CNRS Nantes University UFIP UFIP
home |  start a new run |  job status |  references&downloads |  examples |  help  

Should you encounter any unexpected behaviour,
please let us know.


***  LIPID TRANSPORT 18-DEC-06 2OBD  ***

elNémo ID: 21030116143976167

Job options:

ID        	=	 21030116143976167
JOBID     	=	 LIPID TRANSPORT 18-DEC-06 2OBD
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    LIPID TRANSPORT                         18-DEC-06   2OBD              
TITLE     CRYSTAL STRUCTURE OF CHOLESTERYL ESTER TRANSFER PROTEIN               
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: CHOLESTERYL ESTER TRANSFER PROTEIN;                        
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: LIPID TRANSFER PROTEIN I;                                   
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 GENE: CETP;                                                          
SOURCE   6 EXPRESSION_SYSTEM: CRICETULUS GRISEUS;                               
SOURCE   7 EXPRESSION_SYSTEM_COMMON: CHINESE HAMSTER;                           
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 10029;                                      
SOURCE   9 EXPRESSION_SYSTEM_CELL_LINE: CHINESE HAMSTER OVARY DG44              
KEYWDS    CHOLESTERYL ESTER, LIPID TRANSFER PROTEIN, LIPID TRANSPORT            
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    X.QIU                                                                 
REVDAT   5   29-JUL-20 2OBD    1       COMPND REMARK HETNAM LINK                
REVDAT   5 2                   1       SITE   ATOM                              
REVDAT   4   29-NOV-17 2OBD    1       COMPND REMARK HET    HETNAM              
REVDAT   4 2                   1       HETSYN FORMUL LINK   SITE                
REVDAT   4 3                   1       ATOM                                     
REVDAT   3   24-FEB-09 2OBD    1       VERSN                                    
REVDAT   2   20-FEB-07 2OBD    1       JRNL                                     
REVDAT   1   23-JAN-07 2OBD    0                                                
JRNL        AUTH   X.QIU,A.MISTRY,M.J.AMMIRATI,B.A.CHRUNYK,R.W.CLARK,Y.CONG,    
JRNL        AUTH 2 J.S.CULP,D.E.DANLEY,T.B.FREEMAN,K.F.GEOGHEGAN,M.C.GRIFFOR,   
JRNL        AUTH 3 S.J.HAWRYLIK,C.M.HAYWARD,P.HENSLEY,L.R.HOTH,G.A.KARAM,       
JRNL        AUTH 4 M.E.LIRA,D.B.LLOYD,K.M.MCGRATH,K.J.STUTZMAN-ENGWALL,         
JRNL        AUTH 5 A.K.SUBASHI,T.A.SUBASHI,J.F.THOMPSON,I.K.WANG,H.ZHAO,        
JRNL        AUTH 6 A.P.SEDDON                                                   
JRNL        TITL   CRYSTAL STRUCTURE OF CHOLESTERYL ESTER TRANSFER PROTEIN      
JRNL        TITL 2 REVEALS A LONG TUNNEL AND FOUR BOUND LIPID MOLECULES.        
JRNL        REF    NAT.STRUCT.MOL.BIOL.          V.  14   106 2007              
JRNL        REFN                   ISSN 1545-9993                               
JRNL        PMID   17237796                                                     
JRNL        DOI    10.1038/NSMB1197                                             
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0005                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 46.88                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 82.0                           
REMARK   3   NUMBER OF REFLECTIONS             : 40673                          
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) : 0.220                           
REMARK   3   R VALUE            (WORKING SET) : 0.217                           
REMARK   3   FREE R VALUE                     : 0.265                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2176                            
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) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.16                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1449                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 39.96                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3000                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 70                           
REMARK   3   BIN FREE R VALUE                    : 0.3910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 3712                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 301                                     
REMARK   3   SOLVENT ATOMS            : 416                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 44.54                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.07000                                              
REMARK   3    B22 (A**2) : 2.07000                                              
REMARK   3    B33 (A**2) : -3.14000                                             
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): 0.219         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.201         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.146         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.674         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.951                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.928                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  4135 ; 0.012 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  5572 ; 1.635 ; 2.024       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   475 ; 6.449 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   166 ;35.902 ;24.819       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   678 ;18.725 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    13 ;15.702 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   644 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  2903 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1869 ; 0.209 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  2745 ; 0.320 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   374 ; 0.171 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    71 ; 0.210 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):    19 ; 0.181 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  2431 ; 0.697 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3855 ; 1.228 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1864 ; 1.862 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  1717 ; 3.018 ; 4.500       
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                                                           
REMARK   4                                                                      
REMARK   4 2OBD COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 08-JAN-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000040922.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 20-MAR-05; NULL                    
REMARK 200  TEMPERATURE           (KELVIN) : 100; NULL                          
REMARK 200  PH                             : 7.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y; Y                               
REMARK 200  RADIATION SOURCE               : APS; ESRF                          
REMARK 200  BEAMLINE                       : 17-ID; ID23-1                      
REMARK 200  X-RAY GENERATOR MODEL          : NULL; NULL                         
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M; NULL                            
REMARK 200  WAVELENGTH OR RANGE        (A) : 1; 1                               
REMARK 200  MONOCHROMATOR                  : SYNCHROTRON; NULL                  
REMARK 200  OPTICS                         : NULL; NULL                         
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD; NULL                          
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 210; NULL             
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 52263                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 88.0                               
REMARK 200  DATA REDUNDANCY                : 5.000                              
REMARK 200  R MERGE                    (I) : 0.07800                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.16                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 50.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.00                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.37800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.100                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH; NULL                        
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MIR                          
REMARK 200 SOFTWARE USED: SOLVE                                                 
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 70.34                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 4.15                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: ~30% PDE 400, 0.2M MGCL2, HEPES 0.1M,    
REMARK 280  PH 7.5, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 298K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 21 21 21                       
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X+1/2,-Y,Z+1/2                                         
REMARK 290       3555   -X,Y+1/2,-Z+1/2                                         
REMARK 290       4555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000       33.39000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       93.81000            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       35.16000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       93.81000            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000       33.39000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000       35.16000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     SER A     2                                                      
REMARK 465     LYS A     3                                                      
REMARK 465     GLY A     4                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   O    HOH A   496     O    HOH A   497              2.14            
REMARK 500   OE1  GLU A   447     O    HOH A   719              2.14            
REMARK 500   OD1  ASP A   341     O    HOH A   588              2.17            
REMARK 500   OH   TYR A   375     O    HOH A   510              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    LEU A  51       -3.97     66.47                                   
REMARK 500    LYS A  80      -64.31   -134.86                                   
REMARK 500    ALA A 140       77.28   -117.42                                   
REMARK 500    ASP A 208      118.51   -169.15                                   
REMARK 500    ASP A 257       35.77   -142.28                                   
REMARK 500    PHE A 315       65.68   -118.37                                   
REMARK 500    THR A 393      109.99   -162.45                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 662        DISTANCE =  5.86 ANGSTROMS                       
REMARK 525    HOH A 771        DISTANCE =  6.37 ANGSTROMS                       
REMARK 525    HOH A 777        DISTANCE =  6.86 ANGSTROMS                       
DBREF  2OBD A    1   476  UNP    P11597   CETP_HUMAN      18    493             
SEQADV 2OBD ALA A    1  UNP  P11597    CYS    18 ENGINEERED                     
SEQADV 2OBD ASP A   88  UNP  P11597    ASN   105 ENGINEERED                     
SEQADV 2OBD ALA A  131  UNP  P11597    CYS   148 ENGINEERED                     
SEQADV 2OBD ASP A  240  UNP  P11597    ASN   257 ENGINEERED                     
SEQADV 2OBD ASP A  341  UNP  P11597    ASN   358 ENGINEERED                     
SEQADV 2OBD ILE A  405  UNP  P11597    VAL   422 ENGINEERED                     
SEQRES   1 A  476  ALA SER LYS GLY THR SER HIS GLU ALA GLY ILE VAL CYS          
SEQRES   2 A  476  ARG ILE THR LYS PRO ALA LEU LEU VAL LEU ASN HIS GLU          
SEQRES   3 A  476  THR ALA LYS VAL ILE GLN THR ALA PHE GLN ARG ALA SER          
SEQRES   4 A  476  TYR PRO ASP ILE THR GLY GLU LYS ALA MET MET LEU LEU          
SEQRES   5 A  476  GLY GLN VAL LYS TYR GLY LEU HIS ASN ILE GLN ILE SER          
SEQRES   6 A  476  HIS LEU SER ILE ALA SER SER GLN VAL GLU LEU VAL GLU          
SEQRES   7 A  476  ALA LYS SER ILE ASP VAL SER ILE GLN ASP VAL SER VAL          
SEQRES   8 A  476  VAL PHE LYS GLY THR LEU LYS TYR GLY TYR THR THR ALA          
SEQRES   9 A  476  TRP TRP LEU GLY ILE ASP GLN SER ILE ASP PHE GLU ILE          
SEQRES  10 A  476  ASP SER ALA ILE ASP LEU GLN ILE ASN THR GLN LEU THR          
SEQRES  11 A  476  ALA ASP SER GLY ARG VAL ARG THR ASP ALA PRO ASP CYS          
SEQRES  12 A  476  TYR LEU SER PHE HIS LYS LEU LEU LEU HIS LEU GLN GLY          
SEQRES  13 A  476  GLU ARG GLU PRO GLY TRP ILE LYS GLN LEU PHE THR ASN          
SEQRES  14 A  476  PHE ILE SER PHE THR LEU LYS LEU VAL LEU LYS GLY GLN          
SEQRES  15 A  476  ILE CYS LYS GLU ILE ASN VAL ILE SER ASN ILE MET ALA          
SEQRES  16 A  476  ASP PHE VAL GLN THR ARG ALA ALA SER ILE LEU SER ASP          
SEQRES  17 A  476  GLY ASP ILE GLY VAL ASP ILE SER LEU THR GLY ASP PRO          
SEQRES  18 A  476  VAL ILE THR ALA SER TYR LEU GLU SER HIS HIS LYS GLY          
SEQRES  19 A  476  HIS PHE ILE TYR LYS ASP VAL SER GLU ASP LEU PRO LEU          
SEQRES  20 A  476  PRO THR PHE SER PRO THR LEU LEU GLY ASP SER ARG MET          
SEQRES  21 A  476  LEU TYR PHE TRP PHE SER GLU ARG VAL PHE HIS SER LEU          
SEQRES  22 A  476  ALA LYS VAL ALA PHE GLN ASP GLY ARG LEU MET LEU SER          
SEQRES  23 A  476  LEU MET GLY ASP GLU PHE LYS ALA VAL LEU GLU THR TRP          
SEQRES  24 A  476  GLY PHE ASN THR ASN GLN GLU ILE PHE GLN GLU VAL VAL          
SEQRES  25 A  476  GLY GLY PHE PRO SER GLN ALA GLN VAL THR VAL HIS CYS          
SEQRES  26 A  476  LEU LYS MET PRO LYS ILE SER CYS GLN ASN LYS GLY VAL          
SEQRES  27 A  476  VAL VAL ASP SER SER VAL MET VAL LYS PHE LEU PHE PRO          
SEQRES  28 A  476  ARG PRO ASP GLN GLN HIS SER VAL ALA TYR THR PHE GLU          
SEQRES  29 A  476  GLU ASP ILE VAL THR THR VAL GLN ALA SER TYR SER LYS          
SEQRES  30 A  476  LYS LYS LEU PHE LEU SER LEU LEU ASP PHE GLN ILE THR          
SEQRES  31 A  476  PRO LYS THR VAL SER ASN LEU THR GLU SER SER SER GLU          
SEQRES  32 A  476  SER ILE GLN SER PHE LEU GLN SER MET ILE THR ALA VAL          
SEQRES  33 A  476  GLY ILE PRO GLU VAL MET SER ARG LEU GLU VAL VAL PHE          
SEQRES  34 A  476  THR ALA LEU MET ASN SER LYS GLY VAL SER LEU PHE ASP          
SEQRES  35 A  476  ILE ILE ASN PRO GLU ILE ILE THR ARG ASP GLY PHE LEU          
SEQRES  36 A  476  LEU LEU GLN MET ASP PHE GLY PHE PRO GLU HIS LEU LEU          
SEQRES  37 A  476  VAL ASP PHE LEU GLN SER LEU SER                              
MODRES 2OBD ASN A  396  ASN  GLYCOSYLATION SITE                                 
HET    NAG  B   1      14                                                       
HET    NDG  B   2      14                                                       
HET    FUC  B   3      10                                                       
HET     CL  A 493       1                                                       
HET    2OB  A 485      47                                                       
HET    2OB  A 486      47                                                       
HET    PCW  A 487      54                                                       
HET    PCW  A 488      54                                                       
HET    EPE  A 489      15                                                       
HET    1PE  A 490      16                                                       
HET    1PE  A 491      16                                                       
HET    PG4  A 492      13                                                       
HETNAM     NAG 2-ACETAMIDO-2-DEOXY-BETA-D-GLUCOPYRANOSE                         
HETNAM     NDG 2-ACETAMIDO-2-DEOXY-ALPHA-D-GLUCOPYRANOSE                        
HETNAM     FUC ALPHA-L-FUCOPYRANOSE                                             
HETNAM      CL CHLORIDE ION                                                     
HETNAM     2OB CHOLESTERYL OLEATE                                               
HETNAM     PCW 1,2-DIOLEOYL-SN-GLYCERO-3-PHOSPHOCHOLINE                         
HETNAM     EPE 4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID              
HETNAM     1PE PENTAETHYLENE GLYCOL                                             
HETNAM     PG4 TETRAETHYLENE GLYCOL                                             
HETSYN     2OB (3BETA,9BETA,14BETA,17ALPHA)-CHOLEST-5-EN-3-YL (9Z)-             
HETSYN   2 2OB  OCTADEC-9-ENOATE                                                
HETSYN     PCW (Z,Z)-4-HYDROXY-N,N,N-TRIMETHYL-10-OXO-7-[(1-OXO-9-              
HETSYN   2 PCW  OCTADECENYL)OXY]-3,5,9-TRIOXA-4-PHOSPHAHEPTACOS-18-EN-          
HETSYN   3 PCW  1-AMINIUM-4-OXIDE                                               
HETSYN     EPE HEPES                                                            
HETSYN     1PE PEG400                                                           
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   2  NDG    C8 H15 N O6                                                  
FORMUL   2  FUC    C6 H12 O5                                                    
FORMUL   3   CL    CL 1-                                                        
FORMUL   4  2OB    2(C45 H78 O2)                                                
FORMUL   6  PCW    2(C44 H85 N O8 P 1+)                                         
FORMUL   8  EPE    C8 H18 N2 O4 S                                               
FORMUL   9  1PE    2(C10 H22 O6)                                                
FORMUL  11  PG4    C8 H18 O5                                                    
FORMUL  12  HOH   *416(H2 O)                                                    
HELIX    1   1 LYS A   17  ASN A   24  1                                   8    
HELIX    2   2 GLU A   26  ALA A   38  1                                  13    
HELIX    3   3 ALA A  104  GLY A  108  5                                   5    
HELIX    4   4 TRP A  162  ILE A  171  1                                  10    
HELIX    5   5 ILE A  171  LEU A  206  1                                  36    
HELIX    6   6 SER A  251  LEU A  255  5                                   5    
HELIX    7   7 GLU A  267  ASP A  280  1                                  14    
HELIX    8   8 MET A  288  TRP A  299  1                                  12    
HELIX    9   9 GLN A  305  ILE A  307  5                                   3    
HELIX   10  10 PHE A  308  GLY A  313  1                                   6    
HELIX   11  11 PHE A  315  ALA A  319  5                                   5    
HELIX   12  12 ASP A  354  SER A  358  5                                   5    
HELIX   13  13 SER A  402  VAL A  416  1                                  15    
HELIX   14  14 VAL A  416  SER A  435  1                                  20    
HELIX   15  15 LYS A  436  PHE A  441  5                                   6    
HELIX   16  16 PRO A  464  SER A  474  1                                  11    
SHEET    1   A 2 HIS A   7  GLU A   8  0                                        
SHEET    2   A 2 THR A 249  PHE A 250 -1  O  PHE A 250   N  HIS A   7           
SHEET    1   B 6 VAL A 222  ILE A 223  0                                        
SHEET    2   B 6 TYR A 227  HIS A 232 -1  O  GLU A 229   N  VAL A 222           
SHEET    3   B 6 ILE A  11  THR A  16 -1  N  ILE A  11   O  HIS A 232           
SHEET    4   B 6 LEU A 261  SER A 266 -1  O  TRP A 264   N  VAL A  12           
SHEET    5   B 6 PHE A 454  GLY A 462 -1  O  LEU A 455   N  PHE A 265           
SHEET    6   B 6 ASP A 442  ARG A 451 -1  N  GLU A 447   O  GLN A 458           
SHEET    1   C 5 ILE A  43  MET A  49  0                                        
SHEET    2   C 5 GLY A  53  VAL A  77 -1  O  LEU A  59   N  ILE A  43           
SHEET    3   C 5 SER A  81  TYR A 101 -1  O  ASP A  83   N  GLU A  75           
SHEET    4   C 5 GLN A 111  ASP A 132 -1  O  ILE A 113   N  LEU A  97           
SHEET    5   C 5 ARG A 135  LEU A 154 -1  O  HIS A 148   N  ALA A 120           
SHEET    1   D 2 ILE A 211  ASP A 214  0                                        
SHEET    2   D 2 HIS A 235  TYR A 238 -1  O  HIS A 235   N  ASP A 214           
SHEET    1   E 4 MET A 284  LEU A 287  0                                        
SHEET    2   E 4 GLN A 320  CYS A 325 -1  O  VAL A 321   N  LEU A 287           
SHEET    3   E 4 GLY A 337  LEU A 349 -1  O  LYS A 347   N  THR A 322           
SHEET    4   E 4 LYS A 330  GLN A 334 -1  N  LYS A 330   O  ASP A 341           
SHEET    1   F 5 MET A 284  LEU A 287  0                                        
SHEET    2   F 5 GLN A 320  CYS A 325 -1  O  VAL A 321   N  LEU A 287           
SHEET    3   F 5 GLY A 337  LEU A 349 -1  O  LYS A 347   N  THR A 322           
SHEET    4   F 5 TYR A 361  SER A 376 -1  O  VAL A 371   N  VAL A 338           
SHEET    5   F 5 LYS A 379  ASN A 396 -1  O  LYS A 392   N  GLU A 364           
SSBOND   1 CYS A  143    CYS A  184                          1555   1555  2.09  
LINK         ND2 ASN A 396                 C1  NAG B   1     1555   1555  1.46  
LINK         O4  NAG B   1                 C1  NDG B   2     1555   1555  1.48  
LINK         O6  NAG B   1                 C1  FUC B   3     1555   1555  1.33  
CISPEP   1 VAL A  312    GLY A  313          0       -21.39                     
CRYST1   66.780   70.320  187.620  90.00  90.00  90.00 P 21 21 21    4          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.014975  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.014221  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005330        0.00000                         
ATOM      1  N   THR A   5      -3.036 -11.483  27.608  1.00 62.31           N  
ATOM      2  CA  THR A   5      -3.835 -10.317  27.109  1.00 62.40           C  
ATOM      3  C   THR A   5      -2.953  -9.269  26.392  1.00 61.65           C  
ATOM      4  O   THR A   5      -1.972  -9.611  25.710  1.00 61.56           O  
ATOM      5  CB  THR A   5      -4.650  -9.637  28.258  1.00 62.66           C  
ATOM      6  OG1 THR A   5      -4.912 -10.591  29.299  1.00 63.83           O  
ATOM      7  CG2 THR A   5      -5.977  -9.064  27.731  1.00 63.10           C  
ATOM      8  N   SER A   6      -3.323  -7.999  26.552  1.00 60.60           N  
ATOM      9  CA  SER A   6      -2.691  -6.883  25.866  1.00 59.38           C  
ATOM     10  C   SER A   6      -3.023  -5.594  26.626  1.00 58.33           C  
ATOM     11  O   SER A   6      -4.117  -5.453  27.192  1.00 58.45           O  
ATOM     12  CB  SER A   6      -3.201  -6.797  24.425  1.00 59.80           C  
ATOM     13  OG  SER A   6      -2.286  -6.112  23.590  1.00 59.90           O  
ATOM     14  N   HIS A   7      -2.076  -4.660  26.634  1.00 56.52           N  
ATOM     15  CA  HIS A   7      -2.198  -3.430  27.419  1.00 54.35           C  
ATOM     16  C   HIS A   7      -1.865  -2.213  26.570  1.00 53.10           C  
ATOM     17  O   HIS A   7      -1.032  -2.288  25.675  1.00 53.13           O  
ATOM     18  CB  HIS A   7      -1.268  -3.513  28.630  1.00 53.89           C  
ATOM     19  CG  HIS A   7      -1.440  -4.768  29.426  1.00 53.62           C  
ATOM     20  ND1 HIS A   7      -2.321  -4.866  30.483  1.00 53.64           N  
ATOM     21  CD2 HIS A   7      -0.875  -5.991  29.293  1.00 53.31           C  
ATOM     22  CE1 HIS A   7      -2.283  -6.093  30.971  1.00 53.70           C  
ATOM     23  NE2 HIS A   7      -1.410  -6.795  30.271  1.00 52.76           N  
ATOM     24  N   GLU A   8      -2.525  -1.097  26.837  1.00 51.62           N  
ATOM     25  CA  GLU A   8      -2.148   0.167  26.219  1.00 50.74           C  
ATOM     26  C   GLU A   8      -1.110   0.859  27.096  1.00 48.68           C  
ATOM     27  O   GLU A   8      -1.394   1.225  28.228  1.00 48.97           O  
ATOM     28  CB  GLU A   8      -3.355   1.082  26.058  1.00 50.68           C  
ATOM     29  CG  GLU A   8      -4.351   0.677  24.998  1.00 52.27           C  
ATOM     30  CD  GLU A   8      -5.460   1.720  24.842  1.00 54.02           C  
ATOM     31  OE1 GLU A   8      -6.025   1.822  23.723  1.00 57.87           O  
ATOM     32  OE2 GLU A   8      -5.765   2.442  25.836  1.00 57.06           O  
ATOM     33  N   ALA A   9       0.095   1.035  26.575  1.00 46.13           N  
ATOM     34  CA  ALA A   9       1.172   1.617  27.352  1.00 43.74           C  
ATOM     35  C   ALA A   9       2.206   2.211  26.417  1.00 41.96           C  
ATOM     36  O   ALA A   9       2.418   1.704  25.321  1.00 42.19           O  
ATOM     37  CB  ALA A   9       1.810   0.554  28.197  1.00 44.09           C  
ATOM     38  N   GLY A  10       2.857   3.276  26.859  1.00 39.90           N  
ATOM     39  CA  GLY A  10       4.008   3.823  26.163  1.00 37.22           C  
ATOM     40  C   GLY A  10       5.302   3.219  26.658  1.00 35.92           C  
ATOM     41  O   GLY A  10       6.244   3.025  25.886  1.00 35.43           O  
ATOM     42  N   ILE A  11       5.354   2.938  27.960  1.00 34.12           N  
ATOM     43  CA  ILE A  11       6.544   2.392  28.618  1.00 33.03           C  
ATOM     44  C   ILE A  11       6.112   1.218  29.494  1.00 32.91           C  
ATOM     45  O   ILE A  11       5.128   1.309  30.210  1.00 32.61           O  
ATOM     46  CB  ILE A  11       7.266   3.454  29.488  1.00 32.13           C  
ATOM     47  CG1 ILE A  11       7.748   4.615  28.624  1.00 31.98           C  
ATOM     48  CG2 ILE A  11       8.437   2.817  30.281  1.00 33.32           C  
ATOM     49  CD1 ILE A  11       8.404   5.725  29.353  1.00 32.23           C  
ATOM     50  N   VAL A  12       6.838   0.114  29.422  1.00 32.54           N  
ATOM     51  CA  VAL A  12       6.499  -1.050  30.213  1.00 32.57           C  
ATOM     52  C   VAL A  12       7.736  -1.497  30.984  1.00 32.90           C  
ATOM     53  O   VAL A  12       8.834  -1.541  30.429  1.00 32.25           O  
ATOM     54  CB  VAL A  12       5.919  -2.178  29.355  1.00 33.04           C  
ATOM     55  CG1 VAL A  12       5.862  -3.498  30.128  1.00 30.59           C  
ATOM     56  CG2 VAL A  12       4.521  -1.814  28.871  1.00 34.01           C  
ATOM     57  N   CYS A  13       7.556  -1.769  32.279  1.00 33.18           N  
ATOM     58  CA  CYS A  13       8.640  -2.251  33.161  1.00 32.45           C  
ATOM     59  C   CYS A  13       8.293  -3.641  33.684  1.00 31.91           C  
ATOM     60  O   CYS A  13       7.219  -3.862  34.211  1.00 31.91           O  
ATOM     61  CB  CYS A  13       8.847  -1.289  34.328  1.00 32.63           C  
ATOM     62  SG  CYS A  13      10.112  -1.792  35.530  1.00 35.16           S  
ATOM     63  N   ARG A  14       9.198  -4.578  33.495  1.00 31.90           N  
ATOM     64  CA  ARG A  14       8.974  -5.962  33.886  1.00 31.63           C  
ATOM     65  C   ARG A  14      10.123  -6.376  34.782  1.00 32.49           C  
ATOM     66  O   ARG A  14      11.279  -6.319  34.380  1.00 31.86           O  
ATOM     67  CB  ARG A  14       8.912  -6.875  32.676  1.00 31.27           C  
ATOM     68  CG  ARG A  14       8.745  -8.327  33.063  1.00 30.99           C  
ATOM     69  CD  ARG A  14       8.710  -9.189  31.879  1.00 31.56           C  
ATOM     70  NE  ARG A  14       7.458  -9.000  31.163  1.00 32.92           N  
ATOM     71  CZ  ARG A  14       6.915  -9.922  30.378  1.00 31.57           C  
ATOM     72  NH1 ARG A  14       7.524 -11.089  30.188  1.00 30.32           N  
ATOM     73  NH2 ARG A  14       5.787  -9.665  29.764  1.00 27.52           N  
ATOM     74  N   ILE A  15       9.780  -6.721  36.019  1.00 34.00           N  
ATOM     75  CA  ILE A  15      10.731  -7.141  37.046  1.00 35.55           C  
ATOM     76  C   ILE A  15      10.491  -8.620  37.268  1.00 35.88           C  
ATOM     77  O   ILE A  15       9.387  -9.025  37.638  1.00 36.49           O  
ATOM     78  CB  ILE A  15      10.499  -6.354  38.351  1.00 35.59           C  
ATOM     79  CG1 ILE A  15      10.797  -4.860  38.128  1.00 36.54           C  
ATOM     80  CG2 ILE A  15      11.399  -6.880  39.478  1.00 37.06           C  
ATOM     81  CD1 ILE A  15      10.256  -3.960  39.211  1.00 38.18           C  
ATOM     82  N   THR A  16      11.503  -9.435  37.007  1.00 36.88           N  
ATOM     83  CA  THR A  16      11.301 -10.873  37.017  1.00 37.39           C  
ATOM     84  C   THR A  16      11.616 -11.500  38.378  1.00 38.23           C  
ATOM     85  O   THR A  16      12.217 -10.871  39.247  1.00 38.53           O  
ATOM     86  CB  THR A  16      12.121 -11.579  35.924  1.00 37.18           C  
ATOM     87  OG1 THR A  16      13.515 -11.520  36.251  1.00 37.47           O  
ATOM     88  CG2 THR A  16      11.892 -10.939  34.566  1.00 36.70           C  
ATOM     89  N   LYS A  17      11.220 -12.759  38.537  1.00 39.37           N  
ATOM     90  CA  LYS A  17      11.540 -13.536  39.725  1.00 39.43           C  
ATOM     91  C   LYS A  17      13.035 -13.467  40.091  1.00 39.98           C  
ATOM     92  O   LYS A  17      13.364 -13.118  41.236  1.00 40.01           O  
ATOM     93  CB  LYS A  17      11.046 -14.971  39.547  1.00 39.69           C  
ATOM     94  CG  LYS A  17      11.164 -15.850  40.783  1.00 41.53           C  
ATOM     95  CD  LYS A  17      10.316 -15.364  41.953  1.00 42.88           C  
ATOM     96  CE  LYS A  17      10.706 -16.090  43.239  1.00 44.59           C  
ATOM     97  NZ  LYS A  17      10.367 -17.555  43.201  1.00 44.78           N  
ATOM     98  N   PRO A  18      13.956 -13.784  39.136  1.00 40.13           N  
ATOM     99  CA  PRO A  18      15.398 -13.595  39.426  1.00 39.36           C  
ATOM    100  C   PRO A  18      15.767 -12.241  40.037  1.00 39.46           C  
ATOM    101  O   PRO A  18      16.669 -12.176  40.885  1.00 39.28           O  
ATOM    102  CB  PRO A  18      16.061 -13.747  38.055  1.00 39.11           C  
ATOM    103  CG  PRO A  18      15.148 -14.604  37.287  1.00 39.66           C  
ATOM    104  CD  PRO A  18      13.748 -14.400  37.806  1.00 39.60           C  
ATOM    105  N   ALA A  19      15.094 -11.170  39.621  1.00 39.30           N  
ATOM    106  CA  ALA A  19      15.378  -9.849  40.209  1.00 39.08           C  
ATOM    107  C   ALA A  19      14.908  -9.773  41.678  1.00 39.16           C  
ATOM    108  O   ALA A  19      15.560  -9.149  42.519  1.00 38.15           O  
ATOM    109  CB  ALA A  19      14.717  -8.757  39.408  1.00 38.89           C  
ATOM    110  N   LEU A  20      13.749 -10.374  41.951  1.00 39.33           N  
ATOM    111  CA  LEU A  20      13.160 -10.373  43.292  1.00 39.81           C  
ATOM    112  C   LEU A  20      14.069 -11.149  44.233  1.00 40.32           C  
ATOM    113  O   LEU A  20      14.351 -10.690  45.347  1.00 40.53           O  
ATOM    114  CB  LEU A  20      11.761 -10.976  43.244  1.00 39.43           C  
ATOM    115  CG  LEU A  20      10.563 -10.035  43.069  1.00 38.51           C  
ATOM    116  CD1 LEU A  20      10.920  -8.594  42.729  1.00 39.15           C  
ATOM    117  CD2 LEU A  20       9.612 -10.584  42.072  1.00 37.76           C  
ATOM    118  N   LEU A  21      14.570 -12.287  43.747  1.00 40.52           N  
ATOM    119  CA  LEU A  21      15.535 -13.110  44.472  1.00 41.07           C  
ATOM    120  C   LEU A  21      16.810 -12.380  44.922  1.00 41.44           C  
ATOM    121  O   LEU A  21      17.279 -12.601  46.042  1.00 41.95           O  
ATOM    122  CB  LEU A  21      15.876 -14.381  43.690  1.00 40.36           C  
ATOM    123  CG  LEU A  21      14.728 -15.383  43.484  1.00 41.59           C  
ATOM    124  CD1 LEU A  21      15.117 -16.508  42.532  1.00 40.47           C  
ATOM    125  CD2 LEU A  21      14.211 -15.963  44.817  1.00 41.82           C  
ATOM    126  N   VAL A  22      17.387 -11.517  44.091  1.00 41.57           N  
ATOM    127  CA  VAL A  22      18.540 -10.751  44.574  1.00 41.73           C  
ATOM    128  C   VAL A  22      18.057  -9.603  45.459  1.00 41.66           C  
ATOM    129  O   VAL A  22      18.779  -9.132  46.346  1.00 41.88           O  
ATOM    130  CB  VAL A  22      19.549 -10.256  43.442  1.00 42.66           C  
ATOM    131  CG1 VAL A  22      19.498 -11.147  42.181  1.00 42.01           C  
ATOM    132  CG2 VAL A  22      19.375  -8.768  43.107  1.00 42.15           C  
ATOM    133  N   LEU A  23      16.839  -9.139  45.222  1.00 41.41           N  
ATOM    134  CA  LEU A  23      16.264  -8.109  46.085  1.00 41.28           C  
ATOM    135  C   LEU A  23      15.944  -8.675  47.480  1.00 41.64           C  
ATOM    136  O   LEU A  23      15.990  -7.954  48.457  1.00 42.16           O  
ATOM    137  CB  LEU A  23      15.014  -7.499  45.457  1.00 41.20           C  
ATOM    138  CG  LEU A  23      15.178  -6.458  44.341  1.00 39.67           C  
ATOM    139  CD1 LEU A  23      13.853  -5.839  44.076  1.00 39.00           C  
ATOM    140  CD2 LEU A  23      16.180  -5.387  44.700  1.00 38.93           C  
ATOM    141  N   ASN A  24      15.649  -9.971  47.554  1.00 42.17           N  
ATOM    142  CA  ASN A  24      15.293 -10.637  48.796  1.00 42.69           C  
ATOM    143  C   ASN A  24      16.440 -10.662  49.803  1.00 43.52           C  
ATOM    144  O   ASN A  24      16.212 -10.749  51.012  1.00 43.49           O  
ATOM    145  CB  ASN A  24      14.773 -12.049  48.509  1.00 42.16           C  
ATOM    146  CG  ASN A  24      14.405 -12.815  49.770  1.00 41.53           C  
ATOM    147  OD1 ASN A  24      13.735 -12.291  50.658  1.00 38.95           O  
ATOM    148  ND2 ASN A  24      14.821 -14.078  49.834  1.00 39.01           N  
ATOM    149  N  AHIS A  25      17.664 -10.556  49.289  0.40 43.99           N  
ATOM    150  N  BHIS A  25      17.667 -10.567  49.300  0.60 44.07           N  
ATOM    151  CA AHIS A  25      18.877 -10.524  50.099  0.40 44.59           C  
ATOM    152  CA BHIS A  25      18.850 -10.535  50.144  0.60 44.75           C  
ATOM    153  C  AHIS A  25      18.920  -9.321  51.049  0.40 44.95           C  
ATOM    154  C  BHIS A  25      18.826  -9.393  51.152  0.60 45.12           C  
ATOM    155  O  AHIS A  25      19.830  -9.206  51.875  0.40 45.27           O  
ATOM    156  O  BHIS A  25      19.591  -9.394  52.119  0.60 45.59           O  
ATOM    157  CB AHIS A  25      20.112 -10.533  49.189  0.40 44.74           C  
ATOM    158  CB BHIS A  25      20.112 -10.469  49.286  0.60 44.99           C  
ATOM    159  CG AHIS A  25      21.371 -10.964  49.877  0.40 45.27           C  
ATOM    160  CG BHIS A  25      20.447 -11.764  48.619  0.60 45.82           C  
ATOM    161  ND1AHIS A  25      22.151 -10.098  50.615  0.40 46.32           N  
ATOM    162  ND1BHIS A  25      20.884 -12.867  49.320  0.60 47.18           N  
ATOM    163  CD2AHIS A  25      21.988 -12.170  49.937  0.40 46.18           C  
ATOM    164  CD2BHIS A  25      20.400 -12.137  47.319  0.60 46.50           C  
ATOM    165  CE1AHIS A  25      23.192 -10.753  51.102  0.40 46.76           C  
ATOM    166  CE1BHIS A  25      21.093 -13.864  48.479  0.60 48.03           C  
ATOM    167  NE2AHIS A  25      23.116 -12.012  50.707  0.40 46.36           N  
ATOM    168  NE2BHIS A  25      20.806 -13.447  47.258  0.60 47.60           N  
ATOM    169  N   GLU A  26      17.937  -8.430  50.934  1.00 45.03           N  
