.00 69.29           C  
ATOM   1516  O   ALA A 204       4.040  26.696   3.835  1.00 65.10           O  
ATOM   1517  CB  ALA A 204       6.426  26.204   1.625  1.00 66.59           C  
ATOM   1518  N   ARG A 205       5.257  24.855   4.271  1.00 73.48           N  
ATOM   1519  CA  ARG A 205       4.193  24.159   4.992  1.00 77.67           C  
ATOM   1520  C   ARG A 205       3.796  24.868   6.299  1.00 80.92           C  
ATOM   1521  O   ARG A 205       2.621  24.875   6.670  1.00 82.66           O  
ATOM   1522  CB  ARG A 205       4.598  22.709   5.263  1.00 76.34           C  
ATOM   1523  CG  ARG A 205       3.424  21.773   5.450  1.00 79.77           C  
ATOM   1524  CD  ARG A 205       3.825  20.327   5.242  1.00 84.83           C  
ATOM   1525  NE  ARG A 205       4.442  19.737   6.430  1.00 89.49           N  
ATOM   1526  CZ  ARG A 205       4.743  18.446   6.558  1.00 93.40           C  
ATOM   1527  NH1 ARG A 205       4.483  17.595   5.571  1.00 94.77           N  
ATOM   1528  NH2 ARG A 205       5.303  18.000   7.677  1.00 94.04           N  
ATOM   1529  N   ARG A 206       4.772  25.466   6.981  1.00 82.45           N  
ATOM   1530  CA  ARG A 206       4.509  26.211   8.216  1.00 82.21           C  
ATOM   1531  C   ARG A 206       3.799  27.533   7.940  1.00 79.78           C  
ATOM   1532  O   ARG A 206       2.882  27.908   8.669  1.00 78.66           O  
ATOM   1533  CB  ARG A 206       5.796  26.451   9.013  1.00 86.26           C  
ATOM   1534  CG  ARG A 206       6.411  25.190   9.600  1.00 91.21           C  
ATOM   1535  CD  ARG A 206       7.571  25.513  10.531  1.00 97.98           C  
ATOM   1536  NE  ARG A 206       8.519  24.403  10.636  1.00103.83           N  
ATOM   1537  CZ  ARG A 206       8.401  23.374  11.475  1.00108.60           C  
ATOM   1538  NH1 ARG A 206       7.365  23.289  12.305  1.00106.93           N  
ATOM   1539  NH2 ARG A 206       9.326  22.422  11.481  1.00109.59           N  
ATOM   1540  N   GLN A 207       4.230  28.231   6.890  1.00 78.36           N  
ATOM   1541  CA  GLN A 207       3.582  29.466   6.449  1.00 78.69           C  
ATOM   1542  C   GLN A 207       2.144  29.194   6.020  1.00 79.55           C  
ATOM   1543  O   GLN A 207       1.242  29.987   6.295  1.00 78.37           O  
ATOM   1544  CB  GLN A 207       4.343  30.093   5.280  1.00 78.37           C  
ATOM   1545  CG  GLN A 207       5.666  30.739   5.647  1.00 84.02           C  
ATOM   1546  CD  GLN A 207       5.495  32.039   6.402  1.00 87.07           C  
ATOM   1547  OE1 GLN A 207       5.849  32.136   7.579  1.00 90.79           O  
ATOM   1548  NE2 GLN A 207       4.941  33.045   5.733  1.00 85.38           N  
ATOM   1549  N   LEU A 208       1.949  28.062   5.348  1.00 79.78           N  
ATOM   1550  CA  LEU A 208       0.649  27.668   4.833  1.00 79.27           C  
ATOM   1551  C   LEU A 208      -0.310  27.295   5.960  1.00 82.11           C  
ATOM   1552  O   LEU A 208      -1.513  27.540   5.860  1.00 81.46           O  
ATOM   1553  CB  LEU A 208       0.801  26.504   3.851  1.00 75.95           C  
ATOM   1554  CG  LEU A 208      -0.332  26.247   2.855  1.00 77.34           C  
ATOM   1555  CD1 LEU A 208      -0.589  27.456   1.945  1.00 73.15           C  
ATOM   1556  CD2 LEU A 208      -0.017  25.008   2.033  1.00 76.24           C  
ATOM   1557  N   LYS A 209       0.227  26.716   7.031  1.00 82.17           N  
ATOM   1558  CA  LYS A 209      -0.589  26.339   8.182  1.00 86.07           C  
ATOM   1559  C   LYS A 209      -1.057  27.549   9.000  1.00 88.27           C  
ATOM   1560  O   LYS A 209      -2.089  27.487   9.670  1.00 94.77           O  
ATOM   1561  CB  LYS A 209       0.147  25.335   9.073  1.00 85.70           C  
ATOM   1562  CG  LYS A 209      -0.797  24.438   9.851  1.00 90.67           C  
ATOM   1563  CD  LYS A 209      -0.064  23.478  10.760  1.00 96.10           C  
ATOM   1564  CE  LYS A 209      -1.050  22.570  11.478  1.00 96.28           C  
ATOM   1565  NZ  LYS A 209      -0.369  21.695  12.470  1.00 99.86           N  
ATOM   1566  N   GLN A 210      -0.303  28.643   8.939  1.00 89.16           N  
ATOM   1567  CA  GLN A 210      -0.668  29.879   9.635  1.00 90.16           C  
ATOM   1568  C   GLN A 210      -1.824  30.601   8.948  1.00 88.03           C  
ATOM   1569  O   GLN A 210      -2.557  31.360   9.586  1.00 86.89           O  
ATOM   1570  CB  GLN A 210       0.540  30.811   9.765  1.00 93.38           C  
ATOM   1571  CG  GLN A 210       1.478  30.444  10.910  1.00100.22           C  
ATOM   1572  CD  GLN A 210       2.839  31.119  10.815  1.00104.85           C  
ATOM   1573  OE1 GLN A 210       3.014  32.114  10.106  1.00106.98           O  
ATOM   1574  NE2 GLN A 210       3.814  30.574  11.537  1.00104.79           N  
ATOM   1575  N   MET A 211      -1.980  30.351   7.649  1.00 84.73           N  
ATOM   1576  CA  MET A 211      -3.065  30.933   6.859  1.00 84.83           C  
ATOM   1577  C   MET A 211      -4.431  30.326   7.202  1.00 87.08           C  
ATOM   1578  O   MET A 211      -5.467  30.801   6.726  1.00 87.73           O  
ATOM   1579  CB  MET A 211      -2.772  30.794   5.367  1.00 85.00           C  
ATOM   1580  CG  MET A 211      -1.563  31.584   4.913  1.00 87.29           C  
ATOM   1581  SD  MET A 211      -1.458  31.723   3.125  1.00 91.60           S  
ATOM   1582  CE  MET A 211       0.074  32.632   2.950  1.00 92.09           C  
ATOM   1583  N   GLU A 212      -4.419  29.284   8.035  1.00 85.05           N  
ATOM   1584  CA  GLU A 212      -5.638  28.692   8.589  1.00 87.23           C  
ATOM   1585  C   GLU A 212      -6.170  29.488   9.792  1.00 91.22           C  
ATOM   1586  O   GLU A 212      -6.913  28.959  10.623  1.00 92.45           O  
ATOM   1587  CB  GLU A 212      -5.396  27.230   8.971  1.00 81.73           C  
ATOM   1588  CG  GLU A 212      -5.090  26.337   7.784  1.00 83.07           C  
ATOM   1589  CD  GLU A 212      -4.826  24.894   8.167  1.00 86.09           C  
ATOM   1590  OE1 GLU A 212      -4.707  24.597   9.376  1.00 87.27           O  
ATOM   1591  OE2 GLU A 212      -4.733  24.051   7.250  1.00 87.70           O  
ATOM   1592  N   SER A 213      -5.763  30.754   9.876  1.00 92.47           N  
ATOM   1593  CA  SER A 213      -6.289  31.724  10.837  1.00 93.04           C  
ATOM   1594  C   SER A 213      -6.261  33.096  10.170  1.00 97.73           C  
ATOM   1595  O   SER A 213      -5.286  33.439   9.496  1.00101.98           O  
ATOM   1596  CB  SER A 213      -5.453  31.747  12.119  1.00 87.64           C  
ATOM   1597  OG  SER A 213      -5.395  30.467  12.720  1.00 82.33           O  
ATOM   1598  N   GLN A 214      -7.331  33.870  10.343  1.00102.41           N  
ATOM   1599  CA  GLN A 214      -7.443  35.186   9.700  1.00104.54           C  
ATOM   1600  C   GLN A 214      -7.003  36.327  10.620  1.00102.99           C  
ATOM   1601  O   GLN A 214      -5.940  36.919  10.425  1.00 94.46           O  
ATOM   1602  CB  GLN A 214      -8.864  35.425   9.157  1.00104.62           C  
ATOM   1603  CG  GLN A 214      -9.993  35.339  10.192  1.00105.35           C  
ATOM   1604  CD  GLN A 214     -11.380  35.487   9.574  1.00104.20           C  
ATOM   1605  OE1 GLN A 214     -11.680  34.893   8.537  1.00106.59           O  
ATOM   1606  NE2 GLN A 214     -12.233  36.275  10.217  1.00 99.43           N  
ATOM   1607  N   SER A 223       4.086  37.602   1.905  1.00103.86           N  
ATOM   1608  CA  SER A 223       4.758  37.472   0.614  1.00100.35           C  
ATOM   1609  C   SER A 223       5.925  36.483   0.666  1.00100.52           C  
ATOM   1610  O   SER A 223       6.491  36.124  -0.372  1.00101.54           O  
ATOM   1611  CB  SER A 223       5.244  38.839   0.125  1.00 99.08           C  
ATOM   1612  OG  SER A 223       5.776  38.748  -1.186  1.00 98.94           O  
ATOM   1613  N   THR A 224       6.273  36.049   1.877  1.00100.02           N  
ATOM   1614  CA  THR A 224       7.351  35.082   2.097  1.00 97.66           C  
ATOM   1615  C   THR A 224       6.961  33.690   1.589  1.00 95.83           C  
ATOM   1616  O   THR A 224       7.819  32.917   1.153  1.00 97.62           O  
ATOM   1617  CB  THR A 224       7.754  35.011   3.591  1.00 97.44           C  
ATOM   1618  OG1 THR A 224       7.883  36.337   4.115  1.00101.09           O  
ATOM   1619  CG2 THR A 224       9.080  34.286   3.770  1.00 98.77           C  
ATOM   1620  N   LEU A 225       5.665  33.385   1.638  1.00 91.25           N  
ATOM   1621  CA  LEU A 225       5.144  32.111   1.145  1.00 86.16           C  
ATOM   1622  C   LEU A 225       5.360  31.938  -0.364  1.00 83.49           C  
ATOM   1623  O   LEU A 225       5.696  30.846  -0.819  1.00 81.04           O  
ATOM   1624  CB  LEU A 225       3.662  31.952   1.522  1.00 84.35           C  
ATOM   1625  CG  LEU A 225       2.913  30.612   1.395  1.00 84.59           C  
ATOM   1626  CD1 LEU A 225       2.278  30.448   0.026  1.00 82.03           C  
ATOM   1627  CD2 LEU A 225       3.786  29.398   1.721  1.00 82.83           C  
ATOM   1628  N   GLN A 226       5.183  33.014  -1.129  1.00 81.88           N  
ATOM   1629  CA  GLN A 226       5.399  32.971  -2.579  1.00 80.05           C  
ATOM   1630  C   GLN A 226       6.873  32.751  -2.943  1.00 80.24           C  
ATOM   1631  O   GLN A 226       7.179  32.037  -3.901  1.00 77.61           O  
ATOM   1632  CB  GLN A 226       4.846  34.228  -3.258  1.00 82.74           C  
ATOM   1633  CG  GLN A 226       4.763  34.128  -4.786  1.00 86.48           C  
ATOM   1634  CD  GLN A 226       3.835  35.161  -5.414  1.00 90.75           C  
ATOM   1635  OE1 GLN A 226       3.414  36.123  -4.764  1.00 90.56           O  
ATOM   1636  NE2 GLN A 226       3.511  34.963  -6.693  1.00 91.63           N  
ATOM   1637  N   LYS A 227       7.773  33.367  -2.177  1.00 80.58           N  
ATOM   1638  CA  LYS A 227       9.214  33.187  -2.367  1.00 78.71           C  
ATOM   1639  C   LYS A 227       9.639  31.747  -2.093  1.00 76.53           C  
ATOM   1640  O   LYS A 227      10.410  31.165  -2.859  1.00 77.62           O  
ATOM   1641  CB  LYS A 227      10.010  34.146  -1.477  1.00 82.58           C  
ATOM   1642  CG  LYS A 227       9.981  35.597  -1.937  1.00 86.48           C  
ATOM   1643  CD  LYS A 227      10.767  36.498  -0.993  1.00 86.84           C  
ATOM   1644  CE  LYS A 227      10.485  37.971  -1.264  1.00 87.52           C  
ATOM   1645  NZ  LYS A 227      11.074  38.442  -2.551  1.00 88.56           N  
ATOM   1646  N   GLU A 228       9.117  31.177  -1.009  1.00 73.43           N  
ATOM   1647  CA  GLU A 228       9.454  29.813  -0.600  1.00 69.62           C  
ATOM   1648  C   GLU A 228       8.888  28.734  -1.521  1.00 67.88           C  
ATOM   1649  O   GLU A 228       9.560  27.735  -1.787  1.00 68.53           O  
ATOM   1650  CB  GLU A 228       9.015  29.566   0.839  1.00 69.99           C  
ATOM   1651  CG  GLU A 228       9.875  30.292   1.859  1.00 74.13           C  
ATOM   1652  CD  GLU A 228       9.282  30.282   3.253  1.00 78.10           C  
ATOM   1653  OE1 GLU A 228       8.156  29.766   3.432  1.00 83.05           O1-
ATOM   1654  OE2 GLU A 228       9.946  30.796   4.176  1.00 80.10           O  
ATOM   1655  N   VAL A 229       7.660  28.932  -1.999  1.00 63.52           N  
ATOM   1656  CA  VAL A 229       7.031  27.988  -2.928  1.00 61.83           C  
ATOM   1657  C   VAL A 229       7.782  27.990  -4.263  1.00 62.26           C  
ATOM   1658  O   VAL A 229       8.061  26.929  -4.827  1.00 59.82           O  
ATOM   1659  CB  VAL A 229       5.514  28.284  -3.129  1.00 61.59           C  
ATOM   1660  CG1 VAL A 229       4.928  27.453  -4.264  1.00 57.41           C  
ATOM   1661  CG2 VAL A 229       4.745  28.026  -1.843  1.00 61.34           C  
ATOM   1662  N   HIS A 230       8.119  29.182  -4.753  1.00 63.99           N  
ATOM   1663  CA  HIS A 230       8.942  29.311  -5.954  1.00 66.33           C  
ATOM   1664  C   HIS A 230      10.323  28.656  -5.761  1.00 64.86           C  
ATOM   1665  O   HIS A 230      10.799  27.936  -6.644  1.00 64.23           O  
ATOM   1666  CB  HIS A 230       9.084  30.781  -6.373  1.00 68.01           C  
ATOM   1667  CG  HIS A 230      10.022  30.990  -7.522  1.00 72.74           C  