ATOM    170  CA  GLU A  26      17.872  -7.252  51.787  1.00 45.28           C  
ATOM    171  C   GLU A  26      16.531  -7.124  52.525  1.00 44.60           C  
ATOM    172  O   GLU A  26      16.278  -6.104  53.159  1.00 44.16           O  
ATOM    173  CB  GLU A  26      18.145  -5.989  50.972  1.00 46.12           C  
ATOM    174  CG  GLU A  26      19.240  -6.138  49.912  1.00 49.34           C  
ATOM    175  CD  GLU A  26      20.613  -5.800  50.428  1.00 53.58           C  
ATOM    176  OE1 GLU A  26      21.559  -6.614  50.237  1.00 55.35           O  
ATOM    177  OE2 GLU A  26      20.750  -4.699  51.006  1.00 56.18           O  
ATOM    178  N   THR A  27      15.687  -8.156  52.435  1.00 43.32           N  
ATOM    179  CA  THR A  27      14.421  -8.191  53.136  1.00 43.30           C  
ATOM    180  C   THR A  27      14.569  -7.908  54.638  1.00 42.95           C  
ATOM    181  O   THR A  27      13.736  -7.212  55.203  1.00 42.92           O  
ATOM    182  CB  THR A  27      13.721  -9.539  52.961  1.00 43.31           C  
ATOM    183  OG1 THR A  27      13.483  -9.760  51.571  1.00 44.20           O  
ATOM    184  CG2 THR A  27      12.389  -9.539  53.684  1.00 43.84           C  
ATOM    185  N   ALA A  28      15.634  -8.430  55.253  1.00 42.17           N  
ATOM    186  CA  ALA A  28      15.884  -8.274  56.682  1.00 41.79           C  
ATOM    187  C   ALA A  28      16.114  -6.826  57.094  1.00 42.27           C  
ATOM    188  O   ALA A  28      15.678  -6.407  58.171  1.00 42.11           O  
ATOM    189  CB  ALA A  28      17.049  -9.142  57.111  1.00 41.86           C  
ATOM    190  N   LYS A  29      16.797  -6.063  56.245  1.00 41.88           N  
ATOM    191  CA  LYS A  29      16.996  -4.635  56.481  1.00 42.49           C  
ATOM    192  C   LYS A  29      15.656  -3.925  56.560  1.00 41.80           C  
ATOM    193  O   LYS A  29      15.460  -3.033  57.385  1.00 42.63           O  
ATOM    194  CB  LYS A  29      17.848  -4.022  55.376  1.00 42.08           C  
ATOM    195  CG  LYS A  29      19.202  -4.699  55.233  1.00 44.31           C  
ATOM    196  CD  LYS A  29      20.217  -3.867  54.420  1.00 44.38           C  
ATOM    197  CE  LYS A  29      21.601  -4.510  54.505  1.00 46.90           C  
ATOM    198  NZ  LYS A  29      21.608  -5.904  53.921  1.00 50.07           N  
ATOM    199  N   VAL A  30      14.726  -4.342  55.705  1.00 41.26           N  
ATOM    200  CA  VAL A  30      13.391  -3.749  55.653  1.00 40.54           C  
ATOM    201  C   VAL A  30      12.568  -4.095  56.908  1.00 40.62           C  
ATOM    202  O   VAL A  30      11.928  -3.222  57.488  1.00 39.81           O  
ATOM    203  CB  VAL A  30      12.639  -4.163  54.354  1.00 40.64           C  
ATOM    204  CG1 VAL A  30      11.239  -3.569  54.323  1.00 39.57           C  
ATOM    205  CG2 VAL A  30      13.446  -3.720  53.120  1.00 39.48           C  
ATOM    206  N   ILE A  31      12.591  -5.365  57.311  1.00 40.90           N  
ATOM    207  CA  ILE A  31      11.884  -5.819  58.512  1.00 41.44           C  
ATOM    208  C   ILE A  31      12.456  -5.146  59.767  1.00 41.79           C  
ATOM    209  O   ILE A  31      11.708  -4.763  60.664  1.00 41.30           O  
ATOM    210  CB  ILE A  31      11.938  -7.356  58.675  1.00 41.67           C  
ATOM    211  CG1 ILE A  31      11.274  -8.074  57.492  1.00 40.38           C  
ATOM    212  CG2 ILE A  31      11.286  -7.779  59.988  1.00 43.15           C  
ATOM    213  CD1 ILE A  31       9.821  -7.708  57.244  1.00 40.29           C  
ATOM    214  N   GLN A  32      13.773  -4.985  59.803  1.00 41.88           N  
ATOM    215  CA  GLN A  32      14.442  -4.274  60.880  1.00 43.12           C  
ATOM    216  C   GLN A  32      13.915  -2.846  61.034  1.00 42.94           C  
ATOM    217  O   GLN A  32      13.481  -2.469  62.120  1.00 43.11           O  
ATOM    218  CB  GLN A  32      15.936  -4.263  60.626  1.00 43.46           C  
ATOM    219  CG  GLN A  32      16.776  -4.065  61.853  1.00 48.33           C  
ATOM    220  CD  GLN A  32      18.162  -4.629  61.658  1.00 54.72           C  
ATOM    221  OE1 GLN A  32      19.142  -3.875  61.558  1.00 57.59           O  
ATOM    222  NE2 GLN A  32      18.259  -5.965  61.573  1.00 55.42           N  
ATOM    223  N   THR A  33      13.952  -2.070  59.947  1.00 42.25           N  
ATOM    224  CA  THR A  33      13.329  -0.740  59.872  1.00 42.06           C  
ATOM    225  C   THR A  33      11.889  -0.713  60.364  1.00 41.59           C  
ATOM    226  O   THR A  33      11.487   0.230  61.025  1.00 41.78           O  
ATOM    227  CB  THR A  33      13.348  -0.202  58.418  1.00 41.82           C  
ATOM    228  OG1 THR A  33      14.684  -0.290  57.918  1.00 44.25           O  
ATOM    229  CG2 THR A  33      12.903   1.232  58.353  1.00 40.60           C  
ATOM    230  N   ALA A  34      11.105  -1.726  60.012  1.00 41.52           N  
ATOM    231  CA  ALA A  34       9.699  -1.776  60.404  1.00 41.90           C  
ATOM    232  C   ALA A  34       9.528  -1.910  61.941  1.00 42.59           C  
ATOM    233  O   ALA A  34       8.720  -1.212  62.558  1.00 42.22           O  
ATOM    234  CB  ALA A  34       9.000  -2.891  59.671  1.00 40.99           C  
ATOM    235  N   PHE A  35      10.301  -2.805  62.542  1.00 43.67           N  
ATOM    236  CA  PHE A  35      10.349  -2.956  64.003  1.00 44.57           C  
ATOM    237  C   PHE A  35      10.870  -1.726  64.736  1.00 45.57           C  
ATOM    238  O   PHE A  35      10.358  -1.379  65.809  1.00 46.09           O  
ATOM    239  CB  PHE A  35      11.215  -4.145  64.366  1.00 44.03           C  
ATOM    240  CG  PHE A  35      10.477  -5.439  64.376  1.00 44.48           C  
ATOM    241  CD1 PHE A  35      10.263  -6.138  63.206  1.00 44.29           C  
ATOM    242  CD2 PHE A  35       9.987  -5.963  65.564  1.00 43.69           C  
ATOM    243  CE1 PHE A  35       9.580  -7.341  63.216  1.00 43.79           C  
ATOM    244  CE2 PHE A  35       9.300  -7.158  65.579  1.00 42.39           C  
ATOM    245  CZ  PHE A  35       9.100  -7.850  64.406  1.00 43.68           C  
ATOM    246  N   GLN A  36      11.892  -1.079  64.174  1.00 45.94           N  
ATOM    247  CA  GLN A  36      12.456   0.118  64.781  1.00 47.07           C  
ATOM    248  C   GLN A  36      11.495   1.307  64.702  1.00 46.27           C  
ATOM    249  O   GLN A  36      11.555   2.212  65.528  1.00 46.97           O  
ATOM    250  CB  GLN A  36      13.803   0.480  64.140  1.00 47.19           C  
ATOM    251  CG  GLN A  36      14.965  -0.510  64.431  1.00 49.60           C  
ATOM    252  CD  GLN A  36      16.238  -0.238  63.584  1.00 49.94           C  
ATOM    253  OE1 GLN A  36      16.261   0.654  62.712  1.00 52.87           O  
ATOM    254  NE2 GLN A  36      17.292  -1.024  63.837  1.00 52.32           N  
ATOM    255  N   ARG A  37      10.619   1.320  63.703  1.00 45.22           N  
ATOM    256  CA  ARG A  37       9.669   2.418  63.543  1.00 43.65           C  
ATOM    257  C   ARG A  37       8.368   2.199  64.308  1.00 42.90           C  
ATOM    258  O   ARG A  37       7.605   3.143  64.525  1.00 41.60           O  
ATOM    259  CB  ARG A  37       9.382   2.720  62.054  1.00 43.77           C  
ATOM    260  CG AARG A  37       9.957   4.088  61.661  0.50 44.28           C  
ATOM    261  CG BARG A  37      10.486   3.396  61.232  0.50 43.66           C  
ATOM    262  CD AARG A  37      10.656   4.119  60.309  0.50 45.37           C  
ATOM    263  CD BARG A  37      10.055   3.537  59.746  0.50 43.22           C  
ATOM    264  NE AARG A  37      11.315   5.412  60.103  0.50 46.21           N  
ATOM    265  NE BARG A  37       8.689   4.059  59.609  0.50 41.77           N  
ATOM    266  CZ AARG A  37      12.626   5.622  60.202  0.50 47.02           C  
ATOM    267  CZ BARG A  37       8.372   5.303  59.246  0.50 40.96           C  
ATOM    268  NH1AARG A  37      13.453   4.628  60.487  0.50 46.93           N  
ATOM    269  NH1BARG A  37       9.319   6.183  58.940  0.50 40.26           N  
ATOM    270  NH2AARG A  37      13.118   6.837  60.009  0.50 47.67           N  
ATOM    271  NH2BARG A  37       7.096   5.668  59.183  0.50 40.06           N  
ATOM    272  N   ALA A  38       8.106   0.956  64.705  1.00 42.40           N  
ATOM    273  CA  ALA A  38       6.861   0.634  65.399  1.00 42.31           C  
ATOM    274  C   ALA A  38       6.845   1.278  66.792  1.00 42.66           C  
ATOM    275  O   ALA A  38       7.903   1.429  67.420  1.00 42.63           O  
ATOM    276  CB  ALA A  38       6.671  -0.869  65.480  1.00 41.91           C  
ATOM    277  N   SER A  39       5.661   1.717  67.225  1.00 42.94           N  
ATOM    278  CA  SER A  39       5.425   2.200  68.590  1.00 43.76           C  
ATOM    279  C   SER A  39       4.935   1.035  69.479  1.00 44.04           C  
ATOM    280  O   SER A  39       4.036   0.293  69.082  1.00 44.52           O  
ATOM    281  CB  SER A  39       4.367   3.313  68.587  1.00 43.79           C  
ATOM    282  OG  SER A  39       4.951   4.577  68.293  1.00 44.41           O  
ATOM    283  N   TYR A  40       5.511   0.866  70.668  1.00 44.02           N  
ATOM    284  CA  TYR A  40       4.976  -0.126  71.611  1.00 44.19           C  
ATOM    285  C   TYR A  40       4.484   0.586  72.876  1.00 44.22           C  
ATOM    286  O   TYR A  40       5.293   0.981  73.723  1.00 44.90           O  
ATOM    287  CB  TYR A  40       6.018  -1.203  71.928  1.00 43.78           C  
ATOM    288  CG  TYR A  40       6.768  -1.665  70.705  1.00 43.49           C  
ATOM    289  CD1 TYR A  40       8.030  -1.146  70.409  1.00 42.25           C  
ATOM    290  CD2 TYR A  40       6.209  -2.589  69.826  1.00 43.97           C  
ATOM    291  CE1 TYR A  40       8.715  -1.526  69.288  1.00 42.04           C  
ATOM    292  CE2 TYR A  40       6.901  -2.994  68.683  1.00 44.18           C  
ATOM    293  CZ  TYR A  40       8.156  -2.449  68.425  1.00 43.69           C  
ATOM    294  OH  TYR A  40       8.869  -2.842  67.320  1.00 43.94           O  
ATOM    295  N   PRO A  41       3.160   0.748  73.015  1.00 43.91           N  
ATOM    296  CA  PRO A  41       2.660   1.600  74.093  1.00 44.05           C  
ATOM    297  C   PRO A  41       2.761   0.934  75.494  1.00 44.36           C  
ATOM    298  O   PRO A  41       2.688  -0.311  75.621  1.00 43.51           O  
ATOM    299  CB  PRO A  41       1.182   1.815  73.723  1.00 43.99           C  
ATOM    300  CG  PRO A  41       0.923   1.022  72.465  1.00 43.83           C  
ATOM    301  CD  PRO A  41       2.072   0.095  72.271  1.00 43.95           C  
ATOM    302  N   ASP A  42       2.907   1.767  76.528  1.00 44.66           N  
ATOM    303  CA  ASP A  42       2.880   1.310  77.924  1.00 44.24           C  
ATOM    304  C   ASP A  42       1.666   0.417  78.126  1.00 44.16           C  
ATOM    305  O   ASP A  42       0.563   0.766  77.694  1.00 44.01           O  
ATOM    306  CB  ASP A  42       2.751   2.497  78.878  1.00 44.28           C  
ATOM    307  CG  ASP A  42       4.033   3.278  79.043  1.00 45.44           C  
ATOM    308  OD1 ASP A  42       5.054   2.949  78.402  1.00 47.99           O  
ATOM    309  OD2 ASP A  42       4.023   4.245  79.837  1.00 47.83           O  
ATOM    310  N   ILE A  43       1.875  -0.720  78.784  1.00 44.05           N  
ATOM    311  CA  ILE A  43       0.787  -1.597  79.235  1.00 44.27           C  
ATOM    312  C   ILE A  43       0.534  -1.406  80.747  1.00 44.80           C  
ATOM    313  O   ILE A  43       1.397  -1.716  81.562  1.00 45.74           O  
ATOM    314  CB  ILE A  43       1.121  -3.074  78.994  1.00 43.64           C  
ATOM    315  CG1 ILE A  43       1.544  -3.311  77.541  1.00 42.42           C  
ATOM    316  CG2 ILE A  43      -0.051  -3.937  79.378  1.00 43.65           C  
ATOM    317  CD1 ILE A  43       2.468  -4.462  77.395  1.00 38.78           C  
ATOM    318  N   THR A  44      -0.653  -0.929  81.101  1.00 44.53           N  
ATOM    319  CA  THR A  44      -0.980  -0.576  82.467  1.00 44.75           C  
ATOM    320  C   THR A  44      -2.339  -1.149  82.862  1.00 44.84           C  
ATOM    321  O   THR A  44      -3.123  -1.562  82.007  1.00 44.58           O  
ATOM    322  CB  THR A  44      -1.065   0.955  82.645  1.00 45.09           C  
ATOM    323  OG1 THR A  44      -2.266   1.431  82.027  1.00 45.51           O  
ATOM    324  CG2 THR A  44       0.145   1.675  82.030  1.00 44.71           C  
ATOM    325  N   GLY A  45      -2.609  -1.155  84.168  1.00 44.80           N  
ATOM    326  CA  GLY A  45      -3.886  -1.597  84.738  1.00 44.57           C  
ATOM    327  C   GLY A  45      -3.803  -1.786  86.251  1.00 44.62           C  
ATOM    328  O   GLY A  45      -2.773  -1.539  86.865  1.00 44.30           O  
ATOM    329  N   GLU A  46      -4.901  -2.219  86.845  1.00 45.26           N  
ATOM    330  CA  GLU A  46      -4.978  -2.473  88.275  1.00 46.19           C  
ATOM    331  C   GLU A  46      -5.994  -3.567  88.455  1.00 45.98           C  
ATOM    332  O   GLU A  46      -7.186  -3.352  88.261  1.00 46.69           O  
ATOM    333  CB  GLU A  46      -5.373  -1.216  89.058  1.00 45.83           C  
ATOM    334  CG  GLU A  46      -5.450  -1.437  90.575  1.00 47.44           C  
ATOM    335  CD  GLU A  46      -5.524  -0.145  91.393  1.00 47.95           C  
ATOM    336  OE1 GLU A  46      -5.831   0.936  90.854  1.00 50.56           O  
ATOM    337  OE2 GLU A  46      -5.267  -0.210  92.603  1.00 51.17           O  
ATOM    338  N   LYS A  47      -5.500  -4.747  88.814  1.00 46.27           N  
ATOM    339  CA  LYS A  47      -6.279  -5.977  88.861  1.00 46.03           C  
ATOM    340  C   LYS A  47      -6.183  -6.598  90.268  1.00 46.13           C  
ATOM    341  O   LYS A  47      -5.143  -6.507  90.922  1.00 46.37           O  
ATOM    342  CB  LYS A  47      -5.685  -6.943  87.834  1.00 46.08           C  
ATOM    343  CG  LYS A  47      -6.644  -7.964  87.286  1.00 46.98           C  
ATOM    344  CD  LYS A  47      -6.154  -8.533  85.950  1.00 48.92           C  
ATOM    345  CE  LYS A  47      -7.198  -9.473  85.315  1.00 50.46           C  
ATOM    346  NZ  LYS A  47      -8.486  -8.771  84.935  1.00 49.68           N  
ATOM    347  N   ALA A  48      -7.259  -7.222  90.726  1.00 46.02           N  
ATOM    348  CA  ALA A  48      -7.218  -8.046  91.922  1.00 46.32           C  
ATOM    349  C   ALA A  48      -6.398  -9.286  91.599  1.00 46.15           C  
ATOM    350  O   ALA A  48      -6.704  -9.986  90.639  1.00 46.47           O  
ATOM    351  CB  ALA A  48      -8.622  -8.441  92.348  1.00 46.53           C  
ATOM    352  N   MET A  49      -5.330  -9.508  92.363  1.00 45.63           N  
ATOM    353  CA  MET A  49      -4.506 -10.707  92.260  1.00 45.44           C  
ATOM    354  C   MET A  49      -4.790 -11.643  93.434  1.00 45.92           C  
ATOM    355  O   MET A  49      -5.094 -11.203  94.555  1.00 45.78           O  
ATOM    356  CB  MET A  49      -3.004 -10.368  92.246  1.00 44.88           C  
ATOM    357  CG  MET A  49      -2.585  -9.143  91.422  1.00 45.22           C  
ATOM    358  SD  MET A  49      -2.576  -9.407  89.626  1.00 42.03           S  
ATOM    359  CE  MET A  49      -2.226  -7.771  88.971  1.00 43.92           C  
ATOM    360  N   MET A  50      -4.641 -12.936  93.182  1.00 46.28           N  
ATOM    361  CA  MET A  50      -4.956 -13.963  94.161  1.00 46.97           C  
ATOM    362  C   MET A  50      -4.196 -13.759  95.472  1.00 46.18           C  
ATOM    363  O   MET A  50      -2.970 -13.644  95.461  1.00 46.42           O  
ATOM    364  CB  MET A  50      -4.618 -15.333  93.580  1.00 47.84           C  
ATOM    365  CG  MET A  50      -5.505 -16.433  94.116  1.00 51.55           C  
ATOM    366  SD  MET A  50      -7.043 -16.562  93.194  1.00 59.55           S  
ATOM    367  CE  MET A  50      -6.578 -17.753  91.928  1.00 58.69           C  
ATOM    368  N   LEU A  51      -4.932 -13.724  96.588  1.00 45.33           N  
ATOM    369  CA  LEU A  51      -4.381 -13.581  97.973  1.00 44.43           C  
ATOM    370  C   LEU A  51      -3.719 -12.246  98.272  1.00 44.15           C  
ATOM    371  O   LEU A  51      -3.320 -11.987  99.413  1.00 44.28           O  
ATOM    372  CB  LEU A  51      -3.403 -14.714  98.332  1.00 43.73           C  
ATOM    373  CG  LEU A  51      -3.901 -16.149  98.162  1.00 44.35           C  
ATOM    374  CD1 LEU A  51      -2.893 -17.136  98.696  1.00 43.54           C  
ATOM    375  CD2 LEU A  51      -5.261 -16.345  98.838  1.00 44.69           C  
ATOM    376  N   LEU A  52      -3.629 -11.391  97.257  1.00 43.79           N  
ATOM    377  CA  LEU A  52      -2.786 -10.203  97.309  1.00 43.31           C  
ATOM    378  C   LEU A  52      -3.552  -8.888  97.151  1.00 43.36           C  
ATOM    379  O   LEU A  52      -2.949  -7.813  97.232  1.00 44.07           O  
ATOM    380  CB  LEU A  52      -1.712 -10.280  96.214  1.00 42.93           C  
ATOM    381  CG  LEU A  52      -0.261 -10.743  96.359  1.00 43.64           C  
ATOM    382  CD1 LEU A  52       0.195 -10.703  97.815  1.00 43.58           C  
ATOM    383  CD2 LEU A  52       0.021 -12.106  95.729  1.00 42.25           C  
ATOM    384  N   GLY A  53      -4.857  -8.951  96.910  1.00 43.22           N  
ATOM    385  CA  GLY A  53      -5.649  -7.719  96.681  1.00 43.69           C  
ATOM    386  C   GLY A  53      -5.390  -6.957  95.375  1.00 43.86           C  
ATOM    387  O   GLY A  53      -4.779  -7.488  94.444  1.00 44.27           O  
ATOM    388  N   GLN A  54      -5.856  -5.708  95.300  1.00 43.79           N  
ATOM    389  CA  GLN A  54      -5.666  -4.890  94.110  1.00 43.36           C  
ATOM    390  C   GLN A  54      -4.201  -4.565  93.976  1.00 42.87           C  
ATOM    391  O   GLN A  54      -3.575  -4.057  94.912  1.00 42.37           O  
ATOM    392  CB  GLN A  54      -6.454  -3.572  94.165  1.00 43.90           C  
ATOM    393  CG  GLN A  54      -7.947  -3.677  94.053  1.00 46.78           C  
ATOM    394  CD  GLN A  54      -8.438  -4.411  92.791  1.00 50.62           C  
ATOM    395  OE1 GLN A  54      -9.180  -5.379  92.891  1.00 49.64           O  
ATOM    396  NE2 GLN A  54      -8.044  -3.930  91.612  1.00 52.11           N  
ATOM    397  N   VAL A  55      -3.664  -4.874  92.803  1.00 41.83           N  
ATOM    398  CA  VAL A  55      -2.287  -4.579  92.455  1.00 41.11           C  
ATOM    399  C   VAL A  55      -2.331  -3.698  91.211  1.00 40.99           C  
ATOM    400  O   VAL A  55      -2.957  -4.055  90.217  1.00 41.04           O  
ATOM    401  CB  VAL A  55      -1.480  -5.883  92.183  1.00 40.90           C  
ATOM    402  CG1 VAL A  55      -0.085  -5.577  91.709  1.00 40.75           C  
ATOM    403  CG2 VAL A  55      -1.410  -6.752  93.434  1.00 41.34           C  
ATOM    404  N   LYS A  56      -1.688  -2.537  91.291  1.00 40.49           N  
ATOM    405  CA  LYS A  56      -1.564  -1.621  90.181  1.00 40.13           C  
ATOM    406  C   LYS A  56      -0.212  -1.851  89.526  1.00 40.17           C  
ATOM    407  O   LYS A  56       0.817  -1.843  90.211  1.00 39.91           O  
ATOM    408  CB  LYS A  56      -1.680  -0.186  90.689  1.00 40.41           C  
ATOM    409  CG  LYS A  56      -1.363   0.892  89.669  1.00 42.29           C  
ATOM    410  CD  LYS A  56      -2.080   2.178  90.047  1.00 46.24           C  
ATOM    411  CE  LYS A  56      -2.023   3.191  88.927  1.00 48.41           C  
ATOM    412  NZ  LYS A  56      -0.760   3.978  89.004  1.00 49.46           N  
ATOM    413  N   TYR A  57      -0.213  -2.047  88.204  1.00 39.72           N  
ATOM    414  CA  TYR A  57       1.000  -2.428  87.454  1.00 39.67           C  
ATOM    415  C   TYR A  57       1.157  -1.650  86.136  1.00 40.09           C  
ATOM    416  O   TYR A  57       0.189  -1.102  85.600  1.00 39.52           O  
ATOM    417  CB  TYR A  57       0.973  -3.937  87.167  1.00 39.07           C  
ATOM    418  CG  TYR A  57      -0.177  -4.364  86.271  1.00 39.32           C  
ATOM    419  CD1 TYR A  57      -0.040  -4.329  84.867  1.00 38.43           C  
ATOM    420  CD2 TYR A  57      -1.401  -4.808  86.815  1.00 37.04           C  
ATOM    421  CE1 TYR A  57      -1.095  -4.716  84.025  1.00 37.69           C  
ATOM    422  CE2 TYR A  57      -2.456  -5.200  85.992  1.00 36.43           C  
ATOM    423  CZ  TYR A  57      -2.291  -5.152  84.582  1.00 38.59           C  
ATOM    424  OH  TYR A  57      -3.317  -5.528  83.736  1.00 37.58           O  
ATOM    425  N   GLY A  58       2.380  -1.593  85.628  1.00 40.43           N  
ATOM    426  CA  GLY A  58       2.631  -1.034  84.310  1.00 41.23           C  
ATOM    427  C   GLY A  58       3.925  -1.555  83.730  1.00 41.96           C  
ATOM    428  O   GLY A  58       4.937  -1.598  84.428  1.00 42.43           O  
ATOM    429  N   LEU A  59       3.904  -1.984  82.468  1.00 42.38           N  
ATOM    430  CA  LEU A  59       5.162  -2.220  81.749  1.00 42.31           C  
ATOM    431  C   LEU A  59       5.414  -0.969  80.929  1.00 42.91           C  
ATOM    432  O   LEU A  59       4.558  -0.533  80.147  1.00 42.58           O  
ATOM    433  CB  LEU A  59       5.115  -3.455  80.848  1.00 42.73           C  
ATOM    434  CG  LEU A  59       4.442  -4.802  81.187  1.00 42.60           C  
ATOM    435  CD1 LEU A  59       5.377  -6.012  81.074  1.00 41.61           C  
ATOM    436  CD2 LEU A  59       3.687  -4.797  82.517  1.00 41.67           C  
ATOM    437  N   HIS A  60       6.588  -0.383  81.129  1.00 42.85           N  
ATOM    438  CA  HIS A  60       6.872   0.959  80.656  1.00 42.76           C  
ATOM    439  C   HIS A  60       8.108   1.019  79.769  1.00 43.29           C  
ATOM    440  O   HIS A  60       9.037   0.211  79.912  1.00 42.85           O  
ATOM    441  CB  HIS A  60       7.076   1.892  81.845  1.00 42.53           C  
ATOM    442  CG  HIS A  60       5.827   2.177  82.622  1.00 41.98           C  
ATOM    443  ND1 HIS A  60       5.582   1.639  83.866  1.00 42.24           N  
ATOM    444  CD2 HIS A  60       4.763   2.965  82.341  1.00 40.32           C  
ATOM    445  CE1 HIS A  60       4.415   2.071  84.310  1.00 41.14           C  
ATOM    446  NE2 HIS A  60       3.895   2.871  83.401  1.00 40.94           N  
ATOM    447  N   ASN A  61       8.113   2.003  78.864  1.00 43.90           N  
ATOM    448  CA  ASN A  61       9.251   2.275  77.993  1.00 44.48           C  
ATOM    449  C   ASN A  61       9.723   1.024  77.262  1.00 43.76           C  
ATOM    450  O   ASN A  61      10.901   0.720  77.279  1.00 43.21           O  
ATOM    451  CB  ASN A  61      10.405   2.921  78.780  1.00 45.20           C  
ATOM    452  CG  ASN A  61      11.509   3.476  77.867  1.00 49.35           C  
ATOM    453  OD1 ASN A  61      11.296   3.681  76.663  1.00 53.80           O  
ATOM    454  ND2 ASN A  61      12.691   3.728  78.439  1.00 50.57           N  
ATOM    455  N   ILE A  62       8.794   0.292  76.642  1.00 43.98           N  
ATOM    456  CA  ILE A  62       9.146  -0.913  75.878  1.00 44.84           C  
ATOM    457  C   ILE A  62       9.919  -0.509  74.616  1.00 45.82           C  
ATOM    458  O   ILE A  62       9.445   0.281  73.801  1.00 45.10           O  
ATOM    459  CB  ILE A  62       7.911  -1.772  75.539  1.00 45.18           C  
ATOM    460  CG1 ILE A  62       7.167  -2.170  76.835  1.00 44.11           C  
ATOM    461  CG2 ILE A  62       8.317  -2.983  74.681  1.00 44.43           C  
ATOM    462  CD1 ILE A  62       5.767  -2.738  76.613  1.00 45.14           C  
ATOM    463  N   GLN A  63      11.126  -1.045  74.502  1.00 46.53           N  
ATOM    464  CA  GLN A  63      12.089  -0.636  73.508  1.00 47.64           C  
ATOM    465  C   GLN A  63      12.647  -1.908  72.928  1.00 47.61           C  
ATOM    466  O   GLN A  63      12.850  -2.866  73.664  1.00 47.53           O  
ATOM    467  CB  GLN A  63      13.227   0.076  74.223  1.00 48.14           C  
ATOM    468  CG  GLN A  63      13.700   1.312  73.572  1.00 50.92           C  
ATOM    469  CD  GLN A  63      13.059   2.541  74.157  1.00 55.48           C  
ATOM    470  OE1 GLN A  63      11.854   2.772  73.985  1.00 57.04           O  
ATOM    471  NE2 GLN A  63      13.868   3.367  74.839  1.00 56.23           N  
ATOM    472  N   ILE A  64      12.913  -1.938  71.624  1.00 48.00           N  
ATOM    473  CA  ILE A  64      13.644  -3.069  71.058  1.00 47.94           C  
ATOM    474  C   ILE A  64      15.104  -2.997  71.468  1.00 48.03           C  
ATOM    475  O   ILE A  64      15.746  -1.959  71.346  1.00 48.42           O  
ATOM    476  CB  ILE A  64      13.524  -3.177  69.528  1.00 48.04           C  
ATOM    477  CG1 ILE A  64      12.079  -3.438  69.155  1.00 48.11           C  
ATOM    478  CG2 ILE A  64      14.354  -4.351  69.009  1.00 47.73           C  
ATOM    479  CD1 ILE A  64      11.908  -3.938  67.776  1.00 49.94           C  
ATOM    480  N   SER A  65      15.617  -4.126  71.931  1.00 48.19           N  
ATOM    481  CA  SER A  65      16.974  -4.226  72.426  1.00 48.58           C  
ATOM    482  C   SER A  65      17.872  -5.033  71.483  1.00 48.84           C  
ATOM    483  O   SER A  65      19.060  -4.744  71.341  1.00 49.65           O  
ATOM    484  CB  SER A  65      16.947  -4.859  73.813  1.00 48.04           C  
ATOM    485  OG  SER A  65      18.200  -5.409  74.126  1.00 49.26           O  
ATOM    486  N   HIS A  66      17.306  -6.046  70.845  1.00 49.16           N  
ATOM    487  CA  HIS A  66      18.031  -6.857  69.877  1.00 49.20           C  
ATOM    488  C   HIS A  66      17.031  -7.321  68.829  1.00 48.74           C  
ATOM    489  O   HIS A  66      15.864  -7.533  69.144  1.00 47.84           O  
ATOM    490  CB  HIS A  66      18.682  -8.055  70.562  1.00 49.53           C  
ATOM    491  CG  HIS A  66      19.158  -9.116  69.615  1.00 52.44           C  
ATOM    492  ND1 HIS A  66      18.360 -10.171  69.211  1.00 54.76           N  
ATOM    493  CD2 HIS A  66      20.349  -9.283  68.986  1.00 54.44           C  
ATOM    494  CE1 HIS A  66      19.043 -10.945  68.381  1.00 54.70           C  
ATOM    495  NE2 HIS A  66      20.252 -10.429  68.229  1.00 54.28           N  
ATOM    496  N   LEU A  67      17.492  -7.448  67.581  1.00 48.16           N  
ATOM    497  CA  LEU A  67      16.678  -7.993  66.498  1.00 47.14           C  
ATOM    498  C   LEU A  67      17.569  -8.665  65.457  1.00 46.84           C  
ATOM    499  O   LEU A  67      18.504  -8.044  64.950  1.00 46.81           O  
ATOM    500  CB  LEU A  67      15.883  -6.875  65.833  1.00 47.14           C  
ATOM    501  CG  LEU A  67      14.495  -7.155  65.229  1.00 46.61           C  
ATOM    502  CD1 LEU A  67      14.075  -5.932  64.486  1.00 47.54           C  
ATOM    503  CD2 LEU A  67      14.434  -8.346  64.299  1.00 47.20           C  
ATOM    504  N   SER A  68      17.300  -9.939  65.176  1.00 46.01           N  
ATOM    505  CA  SER A  68      17.913 -10.644  64.049  1.00 45.56           C  
ATOM    506  C   SER A  68      16.834 -11.400  63.274  1.00 45.47           C  
ATOM    507  O   SER A  68      15.701 -11.526  63.751  1.00 45.25           O  
ATOM    508  CB  SER A  68      19.013 -11.603  64.518  1.00 45.68           C  
ATOM    509  OG  SER A  68      18.472 -12.757  65.144  1.00 45.24           O  
ATOM    510  N   ILE A  69      17.184 -11.889  62.083  1.00 44.95           N  
ATOM    511  CA  ILE A  69      16.263 -12.655  61.229  1.00 44.61           C  
ATOM    512  C   ILE A  69      17.042 -13.822  60.637  1.00 44.42           C  
ATOM    513  O   ILE A  69      18.188 -13.649  60.233  1.00 44.76           O  
ATOM    514  CB  ILE A  69      15.632 -11.755  60.125  1.00 44.89           C  
ATOM    515  CG1 ILE A  69      14.689 -10.728  60.757  1.00 44.45           C  
ATOM    516  CG2 ILE A  69      14.868 -12.580  59.104  1.00 45.76           C  
ATOM    517  CD1 ILE A  69      14.699  -9.379  60.118  1.00 46.00           C  
ATOM    518  N   ALA A  70      16.440 -15.008  60.621  1.00 43.55           N  
ATOM    519  CA  ALA A  70      17.096 -16.218  60.117  1.00 43.49           C  
ATOM    520  C   ALA A  70      17.101 -16.320  58.585  1.00 43.54           C  
ATOM    521  O   ALA A  70      18.130 -16.646  57.986  1.00 43.88           O  
ATOM    522  CB  ALA A  70      16.447 -17.467  60.714  1.00 42.83           C  
ATOM    523  N   SER A  71      15.946 -16.066  57.962  1.00 43.13           N  
ATOM    524  CA  SER A  71      15.801 -16.187  56.510  1.00 42.38           C  
ATOM    525  C   SER A  71      14.472 -15.678  55.989  1.00 41.75           C  
ATOM    526  O   SER A  71      13.505 -15.534  56.740  1.00 41.27           O  
ATOM    527  CB  SER A  71      15.953 -17.642  56.096  1.00 42.26           C  
ATOM    528  OG  SER A  71      15.145 -18.445  56.916  1.00 43.35           O  
ATOM    529  N   SER A  72      14.443 -15.418  54.683  1.00 41.22           N  
ATOM    530  CA  SER A  72      13.249 -14.962  53.978  1.00 40.87           C  
ATOM    531  C   SER A  72      13.208 -15.571  52.588  1.00 40.86           C  
ATOM    532  O   SER A  72      14.239 -15.691  51.937  1.00 39.63           O  
ATOM    533  CB  SER A  72      13.222 -13.441  53.872  1.00 40.92           C  
ATOM    534  OG  SER A  72      14.487 -12.934  53.465  1.00 42.03           O  
ATOM    535  N   GLN A  73      12.010 -15.976  52.165  1.00 41.23           N  
ATOM    536  CA  GLN A  73      11.769 -16.475  50.827  1.00 41.94           C  
ATOM    537  C   GLN A  73      10.778 -15.560  50.155  1.00 42.05           C  
ATOM    538  O   GLN A  73      10.010 -14.883  50.831  1.00 42.20           O  
ATOM    539  CB  GLN A  73      11.203 -17.880  50.873  1.00 42.26           C  
ATOM    540  CG  GLN A  73      12.184 -18.894  51.391  1.00 44.77           C  
ATOM    541  CD  GLN A  73      12.178 -18.964  52.898  1.00 47.21           C  
ATOM    542  OE1 GLN A  73      13.229 -18.924  53.545  1.00 49.33           O  
ATOM    543  NE2 GLN A  73      10.991 -19.056  53.468  1.00 47.07           N  
ATOM    544  N   VAL A  74      10.817 -15.510  48.825  1.00 42.34           N  
ATOM    545  CA  VAL A  74       9.864 -14.697  48.048  1.00 42.38           C  
ATOM    546  C   VAL A  74       9.212 -15.562  46.963  1.00 42.40           C  
ATOM    547  O   VAL A  74       9.848 -16.424  46.359  1.00 42.91           O  
ATOM    548  CB  VAL A  74      10.497 -13.360  47.521  1.00 42.20           C  
ATOM    549  CG1 VAL A  74      11.666 -13.625  46.573  1.00 43.80           C  
ATOM    550  CG2 VAL A  74       9.458 -12.483  46.862  1.00 41.94           C  
ATOM    551  N   GLU A  75       7.920 -15.383  46.783  1.00 42.18           N  
ATOM    552  CA  GLU A  75       7.196 -16.123  45.784  1.00 42.46           C  
ATOM    553  C   GLU A  75       6.146 -15.223  45.171  1.00 41.36           C  
ATOM    554  O   GLU A  75       5.539 -14.412  45.863  1.00 40.55           O  
ATOM    555  CB  GLU A  75       6.580 -17.388  46.391  1.00 43.41           C  
ATOM    556  CG  GLU A  75       5.117 -17.609  46.029  1.00 47.30           C  
ATOM    557  CD  GLU A  75       4.764 -19.070  45.789  1.00 53.32           C  
ATOM    558  OE1 GLU A  75       3.650 -19.321  45.261  1.00 55.51           O  
ATOM    559  OE2 GLU A  75       5.596 -19.957  46.111  1.00 55.66           O  
ATOM    560  N   LEU A  76       5.961 -15.346  43.857  1.00 40.93           N  
ATOM    561  CA  LEU A  76       4.929 -14.596  43.160  1.00 40.20           C  
ATOM    562  C   LEU A  76       3.731 -15.486  42.975  1.00 39.90           C  
ATOM    563  O   LEU A  76       3.855 -16.599  42.521  1.00 39.65           O  
ATOM    564  CB  LEU A  76       5.436 -14.105  41.804  1.00 40.32           C  
ATOM    565  CG  LEU A  76       6.626 -13.148  41.849  1.00 40.85           C  
ATOM    566  CD1 LEU A  76       7.208 -12.899  40.463  1.00 39.57           C  
ATOM    567  CD2 LEU A  76       6.168 -11.867  42.496  1.00 40.96           C  
ATOM    568  N   VAL A  77       2.562 -14.989  43.339  1.00 40.44           N  
ATOM    569  CA  VAL A  77       1.351 -15.760  43.182  1.00 40.67           C  
ATOM    570  C   VAL A  77       0.574 -15.108  42.050  1.00 41.66           C  
ATOM    571  O   VAL A  77       0.206 -13.924  42.137  1.00 41.13           O  
ATOM    572  CB  VAL A  77       0.549 -15.829  44.504  1.00 40.33           C  
ATOM    573  CG1 VAL A  77      -0.769 -16.541  44.306  1.00 40.13           C  
ATOM    574  CG2 VAL A  77       1.384 -16.509  45.585  1.00 39.63           C  
ATOM    575  N   GLU A  78       0.365 -15.886  40.982  1.00 42.41           N  
ATOM    576  CA  GLU A  78      -0.234 -15.410  39.733  1.00 43.52           C  
ATOM    577  C   GLU A  78      -1.498 -14.622  39.996  1.00 43.55           C  
ATOM    578  O   GLU A  78      -2.409 -15.124  40.647  1.00 43.69           O  
ATOM    579  CB  GLU A  78      -0.560 -16.600  38.828  1.00 43.97           C  
ATOM    580  CG  GLU A  78      -1.105 -16.247  37.429  1.00 47.83           C  
ATOM    581  CD  GLU A  78      -0.122 -16.486  36.270  1.00 52.20           C  
ATOM    582  OE1 GLU A  78      -0.502 -16.112  35.130  1.00 55.30           O  
ATOM    583  OE2 GLU A  78       1.002 -17.042  36.466  1.00 51.45           O  
ATOM    584  N   ALA A  79      -1.541 -13.388  39.490  1.00 43.37           N  
ATOM    585  CA  ALA A  79      -2.716 -12.520  39.612  1.00 43.65           C  
ATOM    586  C   ALA A  79      -3.102 -12.136  41.044  1.00 44.00           C  
ATOM    587  O   ALA A  79      -4.234 -11.691  41.291  1.00 44.46           O  
ATOM    588  CB  ALA A  79      -3.921 -13.148  38.899  1.00 43.95           C  
ATOM    589  N   LYS A  80      -2.184 -12.271  41.993  1.00 43.72           N  
ATOM    590  CA  LYS A  80      -2.571 -12.031  43.374  1.00 43.37           C  
ATOM    591  C   LYS A  80      -1.593 -11.193  44.139  1.00 42.23           C  
ATOM    592  O   LYS A  80      -1.924 -10.088  44.533  1.00 42.01           O  
ATOM    593  CB  LYS A  80      -2.853 -13.338  44.099  1.00 43.95           C  
ATOM    594  CG  LYS A  80      -4.307 -13.696  44.051  1.00 47.82           C  
ATOM    595  CD  LYS A  80      -4.502 -15.201  44.134  1.00 53.26           C  
ATOM    596  CE  LYS A  80      -5.897 -15.594  43.614  1.00 55.73           C  
ATOM    597  NZ  LYS A  80      -6.124 -17.071  43.745  1.00 57.38           N  
ATOM    598  N   SER A  81      -0.380 -11.694  44.334  1.00 41.48           N  
ATOM    599  CA  SER A  81       0.502 -11.040  45.271  1.00 40.54           C  
ATOM    600  C   SER A  81       1.929 -11.510  45.186  1.00 39.91           C  
ATOM    601  O   SER A  81       2.215 -12.565  44.629  1.00 39.96           O  
ATOM    602  CB  SER A  81      -0.046 -11.227  46.706  1.00 40.69           C  
ATOM    603  OG  SER A  81      -0.302 -12.593  47.003  1.00 38.10           O  
ATOM    604  N   ILE A  82       2.809 -10.676  45.731  1.00 39.95           N  
ATOM    605  CA  ILE A  82       4.202 -11.000  46.056  1.00 40.59           C  
ATOM    606  C   ILE A  82       4.202 -11.433  47.523  1.00 40.21           C  
ATOM    607  O   ILE A  82       3.863 -10.636  48.404  1.00 39.85           O  
ATOM    608  CB  ILE A  82       5.108  -9.737  45.954  1.00 41.06           C  
ATOM    609  CG1 ILE A  82       4.872  -9.005  44.631  1.00 41.98           C  
ATOM    610  CG2 ILE A  82       6.590 -10.101  46.138  1.00 41.29           C  
ATOM    611  CD1 ILE A  82       4.950  -7.535  44.742  1.00 43.71           C  
ATOM    612  N   ASP A  83       4.560 -12.693  47.764  1.00 40.25           N  
ATOM    613  CA  ASP A  83       4.433 -13.343  49.072  1.00 40.20           C  
ATOM    614  C   ASP A  83       5.804 -13.561  49.694  1.00 40.02           C  
ATOM    615  O   ASP A  83       6.573 -14.375  49.202  1.00 40.33           O  
ATOM    616  CB  ASP A  83       3.753 -14.704  48.914  1.00 40.72           C  
ATOM    617  CG  ASP A  83       2.273 -14.604  48.591  1.00 42.92           C  
ATOM    618  OD1 ASP A  83       1.633 -15.680  48.594  1.00 45.44           O  
ATOM    619  OD2 ASP A  83       1.739 -13.484  48.343  1.00 43.41           O  
ATOM    620  N   VAL A  84       6.125 -12.838  50.766  1.00 39.70           N  
ATOM    621  CA  VAL A  84       7.390 -13.091  51.446  1.00 39.84           C  
ATOM    622  C   VAL A  84       7.236 -13.681  52.846  1.00 40.00           C  
ATOM    623  O   VAL A  84       6.478 -13.176  53.679  1.00 40.08           O  
ATOM    624  CB  VAL A  84       8.441 -11.922  51.321  1.00 40.04           C  
ATOM    625  CG1 VAL A  84       7.922 -10.763  50.474  1.00 39.66           C  
ATOM    626  CG2 VAL A  84       8.991 -11.491  52.669  1.00 39.28           C  
ATOM    627  N   SER A  85       7.907 -14.810  53.032  1.00 40.07           N  
ATOM    628  CA  SER A  85       7.901 -15.562  54.262  1.00 40.38           C  
ATOM    629  C   SER A  85       9.193 -15.225  54.920  1.00 40.54           C  
ATOM    630  O   SER A  85      10.231 -15.242  54.268  1.00 41.02           O  
ATOM    631  CB  SER A  85       7.895 -17.054  53.986  1.00 40.76           C  
ATOM    632  OG  SER A  85       6.905 -17.399  53.047  1.00 40.92           O  
ATOM    633  N   ILE A  86       9.121 -14.902  56.208  1.00 39.98           N  
ATOM    634  CA  ILE A  86      10.278 -14.617  57.020  1.00 39.56           C  
ATOM    635  C   ILE A  86      10.263 -15.559  58.226  1.00 40.11           C  
ATOM    636  O   ILE A  86       9.273 -15.628  58.957  1.00 39.97           O  
ATOM    637  CB  ILE A  86      10.253 -13.154  57.452  1.00 39.86           C  
ATOM    638  CG1 ILE A  86      10.241 -12.259  56.210  1.00 38.10           C  
ATOM    639  CG2 ILE A  86      11.422 -12.832  58.370  1.00 38.36           C  
ATOM    640  CD1 ILE A  86       9.372 -11.096  56.395  1.00 41.14           C  
ATOM    641  N   GLN A  87      11.337 -16.330  58.385  1.00 40.40           N  
ATOM    642  CA  GLN A  87      11.443 -17.280  59.485  1.00 40.91           C  
ATOM    643  C   GLN A  87      12.319 -16.752  60.594  1.00 40.86           C  
ATOM    644  O   GLN A  87      13.431 -16.247  60.354  1.00 40.11           O  
ATOM    645  CB  GLN A  87      12.018 -18.618  59.040  1.00 41.11           C  
ATOM    646  CG  GLN A  87      11.114 -19.433  58.150  1.00 43.06           C  
ATOM    647  CD  GLN A  87      11.350 -19.112  56.691  1.00 45.88           C  
ATOM    648  OE1 GLN A  87      10.435 -19.199  55.868  1.00 47.07           O  
ATOM    649  NE2 GLN A  87      12.584 -18.718  56.360  1.00 46.89           N  
ATOM    650  N   ASP A  88      11.790 -16.882  61.811  1.00 41.11           N  
ATOM    651  CA  ASP A  88      12.553 -16.731  63.046  1.00 40.92           C  
ATOM    652  C   ASP A  88      13.196 -15.380  63.204  1.00 40.21           C  
ATOM    653  O   ASP A  88      14.415 -15.272  63.306  1.00 39.23           O  
ATOM    654  CB  ASP A  88      13.607 -17.819  63.151  1.00 41.40           C  
ATOM    655  CG  ASP A  88      13.004 -19.179  63.314  1.00 46.41           C  
ATOM    656  OD1 ASP A  88      11.864 -19.247  63.848  1.00 52.06           O  
ATOM    657  OD2 ASP A  88      13.654 -20.185  62.918  1.00 49.83           O  
ATOM    658  N   VAL A  89      12.368 -14.345  63.194  1.00 39.97           N  
ATOM    659  CA  VAL A  89      12.799 -13.086  63.728  1.00 39.98           C  
ATOM    660  C   VAL A  89      12.757 -13.200  65.255  1.00 40.09           C  
ATOM    661  O   VAL A  89      11.706 -13.466  65.858  1.00 39.55           O  
ATOM    662  CB  VAL A  89      12.061 -11.852  63.099  1.00 40.35           C  
ATOM    663  CG1 VAL A  89      10.978 -12.273  62.119  1.00 39.58           C  
ATOM    664  CG2 VAL A  89      11.559 -10.873  64.142  1.00 40.70           C  
ATOM    665  N   SER A  90      13.936 -13.125  65.862  1.00 40.12           N  
ATOM    666  CA  SER A  90      14.026 -13.096  67.308  1.00 40.16           C  
ATOM    667  C   SER A  90      14.218 -11.660  67.761  1.00 40.16           C  
ATOM    668  O   SER A  90      15.163 -10.991  67.347  1.00 40.11           O  
ATOM    669  CB  SER A  90      15.124 -14.021  67.810  1.00 40.42           C  
ATOM    670  OG  SER A  90      16.381 -13.390  67.793  1.00 44.08           O  
ATOM    671  N   VAL A  91      13.269 -11.179  68.560  1.00 40.26           N  
ATOM    672  CA  VAL A  91      13.310  -9.821  69.107  1.00 40.66           C  
ATOM    673  C   VAL A  91      13.458  -9.898  70.627  1.00 40.61           C  
ATOM    674  O   VAL A  91      12.733 -10.630  71.303  1.00 41.26           O  
ATOM    675  CB  VAL A  91      12.014  -9.025  68.822  1.00 40.67           C  
ATOM    676  CG1 VAL A  91      12.301  -7.515  68.842  1.00 40.85           C  
ATOM    677  CG2 VAL A  91      11.411  -9.429  67.506  1.00 41.11           C  
ATOM    678  N   VAL A  92      14.404  -9.143  71.168  1.00 39.85           N  
ATOM    679  CA  VAL A  92      14.484  -8.989  72.601  1.00 39.04           C  
ATOM    680  C   VAL A  92      14.048  -7.530  72.827  1.00 38.77           C  
ATOM    681  O   VAL A  92      14.619  -6.611  72.228  1.00 38.13           O  
ATOM    682  CB  VAL A  92      15.904  -9.269  73.133  1.00 38.75           C  
ATOM    683  CG1 VAL A  92      15.910  -9.382  74.635  1.00 38.37           C  
ATOM    684  CG2 VAL A  92      16.499 -10.533  72.516  1.00 40.27           C  
ATOM    685  N   PHE A  93      12.984  -7.352  73.621  1.00 38.10           N  
ATOM    686  CA  PHE A  93      12.550  -6.051  74.125  1.00 37.91           C  
ATOM    687  C   PHE A  93      13.049  -5.858  75.552  1.00 37.98           C  
ATOM    688  O   PHE A  93      13.145  -6.807  76.315  1.00 37.79           O  
ATOM    689  CB  PHE A  93      11.028  -5.950  74.181  1.00 37.95           C  
ATOM    690  CG  PHE A  93      10.351  -6.090  72.860  1.00 38.42           C  
ATOM    691  CD1 PHE A  93       9.952  -7.344  72.397  1.00 39.81           C  
ATOM    692  CD2 PHE A  93      10.084  -4.962  72.084  1.00 39.56           C  
ATOM    693  CE1 PHE A  93       9.325  -7.477  71.162  1.00 40.13           C  
ATOM    694  CE2 PHE A  93       9.442  -5.079  70.853  1.00 39.63           C  
ATOM    695  CZ  PHE A  93       9.061  -6.341  70.395  1.00 38.53           C  
ATOM    696  N   LYS A  94      13.318  -4.615  75.911  1.00 37.97           N  
ATOM    697  CA  LYS A  94      13.580  -4.230  77.285  1.00 38.34           C  
ATOM    698  C   LYS A  94      12.511  -3.244  77.734  1.00 37.74           C  
ATOM    699  O   LYS A  94      11.945  -2.529  76.914  1.00 37.76           O  
ATOM    700  CB  LYS A  94      14.961  -3.587  77.384  1.00 38.57           C  
ATOM    701  CG  LYS A  94      15.054  -2.285  76.629  1.00 42.08           C  
ATOM    702  CD  LYS A  94      16.501  -1.834  76.424  1.00 46.96           C  
ATOM    703  CE  LYS A  94      16.540  -0.411  75.876  1.00 47.00           C  
ATOM    704  NZ  LYS A  94      17.939   0.141  75.814  1.00 50.71           N  
ATOM    705  N   GLY A  95      12.249  -3.194  79.039  1.00 36.96           N  
ATOM    706  CA  GLY A  95      11.328  -2.205  79.625  1.00 36.82           C  
ATOM    707  C   GLY A  95      11.452  -2.145  81.148  1.00 36.51           C  
ATOM    708  O   GLY A  95      12.340  -2.771  81.721  1.00 36.44           O  
ATOM    709  N   THR A  96      10.576  -1.383  81.791  1.00 36.73           N  
ATOM    710  CA  THR A  96      10.555  -1.260  83.259  1.00 36.89           C  
ATOM    711  C   THR A  96       9.171  -1.564  83.802  1.00 36.59           C  
ATOM    712  O   THR A  96       8.200  -0.887  83.444  1.00 36.12           O  
ATOM    713  CB  THR A  96      10.998   0.151  83.746  1.00 37.78           C  
ATOM    714  OG1 THR A  96      12.339   0.401  83.314  1.00 38.71           O  
ATOM    715  CG2 THR A  96      10.959   0.260  85.318  1.00 37.44           C  
ATOM    716  N   LEU A  97       9.093  -2.605  84.635  1.00 36.42           N  
ATOM    717  CA  LEU A  97       7.871  -2.944  85.385  1.00 36.80           C  
ATOM    718  C   LEU A  97       7.766  -2.144  86.694  1.00 37.29           C  
ATOM    719  O   LEU A  97       8.682  -2.190  87.530  1.00 38.22           O  
ATOM    720  CB  LEU A  97       7.839  -4.444  85.704  1.00 36.36           C  
ATOM    721  CG  LEU A  97       6.650  -4.886  86.571  1.00 36.07           C  
ATOM    722  CD1 LEU A  97       5.360  -4.706  85.829  1.00 33.26           C  
ATOM    723  CD2 LEU A  97       6.812  -6.347  87.038  1.00 35.61           C  
ATOM    724  N   LYS A  98       6.652  -1.427  86.863  1.00 37.42           N  
ATOM    725  CA  LYS A  98       6.352  -0.665  88.068  1.00 36.79           C  
ATOM    726  C   LYS A  98       5.005  -1.105  88.616  1.00 36.62           C  
ATOM    727  O   LYS A  98       4.014  -1.149  87.885  1.00 36.52           O  
ATOM    728  CB  LYS A  98       6.316   0.839  87.779  1.00 37.36           C  
ATOM    729  CG  LYS A  98       7.618   1.379  87.242  1.00 39.63           C  
ATOM    730  CD  LYS A  98       7.697   2.888  87.282  1.00 42.39           C  
ATOM    731  CE  LYS A  98       9.004   3.301  86.642  1.00 44.57           C  
ATOM    732  NZ  LYS A  98       9.274   4.778  86.676  1.00 47.58           N  
ATOM    733  N   TYR A  99       4.968  -1.433  89.911  1.00 35.56           N  
ATOM    734  CA  TYR A  99       3.732  -1.827  90.569  1.00 34.09           C  
ATOM    735  C   TYR A  99       3.699  -1.473  92.047  1.00 34.03           C  
ATOM    736  O   TYR A  99       4.710  -1.117  92.641  1.00 33.49           O  
ATOM    737  CB  TYR A  99       3.494  -3.328  90.405  1.00 33.56           C  
ATOM    738  CG  TYR A  99       4.535  -4.199  91.030  1.00 32.88           C  
ATOM    739  CD1 TYR A  99       4.461  -4.547  92.387  1.00 33.23           C  
ATOM    740  CD2 TYR A  99       5.592  -4.691  90.277  1.00 33.10           C  
ATOM    741  CE1 TYR A  99       5.435  -5.368  92.979  1.00 30.79           C  
ATOM    742  CE2 TYR A  99       6.568  -5.507  90.849  1.00 34.64           C  
ATOM    743  CZ  TYR A  99       6.475  -5.844  92.212  1.00 32.79           C  
ATOM    744  OH  TYR A  99       7.432  -6.658  92.775  1.00 30.91           O  
ATOM    745  N   GLY A 100       2.533  -1.614  92.648  1.00 33.73           N  
ATOM    746  CA  GLY A 100       2.420  -1.411  94.083  1.00 34.73           C  
ATOM    747  C   GLY A 100       1.214  -2.161  94.535  1.00 34.78           C  
ATOM    748  O   GLY A 100       0.247  -2.270  93.783  1.00 35.29           O  
ATOM    749  N   TYR A 101       1.287  -2.694  95.754  1.00 35.00           N  
ATOM    750  CA  TYR A 101       0.176  -3.394  96.379  1.00 33.95           C  
ATOM    751  C   TYR A 101      -0.747  -2.349  96.951  1.00 35.11           C  
ATOM    752  O   TYR A 101      -0.469  -1.746  98.009  1.00 35.49           O  
ATOM    753  CB  TYR A 101       0.705  -4.318  97.448  1.00 33.16           C  
ATOM    754  CG  TYR A 101       1.654  -5.346  96.864  1.00 30.33           C  
ATOM    755  CD1 TYR A 101       3.018  -5.141  96.907  1.00 27.33           C  
ATOM    756  CD2 TYR A 101       1.179  -6.497  96.241  1.00 26.39           C  
ATOM    757  CE1 TYR A 101       3.899  -6.051  96.375  1.00 26.77           C  
ATOM    758  CE2 TYR A 101       2.084  -7.461  95.706  1.00 27.54           C  
ATOM    759  CZ  TYR A 101       3.436  -7.202  95.771  1.00 28.41           C  
ATOM    760  OH  TYR A 101       4.375  -8.081  95.269  1.00 31.45           O  
ATOM    761  N   THR A 102      -1.841  -2.132  96.226  1.00 35.79           N  
ATOM    762  CA  THR A 102      -2.746  -1.023  96.474  1.00 36.32           C  
ATOM    763  C   THR A 102      -3.529  -1.240  97.746  1.00 37.31           C  
ATOM    764  O   THR A 102      -3.501  -0.386  98.643  1.00 37.79           O  
ATOM    765  CB  THR A 102      -3.678  -0.749  95.265  1.00 36.05           C  
ATOM    766  OG1 THR A 102      -2.879  -0.319  94.144  1.00 36.09           O  
ATOM    767  CG2 THR A 102      -4.685   0.353  95.590  1.00 35.06           C  
ATOM    768  N   THR A 103      -4.236  -2.366  97.835  1.00 37.64           N  
ATOM    769  CA  THR A 103      -5.024  -2.601  99.017  1.00 38.65           C  
ATOM    770  C   THR A 103      -4.131  -3.102 100.175  1.00 38.94           C  
ATOM    771  O   THR A 103      -4.312  -2.654 101.320  1.00 39.17           O  
ATOM    772  CB  THR A 103      -6.262  -3.499  98.751  1.00 39.07           C  
ATOM    773  OG1 THR A 103      -5.882  -4.611  97.942  1.00 40.58           O  
ATOM    774  CG2 THR A 103      -7.394  -2.706  98.016  1.00 39.03           C  
ATOM    775  N   ALA A 104      -3.158  -3.973  99.873  1.00 38.20           N  
ATOM    776  CA  ALA A 104      -2.231  -4.527 100.890  1.00 38.05           C  
ATOM    777  C   ALA A 104      -1.099  -3.564 101.297  1.00 38.62           C  
ATOM    778  O   ALA A 104       0.087  -3.818 101.008  1.00 38.01           O  
ATOM    779  CB  ALA A 104      -1.656  -5.839 100.409  1.00 37.08           C  
ATOM    780  N   TRP A 105      -1.459  -2.464 101.959  1.00 39.26           N  
ATOM    781  CA  TRP A 105      -0.475  -1.448 102.359  1.00 40.29           C  
ATOM    782  C   TRP A 105       0.621  -2.002 103.272  1.00 39.81           C  
ATOM    783  O   TRP A 105       1.721  -1.442 103.363  1.00 39.74           O  
ATOM    784  CB  TRP A 105      -1.154  -0.232 103.004  1.00 41.65           C  
ATOM    785  CG  TRP A 105      -1.999  -0.559 104.193  1.00 44.00           C  
ATOM    786  CD1 TRP A 105      -3.349  -0.765 104.203  1.00 45.59           C  
ATOM    787  CD2 TRP A 105      -1.558  -0.719 105.555  1.00 45.54           C  
ATOM    788  NE1 TRP A 105      -3.778  -1.052 105.482  1.00 45.79           N  
ATOM    789  CE2 TRP A 105      -2.700  -1.030 106.330  1.00 46.45           C  
ATOM    790  CE3 TRP A 105      -0.306  -0.640 106.194  1.00 46.07           C  
ATOM    791  CZ2 TRP A 105      -2.633  -1.254 107.720  1.00 46.10           C  
ATOM    792  CZ3 TRP A 105      -0.240  -0.868 107.575  1.00 45.44           C  
ATOM    793  CH2 TRP A 105      -1.399  -1.176 108.320  1.00 45.13           C  
ATOM    794  N   TRP A 106       0.329  -3.128 103.917  1.00 38.95           N  
ATOM    795  CA  TRP A 106       1.255  -3.723 104.880  1.00 37.35           C  
ATOM    796  C   TRP A 106       2.330  -4.545 104.200  1.00 37.22           C  
ATOM    797  O   TRP A 106       3.215  -5.085 104.868  1.00 37.38           O  
ATOM    798  CB  TRP A 106       0.502  -4.599 105.868  1.00 36.73           C  
ATOM    799  CG  TRP A 106      -0.293  -5.687 105.234  1.00 34.94           C  
ATOM    800  CD1 TRP A 106       0.121  -6.973 104.981  1.00 35.51           C  
ATOM    801  CD2 TRP A 106      -1.653  -5.606 104.789  1.00 34.36           C  
ATOM    802  NE1 TRP A 106      -0.912  -7.698 104.403  1.00 34.62           N  
ATOM    803  CE2 TRP A 106      -2.006  -6.878 104.276  1.00 33.16           C  
ATOM    804  CE3 TRP A 106      -2.616  -4.582 104.782  1.00 33.52           C  
ATOM    805  CZ2 TRP A 106      -3.274  -7.147 103.752  1.00 35.07           C  
ATOM    806  CZ3 TRP A 106      -3.882  -4.853 104.268  1.00 34.31           C  
ATOM    807  CH2 TRP A 106      -4.202  -6.132 103.765  1.00 35.05           C  
ATOM    808  N   LEU A 107       2.255  -4.665 102.875  1.00 35.94           N  
ATOM    809  CA  LEU A 107       3.299  -5.384 102.129  1.00 34.04           C  
ATOM    810  C   LEU A 107       4.449  -4.458 101.663  1.00 33.64           C  
ATOM    811  O   LEU A 107       5.438  -4.919 101.094  1.00 33.99           O  
ATOM    812  CB  LEU A 107       2.689  -6.172 100.968  1.00 33.41           C  
ATOM    813  CG  LEU A 107       1.849  -7.396 101.392  1.00 33.44           C  
ATOM    814  CD1 LEU A 107       1.437  -8.219 100.205  1.00 27.39           C  
ATOM    815  CD2 LEU A 107       2.602  -8.287 102.390  1.00 33.22           C  
ATOM    816  N   GLY A 108       4.343  -3.164 101.913  1.00 33.05           N  
ATOM    817  CA  GLY A 108       5.455  -2.269 101.595  1.00 33.10           C  
ATOM    818  C   GLY A 108       5.319  -1.359 100.385  1.00 34.07           C  
ATOM    819  O   GLY A 108       4.251  -1.291  99.739  1.00 33.77           O  
ATOM    820  N   ILE A 109       6.410  -0.648 100.087  1.00 33.77           N  
ATOM    821  CA  ILE A 109       6.422   0.388  99.076  1.00 34.85           C  
ATOM    822  C   ILE A 109       6.356  -0.155  97.642  1.00 35.60           C  
ATOM    823  O   ILE A 109       6.641  -1.328  97.379  1.00 34.53           O  
ATOM    824  CB  ILE A 109       7.686   1.321  99.200  1.00 34.85           C  
ATOM    825  CG1 ILE A 109       8.991   0.524  99.028  1.00 34.68           C  
ATOM    826  CG2 ILE A 109       7.686   2.035 100.535  1.00 35.31           C  
ATOM    827  CD1 ILE A 109      10.212   1.420  98.816  1.00 34.45           C  
ATOM    828  N   ASP A 110       5.987   0.745  96.724  1.00 36.91           N  
ATOM    829  CA  ASP A 110       5.914   0.436  95.289  1.00 36.92           C  
ATOM    830  C   ASP A 110       7.239  -0.038  94.744  1.00 36.67           C  
ATOM    831  O   ASP A 110       8.296   0.321  95.267  1.00 37.17           O  
ATOM    832  CB  ASP A 110       5.449   1.664  94.521  1.00 37.06           C  
ATOM    833  CG  ASP A 110       3.996   1.999  94.792  1.00 38.39           C  
ATOM    834  OD1 ASP A 110       3.410   1.466  95.764  1.00 41.13           O  
ATOM    835  OD2 ASP A 110       3.431   2.797  94.022  1.00 41.27           O  
ATOM    836  N   GLN A 111       7.179  -0.828  93.673  1.00 36.47           N  
ATOM    837  CA  GLN A 111       8.376  -1.457  93.119  1.00 36.99           C  
ATOM    838  C   GLN A 111       8.638  -1.059  91.680  1.00 37.64           C  
ATOM    839  O   GLN A 111       7.732  -0.586  90.970  1.00 36.57           O  
ATOM    840  CB  GLN A 111       8.292  -2.975  93.223  1.00 36.15           C  
ATOM    841  CG  GLN A 111       8.127  -3.486  94.632  1.00 37.22           C  
ATOM    842  CD  GLN A 111       9.348  -3.232  95.498  1.00 38.09           C  
ATOM    843  OE1 GLN A 111      10.424  -3.798  95.277  1.00 36.49           O  
ATOM    844  NE2 GLN A 111       9.176  -2.399  96.513  1.00 38.68           N  
ATOM    845  N   SER A 112       9.900  -1.247  91.283  1.00 38.67           N  
ATOM    846  CA  SER A 112      10.405  -0.934  89.938  1.00 39.79           C  
ATOM    847  C   SER A 112      11.386  -2.031  89.554  1.00 40.35           C  
ATOM    848  O   SER A 112      12.432  -2.150  90.183  1.00 40.75           O  
ATOM    849  CB  SER A 112      11.137   0.403  89.965  1.00 40.27           C  
ATOM    850  OG  SER A 112      11.307   0.926  88.668  1.00 42.99           O  
ATOM    851  N   ILE A 113      11.041  -2.853  88.560  1.00 40.12           N  
ATOM    852  CA  ILE A 113      11.933  -3.928  88.109  1.00 40.37           C  
ATOM    853  C   ILE A 113      12.179  -3.848  86.589  1.00 40.55           C  
ATOM    854  O   ILE A 113      11.227  -3.832  85.808  1.00 40.36           O  
ATOM    855  CB  ILE A 113      11.368  -5.351  88.456  1.00 40.08           C  
ATOM    856  CG1 ILE A 113      10.778  -5.407  89.887  1.00 40.34           C  
ATOM    857  CG2 ILE A 113      12.424  -6.403  88.254  1.00 39.29           C  
ATOM    858  CD1 ILE A 113      10.204  -6.818  90.275  1.00 39.93           C  
ATOM    859  N   ASP A 114      13.446  -3.796  86.177  1.00 40.62           N  
ATOM    860  CA  ASP A 114      13.765  -3.873  84.751  1.00 40.94           C  
ATOM    861  C   ASP A 114      13.465  -5.286  84.250  1.00 41.43           C  
ATOM    862  O   ASP A 114      13.582  -6.274  84.999  1.00 41.72           O  
ATOM    863  CB  ASP A 114      15.220  -3.488  84.472  1.00 40.48           C  
ATOM    864  CG  ASP A 114      15.473  -1.992  84.585  1.00 41.52           C  
ATOM    865  OD1 ASP A 114      14.516  -1.182  84.548  1.00 43.59           O  
ATOM    866  OD2 ASP A 114      16.656  -1.609  84.702  1.00 43.12           O  
ATOM    867  N   PHE A 115      13.027  -5.368  83.006  1.00 41.37           N  
ATOM    868  CA  PHE A 115      12.682  -6.638  82.403  1.00 42.48           C  
ATOM    869  C   PHE A 115      13.143  -6.690  80.956  1.00 42.53           C  
ATOM    870  O   PHE A 115      13.545  -5.678  80.370  1.00 42.78           O  
ATOM    871  CB  PHE A 115      11.169  -6.923  82.500  1.00 42.50           C  
ATOM    872  CG  PHE A 115      10.304  -6.005  81.671  1.00 43.47           C  
ATOM    873  CD1 PHE A 115      10.151  -6.211  80.294  1.00 44.88           C  
ATOM    874  CD2 PHE A 115       9.610  -4.958  82.266  1.00 43.35           C  
ATOM    875  CE1 PHE A 115       9.354  -5.376  79.528  1.00 43.32           C  
ATOM    876  CE2 PHE A 115       8.801  -4.115  81.513  1.00 43.28           C  
ATOM    877  CZ  PHE A 115       8.664  -4.323  80.141  1.00 43.47           C  
ATOM    878  N   GLU A 116      13.110  -7.892  80.415  1.00 42.27           N  
ATOM    879  CA  GLU A 116      13.178  -8.117  78.986  1.00 41.94           C  
ATOM    880  C   GLU A 116      12.025  -9.020  78.593  1.00 41.71           C  
ATOM    881  O   GLU A 116      11.610  -9.876  79.386  1.00 40.21           O  
ATOM    882  CB  GLU A 116      14.490  -8.786  78.610  1.00 41.81           C  
ATOM    883  CG  GLU A 116      15.680  -7.865  78.734  1.00 43.16           C  
ATOM    884  CD  GLU A 116      16.952  -8.511  78.252  1.00 46.27           C  
ATOM    885  OE1 GLU A 116      17.955  -7.776  78.068  1.00 46.14           O  
ATOM    886  OE2 GLU A 116      16.940  -9.753  78.056  1.00 45.57           O  
ATOM    887  N   ILE A 117      11.506  -8.796  77.377  1.00 41.71           N  
ATOM    888  CA  ILE A 117      10.619  -9.754  76.688  1.00 41.14           C  
ATOM    889  C   ILE A 117      11.337 -10.370  75.468  1.00 42.03           C  
ATOM    890  O   ILE A 117      11.858  -9.661  74.597  1.00 42.05           O  
ATOM    891  CB  ILE A 117       9.244  -9.129  76.318  1.00 40.91           C  
ATOM    892  CG1 ILE A 117       8.488  -8.690  77.579  1.00 38.63           C  
ATOM    893  CG2 ILE A 117       8.390 -10.117  75.552  1.00 39.48           C  
ATOM    894  CD1 ILE A 117       7.401  -7.657  77.314  1.00 38.53           C  
ATOM    895  N   ASP A 118      11.397 -11.694  75.458  1.00 42.51           N  
ATOM    896  CA  ASP A 118      12.041 -12.493  74.426  1.00 43.16           C  
ATOM    897  C   ASP A 118      10.994 -13.119  73.531  1.00 42.54           C  
ATOM    898  O   ASP A 118      10.175 -13.875  74.032  1.00 42.10           O  
ATOM    899  CB  ASP A 118      12.736 -13.671  75.092  1.00 44.25           C  
ATOM    900  CG  ASP A 118      14.222 -13.615  74.967  1.00 48.26           C  
ATOM    901  OD1 ASP A 118      14.735 -14.334  74.077  1.00 52.23           O  
ATOM    902  OD2 ASP A 118      14.871 -12.862  75.754  1.00 53.98           O  
ATOM    903  N   SER A 119      11.004 -12.817  72.231  1.00 41.77           N  
ATOM    904  CA  SER A 119      10.119 -13.532  71.294  1.00 41.79           C  
ATOM    905  C   SER A 119      10.802 -14.048  70.028  1.00 40.84           C  
ATOM    906  O   SER A 119      11.866 -13.555  69.634  1.00 40.55           O  
ATOM    907  CB  SER A 119       8.830 -12.759  70.947  1.00 41.72           C  
ATOM    908  OG  SER A 119       9.101 -11.435  70.527  1.00 45.51           O  
ATOM    909  N   ALA A 120      10.180 -15.070  69.433  1.00 39.87           N  
ATOM    910  CA  ALA A 120      10.555 -15.596  68.136  1.00 38.38           C  
ATOM    911  C   ALA A 120       9.285 -15.643  67.303  1.00 38.29           C  
ATOM    912  O   ALA A 120       8.230 -16.134  67.768  1.00 38.21           O  
ATOM    913  CB  ALA A 120      11.158 -16.957  68.271  1.00 38.25           C  
ATOM    914  N   ILE A 121       9.376 -15.093  66.090  1.00 36.83           N  
ATOM    915  CA  ILE A 121       8.199 -14.893  65.236  1.00 36.32           C  
ATOM    916  C   ILE A 121       8.498 -15.341  63.793  1.00 35.38           C  
ATOM    917  O   ILE A 121       9.582 -15.089  63.278  1.00 35.36           O  
ATOM    918  CB  ILE A 121       7.739 -13.391  65.240  1.00 36.27           C  
ATOM    919  CG1 ILE A 121       7.767 -12.803  66.652  1.00 36.31           C  
ATOM    920  CG2 ILE A 121       6.321 -13.229  64.677  1.00 37.14           C  
ATOM    921  CD1 ILE A 121       7.449 -11.309  66.707  1.00 36.22           C  
ATOM    922  N   ASP A 122       7.558 -16.046  63.173  1.00 34.76           N  
ATOM    923  CA  ASP A 122       7.558 -16.239  61.715  1.00 34.03           C  
ATOM    924  C   ASP A 122       6.506 -15.290  61.130  1.00 34.46           C  
ATOM    925  O   ASP A 122       5.405 -15.200  61.671  1.00 33.44           O  
ATOM    926  CB  ASP A 122       7.191 -17.667  61.366  1.00 33.85           C  
ATOM    927  CG  ASP A 122       8.234 -18.678  61.829  1.00 34.62           C  
ATOM    928  OD1 ASP A 122       7.877 -19.875  61.941  1.00 37.88           O  
ATOM    929  OD2 ASP A 122       9.407 -18.300  62.094  1.00 34.51           O  
ATOM    930  N   LEU A 123       6.864 -14.552  60.069  1.00 34.33           N  
ATOM    931  CA  LEU A 123       5.922 -13.676  59.371  1.00 35.02           C  
ATOM    932  C   LEU A 123       5.629 -14.141  57.935  1.00 34.69           C  
ATOM    933  O   LEU A 123       6.476 -14.741  57.265  1.00 35.07           O  
ATOM    934  CB  LEU A 123       6.442 -12.236  59.318  1.00 34.73           C  
ATOM    935  CG  LEU A 123       6.639 -11.353  60.544  1.00 35.63           C  
ATOM    936  CD1 LEU A 123       7.984 -11.583  61.129  1.00 34.90           C  
ATOM    937  CD2 LEU A 123       6.546  -9.894  60.119  1.00 36.36           C  
ATOM    938  N   GLN A 124       4.427 -13.839  57.471  1.00 34.65           N  
ATOM    939  CA  GLN A 124       4.032 -14.078  56.092  1.00 34.42           C  
ATOM    940  C   GLN A 124       3.364 -12.786  55.639  1.00 34.29           C  
ATOM    941  O   GLN A 124       2.328 -12.400  56.176  1.00 34.21           O  
ATOM    942  CB  GLN A 124       3.072 -15.264  56.021  1.00 34.72           C  
ATOM    943  CG  GLN A 124       2.467 -15.550  54.658  1.00 35.79           C  
ATOM    944  CD  GLN A 124       3.472 -16.082  53.685  1.00 37.33           C  
ATOM    945  OE1 GLN A 124       4.363 -16.839  54.057  1.00 40.78           O  
ATOM    946  NE2 GLN A 124       3.344 -15.694  52.427  1.00 36.15           N  
ATOM    947  N   ILE A 125       4.002 -12.093  54.699  1.00 33.65           N  
ATOM    948  CA  ILE A 125       3.480 -10.833  54.174  1.00 33.47           C  
ATOM    949  C   ILE A 125       3.123 -10.978  52.696  1.00 33.16           C  
ATOM    950  O   ILE A 125       4.008 -11.108  51.862  1.00 33.55           O  
ATOM    951  CB  ILE A 125       4.507  -9.674  54.361  1.00 33.41           C  
ATOM    952  CG1 ILE A 125       4.954  -9.601  55.830  1.00 32.54           C  
ATOM    953  CG2 ILE A 125       3.901  -8.347  53.928  1.00 31.43           C  
ATOM    954  CD1 ILE A 125       6.401  -9.389  55.995  1.00 32.49           C  
ATOM    955  N   ASN A 126       1.834 -10.946  52.386  1.00 33.15           N  
ATOM    956  CA  ASN A 126       1.340 -11.049  51.001  1.00 32.96           C  
ATOM    957  C   ASN A 126       0.927  -9.678  50.460  1.00 34.00           C  
ATOM    958  O   ASN A 126      -0.140  -9.148  50.812  1.00 33.71           O  
ATOM    959  CB  ASN A 126       0.162 -12.009  50.953  1.00 33.18           C  
ATOM    960  CG  ASN A 126       0.536 -13.395  51.403  1.00 32.49           C  
ATOM    961  OD1 ASN A 126      -0.331 -14.235  51.638  1.00 34.19           O  
ATOM    962  ND2 ASN A 126       1.831 -13.647  51.523  1.00 29.76           N  
ATOM    963  N   THR A 127       1.812  -9.079  49.661  1.00 34.60           N  
ATOM    964  CA  THR A 127       1.642  -7.707  49.208  1.00 35.00           C  
ATOM    965  C   THR A 127       0.930  -7.683  47.851  1.00 35.85           C  
ATOM    966  O   THR A 127       1.369  -8.342  46.897  1.00 36.73           O  
ATOM    967  CB  THR A 127       3.005  -6.964  49.128  1.00 34.83           C  
ATOM    968  OG1 THR A 127       3.606  -6.893  50.437  1.00 34.81           O  
ATOM    969  CG2 THR A 127       2.805  -5.558  48.589  1.00 34.52           C  
ATOM    970  N   GLN A 128      -0.173  -6.946  47.784  1.00 35.95           N  
ATOM    971  CA  GLN A 128      -0.894  -6.695  46.545  1.00 37.33           C  
ATOM    972  C   GLN A 128      -0.515  -5.325  45.956  1.00 37.83           C  
ATOM    973  O   GLN A 128      -0.307  -4.353  46.678  1.00 37.52           O  
ATOM    974  CB  GLN A 128      -2.412  -6.740  46.780  1.00 37.00           C  
ATOM    975  CG  GLN A 128      -2.911  -7.953  47.547  1.00 37.40           C  
ATOM    976  CD  GLN A 128      -4.391  -7.867  47.888  1.00 38.57           C  
ATOM    977  OE1 GLN A 128      -5.222  -7.563  47.042  1.00 42.99           O  
ATOM    978  NE2 GLN A 128      -4.726  -8.148  49.125  1.00 39.58           N  
ATOM    979  N   LEU A 129      -0.451  -5.260  44.628  1.00 38.69           N  
ATOM    980  CA  LEU A 129      -0.059  -4.041  43.911  1.00 39.05           C  
ATOM    981  C   LEU A 129      -1.243  -3.537  43.105  1.00 39.00           C  
ATOM    982  O   LEU A 129      -1.861  -4.295  42.343  1.00 38.92           O  
ATOM    983  CB  LEU A 129       1.104  -4.353  42.966  1.00 39.32           C  
ATOM    984  CG  LEU A 129       2.561  -4.429  43.407  1.00 39.97           C  
ATOM    985  CD1 LEU A 129       2.795  -4.978  44.780  1.00 40.11           C  
ATOM    986  CD2 LEU A 129       3.343  -5.208  42.367  1.00 39.02           C  
ATOM    987  N   THR A 130      -1.558  -2.260  43.277  1.00 38.73           N  
ATOM    988  CA  THR A 130      -2.675  -1.658  42.604  1.00 39.02           C  
ATOM    989  C   THR A 130      -2.316  -0.238  42.177  1.00 39.73           C  
ATOM    990  O   THR A 130      -1.385   0.376  42.719  1.00 39.67           O  
ATOM    991  CB  THR A 130      -3.951  -1.621  43.498  1.00 39.16           C  
ATOM    992  OG1 THR A 130      -3.689  -0.867  44.683  1.00 37.95           O  
ATOM    993  CG2 THR A 130      -4.423  -3.042  43.890  1.00 38.41           C  
ATOM    994  N   ALA A 131      -3.070   0.270  41.205  1.00 39.85           N  
ATOM    995  CA  ALA A 131      -2.932   1.625  40.721  1.00 40.19           C  
ATOM    996  C   ALA A 131      -3.708   2.555  41.630  1.00 40.91           C  
ATOM    997  O   ALA A 131      -4.870   2.291  41.965  1.00 40.50           O  
ATOM    998  CB  ALA A 131      -3.476   1.717  39.302  1.00 40.09           C  
ATOM    999  N   ASP A 132      -3.068   3.645  42.039  1.00 41.57           N  
ATOM   1000  CA  ASP A 132      -3.753   4.668  42.806  1.00 42.76           C  
ATOM   1001  C   ASP A 132      -3.148   6.015  42.463  1.00 42.90           C  
ATOM   1002  O   ASP A 132      -1.955   6.238  42.676  1.00 42.74           O  
ATOM   1003  CB  ASP A 132      -3.651   4.386  44.315  1.00 42.98           C  
ATOM   1004  CG  ASP A 132      -4.278   5.492  45.185  1.00 45.69           C  
ATOM   1005  OD1 ASP A 132      -3.725   5.775  46.266  1.00 49.29           O  
ATOM   1006  OD2 ASP A 132      -5.322   6.079  44.815  1.00 48.42           O  
ATOM   1007  N   SER A 133      -3.973   6.912  41.936  1.00 43.58           N  
ATOM   1008  CA  SER A 133      -3.483   8.215  41.520  1.00 44.49           C  
ATOM   1009  C   SER A 133      -2.411   8.093  40.415  1.00 43.87           C  
ATOM   1010  O   SER A 133      -1.472   8.889  40.377  1.00 44.00           O  
ATOM   1011  CB  SER A 133      -2.891   8.958  42.735  1.00 44.96           C  
ATOM   1012  OG  SER A 133      -3.890   9.298  43.690  1.00 48.62           O  
ATOM   1013  N   GLY A 134      -2.533   7.087  39.539  1.00 43.18           N  
ATOM   1014  CA  GLY A 134      -1.506   6.839  38.504  1.00 41.57           C  
ATOM   1015  C   GLY A 134      -0.194   6.289  39.032  1.00 40.61           C  
ATOM   1016  O   GLY A 134       0.782   6.178  38.307  1.00 40.10           O  
ATOM   1017  N   ARG A 135      -0.201   5.892  40.297  1.00 40.13           N  
ATOM   1018  CA  ARG A 135       0.978   5.463  41.006  1.00 40.39           C  
ATOM   1019  C   ARG A 135       0.738   4.041  41.428  1.00 40.16           C  
ATOM   1020  O   ARG A 135      -0.398   3.685  41.703  1.00 40.01           O  
ATOM   1021  CB  ARG A 135       1.129   6.309  42.258  1.00 40.99           C  
ATOM   1022  CG  ARG A 135       1.607   7.715  41.988  1.00 43.83           C  
ATOM   1023  CD  ARG A 135       3.081   7.800  42.279  1.00 48.42           C  
ATOM   1024  NE  ARG A 135       3.830   8.477  41.224  1.00 51.52           N  
ATOM   1025  CZ  ARG A 135       5.062   8.929  41.396  1.00 53.08           C  
ATOM   1026  NH1 ARG A 135       5.645   8.767  42.585  1.00 52.66           N  
ATOM   1027  NH2 ARG A 135       5.706   9.531  40.390  1.00 53.87           N  
ATOM   1028  N   VAL A 136       1.782   3.221  41.486  1.00 39.85           N  
ATOM   1029  CA  VAL A 136       1.590   1.912  42.096  1.00 40.40           C  
ATOM   1030  C   VAL A 136       1.650   1.976  43.641  1.00 40.58           C  
ATOM   1031  O   VAL A 136       2.613   2.488  44.225  1.00 40.11           O  
ATOM   1032  CB  VAL A 136       2.369   0.689  41.423  1.00 40.41           C  
ATOM   1033  CG1 VAL A 136       3.219   1.084  40.205  1.00 41.51           C  
ATOM   1034  CG2 VAL A 136       3.149  -0.147  42.428  1.00 40.00           C  
ATOM   1035  N   ARG A 137       0.559   1.510  44.250  1.00 39.65           N  
ATOM   1036  CA  ARG A 137       0.403   1.345  45.690  1.00 39.60           C  
ATOM   1037  C   ARG A 137       0.660  -0.094  46.102  1.00 38.98           C  
ATOM   1038  O   ARG A 137       0.378  -1.022  45.346  1.00 37.81           O  
ATOM   1039  CB  ARG A 137      -1.055   1.535  46.043  1.00 39.93           C  
ATOM   1040  CG  ARG A 137      -1.463   2.856  46.433  1.00 42.40           C  
ATOM   1041  CD  ARG A 137      -2.754   2.684  47.241  1.00 48.22           C  
ATOM   1042  NE  ARG A 137      -2.515   1.862  48.429  1.00 49.92           N  
ATOM   1043  CZ  ARG A 137      -2.023   2.329  49.571  1.00 51.69           C  
ATOM   1044  NH1 ARG A 137      -1.725   3.620  49.701  1.00 50.75           N  
ATOM   1045  NH2 ARG A 137      -1.825   1.500  50.583  1.00 52.37           N  