ATOM   1668  ND1 HIS A 230      11.330  31.396  -7.351  1.00 73.44           N  
ATOM   1669  CD2 HIS A 230       9.850  30.827  -8.856  1.00 72.67           C  
ATOM   1670  CE1 HIS A 230      11.920  31.480  -8.530  1.00 74.53           C  
ATOM   1671  NE2 HIS A 230      11.044  31.140  -9.459  1.00 75.72           N  
ATOM   1672  N   ALA A 231      10.945  28.899  -4.606  1.00 59.55           N  
ATOM   1673  CA  ALA A 231      12.250  28.317  -4.282  1.00 61.06           C  
ATOM   1674  C   ALA A 231      12.217  26.786  -4.195  1.00 62.79           C  
ATOM   1675  O   ALA A 231      13.090  26.115  -4.751  1.00 64.09           O  
ATOM   1676  CB  ALA A 231      12.796  28.911  -2.989  1.00 61.90           C  
ATOM   1677  N   ALA A 232      11.208  26.246  -3.509  1.00 60.29           N  
ATOM   1678  CA  ALA A 232      11.058  24.801  -3.345  1.00 58.45           C  
ATOM   1679  C   ALA A 232      10.872  24.102  -4.686  1.00 57.61           C  
ATOM   1680  O   ALA A 232      11.388  23.004  -4.901  1.00 56.96           O  
ATOM   1681  CB  ALA A 232       9.902  24.486  -2.416  1.00 59.26           C  
ATOM   1682  N   LYS A 233      10.146  24.756  -5.586  1.00 58.25           N  
ATOM   1683  CA  LYS A 233       9.951  24.248  -6.938  1.00 59.21           C  
ATOM   1684  C   LYS A 233      11.283  24.234  -7.693  1.00 59.37           C  
ATOM   1685  O   LYS A 233      11.624  23.238  -8.342  1.00 58.66           O  
ATOM   1686  CB  LYS A 233       8.900  25.084  -7.681  1.00 58.61           C  
ATOM   1687  CG  LYS A 233       8.565  24.605  -9.090  1.00 60.26           C  
ATOM   1688  CD  LYS A 233       7.971  23.203  -9.108  1.00 62.42           C  
ATOM   1689  CE  LYS A 233       7.747  22.721 -10.540  1.00 65.91           C  
ATOM   1690  NZ  LYS A 233       7.165  21.343 -10.590  1.00 66.93           N  
ATOM   1691  N   SER A 234      12.034  25.329  -7.584  1.00 57.23           N  
ATOM   1692  CA  SER A 234      13.354  25.438  -8.209  1.00 58.87           C  
ATOM   1693  C   SER A 234      14.325  24.352  -7.735  1.00 58.32           C  
ATOM   1694  O   SER A 234      15.096  23.814  -8.523  1.00 57.17           O  
ATOM   1695  CB  SER A 234      13.950  26.824  -7.961  1.00 60.01           C  
ATOM   1696  OG  SER A 234      13.318  27.793  -8.775  1.00 62.53           O  
ATOM   1697  N   LEU A 235      14.271  24.028  -6.449  1.00 58.85           N  
ATOM   1698  CA  LEU A 235      15.140  23.005  -5.887  1.00 58.40           C  
ATOM   1699  C   LEU A 235      14.686  21.590  -6.191  1.00 57.89           C  
ATOM   1700  O   LEU A 235      15.514  20.677  -6.262  1.00 60.46           O  
ATOM   1701  CB  LEU A 235      15.289  23.196  -4.384  1.00 61.45           C  
ATOM   1702  CG  LEU A 235      16.513  23.997  -3.940  1.00 63.75           C  
ATOM   1703  CD1 LEU A 235      16.524  25.437  -4.468  1.00 62.76           C  
ATOM   1704  CD2 LEU A 235      16.528  23.996  -2.448  1.00 66.71           C  
ATOM   1705  N   ALA A 236      13.380  21.400  -6.351  1.00 55.54           N  
ATOM   1706  CA  ALA A 236      12.853  20.103  -6.763  1.00 53.69           C  
ATOM   1707  C   ALA A 236      13.313  19.779  -8.186  1.00 53.70           C  
ATOM   1708  O   ALA A 236      13.652  18.636  -8.489  1.00 56.07           O  
ATOM   1709  CB  ALA A 236      11.331  20.076  -6.659  1.00 52.29           C  
ATOM   1710  N   ILE A 237      13.347  20.793  -9.045  1.00 53.58           N  
ATOM   1711  CA  ILE A 237      13.807  20.620 -10.423  1.00 56.57           C  
ATOM   1712  C   ILE A 237      15.297  20.222 -10.466  1.00 56.80           C  
ATOM   1713  O   ILE A 237      15.653  19.207 -11.070  1.00 56.45           O  
ATOM   1714  CB  ILE A 237      13.492  21.872 -11.300  1.00 57.14           C  
ATOM   1715  CG1 ILE A 237      11.974  21.991 -11.503  1.00 58.99           C  
ATOM   1716  CG2 ILE A 237      14.182  21.773 -12.657  1.00 57.46           C  
ATOM   1717  CD1 ILE A 237      11.501  23.309 -12.091  1.00 58.34           C  
ATOM   1718  N   ILE A 238      16.142  21.014  -9.804  1.00 55.69           N  
ATOM   1719  CA  ILE A 238      17.574  20.732  -9.672  1.00 57.07           C  
ATOM   1720  C   ILE A 238      17.852  19.292  -9.221  1.00 60.03           C  
ATOM   1721  O   ILE A 238      18.626  18.574  -9.863  1.00 60.19           O  
ATOM   1722  CB  ILE A 238      18.254  21.715  -8.677  1.00 56.67           C  
ATOM   1723  CG1 ILE A 238      18.266  23.141  -9.243  1.00 55.84           C  
ATOM   1724  CG2 ILE A 238      19.681  21.257  -8.347  1.00 57.98           C  
ATOM   1725  CD1 ILE A 238      18.743  24.208  -8.259  1.00 54.78           C  
ATOM   1726  N   VAL A 239      17.209  18.889  -8.123  1.00 60.00           N  
ATOM   1727  CA  VAL A 239      17.459  17.599  -7.474  1.00 58.49           C  
ATOM   1728  C   VAL A 239      16.915  16.440  -8.301  1.00 57.67           C  
ATOM   1729  O   VAL A 239      17.600  15.434  -8.480  1.00 58.61           O  
ATOM   1730  CB  VAL A 239      16.869  17.567  -6.030  1.00 59.23           C  
ATOM   1731  CG1 VAL A 239      16.808  16.146  -5.475  1.00 58.78           C  
ATOM   1732  CG2 VAL A 239      17.678  18.446  -5.111  1.00 58.39           C  
ATOM   1733  N   GLY A 240      15.686  16.590  -8.798  1.00 55.70           N  
ATOM   1734  CA  GLY A 240      15.058  15.582  -9.648  1.00 53.27           C  
ATOM   1735  C   GLY A 240      15.881  15.310 -10.893  1.00 54.45           C  
ATOM   1736  O   GLY A 240      16.164  14.157 -11.218  1.00 54.39           O  
ATOM   1737  N   LEU A 241      16.280  16.379 -11.580  1.00 53.61           N  
ATOM   1738  CA  LEU A 241      17.121  16.260 -12.770  1.00 55.22           C  
ATOM   1739  C   LEU A 241      18.511  15.695 -12.471  1.00 55.48           C  
ATOM   1740  O   LEU A 241      19.006  14.826 -13.203  1.00 52.71           O  
ATOM   1741  CB  LEU A 241      17.227  17.600 -13.500  1.00 54.23           C  
ATOM   1742  CG  LEU A 241      15.945  18.011 -14.229  1.00 55.04           C  
ATOM   1743  CD1 LEU A 241      16.063  19.446 -14.692  1.00 54.37           C  
ATOM   1744  CD2 LEU A 241      15.604  17.067 -15.401  1.00 50.21           C  
ATOM   1745  N   PHE A 242      19.119  16.185 -11.390  1.00 53.45           N  
ATOM   1746  CA  PHE A 242      20.437  15.729 -10.949  1.00 52.37           C  
ATOM   1747  C   PHE A 242      20.457  14.227 -10.654  1.00 51.70           C  
ATOM   1748  O   PHE A 242      21.426  13.544 -10.988  1.00 52.56           O  
ATOM   1749  CB  PHE A 242      20.891  16.528  -9.721  1.00 53.91           C  
ATOM   1750  CG  PHE A 242      22.292  16.219  -9.272  1.00 54.57           C  
ATOM   1751  CD1 PHE A 242      22.534  15.208  -8.340  1.00 54.13           C  
ATOM   1752  CD2 PHE A 242      23.372  16.939  -9.775  1.00 54.45           C  
ATOM   1753  CE1 PHE A 242      23.830  14.912  -7.927  1.00 53.43           C  
ATOM   1754  CE2 PHE A 242      24.672  16.652  -9.364  1.00 54.55           C  
ATOM   1755  CZ  PHE A 242      24.899  15.635  -8.435  1.00 52.57           C  
ATOM   1756  N   ALA A 243      19.393  13.717 -10.042  1.00 50.52           N  
ATOM   1757  CA  ALA A 243      19.310  12.291  -9.724  1.00 53.82           C  
ATOM   1758  C   ALA A 243      19.047  11.456 -10.972  1.00 55.38           C  
ATOM   1759  O   ALA A 243      19.596  10.365 -11.136  1.00 57.64           O  
ATOM   1760  CB  ALA A 243      18.245  12.033  -8.664  1.00 52.25           C  
ATOM   1761  N   LEU A 244      18.207  11.985 -11.851  1.00 57.80           N  
ATOM   1762  CA  LEU A 244      17.886  11.341 -13.113  1.00 59.24           C  
ATOM   1763  C   LEU A 244      19.101  11.300 -14.044  1.00 58.99           C  
ATOM   1764  O   LEU A 244      19.283  10.341 -14.793  1.00 61.02           O  
ATOM   1765  CB  LEU A 244      16.734  12.088 -13.785  1.00 60.66           C  
ATOM   1766  CG  LEU A 244      15.842  11.336 -14.765  1.00 62.01           C  
ATOM   1767  CD1 LEU A 244      14.764  10.560 -14.015  1.00 62.38           C  
ATOM   1768  CD2 LEU A 244      15.215  12.327 -15.732  1.00 63.45           C  
ATOM   1769  N   CYS A 245      19.931  12.336 -13.993  1.00 57.45           N  
ATOM   1770  CA  CYS A 245      21.101  12.417 -14.871  1.00 57.47           C  
ATOM   1771  C   CYS A 245      22.300  11.605 -14.381  1.00 55.84           C  
ATOM   1772  O   CYS A 245      22.981  10.958 -15.182  1.00 55.05           O  
ATOM   1773  CB  CYS A 245      21.514  13.873 -15.098  1.00 58.91           C  
ATOM   1774  SG  CYS A 245      20.346  14.820 -16.101  1.00 58.30           S  
ATOM   1775  N   TRP A 246      22.546  11.631 -13.072  1.00 52.02           N  
ATOM   1776  CA  TRP A 246      23.773  11.056 -12.506  1.00 50.16           C  
ATOM   1777  C   TRP A 246      23.683   9.632 -11.945  1.00 49.67           C  
ATOM   1778  O   TRP A 246      24.647   8.874 -12.050  1.00 47.39           O  
ATOM   1779  CB  TRP A 246      24.365  11.999 -11.457  1.00 48.29           C  
ATOM   1780  CG  TRP A 246      25.067  13.189 -12.058  1.00 47.18           C  
ATOM   1781  CD1 TRP A 246      24.643  14.486 -12.041  1.00 45.71           C  
ATOM   1782  CD2 TRP A 246      26.316  13.185 -12.768  1.00 45.61           C  
ATOM   1783  NE1 TRP A 246      25.550  15.290 -12.692  1.00 45.26           N  
ATOM   1784  CE2 TRP A 246      26.587  14.518 -13.144  1.00 44.69           C  
ATOM   1785  CE3 TRP A 246      27.234  12.185 -13.114  1.00 45.88           C  
ATOM   1786  CZ2 TRP A 246      27.738  14.879 -13.847  1.00 44.54           C  
ATOM   1787  CZ3 TRP A 246      28.382  12.546 -13.820  1.00 44.42           C  
ATOM   1788  CH2 TRP A 246      28.617  13.880 -14.182  1.00 44.53           C  
ATOM   1789  N   LEU A 247      22.547   9.268 -11.352  1.00 51.70           N  
ATOM   1790  CA  LEU A 247      22.419   7.955 -10.704  1.00 53.35           C  
ATOM   1791  C   LEU A 247      22.503   6.740 -11.641  1.00 56.27           C  
ATOM   1792  O   LEU A 247      23.143   5.752 -11.277  1.00 60.66           O  
ATOM   1793  CB  LEU A 247      21.166   7.865  -9.830  1.00 53.10           C  
ATOM   1794  CG  LEU A 247      21.067   8.728  -8.567  1.00 54.56           C  
ATOM   1795  CD1 LEU A 247      19.683   8.543  -7.925  1.00 52.34           C  
ATOM   1796  CD2 LEU A 247      22.185   8.437  -7.560  1.00 49.88           C  
ATOM   1797  N   PRO A 248      21.870   6.794 -12.838  1.00 54.94           N  
ATOM   1798  CA  PRO A 248      21.927   5.594 -13.689  1.00 53.93           C  
ATOM   1799  C   PRO A 248      23.350   5.109 -13.999  1.00 51.99           C  
ATOM   1800  O   PRO A 248      23.631   3.922 -13.844  1.00 53.81           O  
ATOM   1801  CB  PRO A 248      21.193   6.029 -14.962  1.00 54.39           C  
ATOM   1802  CG  PRO A 248      20.228   7.064 -14.482  1.00 54.29           C  
ATOM   1803  CD  PRO A 248      20.982   7.822 -13.418  1.00 54.07           C  
ATOM   1804  N   LEU A 249      24.238   6.016 -14.399  1.00 50.23           N  
ATOM   1805  CA  LEU A 249      25.629   5.655 -14.697  1.00 51.54           C  
ATOM   1806  C   LEU A 249      26.369   5.085 -13.482  1.00 53.37           C  
ATOM   1807  O   LEU A 249      27.111   4.101 -13.597  1.00 54.57           O  
ATOM   1808  CB  LEU A 249      26.403   6.852 -15.280  1.00 49.67           C  
ATOM   1809  CG  LEU A 249      27.871   6.605 -15.674  1.00 49.00           C  
ATOM   1810  CD1 LEU A 249      28.028   5.406 -16.610  1.00 46.99           C  
ATOM   1811  CD2 LEU A 249      28.505   7.843 -16.284  1.00 48.90           C  
ATOM   1812  N   HIS A 250      26.169   5.705 -12.322  1.00 53.50           N  
ATOM   1813  CA  HIS A 250      26.857   5.271 -11.113  1.00 52.96           C  
ATOM   1814  C   HIS A 250      26.269   3.994 -10.522  1.00 51.63           C  
ATOM   1815  O   HIS A 250      27.012   3.143 -10.029  1.00 48.89           O  
ATOM   1816  CB  HIS A 250      26.940   6.414 -10.103  1.00 54.40           C  
ATOM   1817  CG  HIS A 250      27.891   7.492 -10.518  1.00 54.98           C  
ATOM   1818  ND1 HIS A 250      29.198   7.539 -10.086  1.00 55.17           N  
ATOM   1819  CD2 HIS A 250      27.741   8.531 -11.375  1.00 55.66           C  
ATOM   1820  CE1 HIS A 250      29.805   8.575 -10.639  1.00 56.50           C  