ATOM   1046  N   THR A 138       1.109  -0.268  47.344  1.00 38.79           N  
ATOM   1047  CA  THR A 138       1.212  -1.592  47.946  1.00 38.75           C  
ATOM   1048  C   THR A 138       0.217  -1.744  49.102  1.00 39.08           C  
ATOM   1049  O   THR A 138      -0.085  -0.783  49.826  1.00 37.62           O  
ATOM   1050  CB  THR A 138       2.639  -1.895  48.400  1.00 39.16           C  
ATOM   1051  OG1 THR A 138       2.959  -1.100  49.547  1.00 40.21           O  
ATOM   1052  CG2 THR A 138       3.647  -1.588  47.268  1.00 38.37           C  
ATOM   1053  N   ASP A 139      -0.318  -2.951  49.254  1.00 39.42           N  
ATOM   1054  CA  ASP A 139      -1.253  -3.227  50.336  1.00 39.81           C  
ATOM   1055  C   ASP A 139      -1.070  -4.672  50.758  1.00 39.45           C  
ATOM   1056  O   ASP A 139      -1.169  -5.590  49.936  1.00 37.70           O  
ATOM   1057  CB  ASP A 139      -2.692  -2.948  49.900  1.00 40.28           C  
ATOM   1058  CG  ASP A 139      -2.991  -1.438  49.765  1.00 43.99           C  
ATOM   1059  OD1 ASP A 139      -3.167  -0.757  50.805  1.00 47.52           O  
ATOM   1060  OD2 ASP A 139      -3.063  -0.919  48.624  1.00 44.90           O  
ATOM   1061  N   ALA A 140      -0.763  -4.864  52.041  1.00 39.59           N  
ATOM   1062  CA  ALA A 140      -0.710  -6.202  52.619  1.00 40.04           C  
ATOM   1063  C   ALA A 140      -1.768  -6.335  53.725  1.00 41.12           C  
ATOM   1064  O   ALA A 140      -1.424  -6.256  54.912  1.00 40.72           O  
ATOM   1065  CB  ALA A 140       0.670  -6.477  53.170  1.00 39.47           C  
ATOM   1066  N   PRO A 141      -3.055  -6.512  53.350  1.00 41.81           N  
ATOM   1067  CA  PRO A 141      -4.039  -6.751  54.409  1.00 43.20           C  
ATOM   1068  C   PRO A 141      -3.869  -8.127  55.053  1.00 44.16           C  
ATOM   1069  O   PRO A 141      -4.310  -8.333  56.175  1.00 44.55           O  
ATOM   1070  CB  PRO A 141      -5.379  -6.683  53.665  1.00 42.99           C  
ATOM   1071  CG  PRO A 141      -5.044  -7.117  52.275  1.00 42.02           C  
ATOM   1072  CD  PRO A 141      -3.690  -6.504  52.018  1.00 41.95           C  
ATOM   1073  N   ASP A 142      -3.228  -9.041  54.326  1.00 45.57           N  
ATOM   1074  CA  ASP A 142      -2.944 -10.402  54.767  1.00 46.07           C  
ATOM   1075  C   ASP A 142      -1.504 -10.468  55.227  1.00 45.96           C  
ATOM   1076  O   ASP A 142      -0.583 -10.794  54.443  1.00 45.25           O  
ATOM   1077  CB  ASP A 142      -3.133 -11.377  53.605  1.00 47.14           C  
ATOM   1078  CG  ASP A 142      -4.565 -11.426  53.109  1.00 49.99           C  
ATOM   1079  OD1 ASP A 142      -5.495 -11.348  53.951  1.00 53.64           O  
ATOM   1080  OD2 ASP A 142      -4.750 -11.552  51.874  1.00 54.02           O  
ATOM   1081  N   CYS A 143      -1.322 -10.163  56.504  1.00 45.11           N  
ATOM   1082  CA  CYS A 143      -0.006 -10.063  57.097  1.00 44.40           C  
ATOM   1083  C   CYS A 143      -0.069 -10.906  58.368  1.00 43.63           C  
ATOM   1084  O   CYS A 143      -0.683 -10.500  59.340  1.00 43.58           O  
ATOM   1085  CB  CYS A 143       0.320  -8.591  57.364  1.00 43.79           C  
ATOM   1086  SG  CYS A 143       1.874  -8.310  58.205  1.00 47.04           S  
ATOM   1087  N   TYR A 144       0.495 -12.113  58.305  1.00 42.79           N  
ATOM   1088  CA  TYR A 144       0.321 -13.140  59.318  1.00 42.42           C  
ATOM   1089  C   TYR A 144       1.527 -13.137  60.251  1.00 41.77           C  
ATOM   1090  O   TYR A 144       2.663 -12.996  59.790  1.00 41.60           O  
ATOM   1091  CB  TYR A 144       0.192 -14.542  58.681  1.00 43.68           C  
ATOM   1092  CG  TYR A 144      -0.817 -14.640  57.539  1.00 45.55           C  
ATOM   1093  CD1 TYR A 144      -0.427 -14.473  56.206  1.00 47.71           C  
ATOM   1094  CD2 TYR A 144      -2.169 -14.897  57.795  1.00 48.81           C  
ATOM   1095  CE1 TYR A 144      -1.357 -14.557  55.159  1.00 47.75           C  
ATOM   1096  CE2 TYR A 144      -3.109 -14.977  56.755  1.00 48.62           C  
ATOM   1097  CZ  TYR A 144      -2.699 -14.812  55.446  1.00 47.85           C  
ATOM   1098  OH  TYR A 144      -3.642 -14.899  54.434  1.00 47.32           O  
ATOM   1099  N   LEU A 145       1.273 -13.279  61.554  1.00 39.91           N  
ATOM   1100  CA  LEU A 145       2.326 -13.488  62.537  1.00 39.52           C  
ATOM   1101  C   LEU A 145       2.104 -14.772  63.316  1.00 38.79           C  
ATOM   1102  O   LEU A 145       0.986 -15.094  63.711  1.00 38.90           O  
ATOM   1103  CB  LEU A 145       2.421 -12.328  63.503  1.00 38.55           C  
ATOM   1104  CG  LEU A 145       3.418 -11.230  63.188  1.00 38.41           C  
ATOM   1105  CD1 LEU A 145       2.918 -10.378  62.040  1.00 38.24           C  
ATOM   1106  CD2 LEU A 145       3.653 -10.370  64.431  1.00 38.01           C  
ATOM   1107  N   SER A 146       3.181 -15.506  63.515  1.00 38.07           N  
ATOM   1108  CA  SER A 146       3.139 -16.741  64.269  1.00 38.00           C  
ATOM   1109  C   SER A 146       4.235 -16.691  65.317  1.00 37.57           C  
ATOM   1110  O   SER A 146       5.411 -16.727  64.967  1.00 37.54           O  
ATOM   1111  CB  SER A 146       3.345 -17.916  63.338  1.00 38.16           C  
ATOM   1112  OG  SER A 146       3.679 -19.099  64.048  1.00 39.32           O  
ATOM   1113  N   PHE A 147       3.844 -16.581  66.594  1.00 36.79           N  
ATOM   1114  CA  PHE A 147       4.801 -16.518  67.716  1.00 35.77           C  
ATOM   1115  C   PHE A 147       5.215 -17.904  68.192  1.00 36.75           C  
ATOM   1116  O   PHE A 147       4.374 -18.759  68.437  1.00 36.44           O  
ATOM   1117  CB  PHE A 147       4.208 -15.724  68.889  1.00 34.29           C  
ATOM   1118  CG  PHE A 147       3.980 -14.268  68.584  1.00 30.72           C  
ATOM   1119  CD1 PHE A 147       2.880 -13.869  67.849  1.00 28.03           C  
ATOM   1120  CD2 PHE A 147       4.887 -13.306  69.016  1.00 28.28           C  
ATOM   1121  CE1 PHE A 147       2.677 -12.508  67.539  1.00 30.37           C  
ATOM   1122  CE2 PHE A 147       4.688 -11.972  68.748  1.00 27.90           C  
ATOM   1123  CZ  PHE A 147       3.589 -11.563  67.992  1.00 28.02           C  
ATOM   1124  N   HIS A 148       6.514 -18.132  68.294  1.00 38.72           N  
ATOM   1125  CA  HIS A 148       7.032 -19.376  68.866  1.00 40.96           C  
ATOM   1126  C   HIS A 148       7.119 -19.207  70.363  1.00 41.36           C  
ATOM   1127  O   HIS A 148       6.912 -20.153  71.108  1.00 41.96           O  
ATOM   1128  CB  HIS A 148       8.440 -19.680  68.367  1.00 41.95           C  
ATOM   1129  CG  HIS A 148       8.513 -19.946  66.903  1.00 45.78           C  
ATOM   1130  ND1 HIS A 148       7.977 -21.079  66.328  1.00 49.24           N  
ATOM   1131  CD2 HIS A 148       9.055 -19.224  65.893  1.00 47.77           C  
ATOM   1132  CE1 HIS A 148       8.190 -21.046  65.023  1.00 51.01           C  
ATOM   1133  NE2 HIS A 148       8.844 -19.932  64.735  1.00 51.57           N  
ATOM   1134  N   LYS A 149       7.453 -17.993  70.795  1.00 41.75           N  
ATOM   1135  CA  LYS A 149       7.529 -17.671  72.214  1.00 42.05           C  
ATOM   1136  C   LYS A 149       7.345 -16.186  72.431  1.00 42.60           C  
ATOM   1137  O   LYS A 149       7.567 -15.370  71.525  1.00 42.94           O  
ATOM   1138  CB  LYS A 149       8.876 -18.123  72.811  1.00 41.94           C  
ATOM   1139  CG  LYS A 149      10.105 -17.411  72.279  1.00 41.70           C  
ATOM   1140  CD  LYS A 149      11.400 -17.951  72.892  1.00 42.61           C  
ATOM   1141  CE  LYS A 149      12.610 -17.388  72.140  1.00 46.50           C  
ATOM   1142  NZ  LYS A 149      13.945 -17.746  72.722  1.00 49.48           N  
ATOM   1143  N   LEU A 150       6.926 -15.858  73.644  1.00 42.33           N  
ATOM   1144  CA  LEU A 150       6.956 -14.510  74.170  1.00 42.21           C  
ATOM   1145  C   LEU A 150       7.075 -14.670  75.687  1.00 42.23           C  
ATOM   1146  O   LEU A 150       6.085 -14.935  76.367  1.00 41.97           O  
ATOM   1147  CB  LEU A 150       5.694 -13.742  73.783  1.00 42.12           C  
ATOM   1148  CG  LEU A 150       5.633 -12.262  74.122  1.00 41.13           C  
ATOM   1149  CD1 LEU A 150       6.543 -11.400  73.255  1.00 40.12           C  
ATOM   1150  CD2 LEU A 150       4.212 -11.789  73.992  1.00 42.19           C  
ATOM   1151  N   LEU A 151       8.305 -14.552  76.180  1.00 42.20           N  
ATOM   1152  CA  LEU A 151       8.657 -14.821  77.589  1.00 42.53           C  
ATOM   1153  C   LEU A 151       9.151 -13.562  78.288  1.00 42.46           C  
ATOM   1154  O   LEU A 151      10.018 -12.873  77.763  1.00 42.66           O  
ATOM   1155  CB  LEU A 151       9.757 -15.867  77.679  1.00 42.15           C  
ATOM   1156  CG  LEU A 151       9.521 -17.221  77.019  1.00 43.13           C  
ATOM   1157  CD1 LEU A 151      10.833 -18.005  76.927  1.00 43.62           C  
ATOM   1158  CD2 LEU A 151       8.460 -17.990  77.771  1.00 42.99           C  
ATOM   1159  N   LEU A 152       8.611 -13.286  79.475  1.00 42.17           N  
ATOM   1160  CA  LEU A 152       9.041 -12.169  80.298  1.00 42.14           C  
ATOM   1161  C   LEU A 152      10.144 -12.637  81.235  1.00 42.40           C  
ATOM   1162  O   LEU A 152      10.047 -13.714  81.809  1.00 43.94           O  
ATOM   1163  CB  LEU A 152       7.848 -11.644  81.080  1.00 41.98           C  
ATOM   1164  CG  LEU A 152       7.971 -10.621  82.204  1.00 42.01           C  
ATOM   1165  CD1 LEU A 152       8.134  -9.183  81.696  1.00 40.43           C  
ATOM   1166  CD2 LEU A 152       6.728 -10.743  83.052  1.00 39.23           C  
ATOM   1167  N   HIS A 153      11.212 -11.856  81.354  1.00 42.28           N  
ATOM   1168  CA  HIS A 153      12.319 -12.180  82.240  1.00 42.55           C  
ATOM   1169  C   HIS A 153      12.617 -10.953  83.066  1.00 42.44           C  
ATOM   1170  O   HIS A 153      13.010  -9.936  82.515  1.00 42.69           O  
ATOM   1171  CB  HIS A 153      13.559 -12.570  81.449  1.00 42.19           C  
ATOM   1172  CG  HIS A 153      13.391 -13.816  80.640  1.00 45.14           C  
ATOM   1173  ND1 HIS A 153      12.622 -14.881  81.065  1.00 46.33           N  
ATOM   1174  CD2 HIS A 153      13.880 -14.165  79.422  1.00 46.23           C  
ATOM   1175  CE1 HIS A 153      12.663 -15.840  80.153  1.00 47.13           C  
ATOM   1176  NE2 HIS A 153      13.418 -15.431  79.147  1.00 46.60           N  
ATOM   1177  N   LEU A 154      12.401 -11.032  84.375  1.00 42.77           N  
ATOM   1178  CA  LEU A 154      12.750  -9.909  85.281  1.00 42.71           C  
ATOM   1179  C   LEU A 154      14.216  -9.903  85.670  1.00 42.28           C  
ATOM   1180  O   LEU A 154      14.829 -10.968  85.810  1.00 41.45           O  
ATOM   1181  CB  LEU A 154      11.892  -9.921  86.547  1.00 42.91           C  
ATOM   1182  CG  LEU A 154      10.387 -10.112  86.382  1.00 42.76           C  
ATOM   1183  CD1 LEU A 154       9.754  -9.972  87.739  1.00 43.16           C  
ATOM   1184  CD2 LEU A 154       9.810  -9.111  85.427  1.00 43.31           C  
ATOM   1185  N   GLN A 155      14.783  -8.704  85.817  1.00 42.86           N  
ATOM   1186  CA  GLN A 155      16.138  -8.568  86.361  1.00 44.30           C  
ATOM   1187  C   GLN A 155      16.142  -9.101  87.791  1.00 43.67           C  
ATOM   1188  O   GLN A 155      15.333  -8.671  88.616  1.00 43.74           O  
ATOM   1189  CB  GLN A 155      16.615  -7.109  86.352  1.00 44.29           C  
ATOM   1190  CG  GLN A 155      17.822  -6.827  85.451  1.00 46.00           C  
ATOM   1191  CD  GLN A 155      18.518  -5.523  85.816  1.00 47.38           C  
ATOM   1192  OE1 GLN A 155      18.503  -5.101  86.985  1.00 51.36           O  
ATOM   1193  NE2 GLN A 155      19.136  -4.876  84.825  1.00 49.18           N  
ATOM   1194  N   GLY A 156      17.018 -10.063  88.056  1.00 43.23           N  
ATOM   1195  CA  GLY A 156      17.104 -10.690  89.364  1.00 42.93           C  
ATOM   1196  C   GLY A 156      16.115 -11.814  89.632  1.00 43.34           C  
ATOM   1197  O   GLY A 156      16.050 -12.311  90.756  1.00 44.28           O  
ATOM   1198  N   GLU A 157      15.343 -12.211  88.620  1.00 42.37           N  
ATOM   1199  CA  GLU A 157      14.380 -13.316  88.714  1.00 42.11           C  
ATOM   1200  C   GLU A 157      13.445 -13.282  89.958  1.00 40.28           C  
ATOM   1201  O   GLU A 157      13.151 -14.316  90.575  1.00 40.41           O  
ATOM   1202  CB  GLU A 157      15.090 -14.678  88.520  1.00 42.07           C  
ATOM   1203  CG  GLU A 157      15.987 -14.701  87.249  1.00 44.91           C  
ATOM   1204  CD  GLU A 157      16.488 -16.091  86.829  1.00 45.54           C  
ATOM   1205  OE1 GLU A 157      16.729 -16.296  85.614  1.00 49.90           O  
ATOM   1206  OE2 GLU A 157      16.649 -16.981  87.692  1.00 51.68           O  
ATOM   1207  N   ARG A 158      12.965 -12.086  90.290  1.00 38.19           N  
ATOM   1208  CA  ARG A 158      12.011 -11.885  91.380  1.00 36.31           C  
ATOM   1209  C   ARG A 158      10.662 -12.485  91.037  1.00 36.29           C  
ATOM   1210  O   ARG A 158      10.193 -12.356  89.900  1.00 36.09           O  
ATOM   1211  CB  ARG A 158      11.873 -10.393  91.707  1.00 35.60           C  
ATOM   1212  CG  ARG A 158      13.120  -9.800  92.345  1.00 35.34           C  
ATOM   1213  CD  ARG A 158      12.986  -8.291  92.581  1.00 34.59           C  
ATOM   1214  NE  ARG A 158      11.831  -7.977  93.408  1.00 30.89           N  
ATOM   1215  CZ  ARG A 158      11.435  -6.743  93.718  1.00 32.62           C  
ATOM   1216  NH1 ARG A 158      12.098  -5.666  93.299  1.00 27.33           N  
ATOM   1217  NH2 ARG A 158      10.378  -6.580  94.482  1.00 33.50           N  
ATOM   1218  N   GLU A 159      10.054 -13.180  91.999  1.00 36.69           N  
ATOM   1219  CA  GLU A 159       8.654 -13.649  91.878  1.00 35.96           C  
ATOM   1220  C   GLU A 159       7.852 -13.641  93.192  1.00 35.72           C  
ATOM   1221  O   GLU A 159       7.914 -14.587  93.960  1.00 35.42           O  
ATOM   1222  CB  GLU A 159       8.540 -15.023  91.201  1.00 37.15           C  
ATOM   1223  CG  GLU A 159       7.054 -15.464  90.868  1.00 36.94           C  
ATOM   1224  CD  GLU A 159       6.304 -14.472  89.952  1.00 38.51           C  
ATOM   1225  OE1 GLU A 159       6.673 -14.323  88.764  1.00 45.65           O  
ATOM   1226  OE2 GLU A 159       5.365 -13.806  90.400  1.00 36.70           O  
ATOM   1227  N   PRO A 160       7.054 -12.584  93.417  1.00 35.38           N  
ATOM   1228  CA  PRO A 160       6.171 -12.477  94.563  1.00 35.18           C  
ATOM   1229  C   PRO A 160       5.000 -13.448  94.444  1.00 35.83           C  
ATOM   1230  O   PRO A 160       4.345 -13.745  95.454  1.00 35.96           O  
ATOM   1231  CB  PRO A 160       5.651 -11.045  94.455  1.00 35.43           C  
ATOM   1232  CG  PRO A 160       5.679 -10.758  93.002  1.00 35.03           C  
ATOM   1233  CD  PRO A 160       6.952 -11.404  92.542  1.00 35.29           C  
ATOM   1234  N   GLY A 161       4.735 -13.932  93.222  1.00 35.11           N  
ATOM   1235  CA  GLY A 161       3.658 -14.895  92.976  1.00 34.29           C  
ATOM   1236  C   GLY A 161       2.628 -14.547  91.898  1.00 34.10           C  
ATOM   1237  O   GLY A 161       1.943 -15.440  91.386  1.00 33.73           O  
ATOM   1238  N   TRP A 162       2.514 -13.271  91.551  1.00 33.15           N  
ATOM   1239  CA  TRP A 162       1.424 -12.813  90.685  1.00 33.50           C  
ATOM   1240  C   TRP A 162       1.872 -12.387  89.282  1.00 34.06           C  
ATOM   1241  O   TRP A 162       1.025 -12.102  88.438  1.00 34.26           O  
ATOM   1242  CB  TRP A 162       0.654 -11.659  91.334  1.00 32.84           C  
ATOM   1243  CG  TRP A 162       1.521 -10.496  91.652  1.00 32.69           C  
ATOM   1244  CD1 TRP A 162       2.216 -10.288  92.809  1.00 31.24           C  
ATOM   1245  CD2 TRP A 162       1.805  -9.363  90.799  1.00 33.11           C  
ATOM   1246  NE1 TRP A 162       2.931  -9.103  92.723  1.00 30.50           N  
ATOM   1247  CE2 TRP A 162       2.695  -8.526  91.500  1.00 31.73           C  
ATOM   1248  CE3 TRP A 162       1.410  -8.993  89.498  1.00 32.58           C  
ATOM   1249  CZ2 TRP A 162       3.177  -7.331  90.957  1.00 32.72           C  
ATOM   1250  CZ3 TRP A 162       1.897  -7.820  88.959  1.00 31.39           C  
ATOM   1251  CH2 TRP A 162       2.771  -7.001  89.680  1.00 32.54           C  
ATOM   1252  N   ILE A 163       3.184 -12.320  89.042  1.00 34.63           N  
ATOM   1253  CA  ILE A 163       3.712 -11.672  87.840  1.00 34.37           C  
ATOM   1254  C   ILE A 163       3.685 -12.603  86.630  1.00 35.77           C  
ATOM   1255  O   ILE A 163       3.112 -12.267  85.583  1.00 36.21           O  
ATOM   1256  CB  ILE A 163       5.147 -11.109  88.064  1.00 34.44           C  
ATOM   1257  CG1 ILE A 163       5.155 -10.058  89.198  1.00 34.33           C  
ATOM   1258  CG2 ILE A 163       5.707 -10.489  86.759  1.00 34.41           C  
ATOM   1259  CD1 ILE A 163       6.541  -9.589  89.642  1.00 32.35           C  
ATOM   1260  N   LYS A 164       4.311 -13.765  86.764  1.00 36.16           N  
ATOM   1261  CA  LYS A 164       4.375 -14.700  85.657  1.00 37.47           C  
ATOM   1262  C   LYS A 164       2.966 -15.081  85.195  1.00 37.73           C  
ATOM   1263  O   LYS A 164       2.713 -15.167  83.989  1.00 38.02           O  
ATOM   1264  CB  LYS A 164       5.244 -15.917  86.012  1.00 38.03           C  
ATOM   1265  CG  LYS A 164       5.449 -16.896  84.851  1.00 41.25           C  
ATOM   1266  CD  LYS A 164       6.813 -17.583  84.953  1.00 44.97           C  
ATOM   1267  CE  LYS A 164       7.022 -18.580  83.830  1.00 45.93           C  
ATOM   1268  NZ  LYS A 164       5.853 -19.494  83.687  1.00 48.14           N  
ATOM   1269  N   GLN A 165       2.042 -15.251  86.145  1.00 37.33           N  
ATOM   1270  CA  GLN A 165       0.634 -15.572  85.854  1.00 36.87           C  
ATOM   1271  C   GLN A 165      -0.149 -14.474  85.137  1.00 37.08           C  
ATOM   1272  O   GLN A 165      -0.995 -14.753  84.262  1.00 36.61           O  
ATOM   1273  CB  GLN A 165      -0.099 -15.925  87.155  1.00 37.15           C  
ATOM   1274  CG AGLN A 165      -0.516 -17.413  87.253  0.50 37.41           C  
ATOM   1275  CG BGLN A 165      -0.092 -17.397  87.503  0.50 37.26           C  
ATOM   1276  CD AGLN A 165       0.382 -18.359  86.452  0.50 37.59           C  
ATOM   1277  CD BGLN A 165      -1.370 -18.082  87.100  0.50 36.34           C  
ATOM   1278  OE1AGLN A 165      -0.109 -19.211  85.715  0.50 38.44           O  
ATOM   1279  OE1BGLN A 165      -2.468 -17.649  87.469  0.50 35.89           O  
ATOM   1280  NE2AGLN A 165       1.699 -18.201  86.586  0.50 37.26           N  
ATOM   1281  NE2BGLN A 165      -1.242 -19.167  86.348  0.50 37.11           N  
ATOM   1282  N   LEU A 166       0.089 -13.234  85.554  1.00 35.96           N  
ATOM   1283  CA  LEU A 166      -0.568 -12.104  84.955  1.00 35.67           C  
ATOM   1284  C   LEU A 166      -0.097 -11.938  83.507  1.00 36.02           C  
ATOM   1285  O   LEU A 166      -0.912 -11.823  82.606  1.00 36.33           O  
ATOM   1286  CB  LEU A 166      -0.302 -10.838  85.758  1.00 34.95           C  
ATOM   1287  CG  LEU A 166      -0.622  -9.510  85.075  1.00 33.61           C  
ATOM   1288  CD1 LEU A 166      -2.092  -9.186  85.138  1.00 32.99           C  
ATOM   1289  CD2 LEU A 166       0.176  -8.444  85.743  1.00 30.33           C  
ATOM   1290  N   PHE A 167       1.213 -11.919  83.299  1.00 36.41           N  
ATOM   1291  CA  PHE A 167       1.764 -11.815  81.957  1.00 36.70           C  
ATOM   1292  C   PHE A 167       1.168 -12.878  81.025  1.00 37.38           C  
ATOM   1293  O   PHE A 167       0.606 -12.550  79.974  1.00 37.91           O  
ATOM   1294  CB  PHE A 167       3.293 -11.905  81.983  1.00 35.99           C  
ATOM   1295  CG  PHE A 167       3.924 -11.712  80.619  1.00 36.38           C  
ATOM   1296  CD1 PHE A 167       4.083 -10.447  80.097  1.00 36.41           C  
ATOM   1297  CD2 PHE A 167       4.315 -12.816  79.848  1.00 36.29           C  
ATOM   1298  CE1 PHE A 167       4.644 -10.269  78.824  1.00 38.33           C  
ATOM   1299  CE2 PHE A 167       4.865 -12.646  78.588  1.00 35.50           C  
ATOM   1300  CZ  PHE A 167       5.031 -11.371  78.079  1.00 34.50           C  
ATOM   1301  N   THR A 168       1.248 -14.135  81.450  1.00 37.02           N  
ATOM   1302  CA  THR A 168       0.717 -15.270  80.729  1.00 37.17           C  
ATOM   1303  C   THR A 168      -0.781 -15.210  80.431  1.00 38.03           C  
ATOM   1304  O   THR A 168      -1.180 -15.449  79.290  1.00 38.40           O  
ATOM   1305  CB  THR A 168       1.056 -16.543  81.485  1.00 37.03           C  
ATOM   1306  OG1 THR A 168       2.482 -16.638  81.556  1.00 36.62           O  
ATOM   1307  CG2 THR A 168       0.492 -17.795  80.779  1.00 37.74           C  
ATOM   1308  N   ASN A 169      -1.610 -14.904  81.430  1.00 37.43           N  
ATOM   1309  CA  ASN A 169      -3.059 -14.895  81.236  1.00 37.86           C  
ATOM   1310  C   ASN A 169      -3.686 -13.565  80.794  1.00 37.77           C  
ATOM   1311  O   ASN A 169      -4.718 -13.565  80.147  1.00 37.89           O  
ATOM   1312  CB  ASN A 169      -3.778 -15.401  82.496  1.00 38.23           C  
ATOM   1313  CG  ASN A 169      -3.346 -16.808  82.905  1.00 39.80           C  
ATOM   1314  OD1 ASN A 169      -3.147 -17.074  84.085  1.00 44.62           O  
ATOM   1315  ND2 ASN A 169      -3.189 -17.700  81.941  1.00 39.92           N  
ATOM   1316  N   PHE A 170      -3.101 -12.434  81.170  1.00 37.86           N  
ATOM   1317  CA  PHE A 170      -3.707 -11.142  80.811  1.00 37.70           C  
ATOM   1318  C   PHE A 170      -2.861 -10.324  79.864  1.00 37.03           C  
ATOM   1319  O   PHE A 170      -3.374  -9.419  79.234  1.00 37.58           O  
ATOM   1320  CB  PHE A 170      -4.065 -10.309  82.059  1.00 37.58           C  
ATOM   1321  CG  PHE A 170      -4.996  -9.117  81.787  1.00 38.05           C  
ATOM   1322  CD1 PHE A 170      -6.373  -9.299  81.631  1.00 37.87           C  
ATOM   1323  CD2 PHE A 170      -4.495  -7.813  81.740  1.00 37.47           C  
ATOM   1324  CE1 PHE A 170      -7.245  -8.200  81.411  1.00 34.91           C  
ATOM   1325  CE2 PHE A 170      -5.351  -6.713  81.519  1.00 36.82           C  
ATOM   1326  CZ  PHE A 170      -6.734  -6.915  81.355  1.00 37.01           C  
ATOM   1327  N   ILE A 171      -1.570 -10.605  79.757  1.00 36.79           N  
ATOM   1328  CA  ILE A 171      -0.753  -9.694  78.963  1.00 36.72           C  
ATOM   1329  C   ILE A 171      -0.277 -10.220  77.592  1.00 37.20           C  
ATOM   1330  O   ILE A 171      -0.408  -9.492  76.617  1.00 37.22           O  
ATOM   1331  CB  ILE A 171       0.403  -9.061  79.746  1.00 36.60           C  
ATOM   1332  CG1 ILE A 171      -0.134  -8.163  80.864  1.00 35.53           C  
ATOM   1333  CG2 ILE A 171       1.252  -8.190  78.839  1.00 35.96           C  
ATOM   1334  CD1 ILE A 171       0.956  -7.652  81.801  1.00 33.81           C  
ATOM   1335  N   SER A 172       0.246 -11.449  77.503  1.00 36.55           N  
ATOM   1336  CA  SER A 172       0.896 -11.835  76.262  1.00 37.72           C  
ATOM   1337  C   SER A 172      -0.017 -11.849  75.026  1.00 37.53           C  
ATOM   1338  O   SER A 172       0.369 -11.290  74.032  1.00 37.73           O  
ATOM   1339  CB  SER A 172       1.770 -13.091  76.376  1.00 37.69           C  
ATOM   1340  OG  SER A 172       1.035 -14.182  76.842  1.00 40.06           O  
ATOM   1341  N   PHE A 173      -1.200 -12.474  75.080  1.00 38.25           N  
ATOM   1342  CA  PHE A 173      -2.014 -12.609  73.861  1.00 38.42           C  
ATOM   1343  C   PHE A 173      -2.492 -11.278  73.327  1.00 38.43           C  
ATOM   1344  O   PHE A 173      -2.494 -11.063  72.110  1.00 39.64           O  
ATOM   1345  CB  PHE A 173      -3.207 -13.566  73.993  1.00 38.71           C  
ATOM   1346  CG  PHE A 173      -3.868 -13.894  72.659  1.00 39.20           C  
ATOM   1347  CD1 PHE A 173      -5.236 -13.767  72.489  1.00 39.99           C  
ATOM   1348  CD2 PHE A 173      -3.106 -14.312  71.575  1.00 41.30           C  
ATOM   1349  CE1 PHE A 173      -5.853 -14.067  71.268  1.00 41.49           C  
ATOM   1350  CE2 PHE A 173      -3.716 -14.621  70.350  1.00 43.29           C  
ATOM   1351  CZ  PHE A 173      -5.102 -14.491  70.206  1.00 42.13           C  
ATOM   1352  N   THR A 174      -2.874 -10.367  74.209  1.00 37.23           N  
ATOM   1353  CA  THR A 174      -3.249  -9.051  73.724  1.00 36.20           C  
ATOM   1354  C   THR A 174      -2.034  -8.218  73.283  1.00 35.51           C  
ATOM   1355  O   THR A 174      -2.161  -7.292  72.475  1.00 34.47           O  
ATOM   1356  CB  THR A 174      -4.181  -8.298  74.709  1.00 36.50           C  
ATOM   1357  OG1 THR A 174      -3.406  -7.564  75.625  1.00 35.53           O  
ATOM   1358  CG2 THR A 174      -5.019  -9.280  75.476  1.00 35.43           C  
ATOM   1359  N   LEU A 175      -0.860  -8.563  73.790  1.00 34.39           N  
ATOM   1360  CA  LEU A 175       0.347  -7.892  73.380  1.00 33.34           C  
ATOM   1361  C   LEU A 175       0.732  -8.387  71.979  1.00 33.75           C  
ATOM   1362  O   LEU A 175       0.971  -7.574  71.090  1.00 33.76           O  
ATOM   1363  CB  LEU A 175       1.477  -8.142  74.371  1.00 33.48           C  
ATOM   1364  CG  LEU A 175       2.902  -7.699  74.027  1.00 31.05           C  
ATOM   1365  CD1 LEU A 175       2.978  -6.221  73.631  1.00 31.89           C  
ATOM   1366  CD2 LEU A 175       3.782  -7.972  75.211  1.00 28.65           C  
ATOM   1367  N   LYS A 176       0.814  -9.712  71.800  1.00 32.91           N  
ATOM   1368  CA  LYS A 176       0.988 -10.337  70.484  1.00 32.59           C  
ATOM   1369  C   LYS A 176       0.168  -9.645  69.398  1.00 33.43           C  
ATOM   1370  O   LYS A 176       0.692  -9.307  68.341  1.00 33.93           O  
ATOM   1371  CB  LYS A 176       0.634 -11.814  70.560  1.00 31.57           C  
ATOM   1372  CG  LYS A 176       1.767 -12.636  71.059  1.00 28.82           C  
ATOM   1373  CD  LYS A 176       1.346 -14.066  71.406  1.00 31.17           C  
ATOM   1374  CE  LYS A 176       2.460 -14.682  72.282  1.00 33.04           C  
ATOM   1375  NZ  LYS A 176       2.215 -16.096  72.705  1.00 34.97           N  
ATOM   1376  N   LEU A 177      -1.104  -9.407  69.689  1.00 34.29           N  
ATOM   1377  CA  LEU A 177      -2.028  -8.739  68.782  1.00 35.02           C  
ATOM   1378  C   LEU A 177      -1.687  -7.273  68.534  1.00 35.83           C  
ATOM   1379  O   LEU A 177      -1.920  -6.761  67.439  1.00 35.93           O  
ATOM   1380  CB  LEU A 177      -3.457  -8.861  69.307  1.00 34.27           C  
ATOM   1381  CG  LEU A 177      -4.069 -10.257  69.239  1.00 35.34           C  
ATOM   1382  CD1 LEU A 177      -5.356 -10.298  70.086  1.00 34.01           C  
ATOM   1383  CD2 LEU A 177      -4.382 -10.649  67.802  1.00 34.56           C  
ATOM   1384  N   VAL A 178      -1.157  -6.596  69.553  1.00 37.06           N  
ATOM   1385  CA  VAL A 178      -0.672  -5.211  69.427  1.00 36.98           C  
ATOM   1386  C   VAL A 178       0.594  -5.159  68.581  1.00 37.50           C  
ATOM   1387  O   VAL A 178       0.748  -4.275  67.733  1.00 38.00           O  
ATOM   1388  CB  VAL A 178      -0.376  -4.561  70.801  1.00 37.51           C  
ATOM   1389  CG1 VAL A 178       0.543  -3.325  70.647  1.00 36.88           C  
ATOM   1390  CG2 VAL A 178      -1.674  -4.153  71.500  1.00 37.96           C  
ATOM   1391  N   LEU A 179       1.510  -6.085  68.856  1.00 37.50           N  
ATOM   1392  CA  LEU A 179       2.726  -6.262  68.091  1.00 37.05           C  
ATOM   1393  C   LEU A 179       2.402  -6.380  66.608  1.00 37.12           C  
ATOM   1394  O   LEU A 179       2.945  -5.633  65.810  1.00 37.52           O  
ATOM   1395  CB  LEU A 179       3.523  -7.486  68.583  1.00 36.76           C  
ATOM   1396  CG  LEU A 179       4.179  -7.334  69.959  1.00 37.49           C  
ATOM   1397  CD1 LEU A 179       5.013  -8.552  70.409  1.00 36.09           C  
ATOM   1398  CD2 LEU A 179       5.029  -6.066  69.982  1.00 38.46           C  
ATOM   1399  N   LYS A 180       1.510  -7.301  66.263  1.00 36.80           N  
ATOM   1400  CA  LYS A 180       1.061  -7.512  64.895  1.00 37.23           C  
ATOM   1401  C   LYS A 180       0.488  -6.266  64.241  1.00 37.55           C  
ATOM   1402  O   LYS A 180       0.778  -5.992  63.088  1.00 38.28           O  
ATOM   1403  CB  LYS A 180      -0.014  -8.586  64.841  1.00 36.59           C  
ATOM   1404  CG  LYS A 180      -0.389  -8.971  63.408  1.00 35.77           C  
ATOM   1405  CD  LYS A 180      -1.868  -8.973  63.202  1.00 33.53           C  
ATOM   1406  CE  LYS A 180      -2.176  -9.031  61.726  1.00 35.76           C  
ATOM   1407  NZ  LYS A 180      -3.463  -8.354  61.486  1.00 34.91           N  
ATOM   1408  N   GLY A 181      -0.366  -5.550  64.954  1.00 37.61           N  
ATOM   1409  CA  GLY A 181      -0.933  -4.314  64.445  1.00 37.94           C  
ATOM   1410  C   GLY A 181       0.161  -3.333  64.076  1.00 38.94           C  
ATOM   1411  O   GLY A 181       0.097  -2.698  63.018  1.00 38.94           O  
ATOM   1412  N   GLN A 182       1.176  -3.217  64.932  1.00 38.39           N  
ATOM   1413  CA  GLN A 182       2.223  -2.218  64.743  1.00 38.86           C  
ATOM   1414  C   GLN A 182       3.197  -2.587  63.640  1.00 39.01           C  
ATOM   1415  O   GLN A 182       3.524  -1.762  62.796  1.00 38.79           O  
ATOM   1416  CB  GLN A 182       2.981  -1.959  66.051  1.00 39.03           C  
ATOM   1417  CG  GLN A 182       2.139  -1.211  67.074  1.00 39.17           C  
ATOM   1418  CD  GLN A 182       1.961   0.237  66.697  1.00 41.91           C  
ATOM   1419  OE1 GLN A 182       2.911   0.899  66.252  1.00 42.70           O  
ATOM   1420  NE2 GLN A 182       0.748   0.743  66.859  1.00 41.35           N  
ATOM   1421  N   ILE A 183       3.667  -3.824  63.676  1.00 39.10           N  
ATOM   1422  CA  ILE A 183       4.603  -4.339  62.704  1.00 40.05           C  
ATOM   1423  C   ILE A 183       3.988  -4.351  61.294  1.00 40.02           C  
ATOM   1424  O   ILE A 183       4.555  -3.791  60.362  1.00 39.69           O  
ATOM   1425  CB  ILE A 183       5.069  -5.762  63.122  1.00 40.12           C  
ATOM   1426  CG1 ILE A 183       5.883  -5.677  64.410  1.00 40.46           C  
ATOM   1427  CG2 ILE A 183       5.851  -6.446  62.012  1.00 40.45           C  
ATOM   1428  CD1 ILE A 183       6.954  -4.612  64.381  1.00 42.74           C  
ATOM   1429  N   CYS A 184       2.828  -4.983  61.149  1.00 39.99           N  
ATOM   1430  CA  CYS A 184       2.193  -5.056  59.856  1.00 40.47           C  
ATOM   1431  C   CYS A 184       1.921  -3.646  59.339  1.00 40.19           C  
ATOM   1432  O   CYS A 184       2.139  -3.359  58.171  1.00 39.54           O  
ATOM   1433  CB  CYS A 184       0.937  -5.919  59.920  1.00 40.27           C  
ATOM   1434  SG  CYS A 184       1.362  -7.680  60.133  1.00 44.62           S  
ATOM   1435  N   LYS A 185       1.486  -2.749  60.214  1.00 40.28           N  
ATOM   1436  CA  LYS A 185       1.191  -1.386  59.790  1.00 40.40           C  
ATOM   1437  C   LYS A 185       2.441  -0.682  59.247  1.00 40.15           C  
ATOM   1438  O   LYS A 185       2.392   0.040  58.243  1.00 40.26           O  
ATOM   1439  CB  LYS A 185       0.527  -0.602  60.917  1.00 40.55           C  
ATOM   1440  CG  LYS A 185       0.044   0.783  60.525  1.00 43.68           C  
ATOM   1441  CD  LYS A 185       1.007   1.843  60.999  1.00 48.11           C  
ATOM   1442  CE  LYS A 185       0.634   2.331  62.389  1.00 51.12           C  
ATOM   1443  NZ  LYS A 185      -0.405   3.411  62.298  1.00 53.47           N  
ATOM   1444  N   GLU A 186       3.566  -0.945  59.884  1.00 39.53           N  
ATOM   1445  CA  GLU A 186       4.814  -0.305  59.549  1.00 39.04           C  
ATOM   1446  C   GLU A 186       5.528  -0.956  58.358  1.00 38.27           C  
ATOM   1447  O   GLU A 186       6.329  -0.307  57.683  1.00 37.40           O  
ATOM   1448  CB  GLU A 186       5.706  -0.281  60.794  1.00 39.36           C  
ATOM   1449  CG  GLU A 186       6.496   0.997  60.966  1.00 41.20           C  
ATOM   1450  CD  GLU A 186       5.650   2.266  61.099  1.00 45.02           C  
ATOM   1451  OE1 GLU A 186       6.143   3.329  60.636  1.00 46.08           O  
ATOM   1452  OE2 GLU A 186       4.529   2.227  61.673  1.00 43.45           O  
ATOM   1453  N   ILE A 187       5.259  -2.240  58.134  1.00 37.73           N  
ATOM   1454  CA  ILE A 187       5.627  -2.936  56.901  1.00 37.72           C  
ATOM   1455  C   ILE A 187       4.922  -2.283  55.704  1.00 38.48           C  
ATOM   1456  O   ILE A 187       5.514  -2.109  54.635  1.00 38.91           O  
ATOM   1457  CB  ILE A 187       5.262  -4.447  56.972  1.00 37.90           C  
ATOM   1458  CG1 ILE A 187       6.318  -5.203  57.811  1.00 37.23           C  
ATOM   1459  CG2 ILE A 187       5.126  -5.038  55.567  1.00 37.71           C  
ATOM   1460  CD1 ILE A 187       6.016  -6.663  58.081  1.00 36.29           C  
ATOM   1461  N   ASN A 188       3.661  -1.917  55.914  1.00 38.10           N  
ATOM   1462  CA  ASN A 188       2.872  -1.243  54.927  1.00 38.63           C  
ATOM   1463  C   ASN A 188       3.388   0.148  54.607  1.00 38.57           C  
ATOM   1464  O   ASN A 188       3.407   0.520  53.431  1.00 39.05           O  
ATOM   1465  CB  ASN A 188       1.405  -1.217  55.336  1.00 38.42           C  
ATOM   1466  CG  ASN A 188       0.659  -2.459  54.896  1.00 40.47           C  
ATOM   1467  OD1 ASN A 188       0.236  -2.554  53.740  1.00 43.88           O  
ATOM   1468  ND2 ASN A 188       0.480  -3.420  55.811  1.00 39.28           N  
ATOM   1469  N   VAL A 189       3.830   0.913  55.610  1.00 37.56           N  
ATOM   1470  CA  VAL A 189       4.335   2.256  55.297  1.00 37.64           C  
ATOM   1471  C   VAL A 189       5.696   2.257  54.577  1.00 37.81           C  
ATOM   1472  O   VAL A 189       5.894   3.065  53.666  1.00 38.63           O  
ATOM   1473  CB  VAL A 189       4.294   3.335  56.467  1.00 37.17           C  
ATOM   1474  CG1 VAL A 189       3.336   2.970  57.586  1.00 35.48           C  
ATOM   1475  CG2 VAL A 189       5.658   3.628  56.987  1.00 37.84           C  
ATOM   1476  N   ILE A 190       6.614   1.387  54.995  1.00 36.91           N  
ATOM   1477  CA  ILE A 190       7.910   1.274  54.363  1.00 37.35           C  
ATOM   1478  C   ILE A 190       7.783   0.798  52.887  1.00 36.92           C  
ATOM   1479  O   ILE A 190       8.408   1.372  52.014  1.00 36.67           O  
ATOM   1480  CB  ILE A 190       8.900   0.405  55.199  1.00 37.86           C  
ATOM   1481  CG1 ILE A 190      10.311   0.463  54.627  1.00 39.11           C  
ATOM   1482  CG2 ILE A 190       8.464  -1.053  55.257  1.00 39.74           C  
ATOM   1483  CD1 ILE A 190      10.886   1.879  54.527  1.00 40.92           C  