ATOM   1821  NE2 HIS A 250      28.943   9.192 -11.427  1.00 55.34           N  
ATOM   1822  N   ILE A 251      24.950   3.840 -10.611  1.00 50.37           N  
ATOM   1823  CA  ILE A 251      24.309   2.575 -10.245  1.00 52.84           C  
ATOM   1824  C   ILE A 251      24.817   1.439 -11.144  1.00 54.14           C  
ATOM   1825  O   ILE A 251      25.114   0.343 -10.661  1.00 54.41           O  
ATOM   1826  CB  ILE A 251      22.766   2.675 -10.269  1.00 53.95           C  
ATOM   1827  CG1 ILE A 251      22.274   3.530  -9.094  1.00 54.52           C  
ATOM   1828  CG2 ILE A 251      22.124   1.289 -10.205  1.00 54.73           C  
ATOM   1829  CD1 ILE A 251      20.849   4.058  -9.270  1.00 56.27           C  
ATOM   1830  N   ILE A 252      24.940   1.707 -12.444  1.00 54.19           N  
ATOM   1831  CA  ILE A 252      25.537   0.738 -13.362  1.00 54.81           C  
ATOM   1832  C   ILE A 252      26.951   0.362 -12.910  1.00 55.02           C  
ATOM   1833  O   ILE A 252      27.292  -0.824 -12.856  1.00 55.68           O  
ATOM   1834  CB  ILE A 252      25.535   1.238 -14.829  1.00 55.34           C  
ATOM   1835  CG1 ILE A 252      24.123   1.142 -15.414  1.00 54.57           C  
ATOM   1836  CG2 ILE A 252      26.514   0.427 -15.683  1.00 54.63           C  
ATOM   1837  CD1 ILE A 252      23.891   2.006 -16.644  1.00 54.18           C  
ATOM   1838  N   ASN A 253      27.762   1.370 -12.580  1.00 54.47           N  
ATOM   1839  CA  ASN A 253      29.116   1.148 -12.056  1.00 52.15           C  
ATOM   1840  C   ASN A 253      29.139   0.219 -10.828  1.00 52.52           C  
ATOM   1841  O   ASN A 253      30.021  -0.629 -10.707  1.00 52.35           O  
ATOM   1842  CB  ASN A 253      29.809   2.487 -11.748  1.00 51.91           C  
ATOM   1843  CG  ASN A 253      30.403   3.159 -12.997  1.00 50.25           C  
ATOM   1844  OD1 ASN A 253      30.583   2.529 -14.036  1.00 52.28           O  
ATOM   1845  ND2 ASN A 253      30.723   4.439 -12.882  1.00 46.00           N  
ATOM   1846  N   CYS A 254      28.153   0.365  -9.943  1.00 53.30           N  
ATOM   1847  CA  CYS A 254      28.016  -0.502  -8.767  1.00 55.57           C  
ATOM   1848  C   CYS A 254      27.700  -1.945  -9.134  1.00 59.17           C  
ATOM   1849  O   CYS A 254      28.258  -2.876  -8.540  1.00 59.71           O  
ATOM   1850  CB  CYS A 254      26.952   0.035  -7.816  1.00 54.62           C  
ATOM   1851  SG  CYS A 254      27.371   1.646  -7.139  1.00 57.36           S  
ATOM   1852  N   PHE A 255      26.809  -2.126 -10.109  1.00 61.84           N  
ATOM   1853  CA  PHE A 255      26.505  -3.450 -10.651  1.00 64.51           C  
ATOM   1854  C   PHE A 255      27.769  -4.128 -11.188  1.00 63.86           C  
ATOM   1855  O   PHE A 255      28.037  -5.290 -10.873  1.00 66.66           O  
ATOM   1856  CB  PHE A 255      25.431  -3.358 -11.745  1.00 69.91           C  
ATOM   1857  CG  PHE A 255      25.272  -4.622 -12.555  1.00 74.38           C  
ATOM   1858  CD1 PHE A 255      24.474  -5.666 -12.092  1.00 77.35           C  
ATOM   1859  CD2 PHE A 255      25.921  -4.766 -13.782  1.00 77.99           C  
ATOM   1860  CE1 PHE A 255      24.327  -6.837 -12.838  1.00 80.20           C  
ATOM   1861  CE2 PHE A 255      25.783  -5.933 -14.535  1.00 81.20           C  
ATOM   1862  CZ  PHE A 255      24.981  -6.969 -14.064  1.00 81.95           C  
ATOM   1863  N   THR A 256      28.539  -3.391 -11.988  1.00 61.06           N  
ATOM   1864  CA  THR A 256      29.785  -3.893 -12.571  1.00 60.71           C  
ATOM   1865  C   THR A 256      30.777  -4.317 -11.490  1.00 64.26           C  
ATOM   1866  O   THR A 256      31.437  -5.351 -11.614  1.00 65.80           O  
ATOM   1867  CB  THR A 256      30.453  -2.826 -13.462  1.00 58.63           C  
ATOM   1868  OG1 THR A 256      29.474  -2.246 -14.332  1.00 58.18           O  
ATOM   1869  CG2 THR A 256      31.589  -3.427 -14.286  1.00 55.43           C  
ATOM   1870  N   PHE A 257      30.875  -3.514 -10.432  1.00 64.98           N  
ATOM   1871  CA  PHE A 257      31.832  -3.773  -9.362  1.00 67.31           C  
ATOM   1872  C   PHE A 257      31.412  -4.924  -8.449  1.00 70.61           C  
ATOM   1873  O   PHE A 257      32.246  -5.748  -8.067  1.00 69.96           O  
ATOM   1874  CB  PHE A 257      32.082  -2.507  -8.543  1.00 62.81           C  
ATOM   1875  CG  PHE A 257      33.129  -2.670  -7.485  1.00 60.04           C  
ATOM   1876  CD1 PHE A 257      34.475  -2.769  -7.829  1.00 58.69           C  
ATOM   1877  CD2 PHE A 257      32.771  -2.724  -6.138  1.00 60.92           C  
ATOM   1878  CE1 PHE A 257      35.455  -2.925  -6.846  1.00 58.09           C  
ATOM   1879  CE2 PHE A 257      33.741  -2.878  -5.145  1.00 58.27           C  
ATOM   1880  CZ  PHE A 257      35.086  -2.978  -5.501  1.00 58.55           C  
ATOM   1881  N   PHE A 258      30.128  -4.976  -8.104  1.00 74.67           N  
ATOM   1882  CA  PHE A 258      29.632  -5.992  -7.179  1.00 79.00           C  
ATOM   1883  C   PHE A 258      29.237  -7.298  -7.858  1.00 84.45           C  
ATOM   1884  O   PHE A 258      29.049  -8.308  -7.180  1.00 86.21           O  
ATOM   1885  CB  PHE A 258      28.495  -5.445  -6.309  1.00 78.18           C  
ATOM   1886  CG  PHE A 258      28.947  -4.424  -5.298  1.00 76.58           C  
ATOM   1887  CD1 PHE A 258      29.895  -4.752  -4.333  1.00 74.92           C  
ATOM   1888  CD2 PHE A 258      28.437  -3.129  -5.321  1.00 76.99           C  
ATOM   1889  CE1 PHE A 258      30.324  -3.811  -3.402  1.00 75.34           C  
ATOM   1890  CE2 PHE A 258      28.856  -2.179  -4.392  1.00 78.06           C  
ATOM   1891  CZ  PHE A 258      29.802  -2.521  -3.430  1.00 77.07           C  
ATOM   1892  N   CYS A 259      29.120  -7.289  -9.184  1.00 92.58           N  
ATOM   1893  CA  CYS A 259      28.964  -8.543  -9.927  1.00 99.23           C  
ATOM   1894  C   CYS A 259      30.070  -8.746 -10.968  1.00100.94           C  
ATOM   1895  O   CYS A 259      29.875  -8.453 -12.153  1.00 99.38           O  
ATOM   1896  CB  CYS A 259      27.573  -8.681 -10.561  1.00101.31           C  
ATOM   1897  SG  CYS A 259      27.164 -10.426 -10.862  1.00118.90           S  
ATOM   1898  N   PRO A 260      31.239  -9.251 -10.525  1.00103.97           N  
ATOM   1899  CA  PRO A 260      32.358  -9.488 -11.442  1.00107.20           C  
ATOM   1900  C   PRO A 260      32.118 -10.675 -12.379  1.00108.69           C  
ATOM   1901  O   PRO A 260      32.724 -10.744 -13.451  1.00109.07           O  
ATOM   1902  CB  PRO A 260      33.530  -9.774 -10.498  1.00107.76           C  
ATOM   1903  CG  PRO A 260      32.898 -10.307  -9.259  1.00106.78           C  
ATOM   1904  CD  PRO A 260      31.578  -9.608  -9.133  1.00103.75           C  
ATOM   1905  N   ASP A 261      31.240 -11.590 -11.969  1.00110.78           N  
ATOM   1906  CA  ASP A 261      30.908 -12.780 -12.757  1.00112.72           C  
ATOM   1907  C   ASP A 261      29.823 -12.519 -13.804  1.00111.86           C  
ATOM   1908  O   ASP A 261      29.800 -13.174 -14.849  1.00115.57           O  
ATOM   1909  CB  ASP A 261      30.496 -13.936 -11.840  1.00114.10           C  
ATOM   1910  CG  ASP A 261      31.654 -14.471 -11.008  1.00118.20           C  
ATOM   1911  OD1 ASP A 261      32.829 -14.250 -11.381  1.00117.40           O  
ATOM   1912  OD2 ASP A 261      31.386 -15.124  -9.977  1.00119.86           O1-
ATOM   1913  N   CYS A 262      28.930 -11.572 -13.513  1.00108.43           N  
ATOM   1914  CA  CYS A 262      27.895 -11.139 -14.454  1.00101.41           C  
ATOM   1915  C   CYS A 262      28.507 -10.629 -15.748  1.00 95.54           C  
ATOM   1916  O   CYS A 262      29.554  -9.977 -15.732  1.00 92.45           O  
ATOM   1917  CB  CYS A 262      27.065 -10.004 -13.856  1.00105.41           C  
ATOM   1918  SG  CYS A 262      25.966 -10.445 -12.507  1.00116.28           S  
ATOM   1919  N   SER A 263      27.852 -10.925 -16.867  1.00 92.57           N  
ATOM   1920  CA  SER A 263      28.215 -10.313 -18.140  1.00 88.98           C  
ATOM   1921  C   SER A 263      27.932  -8.816 -18.054  1.00 85.36           C  
ATOM   1922  O   SER A 263      26.961  -8.387 -17.417  1.00 83.20           O  
ATOM   1923  CB  SER A 263      27.455 -10.954 -19.305  1.00 89.56           C  
ATOM   1924  OG  SER A 263      26.064 -11.006 -19.047  1.00 92.61           O  
ATOM   1925  N   HIS A 264      28.796  -8.028 -18.681  1.00 78.90           N  
ATOM   1926  CA  HIS A 264      28.750  -6.580 -18.554  1.00 74.74           C  
ATOM   1927  C   HIS A 264      27.431  -6.000 -19.058  1.00 75.27           C  
ATOM   1928  O   HIS A 264      26.838  -6.520 -20.002  1.00 78.57           O  
ATOM   1929  CB  HIS A 264      29.925  -5.959 -19.302  1.00 70.88           C  
ATOM   1930  CG  HIS A 264      30.289  -4.590 -18.822  1.00 71.91           C  
ATOM   1931  ND1 HIS A 264      29.566  -3.467 -19.157  1.00 70.90           N  
ATOM   1932  CD2 HIS A 264      31.309  -4.162 -18.041  1.00 72.07           C  
ATOM   1933  CE1 HIS A 264      30.119  -2.406 -18.597  1.00 72.21           C  
ATOM   1934  NE2 HIS A 264      31.181  -2.800 -17.918  1.00 71.93           N  
ATOM   1935  N   ALA A 265      26.972  -4.932 -18.408  1.00 76.18           N  
ATOM   1936  CA  ALA A 265      25.797  -4.191 -18.850  1.00 74.96           C  
ATOM   1937  C   ALA A 265      25.998  -3.741 -20.293  1.00 78.18           C  
ATOM   1938  O   ALA A 265      27.067  -3.224 -20.630  1.00 80.15           O  
ATOM   1939  CB  ALA A 265      25.555  -2.994 -17.949  1.00 75.92           C  
ATOM   1940  N   PRO A 266      24.976  -3.949 -21.152  1.00 79.13           N  
ATOM   1941  CA  PRO A 266      25.053  -3.666 -22.588  1.00 77.37           C  
ATOM   1942  C   PRO A 266      25.654  -2.308 -22.933  1.00 75.96           C  
ATOM   1943  O   PRO A 266      25.447  -1.326 -22.217  1.00 77.45           O  
ATOM   1944  CB  PRO A 266      23.586  -3.734 -23.047  1.00 76.64           C  
ATOM   1945  CG  PRO A 266      22.764  -3.896 -21.797  1.00 77.59           C  
ATOM   1946  CD  PRO A 266      23.667  -4.520 -20.796  1.00 78.22           C  
ATOM   1947  N   LEU A 267      26.384  -2.275 -24.042  1.00 76.03           N  
ATOM   1948  CA  LEU A 267      27.069  -1.080 -24.528  1.00 75.98           C  
ATOM   1949  C   LEU A 267      26.133   0.089 -24.853  1.00 73.94           C  
ATOM   1950  O   LEU A 267      26.533   1.250 -24.738  1.00 77.46           O  
ATOM   1951  CB  LEU A 267      27.921  -1.447 -25.748  1.00 78.34           C  
ATOM   1952  CG  LEU A 267      28.982  -0.512 -26.336  1.00 81.71           C  
ATOM   1953  CD1 LEU A 267      29.822   0.175 -25.265  1.00 82.92           C  
ATOM   1954  CD2 LEU A 267      29.867  -1.306 -27.293  1.00 81.77           C  
ATOM   1955  N   TRP A 268      24.898  -0.210 -25.258  1.00 71.19           N  
ATOM   1956  CA  TRP A 268      23.921   0.842 -25.572  1.00 69.44           C  
ATOM   1957  C   TRP A 268      23.448   1.534 -24.294  1.00 68.33           C  
ATOM   1958  O   TRP A 268      23.187   2.738 -24.290  1.00 65.42           O  
ATOM   1959  CB  TRP A 268      22.726   0.297 -26.381  1.00 67.53           C  
ATOM   1960  CG  TRP A 268      21.801  -0.599 -25.596  1.00 66.85           C  
ATOM   1961  CD1 TRP A 268      21.838  -1.961 -25.535  1.00 67.01           C  
ATOM   1962  CD2 TRP A 268      20.710  -0.190 -24.755  1.00 67.19           C  
ATOM   1963  NE1 TRP A 268      20.844  -2.428 -24.708  1.00 68.16           N  
ATOM   1964  CE2 TRP A 268      20.138  -1.363 -24.214  1.00 67.47           C  
ATOM   1965  CE3 TRP A 268      20.166   1.055 -24.403  1.00 68.23           C  
ATOM   1966  CZ2 TRP A 268      19.043  -1.331 -23.342  1.00 67.82           C  
ATOM   1967  CZ3 TRP A 268      19.077   1.086 -23.532  1.00 68.14           C  
ATOM   1968  CH2 TRP A 268      18.527  -0.102 -23.015  1.00 67.81           C  
ATOM   1969  N   LEU A 269      23.338   0.758 -23.216  1.00 67.76           N  
ATOM   1970  CA  LEU A 269      22.961   1.293 -21.911  1.00 67.74           C  
ATOM   1971  C   LEU A 269      24.093   2.156 -21.345  1.00 67.49           C  
ATOM   1972  O   LEU A 269      23.837   3.187 -20.713  1.00 65.96           O  
ATOM   1973  CB  LEU A 269      22.600   0.156 -20.954  1.00 66.97           C  
ATOM   1974  CG  LEU A 269      22.024   0.485 -19.574  1.00 67.56           C  
ATOM   1975  CD1 LEU A 269      20.747   1.316 -19.660  1.00 65.79           C  
ATOM   1976  CD2 LEU A 269      21.780  -0.808 -18.794  1.00 67.54           C  
ATOM   1977  N   MET A 270      25.336   1.740 -21.595  1.00 63.57           N  
ATOM   1978  CA  MET A 270      26.501   2.527 -21.205  1.00 64.41           C  
ATOM   1979  C   MET A 270      26.444   3.911 -21.851  1.00 66.04           C  
ATOM   1980  O   MET A 270      26.504   4.926 -21.144  1.00 65.96           O  
ATOM   1981  CB  MET A 270      27.817   1.811 -21.556  1.00 62.90           C  
ATOM   1982  CG  MET A 270      28.114   0.521 -20.760  1.00 65.46           C  
ATOM   1983  SD  MET A 270      28.142   0.648 -18.939  1.00 63.96           S  
ATOM   1984  CE  MET A 270      29.359   1.938 -18.677  1.00 61.87           C  
ATOM   1985  N   TYR A 271      26.303   3.941 -23.181  1.00 67.06           N  
ATOM   1986  CA  TYR A 271      26.255   5.192 -23.951  1.00 65.99           C  
ATOM   1987  C   TYR A 271      25.101   6.089 -23.528  1.00 61.26           C  
ATOM   1988  O   TYR A 271      25.265   7.304 -23.411  1.00 62.59           O  
ATOM   1989  CB  TYR A 271      26.162   4.920 -25.455  1.00 76.00           C  
ATOM   1990  CG  TYR A 271      27.393   4.293 -26.077  1.00 83.27           C  
ATOM   1991  CD1 TYR A 271      28.678   4.726 -25.737  1.00 85.60           C  
ATOM   1992  CD2 TYR A 271      27.271   3.286 -27.032  1.00 86.27           C  
ATOM   1993  CE1 TYR A 271      29.810   4.155 -26.320  1.00 87.83           C  
ATOM   1994  CE2 TYR A 271      28.393   2.710 -27.621  1.00 89.12           C  
ATOM   1995  CZ  TYR A 271      29.659   3.147 -27.261  1.00 89.50           C  
ATOM   1996  OH  TYR A 271      30.768   2.574 -27.843  1.00 90.47           O  
ATOM   1997  N   LEU A 272      23.938   5.484 -23.299  1.00 58.37           N  
ATOM   1998  CA  LEU A 272      22.769   6.201 -22.782  1.00 57.23           C  
ATOM   1999  C   LEU A 272      23.040   6.867 -21.422  1.00 57.86           C  
ATOM   2000  O   LEU A 272      22.710   8.042 -21.233  1.00 58.08           O  
ATOM   2001  CB  LEU A 272      21.556   5.265 -22.704  1.00 54.13           C  
ATOM   2002  CG  LEU A 272      20.228   5.803 -22.163  1.00 55.77           C  
ATOM   2003  CD1 LEU A 272      19.700   6.974 -22.983  1.00 54.36           C  
ATOM   2004  CD2 LEU A 272      19.193   4.683 -22.080  1.00 55.37           C  
ATOM   2005  N   ALA A 273      23.656   6.123 -20.499  1.00 57.13           N  
ATOM   2006  CA  ALA A 273      23.962   6.624 -19.149  1.00 57.16           C  
ATOM   2007  C   ALA A 273      25.032   7.723 -19.142  1.00 57.14           C  
ATOM   2008  O   ALA A 273      24.897   8.717 -18.426  1.00 56.13           O  
ATOM   2009  CB  ALA A 273      24.360   5.473 -18.226  1.00 54.97           C  
ATOM   2010  N   ILE A 274      26.081   7.546 -19.946  1.00 57.80           N  
ATOM   2011  CA  ILE A 274      27.125   8.565 -20.103  1.00 58.28           C  
ATOM   2012  C   ILE A 274      26.514   9.864 -20.641  1.00 59.98           C  
ATOM   2013  O   ILE A 274      26.729  10.942 -20.085  1.00 61.30           O  
ATOM   2014  CB  ILE A 274      28.271   8.073 -21.034  1.00 56.75           C  
ATOM   2015  CG1 ILE A 274      29.047   6.920 -20.379  1.00 54.17           C  
ATOM   2016  CG2 ILE A 274      29.209   9.223 -21.396  1.00 54.11           C  
ATOM   2017  CD1 ILE A 274      29.831   6.043 -21.357  1.00 53.31           C  
ATOM   2018  N   VAL A 275      25.743   9.741 -21.720  1.00 63.15           N  
ATOM   2019  CA  VAL A 275      25.027  10.867 -22.326  1.00 63.84           C  
ATOM   2020  C   VAL A 275      24.079  11.534 -21.319  1.00 61.91           C  
ATOM   2021  O   VAL A 275      24.033  12.765 -21.211  1.00 62.42           O  
ATOM   2022  CB  VAL A 275      24.273  10.408 -23.612  1.00 65.58           C  
ATOM   2023  CG1 VAL A 275      23.077  11.300 -23.933  1.00 65.29           C  
ATOM   2024  CG2 VAL A 275      25.232  10.342 -24.790  1.00 66.47           C  
ATOM   2025  N   LEU A 276      23.341  10.710 -20.578  1.00 59.78           N  
ATOM   2026  CA  LEU A 276      22.424  11.195 -19.551  1.00 58.16           C  
ATOM   2027  C   LEU A 276      23.154  12.047 -18.504  1.00 57.43           C  
ATOM   2028  O   LEU A 276      22.685  13.119 -18.138  1.00 55.41           O  
ATOM   2029  CB  LEU A 276      21.700  10.016 -18.895  1.00 57.38           C  
ATOM   2030  CG  LEU A 276      20.235  10.185 -18.481  1.00 59.09           C  
ATOM   2031  CD1 LEU A 276      19.338  10.506 -19.666  1.00 57.67           C  
ATOM   2032  CD2 LEU A 276      19.750   8.921 -17.783  1.00 60.39           C  
ATOM   2033  N   SER A 277      24.317  11.580 -18.050  1.00 58.19           N  
ATOM   2034  CA  SER A 277      25.119  12.325 -17.080  1.00 54.97           C  
ATOM   2035  C   SER A 277      25.580  13.679 -17.625  1.00 55.54           C  
ATOM   2036  O   SER A 277      25.624  14.671 -16.892  1.00 53.65           O  
ATOM   2037  CB  SER A 277      26.296  11.477 -16.579  1.00 53.21           C  
ATOM   2038  OG  SER A 277      27.378  11.446 -17.489  1.00 53.83           O  
ATOM   2039  N   HIS A 278      25.893  13.728 -18.916  1.00 58.03           N  
ATOM   2040  CA  HIS A 278      26.317  14.981 -19.543  1.00 61.19           C  
ATOM   2041  C   HIS A 278      25.179  15.983 -19.733  1.00 60.56           C  
ATOM   2042  O   HIS A 278      25.411  17.196 -19.715  1.00 58.74           O  
ATOM   2043  CB  HIS A 278      27.048  14.716 -20.855  1.00 62.65           C  
ATOM   2044  CG  HIS A 278      28.334  13.972 -20.678  1.00 67.72           C  
ATOM   2045  ND1 HIS A 278      28.662  12.861 -21.422  1.00 71.59           N  
ATOM   2046  CD2 HIS A 278      29.364  14.169 -19.821  1.00 71.43           C  
ATOM   2047  CE1 HIS A 278      29.846  12.415 -21.043  1.00 70.15           C  
ATOM   2048  NE2 HIS A 278      30.291  13.188 -20.069  1.00 69.42           N  
ATOM   2049  N   THR A 279      23.954  15.479 -19.880  1.00 62.77           N  
ATOM   2050  CA  THR A 279      22.786  16.347 -20.026  1.00 65.25           C  
ATOM   2051  C   THR A 279      22.422  17.140 -18.753  1.00 68.02           C  
ATOM   2052  O   THR A 279      21.569  18.032 -18.794  1.00 71.44           O  
ATOM   2053  CB  THR A 279      21.557  15.602 -20.613  1.00 67.24           C  
ATOM   2054  OG1 THR A 279      20.571  16.557 -21.014  1.00 70.23           O  
ATOM   2055  CG2 THR A 279      20.929  14.673 -19.606  1.00 70.35           C  
ATOM   2056  N   ASN A 280      23.075  16.829 -17.634  1.00 67.70           N  
ATOM   2057  CA  ASN A 280      22.950  17.654 -16.429  1.00 64.32           C  
ATOM   2058  C   ASN A 280      23.535  19.047 -16.632  1.00 62.33           C  
ATOM   2059  O   ASN A 280      23.107  20.005 -15.995  1.00 64.09           O  
ATOM   2060  CB  ASN A 280      23.618  16.991 -15.221  1.00 63.13           C  
ATOM   2061  CG  ASN A 280      23.273  17.688 -13.911  1.00 62.30           C  
ATOM   2062  OD1 ASN A 280      22.135  17.639 -13.458  1.00 62.96           O  
ATOM   2063  ND2 ASN A 280      24.255  18.345 -13.305  1.00 61.83           N  
ATOM   2064  N   SER A 281      24.515  19.148 -17.526  1.00 65.60           N  
ATOM   2065  CA  SER A 281      25.202  20.415 -17.802  1.00 65.96           C  
ATOM   2066  C   SER A 281      24.413  21.368 -18.705  1.00 63.61           C  
ATOM   2067  O   SER A 281      24.777  22.536 -18.847  1.00 65.70           O  
ATOM   2068  CB  SER A 281      26.593  20.155 -18.390  1.00 66.09           C  
ATOM   2069  OG  SER A 281      27.471  19.647 -17.400  1.00 65.73           O  
ATOM   2070  N   VAL A 282      23.345  20.870 -19.318  1.00 61.91           N  
ATOM   2071  CA  VAL A 282      22.464  21.729 -20.102  1.00 63.75           C  
ATOM   2072  C   VAL A 282      21.244  22.194 -19.291  1.00 62.60           C  
ATOM   2073  O   VAL A 282      20.820  23.343 -19.413  1.00 64.64           O  
ATOM   2074  CB  VAL A 282      22.090  21.110 -21.496  1.00 63.07           C  
ATOM   2075  CG1 VAL A 282      21.788  19.633 -21.389  1.00 63.77           C  
ATOM   2076  CG2 VAL A 282      20.929  21.862 -22.152  1.00 62.20           C  
ATOM   2077  N   VAL A 283      20.705  21.319 -18.447  1.00 61.28           N  
ATOM   2078  CA  VAL A 283      19.540  21.679 -17.630  1.00 60.45           C  
ATOM   2079  C   VAL A 283      19.906  22.383 -16.315  1.00 63.76           C  
ATOM   2080  O   VAL A 283      19.168  23.261 -15.859  1.00 65.23           O  
ATOM   2081  CB  VAL A 283      18.583  20.478 -17.385  1.00 60.60           C  
ATOM   2082  CG1 VAL A 283      18.038  19.948 -18.717  1.00 60.26           C  
ATOM   2083  CG2 VAL A 283      19.268  19.361 -16.596  1.00 62.26           C  
ATOM   2084  N   ASN A 284      21.043  22.012 -15.722  1.00 62.50           N  
ATOM   2085  CA  ASN A 284      21.510  22.632 -14.477  1.00 60.42           C  
ATOM   2086  C   ASN A 284      22.712  23.537 -14.723  1.00 59.31           C  
ATOM   2087  O   ASN A 284      23.725  23.072 -15.241  1.00 61.85           O  
ATOM   2088  CB  ASN A 284      21.886  21.567 -13.441  1.00 60.88           C  
ATOM   2089  CG  ASN A 284      20.681  20.974 -12.730  1.00 60.99           C  
ATOM   2090  OD1 ASN A 284      19.856  21.695 -12.169  1.00 60.11           O  
ATOM   2091  ND2 ASN A 284      20.596  19.647 -12.720  1.00 59.29           N  
ATOM   2092  N   PRO A 285      22.606  24.832 -14.372  1.00 57.81           N  
ATOM   2093  CA  PRO A 285      21.420  25.482 -13.837  1.00 59.27           C  
ATOM   2094  C   PRO A 285      20.710  26.395 -14.858  1.00 61.75           C  
ATOM   2095  O   PRO A 285      20.345  27.526 -14.511  1.00 60.91           O  
ATOM   2096  CB  PRO A 285      22.010  26.342 -12.724  1.00 54.89           C  
ATOM   2097  CG  PRO A 285      23.335  26.798 -13.308  1.00 55.53           C  
ATOM   2098  CD  PRO A 285      23.758  25.751 -14.335  1.00 55.54           C  
ATOM   2099  N   PHE A 286      20.521  25.937 -16.096  1.00 60.52           N  
ATOM   2100  CA  PHE A 286      19.781  26.757 -17.053  1.00 63.73           C  
ATOM   2101  C   PHE A 286      18.354  26.964 -16.555  1.00 62.44           C  
ATOM   2102  O   PHE A 286      17.940  28.102 -16.315  1.00 63.03           O  
ATOM   2103  CB  PHE A 286      19.782  26.181 -18.477  1.00 67.17           C  
ATOM   2104  CG  PHE A 286      19.045  27.046 -19.473  1.00 72.33           C  
ATOM   2105  CD1 PHE A 286      19.638  28.198 -19.991  1.00 74.32           C  
ATOM   2106  CD2 PHE A 286      17.745  26.725 -19.874  1.00 74.29           C  
ATOM   2107  CE1 PHE A 286      18.952  29.012 -20.907  1.00 74.32           C  
ATOM   2108  CE2 PHE A 286      17.052  27.528 -20.788  1.00 72.84           C  
ATOM   2109  CZ  PHE A 286      17.658  28.675 -21.304  1.00 71.61           C  
ATOM   2110  N   ILE A 287      17.630  25.858 -16.379  1.00 58.69           N  
ATOM   2111  CA  ILE A 287      16.252  25.878 -15.893  1.00 57.71           C  
ATOM   2112  C   ILE A 287      16.097  26.688 -14.602  1.00 60.46           C  
ATOM   2113  O   ILE A 287      15.096  27.385 -14.420  1.00 63.67           O  
ATOM   2114  CB  ILE A 287      15.688  24.453 -15.713  1.00 57.33           C  
ATOM   2115  CG1 ILE A 287      15.723  23.700 -17.055  1.00 55.15           C  
ATOM   2116  CG2 ILE A 287      14.267  24.511 -15.133  1.00 58.48           C  
ATOM   2117  CD1 ILE A 287      15.218  22.264 -17.012  1.00 51.17           C  
ATOM   2118  N   TYR A 288      17.092  26.621 -13.722  1.00 59.93           N  
ATOM   2119  CA  TYR A 288      17.054  27.410 -12.497  1.00 60.32           C  
ATOM   2120  C   TYR A 288      17.014  28.903 -12.821  1.00 64.00           C  
ATOM   2121  O   TYR A 288      16.122  29.618 -12.357  1.00 64.88           O  
ATOM   2122  CB  TYR A 288      18.229  27.068 -11.567  1.00 57.65           C  
ATOM   2123  CG  TYR A 288      18.329  27.985 -10.365  1.00 53.64           C  
ATOM   2124  CD1 TYR A 288      17.500  27.813  -9.261  1.00 52.25           C  
ATOM   2125  CD2 TYR A 288      19.243  29.038 -10.345  1.00 53.85           C  