ATOM   1484  N   SER A 191       6.952  -0.221  52.648  1.00 36.29           N  
ATOM   1485  CA  SER A 191       6.621  -0.746  51.334  1.00 36.22           C  
ATOM   1486  C   SER A 191       6.091   0.309  50.364  1.00 37.10           C  
ATOM   1487  O   SER A 191       6.460   0.305  49.175  1.00 37.23           O  
ATOM   1488  CB  SER A 191       5.608  -1.872  51.472  1.00 36.12           C  
ATOM   1489  OG  SER A 191       6.223  -2.947  52.149  1.00 36.45           O  
ATOM   1490  N   ASN A 192       5.242   1.206  50.869  1.00 36.99           N  
ATOM   1491  CA  ASN A 192       4.723   2.304  50.082  1.00 37.08           C  
ATOM   1492  C   ASN A 192       5.726   3.447  49.895  1.00 38.03           C  
ATOM   1493  O   ASN A 192       5.734   4.091  48.846  1.00 38.60           O  
ATOM   1494  CB  ASN A 192       3.408   2.799  50.657  1.00 36.33           C  
ATOM   1495  CG  ASN A 192       2.249   1.921  50.267  1.00 36.58           C  
ATOM   1496  OD1 ASN A 192       1.749   1.118  51.074  1.00 36.15           O  
ATOM   1497  ND2 ASN A 192       1.811   2.046  49.020  1.00 31.78           N  
ATOM   1498  N   ILE A 193       6.585   3.688  50.883  1.00 38.47           N  
ATOM   1499  CA  ILE A 193       7.700   4.620  50.725  1.00 38.54           C  
ATOM   1500  C   ILE A 193       8.698   4.151  49.645  1.00 39.49           C  
ATOM   1501  O   ILE A 193       9.223   4.965  48.869  1.00 39.95           O  
ATOM   1502  CB  ILE A 193       8.474   4.849  52.065  1.00 38.89           C  
ATOM   1503  CG1 ILE A 193       7.661   5.726  53.035  1.00 38.91           C  
ATOM   1504  CG2 ILE A 193       9.804   5.549  51.793  1.00 38.63           C  
ATOM   1505  CD1 ILE A 193       8.311   5.944  54.435  1.00 37.40           C  
ATOM   1506  N   MET A 194       8.992   2.856  49.636  1.00 39.62           N  
ATOM   1507  CA  MET A 194       9.935   2.266  48.694  1.00 40.36           C  
ATOM   1508  C   MET A 194       9.375   2.186  47.264  1.00 40.44           C  
ATOM   1509  O   MET A 194      10.135   2.317  46.313  1.00 40.83           O  
ATOM   1510  CB  MET A 194      10.341   0.862  49.139  1.00 40.51           C  
ATOM   1511  CG  MET A 194      11.424   0.780  50.227  1.00 40.34           C  
ATOM   1512  SD  MET A 194      11.599  -0.965  50.657  1.00 41.51           S  
ATOM   1513  CE  MET A 194      13.346  -0.961  50.960  1.00 42.90           C  
ATOM   1514  N   ALA A 195       8.075   1.917  47.125  1.00 39.87           N  
ATOM   1515  CA  ALA A 195       7.399   1.904  45.824  1.00 39.94           C  
ATOM   1516  C   ALA A 195       7.339   3.299  45.219  1.00 40.26           C  
ATOM   1517  O   ALA A 195       7.653   3.484  44.047  1.00 40.20           O  
ATOM   1518  CB  ALA A 195       5.992   1.344  45.956  1.00 39.64           C  
ATOM   1519  N   ASP A 196       6.905   4.268  46.018  1.00 40.21           N  
ATOM   1520  CA  ASP A 196       6.773   5.647  45.582  1.00 41.04           C  
ATOM   1521  C   ASP A 196       8.124   6.299  45.231  1.00 40.29           C  
ATOM   1522  O   ASP A 196       8.218   7.117  44.307  1.00 40.14           O  
ATOM   1523  CB  ASP A 196       6.047   6.461  46.649  1.00 41.41           C  
ATOM   1524  CG  ASP A 196       6.307   7.929  46.522  1.00 45.14           C  
ATOM   1525  OD1 ASP A 196       7.197   8.432  47.258  1.00 48.80           O  
ATOM   1526  OD2 ASP A 196       5.654   8.579  45.660  1.00 48.75           O  
ATOM   1527  N   PHE A 197       9.162   5.932  45.970  1.00 39.63           N  
ATOM   1528  CA  PHE A 197      10.506   6.437  45.730  1.00 38.86           C  
ATOM   1529  C   PHE A 197      11.061   5.989  44.365  1.00 38.95           C  
ATOM   1530  O   PHE A 197      11.598   6.804  43.622  1.00 38.64           O  
ATOM   1531  CB  PHE A 197      11.452   6.023  46.867  1.00 38.34           C  
ATOM   1532  CG  PHE A 197      12.905   6.266  46.568  1.00 37.60           C  
ATOM   1533  CD1 PHE A 197      13.456   7.532  46.716  1.00 36.90           C  
ATOM   1534  CD2 PHE A 197      13.726   5.218  46.134  1.00 36.73           C  
ATOM   1535  CE1 PHE A 197      14.801   7.761  46.429  1.00 38.05           C  
ATOM   1536  CE2 PHE A 197      15.061   5.435  45.838  1.00 36.67           C  
ATOM   1537  CZ  PHE A 197      15.609   6.708  45.997  1.00 37.39           C  
ATOM   1538  N   VAL A 198      10.962   4.696  44.069  1.00 39.09           N  
ATOM   1539  CA  VAL A 198      11.351   4.156  42.766  1.00 39.66           C  
ATOM   1540  C   VAL A 198      10.622   4.879  41.630  1.00 39.40           C  
ATOM   1541  O   VAL A 198      11.238   5.344  40.678  1.00 39.63           O  
ATOM   1542  CB  VAL A 198      11.087   2.646  42.664  1.00 39.58           C  
ATOM   1543  CG1 VAL A 198      11.282   2.179  41.238  1.00 39.97           C  
ATOM   1544  CG2 VAL A 198      12.045   1.882  43.583  1.00 40.61           C  
ATOM   1545  N   GLN A 199       9.313   4.998  41.741  1.00 39.10           N  
ATOM   1546  CA  GLN A 199       8.565   5.657  40.698  1.00 39.77           C  
ATOM   1547  C   GLN A 199       8.990   7.096  40.482  1.00 40.19           C  
ATOM   1548  O   GLN A 199       9.031   7.550  39.347  1.00 40.07           O  
ATOM   1549  CB  GLN A 199       7.086   5.564  40.971  1.00 39.27           C  
ATOM   1550  CG  GLN A 199       6.549   4.243  40.556  1.00 39.32           C  
ATOM   1551  CD  GLN A 199       5.188   4.019  41.099  1.00 39.06           C  
ATOM   1552  OE1 GLN A 199       4.190   4.199  40.394  1.00 38.14           O  
ATOM   1553  NE2 GLN A 199       5.116   3.660  42.385  1.00 39.08           N  
ATOM   1554  N   THR A 200       9.342   7.791  41.559  1.00 40.93           N  
ATOM   1555  CA  THR A 200       9.700   9.211  41.483  1.00 41.33           C  
ATOM   1556  C   THR A 200      11.086   9.348  40.895  1.00 41.91           C  
ATOM   1557  O   THR A 200      11.350  10.299  40.176  1.00 42.88           O  
ATOM   1558  CB  THR A 200       9.616   9.917  42.865  1.00 41.38           C  
ATOM   1559  OG1ATHR A 200       8.328   9.659  43.448  0.50 41.69           O  
ATOM   1560  OG1BTHR A 200      10.272   9.121  43.854  0.50 42.11           O  
ATOM   1561  CG2ATHR A 200       9.825  11.423  42.749  0.50 40.51           C  
ATOM   1562  CG2BTHR A 200       8.164  10.130  43.273  0.50 42.00           C  
ATOM   1563  N   ARG A 201      11.960   8.391  41.193  1.00 42.14           N  
ATOM   1564  CA  ARG A 201      13.298   8.364  40.629  1.00 42.07           C  
ATOM   1565  C   ARG A 201      13.281   7.950  39.151  1.00 41.62           C  
ATOM   1566  O   ARG A 201      14.089   8.446  38.369  1.00 40.97           O  
ATOM   1567  CB  ARG A 201      14.205   7.447  41.433  1.00 42.55           C  
ATOM   1568  CG  ARG A 201      15.512   7.085  40.724  1.00 45.85           C  
ATOM   1569  CD  ARG A 201      16.465   8.297  40.539  1.00 51.62           C  
ATOM   1570  NE  ARG A 201      17.399   8.369  41.661  1.00 55.27           N  
ATOM   1571  CZ  ARG A 201      17.131   8.962  42.816  1.00 56.56           C  
ATOM   1572  NH1 ARG A 201      15.962   9.566  43.007  1.00 57.84           N  
ATOM   1573  NH2 ARG A 201      18.036   8.948  43.781  1.00 57.13           N  
ATOM   1574  N   ALA A 202      12.387   7.029  38.786  1.00 41.08           N  
ATOM   1575  CA  ALA A 202      12.153   6.671  37.388  1.00 41.05           C  
ATOM   1576  C   ALA A 202      11.778   7.919  36.599  1.00 41.56           C  
ATOM   1577  O   ALA A 202      12.373   8.200  35.568  1.00 42.51           O  
ATOM   1578  CB  ALA A 202      11.069   5.630  37.272  1.00 41.02           C  
ATOM   1579  N   ALA A 203      10.818   8.684  37.100  1.00 41.33           N  
ATOM   1580  CA  ALA A 203      10.373   9.894  36.429  1.00 41.25           C  
ATOM   1581  C   ALA A 203      11.492  10.927  36.345  1.00 41.39           C  
ATOM   1582  O   ALA A 203      11.611  11.638  35.346  1.00 41.84           O  
ATOM   1583  CB  ALA A 203       9.153  10.474  37.124  1.00 40.64           C  
ATOM   1584  N   SER A 204      12.322  10.982  37.381  1.00 41.03           N  
ATOM   1585  CA  SER A 204      13.419  11.935  37.477  1.00 40.54           C  
ATOM   1586  C   SER A 204      14.506  11.633  36.440  1.00 40.01           C  
ATOM   1587  O   SER A 204      15.119  12.528  35.873  1.00 39.54           O  
ATOM   1588  CB  SER A 204      14.007  11.879  38.887  1.00 41.03           C  
ATOM   1589  OG  SER A 204      14.988  12.888  39.088  1.00 41.75           O  
ATOM   1590  N   ILE A 205      14.744  10.356  36.201  1.00 39.17           N  
ATOM   1591  CA  ILE A 205      15.662   9.928  35.165  1.00 39.07           C  
ATOM   1592  C   ILE A 205      15.200  10.401  33.771  1.00 38.99           C  
ATOM   1593  O   ILE A 205      16.033  10.680  32.890  1.00 39.25           O  
ATOM   1594  CB  ILE A 205      15.797   8.389  35.181  1.00 39.13           C  
ATOM   1595  CG1 ILE A 205      16.661   7.946  36.376  1.00 39.31           C  
ATOM   1596  CG2 ILE A 205      16.371   7.892  33.858  1.00 38.38           C  
ATOM   1597  CD1 ILE A 205      16.693   6.428  36.622  1.00 38.88           C  
ATOM   1598  N   LEU A 206      13.883  10.494  33.584  1.00 38.26           N  
ATOM   1599  CA  LEU A 206      13.312  10.896  32.305  1.00 37.93           C  
ATOM   1600  C   LEU A 206      12.938  12.373  32.247  1.00 37.80           C  
ATOM   1601  O   LEU A 206      12.206  12.779  31.363  1.00 39.01           O  
ATOM   1602  CB  LEU A 206      12.112  10.010  31.948  1.00 37.94           C  
ATOM   1603  CG  LEU A 206      12.265   8.483  31.995  1.00 37.38           C  
ATOM   1604  CD1 LEU A 206      10.919   7.822  31.966  1.00 38.74           C  
ATOM   1605  CD2 LEU A 206      13.104   7.952  30.865  1.00 39.77           C  
ATOM   1606  N   SER A 207      13.468  13.174  33.164  1.00 36.98           N  
ATOM   1607  CA  SER A 207      13.136  14.596  33.269  1.00 37.09           C  
ATOM   1608  C   SER A 207      14.406  15.440  33.239  1.00 36.94           C  
ATOM   1609  O   SER A 207      15.471  14.949  33.589  1.00 36.44           O  
ATOM   1610  CB  SER A 207      12.384  14.857  34.583  1.00 36.73           C  
ATOM   1611  OG  SER A 207      11.254  13.988  34.699  1.00 37.13           O  
ATOM   1612  N   ASP A 208      14.302  16.712  32.839  1.00 37.78           N  
ATOM   1613  CA  ASP A 208      15.472  17.621  32.767  1.00 37.92           C  
ATOM   1614  C   ASP A 208      14.997  19.033  32.544  1.00 38.39           C  
ATOM   1615  O   ASP A 208      14.378  19.326  31.517  1.00 38.60           O  
ATOM   1616  CB  ASP A 208      16.401  17.239  31.617  1.00 38.38           C  
ATOM   1617  CG  ASP A 208      17.765  17.951  31.680  1.00 40.36           C  
ATOM   1618  OD1 ASP A 208      18.103  18.681  30.729  1.00 42.85           O  
ATOM   1619  OD2 ASP A 208      18.511  17.787  32.674  1.00 41.56           O  
ATOM   1620  N   GLY A 209      15.295  19.921  33.487  1.00 38.02           N  
ATOM   1621  CA  GLY A 209      14.862  21.307  33.381  1.00 37.43           C  
ATOM   1622  C   GLY A 209      13.385  21.355  33.081  1.00 37.57           C  
ATOM   1623  O   GLY A 209      12.591  20.729  33.806  1.00 37.78           O  
ATOM   1624  N   ASP A 210      13.013  22.052  31.999  1.00 36.75           N  
ATOM   1625  CA  ASP A 210      11.598  22.257  31.632  1.00 36.82           C  
ATOM   1626  C   ASP A 210      10.948  21.016  31.023  1.00 35.50           C  
ATOM   1627  O   ASP A 210       9.758  21.012  30.730  1.00 34.77           O  
ATOM   1628  CB  ASP A 210      11.450  23.430  30.662  1.00 37.55           C  
ATOM   1629  CG  ASP A 210      11.414  24.791  31.364  1.00 41.04           C  
ATOM   1630  OD1 ASP A 210      10.845  24.913  32.481  1.00 44.74           O  
ATOM   1631  OD2 ASP A 210      11.925  25.768  30.770  1.00 44.49           O  
ATOM   1632  N   ILE A 211      11.731  19.958  30.857  1.00 34.82           N  
ATOM   1633  CA  ILE A 211      11.231  18.696  30.319  1.00 34.73           C  
ATOM   1634  C   ILE A 211      10.948  17.719  31.469  1.00 35.22           C  
ATOM   1635  O   ILE A 211      11.848  17.386  32.228  1.00 35.00           O  
ATOM   1636  CB  ILE A 211      12.245  18.073  29.293  1.00 35.19           C  
ATOM   1637  CG1 ILE A 211      12.273  18.881  27.972  1.00 34.49           C  
ATOM   1638  CG2 ILE A 211      11.927  16.600  28.994  1.00 33.96           C  
ATOM   1639  CD1 ILE A 211      13.467  18.557  27.069  1.00 33.74           C  
ATOM   1640  N   GLY A 212       9.700  17.266  31.564  1.00 35.57           N  
ATOM   1641  CA  GLY A 212       9.283  16.210  32.471  1.00 35.63           C  
ATOM   1642  C   GLY A 212       8.685  15.056  31.694  1.00 36.34           C  
ATOM   1643  O   GLY A 212       8.665  15.062  30.458  1.00 37.16           O  
ATOM   1644  N   VAL A 213       8.213  14.050  32.418  1.00 35.92           N  
ATOM   1645  CA  VAL A 213       7.558  12.877  31.836  1.00 34.67           C  
ATOM   1646  C   VAL A 213       6.358  12.506  32.703  1.00 35.03           C  
ATOM   1647  O   VAL A 213       6.384  12.650  33.938  1.00 35.10           O  
ATOM   1648  CB  VAL A 213       8.500  11.689  31.776  1.00 34.23           C  
ATOM   1649  CG1 VAL A 213       8.711  11.105  33.172  1.00 33.42           C  
ATOM   1650  CG2 VAL A 213       7.989  10.601  30.773  1.00 33.95           C  
ATOM   1651  N   ASP A 214       5.312  12.027  32.058  1.00 34.15           N  
ATOM   1652  CA  ASP A 214       4.188  11.485  32.765  1.00 33.76           C  
ATOM   1653  C   ASP A 214       4.266   9.974  32.608  1.00 33.35           C  
ATOM   1654  O   ASP A 214       4.107   9.459  31.509  1.00 32.98           O  
ATOM   1655  CB  ASP A 214       2.899  12.054  32.187  1.00 34.39           C  
ATOM   1656  CG  ASP A 214       1.662  11.421  32.777  1.00 36.49           C  
ATOM   1657  OD1 ASP A 214       1.776  10.418  33.516  1.00 38.56           O  
ATOM   1658  OD2 ASP A 214       0.567  11.937  32.502  1.00 37.92           O  
ATOM   1659  N   ILE A 215       4.574   9.270  33.701  1.00 32.62           N  
ATOM   1660  CA  ILE A 215       4.590   7.806  33.694  1.00 32.13           C  
ATOM   1661  C   ILE A 215       3.445   7.227  34.531  1.00 32.49           C  
ATOM   1662  O   ILE A 215       3.548   6.115  35.088  1.00 31.83           O  
ATOM   1663  CB  ILE A 215       5.943   7.213  34.122  1.00 31.47           C  
ATOM   1664  CG1 ILE A 215       6.428   7.769  35.469  1.00 32.74           C  
ATOM   1665  CG2 ILE A 215       7.007   7.437  33.058  1.00 32.09           C  
ATOM   1666  CD1 ILE A 215       7.649   6.995  36.010  1.00 31.89           C  
ATOM   1667  N   SER A 216       2.361   7.992  34.611  1.00 32.54           N  
ATOM   1668  CA  SER A 216       1.120   7.528  35.191  1.00 34.22           C  
ATOM   1669  C   SER A 216       0.827   6.146  34.679  1.00 35.25           C  
ATOM   1670  O   SER A 216       1.037   5.874  33.487  1.00 35.35           O  
ATOM   1671  CB  SER A 216      -0.035   8.399  34.729  1.00 33.75           C  
ATOM   1672  OG  SER A 216      -0.152   9.540  35.527  1.00 36.65           O  
ATOM   1673  N   LEU A 217       0.276   5.301  35.555  1.00 36.48           N  
ATOM   1674  CA  LEU A 217      -0.128   3.942  35.199  1.00 37.36           C  
ATOM   1675  C   LEU A 217      -1.400   3.900  34.369  1.00 38.12           C  
ATOM   1676  O   LEU A 217      -2.329   4.667  34.600  1.00 38.56           O  
ATOM   1677  CB  LEU A 217      -0.370   3.105  36.445  1.00 37.69           C  
ATOM   1678  CG  LEU A 217       0.699   2.550  37.380  1.00 37.46           C  
ATOM   1679  CD1 LEU A 217      -0.054   1.720  38.392  1.00 36.76           C  
ATOM   1680  CD2 LEU A 217       1.737   1.705  36.719  1.00 35.48           C  
ATOM   1681  N   THR A 218      -1.451   2.951  33.434  1.00 39.16           N  
ATOM   1682  CA  THR A 218      -2.598   2.757  32.553  1.00 39.42           C  
ATOM   1683  C   THR A 218      -3.546   1.639  33.037  1.00 40.18           C  
ATOM   1684  O   THR A 218      -4.630   1.454  32.480  1.00 41.07           O  
ATOM   1685  CB  THR A 218      -2.140   2.485  31.108  1.00 38.89           C  
ATOM   1686  OG1 THR A 218      -1.332   1.315  31.091  1.00 39.65           O  
ATOM   1687  CG2 THR A 218      -1.313   3.635  30.596  1.00 38.18           C  
ATOM   1688  N   GLY A 219      -3.147   0.914  34.077  1.00 40.27           N  
ATOM   1689  CA  GLY A 219      -3.976  -0.133  34.664  1.00 40.34           C  
ATOM   1690  C   GLY A 219      -3.231  -0.710  35.847  1.00 40.66           C  
ATOM   1691  O   GLY A 219      -2.074  -0.357  36.068  1.00 39.99           O  
ATOM   1692  N   ASP A 220      -3.877  -1.597  36.608  1.00 41.01           N  
ATOM   1693  CA  ASP A 220      -3.245  -2.173  37.797  1.00 41.47           C  
ATOM   1694  C   ASP A 220      -2.018  -2.895  37.325  1.00 40.60           C  
ATOM   1695  O   ASP A 220      -2.013  -3.406  36.200  1.00 40.91           O  
ATOM   1696  CB  ASP A 220      -4.151  -3.190  38.507  1.00 42.43           C  
ATOM   1697  CG  ASP A 220      -5.262  -2.537  39.340  1.00 44.80           C  
ATOM   1698  OD1 ASP A 220      -6.266  -3.251  39.587  1.00 47.83           O  
ATOM   1699  OD2 ASP A 220      -5.147  -1.348  39.744  1.00 45.31           O  
ATOM   1700  N   PRO A 221      -0.967  -2.946  38.162  1.00 39.60           N  
ATOM   1701  CA  PRO A 221       0.159  -3.739  37.701  1.00 38.67           C  
ATOM   1702  C   PRO A 221      -0.282  -5.190  37.543  1.00 37.85           C  
ATOM   1703  O   PRO A 221      -1.381  -5.555  37.982  1.00 38.38           O  
ATOM   1704  CB  PRO A 221       1.191  -3.597  38.835  1.00 38.72           C  
ATOM   1705  CG  PRO A 221       0.788  -2.431  39.595  1.00 38.77           C  
ATOM   1706  CD  PRO A 221      -0.708  -2.333  39.475  1.00 39.51           C  
ATOM   1707  N   VAL A 222       0.557  -6.004  36.912  1.00 36.52           N  
ATOM   1708  CA  VAL A 222       0.244  -7.410  36.647  1.00 34.49           C  
ATOM   1709  C   VAL A 222       1.275  -8.273  37.359  1.00 34.64           C  
ATOM   1710  O   VAL A 222       2.450  -7.916  37.406  1.00 33.97           O  
ATOM   1711  CB  VAL A 222       0.289  -7.721  35.105  1.00 34.66           C  
ATOM   1712  CG1 VAL A 222       0.537  -9.207  34.831  1.00 32.57           C  
ATOM   1713  CG2 VAL A 222      -0.986  -7.243  34.416  1.00 33.16           C  
ATOM   1714  N   ILE A 223       0.832  -9.398  37.915  1.00 33.80           N  
ATOM   1715  CA  ILE A 223       1.715 -10.334  38.581  1.00 34.05           C  
ATOM   1716  C   ILE A 223       1.466 -11.705  37.978  1.00 34.29           C  
ATOM   1717  O   ILE A 223       0.326 -12.103  37.803  1.00 33.15           O  
ATOM   1718  CB  ILE A 223       1.432 -10.399  40.131  1.00 35.08           C  
ATOM   1719  CG1 ILE A 223       1.647  -9.023  40.781  1.00 33.49           C  
ATOM   1720  CG2 ILE A 223       2.295 -11.492  40.813  1.00 32.12           C  
ATOM   1721  CD1 ILE A 223       1.111  -8.922  42.208  1.00 34.37           C  
ATOM   1722  N   THR A 224       2.539 -12.398  37.623  1.00 34.90           N  
ATOM   1723  CA  THR A 224       2.457 -13.792  37.187  1.00 35.68           C  
ATOM   1724  C   THR A 224       3.472 -14.529  38.043  1.00 36.24           C  
ATOM   1725  O   THR A 224       4.221 -13.896  38.780  1.00 36.41           O  
ATOM   1726  CB  THR A 224       2.845 -13.976  35.663  1.00 35.56           C  
ATOM   1727  OG1 THR A 224       4.263 -13.869  35.498  1.00 36.25           O  
ATOM   1728  CG2 THR A 224       2.169 -12.942  34.774  1.00 35.82           C  
ATOM   1729  N   ALA A 225       3.540 -15.849  37.908  1.00 36.86           N  
ATOM   1730  CA  ALA A 225       4.521 -16.654  38.634  1.00 37.14           C  
ATOM   1731  C   ALA A 225       5.959 -16.314  38.305  1.00 37.69           C  
ATOM   1732  O   ALA A 225       6.875 -16.768  39.015  1.00 38.41           O  
ATOM   1733  CB  ALA A 225       4.274 -18.118  38.387  1.00 37.24           C  
ATOM   1734  N   SER A 226       6.164 -15.523  37.246  1.00 37.14           N  
ATOM   1735  CA  SER A 226       7.506 -15.272  36.711  1.00 37.06           C  
ATOM   1736  C   SER A 226       7.964 -13.829  36.795  1.00 36.07           C  
ATOM   1737  O   SER A 226       9.169 -13.540  36.764  1.00 36.75           O  
ATOM   1738  CB  SER A 226       7.546 -15.685  35.238  1.00 38.31           C  
ATOM   1739  OG  SER A 226       7.656 -17.093  35.125  1.00 41.24           O  
ATOM   1740  N   TYR A 227       7.019 -12.910  36.866  1.00 34.41           N  
ATOM   1741  CA  TYR A 227       7.393 -11.505  36.858  1.00 34.12           C  
ATOM   1742  C   TYR A 227       6.299 -10.638  37.409  1.00 34.19           C  
ATOM   1743  O   TYR A 227       5.163 -11.095  37.625  1.00 33.63           O  
ATOM   1744  CB  TYR A 227       7.731 -11.052  35.418  1.00 33.61           C  
ATOM   1745  CG  TYR A 227       6.582 -11.186  34.417  1.00 33.28           C  
ATOM   1746  CD1 TYR A 227       6.493 -12.291  33.562  1.00 34.02           C  
ATOM   1747  CD2 TYR A 227       5.606 -10.203  34.314  1.00 32.98           C  
ATOM   1748  CE1 TYR A 227       5.453 -12.410  32.646  1.00 33.25           C  
ATOM   1749  CE2 TYR A 227       4.570 -10.313  33.419  1.00 33.77           C  
ATOM   1750  CZ  TYR A 227       4.493 -11.414  32.587  1.00 33.65           C  
ATOM   1751  OH  TYR A 227       3.461 -11.490  31.692  1.00 33.51           O  
ATOM   1752  N   LEU A 228       6.640  -9.372  37.609  1.00 34.87           N  
ATOM   1753  CA  LEU A 228       5.619  -8.354  37.713  1.00 35.67           C  
ATOM   1754  C   LEU A 228       5.853  -7.231  36.695  1.00 35.55           C  
ATOM   1755  O   LEU A 228       6.996  -6.911  36.332  1.00 35.61           O  
ATOM   1756  CB  LEU A 228       5.513  -7.835  39.147  1.00 36.47           C  
ATOM   1757  CG  LEU A 228       6.765  -7.234  39.757  1.00 37.62           C  
ATOM   1758  CD1 LEU A 228       6.733  -5.739  39.524  1.00 41.22           C  
ATOM   1759  CD2 LEU A 228       6.811  -7.540  41.234  1.00 37.87           C  
ATOM   1760  N   GLU A 229       4.761  -6.623  36.259  1.00 34.72           N  
ATOM   1761  CA  GLU A 229       4.796  -5.744  35.128  1.00 34.57           C  
ATOM   1762  C   GLU A 229       3.923  -4.542  35.409  1.00 34.08           C  
ATOM   1763  O   GLU A 229       2.768  -4.703  35.805  1.00 33.57           O  
ATOM   1764  CB  GLU A 229       4.261  -6.501  33.909  1.00 35.15           C  
ATOM   1765  CG  GLU A 229       4.586  -5.903  32.569  1.00 35.62           C  
ATOM   1766  CD  GLU A 229       4.209  -6.848  31.457  1.00 38.08           C  
ATOM   1767  OE1 GLU A 229       2.994  -6.932  31.131  1.00 35.40           O  
ATOM   1768  OE2 GLU A 229       5.131  -7.522  30.940  1.00 37.24           O  
ATOM   1769  N   SER A 230       4.500  -3.352  35.240  1.00 33.05           N  
ATOM   1770  CA  SER A 230       3.764  -2.094  35.298  1.00 33.18           C  
ATOM   1771  C   SER A 230       3.704  -1.407  33.915  1.00 33.37           C  
ATOM   1772  O   SER A 230       4.665  -1.450  33.141  1.00 33.15           O  
ATOM   1773  CB  SER A 230       4.354  -1.154  36.352  1.00 33.52           C  
ATOM   1774  OG  SER A 230       5.747  -1.362  36.530  1.00 33.68           O  
ATOM   1775  N   HIS A 231       2.561  -0.796  33.605  1.00 33.32           N  
ATOM   1776  CA  HIS A 231       2.357  -0.153  32.301  1.00 33.52           C  
ATOM   1777  C   HIS A 231       2.122   1.326  32.468  1.00 32.71           C  
ATOM   1778  O   HIS A 231       1.225   1.724  33.196  1.00 32.64           O  
ATOM   1779  CB  HIS A 231       1.202  -0.831  31.579  1.00 33.89           C  
ATOM   1780  CG  HIS A 231       1.275  -2.323  31.656  1.00 34.90           C  
ATOM   1781  ND1 HIS A 231       0.481  -3.061  32.506  1.00 35.72           N  
ATOM   1782  CD2 HIS A 231       2.108  -3.203  31.053  1.00 35.23           C  
ATOM   1783  CE1 HIS A 231       0.793  -4.342  32.385  1.00 38.06           C  
ATOM   1784  NE2 HIS A 231       1.779  -4.455  31.509  1.00 33.88           N  
ATOM   1785  N   HIS A 232       2.943   2.135  31.801  1.00 32.63           N  
ATOM   1786  CA  HIS A 232       2.932   3.586  31.987  1.00 32.38           C  
ATOM   1787  C   HIS A 232       2.656   4.353  30.684  1.00 33.36           C  
ATOM   1788  O   HIS A 232       2.885   3.823  29.598  1.00 32.85           O  
ATOM   1789  CB  HIS A 232       4.268   4.036  32.584  1.00 32.17           C  
ATOM   1790  CG  HIS A 232       4.741   3.188  33.727  1.00 30.61           C  
ATOM   1791  ND1 HIS A 232       4.508   3.520  35.042  1.00 26.55           N  
ATOM   1792  CD2 HIS A 232       5.447   2.031  33.749  1.00 30.19           C  
ATOM   1793  CE1 HIS A 232       5.039   2.604  35.829  1.00 29.64           C  
ATOM   1794  NE2 HIS A 232       5.609   1.681  35.069  1.00 33.04           N  
ATOM   1795  N   LYS A 233       2.198   5.602  30.788  1.00 33.63           N  
ATOM   1796  CA  LYS A 233       1.872   6.378  29.582  1.00 34.56           C  
ATOM   1797  C   LYS A 233       3.129   6.721  28.801  1.00 34.46           C  
ATOM   1798  O   LYS A 233       3.227   6.371  27.621  1.00 34.85           O  
ATOM   1799  CB  LYS A 233       1.013   7.636  29.868  1.00 34.34           C  
ATOM   1800  CG  LYS A 233      -0.086   7.420  30.909  1.00 36.41           C  
ATOM   1801  CD  LYS A 233      -1.463   7.940  30.551  1.00 37.19           C  
ATOM   1802  CE  LYS A 233      -1.559   9.444  30.500  1.00 41.37           C  
ATOM   1803  NZ  LYS A 233      -3.000   9.839  30.291  1.00 40.99           N  
ATOM   1804  N   GLY A 234       4.080   7.403  29.437  1.00 34.08           N  
ATOM   1805  CA  GLY A 234       5.305   7.831  28.772  1.00 33.85           C  
ATOM   1806  C   GLY A 234       5.177   9.063  27.877  1.00 35.25           C  
ATOM   1807  O   GLY A 234       5.875   9.184  26.838  1.00 35.73           O  
ATOM   1808  N   HIS A 235       4.309   9.995  28.265  1.00 34.19           N  
ATOM   1809  CA  HIS A 235       4.183  11.263  27.556  1.00 33.02           C  
ATOM   1810  C   HIS A 235       5.133  12.287  28.131  1.00 33.07           C  
ATOM   1811  O   HIS A 235       5.111  12.532  29.342  1.00 33.22           O  
ATOM   1812  CB  HIS A 235       2.763  11.831  27.684  1.00 33.02           C  
ATOM   1813  CG  HIS A 235       1.682  10.937  27.159  1.00 33.00           C  
ATOM   1814  ND1 HIS A 235       0.368  11.061  27.555  1.00 35.30           N  
ATOM   1815  CD2 HIS A 235       1.705   9.920  26.263  1.00 33.70           C  
ATOM   1816  CE1 HIS A 235      -0.374  10.165  26.919  1.00 31.63           C  
ATOM   1817  NE2 HIS A 235       0.416   9.450  26.144  1.00 31.51           N  
ATOM   1818  N   PHE A 236       5.952  12.916  27.285  1.00 32.22           N  
ATOM   1819  CA  PHE A 236       6.835  13.963  27.762  1.00 31.68           C  
ATOM   1820  C   PHE A 236       6.083  15.251  27.921  1.00 32.17           C  
ATOM   1821  O   PHE A 236       5.110  15.534  27.194  1.00 31.63           O  
ATOM   1822  CB  PHE A 236       8.109  14.108  26.921  1.00 32.09           C  
ATOM   1823  CG  PHE A 236       9.114  13.044  27.204  1.00 31.61           C  
ATOM   1824  CD1 PHE A 236       9.088  11.858  26.510  1.00 32.92           C  
ATOM   1825  CD2 PHE A 236      10.030  13.196  28.238  1.00 32.00           C  
ATOM   1826  CE1 PHE A 236       9.977  10.847  26.806  1.00 34.09           C  
ATOM   1827  CE2 PHE A 236      10.931  12.185  28.544  1.00 31.51           C  
ATOM   1828  CZ  PHE A 236      10.910  11.017  27.832  1.00 33.50           C  
ATOM   1829  N   ILE A 237       6.519  16.017  28.918  1.00 31.43           N  
ATOM   1830  CA  ILE A 237       5.829  17.212  29.332  1.00 31.20           C  
ATOM   1831  C   ILE A 237       6.824  18.332  29.101  1.00 31.02           C  
ATOM   1832  O   ILE A 237       8.008  18.148  29.364  1.00 31.12           O  
ATOM   1833  CB  ILE A 237       5.437  17.105  30.831  1.00 31.12           C  
ATOM   1834  CG1 ILE A 237       4.554  15.880  31.063  1.00 31.32           C  
ATOM   1835  CG2 ILE A 237       4.727  18.344  31.269  1.00 29.74           C  
ATOM   1836  CD1 ILE A 237       4.372  15.513  32.533  1.00 33.10           C  
ATOM   1837  N   TYR A 238       6.372  19.462  28.553  1.00 30.86           N  
ATOM   1838  CA  TYR A 238       7.268  20.595  28.320  1.00 30.42           C  
ATOM   1839  C   TYR A 238       6.621  21.783  28.965  1.00 30.64           C  
ATOM   1840  O   TYR A 238       5.470  22.072  28.676  1.00 30.34           O  
ATOM   1841  CB  TYR A 238       7.501  20.871  26.812  1.00 29.90           C  
ATOM   1842  CG  TYR A 238       8.418  22.057  26.563  1.00 28.51           C  
ATOM   1843  CD1 TYR A 238       9.705  22.050  27.059  1.00 27.45           C  
ATOM   1844  CD2 TYR A 238       7.989  23.186  25.862  1.00 26.64           C  
ATOM   1845  CE1 TYR A 238      10.558  23.122  26.884  1.00 27.92           C  
ATOM   1846  CE2 TYR A 238       8.833  24.283  25.690  1.00 26.61           C  
ATOM   1847  CZ  TYR A 238      10.131  24.232  26.196  1.00 28.78           C  
ATOM   1848  OH  TYR A 238      11.045  25.278  26.038  1.00 31.04           O  
ATOM   1849  N   LYS A 239       7.356  22.458  29.846  1.00 31.57           N  
ATOM   1850  CA  LYS A 239       6.820  23.581  30.600  1.00 32.53           C  
ATOM   1851  C   LYS A 239       5.391  23.289  31.081  1.00 32.63           C  
ATOM   1852  O   LYS A 239       4.486  24.105  30.891  1.00 33.53           O  
ATOM   1853  CB  LYS A 239       6.887  24.867  29.774  1.00 32.81           C  
ATOM   1854  CG  LYS A 239       8.303  25.338  29.434  1.00 33.92           C  
ATOM   1855  CD  LYS A 239       8.223  26.654  28.684  1.00 38.81           C  
ATOM   1856  CE  LYS A 239       9.600  27.192  28.266  1.00 41.79           C  
ATOM   1857  NZ  LYS A 239      10.407  27.558  29.463  1.00 47.86           N  
ATOM   1858  N   ASP A 240       5.195  22.108  31.678  1.00 33.09           N  
ATOM   1859  CA  ASP A 240       3.880  21.672  32.236  1.00 33.79           C  
ATOM   1860  C   ASP A 240       2.692  21.648  31.262  1.00 34.52           C  
ATOM   1861  O   ASP A 240       1.511  21.730  31.694  1.00 33.55           O  
ATOM   1862  CB  ASP A 240       3.496  22.489  33.477  1.00 33.20           C  
ATOM   1863  CG  ASP A 240       4.540  22.431  34.562  1.00 33.92           C  
ATOM   1864  OD1 ASP A 240       5.017  21.304  34.861  1.00 31.76           O  
ATOM   1865  OD2 ASP A 240       4.864  23.517  35.121  1.00 30.40           O  
ATOM   1866  N   VAL A 241       2.988  21.554  29.958  1.00 34.85           N  
ATOM   1867  CA  VAL A 241       1.969  21.218  28.985  1.00 34.81           C  
ATOM   1868  C   VAL A 241       2.238  19.781  28.517  1.00 35.26           C  
ATOM   1869  O   VAL A 241       3.370  19.415  28.219  1.00 34.53           O  
ATOM   1870  CB  VAL A 241       1.946  22.195  27.795  1.00 35.48           C  
ATOM   1871  CG1 VAL A 241       0.943  21.731  26.737  1.00 35.28           C  
ATOM   1872  CG2 VAL A 241       1.575  23.600  28.264  1.00 34.87           C  
ATOM   1873  N   SER A 242       1.208  18.952  28.524  1.00 36.11           N  
ATOM   1874  CA  SER A 242       1.304  17.664  27.867  1.00 37.74           C  
ATOM   1875  C   SER A 242       0.143  17.463  26.898  1.00 38.23           C  
ATOM   1876  O   SER A 242      -0.858  18.191  26.935  1.00 38.22           O  
ATOM   1877  CB  SER A 242       1.452  16.508  28.859  1.00 37.40           C  
ATOM   1878  OG  SER A 242       0.413  16.499  29.793  1.00 39.29           O  
ATOM   1879  N   GLU A 243       0.312  16.489  26.007  1.00 39.71           N  
ATOM   1880  CA  GLU A 243      -0.726  16.143  25.048  1.00 40.44           C  
ATOM   1881  C   GLU A 243      -1.121  14.729  25.325  1.00 40.38           C  
ATOM   1882  O   GLU A 243      -0.297  13.842  25.242  1.00 40.43           O  
ATOM   1883  CB  GLU A 243      -0.202  16.266  23.632  1.00 41.35           C  
ATOM   1884  CG  GLU A 243       0.207  17.649  23.261  1.00 44.31           C  
ATOM   1885  CD  GLU A 243       0.927  17.677  21.931  1.00 49.11           C  
ATOM   1886  OE1 GLU A 243       0.425  18.383  21.032  1.00 50.98           O  
ATOM   1887  OE2 GLU A 243       1.979  17.004  21.793  1.00 48.78           O  
ATOM   1888  N   ASP A 244      -2.379  14.525  25.689  1.00 40.51           N  
ATOM   1889  CA  ASP A 244      -2.811  13.220  26.106  1.00 41.40           C  
ATOM   1890  C   ASP A 244      -3.220  12.421  24.872  1.00 41.05           C  
ATOM   1891  O   ASP A 244      -4.404  12.299  24.561  1.00 41.33           O  
ATOM   1892  CB  ASP A 244      -3.946  13.328  27.126  1.00 42.27           C  
ATOM   1893  CG  ASP A 244      -4.130  12.054  27.914  1.00 44.32           C  
ATOM   1894  OD1 ASP A 244      -3.319  11.121  27.733  1.00 48.75           O  
ATOM   1895  OD2 ASP A 244      -5.083  11.968  28.711  1.00 48.56           O  
ATOM   1896  N   LEU A 245      -2.216  11.881  24.181  1.00 40.78           N  
ATOM   1897  CA  LEU A 245      -2.383  11.240  22.860  1.00 40.19           C  
ATOM   1898  C   LEU A 245      -2.726   9.768  23.061  1.00 40.56           C  
ATOM   1899  O   LEU A 245      -2.466   9.247  24.140  1.00 41.07           O  
ATOM   1900  CB  LEU A 245      -1.103  11.390  22.028  1.00 39.54           C  
ATOM   1901  CG  LEU A 245      -0.589  12.802  21.728  1.00 38.50           C  
ATOM   1902  CD1 LEU A 245       0.553  12.728  20.760  1.00 36.91           C  
ATOM   1903  CD2 LEU A 245      -1.692  13.686  21.126  1.00 36.99           C  
ATOM   1904  N   PRO A 246      -3.340   9.108  22.052  1.00 40.38           N  
ATOM   1905  CA  PRO A 246      -3.700   7.690  22.196  1.00 40.53           C  
ATOM   1906  C   PRO A 246      -2.484   6.843  22.485  1.00 40.24           C  
ATOM   1907  O   PRO A 246      -1.375   7.198  22.087  1.00 40.07           O  
ATOM   1908  CB  PRO A 246      -4.265   7.316  20.809  1.00 40.45           C  
ATOM   1909  CG  PRO A 246      -4.776   8.646  20.251  1.00 40.80           C  
ATOM   1910  CD  PRO A 246      -3.758   9.653  20.738  1.00 40.54           C  
ATOM   1911  N   LEU A 247      -2.700   5.722  23.161  1.00 40.22           N  
ATOM   1912  CA  LEU A 247      -1.602   4.901  23.624  1.00 40.60           C  
ATOM   1913  C   LEU A 247      -1.360   3.724  22.681  1.00 41.57           C  
ATOM   1914  O   LEU A 247      -2.308   3.103  22.188  1.00 41.76           O  
ATOM   1915  CB  LEU A 247      -1.865   4.410  25.050  1.00 40.40           C  
ATOM   1916  CG  LEU A 247      -2.039   5.455  26.166  1.00 40.04           C  
ATOM   1917  CD1 LEU A 247      -2.791   4.862  27.352  1.00 40.62           C  
ATOM   1918  CD2 LEU A 247      -0.691   5.994  26.605  1.00 37.66           C  
ATOM   1919  N   PRO A 248      -0.085   3.406  22.423  1.00 41.85           N  
ATOM   1920  CA  PRO A 248       0.170   2.265  21.579  1.00 42.23           C  
ATOM   1921  C   PRO A 248      -0.145   0.972  22.336  1.00 42.99           C  
ATOM   1922  O   PRO A 248      -0.197   0.970  23.571  1.00 43.17           O  