ATOM   2126  CE1 TYR A 288      17.581  28.663  -8.165  1.00 52.83           C  
ATOM   2127  CE2 TYR A 288      19.332  29.893  -9.252  1.00 52.21           C  
ATOM   2128  CZ  TYR A 288      18.500  29.700  -8.171  1.00 52.71           C  
ATOM   2129  OH  TYR A 288      18.591  30.551  -7.094  1.00 57.04           O  
ATOM   2130  N   ALA A 289      17.976  29.357 -13.625  1.00 67.81           N  
ATOM   2131  CA  ALA A 289      18.068  30.758 -14.043  1.00 66.03           C  
ATOM   2132  C   ALA A 289      16.830  31.181 -14.835  1.00 66.35           C  
ATOM   2133  O   ALA A 289      16.246  32.234 -14.569  1.00 61.15           O  
ATOM   2134  CB  ALA A 289      19.340  30.990 -14.856  1.00 62.89           C  
ATOM   2135  N   TYR A 290      16.429  30.334 -15.783  1.00 68.81           N  
ATOM   2136  CA  TYR A 290      15.254  30.569 -16.623  1.00 76.21           C  
ATOM   2137  C   TYR A 290      13.965  30.806 -15.824  1.00 77.12           C  
ATOM   2138  O   TYR A 290      12.988  31.333 -16.356  1.00 80.14           O  
ATOM   2139  CB  TYR A 290      15.064  29.404 -17.602  1.00 82.01           C  
ATOM   2140  CG  TYR A 290      13.868  29.547 -18.527  1.00 91.89           C  
ATOM   2141  CD1 TYR A 290      13.886  30.451 -19.593  1.00 93.53           C  
ATOM   2142  CD2 TYR A 290      12.719  28.774 -18.339  1.00 95.34           C  
ATOM   2143  CE1 TYR A 290      12.793  30.584 -20.441  1.00 96.97           C  
ATOM   2144  CE2 TYR A 290      11.621  28.899 -19.184  1.00 96.83           C  
ATOM   2145  CZ  TYR A 290      11.666  29.806 -20.230  1.00 98.09           C  
ATOM   2146  OH  TYR A 290      10.585  29.934 -21.068  1.00102.22           O  
ATOM   2147  N   ARG A 291      13.974  30.419 -14.551  1.00 74.47           N  
ATOM   2148  CA  ARG A 291      12.810  30.560 -13.685  1.00 69.29           C  
ATOM   2149  C   ARG A 291      12.878  31.811 -12.814  1.00 71.49           C  
ATOM   2150  O   ARG A 291      12.027  32.019 -11.946  1.00 73.03           O  
ATOM   2151  CB  ARG A 291      12.634  29.312 -12.823  1.00 64.87           C  
ATOM   2152  CG  ARG A 291      12.056  28.111 -13.559  1.00 60.24           C  
ATOM   2153  CD  ARG A 291      11.987  26.908 -12.632  1.00 61.19           C  
ATOM   2154  NE  ARG A 291      11.520  27.294 -11.297  1.00 63.35           N  
ATOM   2155  CZ  ARG A 291      10.243  27.344 -10.924  1.00 60.60           C  
ATOM   2156  NH1 ARG A 291       9.278  27.010 -11.771  1.00 57.62           N  
ATOM   2157  NH2 ARG A 291       9.934  27.715  -9.692  1.00 62.40           N  
ATOM   2158  N   ILE A 292      13.904  32.628 -13.031  1.00 75.70           N  
ATOM   2159  CA  ILE A 292      13.935  33.981 -12.481  1.00 81.68           C  
ATOM   2160  C   ILE A 292      13.556  34.923 -13.623  1.00 85.87           C  
ATOM   2161  O   ILE A 292      14.209  34.924 -14.674  1.00 88.92           O  
ATOM   2162  CB  ILE A 292      15.322  34.362 -11.880  1.00 80.48           C  
ATOM   2163  CG1 ILE A 292      15.670  33.470 -10.687  1.00 82.76           C  
ATOM   2164  CG2 ILE A 292      15.351  35.819 -11.428  1.00 77.68           C  
ATOM   2165  CD1 ILE A 292      16.730  32.434 -10.977  1.00 83.32           C  
ATOM   2166  N   ARG A 293      12.494  35.704 -13.424  1.00 88.35           N  
ATOM   2167  CA  ARG A 293      11.973  36.587 -14.477  1.00 90.33           C  
ATOM   2168  C   ARG A 293      13.049  37.490 -15.084  1.00 86.40           C  
ATOM   2169  O   ARG A 293      13.172  37.574 -16.308  1.00 81.27           O  
ATOM   2170  CB  ARG A 293      10.761  37.400 -13.990  1.00 95.49           C  
ATOM   2171  CG  ARG A 293      10.952  38.168 -12.682  1.00101.06           C  
ATOM   2172  CD  ARG A 293       9.768  39.083 -12.384  1.00103.10           C  
ATOM   2173  NE  ARG A 293       9.789  40.299 -13.198  1.00107.79           N  
ATOM   2174  CZ  ARG A 293       9.124  40.464 -14.341  1.00111.59           C  
ATOM   2175  NH1 ARG A 293       8.365  39.491 -14.833  1.00112.20           N  
ATOM   2176  NH2 ARG A 293       9.219  41.613 -14.998  1.00111.60           N  
ATOM   2177  N   GLU A 294      13.837  38.129 -14.217  1.00 84.91           N  
ATOM   2178  CA  GLU A 294      14.915  39.031 -14.620  1.00 86.60           C  
ATOM   2179  C   GLU A 294      15.902  38.374 -15.593  1.00 89.48           C  
ATOM   2180  O   GLU A 294      16.344  39.005 -16.555  1.00 93.07           O  
ATOM   2181  CB  GLU A 294      15.646  39.558 -13.383  1.00 89.19           C  
ATOM   2182  CG  GLU A 294      16.337  40.908 -13.578  1.00 94.35           C  
ATOM   2183  CD  GLU A 294      15.385  42.098 -13.495  1.00 95.29           C  
ATOM   2184  OE1 GLU A 294      14.398  42.032 -12.728  1.00 93.48           O  
ATOM   2185  OE2 GLU A 294      15.636  43.107 -14.193  1.00 92.20           O1-
ATOM   2186  N   PHE A 295      16.239  37.110 -15.341  1.00 87.09           N  
ATOM   2187  CA  PHE A 295      17.043  36.325 -16.273  1.00 85.72           C  
ATOM   2188  C   PHE A 295      16.269  36.038 -17.553  1.00 88.65           C  
ATOM   2189  O   PHE A 295      16.805  36.177 -18.655  1.00 90.10           O  
ATOM   2190  CB  PHE A 295      17.474  34.993 -15.643  1.00 83.27           C  
ATOM   2191  CG  PHE A 295      18.842  35.018 -15.029  1.00 79.83           C  
ATOM   2192  CD1 PHE A 295      19.978  34.831 -15.815  1.00 80.50           C  
ATOM   2193  CD2 PHE A 295      18.999  35.207 -13.660  1.00 77.71           C  
ATOM   2194  CE1 PHE A 295      21.253  34.850 -15.245  1.00 78.43           C  
ATOM   2195  CE2 PHE A 295      20.267  35.226 -13.081  1.00 75.60           C  
ATOM   2196  CZ  PHE A 295      21.394  35.048 -13.872  1.00 75.06           C  
ATOM   2197  N   ARG A 296      15.009  35.634 -17.393  1.00 92.28           N  
ATOM   2198  CA  ARG A 296      14.166  35.200 -18.510  1.00 91.16           C  
ATOM   2199  C   ARG A 296      13.893  36.325 -19.510  1.00 87.00           C  
ATOM   2200  O   ARG A 296      13.878  36.092 -20.717  1.00 84.72           O  
ATOM   2201  CB  ARG A 296      12.853  34.611 -17.985  1.00 91.20           C  
ATOM   2202  CG  ARG A 296      12.038  33.843 -19.022  1.00 92.07           C  
ATOM   2203  CD  ARG A 296      10.801  33.190 -18.414  1.00 92.01           C  
ATOM   2204  NE  ARG A 296       9.929  34.160 -17.754  1.00 93.15           N  
ATOM   2205  CZ  ARG A 296       9.819  34.304 -16.436  1.00 96.80           C  
ATOM   2206  NH1 ARG A 296      10.520  33.534 -15.612  1.00 98.12           N  
ATOM   2207  NH2 ARG A 296       9.002  35.221 -15.937  1.00 98.40           N  
ATOM   2208  N   GLN A 297      13.690  37.538 -19.000  1.00 85.49           N  
ATOM   2209  CA  GLN A 297      13.461  38.707 -19.851  1.00 89.85           C  
ATOM   2210  C   GLN A 297      14.726  39.114 -20.604  1.00 88.80           C  
ATOM   2211  O   GLN A 297      14.666  39.446 -21.790  1.00 89.15           O  
ATOM   2212  CB  GLN A 297      12.903  39.881 -19.037  1.00 93.27           C  
ATOM   2213  CG  GLN A 297      11.460  39.673 -18.572  1.00 98.62           C  
ATOM   2214  CD  GLN A 297      10.801  40.937 -18.037  1.00104.37           C  
ATOM   2215  OE1 GLN A 297      11.472  41.901 -17.654  1.00106.22           O  
ATOM   2216  NE2 GLN A 297       9.473  40.933 -18.003  1.00105.79           N  
ATOM   2217  N   THR A 298      15.864  39.073 -19.910  1.00 89.14           N  
ATOM   2218  CA  THR A 298      17.168  39.381 -20.501  1.00 83.79           C  
ATOM   2219  C   THR A 298      17.538  38.362 -21.579  1.00 85.11           C  
ATOM   2220  O   THR A 298      18.143  38.717 -22.592  1.00 85.78           O  
ATOM   2221  CB  THR A 298      18.273  39.462 -19.424  1.00 83.62           C  
ATOM   2222  OG1 THR A 298      17.860  40.351 -18.376  1.00 79.58           O  
ATOM   2223  CG2 THR A 298      19.586  39.972 -20.016  1.00 85.35           C  
ATOM   2224  N   PHE A 299      17.156  37.103 -21.363  1.00 89.39           N  
ATOM   2225  CA  PHE A 299      17.334  36.053 -22.368  1.00 92.67           C  
ATOM   2226  C   PHE A 299      16.582  36.382 -23.652  1.00 93.47           C  
ATOM   2227  O   PHE A 299      17.051  36.067 -24.748  1.00 92.35           O  
ATOM   2228  CB  PHE A 299      16.849  34.690 -21.853  1.00 95.17           C  
ATOM   2229  CG  PHE A 299      17.762  34.040 -20.847  1.00 96.69           C  
ATOM   2230  CD1 PHE A 299      19.113  34.370 -20.775  1.00 97.54           C  
ATOM   2231  CD2 PHE A 299      17.268  33.059 -19.990  1.00 99.74           C  
ATOM   2232  CE1 PHE A 299      19.948  33.754 -19.845  1.00 96.67           C  
ATOM   2233  CE2 PHE A 299      18.097  32.436 -19.059  1.00 98.62           C  
ATOM   2234  CZ  PHE A 299      19.440  32.785 -18.988  1.00 96.94           C  
ATOM   2235  N   ARG A 300      15.409  37.000 -23.507  1.00 97.30           N  
ATOM   2236  CA  ARG A 300      14.576  37.357 -24.655  1.00 98.17           C  
ATOM   2237  C   ARG A 300      15.235  38.441 -25.499  1.00 94.91           C  
ATOM   2238  O   ARG A 300      15.327  38.299 -26.715  1.00 91.32           O  
ATOM   2239  CB  ARG A 300      13.163  37.767 -24.223  1.00102.64           C  
ATOM   2240  CG  ARG A 300      12.330  36.615 -23.657  1.00108.47           C  
ATOM   2241  CD  ARG A 300      10.827  36.840 -23.823  1.00113.32           C  
ATOM   2242  NE  ARG A 300      10.353  38.048 -23.145  1.00116.98           N  
ATOM   2243  CZ  ARG A 300       9.942  38.097 -21.880  1.00117.79           C  
ATOM   2244  NH1 ARG A 300       9.940  37.005 -21.124  1.00116.16           N  
ATOM   2245  NH2 ARG A 300       9.531  39.249 -21.368  1.00120.45           N  
ATOM   2246  N   LYS A 301      15.721  39.497 -24.842  1.00 93.49           N  
ATOM   2247  CA  LYS A 301      16.440  40.591 -25.512  1.00 92.74           C  
ATOM   2248  C   LYS A 301      17.633  40.112 -26.347  1.00 98.79           C  
ATOM   2249  O   LYS A 301      17.933  40.691 -27.395  1.00103.97           O  
ATOM   2250  CB  LYS A 301      16.922  41.639 -24.503  1.00 86.32           C  
ATOM   2251  CG  LYS A 301      15.858  42.147 -23.536  1.00 88.25           C  
ATOM   2252  CD  LYS A 301      16.133  43.584 -23.076  1.00 87.62           C  
ATOM   2253  CE  LYS A 301      17.414  43.718 -22.255  1.00 87.87           C  
ATOM   2254  NZ  LYS A 301      17.341  43.019 -20.937  1.00 86.69           N  
ATOM   2255  N   ILE A 302      18.308  39.062 -25.880  1.00 97.43           N  
ATOM   2256  CA  ILE A 302      19.500  38.538 -26.554  1.00 97.34           C  
ATOM   2257  C   ILE A 302      19.146  37.695 -27.787  1.00100.25           C  
ATOM   2258  O   ILE A 302      19.701  37.913 -28.870  1.00101.34           O  
ATOM   2259  CB  ILE A 302      20.426  37.761 -25.574  1.00 94.30           C  
ATOM   2260  CG1 ILE A 302      20.970  38.713 -24.499  1.00 94.67           C  
ATOM   2261  CG2 ILE A 302      21.576  37.083 -26.323  1.00 90.01           C  
ATOM   2262  CD1 ILE A 302      21.452  38.029 -23.224  1.00 93.68           C  
ATOM   2263  N   ILE A 303      18.225  36.745 -27.620  1.00 98.79           N  
ATOM   2264  CA  ILE A 303      17.774  35.896 -28.729  1.00 99.86           C  
ATOM   2265  C   ILE A 303      16.950  36.715 -29.734  1.00103.30           C  
ATOM   2266  O   ILE A 303      16.977  36.439 -30.936  1.00103.72           O  
ATOM   2267  CB  ILE A 303      16.976  34.652 -28.238  1.00 98.54           C  
ATOM   2268  CG1 ILE A 303      17.714  33.952 -27.092  1.00 98.65           C  
ATOM   2269  CG2 ILE A 303      16.738  33.663 -29.385  1.00 94.91           C  
ATOM   2270  CD1 ILE A 303      16.844  33.022 -26.258  1.00 98.30           C  
ATOM   2271  N   ARG A 304      16.234  37.723 -29.231  1.00103.76           N  
ATOM   2272  CA  ARG A 304      15.486  38.662 -30.070  1.00103.52           C  
ATOM   2273  C   ARG A 304      16.439  39.384 -31.023  1.00104.92           C  
ATOM   2274  O   ARG A 304      16.296  39.286 -32.246  1.00101.24           O  
ATOM   2275  CB  ARG A 304      14.725  39.668 -29.195  1.00103.91           C  
ATOM   2276  CG  ARG A 304      13.602  40.432 -29.889  1.00104.36           C  
ATOM   2277  CD  ARG A 304      12.586  40.972 -28.877  1.00105.82           C  
ATOM   2278  NE  ARG A 304      13.138  42.015 -28.007  1.00110.77           N  
ATOM   2279  CZ  ARG A 304      12.859  43.317 -28.098  1.00112.38           C  
ATOM   2280  NH1 ARG A 304      12.022  43.771 -29.025  1.00113.31           N  
ATOM   2281  NH2 ARG A 304      13.418  44.172 -27.253  1.00110.94           N  
ATOM   2282  N   SER A 305      17.426  40.076 -30.449  1.00103.24           N  
ATOM   2283  CA  SER A 305      18.437  40.814 -31.210  1.00102.16           C  
ATOM   2284  C   SER A 305      19.248  39.918 -32.143  1.00103.39           C  
ATOM   2285  O   SER A 305      19.853  40.400 -33.100  1.00108.77           O  
ATOM   2286  CB  SER A 305      19.374  41.570 -30.267  1.00101.39           C  
ATOM   2287  OG  SER A 305      18.658  42.520 -29.496  1.00103.34           O  
ATOM   2288  N   HIS A 306      19.259  38.621 -31.852  1.00105.53           N  
ATOM   2289  CA  HIS A 306      19.916  37.637 -32.706  1.00105.69           C  
ATOM   2290  C   HIS A 306      19.052  37.308 -33.924  1.00108.18           C  
ATOM   2291  O   HIS A 306      19.577  36.967 -34.984  1.00110.04           O  
ATOM   2292  CB  HIS A 306      20.242  36.365 -31.914  1.00 99.41           C  
ATOM   2293  CG  HIS A 306      20.721  35.228 -32.762  1.00 97.00           C  
ATOM   2294  ND1 HIS A 306      22.020  35.130 -33.212  1.00 97.64           N  
ATOM   2295  CD2 HIS A 306      20.072  34.143 -33.248  1.00 96.77           C  
ATOM   2296  CE1 HIS A 306      22.152  34.032 -33.937  1.00 96.58           C  
ATOM   2297  NE2 HIS A 306      20.984  33.416 -33.974  1.00 95.95           N  
ATOM   2298  N   VAL A 307      17.733  37.416 -33.767  1.00109.79           N  
ATOM   2299  CA  VAL A 307      16.791  37.098 -34.848  1.00112.43           C  
ATOM   2300  C   VAL A 307      16.515  38.308 -35.762  1.00111.84           C  
ATOM   2301  O   VAL A 307      16.469  38.163 -36.989  1.00112.04           O  
ATOM   2302  CB  VAL A 307      15.483  36.448 -34.303  1.00111.19           C  
ATOM   2303  CG1 VAL A 307      14.415  36.337 -35.386  1.00110.38           C  
ATOM   2304  CG2 VAL A 307      15.783  35.067 -33.725  1.00109.50           C  
ATOM   2305  N   LEU A 308      16.359  39.494 -35.171  1.00110.11           N  
ATOM   2306  CA  LEU A 308      16.207  40.728 -35.954  1.00111.33           C  
ATOM   2307  C   LEU A 308      17.525  41.197 -36.596  1.00114.74           C  
ATOM   2308  O   LEU A 308      17.636  42.343 -37.044  1.00115.42           O  
ATOM   2309  CB  LEU A 308      15.535  41.849 -35.135  1.00110.26           C  
ATOM   2310  CG  LEU A 308      16.040  42.335 -33.769  1.00108.40           C  
ATOM   2311  CD1 LEU A 308      17.216  43.307 -33.877  1.00105.79           C  
ATOM   2312  CD2 LEU A 308      14.891  42.992 -33.019  1.00107.35           C  
ATOM   2313  N   ARG A 309      18.507  40.297 -36.644  1.00115.66           N  
ATOM   2314  CA  ARG A 309      19.800  40.558 -37.275  1.00116.61           C  
ATOM   2315  C   ARG A 309      20.294  39.380 -38.120  1.00118.76           C  
ATOM   2316  O   ARG A 309      21.302  39.497 -38.822  1.00122.62           O  
ATOM   2317  CB  ARG A 309      20.851  40.943 -36.228  1.00118.49           C  
ATOM   2318  CG  ARG A 309      20.972  42.442 -35.998  1.00123.83           C  
ATOM   2319  CD  ARG A 309      22.111  42.770 -35.043  1.00126.18           C  
ATOM   2320  NE  ARG A 309      21.643  42.956 -33.669  1.00127.94           N  
ATOM   2321  CZ  ARG A 309      21.450  44.141 -33.092  1.00128.69           C  
ATOM   2322  NH1 ARG A 309      21.690  45.265 -33.759  1.00128.02           N  
ATOM   2323  NH2 ARG A 309      21.020  44.203 -31.838  1.00130.41           N  
ATOM   2324  N   GLN A 310      19.586  38.254 -38.048  1.00117.36           N  
ATOM   2325  CA  GLN A 310      19.898  37.079 -38.868  1.00118.52           C  
ATOM   2326  C   GLN A 310      18.869  36.873 -39.974  1.00118.33           C  
ATOM   2327  O   GLN A 310      19.172  36.282 -41.013  1.00116.72           O  
ATOM   2328  CB  GLN A 310      20.002  35.816 -38.007  1.00119.20           C  
ATOM   2329  CG  GLN A 310      21.378  35.587 -37.382  1.00120.74           C  
ATOM   2330  CD  GLN A 310      22.413  35.069 -38.375  1.00121.64           C  
ATOM   2331  OE1 GLN A 310      22.092  34.312 -39.294  1.00121.87           O  
ATOM   2332  NE2 GLN A 310      23.666  35.472 -38.183  1.00118.43           N  
ATOM   2333  N   GLN A 311      17.655  37.361 -39.739  1.00121.31           N  
ATOM   2334  CA  GLN A 311      16.572  37.262 -40.714  1.00123.55           C  
ATOM   2335  C   GLN A 311      16.607  38.413 -41.722  1.00122.00           C  
ATOM   2336  O   GLN A 311      15.883  38.390 -42.719  1.00119.01           O  
ATOM   2337  CB  GLN A 311      15.212  37.217 -40.004  1.00124.81           C  
ATOM   2338  CG  GLN A 311      14.996  36.004 -39.096  1.00124.29           C  
ATOM   2339  CD  GLN A 311      14.618  34.743 -39.855  1.00126.06           C  
ATOM   2340  OE1 GLN A 311      13.465  34.313 -39.824  1.00127.51           O  
ATOM   2341  NE2 GLN A 311      15.588  34.143 -40.540  1.00125.86           N  
ATOM   2342  N   GLU A 312      17.463  39.401 -41.455  1.00121.69           N  
ATOM   2343  CA  GLU A 312      17.554  40.631 -42.252  1.00118.90           C  
ATOM   2344  C   GLU A 312      17.795  40.411 -43.755  1.00117.86           C  
ATOM   2345  O   GLU A 312      17.088  41.008 -44.569  1.00114.03           O  
ATOM   2346  CB  GLU A 312      18.599  41.589 -41.661  1.00118.05           C  
ATOM   2347  CG  GLU A 312      18.383  43.058 -42.007  1.00121.30           C  
ATOM   2348  CD  GLU A 312      17.197  43.669 -41.277  1.00123.73           C  
ATOM   2349  OE1 GLU A 312      16.044  43.422 -41.690  1.00124.25           O  
ATOM   2350  OE2 GLU A 312      17.419  44.392 -40.284  1.00123.53           O  
ATOM   2351  N   PRO A 313      18.784  39.564 -44.128  1.00118.31           N  
ATOM   2352  CA  PRO A 313      18.974  39.243 -45.550  1.00116.62           C  
ATOM   2353  C   PRO A 313      17.710  38.734 -46.252  1.00115.57           C  
ATOM   2354  O   PRO A 313      17.459  39.098 -47.402  1.00117.32           O  
ATOM   2355  CB  PRO A 313      20.041  38.144 -45.515  1.00115.67           C  
ATOM   2356  CG  PRO A 313      20.847  38.468 -44.319  1.00113.94           C  
ATOM   2357  CD  PRO A 313      19.868  38.991 -43.303  1.00115.96           C  
ATOM   2358  N   PHE A 314      16.928  37.910 -45.558  1.00115.46           N  
ATOM   2359  CA  PHE A 314      15.715  37.315 -46.124  1.00112.91           C  
ATOM   2360  C   PHE A 314      14.495  38.231 -46.005  1.00107.33           C  
ATOM   2361  O   PHE A 314      13.556  38.126 -46.797  1.00105.64           O  
ATOM   2362  CB  PHE A 314      15.440  35.948 -45.483  1.00116.09           C  
ATOM   2363  CG  PHE A 314      16.478  34.907 -45.810  1.00120.46           C  
ATOM   2364  CD1 PHE A 314      16.352  34.112 -46.948  1.00122.35           C  
ATOM   2365  CD2 PHE A 314      17.587  34.726 -44.986  1.00121.59           C  
ATOM   2366  CE1 PHE A 314      17.314  33.150 -47.261  1.00123.24           C  
ATOM   2367  CE2 PHE A 314      18.555  33.767 -45.290  1.00122.24           C  
ATOM   2368  CZ  PHE A 314      18.417  32.977 -46.429  1.00123.57           C  
ATOM   2369  N   LYS A 315      14.523  39.122 -45.015  1.00102.75           N  
ATOM   2370  CA  LYS A 315      13.467  40.114 -44.806  1.00 98.88           C  
ATOM   2371  C   LYS A 315      13.541  41.205 -45.877  1.00 97.60           C  
ATOM   2372  O   LYS A 315      12.523  41.579 -46.470  1.00 93.71           O  
ATOM   2373  CB  LYS A 315      13.590  40.730 -43.408  1.00 96.86           C  
ATOM   2374  CG  LYS A 315      12.444  41.647 -43.009  1.00 97.19           C  
ATOM   2375  CD  LYS A 315      12.831  42.516 -41.820  1.00 98.14           C  
ATOM   2376  CE  LYS A 315      11.638  43.261 -41.254  1.00 97.49           C  
ATOM   2377  NZ  LYS A 315      10.675  42.333 -40.598  1.00100.70           N  
ATOM   2378  N   ALA A 316      14.756  41.703 -46.110  1.00 95.95           N  
ATOM   2379  CA  ALA A 316      15.023  42.696 -47.146  1.00 90.67           C  
ATOM   2380  C   ALA A 316      14.695  42.149 -48.534  1.00 91.08           C  
ATOM   2381  O   ALA A 316      14.109  42.856 -49.357  1.00 93.89           O  
ATOM   2382  CB  ALA A 316      16.470  43.156 -47.079  1.00 86.81           C  
ATOM   2383  N   ALA A 317      15.064  40.891 -48.780  1.00 87.49           N  
ATOM   2384  CA  ALA A 317      14.763  40.222 -50.046  1.00 88.69           C  
ATOM   2385  C   ALA A 317      13.259  40.154 -50.302  1.00 89.52           C  
ATOM   2386  O   ALA A 317      12.793  40.544 -51.372  1.00 95.10           O  
ATOM   2387  CB  ALA A 317      15.380  38.825 -50.083  1.00 86.97           C  
ATOM   2388  N   ALA A 318      12.510  39.679 -49.308  1.00 89.73           N  
ATOM   2389  CA  ALA A 318      11.057  39.535 -49.413  1.00 87.37           C  
ATOM   2390  C   ALA A 318      10.345  40.874 -49.613  1.00 86.96           C  
ATOM   2391  O   ALA A 318       9.391  40.959 -50.387  1.00 85.46           O  
ATOM   2392  CB  ALA A 318      10.504  38.814 -48.189  1.00 86.71           C  
ATOM   2393  N   ALA A 319      10.813  41.909 -48.916  1.00 86.41           N  
ATOM   2394  CA  ALA A 319      10.240  43.252 -49.031  1.00 87.95           C  
ATOM   2395  C   ALA A 319      10.513  43.868 -50.405  1.00 91.93           C  
ATOM   2396  O   ALA A 319       9.696  44.629 -50.926  1.00 95.13           O  
ATOM   2397  CB  ALA A 319      10.766  44.154 -47.926  1.00 84.97           C  
ATOM   2398  N   GLU A 320      11.665  43.529 -50.980  1.00 91.45           N  
ATOM   2399  CA  GLU A 320      12.036  43.987 -52.312  1.00 91.00           C  
ATOM   2400  C   GLU A 320      11.272  43.207 -53.380  1.00 90.91           C  
ATOM   2401  O   GLU A 320      10.906  43.765 -54.417  1.00 92.72           O  
ATOM   2402  CB  GLU A 320      13.545  43.843 -52.525  1.00 91.91           C  
ATOM   2403  CG  GLU A 320      14.110  44.714 -53.638  1.00 92.12           C  
ATOM   2404  CD  GLU A 320      15.582  44.455 -53.893  1.00 91.78           C  
ATOM   2405  OE1 GLU A 320      15.922  43.338 -54.328  1.00 95.96           O  
ATOM   2406  OE2 GLU A 320      16.402  45.368 -53.669  1.00 92.14           O  
ATOM   2407  N   ASN A 321      11.038  41.920 -53.120  1.00 87.69           N  
ATOM   2408  CA  ASN A 321      10.271  41.062 -54.024  1.00 87.49           C  
ATOM   2409  C   ASN A 321       8.806  41.479 -54.134  1.00 84.54           C  
ATOM   2410  O   ASN A 321       8.183  41.303 -55.181  1.00 82.62           O  
ATOM   2411  CB  ASN A 321      10.362  39.597 -53.589  1.00 91.18           C  
ATOM   2412  CG  ASN A 321      11.759  39.016 -53.757  1.00 97.45           C  
ATOM   2413  OD1 ASN A 321      12.427  39.243 -54.768  1.00 98.01           O  
ATOM   2414  ND2 ASN A 321      12.203  38.250 -52.764  1.00 98.91           N  
ATOM   2415  N   LEU A 322       8.267  42.030 -53.048  1.00 82.70           N  
ATOM   2416  CA  LEU A 322       6.877  42.480 -53.006  1.00 80.58           C  
ATOM   2417  C   LEU A 322       6.722  43.854 -53.655  1.00 78.49           C  
ATOM   2418  O   LEU A 322       5.681  44.159 -54.233  1.00 78.50           O  
ATOM   2419  CB  LEU A 322       6.361  42.515 -51.562  1.00 79.42           C  
ATOM   2420  CG  LEU A 322       4.855  42.710 -51.352  1.00 80.07           C  
ATOM   2421  CD1 LEU A 322       4.089  41.434 -51.672  1.00 82.44           C  
ATOM   2422  CD2 LEU A 322       4.561  43.170 -49.931  1.00 81.39           C  
ATOM   2423  N   TYR A 323       7.764  44.673 -53.547  1.00 75.79           N  
ATOM   2424  CA  TYR A 323       7.789  46.011 -54.133  1.00 73.68           C  
ATOM   2425  C   TYR A 323       7.615  45.966 -55.661  1.00 74.17           C  
ATOM   2426  O   TYR A 323       6.771  46.674 -56.210  1.00 72.79           O  
ATOM   2427  CB  TYR A 323       9.099  46.707 -53.751  1.00 73.83           C  
ATOM   2428  CG  TYR A 323       9.116  48.214 -53.920  1.00 75.47           C  
ATOM   2429  CD1 TYR A 323       9.381  48.796 -55.163  1.00 75.74           C  
ATOM   2430  CD2 TYR A 323       8.900  49.060 -52.832  1.00 73.53           C  