ATOM   1923  CB  PRO A 248       1.648   2.401  21.247  1.00 41.93           C  
ATOM   1924  CG  PRO A 248       2.211   3.229  22.309  1.00 42.11           C  
ATOM   1925  CD  PRO A 248       1.147   4.069  22.878  1.00 41.72           C  
ATOM   1926  N   THR A 249      -0.417  -0.099  21.601  1.00 43.49           N  
ATOM   1927  CA  THR A 249      -0.713  -1.400  22.208  1.00 43.78           C  
ATOM   1928  C   THR A 249       0.562  -2.158  22.567  1.00 43.41           C  
ATOM   1929  O   THR A 249       1.567  -2.074  21.859  1.00 44.08           O  
ATOM   1930  CB  THR A 249      -1.676  -2.234  21.324  1.00 44.32           C  
ATOM   1931  OG1 THR A 249      -3.024  -1.790  21.564  1.00 45.70           O  
ATOM   1932  CG2 THR A 249      -1.600  -3.744  21.658  1.00 43.21           C  
ATOM   1933  N   PHE A 250       0.525  -2.861  23.700  1.00 42.92           N  
ATOM   1934  CA  PHE A 250       1.665  -3.634  24.186  1.00 41.34           C  
ATOM   1935  C   PHE A 250       1.283  -5.096  24.344  1.00 42.30           C  
ATOM   1936  O   PHE A 250       0.225  -5.407  24.894  1.00 41.81           O  
ATOM   1937  CB  PHE A 250       2.168  -3.099  25.526  1.00 40.71           C  
ATOM   1938  CG  PHE A 250       3.189  -3.991  26.185  1.00 37.78           C  
ATOM   1939  CD1 PHE A 250       4.512  -3.960  25.783  1.00 36.29           C  
ATOM   1940  CD2 PHE A 250       2.822  -4.876  27.191  1.00 35.34           C  
ATOM   1941  CE1 PHE A 250       5.472  -4.801  26.380  1.00 35.47           C  
ATOM   1942  CE2 PHE A 250       3.761  -5.702  27.790  1.00 33.73           C  
ATOM   1943  CZ  PHE A 250       5.085  -5.676  27.371  1.00 37.17           C  
ATOM   1944  N   SER A 251       2.179  -5.979  23.903  1.00 43.05           N  
ATOM   1945  CA  SER A 251       1.955  -7.418  23.939  1.00 44.44           C  
ATOM   1946  C   SER A 251       2.965  -8.135  24.844  1.00 44.52           C  
ATOM   1947  O   SER A 251       4.137  -8.271  24.489  1.00 44.33           O  
ATOM   1948  CB  SER A 251       2.008  -7.992  22.513  1.00 44.74           C  
ATOM   1949  OG  SER A 251       2.022  -9.417  22.532  1.00 46.34           O  
ATOM   1950  N   PRO A 252       2.508  -8.592  26.021  1.00 45.11           N  
ATOM   1951  CA  PRO A 252       3.303  -9.336  26.999  1.00 45.64           C  
ATOM   1952  C   PRO A 252       4.247 -10.403  26.415  1.00 46.26           C  
ATOM   1953  O   PRO A 252       5.337 -10.585  26.937  1.00 46.42           O  
ATOM   1954  CB  PRO A 252       2.228 -10.002  27.860  1.00 45.22           C  
ATOM   1955  CG  PRO A 252       1.103  -9.060  27.836  1.00 45.00           C  
ATOM   1956  CD  PRO A 252       1.132  -8.370  26.504  1.00 45.16           C  
ATOM   1957  N   THR A 253       3.827 -11.106  25.362  1.00 47.43           N  
ATOM   1958  CA  THR A 253       4.668 -12.130  24.699  1.00 48.93           C  
ATOM   1959  C   THR A 253       5.936 -11.575  24.037  1.00 48.79           C  
ATOM   1960  O   THR A 253       6.872 -12.324  23.762  1.00 49.01           O  
ATOM   1961  CB  THR A 253       3.876 -12.963  23.651  1.00 49.16           C  
ATOM   1962  OG1 THR A 253       3.053 -12.095  22.848  1.00 51.67           O  
ATOM   1963  CG2 THR A 253       2.996 -13.996  24.342  1.00 49.91           C  
ATOM   1964  N   LEU A 254       5.969 -10.267  23.793  1.00 48.91           N  
ATOM   1965  CA  LEU A 254       7.173  -9.614  23.260  1.00 49.27           C  
ATOM   1966  C   LEU A 254       8.401  -9.740  24.171  1.00 49.26           C  
ATOM   1967  O   LEU A 254       9.551  -9.598  23.713  1.00 49.86           O  
ATOM   1968  CB  LEU A 254       6.899  -8.130  23.001  1.00 49.08           C  
ATOM   1969  CG  LEU A 254       6.520  -7.665  21.600  1.00 50.00           C  
ATOM   1970  CD1 LEU A 254       5.878  -8.772  20.756  1.00 50.75           C  
ATOM   1971  CD2 LEU A 254       5.635  -6.389  21.689  1.00 49.26           C  
ATOM   1972  N   LEU A 255       8.158  -9.982  25.461  1.00 48.91           N  
ATOM   1973  CA  LEU A 255       9.230  -9.967  26.454  1.00 48.34           C  
ATOM   1974  C   LEU A 255       9.544 -11.357  26.995  1.00 48.28           C  
ATOM   1975  O   LEU A 255       8.651 -12.190  27.189  1.00 47.79           O  
ATOM   1976  CB  LEU A 255       8.902  -8.991  27.596  1.00 48.31           C  
ATOM   1977  CG  LEU A 255       9.189  -7.485  27.448  1.00 47.86           C  
ATOM   1978  CD1 LEU A 255       8.558  -6.886  26.212  1.00 49.86           C  
ATOM   1979  CD2 LEU A 255       8.701  -6.741  28.670  1.00 48.06           C  
ATOM   1980  N   GLY A 256      10.829 -11.605  27.213  1.00 48.23           N  
ATOM   1981  CA  GLY A 256      11.272 -12.822  27.871  1.00 48.80           C  
ATOM   1982  C   GLY A 256      11.162 -12.566  29.361  1.00 49.20           C  
ATOM   1983  O   GLY A 256      10.738 -11.478  29.774  1.00 49.13           O  
ATOM   1984  N   ASP A 257      11.521 -13.560  30.172  1.00 48.82           N  
ATOM   1985  CA  ASP A 257      11.483 -13.386  31.620  1.00 48.45           C  
ATOM   1986  C   ASP A 257      12.653 -14.079  32.335  1.00 48.23           C  
ATOM   1987  O   ASP A 257      12.497 -14.602  33.448  1.00 48.45           O  
ATOM   1988  CB  ASP A 257      10.121 -13.833  32.176  1.00 48.76           C  
ATOM   1989  CG  ASP A 257       9.899 -15.331  32.047  1.00 48.70           C  
ATOM   1990  OD1 ASP A 257       8.779 -15.787  32.322  1.00 49.40           O  
ATOM   1991  OD2 ASP A 257      10.844 -16.057  31.663  1.00 50.64           O  
ATOM   1992  N   SER A 258      13.819 -14.071  31.694  1.00 47.75           N  
ATOM   1993  CA  SER A 258      15.021 -14.684  32.249  1.00 47.58           C  
ATOM   1994  C   SER A 258      16.022 -13.646  32.753  1.00 46.98           C  
ATOM   1995  O   SER A 258      16.766 -13.906  33.712  1.00 47.31           O  
ATOM   1996  CB  SER A 258      15.675 -15.614  31.218  1.00 48.12           C  
ATOM   1997  OG  SER A 258      15.738 -14.978  29.957  1.00 49.08           O  
ATOM   1998  N   ARG A 259      16.047 -12.470  32.117  1.00 45.49           N  
ATOM   1999  CA  ARG A 259      16.832 -11.354  32.648  1.00 44.38           C  
ATOM   2000  C   ARG A 259      16.090 -10.776  33.841  1.00 43.78           C  
ATOM   2001  O   ARG A 259      14.919 -11.073  34.054  1.00 43.39           O  
ATOM   2002  CB  ARG A 259      17.070 -10.249  31.598  1.00 44.22           C  
ATOM   2003  CG  ARG A 259      17.558 -10.729  30.237  1.00 44.49           C  
ATOM   2004  CD  ARG A 259      18.853 -11.544  30.325  1.00 43.88           C  
ATOM   2005  NE  ARG A 259      19.936 -10.803  30.968  1.00 44.25           N  
ATOM   2006  CZ  ARG A 259      20.674  -9.865  30.382  1.00 45.09           C  
ATOM   2007  NH1 ARG A 259      20.449  -9.530  29.122  1.00 45.84           N  
ATOM   2008  NH2 ARG A 259      21.642  -9.252  31.062  1.00 44.30           N  
ATOM   2009  N   MET A 260      16.767  -9.933  34.603  1.00 42.83           N  
ATOM   2010  CA  MET A 260      16.183  -9.390  35.812  1.00 42.19           C  
ATOM   2011  C   MET A 260      15.236  -8.232  35.546  1.00 42.21           C  
ATOM   2012  O   MET A 260      14.282  -8.025  36.292  1.00 42.40           O  
ATOM   2013  CB  MET A 260      17.291  -8.958  36.765  1.00 42.19           C  
ATOM   2014  CG  MET A 260      17.977 -10.120  37.422  1.00 40.99           C  
ATOM   2015  SD  MET A 260      19.332  -9.608  38.443  1.00 42.19           S  
ATOM   2016  CE  MET A 260      20.247 -11.164  38.487  1.00 42.46           C  
ATOM   2017  N   LEU A 261      15.494  -7.487  34.477  1.00 41.56           N  
ATOM   2018  CA  LEU A 261      14.782  -6.240  34.214  1.00 41.68           C  
ATOM   2019  C   LEU A 261      14.583  -6.042  32.704  1.00 41.85           C  
ATOM   2020  O   LEU A 261      15.544  -6.076  31.960  1.00 41.07           O  
ATOM   2021  CB  LEU A 261      15.627  -5.105  34.776  1.00 41.34           C  
ATOM   2022  CG  LEU A 261      15.018  -3.841  35.371  1.00 43.62           C  
ATOM   2023  CD1 LEU A 261      13.773  -4.171  36.127  1.00 43.67           C  
ATOM   2024  CD2 LEU A 261      16.052  -3.238  36.302  1.00 43.74           C  
ATOM   2025  N   TYR A 262      13.339  -5.871  32.268  1.00 42.83           N  
ATOM   2026  CA  TYR A 262      13.010  -5.539  30.873  1.00 43.30           C  
ATOM   2027  C   TYR A 262      12.276  -4.219  30.822  1.00 43.31           C  
ATOM   2028  O   TYR A 262      11.321  -4.020  31.568  1.00 44.31           O  
ATOM   2029  CB  TYR A 262      12.098  -6.595  30.261  1.00 44.17           C  
ATOM   2030  CG  TYR A 262      12.694  -7.973  30.197  1.00 45.44           C  
ATOM   2031  CD1 TYR A 262      12.600  -8.849  31.282  1.00 46.78           C  
ATOM   2032  CD2 TYR A 262      13.338  -8.412  29.048  1.00 46.76           C  
ATOM   2033  CE1 TYR A 262      13.159 -10.124  31.226  1.00 47.26           C  
ATOM   2034  CE2 TYR A 262      13.890  -9.681  28.974  1.00 47.59           C  
ATOM   2035  CZ  TYR A 262      13.801 -10.530  30.065  1.00 47.29           C  
ATOM   2036  OH  TYR A 262      14.361 -11.782  29.981  1.00 48.07           O  
ATOM   2037  N   PHE A 263      12.711  -3.314  29.956  1.00 42.76           N  
ATOM   2038  CA  PHE A 263      11.975  -2.088  29.686  1.00 42.16           C  
ATOM   2039  C   PHE A 263      11.606  -1.988  28.216  1.00 41.79           C  
ATOM   2040  O   PHE A 263      12.483  -1.937  27.353  1.00 42.80           O  
ATOM   2041  CB  PHE A 263      12.819  -0.871  29.995  1.00 42.27           C  
ATOM   2042  CG  PHE A 263      13.168  -0.713  31.425  1.00 43.19           C  
ATOM   2043  CD1 PHE A 263      14.445  -1.046  31.876  1.00 44.35           C  
ATOM   2044  CD2 PHE A 263      12.253  -0.173  32.318  1.00 43.08           C  
ATOM   2045  CE1 PHE A 263      14.792  -0.872  33.202  1.00 44.65           C  
ATOM   2046  CE2 PHE A 263      12.593   0.003  33.638  1.00 44.17           C  
ATOM   2047  CZ  PHE A 263      13.866  -0.349  34.085  1.00 43.51           C  
ATOM   2048  N   TRP A 264      10.314  -1.931  27.935  1.00 40.39           N  
ATOM   2049  CA  TRP A 264       9.803  -1.815  26.580  1.00 39.07           C  
ATOM   2050  C   TRP A 264       9.355  -0.364  26.379  1.00 38.19           C  
ATOM   2051  O   TRP A 264       8.545   0.121  27.154  1.00 37.27           O  
ATOM   2052  CB  TRP A 264       8.620  -2.763  26.444  1.00 38.78           C  
ATOM   2053  CG  TRP A 264       7.884  -2.705  25.139  1.00 38.50           C  
ATOM   2054  CD1 TRP A 264       8.102  -3.495  24.065  1.00 37.10           C  
ATOM   2055  CD2 TRP A 264       6.786  -1.841  24.790  1.00 37.48           C  
ATOM   2056  NE1 TRP A 264       7.216  -3.182  23.064  1.00 37.30           N  
ATOM   2057  CE2 TRP A 264       6.398  -2.175  23.478  1.00 36.41           C  
ATOM   2058  CE3 TRP A 264       6.088  -0.831  25.461  1.00 35.56           C  
ATOM   2059  CZ2 TRP A 264       5.352  -1.530  22.813  1.00 37.52           C  
ATOM   2060  CZ3 TRP A 264       5.051  -0.194  24.806  1.00 37.35           C  
ATOM   2061  CH2 TRP A 264       4.694  -0.542  23.493  1.00 37.71           C  
ATOM   2062  N   PHE A 265       9.922   0.329  25.380  1.00 37.37           N  
ATOM   2063  CA  PHE A 265       9.542   1.709  25.019  1.00 36.27           C  
ATOM   2064  C   PHE A 265       8.977   1.744  23.615  1.00 36.28           C  
ATOM   2065  O   PHE A 265       9.679   1.404  22.667  1.00 35.90           O  
ATOM   2066  CB  PHE A 265      10.763   2.637  24.994  1.00 36.33           C  
ATOM   2067  CG  PHE A 265      11.438   2.810  26.317  1.00 37.31           C  
ATOM   2068  CD1 PHE A 265      12.364   1.871  26.779  1.00 35.32           C  
ATOM   2069  CD2 PHE A 265      11.177   3.926  27.097  1.00 37.17           C  
ATOM   2070  CE1 PHE A 265      12.992   2.033  28.008  1.00 36.75           C  
ATOM   2071  CE2 PHE A 265      11.828   4.089  28.338  1.00 37.89           C  
ATOM   2072  CZ  PHE A 265      12.723   3.132  28.785  1.00 35.19           C  
ATOM   2073  N   SER A 266       7.739   2.183  23.470  1.00 36.17           N  
ATOM   2074  CA  SER A 266       7.168   2.498  22.154  1.00 36.56           C  
ATOM   2075  C   SER A 266       7.911   3.634  21.437  1.00 36.09           C  
ATOM   2076  O   SER A 266       8.552   4.471  22.074  1.00 35.50           O  
ATOM   2077  CB  SER A 266       5.708   2.874  22.328  1.00 37.24           C  
ATOM   2078  OG  SER A 266       5.095   3.168  21.088  1.00 38.21           O  
ATOM   2079  N   GLU A 267       7.852   3.658  20.103  1.00 35.50           N  
ATOM   2080  CA  GLU A 267       8.545   4.697  19.346  1.00 33.98           C  
ATOM   2081  C   GLU A 267       7.798   6.011  19.500  1.00 33.53           C  
ATOM   2082  O   GLU A 267       8.374   7.074  19.333  1.00 33.86           O  
ATOM   2083  CB  GLU A 267       8.711   4.311  17.863  1.00 34.66           C  
ATOM   2084  CG  GLU A 267       7.435   4.025  17.119  1.00 33.22           C  
ATOM   2085  CD  GLU A 267       7.672   3.753  15.630  1.00 34.52           C  
ATOM   2086  OE1 GLU A 267       8.715   3.182  15.255  1.00 35.94           O  
ATOM   2087  OE2 GLU A 267       6.806   4.108  14.832  1.00 35.50           O  
ATOM   2088  N   ARG A 268       6.522   5.918  19.850  1.00 32.78           N  
ATOM   2089  CA  ARG A 268       5.712   7.073  20.246  1.00 34.64           C  
ATOM   2090  C   ARG A 268       6.310   7.880  21.419  1.00 34.54           C  
ATOM   2091  O   ARG A 268       6.109   9.086  21.494  1.00 35.04           O  
ATOM   2092  CB  ARG A 268       4.277   6.628  20.528  1.00 34.42           C  
ATOM   2093  CG  ARG A 268       3.602   6.120  19.289  1.00 35.79           C  
ATOM   2094  CD  ARG A 268       2.095   6.116  19.405  1.00 41.87           C  
ATOM   2095  NE  ARG A 268       1.546   4.936  18.731  1.00 44.58           N  
ATOM   2096  CZ  ARG A 268       0.275   4.532  18.798  1.00 47.98           C  
ATOM   2097  NH1 ARG A 268      -0.622   5.217  19.515  1.00 46.92           N  
ATOM   2098  NH2 ARG A 268      -0.097   3.420  18.156  1.00 47.70           N  
ATOM   2099  N   VAL A 269       7.105   7.220  22.271  1.00 34.78           N  
ATOM   2100  CA  VAL A 269       7.820   7.870  23.390  1.00 35.05           C  
ATOM   2101  C   VAL A 269       9.002   8.686  22.850  1.00 35.26           C  
ATOM   2102  O   VAL A 269       9.275   9.815  23.289  1.00 36.36           O  
ATOM   2103  CB  VAL A 269       8.286   6.797  24.446  1.00 34.28           C  
ATOM   2104  CG1 VAL A 269       9.009   7.429  25.601  1.00 35.72           C  
ATOM   2105  CG2 VAL A 269       7.115   6.056  24.974  1.00 33.80           C  
ATOM   2106  N   PHE A 270       9.692   8.116  21.871  1.00 36.04           N  
ATOM   2107  CA  PHE A 270      10.745   8.825  21.137  1.00 36.18           C  
ATOM   2108  C   PHE A 270      10.201  10.021  20.359  1.00 35.67           C  
ATOM   2109  O   PHE A 270      10.776  11.112  20.428  1.00 36.11           O  
ATOM   2110  CB  PHE A 270      11.474   7.869  20.199  1.00 37.81           C  
ATOM   2111  CG  PHE A 270      12.287   6.813  20.912  1.00 39.21           C  
ATOM   2112  CD1 PHE A 270      11.691   5.627  21.347  1.00 41.38           C  
ATOM   2113  CD2 PHE A 270      13.645   6.987  21.117  1.00 41.44           C  
ATOM   2114  CE1 PHE A 270      12.429   4.645  21.998  1.00 40.98           C  
ATOM   2115  CE2 PHE A 270      14.396   6.005  21.767  1.00 43.71           C  
ATOM   2116  CZ  PHE A 270      13.782   4.833  22.216  1.00 42.64           C  
ATOM   2117  N   HIS A 271       9.099   9.832  19.632  1.00 35.09           N  
ATOM   2118  CA  HIS A 271       8.387  10.959  19.016  1.00 34.16           C  
ATOM   2119  C   HIS A 271       8.160  12.073  20.059  1.00 34.35           C  
ATOM   2120  O   HIS A 271       8.455  13.248  19.806  1.00 32.95           O  
ATOM   2121  CB  HIS A 271       7.015  10.553  18.424  1.00 34.02           C  
ATOM   2122  CG AHIS A 271       6.346  11.639  17.626  0.50 35.89           C  
ATOM   2123  CG BHIS A 271       7.056   9.468  17.390  0.50 34.07           C  
ATOM   2124  ND1AHIS A 271       5.781  12.757  18.207  0.50 36.78           N  
ATOM   2125  ND1BHIS A 271       5.919   8.811  16.967  0.50 33.44           N  
ATOM   2126  CD2AHIS A 271       6.140  11.769  16.294  0.50 37.02           C  
ATOM   2127  CD2BHIS A 271       8.081   8.931  16.686  0.50 34.40           C  
ATOM   2128  CE1AHIS A 271       5.253  13.523  17.270  0.50 36.95           C  
ATOM   2129  CE1BHIS A 271       6.241   7.918  16.052  0.50 33.41           C  
ATOM   2130  NE2AHIS A 271       5.462  12.949  16.099  0.50 36.50           N  
ATOM   2131  NE2BHIS A 271       7.548   7.971  15.861  0.50 33.46           N  
ATOM   2132  N   SER A 272       7.616  11.695  21.228  1.00 34.74           N  
ATOM   2133  CA  SER A 272       7.354  12.655  22.317  1.00 34.10           C  
ATOM   2134  C   SER A 272       8.609  13.365  22.790  1.00 33.52           C  
ATOM   2135  O   SER A 272       8.598  14.575  22.971  1.00 34.53           O  
ATOM   2136  CB  SER A 272       6.652  11.969  23.494  1.00 34.87           C  
ATOM   2137  OG  SER A 272       6.259  12.916  24.471  1.00 34.29           O  
ATOM   2138  N   LEU A 273       9.700  12.629  22.967  1.00 33.79           N  
ATOM   2139  CA  LEU A 273      10.968  13.234  23.381  1.00 33.79           C  
ATOM   2140  C   LEU A 273      11.601  14.144  22.325  1.00 34.01           C  
ATOM   2141  O   LEU A 273      12.064  15.262  22.640  1.00 35.11           O  
ATOM   2142  CB  LEU A 273      11.978  12.166  23.816  1.00 34.94           C  
ATOM   2143  CG  LEU A 273      13.316  12.696  24.357  1.00 35.40           C  
ATOM   2144  CD1 LEU A 273      13.130  13.707  25.480  1.00 35.57           C  
ATOM   2145  CD2 LEU A 273      14.175  11.547  24.817  1.00 37.02           C  
ATOM   2146  N   ALA A 274      11.639  13.686  21.077  1.00 32.95           N  
ATOM   2147  CA  ALA A 274      12.094  14.550  19.988  1.00 31.89           C  
ATOM   2148  C   ALA A 274      11.268  15.834  19.972  1.00 31.33           C  
ATOM   2149  O   ALA A 274      11.802  16.919  19.797  1.00 31.25           O  
ATOM   2150  CB  ALA A 274      12.004  13.821  18.652  1.00 31.66           C  
ATOM   2151  N   LYS A 275       9.968  15.706  20.197  1.00 31.50           N  
ATOM   2152  CA  LYS A 275       9.044  16.862  20.164  1.00 32.07           C  
ATOM   2153  C   LYS A 275       9.379  17.951  21.197  1.00 32.33           C  
ATOM   2154  O   LYS A 275       9.541  19.146  20.860  1.00 33.43           O  
ATOM   2155  CB  LYS A 275       7.603  16.367  20.346  1.00 31.95           C  
ATOM   2156  CG  LYS A 275       6.508  17.397  20.009  1.00 31.97           C  
ATOM   2157  CD  LYS A 275       5.185  17.102  20.731  1.00 32.15           C  
ATOM   2158  CE  LYS A 275       5.457  16.854  22.241  1.00 34.12           C  
ATOM   2159  NZ  LYS A 275       4.350  17.098  23.208  1.00 30.10           N  
ATOM   2160  N   VAL A 276       9.454  17.561  22.468  1.00 31.88           N  
ATOM   2161  CA  VAL A 276       9.741  18.522  23.547  1.00 30.55           C  
ATOM   2162  C   VAL A 276      11.168  19.040  23.469  1.00 30.94           C  
ATOM   2163  O   VAL A 276      11.402  20.247  23.715  1.00 30.16           O  
ATOM   2164  CB  VAL A 276       9.382  17.969  24.966  1.00 30.30           C  
ATOM   2165  CG1 VAL A 276       7.897  17.595  25.011  1.00 29.37           C  
ATOM   2166  CG2 VAL A 276      10.236  16.746  25.339  1.00 29.95           C  
ATOM   2167  N   ALA A 277      12.104  18.161  23.088  1.00 30.45           N  
ATOM   2168  CA  ALA A 277      13.516  18.552  22.877  1.00 31.46           C  
ATOM   2169  C   ALA A 277      13.692  19.637  21.810  1.00 32.59           C  
ATOM   2170  O   ALA A 277      14.441  20.604  21.994  1.00 33.26           O  
ATOM   2171  CB  ALA A 277      14.344  17.347  22.514  1.00 31.66           C  
ATOM   2172  N   PHE A 278      12.998  19.468  20.692  1.00 32.67           N  
ATOM   2173  CA  PHE A 278      12.991  20.455  19.632  1.00 32.72           C  
ATOM   2174  C   PHE A 278      12.338  21.752  20.082  1.00 33.36           C  
ATOM   2175  O   PHE A 278      12.894  22.834  19.875  1.00 34.18           O  
ATOM   2176  CB  PHE A 278      12.283  19.901  18.392  1.00 31.67           C  
ATOM   2177  CG  PHE A 278      12.092  20.922  17.309  1.00 31.66           C  
ATOM   2178  CD1 PHE A 278      13.162  21.351  16.543  1.00 30.72           C  
ATOM   2179  CD2 PHE A 278      10.841  21.467  17.066  1.00 29.81           C  
ATOM   2180  CE1 PHE A 278      12.977  22.319  15.559  1.00 30.31           C  
ATOM   2181  CE2 PHE A 278      10.660  22.404  16.075  1.00 30.45           C  
ATOM   2182  CZ  PHE A 278      11.730  22.838  15.334  1.00 29.67           C  
ATOM   2183  N   GLN A 279      11.157  21.647  20.685  1.00 33.72           N  
ATOM   2184  CA  GLN A 279      10.514  22.820  21.251  1.00 34.36           C  
ATOM   2185  C   GLN A 279      11.419  23.593  22.241  1.00 34.75           C  
ATOM   2186  O   GLN A 279      11.361  24.814  22.307  1.00 34.29           O  
ATOM   2187  CB  GLN A 279       9.206  22.439  21.910  1.00 33.80           C  
ATOM   2188  CG  GLN A 279       8.206  23.569  21.871  1.00 35.50           C  
ATOM   2189  CD  GLN A 279       7.639  23.820  20.477  1.00 36.07           C  
ATOM   2190  OE1 GLN A 279       7.092  24.878  20.223  1.00 34.17           O  
ATOM   2191  NE2 GLN A 279       7.747  22.825  19.584  1.00 35.83           N  
ATOM   2192  N   ASP A 280      12.281  22.887  22.976  1.00 34.79           N  
ATOM   2193  CA  ASP A 280      13.146  23.556  23.952  1.00 35.31           C  
ATOM   2194  C   ASP A 280      14.383  24.239  23.330  1.00 36.68           C  
ATOM   2195  O   ASP A 280      15.183  24.890  24.041  1.00 37.16           O  
ATOM   2196  CB  ASP A 280      13.547  22.590  25.060  1.00 34.52           C  
ATOM   2197  CG  ASP A 280      14.055  23.298  26.302  1.00 34.01           C  
ATOM   2198  OD1 ASP A 280      15.017  22.763  26.902  1.00 29.21           O  
ATOM   2199  OD2 ASP A 280      13.500  24.379  26.663  1.00 29.53           O  
ATOM   2200  N   GLY A 281      14.530  24.133  22.007  1.00 37.33           N  
ATOM   2201  CA  GLY A 281      15.640  24.789  21.314  1.00 37.31           C  
ATOM   2202  C   GLY A 281      16.956  24.082  21.575  1.00 37.41           C  
ATOM   2203  O   GLY A 281      18.019  24.693  21.496  1.00 38.56           O  
ATOM   2204  N   ARG A 282      16.887  22.798  21.878  1.00 37.29           N  
ATOM   2205  CA  ARG A 282      18.070  22.037  22.310  1.00 37.47           C  
ATOM   2206  C   ARG A 282      18.848  21.403  21.152  1.00 37.90           C  
ATOM   2207  O   ARG A 282      20.043  21.078  21.292  1.00 37.10           O  
ATOM   2208  CB  ARG A 282      17.672  20.920  23.288  1.00 36.82           C  
ATOM   2209  CG  ARG A 282      17.276  21.394  24.681  1.00 37.35           C  
ATOM   2210  CD  ARG A 282      17.121  20.251  25.652  1.00 37.97           C  
ATOM   2211  NE  ARG A 282      16.473  20.695  26.886  1.00 39.17           N  
ATOM   2212  CZ  ARG A 282      16.641  20.123  28.076  1.00 40.00           C  
ATOM   2213  NH1 ARG A 282      17.467  19.093  28.210  1.00 38.56           N  
ATOM   2214  NH2 ARG A 282      15.999  20.601  29.139  1.00 38.19           N  
ATOM   2215  N   LEU A 283      18.160  21.180  20.033  1.00 38.47           N  
ATOM   2216  CA  LEU A 283      18.755  20.449  18.915  1.00 39.33           C  
ATOM   2217  C   LEU A 283      19.553  21.411  18.060  1.00 40.45           C  
ATOM   2218  O   LEU A 283      19.139  21.812  16.955  1.00 39.87           O  
ATOM   2219  CB  LEU A 283      17.688  19.672  18.149  1.00 38.96           C  
ATOM   2220  CG  LEU A 283      16.866  18.772  19.078  1.00 37.88           C  
ATOM   2221  CD1 LEU A 283      15.752  18.109  18.332  1.00 37.43           C  
ATOM   2222  CD2 LEU A 283      17.719  17.740  19.760  1.00 39.63           C  
ATOM   2223  N   MET A 284      20.680  21.824  18.635  1.00 41.41           N  
ATOM   2224  CA  MET A 284      21.586  22.750  17.998  1.00 44.31           C  
ATOM   2225  C   MET A 284      22.985  22.658  18.563  1.00 44.24           C  
ATOM   2226  O   MET A 284      23.204  22.114  19.649  1.00 44.15           O  
ATOM   2227  CB  MET A 284      21.061  24.190  17.998  1.00 43.45           C  
ATOM   2228  CG  MET A 284      20.773  24.804  19.339  1.00 46.10           C  
ATOM   2229  SD  MET A 284      19.964  26.429  19.169  1.00 49.04           S  
ATOM   2230  CE  MET A 284      18.385  26.035  18.370  1.00 51.15           C  
ATOM   2231  N   LEU A 285      23.917  23.194  17.784  1.00 45.04           N  
ATOM   2232  CA  LEU A 285      25.345  23.104  18.022  1.00 45.84           C  
ATOM   2233  C   LEU A 285      25.989  24.339  17.410  1.00 46.15           C  
ATOM   2234  O   LEU A 285      25.523  24.847  16.395  1.00 45.69           O  
ATOM   2235  CB  LEU A 285      25.886  21.846  17.362  1.00 45.77           C  
ATOM   2236  CG  LEU A 285      27.373  21.529  17.250  1.00 46.45           C  
ATOM   2237  CD1 LEU A 285      28.042  21.614  18.599  1.00 49.15           C  
ATOM   2238  CD2 LEU A 285      27.517  20.135  16.717  1.00 46.17           C  
ATOM   2239  N   SER A 286      27.047  24.817  18.053  1.00 47.09           N  
ATOM   2240  CA  SER A 286      27.804  25.978  17.611  1.00 48.34           C  
ATOM   2241  C   SER A 286      29.272  25.681  17.841  1.00 48.79           C  
ATOM   2242  O   SER A 286      29.652  25.221  18.925  1.00 48.85           O  
ATOM   2243  CB  SER A 286      27.406  27.204  18.420  1.00 48.90           C  
ATOM   2244  OG  SER A 286      28.039  28.383  17.940  1.00 51.43           O  
ATOM   2245  N   LEU A 287      30.093  25.906  16.819  1.00 49.20           N  
ATOM   2246  CA  LEU A 287      31.542  25.781  16.959  1.00 50.27           C  
ATOM   2247  C   LEU A 287      32.212  27.079  16.509  1.00 51.74           C  
ATOM   2248  O   LEU A 287      32.017  27.534  15.382  1.00 51.49           O  
ATOM   2249  CB  LEU A 287      32.090  24.604  16.158  1.00 49.40           C  
ATOM   2250  CG  LEU A 287      31.462  23.212  16.244  1.00 49.34           C  
ATOM   2251  CD1 LEU A 287      32.086  22.297  15.189  1.00 49.15           C  
ATOM   2252  CD2 LEU A 287      31.611  22.598  17.625  1.00 49.03           C  
ATOM   2253  N   MET A 288      32.973  27.693  17.406  1.00 53.51           N  
ATOM   2254  CA  MET A 288      33.717  28.899  17.060  1.00 55.34           C  
ATOM   2255  C   MET A 288      35.183  28.558  16.756  1.00 55.65           C  
ATOM   2256  O   MET A 288      35.534  27.386  16.569  1.00 55.94           O  
ATOM   2257  CB  MET A 288      33.552  29.971  18.143  1.00 56.43           C  
ATOM   2258  CG  MET A 288      32.075  30.308  18.414  1.00 58.26           C  
ATOM   2259  SD  MET A 288      31.398  31.474  17.205  1.00 65.51           S  
ATOM   2260  CE  MET A 288      29.948  30.590  16.599  1.00 60.69           C  
ATOM   2261  N   GLY A 289      36.026  29.581  16.678  1.00 55.55           N  
ATOM   2262  CA  GLY A 289      37.392  29.411  16.207  1.00 55.05           C  
ATOM   2263  C   GLY A 289      38.049  28.095  16.540  1.00 54.83           C  
ATOM   2264  O   GLY A 289      38.069  27.170  15.712  1.00 55.01           O  
ATOM   2265  N   ASP A 290      38.583  28.012  17.757  1.00 54.22           N  
ATOM   2266  CA  ASP A 290      39.343  26.844  18.178  1.00 53.66           C  
ATOM   2267  C   ASP A 290      38.534  25.583  18.486  1.00 52.51           C  
ATOM   2268  O   ASP A 290      39.109  24.495  18.509  1.00 52.68           O  
ATOM   2269  CB  ASP A 290      40.320  27.187  19.318  1.00 54.69           C  
ATOM   2270  CG  ASP A 290      41.670  27.714  18.797  1.00 56.90           C  
ATOM   2271  OD1 ASP A 290      42.712  27.381  19.408  1.00 60.30           O  
ATOM   2272  OD2 ASP A 290      41.696  28.445  17.772  1.00 57.31           O  
ATOM   2273  N  AGLU A 291      37.227  25.720  18.724  0.50 51.74           N  
ATOM   2274  N  BGLU A 291      37.228  25.712  18.709  0.50 51.81           N  
ATOM   2275  CA AGLU A 291      36.373  24.533  18.883  0.50 51.03           C  
ATOM   2276  CA BGLU A 291      36.392  24.517  18.882  0.50 51.11           C  
ATOM   2277  C  AGLU A 291      36.222  23.790  17.547  0.50 50.33           C  
ATOM   2278  C  BGLU A 291      36.147  23.784  17.555  0.50 50.41           C  
ATOM   2279  O  AGLU A 291      36.319  22.565  17.510  0.50 49.80           O  
ATOM   2280  O  BGLU A 291      36.107  22.558  17.530  0.50 49.94           O  
ATOM   2281  CB AGLU A 291      35.002  24.835  19.529  0.50 51.06           C  
ATOM   2282  CB BGLU A 291      35.086  24.798  19.646  0.50 51.31           C  
ATOM   2283  CG AGLU A 291      34.078  23.599  19.540  0.50 50.03           C  
ATOM   2284  CG BGLU A 291      34.420  26.125  19.351  0.50 50.77           C  
ATOM   2285  CD AGLU A 291      33.164  23.454  20.760  0.50 49.08           C  
ATOM   2286  CD BGLU A 291      33.311  26.478  20.341  0.50 50.62           C  
ATOM   2287  OE1AGLU A 291      32.240  24.274  20.933  0.50 49.27           O  
ATOM   2288  OE1BGLU A 291      33.303  25.930  21.461  0.50 49.11           O  
ATOM   2289  OE2AGLU A 291      33.334  22.471  21.512  0.50 47.34           O  
ATOM   2290  OE2BGLU A 291      32.446  27.315  19.998  0.50 49.96           O  
ATOM   2291  N   PHE A 292      36.006  24.537  16.466  1.00 49.82           N  
ATOM   2292  CA  PHE A 292      35.990  23.951  15.116  1.00 49.67           C  
ATOM   2293  C   PHE A 292      37.296  23.173  14.850  1.00 48.97           C  
ATOM   2294  O   PHE A 292      37.251  21.986  14.547  1.00 49.63           O  
ATOM   2295  CB  PHE A 292      35.730  25.005  14.034  1.00 49.62           C  
ATOM   2296  CG  PHE A 292      35.934  24.484  12.640  1.00 51.64           C  
ATOM   2297  CD1 PHE A 292      37.126  24.749  11.946  1.00 51.76           C  
ATOM   2298  CD2 PHE A 292      34.962  23.670  12.033  1.00 51.70           C  
ATOM   2299  CE1 PHE A 292      37.328  24.249  10.659  1.00 51.30           C  
ATOM   2300  CE2 PHE A 292      35.151  23.166  10.760  1.00 50.66           C  
ATOM   2301  CZ  PHE A 292      36.338  23.450  10.067  1.00 52.30           C  
ATOM   2302  N   LYS A 293      38.449  23.826  15.025  1.00 48.22           N  
ATOM   2303  CA  LYS A 293      39.760  23.169  14.916  1.00 47.76           C  
ATOM   2304  C   LYS A 293      39.889  21.894  15.750  1.00 47.21           C  
ATOM   2305  O   LYS A 293      40.432  20.883  15.281  1.00 47.44           O  
ATOM   2306  CB  LYS A 293      40.883  24.116  15.356  1.00 47.63           C  
ATOM   2307  CG  LYS A 293      40.986  25.415  14.602  1.00 48.42           C  
ATOM   2308  CD  LYS A 293      42.163  26.257  15.110  1.00 48.33           C  
ATOM   2309  CE  LYS A 293      43.499  25.546  14.953  1.00 50.22           C  
ATOM   2310  NZ  LYS A 293      44.633  26.468  15.296  1.00 51.75           N  
ATOM   2311  N   ALA A 294      39.433  21.964  17.002  1.00 46.61           N  
ATOM   2312  CA  ALA A 294      39.524  20.845  17.940  1.00 46.10           C  
ATOM   2313  C   ALA A 294      38.709  19.648  17.475  1.00 45.66           C  
ATOM   2314  O   ALA A 294      39.140  18.492  17.636  1.00 45.42           O  
ATOM   2315  CB  ALA A 294      39.080  21.281  19.325  1.00 46.22           C  
ATOM   2316  N   VAL A 295      37.531  19.929  16.913  1.00 45.00           N  
ATOM   2317  CA  VAL A 295      36.672  18.895  16.327  1.00 44.28           C  
ATOM   2318  C   VAL A 295      37.362  18.163  15.160  1.00 44.21           C  
ATOM   2319  O   VAL A 295      37.318  16.939  15.078  1.00 43.82           O  
ATOM   2320  CB  VAL A 295      35.263  19.437  15.925  1.00 44.54           C  
ATOM   2321  CG1 VAL A 295      34.516  18.439  15.061  1.00 43.15           C  
ATOM   2322  CG2 VAL A 295      34.418  19.757  17.166  1.00 43.54           C  
ATOM   2323  N   LEU A 296      38.019  18.901  14.274  1.00 44.73           N  
ATOM   2324  CA  LEU A 296      38.730  18.249  13.171  1.00 44.66           C  
ATOM   2325  C   LEU A 296      39.847  17.341  13.698  1.00 45.11           C  
ATOM   2326  O   LEU A 296      39.981  16.202  13.245  1.00 44.98           O  
ATOM   2327  CB  LEU A 296      39.277  19.276  12.186  1.00 44.85           C  
ATOM   2328  CG  LEU A 296      38.310  20.128  11.353  1.00 44.01           C  
ATOM   2329  CD1 LEU A 296      39.150  21.035  10.475  1.00 44.86           C  
ATOM   2330  CD2 LEU A 296      37.399  19.290  10.509  1.00 42.98           C  
ATOM   2331  N   GLU A 297      40.606  17.828  14.684  1.00 45.35           N  
ATOM   2332  CA  GLU A 297      41.694  17.047  15.282  1.00 46.97           C  
ATOM   2333  C   GLU A 297      41.225  15.737  15.935  1.00 46.55           C  
ATOM   2334  O   GLU A 297      41.954  14.749  15.915  1.00 46.76           O  
ATOM   2335  CB  GLU A 297      42.548  17.901  16.238  1.00 47.16           C  
ATOM   2336  CG  GLU A 297      43.401  18.991  15.518  1.00 48.57           C  
ATOM   2337  CD  GLU A 297      44.041  20.046  16.461  1.00 49.76           C  
ATOM   2338  OE1 GLU A 297      44.276  21.200  15.992  1.00 53.60           O  
ATOM   2339  OE2 GLU A 297      44.306  19.740  17.657  1.00 51.46           O  
ATOM   2340  N   THR A 298      40.006  15.728  16.476  1.00 46.31           N  
ATOM   2341  CA  THR A 298      39.417  14.530  17.081  1.00 46.59           C  
ATOM   2342  C   THR A 298      39.213  13.433  16.047  1.00 46.59           C  
ATOM   2343  O   THR A 298      39.390  12.234  16.342  1.00 46.34           O  
ATOM   2344  CB  THR A 298      38.057  14.852  17.739  1.00 46.47           C  
ATOM   2345  OG1 THR A 298      38.266  15.716  18.860  1.00 46.72           O  
ATOM   2346  CG2 THR A 298      37.359  13.593  18.224  1.00 47.65           C  
ATOM   2347  N   TRP A 299      38.835  13.861  14.835  1.00 46.47           N  
ATOM   2348  CA  TRP A 299      38.494  12.944  13.750  1.00 45.50           C  
ATOM   2349  C   TRP A 299      39.654  12.711  12.773  1.00 46.42           C  
ATOM   2350  O   TRP A 299      39.495  12.028  11.759  1.00 46.99           O  
ATOM   2351  CB  TRP A 299      37.186  13.377  13.075  1.00 43.79           C  
ATOM   2352  CG  TRP A 299      36.092  13.322  14.069  1.00 42.03           C  
ATOM   2353  CD1 TRP A 299      35.533  14.374  14.738  1.00 39.12           C  
ATOM   2354  CD2 TRP A 299      35.471  12.135  14.584  1.00 40.07           C  
ATOM   2355  NE1 TRP A 299      34.596  13.916  15.626  1.00 38.03           N  
ATOM   2356  CE2 TRP A 299      34.539  12.546  15.553  1.00 38.14           C  
ATOM   2357  CE3 TRP A 299      35.620  10.756  14.318  1.00 41.59           C  
ATOM   2358  CZ2 TRP A 299      33.741  11.641  16.247  1.00 39.31           C  
ATOM   2359  CZ3 TRP A 299      34.831   9.848  15.015  1.00 40.21           C  
ATOM   2360  CH2 TRP A 299      33.902  10.295  15.968  1.00 40.91           C  