ATOM   2431  CE1 TYR A 323       9.410  50.180 -55.323  1.00 73.84           C  
ATOM   2432  CE2 TYR A 323       8.929  50.448 -52.981  1.00 74.07           C  
ATOM   2433  CZ  TYR A 323       9.186  50.997 -54.232  1.00 73.57           C  
ATOM   2434  OH  TYR A 323       9.219  52.362 -54.394  1.00 73.43           O  
ATOM   2435  N   PHE A 324       8.402  45.125 -56.334  1.00 73.20           N  
ATOM   2436  CA  PHE A 324       8.352  45.003 -57.796  1.00 74.66           C  
ATOM   2437  C   PHE A 324       7.434  43.869 -58.257  1.00 76.20           C  
ATOM   2438  O   PHE A 324       7.515  43.417 -59.402  1.00 77.73           O  
ATOM   2439  CB  PHE A 324       9.763  44.819 -58.386  1.00 70.57           C  
ATOM   2440  CG  PHE A 324      10.739  45.901 -57.998  1.00 69.46           C  
ATOM   2441  CD1 PHE A 324      10.506  47.231 -58.341  1.00 69.89           C  
ATOM   2442  CD2 PHE A 324      11.900  45.585 -57.304  1.00 68.38           C  
ATOM   2443  CE1 PHE A 324      11.410  48.231 -57.983  1.00 70.09           C  
ATOM   2444  CE2 PHE A 324      12.812  46.575 -56.945  1.00 69.92           C  
ATOM   2445  CZ  PHE A 324      12.567  47.901 -57.285  1.00 68.92           C  
ATOM   2446  N   GLN A 325       6.560  43.421 -57.362  1.00 79.45           N  
ATOM   2447  CA  GLN A 325       5.659  42.303 -57.633  1.00 84.28           C  
ATOM   2448  C   GLN A 325       4.561  42.705 -58.614  1.00 83.92           C  
ATOM   2449  O   GLN A 325       3.964  43.774 -58.482  1.00 83.24           O  
ATOM   2450  CB  GLN A 325       5.043  41.814 -56.322  1.00 86.35           C  
ATOM   2451  CG  GLN A 325       4.190  40.567 -56.422  1.00 88.45           C  
ATOM   2452  CD  GLN A 325       3.408  40.321 -55.149  1.00 91.83           C  
ATOM   2453  OE1 GLN A 325       2.454  41.039 -54.842  1.00 91.93           O  
ATOM   2454  NE2 GLN A 325       3.812  39.306 -54.395  1.00 94.78           N  
TER    2455      GLN A 325                                                      
HETATM 2456  C5' NEC A 400      31.745  11.029 -14.096  1.00 54.01           C  
HETATM 2457  O5' NEC A 400      31.202  10.037 -13.637  1.00 54.61           O  
HETATM 2458  N5' NEC A 400      32.108  12.077 -13.353  1.00 51.73           N  
HETATM 2459  C51 NEC A 400      31.620  12.294 -12.002  1.00 49.76           C  
HETATM 2460  C52 NEC A 400      32.457  13.305 -11.239  1.00 48.97           C  
HETATM 2461  C4' NEC A 400      32.061  11.115 -15.564  1.00 54.40           C  
HETATM 2462  O4' NEC A 400      33.121  10.200 -15.872  1.00 53.72           O  
HETATM 2463  C3' NEC A 400      30.879  10.717 -16.447  1.00 54.87           C  
HETATM 2464  O3' NEC A 400      30.138  11.850 -16.917  1.00 58.06           O  
HETATM 2465  C2' NEC A 400      31.525   9.970 -17.596  1.00 54.76           C  
HETATM 2466  O2' NEC A 400      31.889  10.877 -18.646  1.00 53.51           O  
HETATM 2467  C1' NEC A 400      32.787   9.371 -16.991  1.00 54.13           C  
HETATM 2468  N9  NEC A 400      32.470   7.967 -16.592  1.00 53.42           N  
HETATM 2469  C8  NEC A 400      32.034   7.542 -15.384  1.00 52.52           C  
HETATM 2470  N7  NEC A 400      31.824   6.198 -15.384  1.00 51.81           N  
HETATM 2471  C5  NEC A 400      32.112   5.740 -16.610  1.00 49.87           C  
HETATM 2472  C6  NEC A 400      32.115   4.423 -17.289  1.00 50.61           C  
HETATM 2473  N6  NEC A 400      31.753   3.289 -16.642  1.00 50.68           N  
HETATM 2474  N1  NEC A 400      32.501   4.389 -18.588  1.00 51.01           N  
HETATM 2475  C2  NEC A 400      32.873   5.499 -19.251  1.00 50.91           C  
HETATM 2476  N3  NEC A 400      32.902   6.723 -18.691  1.00 48.94           N  
HETATM 2477  C4  NEC A 400      32.537   6.907 -17.403  1.00 50.07           C  
HETATM 2478  C1  SOG A 501      39.777  -1.560  -1.457  1.00 88.04           C  
HETATM 2479  C2  SOG A 501      38.638  -1.746  -2.451  1.00 88.94           C  
HETATM 2480  C3  SOG A 501      38.715  -3.103  -3.141  1.00 90.13           C  
HETATM 2481  C4  SOG A 501      39.365  -4.139  -2.232  1.00 92.13           C  
HETATM 2482  C5  SOG A 501      40.752  -3.691  -1.748  1.00 91.81           C  
HETATM 2483  C6  SOG A 501      41.875  -4.460  -2.450  1.00 92.12           C  
HETATM 2484  C1' SOG A 501      41.645   0.360  -1.979  1.00 77.89           C  
HETATM 2485  C2' SOG A 501      41.996   1.840  -2.070  1.00 73.86           C  
HETATM 2486  C3' SOG A 501      43.493   2.078  -1.944  1.00 69.72           C  
HETATM 2487  C4' SOG A 501      43.888   3.474  -2.408  1.00 65.19           C  
HETATM 2488  C5' SOG A 501      43.320   4.543  -1.475  1.00 64.16           C  
HETATM 2489  C6' SOG A 501      43.797   5.978  -1.740  1.00 64.33           C  
HETATM 2490  C7' SOG A 501      45.027   6.094  -2.644  1.00 65.70           C  
HETATM 2491  C8' SOG A 501      45.413   7.545  -2.858  1.00 67.03           C  
HETATM 2492  S1  SOG A 501      40.076   0.167  -1.183  1.00 86.11           S  
HETATM 2493  O2  SOG A 501      37.413  -1.656  -1.732  1.00 92.16           O  
HETATM 2494  O3  SOG A 501      39.482  -2.996  -4.340  1.00 93.17           O  
HETATM 2495  O4  SOG A 501      38.484  -4.351  -1.124  1.00 92.74           O  
HETATM 2496  O5  SOG A 501      40.912  -2.280  -1.951  1.00 89.53           O  
HETATM 2497  O6  SOG A 501      43.118  -3.739  -2.399  1.00 90.11           O  
HETATM 2498  C1  SOG A 502      46.158   0.087  -5.700  1.00 97.45           C  
HETATM 2499  C2  SOG A 502      44.749  -0.183  -6.226  1.00 95.70           C  
HETATM 2500  C3  SOG A 502      44.748  -1.017  -7.511  1.00 94.30           C  
HETATM 2501  C4  SOG A 502      45.905  -0.734  -8.469  1.00 95.16           C  
HETATM 2502  C5  SOG A 502      47.226  -0.424  -7.769  1.00 98.08           C  
HETATM 2503  C6  SOG A 502      48.295   0.105  -8.733  1.00 98.16           C  
HETATM 2504  C1' SOG A 502      47.337   2.427  -5.019  1.00 93.79           C  
HETATM 2505  C2' SOG A 502      47.609   3.540  -4.024  1.00 91.25           C  
HETATM 2506  C3' SOG A 502      48.996   4.118  -4.282  1.00 91.99           C  
HETATM 2507  C4' SOG A 502      48.994   5.629  -4.093  1.00 93.44           C  
HETATM 2508  C5' SOG A 502      50.378   6.165  -3.726  1.00 93.19           C  
HETATM 2509  C6' SOG A 502      50.256   7.291  -2.702  1.00 91.76           C  
HETATM 2510  C7' SOG A 502      51.216   8.442  -2.964  1.00 89.30           C  
HETATM 2511  C8' SOG A 502      50.752   9.659  -2.195  1.00 88.46           C  
HETATM 2512  S1  SOG A 502      46.109   1.309  -4.419  1.00 99.04           S  
HETATM 2513  O2  SOG A 502      43.978  -0.859  -5.218  1.00 94.31           O  
HETATM 2514  O3  SOG A 502      43.534  -0.752  -8.223  1.00 92.85           O  
HETATM 2515  O4  SOG A 502      46.087  -1.877  -9.315  1.00 97.24           O  
HETATM 2516  O5  SOG A 502      46.982   0.558  -6.768  1.00 97.50           O  
HETATM 2517  O6  SOG A 502      49.235  -0.924  -9.069  1.00 96.90           O  
HETATM 2518  C1  SOG A 503      33.439  39.466 -10.134  1.00106.10           C  
HETATM 2519  C2  SOG A 503      33.544  40.258  -8.833  1.00106.04           C  
HETATM 2520  C3  SOG A 503      33.233  41.724  -9.090  1.00106.93           C  
HETATM 2521  C4  SOG A 503      34.174  42.259 -10.163  1.00108.09           C  
HETATM 2522  C5  SOG A 503      34.220  41.340 -11.391  1.00107.32           C  
HETATM 2523  C6  SOG A 503      35.319  41.809 -12.342  1.00105.33           C  
HETATM 2524  C1' SOG A 503      34.028  36.952 -11.280  1.00100.90           C  
HETATM 2525  C2' SOG A 503      34.279  35.478 -10.964  1.00 98.90           C  
HETATM 2526  C3' SOG A 503      34.423  34.632 -12.222  1.00 96.88           C  
HETATM 2527  C4' SOG A 503      34.679  33.172 -11.859  1.00 95.88           C  
HETATM 2528  C5' SOG A 503      35.002  32.357 -13.105  1.00 96.72           C  
HETATM 2529  C6' SOG A 503      35.710  31.049 -12.767  1.00 96.37           C  
HETATM 2530  C7' SOG A 503      36.107  30.322 -14.052  1.00 97.15           C  
HETATM 2531  C8' SOG A 503      35.818  28.834 -14.009  1.00 96.30           C  
HETATM 2532  S1  SOG A 503      33.639  37.747  -9.756  1.00105.59           S  
HETATM 2533  O2  SOG A 503      32.651  39.738  -7.845  1.00105.35           O  
HETATM 2534  O3  SOG A 503      33.388  42.474  -7.878  1.00107.50           O  
HETATM 2535  O4  SOG A 503      33.757  43.576 -10.553  1.00109.62           O  
HETATM 2536  O5  SOG A 503      34.438  39.965 -11.028  1.00106.09           O  
HETATM 2537  O6  SOG A 503      35.621  40.787 -13.298  1.00106.31           O  
HETATM 2538  C1  SOG A 504      39.903  29.392 -10.813  1.00114.62           C  
HETATM 2539  C2  SOG A 504      39.152  30.586 -10.215  1.00114.64           C  
HETATM 2540  C3  SOG A 504      39.492  30.874  -8.750  1.00113.40           C  
HETATM 2541  C4  SOG A 504      39.729  29.610  -7.922  1.00111.23           C  
HETATM 2542  C5  SOG A 504      40.593  28.601  -8.677  1.00114.58           C  
HETATM 2543  C6  SOG A 504      40.863  27.349  -7.835  1.00115.74           C  
HETATM 2544  C1' SOG A 504      40.100  27.534 -12.771  1.00105.80           C  
HETATM 2545  C2' SOG A 504      39.737  27.080 -14.176  1.00102.49           C  
HETATM 2546  C3' SOG A 504      40.410  25.753 -14.497  1.00101.72           C  
HETATM 2547  C4' SOG A 504      40.308  25.451 -15.985  1.00102.42           C  
HETATM 2548  C5' SOG A 504      41.094  24.199 -16.352  1.00102.92           C  
HETATM 2549  C6' SOG A 504      41.034  23.934 -17.854  1.00102.45           C  
HETATM 2550  C7' SOG A 504      42.384  23.464 -18.396  1.00102.59           C  
HETATM 2551  C8' SOG A 504      42.250  22.718 -19.710  1.00102.22           C  
HETATM 2552  S1  SOG A 504      39.117  28.929 -12.333  1.00110.15           S  
HETATM 2553  O2  SOG A 504      39.474  31.752 -10.987  1.00116.61           O  
HETATM 2554  O3  SOG A 504      38.423  31.638  -8.167  1.00114.07           O  
HETATM 2555  O4  SOG A 504      40.384  29.970  -6.701  1.00106.33           O  
HETATM 2556  O5  SOG A 504      39.931  28.281  -9.905  1.00115.33           O  
HETATM 2557  O6  SOG A 504      41.476  26.314  -8.620  1.00114.70           O  
HETATM 2558  C1  SOG A 505      40.562  37.149  -7.412  1.00103.90           C  
HETATM 2559  C2  SOG A 505      39.376  37.344  -8.369  1.00105.72           C  
HETATM 2560  C3  SOG A 505      39.067  38.820  -8.606  1.00105.97           C  
HETATM 2561  C4  SOG A 505      38.923  39.532  -7.265  1.00107.73           C  
HETATM 2562  C5  SOG A 505      40.231  39.405  -6.486  1.00108.82           C  
HETATM 2563  C6  SOG A 505      40.177  40.126  -5.134  1.00108.70           C  
HETATM 2564  C1' SOG A 505      39.996  35.698  -5.183  1.00 91.20           C  
HETATM 2565  C2' SOG A 505      39.611  34.367  -4.556  1.00 85.76           C  
HETATM 2566  C3' SOG A 505      39.377  34.512  -3.052  1.00 79.24           C  
HETATM 2567  C4' SOG A 505      39.491  33.158  -2.355  1.00 74.37           C  
HETATM 2568  C5' SOG A 505      40.944  32.722  -2.168  1.00 70.68           C  
HETATM 2569  C6' SOG A 505      41.474  31.815  -3.282  1.00 67.88           C  
HETATM 2570  C7' SOG A 505      42.154  30.579  -2.707  1.00 64.89           C  
HETATM 2571  C8' SOG A 505      42.706  29.691  -3.801  1.00 63.87           C  
HETATM 2572  S1  SOG A 505      40.600  35.470  -6.832  1.00 94.67           S  
HETATM 2573  O2  SOG A 505      39.660  36.714  -9.627  1.00106.57           O  
HETATM 2574  O3  SOG A 505      37.869  38.954  -9.384  1.00105.71           O  
HETATM 2575  O4  SOG A 505      38.557  40.907  -7.459  1.00108.04           O  
HETATM 2576  O5  SOG A 505      40.500  38.017  -6.265  1.00106.65           O  
HETATM 2577  O6  SOG A 505      40.759  39.323  -4.091  1.00106.37           O  
HETATM 2578  O   HOH A2001      33.045   5.972 -22.523  1.00 65.58           O  
HETATM 2579  O   HOH A2002      32.740   8.423 -23.192  1.00 66.97           O  
HETATM 2580  O   HOH A2003      35.508   4.325 -22.396  1.00 74.73           O  
HETATM 2581  O   HOH A2004      31.864   5.294 -29.112  1.00 66.45           O  
HETATM 2582  O   HOH A2005      26.538  23.501 -12.664  1.00 73.26           O  
HETATM 2583  O   HOH A2006      15.227  31.370  -4.820  1.00 67.28           O  