ATOM   2361  N   GLY A 300      40.824  13.251  13.108  1.00 46.80           N  
ATOM   2362  CA  GLY A 300      42.054  12.896  12.414  1.00 47.62           C  
ATOM   2363  C   GLY A 300      42.488  13.873  11.335  1.00 48.66           C  
ATOM   2364  O   GLY A 300      43.353  13.555  10.504  1.00 48.76           O  
ATOM   2365  N   PHE A 301      41.905  15.066  11.356  1.00 48.98           N  
ATOM   2366  CA  PHE A 301      42.242  16.099  10.395  1.00 49.65           C  
ATOM   2367  C   PHE A 301      42.863  17.275  11.116  1.00 50.57           C  
ATOM   2368  O   PHE A 301      42.979  17.268  12.341  1.00 51.20           O  
ATOM   2369  CB  PHE A 301      41.014  16.502   9.572  1.00 48.88           C  
ATOM   2370  CG  PHE A 301      40.318  15.329   8.927  1.00 48.47           C  
ATOM   2371  CD1 PHE A 301      39.124  14.837   9.451  1.00 47.53           C  
ATOM   2372  CD2 PHE A 301      40.881  14.682   7.819  1.00 48.19           C  
ATOM   2373  CE1 PHE A 301      38.490  13.736   8.875  1.00 45.31           C  
ATOM   2374  CE2 PHE A 301      40.248  13.585   7.238  1.00 45.94           C  
ATOM   2375  CZ  PHE A 301      39.058  13.116   7.771  1.00 45.73           C  
ATOM   2376  N   ASN A 302      43.284  18.276  10.355  1.00 51.51           N  
ATOM   2377  CA  ASN A 302      44.065  19.371  10.900  1.00 52.54           C  
ATOM   2378  C   ASN A 302      43.948  20.582   9.999  1.00 52.55           C  
ATOM   2379  O   ASN A 302      44.286  20.545   8.817  1.00 52.64           O  
ATOM   2380  CB  ASN A 302      45.540  18.956  11.068  1.00 52.91           C  
ATOM   2381  CG  ASN A 302      46.352  19.937  11.922  1.00 54.66           C  
ATOM   2382  OD1 ASN A 302      45.932  21.074  12.204  1.00 55.13           O  
ATOM   2383  ND2 ASN A 302      47.548  19.494  12.327  1.00 57.39           N  
ATOM   2384  N   THR A 303      43.456  21.657  10.585  1.00 52.47           N  
ATOM   2385  CA  THR A 303      43.302  22.913   9.904  1.00 52.56           C  
ATOM   2386  C   THR A 303      44.563  23.391   9.117  1.00 52.36           C  
ATOM   2387  O   THR A 303      44.447  24.183   8.184  1.00 52.06           O  
ATOM   2388  CB  THR A 303      42.796  23.961  10.920  1.00 52.53           C  
ATOM   2389  OG1 THR A 303      41.986  24.934  10.254  1.00 53.85           O  
ATOM   2390  CG2 THR A 303      43.950  24.624  11.661  1.00 53.25           C  
ATOM   2391  N   ASN A 304      45.757  22.906   9.469  1.00 52.35           N  
ATOM   2392  CA  ASN A 304      46.974  23.333   8.750  1.00 52.22           C  
ATOM   2393  C   ASN A 304      47.234  22.521   7.490  1.00 51.29           C  
ATOM   2394  O   ASN A 304      48.133  22.847   6.722  1.00 51.03           O  
ATOM   2395  CB  ASN A 304      48.218  23.341   9.648  1.00 52.45           C  
ATOM   2396  CG  ASN A 304      48.830  21.961   9.809  1.00 55.30           C  
ATOM   2397  OD1 ASN A 304      48.112  20.955   9.916  1.00 57.68           O  
ATOM   2398  ND2 ASN A 304      50.168  21.899   9.819  1.00 57.25           N  
ATOM   2399  N   GLN A 305      46.442  21.471   7.288  1.00 50.42           N  
ATOM   2400  CA  GLN A 305      46.553  20.636   6.091  1.00 50.46           C  
ATOM   2401  C   GLN A 305      46.260  21.415   4.820  1.00 49.42           C  
ATOM   2402  O   GLN A 305      45.445  22.345   4.819  1.00 49.28           O  
ATOM   2403  CB  GLN A 305      45.626  19.424   6.174  1.00 50.55           C  
ATOM   2404  CG  GLN A 305      46.238  18.223   6.878  1.00 52.76           C  
ATOM   2405  CD  GLN A 305      45.200  17.173   7.208  1.00 54.42           C  
ATOM   2406  OE1 GLN A 305      44.383  17.362   8.104  1.00 54.52           O  
ATOM   2407  NE2 GLN A 305      45.213  16.067   6.468  1.00 55.67           N  
ATOM   2408  N   GLU A 306      46.942  21.025   3.749  1.00 48.70           N  
ATOM   2409  CA  GLU A 306      46.771  21.618   2.421  1.00 48.12           C  
ATOM   2410  C   GLU A 306      45.300  21.617   1.955  1.00 47.31           C  
ATOM   2411  O   GLU A 306      44.787  22.643   1.505  1.00 47.37           O  
ATOM   2412  CB  GLU A 306      47.665  20.884   1.412  1.00 48.41           C  
ATOM   2413  CG  GLU A 306      47.849  21.598   0.072  1.00 49.82           C  
ATOM   2414  CD  GLU A 306      46.643  21.455  -0.843  1.00 51.11           C  
ATOM   2415  OE1 GLU A 306      46.167  20.308  -1.033  1.00 49.90           O  
ATOM   2416  OE2 GLU A 306      46.167  22.499  -1.353  1.00 52.09           O  
ATOM   2417  N   ILE A 307      44.637  20.471   2.087  1.00 46.34           N  
ATOM   2418  CA  ILE A 307      43.243  20.293   1.646  1.00 45.88           C  
ATOM   2419  C   ILE A 307      42.194  21.190   2.307  1.00 45.87           C  
ATOM   2420  O   ILE A 307      41.087  21.336   1.771  1.00 45.36           O  
ATOM   2421  CB  ILE A 307      42.797  18.822   1.773  1.00 45.82           C  
ATOM   2422  CG1 ILE A 307      42.892  18.336   3.234  1.00 46.09           C  
ATOM   2423  CG2 ILE A 307      43.619  17.946   0.815  1.00 44.68           C  
ATOM   2424  CD1 ILE A 307      42.454  16.858   3.445  1.00 45.50           C  
ATOM   2425  N   PHE A 308      42.538  21.779   3.460  1.00 45.46           N  
ATOM   2426  CA  PHE A 308      41.647  22.702   4.164  1.00 45.11           C  
ATOM   2427  C   PHE A 308      41.920  24.138   3.773  1.00 45.77           C  
ATOM   2428  O   PHE A 308      41.112  25.020   4.053  1.00 44.95           O  
ATOM   2429  CB  PHE A 308      41.762  22.537   5.692  1.00 44.30           C  
ATOM   2430  CG  PHE A 308      41.210  21.224   6.197  1.00 44.14           C  
ATOM   2431  CD1 PHE A 308      42.020  20.092   6.275  1.00 44.12           C  
ATOM   2432  CD2 PHE A 308      39.881  21.114   6.566  1.00 41.61           C  
ATOM   2433  CE1 PHE A 308      41.502  18.867   6.712  1.00 44.45           C  
ATOM   2434  CE2 PHE A 308      39.359  19.904   7.000  1.00 43.77           C  
ATOM   2435  CZ  PHE A 308      40.170  18.777   7.083  1.00 43.29           C  
ATOM   2436  N   GLN A 309      43.059  24.373   3.125  1.00 46.74           N  
ATOM   2437  CA  GLN A 309      43.521  25.745   2.927  1.00 48.24           C  
ATOM   2438  C   GLN A 309      42.578  26.647   2.126  1.00 48.97           C  
ATOM   2439  O   GLN A 309      42.389  27.808   2.504  1.00 48.59           O  
ATOM   2440  CB  GLN A 309      44.959  25.802   2.397  1.00 48.18           C  
ATOM   2441  CG  GLN A 309      46.020  25.276   3.381  1.00 48.97           C  
ATOM   2442  CD  GLN A 309      45.920  25.891   4.791  1.00 48.95           C  
ATOM   2443  OE1 GLN A 309      46.155  27.091   4.986  1.00 51.36           O  
ATOM   2444  NE2 GLN A 309      45.572  25.062   5.771  1.00 46.49           N  
ATOM   2445  N   GLU A 310      41.966  26.140   1.051  1.00 50.07           N  
ATOM   2446  CA  GLU A 310      41.104  27.039   0.248  1.00 51.60           C  
ATOM   2447  C   GLU A 310      39.787  27.398   0.967  1.00 51.84           C  
ATOM   2448  O   GLU A 310      39.251  28.507   0.828  1.00 51.60           O  
ATOM   2449  CB  GLU A 310      40.905  26.544  -1.199  1.00 51.43           C  
ATOM   2450  CG  GLU A 310      39.646  25.737  -1.489  1.00 52.76           C  
ATOM   2451  CD  GLU A 310      39.458  25.467  -2.991  1.00 52.63           C  
ATOM   2452  OE1 GLU A 310      39.378  26.442  -3.782  1.00 51.77           O  
ATOM   2453  OE2 GLU A 310      39.401  24.271  -3.366  1.00 54.28           O  
ATOM   2454  N   VAL A 311      39.293  26.463   1.766  1.00 52.62           N  
ATOM   2455  CA  VAL A 311      38.092  26.709   2.546  1.00 53.32           C  
ATOM   2456  C   VAL A 311      38.359  27.578   3.801  1.00 53.89           C  
ATOM   2457  O   VAL A 311      37.776  28.672   3.910  1.00 53.43           O  
ATOM   2458  CB  VAL A 311      37.342  25.385   2.843  1.00 53.47           C  
ATOM   2459  CG1 VAL A 311      36.218  25.599   3.808  1.00 53.43           C  
ATOM   2460  CG2 VAL A 311      36.796  24.794   1.540  1.00 53.71           C  
ATOM   2461  N   VAL A 312      39.252  27.154   4.712  1.00 54.40           N  
ATOM   2462  CA  VAL A 312      39.269  27.799   6.064  1.00 55.39           C  
ATOM   2463  C   VAL A 312      39.739  29.275   6.230  1.00 56.13           C  
ATOM   2464  O   VAL A 312      39.053  30.036   6.902  1.00 57.00           O  
ATOM   2465  CB  VAL A 312      39.673  26.846   7.264  1.00 55.03           C  
ATOM   2466  CG1 VAL A 312      39.122  25.436   7.054  1.00 54.93           C  
ATOM   2467  CG2 VAL A 312      41.159  26.814   7.517  1.00 55.54           C  
ATOM   2468  N   GLY A 313      40.863  29.736   5.688  1.00 56.77           N  
ATOM   2469  CA  GLY A 313      42.007  28.976   5.263  1.00 57.22           C  
ATOM   2470  C   GLY A 313      43.120  29.587   6.096  1.00 57.47           C  
ATOM   2471  O   GLY A 313      43.845  28.871   6.789  1.00 57.77           O  
ATOM   2472  N   GLY A 314      43.207  30.919   6.065  1.00 57.49           N  
ATOM   2473  CA  GLY A 314      44.263  31.675   6.767  1.00 57.70           C  
ATOM   2474  C   GLY A 314      44.042  31.936   8.255  1.00 57.54           C  
ATOM   2475  O   GLY A 314      45.000  31.941   9.044  1.00 57.49           O  
ATOM   2476  N   PHE A 315      42.780  32.148   8.638  1.00 57.30           N  
ATOM   2477  CA  PHE A 315      42.414  32.469  10.025  1.00 57.01           C  
ATOM   2478  C   PHE A 315      41.490  31.419  10.655  1.00 56.74           C  
ATOM   2479  O   PHE A 315      40.342  31.733  10.981  1.00 55.90           O  
ATOM   2480  CB  PHE A 315      41.760  33.854  10.097  1.00 57.18           C  
ATOM   2481  CG  PHE A 315      42.677  34.979   9.712  1.00 57.65           C  
ATOM   2482  CD1 PHE A 315      42.980  35.226   8.368  1.00 57.86           C  
ATOM   2483  CD2 PHE A 315      43.237  35.798  10.695  1.00 58.62           C  
ATOM   2484  CE1 PHE A 315      43.837  36.270   8.004  1.00 58.62           C  
ATOM   2485  CE2 PHE A 315      44.096  36.856  10.350  1.00 58.86           C  
ATOM   2486  CZ  PHE A 315      44.396  37.094   8.998  1.00 58.86           C  
ATOM   2487  N   PRO A 316      41.999  30.178  10.848  1.00 56.82           N  
ATOM   2488  CA  PRO A 316      41.173  29.059  11.331  1.00 57.20           C  
ATOM   2489  C   PRO A 316      40.635  29.236  12.765  1.00 57.56           C  
ATOM   2490  O   PRO A 316      39.709  28.520  13.170  1.00 57.80           O  
ATOM   2491  CB  PRO A 316      42.129  27.862  11.260  1.00 56.98           C  
ATOM   2492  CG  PRO A 316      43.478  28.442  11.358  1.00 56.66           C  
ATOM   2493  CD  PRO A 316      43.398  29.752  10.638  1.00 56.98           C  
ATOM   2494  N   SER A 317      41.214  30.181  13.503  1.00 57.63           N  
ATOM   2495  CA  SER A 317      40.736  30.552  14.830  1.00 58.07           C  
ATOM   2496  C   SER A 317      39.526  31.472  14.788  1.00 57.78           C  
ATOM   2497  O   SER A 317      39.051  31.929  15.833  1.00 57.96           O  
ATOM   2498  CB  SER A 317      41.852  31.217  15.637  1.00 58.16           C  
ATOM   2499  OG  SER A 317      42.674  30.238  16.247  1.00 59.69           O  
ATOM   2500  N   GLN A 318      39.017  31.740  13.591  1.00 57.50           N  
ATOM   2501  CA  GLN A 318      37.851  32.608  13.456  1.00 57.31           C  
ATOM   2502  C   GLN A 318      36.689  31.957  12.704  1.00 56.51           C  
ATOM   2503  O   GLN A 318      35.687  32.613  12.393  1.00 56.67           O  
ATOM   2504  CB  GLN A 318      38.263  33.934  12.846  1.00 57.62           C  
ATOM   2505  CG  GLN A 318      38.923  34.835  13.866  1.00 60.36           C  
ATOM   2506  CD  GLN A 318      39.733  35.923  13.221  1.00 64.24           C  
ATOM   2507  OE1 GLN A 318      39.176  36.887  12.670  1.00 65.25           O  
ATOM   2508  NE2 GLN A 318      41.067  35.778  13.270  1.00 64.33           N  
ATOM   2509  N   ALA A 319      36.844  30.657  12.453  1.00 55.48           N  
ATOM   2510  CA  ALA A 319      35.842  29.810  11.826  1.00 54.42           C  
ATOM   2511  C   ALA A 319      34.577  29.743  12.667  1.00 53.72           C  
ATOM   2512  O   ALA A 319      34.638  29.732  13.896  1.00 53.97           O  
ATOM   2513  CB  ALA A 319      36.405  28.418  11.628  1.00 54.39           C  
ATOM   2514  N   GLN A 320      33.432  29.702  11.996  1.00 52.58           N  
ATOM   2515  CA  GLN A 320      32.140  29.584  12.663  1.00 51.31           C  
ATOM   2516  C   GLN A 320      31.265  28.568  11.955  1.00 50.39           C  
ATOM   2517  O   GLN A 320      30.982  28.727  10.770  1.00 50.64           O  
ATOM   2518  CB  GLN A 320      31.421  30.929  12.665  1.00 51.19           C  
ATOM   2519  CG  GLN A 320      32.086  31.986  13.526  1.00 52.14           C  
ATOM   2520  CD  GLN A 320      31.460  33.345  13.359  1.00 53.73           C  
ATOM   2521  OE1 GLN A 320      30.236  33.481  13.325  1.00 55.06           O  
ATOM   2522  NE2 GLN A 320      32.295  34.365  13.247  1.00 54.46           N  
ATOM   2523  N   VAL A 321      30.831  27.535  12.674  1.00 48.33           N  
ATOM   2524  CA  VAL A 321      29.817  26.629  12.145  1.00 46.46           C  
ATOM   2525  C   VAL A 321      28.665  26.393  13.126  1.00 45.75           C  
ATOM   2526  O   VAL A 321      28.893  26.113  14.307  1.00 45.55           O  
ATOM   2527  CB  VAL A 321      30.422  25.312  11.612  1.00 46.38           C  
ATOM   2528  CG1 VAL A 321      31.643  24.931  12.381  1.00 47.01           C  
ATOM   2529  CG2 VAL A 321      29.402  24.196  11.606  1.00 45.41           C  
ATOM   2530  N   THR A 322      27.437  26.531  12.631  1.00 44.16           N  
ATOM   2531  CA  THR A 322      26.261  26.202  13.394  1.00 43.55           C  
ATOM   2532  C   THR A 322      25.433  25.135  12.691  1.00 43.64           C  
ATOM   2533  O   THR A 322      25.293  25.151  11.465  1.00 43.47           O  
ATOM   2534  CB  THR A 322      25.361  27.433  13.639  1.00 43.80           C  
ATOM   2535  OG1 THR A 322      24.749  27.845  12.409  1.00 43.24           O  
ATOM   2536  CG2 THR A 322      26.164  28.589  14.237  1.00 42.74           C  
ATOM   2537  N   VAL A 323      24.883  24.216  13.481  1.00 42.72           N  
ATOM   2538  CA  VAL A 323      23.855  23.291  13.029  1.00 42.31           C  
ATOM   2539  C   VAL A 323      22.615  23.548  13.858  1.00 42.44           C  
ATOM   2540  O   VAL A 323      22.714  23.765  15.071  1.00 42.39           O  
ATOM   2541  CB  VAL A 323      24.229  21.841  13.331  1.00 42.34           C  
ATOM   2542  CG1 VAL A 323      23.482  20.886  12.407  1.00 41.39           C  
ATOM   2543  CG2 VAL A 323      25.714  21.648  13.249  1.00 43.15           C  
ATOM   2544  N   HIS A 324      21.450  23.526  13.228  1.00 41.50           N  
ATOM   2545  CA  HIS A 324      20.222  23.406  13.989  1.00 41.26           C  
ATOM   2546  C   HIS A 324      19.143  22.730  13.185  1.00 40.49           C  
ATOM   2547  O   HIS A 324      19.085  22.879  11.950  1.00 39.89           O  
ATOM   2548  CB  HIS A 324      19.752  24.754  14.557  1.00 42.07           C  
ATOM   2549  CG  HIS A 324      19.197  25.701  13.540  1.00 43.85           C  
ATOM   2550  ND1 HIS A 324      19.955  26.694  12.957  1.00 45.85           N  
ATOM   2551  CD2 HIS A 324      17.946  25.840  13.039  1.00 46.35           C  
ATOM   2552  CE1 HIS A 324      19.201  27.386  12.119  1.00 47.63           C  
ATOM   2553  NE2 HIS A 324      17.976  26.892  12.154  1.00 48.01           N  
ATOM   2554  N   CYS A 325      18.329  21.948  13.889  1.00 39.01           N  
ATOM   2555  CA  CYS A 325      17.127  21.356  13.338  1.00 38.38           C  
ATOM   2556  C   CYS A 325      16.139  22.415  12.896  1.00 37.88           C  
ATOM   2557  O   CYS A 325      15.916  23.373  13.609  1.00 37.05           O  
ATOM   2558  CB  CYS A 325      16.458  20.468  14.366  1.00 37.63           C  
ATOM   2559  SG  CYS A 325      17.112  18.841  14.406  1.00 40.36           S  
ATOM   2560  N   LEU A 326      15.527  22.196  11.728  1.00 38.23           N  
ATOM   2561  CA  LEU A 326      14.561  23.121  11.125  1.00 37.75           C  
ATOM   2562  C   LEU A 326      13.133  22.758  11.514  1.00 37.93           C  
ATOM   2563  O   LEU A 326      12.255  23.608  11.573  1.00 38.12           O  
ATOM   2564  CB  LEU A 326      14.719  23.112   9.582  1.00 37.47           C  
ATOM   2565  CG  LEU A 326      15.980  23.759   8.995  1.00 35.94           C  
ATOM   2566  CD1 LEU A 326      16.189  23.418   7.517  1.00 38.38           C  
ATOM   2567  CD2 LEU A 326      15.955  25.247   9.169  1.00 37.18           C  
ATOM   2568  N   LYS A 327      12.900  21.473  11.732  1.00 38.22           N  
ATOM   2569  CA  LYS A 327      11.673  20.997  12.315  1.00 38.88           C  
ATOM   2570  C   LYS A 327      12.031  19.821  13.226  1.00 39.04           C  
ATOM   2571  O   LYS A 327      13.159  19.402  13.276  1.00 38.75           O  
ATOM   2572  CB  LYS A 327      10.675  20.575  11.233  1.00 39.38           C  
ATOM   2573  CG  LYS A 327      11.152  19.428  10.367  1.00 40.19           C  
ATOM   2574  CD  LYS A 327      10.408  19.373   9.061  1.00 41.58           C  
ATOM   2575  CE  LYS A 327      10.128  17.919   8.734  1.00 44.53           C  
ATOM   2576  NZ  LYS A 327       9.977  17.667   7.266  1.00 47.04           N  
ATOM   2577  N   MET A 328      11.048  19.290  13.927  1.00 38.75           N  
ATOM   2578  CA  MET A 328      11.260  18.196  14.847  1.00 39.10           C  
ATOM   2579  C   MET A 328      11.804  16.969  14.126  1.00 39.32           C  
ATOM   2580  O   MET A 328      11.248  16.569  13.095  1.00 39.83           O  
ATOM   2581  CB  MET A 328       9.901  17.888  15.449  1.00 39.03           C  
ATOM   2582  CG  MET A 328       9.824  16.767  16.374  1.00 39.44           C  
ATOM   2583  SD  MET A 328       8.090  16.352  16.534  1.00 38.60           S  
ATOM   2584  CE  MET A 328       8.366  14.638  16.865  1.00 37.85           C  
ATOM   2585  N   PRO A 329      12.875  16.347  14.658  1.00 39.47           N  
ATOM   2586  CA  PRO A 329      13.335  15.099  14.057  1.00 39.13           C  
ATOM   2587  C   PRO A 329      12.283  14.011  14.155  1.00 39.76           C  
ATOM   2588  O   PRO A 329      11.436  14.025  15.065  1.00 39.40           O  
ATOM   2589  CB  PRO A 329      14.554  14.726  14.902  1.00 39.23           C  
ATOM   2590  CG  PRO A 329      14.993  16.033  15.526  1.00 39.24           C  
ATOM   2591  CD  PRO A 329      13.721  16.736  15.804  1.00 39.67           C  
ATOM   2592  N   LYS A 330      12.351  13.071  13.214  1.00 39.74           N  
ATOM   2593  CA  LYS A 330      11.374  12.022  13.064  1.00 40.18           C  
ATOM   2594  C   LYS A 330      12.061  10.727  13.440  1.00 39.47           C  
ATOM   2595  O   LYS A 330      12.980  10.289  12.739  1.00 39.59           O  
ATOM   2596  CB  LYS A 330      10.932  11.973  11.613  1.00 40.86           C  
ATOM   2597  CG  LYS A 330       9.453  11.869  11.395  1.00 44.01           C  
ATOM   2598  CD  LYS A 330       9.073  12.554  10.083  1.00 50.09           C  
ATOM   2599  CE  LYS A 330       9.508  14.042  10.064  1.00 50.88           C  
ATOM   2600  NZ  LYS A 330       9.499  14.601   8.679  1.00 51.50           N  
ATOM   2601  N   ILE A 331      11.634  10.118  14.548  1.00 38.50           N  
ATOM   2602  CA  ILE A 331      12.303   8.920  15.058  1.00 38.17           C  
ATOM   2603  C   ILE A 331      11.396   7.697  14.955  1.00 38.65           C  
ATOM   2604  O   ILE A 331      10.228   7.753  15.357  1.00 38.89           O  
ATOM   2605  CB  ILE A 331      12.803   9.111  16.519  1.00 38.45           C  
ATOM   2606  CG1 ILE A 331      13.651  10.378  16.632  1.00 37.94           C  
ATOM   2607  CG2 ILE A 331      13.564   7.880  17.005  1.00 36.40           C  
ATOM   2608  CD1 ILE A 331      14.469  10.447  17.907  1.00 41.67           C  
ATOM   2609  N   SER A 332      11.939   6.625  14.374  1.00 38.50           N  
ATOM   2610  CA  SER A 332      11.280   5.319  14.232  1.00 38.73           C  
ATOM   2611  C   SER A 332      12.211   4.298  14.811  1.00 38.77           C  
ATOM   2612  O   SER A 332      13.426   4.444  14.703  1.00 39.45           O  
ATOM   2613  CB  SER A 332      11.160   4.893  12.759  1.00 38.51           C  
ATOM   2614  OG  SER A 332      10.779   5.959  11.938  1.00 38.82           O  
ATOM   2615  N   CYS A 333      11.640   3.246  15.372  1.00 38.60           N  
ATOM   2616  CA  CYS A 333      12.385   2.054  15.700  1.00 38.50           C  
ATOM   2617  C   CYS A 333      12.078   1.028  14.636  1.00 39.03           C  
ATOM   2618  O   CYS A 333      10.935   0.900  14.198  1.00 38.45           O  
ATOM   2619  CB  CYS A 333      11.988   1.503  17.078  1.00 39.10           C  
ATOM   2620  SG  CYS A 333      12.282   2.658  18.447  1.00 38.09           S  
ATOM   2621  N   GLN A 334      13.111   0.291  14.249  1.00 39.37           N  
ATOM   2622  CA  GLN A 334      13.023  -0.749  13.242  1.00 40.91           C  
ATOM   2623  C   GLN A 334      13.906  -1.873  13.715  1.00 40.38           C  
ATOM   2624  O   GLN A 334      14.741  -1.645  14.570  1.00 39.91           O  
ATOM   2625  CB  GLN A 334      13.524  -0.214  11.887  1.00 40.87           C  
ATOM   2626  CG  GLN A 334      12.480  -0.237  10.791  1.00 45.23           C  
ATOM   2627  CD  GLN A 334      11.744   1.071  10.660  1.00 50.08           C  
ATOM   2628  OE1 GLN A 334      12.332   2.081  10.278  1.00 54.15           O  
ATOM   2629  NE2 GLN A 334      10.443   1.061  10.944  1.00 49.45           N  
ATOM   2630  N   ASN A 335      13.726  -3.078  13.169  1.00 40.97           N  
ATOM   2631  CA  ASN A 335      14.602  -4.210  13.477  1.00 41.32           C  
ATOM   2632  C   ASN A 335      16.069  -3.853  13.293  1.00 41.20           C  
ATOM   2633  O   ASN A 335      16.910  -4.274  14.079  1.00 41.60           O  
ATOM   2634  CB  ASN A 335      14.276  -5.429  12.600  1.00 42.42           C  
ATOM   2635  CG  ASN A 335      13.020  -6.180  13.046  1.00 45.19           C  
ATOM   2636  OD1 ASN A 335      12.377  -5.831  14.036  1.00 48.47           O  
ATOM   2637  ND2 ASN A 335      12.668  -7.226  12.305  1.00 46.70           N  
ATOM   2638  N   LYS A 336      16.375  -3.077  12.254  1.00 40.61           N  
ATOM   2639  CA  LYS A 336      17.764  -2.762  11.889  1.00 40.18           C  
ATOM   2640  C   LYS A 336      18.436  -1.738  12.811  1.00 38.89           C  
ATOM   2641  O   LYS A 336      19.658  -1.687  12.919  1.00 39.40           O  
ATOM   2642  CB  LYS A 336      17.843  -2.281  10.428  1.00 40.10           C  
ATOM   2643  CG  LYS A 336      17.087  -0.988  10.153  1.00 40.90           C  
ATOM   2644  CD  LYS A 336      17.287  -0.509   8.709  1.00 41.31           C  
ATOM   2645  CE  LYS A 336      16.401   0.698   8.444  1.00 43.97           C  
ATOM   2646  NZ  LYS A 336      16.897   1.563   7.321  1.00 48.00           N  
ATOM   2647  N   GLY A 337      17.636  -0.911  13.467  1.00 38.00           N  
ATOM   2648  CA  GLY A 337      18.164   0.150  14.300  1.00 35.36           C  
ATOM   2649  C   GLY A 337      17.083   1.152  14.597  1.00 34.80           C  
ATOM   2650  O   GLY A 337      15.908   0.926  14.264  1.00 34.41           O  
ATOM   2651  N   VAL A 338      17.492   2.262  15.217  1.00 32.99           N  
ATOM   2652  CA  VAL A 338      16.630   3.388  15.454  1.00 31.98           C  
ATOM   2653  C   VAL A 338      16.945   4.369  14.331  1.00 31.79           C  
ATOM   2654  O   VAL A 338      18.122   4.743  14.142  1.00 30.40           O  
ATOM   2655  CB  VAL A 338      16.907   4.095  16.840  1.00 32.12           C  
ATOM   2656  CG1 VAL A 338      16.206   5.433  16.906  1.00 30.76           C  
ATOM   2657  CG2 VAL A 338      16.472   3.216  18.028  1.00 29.95           C  
ATOM   2658  N   VAL A 339      15.904   4.780  13.590  1.00 30.37           N  
ATOM   2659  CA  VAL A 339      16.137   5.695  12.491  1.00 29.38           C  
ATOM   2660  C   VAL A 339      15.652   7.095  12.817  1.00 29.20           C  
ATOM   2661  O   VAL A 339      14.546   7.288  13.260  1.00 27.54           O  
ATOM   2662  CB  VAL A 339      15.833   5.125  11.043  1.00 29.86           C  
ATOM   2663  CG1 VAL A 339      15.096   3.792  11.046  1.00 27.76           C  
ATOM   2664  CG2 VAL A 339      15.272   6.199  10.055  1.00 29.02           C  
ATOM   2665  N   VAL A 340      16.570   8.039  12.689  1.00 29.52           N  
ATOM   2666  CA  VAL A 340      16.289   9.412  12.972  1.00 30.07           C  
ATOM   2667  C   VAL A 340      16.395  10.149  11.636  1.00 32.01           C  
ATOM   2668  O   VAL A 340      17.458  10.202  11.006  1.00 32.92           O  
ATOM   2669  CB  VAL A 340      17.296  10.041  13.961  1.00 29.63           C  
ATOM   2670  CG1 VAL A 340      16.869  11.511  14.264  1.00 28.97           C  
ATOM   2671  CG2 VAL A 340      17.427   9.222  15.262  1.00 28.85           C  
ATOM   2672  N   ASP A 341      15.309  10.787  11.257  1.00 32.80           N  
ATOM   2673  CA  ASP A 341      15.258  11.521  10.048  1.00 33.65           C  
ATOM   2674  C   ASP A 341      15.176  12.969  10.457  1.00 33.93           C  
ATOM   2675  O   ASP A 341      14.135  13.409  10.946  1.00 33.60           O  
ATOM   2676  CB  ASP A 341      14.015  11.063   9.277  1.00 34.29           C  
ATOM   2677  CG  ASP A 341      13.737  11.893   8.045  1.00 36.41           C  
ATOM   2678  OD1 ASP A 341      14.585  12.749   7.651  1.00 34.76           O  
ATOM   2679  OD2 ASP A 341      12.642  11.677   7.465  1.00 40.46           O  
ATOM   2680  N   SER A 342      16.283  13.691  10.261  1.00 34.39           N  
ATOM   2681  CA  SER A 342      16.447  15.084  10.702  1.00 35.32           C  
ATOM   2682  C   SER A 342      16.556  16.045   9.535  1.00 36.16           C  
ATOM   2683  O   SER A 342      17.336  15.818   8.620  1.00 36.42           O  
ATOM   2684  CB  SER A 342      17.740  15.264  11.517  1.00 35.24           C  
ATOM   2685  OG  SER A 342      17.925  14.240  12.479  1.00 35.14           O  
ATOM   2686  N   SER A 343      15.829  17.150   9.615  1.00 36.29           N  
ATOM   2687  CA  SER A 343      15.987  18.249   8.699  1.00 37.10           C  
ATOM   2688  C   SER A 343      16.814  19.360   9.349  1.00 37.49           C  
ATOM   2689  O   SER A 343      16.351  20.019  10.303  1.00 38.08           O  
ATOM   2690  CB  SER A 343      14.604  18.770   8.305  1.00 37.13           C  
ATOM   2691  OG  SER A 343      14.709  19.852   7.409  1.00 38.62           O  
ATOM   2692  N   VAL A 344      18.030  19.579   8.839  1.00 37.00           N  
ATOM   2693  CA  VAL A 344      18.956  20.517   9.467  1.00 36.37           C  
ATOM   2694  C   VAL A 344      19.361  21.669   8.582  1.00 37.16           C  
ATOM   2695  O   VAL A 344      19.235  21.608   7.353  1.00 37.56           O  
ATOM   2696  CB  VAL A 344      20.242  19.800  10.004  1.00 36.76           C  
ATOM   2697  CG1 VAL A 344      19.869  18.735  11.010  1.00 35.06           C  
ATOM   2698  CG2 VAL A 344      21.081  19.182   8.852  1.00 37.10           C  
ATOM   2699  N   MET A 345      19.873  22.715   9.224  1.00 37.27           N  
ATOM   2700  CA  MET A 345      20.491  23.847   8.567  1.00 37.47           C  
ATOM   2701  C   MET A 345      21.937  23.944   9.057  1.00 37.45           C  
ATOM   2702  O   MET A 345      22.173  24.156  10.257  1.00 36.63           O  
ATOM   2703  CB  MET A 345      19.731  25.111   8.939  1.00 38.23           C  
ATOM   2704  CG  MET A 345      20.360  26.411   8.447  1.00 40.73           C  
ATOM   2705  SD  MET A 345      20.344  26.524   6.641  1.00 50.14           S  
ATOM   2706  CE  MET A 345      18.743  27.328   6.426  1.00 48.34           C  
ATOM   2707  N   VAL A 346      22.903  23.763   8.148  1.00 36.70           N  
ATOM   2708  CA  VAL A 346      24.311  23.872   8.503  1.00 36.83           C  
ATOM   2709  C   VAL A 346      24.893  25.147   7.910  1.00 37.58           C  
ATOM   2710  O   VAL A 346      24.795  25.386   6.707  1.00 36.88           O  
ATOM   2711  CB  VAL A 346      25.144  22.635   8.080  1.00 37.11           C  
ATOM   2712  CG1 VAL A 346      26.541  22.686   8.705  1.00 36.12           C  
ATOM   2713  CG2 VAL A 346      24.439  21.332   8.476  1.00 35.73           C  
ATOM   2714  N   LYS A 347      25.460  25.985   8.777  1.00 38.59           N  
ATOM   2715  CA  LYS A 347      25.969  27.296   8.387  1.00 39.60           C  
ATOM   2716  C   LYS A 347      27.452  27.365   8.626  1.00 40.17           C  
ATOM   2717  O   LYS A 347      27.932  27.005   9.704  1.00 40.51           O  
ATOM   2718  CB  LYS A 347      25.256  28.412   9.152  1.00 40.03           C  
ATOM   2719  CG  LYS A 347      24.010  28.878   8.476  1.00 41.66           C  
ATOM   2720  CD  LYS A 347      22.917  29.222   9.440  1.00 45.82           C  
ATOM   2721  CE  LYS A 347      22.672  30.724   9.478  1.00 47.78           C  
ATOM   2722  NZ  LYS A 347      21.197  30.989   9.647  1.00 48.36           N  
ATOM   2723  N   PHE A 348      28.169  27.798   7.593  1.00 40.44           N  
ATOM   2724  CA  PHE A 348      29.619  27.891   7.581  1.00 40.80           C  
ATOM   2725  C   PHE A 348      30.040  29.349   7.384  1.00 42.40           C  
ATOM   2726  O   PHE A 348      29.364  30.121   6.673  1.00 41.94           O  
ATOM   2727  CB  PHE A 348      30.193  27.053   6.448  1.00 40.18           C  
ATOM   2728  CG  PHE A 348      30.148  25.571   6.692  1.00 38.30           C  
ATOM   2729  CD1 PHE A 348      31.081  24.964   7.507  1.00 37.51           C  
ATOM   2730  CD2 PHE A 348      29.189  24.778   6.070  1.00 37.81           C  
ATOM   2731  CE1 PHE A 348      31.049  23.588   7.736  1.00 36.63           C  
ATOM   2732  CE2 PHE A 348      29.148  23.397   6.282  1.00 37.27           C  
ATOM   2733  CZ  PHE A 348      30.093  22.803   7.115  1.00 38.82           C  
ATOM   2734  N   LEU A 349      31.136  29.720   8.040  1.00 43.65           N  
ATOM   2735  CA  LEU A 349      31.781  31.016   7.848  1.00 45.44           C  
ATOM   2736  C   LEU A 349      33.258  30.891   8.184  1.00 46.81           C  
ATOM   2737  O   LEU A 349      33.622  30.591   9.326  1.00 47.48           O  
ATOM   2738  CB  LEU A 349      31.141  32.095   8.722  1.00 45.77           C  
ATOM   2739  CG  LEU A 349      31.150  33.564   8.273  1.00 46.40           C  
ATOM   2740  CD1 LEU A 349      31.384  34.494   9.475  1.00 47.58           C  
ATOM   2741  CD2 LEU A 349      32.146  33.874   7.175  1.00 45.88           C  
ATOM   2742  N   PHE A 350      34.099  31.102   7.173  1.00 48.09           N  
ATOM   2743  CA  PHE A 350      35.537  31.054   7.310  1.00 49.44           C  
ATOM   2744  C   PHE A 350      36.074  32.392   6.811  1.00 51.29           C  
ATOM   2745  O   PHE A 350      36.508  32.494   5.660  1.00 51.03           O  
ATOM   2746  CB  PHE A 350      36.116  29.908   6.478  1.00 49.43           C  
ATOM   2747  CG  PHE A 350      35.556  28.542   6.822  1.00 49.31           C  
ATOM   2748  CD1 PHE A 350      34.597  27.950   6.010  1.00 48.53           C  
ATOM   2749  CD2 PHE A 350      36.005  27.845   7.947  1.00 48.86           C  
ATOM   2750  CE1 PHE A 350      34.088  26.693   6.302  1.00 47.55           C  
ATOM   2751  CE2 PHE A 350      35.486  26.586   8.256  1.00 49.04           C  
ATOM   2752  CZ  PHE A 350      34.537  26.006   7.425  1.00 48.65           C  
ATOM   2753  N   PRO A 351      36.032  33.432   7.676  1.00 53.07           N  
ATOM   2754  CA  PRO A 351      36.315  34.806   7.252  1.00 54.30           C  
ATOM   2755  C   PRO A 351      37.765  35.101   6.843  1.00 55.67           C  
ATOM   2756  O   PRO A 351      38.706  34.421   7.275  1.00 55.26           O  
ATOM   2757  CB  PRO A 351      35.912  35.639   8.479  1.00 54.29           C  
ATOM   2758  CG  PRO A 351      36.080  34.718   9.616  1.00 53.88           C  
ATOM   2759  CD  PRO A 351      35.701  33.369   9.114  1.00 52.77           C  
ATOM   2760  N   ARG A 352      37.903  36.108   5.985  1.00 57.28           N  
ATOM   2761  CA  ARG A 352      39.186  36.680   5.615  1.00 59.46           C  
ATOM   2762  C   ARG A 352      39.166  38.187   5.963  1.00 61.01           C  
ATOM   2763  O   ARG A 352      38.078  38.776   6.092  1.00 60.90           O  
ATOM   2764  CB  ARG A 352      39.457  36.484   4.109  1.00 59.60           C  
ATOM   2765  CG  ARG A 352      39.093  35.104   3.509  1.00 59.98           C  
ATOM   2766  CD  ARG A 352      39.855  33.946   4.124  1.00 59.96           C  
ATOM   2767  NE  ARG A 352      40.132  32.881   3.163  1.00 59.60           N  
ATOM   2768  CZ  ARG A 352      39.399  31.782   3.005  1.00 59.88           C  
ATOM   2769  NH1 ARG A 352      38.312  31.584   3.745  1.00 60.21           N  
ATOM   2770  NH2 ARG A 352      39.762  30.871   2.105  1.00 57.90           N  
ATOM   2771  N   PRO A 353      40.358  38.817   6.112  1.00 62.39           N  
ATOM   2772  CA  PRO A 353      40.452  40.273   6.336  1.00 63.49           C  
ATOM   2773  C   PRO A 353      39.522  41.070   5.412  1.00 64.54           C  
ATOM   2774  O   PRO A 353      38.856  42.006   5.867  1.00 64.55           O  
ATOM   2775  CB  PRO A 353      41.917  40.586   6.018  1.00 63.45           C  
ATOM   2776  CG  PRO A 353      42.655  39.319   6.335  1.00 63.06           C  
ATOM   2777  CD  PRO A 353      41.693  38.178   6.074  1.00 62.59           C  
ATOM   2778  N   ASP A 354      39.485  40.699   4.131  1.00 65.85           N  
ATOM   2779  CA  ASP A 354      38.451  41.188   3.221  1.00 67.07           C  
ATOM   2780  C   ASP A 354      37.275  40.221   3.259  1.00 67.35           C  
ATOM   2781  O   ASP A 354      37.434  39.023   2.998  1.00 67.54           O  
ATOM   2782  CB  ASP A 354      38.977  41.334   1.785  1.00 67.46           C  
ATOM   2783  CG  ASP A 354      37.966  42.018   0.846  1.00 69.28           C  
ATOM   2784  OD1 ASP A 354      36.997  42.645   1.341  1.00 70.88           O  
ATOM   2785  OD2 ASP A 354      38.143  41.933  -0.394  1.00 70.72           O  
ATOM   2786  N   GLN A 355      36.102  40.759   3.585  1.00 67.75           N  
ATOM   2787  CA  GLN A 355      34.883  39.972   3.751  1.00 68.21           C  
ATOM   2788  C   GLN A 355      34.339  39.403   2.438  1.00 68.11           C  
ATOM   2789  O   GLN A 355      33.523  38.479   2.453  1.00 68.10           O  
ATOM   2790  CB  GLN A 355      33.804  40.804   4.447  1.00 68.67           C  
ATOM   2791  CG  GLN A 355      34.202  41.297   5.839  1.00 70.82           C  
ATOM   2792  CD  GLN A 355      33.009  41.503   6.765  1.00 73.09           C  
ATOM   2793  OE1 GLN A 355      32.093  42.284   6.474  1.00 73.79           O  
ATOM   2794  NE2 GLN A 355      33.022  40.802   7.897  1.00 73.87           N  
ATOM   2795  N   GLN A 356      34.790  39.959   1.314  1.00 67.67           N  
ATOM   2796  CA  GLN A 356      34.411  39.483  -0.015  1.00 67.34           C  
ATOM   2797  C   GLN A 356      34.962  38.080  -0.277  1.00 66.31           C  
ATOM   2798  O   GLN A 356      34.398  37.315  -1.064  1.00 66.05           O  