HETATM 2584  O   HOH A2007      33.150  27.372 -11.365  1.00 71.69           O  
HETATM 2585  O   HOH A2008      44.376  -2.531 -24.635  1.00 71.60           O  
HETATM 2586  O   HOH A2009      45.284  -1.176 -20.693  1.00 72.81           O  
HETATM 2587  O   HOH A2010      43.428  -7.975 -23.534  1.00 75.52           O  
HETATM 2588  O   HOH A2011      35.523   2.006 -20.601  1.00 60.29           O  
HETATM 2589  O   HOH A2012      42.869  -1.296 -22.847  1.00 66.30           O  
HETATM 2590  O   HOH A2013      15.687  24.564 -11.490  1.00 69.45           O  
HETATM 2591  O   HOH A2014      14.906  29.893  -9.727  1.00 52.06           O  
HETATM 2592  O   HOH A2015      23.443   8.394 -15.587  1.00 59.40           O  
HETATM 2593  O   HOH A2016      30.292   5.291 -10.082  1.00 44.14           O  
HETATM 2594  O   HOH A2017      30.044   0.105 -15.574  1.00 53.47           O  
HETATM 2595  O   HOH A2018      27.455  16.873 -16.568  1.00 70.01           O  
HETATM 2596  O   HOH A2019      26.665  18.100 -14.095  1.00 73.09           O  
HETATM 2597  O   HOH A2020      25.278  20.905 -13.526  1.00 88.18           O  
HETATM 2598  O   HOH A2021      22.347  24.848 -21.304  1.00 70.61           O  
HETATM 2599  O   HOH A2022      18.329  23.751 -13.272  1.00 58.66           O  
HETATM 2600  O   HOH A2023      22.733  24.857 -17.433  1.00 67.84           O  
HETATM 2601  O   HOH A2024      15.644  31.623  -7.650  1.00 65.43           O  
HETATM 2602  O   HOH A2025      11.380  53.334 -56.472  1.00 46.54           O  
HETATM 2603  O   HOH A2026      33.189   9.056 -20.360  1.00 47.30           O  
HETATM 2604  O   HOH A2027      32.639   2.195 -20.429  1.00 55.65           O  
CONECT  505 1161                                                                
CONECT  521 1070                                                                
CONECT  541 1205                                                                
CONECT 1070  521                                                                
CONECT 1161  505                                                                
CONECT 1205  541                                                                
CONECT 1897 1918                                                                
CONECT 1918 1897                                                                
CONECT 2456 2457 2458 2461                                                      
CONECT 2457 2456                                                                
CONECT 2458 2456 2459                                                           
CONECT 2459 2458 2460                                                           
CONECT 2460 2459                                                                
CONECT 2461 2456 2462 2463                                                      
CONECT 2462 2461 2467                                                           
CONECT 2463 2461 2464 2465                                                      
CONECT 2464 2463                                                                
CONECT 2465 2463 2466 2467                                                      
CONECT 2466 2465                                                                
CONECT 2467 2462 2465 2468                                                      
CONECT 2468 2467 2469 2477                                                      
CONECT 2469 2468 2470                                                           
CONECT 2470 2469 2471                                                           
CONECT 2471 2470 2472 2477                                                      
CONECT 2472 2471 2473 2474                                                      
CONECT 2473 2472                                                                
CONECT 2474 2472 2475                                                           
CONECT 2475 2474 2476                                                           
CONECT 2476 2475 2477                                                           
CONECT 2477 2468 2471 2476                                                      
CONECT 2478 2479 2492 2496                                                      
CONECT 2479 2478 2480 2493                                                      
CONECT 2480 2479 2481 2494                                                      
CONECT 2481 2480 2482 2495                                                      
CONECT 2482 2481 2483 2496                                                      
CONECT 2483 2482 2497                                                           
CONECT 2484 2485 2492                                                           
CONECT 2485 2484 2486                                                           
CONECT 2486 2485 2487                                                           
CONECT 2487 2486 2488                                                           
CONECT 2488 2487 2489                                                           
CONECT 2489 2488 2490                                                           
CONECT 2490 2489 2491                                                           
CONECT 2491 2490                                                                
CONECT 2492 2478 2484                                                           
CONECT 2493 2479                                                                
CONECT 2494 2480                                                                
CONECT 2495 2481                                                                
CONECT 2496 2478 2482                                                           
CONECT 2497 2483                                                                
CONECT 2498 2499 2512 2516                                                      
CONECT 2499 2498 2500 2513                                                      
CONECT 2500 2499 2501 2514                                                      
CONECT 2501 2500 2502 2515                                                      
CONECT 2502 2501 2503 2516                                                      
CONECT 2503 2502 2517                                                           
CONECT 2504 2505 2512                                                           
CONECT 2505 2504 2506                                                           
CONECT 2506 2505 2507                                                           
CONECT 2507 2506 2508                                                           
CONECT 2508 2507 2509                                                           
CONECT 2509 2508 2510                                                           
CONECT 2510 2509 2511                                                           
CONECT 2511 2510                                                                
CONECT 2512 2498 2504                                                           
CONECT 2513 2499                                                                
CONECT 2514 2500                                                                
CONECT 2515 2501                                                                
CONECT 2516 2498 2502                                                           
CONECT 2517 2503                                                                
CONECT 2518 2519 2532 2536                                                      
CONECT 2519 2518 2520 2533                                                      
CONECT 2520 2519 2521 2534                                                      
CONECT 2521 2520 2522 2535                                                      
CONECT 2522 2521 2523 2536                                                      
CONECT 2523 2522 2537                                                           
CONECT 2524 2525 2532                                                           
CONECT 2525 2524 2526                                                           
CONECT 2526 2525 2527                                                           
CONECT 2527 2526 2528                                                           
CONECT 2528 2527 2529                                                           
CONECT 2529 2528 2530                                                           
CONECT 2530 2529 2531                                                           
CONECT 2531 2530                                                                
CONECT 2532 2518 2524                                                           
CONECT 2533 2519                                                                
CONECT 2534 2520                                                                
CONECT 2535 2521                                                                
CONECT 2536 2518 2522                                                           
CONECT 2537 2523                                                                
CONECT 2538 2539 2552 2556                                                      
CONECT 2539 2538 2540 2553                                                      
CONECT 2540 2539 2541 2554                                                      
CONECT 2541 2540 2542 2555                                                      
CONECT 2542 2541 2543 2556                                                      
CONECT 2543 2542 2557                                                           
CONECT 2544 2545 2552                                                           
CONECT 2545 2544 2546                                                           
CONECT 2546 2545 2547                                                           
CONECT 2547 2546 2548                                                           
CONECT 2548 2547 2549                                                           
CONECT 2549 2548 2550                                                           
CONECT 2550 2549 2551                                                           
CONECT 2551 2550                                                                
CONECT 2552 2538 2544                                                           
CONECT 2553 2539                                                                
CONECT 2554 2540                                                                
CONECT 2555 2541                                                                
CONECT 2556 2538 2542                                                           
CONECT 2557 2543                                                                
CONECT 2558 2559 2572 2576                                                      
CONECT 2559 2558 2560 2573                                                      
CONECT 2560 2559 2561 2574                                                      
CONECT 2561 2560 2562 2575                                                      
CONECT 2562 2561 2563 2576                                                      
CONECT 2563 2562 2577                                                           
CONECT 2564 2565 2572                                                           
CONECT 2565 2564 2566                                                           
CONECT 2566 2565 2567                                                           
CONECT 2567 2566 2568                                                           
CONECT 2568 2567 2569                                                           
CONECT 2569 2568 2570                                                           
CONECT 2570 2569 2571                                                           
CONECT 2571 2570                                                                
CONECT 2572 2558 2564                                                           
CONECT 2573 2559                                                                
CONECT 2574 2560                                                                
CONECT 2575 2561                                                                
CONECT 2576 2558 2562                                                           
CONECT 2577 2563                                                                
MASTER      306    0    6   18    2    0    0    6 2603    1  130   25          
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.