ATOM   2799  CB  GLN A 356      34.933  40.456  -1.083  1.00 67.47           C  
ATOM   2800  CG  GLN A 356      34.572  40.076  -2.525  1.00 68.47           C  
ATOM   2801  CD  GLN A 356      34.784  41.203  -3.537  1.00 68.93           C  
ATOM   2802  OE1 GLN A 356      35.077  40.942  -4.712  1.00 71.28           O  
ATOM   2803  NE2 GLN A 356      34.630  42.458  -3.091  1.00 69.74           N  
ATOM   2804  N   HIS A 357      36.070  37.762   0.389  1.00 65.19           N  
ATOM   2805  CA  HIS A 357      36.801  36.520   0.153  1.00 64.04           C  
ATOM   2806  C   HIS A 357      36.565  35.502   1.249  1.00 62.23           C  
ATOM   2807  O   HIS A 357      37.205  34.450   1.284  1.00 62.00           O  
ATOM   2808  CB  HIS A 357      38.291  36.813  -0.030  1.00 64.68           C  
ATOM   2809  CG  HIS A 357      38.561  37.846  -1.081  1.00 67.63           C  
ATOM   2810  ND1 HIS A 357      38.192  37.677  -2.400  1.00 70.11           N  
ATOM   2811  CD2 HIS A 357      39.131  39.072  -1.003  1.00 70.18           C  
ATOM   2812  CE1 HIS A 357      38.532  38.752  -3.092  1.00 71.78           C  
ATOM   2813  NE2 HIS A 357      39.101  39.615  -2.267  1.00 71.83           N  
ATOM   2814  N   SER A 358      35.628  35.824   2.133  1.00 60.46           N  
ATOM   2815  CA  SER A 358      35.195  34.908   3.172  1.00 58.72           C  
ATOM   2816  C   SER A 358      34.388  33.787   2.537  1.00 57.47           C  
ATOM   2817  O   SER A 358      33.429  34.050   1.821  1.00 57.61           O  
ATOM   2818  CB  SER A 358      34.329  35.646   4.192  1.00 58.75           C  
ATOM   2819  OG  SER A 358      35.050  36.704   4.799  1.00 58.74           O  
ATOM   2820  N   VAL A 359      34.777  32.541   2.778  1.00 55.57           N  
ATOM   2821  CA  VAL A 359      33.931  31.421   2.383  1.00 53.75           C  
ATOM   2822  C   VAL A 359      32.741  31.333   3.357  1.00 52.63           C  
ATOM   2823  O   VAL A 359      32.929  31.208   4.578  1.00 52.06           O  
ATOM   2824  CB  VAL A 359      34.724  30.097   2.327  1.00 54.01           C  
ATOM   2825  CG1 VAL A 359      33.815  28.934   1.968  1.00 53.56           C  
ATOM   2826  CG2 VAL A 359      35.884  30.208   1.336  1.00 54.24           C  
ATOM   2827  N   ALA A 360      31.530  31.422   2.810  1.00 50.99           N  
ATOM   2828  CA  ALA A 360      30.300  31.421   3.603  1.00 49.81           C  
ATOM   2829  C   ALA A 360      29.186  30.629   2.920  1.00 48.99           C  
ATOM   2830  O   ALA A 360      28.617  31.081   1.925  1.00 48.74           O  
ATOM   2831  CB  ALA A 360      29.849  32.859   3.878  1.00 49.82           C  
ATOM   2832  N   TYR A 361      28.873  29.454   3.473  1.00 47.87           N  
ATOM   2833  CA  TYR A 361      27.851  28.562   2.926  1.00 46.77           C  
ATOM   2834  C   TYR A 361      26.691  28.244   3.906  1.00 46.46           C  
ATOM   2835  O   TYR A 361      26.872  28.217   5.125  1.00 46.02           O  
ATOM   2836  CB  TYR A 361      28.519  27.259   2.474  1.00 46.84           C  
ATOM   2837  CG  TYR A 361      28.984  27.247   1.035  1.00 46.29           C  
ATOM   2838  CD1 TYR A 361      30.125  27.944   0.628  1.00 46.43           C  
ATOM   2839  CD2 TYR A 361      28.289  26.521   0.083  1.00 46.68           C  
ATOM   2840  CE1 TYR A 361      30.540  27.924  -0.717  1.00 46.48           C  
ATOM   2841  CE2 TYR A 361      28.690  26.484  -1.247  1.00 46.08           C  
ATOM   2842  CZ  TYR A 361      29.804  27.184  -1.645  1.00 46.89           C  
ATOM   2843  OH  TYR A 361      30.163  27.119  -2.977  1.00 47.32           O  
ATOM   2844  N   THR A 362      25.501  28.001   3.372  1.00 45.49           N  
ATOM   2845  CA  THR A 362      24.459  27.388   4.162  1.00 45.28           C  
ATOM   2846  C   THR A 362      23.913  26.172   3.417  1.00 44.58           C  
ATOM   2847  O   THR A 362      23.660  26.235   2.216  1.00 45.17           O  
ATOM   2848  CB  THR A 362      23.307  28.358   4.478  1.00 45.86           C  
ATOM   2849  OG1 THR A 362      22.500  28.523   3.306  1.00 47.60           O  
ATOM   2850  CG2 THR A 362      23.828  29.728   4.965  1.00 45.61           C  
ATOM   2851  N   PHE A 363      23.732  25.075   4.141  1.00 43.13           N  
ATOM   2852  CA  PHE A 363      23.238  23.820   3.606  1.00 41.79           C  
ATOM   2853  C   PHE A 363      21.945  23.460   4.333  1.00 41.80           C  
ATOM   2854  O   PHE A 363      21.973  23.143   5.526  1.00 41.40           O  
ATOM   2855  CB  PHE A 363      24.248  22.681   3.883  1.00 41.38           C  
ATOM   2856  CG  PHE A 363      25.507  22.718   3.046  1.00 40.59           C  
ATOM   2857  CD1 PHE A 363      26.509  23.663   3.293  1.00 37.90           C  
ATOM   2858  CD2 PHE A 363      25.723  21.755   2.062  1.00 38.76           C  
ATOM   2859  CE1 PHE A 363      27.658  23.693   2.530  1.00 37.84           C  
ATOM   2860  CE2 PHE A 363      26.884  21.767   1.291  1.00 38.85           C  
ATOM   2861  CZ  PHE A 363      27.850  22.736   1.516  1.00 38.96           C  
ATOM   2862  N   GLU A 364      20.813  23.519   3.641  1.00 41.61           N  
ATOM   2863  CA  GLU A 364      19.591  22.911   4.129  1.00 41.61           C  
ATOM   2864  C   GLU A 364      19.579  21.493   3.604  1.00 41.33           C  
ATOM   2865  O   GLU A 364      19.567  21.319   2.395  1.00 41.45           O  
ATOM   2866  CB  GLU A 364      18.384  23.572   3.497  1.00 41.95           C  
ATOM   2867  CG  GLU A 364      17.825  24.754   4.173  1.00 44.59           C  
ATOM   2868  CD  GLU A 364      16.455  25.080   3.613  1.00 49.67           C  
ATOM   2869  OE1 GLU A 364      16.131  26.296   3.489  1.00 51.32           O  
ATOM   2870  OE2 GLU A 364      15.716  24.116   3.279  1.00 47.94           O  
ATOM   2871  N   GLU A 365      19.553  20.488   4.480  1.00 40.57           N  
ATOM   2872  CA  GLU A 365      19.426  19.088   4.057  1.00 40.14           C  
ATOM   2873  C   GLU A 365      18.695  18.222   5.060  1.00 39.37           C  
ATOM   2874  O   GLU A 365      18.697  18.518   6.246  1.00 38.90           O  
ATOM   2875  CB  GLU A 365      20.798  18.439   3.937  1.00 40.99           C  
ATOM   2876  CG  GLU A 365      21.871  19.328   3.439  1.00 42.18           C  
ATOM   2877  CD  GLU A 365      23.216  18.806   3.767  1.00 41.19           C  
ATOM   2878  OE1 GLU A 365      23.356  18.084   4.768  1.00 41.55           O  
ATOM   2879  OE2 GLU A 365      24.138  19.144   3.021  1.00 42.83           O  
ATOM   2880  N   ASP A 366      18.117  17.125   4.574  1.00 38.82           N  
ATOM   2881  CA  ASP A 366      17.707  16.010   5.421  1.00 38.43           C  
ATOM   2882  C   ASP A 366      18.856  15.053   5.545  1.00 37.60           C  
ATOM   2883  O   ASP A 366      19.499  14.697   4.554  1.00 37.52           O  
ATOM   2884  CB  ASP A 366      16.542  15.253   4.814  1.00 38.92           C  
ATOM   2885  CG  ASP A 366      15.414  16.163   4.390  1.00 43.55           C  
ATOM   2886  OD1 ASP A 366      14.423  15.625   3.855  1.00 50.22           O  
ATOM   2887  OD2 ASP A 366      15.507  17.408   4.557  1.00 46.56           O  
ATOM   2888  N   ILE A 367      19.123  14.642   6.776  1.00 36.49           N  
ATOM   2889  CA  ILE A 367      20.085  13.603   7.076  1.00 35.11           C  
ATOM   2890  C   ILE A 367      19.313  12.513   7.809  1.00 34.82           C  
ATOM   2891  O   ILE A 367      18.689  12.776   8.833  1.00 34.53           O  
ATOM   2892  CB  ILE A 367      21.236  14.151   7.941  1.00 35.19           C  
ATOM   2893  CG1 ILE A 367      22.009  15.230   7.163  1.00 33.79           C  
ATOM   2894  CG2 ILE A 367      22.151  13.034   8.398  1.00 35.86           C  
ATOM   2895  CD1 ILE A 367      22.877  16.091   7.994  1.00 33.60           C  
ATOM   2896  N   VAL A 368      19.339  11.303   7.256  1.00 33.71           N  
ATOM   2897  CA  VAL A 368      18.682  10.162   7.855  1.00 32.95           C  
ATOM   2898  C   VAL A 368      19.774   9.235   8.351  1.00 33.24           C  
ATOM   2899  O   VAL A 368      20.714   8.946   7.618  1.00 32.72           O  
ATOM   2900  CB  VAL A 368      17.757   9.460   6.841  1.00 33.60           C  
ATOM   2901  CG1 VAL A 368      16.955   8.316   7.491  1.00 29.98           C  
ATOM   2902  CG2 VAL A 368      16.823  10.488   6.210  1.00 32.27           C  
ATOM   2903  N   THR A 369      19.695   8.837   9.624  1.00 32.77           N  
ATOM   2904  CA  THR A 369      20.698   7.974  10.233  1.00 32.47           C  
ATOM   2905  C   THR A 369      20.023   6.765  10.855  1.00 33.17           C  
ATOM   2906  O   THR A 369      18.995   6.893  11.516  1.00 34.44           O  
ATOM   2907  CB  THR A 369      21.512   8.703  11.335  1.00 33.39           C  
ATOM   2908  OG1 THR A 369      20.619   9.276  12.315  1.00 31.52           O  
ATOM   2909  CG2 THR A 369      22.404   9.769  10.733  1.00 32.50           C  
ATOM   2910  N   THR A 370      20.575   5.590  10.607  1.00 33.54           N  
ATOM   2911  CA  THR A 370      20.160   4.387  11.288  1.00 34.28           C  
ATOM   2912  C   THR A 370      21.221   4.105  12.330  1.00 34.39           C  
ATOM   2913  O   THR A 370      22.404   3.986  12.001  1.00 33.63           O  
ATOM   2914  CB  THR A 370      19.964   3.206  10.304  1.00 34.39           C  
ATOM   2915  OG1 THR A 370      18.937   3.565   9.364  1.00 35.34           O  
ATOM   2916  CG2 THR A 370      19.528   1.969  11.042  1.00 34.79           C  
ATOM   2917  N   VAL A 371      20.781   4.036  13.591  1.00 34.96           N  
ATOM   2918  CA  VAL A 371      21.678   3.988  14.759  1.00 35.65           C  
ATOM   2919  C   VAL A 371      21.386   2.758  15.614  1.00 35.81           C  
ATOM   2920  O   VAL A 371      20.223   2.390  15.800  1.00 35.76           O  
ATOM   2921  CB  VAL A 371      21.543   5.277  15.604  1.00 35.88           C  
ATOM   2922  CG1 VAL A 371      22.357   5.192  16.904  1.00 36.85           C  
ATOM   2923  CG2 VAL A 371      21.975   6.448  14.793  1.00 34.77           C  
ATOM   2924  N   GLN A 372      22.450   2.094  16.052  1.00 36.22           N  
ATOM   2925  CA  GLN A 372      22.373   1.024  17.037  1.00 37.40           C  
ATOM   2926  C   GLN A 372      23.099   1.446  18.322  1.00 36.82           C  
ATOM   2927  O   GLN A 372      23.996   2.257  18.292  1.00 36.15           O  
ATOM   2928  CB  GLN A 372      22.969  -0.280  16.496  1.00 37.78           C  
ATOM   2929  CG  GLN A 372      22.402  -0.701  15.161  1.00 40.68           C  
ATOM   2930  CD  GLN A 372      22.629  -2.172  14.876  1.00 46.90           C  
ATOM   2931  OE1 GLN A 372      23.761  -2.601  14.585  1.00 48.34           O  
ATOM   2932  NE2 GLN A 372      21.555  -2.961  14.959  1.00 47.41           N  
ATOM   2933  N   ALA A 373      22.701   0.882  19.453  1.00 37.55           N  
ATOM   2934  CA  ALA A 373      23.206   1.372  20.741  1.00 37.67           C  
ATOM   2935  C   ALA A 373      23.711   0.257  21.637  1.00 37.76           C  
ATOM   2936  O   ALA A 373      23.250  -0.876  21.572  1.00 37.06           O  
ATOM   2937  CB  ALA A 373      22.143   2.211  21.454  1.00 37.94           C  
ATOM   2938  N   SER A 374      24.660   0.628  22.483  1.00 38.64           N  
ATOM   2939  CA  SER A 374      25.414  -0.278  23.350  1.00 38.61           C  
ATOM   2940  C   SER A 374      25.532   0.445  24.686  1.00 38.31           C  
ATOM   2941  O   SER A 374      25.582   1.681  24.720  1.00 37.42           O  
ATOM   2942  CB  SER A 374      26.819  -0.444  22.778  1.00 38.27           C  
ATOM   2943  OG  SER A 374      27.324  -1.746  22.983  1.00 41.21           O  
ATOM   2944  N   TYR A 375      25.566  -0.323  25.772  1.00 38.27           N  
ATOM   2945  CA  TYR A 375      25.934   0.204  27.089  1.00 38.56           C  
ATOM   2946  C   TYR A 375      27.013  -0.655  27.669  1.00 38.92           C  
ATOM   2947  O   TYR A 375      26.899  -1.896  27.708  1.00 38.77           O  
ATOM   2948  CB  TYR A 375      24.750   0.243  28.046  1.00 37.91           C  
ATOM   2949  CG  TYR A 375      24.979   1.062  29.309  1.00 37.45           C  
ATOM   2950  CD1 TYR A 375      24.833   2.459  29.311  1.00 35.13           C  
ATOM   2951  CD2 TYR A 375      25.316   0.429  30.514  1.00 36.31           C  
ATOM   2952  CE1 TYR A 375      25.021   3.191  30.487  1.00 33.54           C  
ATOM   2953  CE2 TYR A 375      25.490   1.137  31.677  1.00 35.78           C  
ATOM   2954  CZ  TYR A 375      25.341   2.520  31.665  1.00 36.26           C  
ATOM   2955  OH  TYR A 375      25.534   3.197  32.850  1.00 36.26           O  
ATOM   2956  N   SER A 376      28.053   0.010  28.142  1.00 39.70           N  
ATOM   2957  CA  SER A 376      29.309  -0.662  28.407  1.00 41.85           C  
ATOM   2958  C   SER A 376      30.119   0.272  29.269  1.00 42.83           C  
ATOM   2959  O   SER A 376      30.155   1.479  29.015  1.00 43.20           O  
ATOM   2960  CB  SER A 376      30.013  -0.919  27.066  1.00 41.99           C  
ATOM   2961  OG  SER A 376      31.263  -1.543  27.220  1.00 44.34           O  
ATOM   2962  N   LYS A 377      30.719  -0.261  30.331  1.00 43.81           N  
ATOM   2963  CA  LYS A 377      31.585   0.549  31.198  1.00 44.36           C  
ATOM   2964  C   LYS A 377      30.979   1.917  31.553  1.00 43.92           C  
ATOM   2965  O   LYS A 377      31.657   2.958  31.453  1.00 43.85           O  
ATOM   2966  CB  LYS A 377      32.967   0.729  30.562  1.00 45.08           C  
ATOM   2967  CG  LYS A 377      33.735  -0.581  30.385  1.00 47.30           C  
ATOM   2968  CD  LYS A 377      35.231  -0.322  30.564  1.00 52.19           C  
ATOM   2969  CE  LYS A 377      36.070  -1.470  30.027  1.00 55.19           C  
ATOM   2970  NZ  LYS A 377      37.529  -1.161  30.179  1.00 57.48           N  
ATOM   2971  N   LYS A 378      29.707   1.884  31.965  1.00 42.91           N  
ATOM   2972  CA  LYS A 378      28.937   3.054  32.418  1.00 42.81           C  
ATOM   2973  C   LYS A 378      28.761   4.193  31.395  1.00 42.17           C  
ATOM   2974  O   LYS A 378      28.459   5.345  31.764  1.00 41.55           O  
ATOM   2975  CB  LYS A 378      29.445   3.554  33.788  1.00 43.43           C  
ATOM   2976  CG  LYS A 378      29.234   2.486  34.858  1.00 44.62           C  
ATOM   2977  CD  LYS A 378      29.447   2.990  36.256  1.00 46.50           C  
ATOM   2978  CE  LYS A 378      29.635   1.786  37.197  1.00 47.97           C  
ATOM   2979  NZ  LYS A 378      28.328   1.142  37.607  1.00 47.50           N  
ATOM   2980  N   LYS A 379      28.901   3.834  30.114  1.00 40.98           N  
ATOM   2981  CA  LYS A 379      28.716   4.752  28.998  1.00 40.59           C  
ATOM   2982  C   LYS A 379      27.773   4.186  27.947  1.00 38.89           C  
ATOM   2983  O   LYS A 379      27.747   2.992  27.677  1.00 38.14           O  
ATOM   2984  CB  LYS A 379      30.052   5.084  28.327  1.00 40.54           C  
ATOM   2985  CG  LYS A 379      31.021   5.895  29.179  1.00 42.19           C  
ATOM   2986  CD  LYS A 379      32.397   5.978  28.521  1.00 43.13           C  
ATOM   2987  CE  LYS A 379      33.521   5.911  29.580  1.00 48.76           C  
ATOM   2988  NZ  LYS A 379      33.690   4.536  30.190  1.00 49.77           N  
ATOM   2989  N   LEU A 380      27.001   5.089  27.366  1.00 38.27           N  
ATOM   2990  CA  LEU A 380      26.226   4.848  26.157  1.00 37.48           C  
ATOM   2991  C   LEU A 380      27.132   4.974  24.907  1.00 37.39           C  
ATOM   2992  O   LEU A 380      27.889   5.945  24.769  1.00 35.94           O  
ATOM   2993  CB  LEU A 380      25.101   5.888  26.109  1.00 37.43           C  
ATOM   2994  CG  LEU A 380      23.765   5.702  25.379  1.00 36.67           C  
ATOM   2995  CD1 LEU A 380      23.710   6.693  24.264  1.00 35.72           C  
ATOM   2996  CD2 LEU A 380      23.523   4.252  24.901  1.00 33.25           C  
ATOM   2997  N   PHE A 381      27.068   3.966  24.033  1.00 37.05           N  
ATOM   2998  CA  PHE A 381      27.753   3.983  22.728  1.00 37.58           C  
ATOM   2999  C   PHE A 381      26.747   3.910  21.572  1.00 37.62           C  
ATOM   3000  O   PHE A 381      25.904   2.999  21.516  1.00 37.84           O  
ATOM   3001  CB  PHE A 381      28.739   2.818  22.600  1.00 37.70           C  
ATOM   3002  CG  PHE A 381      29.910   2.911  23.522  1.00 38.49           C  
ATOM   3003  CD1 PHE A 381      29.872   2.289  24.774  1.00 39.50           C  
ATOM   3004  CD2 PHE A 381      31.063   3.604  23.139  1.00 39.60           C  
ATOM   3005  CE1 PHE A 381      30.957   2.357  25.643  1.00 40.25           C  
ATOM   3006  CE2 PHE A 381      32.166   3.684  23.995  1.00 41.49           C  
ATOM   3007  CZ  PHE A 381      32.108   3.063  25.262  1.00 40.29           C  
ATOM   3008  N   LEU A 382      26.841   4.875  20.663  1.00 37.40           N  
ATOM   3009  CA  LEU A 382      25.973   4.931  19.487  1.00 37.18           C  
ATOM   3010  C   LEU A 382      26.741   4.587  18.200  1.00 37.72           C  
ATOM   3011  O   LEU A 382      27.867   5.034  17.958  1.00 38.10           O  
ATOM   3012  CB  LEU A 382      25.279   6.300  19.370  1.00 36.70           C  
ATOM   3013  CG  LEU A 382      24.309   6.792  20.467  1.00 34.67           C  
ATOM   3014  CD1 LEU A 382      23.818   8.227  20.192  1.00 30.21           C  
ATOM   3015  CD2 LEU A 382      23.114   5.865  20.618  1.00 33.67           C  
ATOM   3016  N   SER A 383      26.103   3.779  17.379  1.00 37.50           N  
ATOM   3017  CA  SER A 383      26.725   3.175  16.214  1.00 37.67           C  
ATOM   3018  C   SER A 383      25.922   3.548  14.975  1.00 37.07           C  
ATOM   3019  O   SER A 383      24.688   3.491  14.989  1.00 36.69           O  
ATOM   3020  CB  SER A 383      26.658   1.672  16.407  1.00 37.44           C  
ATOM   3021  OG  SER A 383      27.649   1.014  15.675  1.00 39.98           O  
ATOM   3022  N   LEU A 384      26.605   3.924  13.900  1.00 37.36           N  
ATOM   3023  CA  LEU A 384      25.930   4.260  12.630  1.00 37.04           C  
ATOM   3024  C   LEU A 384      25.860   3.028  11.723  1.00 37.73           C  
ATOM   3025  O   LEU A 384      26.892   2.571  11.227  1.00 37.85           O  
ATOM   3026  CB  LEU A 384      26.667   5.407  11.921  1.00 36.87           C  
ATOM   3027  CG  LEU A 384      25.994   6.099  10.726  1.00 35.70           C  
ATOM   3028  CD1 LEU A 384      24.619   6.616  11.131  1.00 32.03           C  
ATOM   3029  CD2 LEU A 384      26.862   7.235  10.218  1.00 36.15           C  
ATOM   3030  N   LEU A 385      24.668   2.460  11.547  1.00 38.29           N  
ATOM   3031  CA  LEU A 385      24.524   1.316  10.641  1.00 39.14           C  
ATOM   3032  C   LEU A 385      24.482   1.809   9.175  1.00 39.22           C  
ATOM   3033  O   LEU A 385      25.067   1.192   8.291  1.00 39.18           O  
ATOM   3034  CB  LEU A 385      23.311   0.428  10.982  1.00 38.93           C  
ATOM   3035  CG  LEU A 385      23.161  -0.875  10.163  1.00 40.02           C  
ATOM   3036  CD1 LEU A 385      24.406  -1.770  10.249  1.00 40.67           C  
ATOM   3037  CD2 LEU A 385      21.910  -1.695  10.544  1.00 39.60           C  
ATOM   3038  N   ASP A 386      23.779   2.908   8.942  1.00 39.15           N  
ATOM   3039  CA  ASP A 386      23.861   3.617   7.672  1.00 40.01           C  
ATOM   3040  C   ASP A 386      23.275   5.014   7.740  1.00 38.93           C  
ATOM   3041  O   ASP A 386      22.752   5.424   8.772  1.00 38.73           O  
ATOM   3042  CB  ASP A 386      23.306   2.811   6.479  1.00 40.74           C  
ATOM   3043  CG  ASP A 386      21.788   2.810   6.398  1.00 43.82           C  
ATOM   3044  OD1 ASP A 386      21.136   2.407   7.382  1.00 47.06           O  
ATOM   3045  OD2 ASP A 386      21.245   3.170   5.327  1.00 43.96           O  
ATOM   3046  N   PHE A 387      23.425   5.745   6.634  1.00 37.87           N  
ATOM   3047  CA  PHE A 387      22.977   7.127   6.516  1.00 36.24           C  
ATOM   3048  C   PHE A 387      22.631   7.467   5.070  1.00 36.11           C  
ATOM   3049  O   PHE A 387      23.103   6.825   4.126  1.00 34.66           O  
ATOM   3050  CB  PHE A 387      24.025   8.116   7.062  1.00 35.85           C  
ATOM   3051  CG  PHE A 387      25.235   8.287   6.172  1.00 35.08           C  
ATOM   3052  CD1 PHE A 387      25.296   9.330   5.242  1.00 34.53           C  
ATOM   3053  CD2 PHE A 387      26.307   7.423   6.269  1.00 32.39           C  
ATOM   3054  CE1 PHE A 387      26.397   9.494   4.421  1.00 32.53           C  
ATOM   3055  CE2 PHE A 387      27.423   7.588   5.464  1.00 33.40           C  
ATOM   3056  CZ  PHE A 387      27.470   8.629   4.541  1.00 33.70           C  
ATOM   3057  N   GLN A 388      21.768   8.457   4.914  1.00 35.89           N  
ATOM   3058  CA  GLN A 388      21.550   9.073   3.621  1.00 36.98           C  
ATOM   3059  C   GLN A 388      21.404  10.568   3.820  1.00 36.24           C  
ATOM   3060  O   GLN A 388      20.856  11.005   4.834  1.00 36.50           O  
ATOM   3061  CB  GLN A 388      20.398   8.438   2.829  1.00 37.16           C  
ATOM   3062  CG  GLN A 388      19.267   7.780   3.596  1.00 42.14           C  
ATOM   3063  CD  GLN A 388      19.570   6.380   4.156  1.00 47.32           C  
ATOM   3064  OE1 GLN A 388      18.916   5.944   5.118  1.00 47.84           O  
ATOM   3065  NE2 GLN A 388      20.546   5.675   3.564  1.00 47.43           N  
ATOM   3066  N   ILE A 389      21.998  11.332   2.906  1.00 35.49           N  
ATOM   3067  CA  ILE A 389      21.977  12.781   2.913  1.00 35.84           C  
ATOM   3068  C   ILE A 389      21.347  13.327   1.625  1.00 36.72           C  
ATOM   3069  O   ILE A 389      21.806  13.010   0.515  1.00 36.12           O  
ATOM   3070  CB  ILE A 389      23.402  13.322   3.085  1.00 36.12           C  
ATOM   3071  CG1 ILE A 389      23.930  12.957   4.480  1.00 36.22           C  
ATOM   3072  CG2 ILE A 389      23.456  14.818   2.801  1.00 35.72           C  
ATOM   3073  CD1 ILE A 389      25.052  13.851   4.974  1.00 39.64           C  
ATOM   3074  N   THR A 390      20.288  14.123   1.762  1.00 37.43           N  
ATOM   3075  CA  THR A 390      19.652  14.740   0.597  1.00 38.99           C  
ATOM   3076  C   THR A 390      19.519  16.237   0.775  1.00 39.62           C  
ATOM   3077  O   THR A 390      18.609  16.689   1.472  1.00 39.59           O  
ATOM   3078  CB  THR A 390      18.274  14.132   0.253  1.00 38.82           C  
ATOM   3079  OG1 THR A 390      17.361  14.390   1.317  1.00 40.76           O  
ATOM   3080  CG2 THR A 390      18.374  12.643   0.037  1.00 37.91           C  
ATOM   3081  N   PRO A 391      20.441  17.016   0.149  1.00 40.59           N  
ATOM   3082  CA  PRO A 391      20.375  18.475   0.213  1.00 41.39           C  
ATOM   3083  C   PRO A 391      19.127  19.001  -0.434  1.00 42.65           C  
ATOM   3084  O   PRO A 391      18.625  18.381  -1.362  1.00 43.09           O  
ATOM   3085  CB  PRO A 391      21.603  18.931  -0.577  1.00 41.68           C  
ATOM   3086  CG  PRO A 391      22.532  17.755  -0.553  1.00 41.82           C  
ATOM   3087  CD  PRO A 391      21.613  16.559  -0.623  1.00 40.33           C  
ATOM   3088  N   LYS A 392      18.630  20.127   0.073  1.00 43.58           N  
ATOM   3089  CA  LYS A 392      17.402  20.752  -0.421  1.00 44.82           C  
ATOM   3090  C   LYS A 392      17.687  22.118  -1.033  1.00 45.42           C  
ATOM   3091  O   LYS A 392      17.088  22.484  -2.043  1.00 45.66           O  
ATOM   3092  CB  LYS A 392      16.356  20.896   0.689  1.00 44.58           C  
ATOM   3093  CG  LYS A 392      15.697  19.591   1.128  1.00 45.66           C  
ATOM   3094  CD  LYS A 392      15.125  18.816  -0.053  1.00 47.50           C  
ATOM   3095  CE  LYS A 392      14.745  17.406   0.326  1.00 46.89           C  
ATOM   3096  NZ  LYS A 392      13.509  17.394   1.175  1.00 49.14           N  
ATOM   3097  N   THR A 393      18.588  22.871  -0.409  1.00 46.21           N  
ATOM   3098  CA  THR A 393      18.999  24.169  -0.922  1.00 47.20           C  
ATOM   3099  C   THR A 393      20.314  24.643  -0.303  1.00 48.00           C  
ATOM   3100  O   THR A 393      20.383  24.979   0.895  1.00 48.21           O  
ATOM   3101  CB  THR A 393      17.865  25.255  -0.854  1.00 47.28           C  
ATOM   3102  OG1 THR A 393      18.425  26.516  -0.473  1.00 48.56           O  
ATOM   3103  CG2 THR A 393      16.787  24.890   0.123  1.00 47.91           C  
ATOM   3104  N   VAL A 394      21.356  24.651  -1.134  1.00 47.99           N  
ATOM   3105  CA  VAL A 394      22.684  25.115  -0.749  1.00 48.38           C  
ATOM   3106  C   VAL A 394      22.896  26.551  -1.240  1.00 49.06           C  
ATOM   3107  O   VAL A 394      22.554  26.900  -2.383  1.00 49.17           O  
ATOM   3108  CB  VAL A 394      23.791  24.180  -1.293  1.00 48.41           C  
ATOM   3109  CG1 VAL A 394      25.173  24.667  -0.888  1.00 48.25           C  
ATOM   3110  CG2 VAL A 394      23.566  22.738  -0.813  1.00 47.09           C  
ATOM   3111  N   SER A 395      23.443  27.385  -0.366  1.00 49.28           N  
ATOM   3112  CA  SER A 395      23.671  28.780  -0.676  1.00 49.78           C  
ATOM   3113  C   SER A 395      25.090  29.195  -0.329  1.00 50.19           C  
ATOM   3114  O   SER A 395      25.601  28.854   0.739  1.00 49.93           O  
ATOM   3115  CB  SER A 395      22.659  29.652   0.069  1.00 49.77           C  
ATOM   3116  OG  SER A 395      21.337  29.255  -0.273  1.00 50.65           O  
ATOM   3117  N   ASN A 396      25.729  29.901  -1.261  1.00 50.26           N  
ATOM   3118  CA  ASN A 396      26.951  30.628  -0.977  1.00 50.69           C  
ATOM   3119  C   ASN A 396      26.608  32.097  -0.737  1.00 51.26           C  
ATOM   3120  O   ASN A 396      25.738  32.666  -1.411  1.00 51.47           O  
ATOM   3121  CB  ASN A 396      28.000  30.452  -2.082  1.00 50.86           C  
ATOM   3122  CG  ASN A 396      27.510  30.922  -3.458  1.00 51.74           C  
ATOM   3123  OD1 ASN A 396      26.713  30.236  -4.118  1.00 47.58           O  
ATOM   3124  ND2 ASN A 396      28.015  32.092  -3.899  1.00 54.61           N  
ATOM   3125  N   LEU A 397      27.266  32.690   0.252  1.00 51.78           N  
ATOM   3126  CA  LEU A 397      26.915  34.019   0.730  1.00 52.65           C  
ATOM   3127  C   LEU A 397      27.895  35.070   0.215  1.00 52.83           C  
ATOM   3128  O   LEU A 397      27.630  36.271   0.312  1.00 53.30           O  
ATOM   3129  CB  LEU A 397      26.814  34.027   2.274  1.00 52.60           C  
ATOM   3130  CG  LEU A 397      25.529  33.592   3.025  1.00 52.74           C  
ATOM   3131  CD1 LEU A 397      24.691  32.513   2.332  1.00 51.69           C  
ATOM   3132  CD2 LEU A 397      25.874  33.126   4.436  1.00 52.69           C  
ATOM   3133  N   THR A 398      29.018  34.605  -0.334  1.00 53.32           N  
ATOM   3134  CA  THR A 398      30.002  35.454  -1.028  1.00 53.63           C  
ATOM   3135  C   THR A 398      30.370  34.840  -2.384  1.00 53.92           C  
ATOM   3136  O   THR A 398      29.954  33.721  -2.714  1.00 53.75           O  
ATOM   3137  CB  THR A 398      31.325  35.620  -0.230  1.00 53.61           C  
ATOM   3138  OG1 THR A 398      32.002  34.359  -0.165  1.00 53.76           O  
ATOM   3139  CG2 THR A 398      31.075  36.133   1.180  1.00 53.93           C  
ATOM   3140  N   GLU A 399      31.187  35.571  -3.145  1.00 54.32           N  
ATOM   3141  CA  GLU A 399      31.633  35.158  -4.480  1.00 54.48           C  
ATOM   3142  C   GLU A 399      32.620  34.011  -4.392  1.00 53.42           C  
ATOM   3143  O   GLU A 399      32.943  33.380  -5.386  1.00 53.09           O  
ATOM   3144  CB  GLU A 399      32.297  36.337  -5.210  1.00 55.29           C  
ATOM   3145  CG  GLU A 399      31.393  37.563  -5.434  1.00 58.27           C  
ATOM   3146  CD  GLU A 399      30.345  37.349  -6.526  1.00 62.40           C  
ATOM   3147  OE1 GLU A 399      29.464  38.234  -6.683  1.00 64.53           O  
ATOM   3148  OE2 GLU A 399      30.397  36.307  -7.228  1.00 63.59           O  
ATOM   3149  N   SER A 400      33.103  33.761  -3.185  1.00 52.69           N  
ATOM   3150  CA  SER A 400      34.129  32.771  -2.943  1.00 51.66           C  
ATOM   3151  C   SER A 400      33.472  31.378  -2.863  1.00 50.78           C  
ATOM   3152  O   SER A 400      33.255  30.851  -1.775  1.00 50.86           O  
ATOM   3153  CB  SER A 400      34.855  33.141  -1.649  1.00 51.55           C  
ATOM   3154  OG  SER A 400      36.243  32.877  -1.728  1.00 52.14           O  
ATOM   3155  N   SER A 401      33.154  30.799  -4.026  1.00 49.81           N  
ATOM   3156  CA  SER A 401      32.306  29.589  -4.124  1.00 48.73           C  
ATOM   3157  C   SER A 401      32.604  28.753  -5.357  1.00 48.29           C  
ATOM   3158  O   SER A 401      32.930  29.294  -6.416  1.00 48.26           O  
ATOM   3159  CB  SER A 401      30.832  29.980  -4.143  1.00 48.52           C  
ATOM   3160  OG  SER A 401      30.412  30.376  -5.433  1.00 48.63           O  
ATOM   3161  N   SER A 402      32.487  27.437  -5.218  1.00 47.48           N  
ATOM   3162  CA  SER A 402      32.829  26.509  -6.288  1.00 46.83           C  
ATOM   3163  C   SER A 402      32.269  25.123  -5.981  1.00 46.84           C  
ATOM   3164  O   SER A 402      32.113  24.739  -4.818  1.00 46.78           O  
ATOM   3165  CB  SER A 402      34.349  26.439  -6.512  1.00 46.71           C  
ATOM   3166  OG  SER A 402      34.973  25.369  -5.796  1.00 47.06           O  
ATOM   3167  N   GLU A 403      31.970  24.375  -7.029  1.00 46.27           N  
ATOM   3168  CA  GLU A 403      31.427  23.051  -6.876  1.00 45.87           C  
ATOM   3169  C   GLU A 403      32.310  22.237  -5.946  1.00 45.59           C  
ATOM   3170  O   GLU A 403      31.801  21.504  -5.103  1.00 45.08           O  
ATOM   3171  CB  GLU A 403      31.256  22.376  -8.235  1.00 46.45           C  
ATOM   3172  CG  GLU A 403      30.039  22.856  -9.017  1.00 47.21           C  
ATOM   3173  CD  GLU A 403      28.734  22.663  -8.260  1.00 50.84           C  
ATOM   3174  OE1 GLU A 403      27.853  23.543  -8.366  1.00 52.05           O  
ATOM   3175  OE2 GLU A 403      28.582  21.639  -7.549  1.00 53.52           O  
ATOM   3176  N   SER A 404      33.624  22.417  -6.061  1.00 44.93           N  
ATOM   3177  CA  SER A 404      34.558  21.738  -5.177  1.00 44.98           C  
ATOM   3178  C   SER A 404      34.662  22.291  -3.739  1.00 44.65           C  
ATOM   3179  O   SER A 404      34.982  21.540  -2.827  1.00 44.78           O  
ATOM   3180  CB  SER A 404      35.943  21.637  -5.814  1.00 45.14           C  
ATOM   3181  OG  SER A 404      36.549  22.900  -5.873  1.00 45.65           O  
ATOM   3182  N   ILE A 405      34.446  23.591  -3.549  1.00 44.49           N  
ATOM   3183  CA  ILE A 405      34.322  24.147  -2.203  1.00 44.51           C  
ATOM   3184  C   ILE A 405      33.072  23.590  -1.537  1.00 44.29           C  
ATOM   3185  O   ILE A 405      33.131  23.149  -0.391  1.00 45.38           O  
ATOM   3186  CB  ILE A 405      34.296  25.692  -2.193  1.00 44.76           C  
ATOM   3187  CG1 ILE A 405      35.713  26.232  -2.362  1.00 45.29           C  
ATOM   3188  CG2 ILE A 405      33.685  26.225  -0.891  1.00 45.00           C  
ATOM   3189  CD1 ILE A 405      35.780  27.656  -2.838  1.00 46.44           C  
ATOM   3190  N   GLN A 406      31.966  23.555  -2.281  1.00 43.19           N  
ATOM   3191  CA  GLN A 406      30.692  23.032  -1.790  1.00 42.41           C  
ATOM   3192  C   GLN A 406      30.722  21.549  -1.451  1.00 41.70           C  
ATOM   3193  O   GLN A 406      30.060  21.096  -0.511  1.00 41.53           O  
ATOM   3194  CB  GLN A 406      29.565  23.290  -2.787  1.00 42.18           C  
ATOM   3195  CG  GLN A 406      28.244  22.694  -2.316  1.00 41.64           C  
ATOM   3196  CD  GLN A 406      27.210  22.631  -3.393  1.00 40.54           C  
ATOM   3197  OE1 GLN A 406      27.074  23.559  -4.176  1.00 39.84           O  
ATOM   3198  NE2 GLN A 406      26.451  21.530  -3.436  1.00 42.10           N  
ATOM   3199  N   SER A 407      31.487  20.797  -2.224  1.00 41.03           N  
ATOM   3200  CA  SER A 407      31.639  19.383  -2.011  1.00 39.76           C  
ATOM   3201  C   SER A 407      32.615  19.048  -0.869  1.00 39.08           C  
ATOM   3202  O   SER A 407      32.489  17.998  -0.232  1.00 38.18           O  
ATOM   3203  CB  SER A 407      32.084  18.733  -3.317  1.00 40.84           C  
ATOM   3204  OG  SER A 407      32.819  17.533  -3.079  1.00 41.03           O  
ATOM   3205  N   PHE A 408      33.610  19.905  -0.642  1.00 38.58           N  
ATOM   3206  CA  PHE A 408      34.435  19.811   0.565  1.00 38.42           C  
ATOM   3207  C   PHE A 408      33.569  19.950   1.831  1.00 37.76           C  
ATOM   3208  O   PHE A 408      33.653  19.147   2.745  1.00 38.08           O  
ATOM   3209  CB  PHE A 408      35.549  20.870   0.585  1.00 38.95           C  
ATOM   3210  CG  PHE A 408      36.596  20.614   1.642  1.00 39.73           C  
ATOM   3211  CD1 PHE A 408      37.553  19.604   1.463  1.00 41.97           C  
ATOM   3212  CD2 PHE A 408      36.620  21.365   2.814  1.00 39.75           C  
ATOM   3213  CE1 PHE A 408      38.531  19.341   2.450  1.00 42.42           C  
ATOM   3214  CE2 PHE A 408      37.579  21.116   3.807  1.00 40.19           C  
ATOM   3215  CZ  PHE A 408      38.539  20.100   3.625  1.00 39.79           C  
ATOM   3216  N   LEU A 409      32.731  20.973   1.856  1.00 37.30           N  
ATOM   3217  CA  LEU A 409      31.913  21.275   3.009  1.00 36.66           C  
ATOM   3218  C   LEU A 409      30.912  20.151   3.267  1.00 36.30           C  
ATOM   3219  O   LEU A 409      30.753  19.707   4.417  1.00 36.47           O  
ATOM   3220  CB  LEU A 409      31.232  22.635   2.813  1.00 36.82           C  
ATOM   3221  CG  LEU A 409      31.837  23.902   3.461  1.00 37.26           C  
ATOM   3222  CD1 LEU A 409      33.163  23.694   4.235  1.00 35.08           C  
ATOM   3223  CD2 LEU A 409      31.947  25.002   2.460  1.00 34.73           C  
ATOM   3224  N   GLN A 410      30.262  19.668   2.205  1.00 35.37           N  
ATOM   3225  CA  GLN A 410      29.356  18.533   2.305  1.00 34.30           C  
ATOM   3226  C   GLN A 410      30.050  17.316   2.870  1.00 35.00           C  
ATOM   3227  O   GLN A 410      29.479  16.615   3.705  1.00 35.31           O  
ATOM   3228  CB  GLN A 410      28.753  18.169   0.954  1.00 34.91           C  
ATOM   3229  CG  GLN A 410      27.773  17.001   1.034  1.00 33.80           C  
ATOM   3230  CD  GLN A 410      26.612  17.317   1.934  1.00 37.75           C  
ATOM   3231  OE1 GLN A 410      25.782  18.136   1.592  1.00 38.24           O  
ATOM   3232  NE2 GLN A 410      26.570  16.695   3.111  1.00 39.55           N  
ATOM   3233  N   SER A 411      31.276  17.063   2.414  1.00 34.56           N  
ATOM   3234  CA  SER A 411      32.036  15.917   2.877  1.00 35.76           C  
ATOM   3235  C   SER A 411      32.438  16.060   4.359  1.00 36.18           C  
ATOM   3236  O   SER A 411      32.736  15.075   5.020  1.00 35.48           O  
ATOM   3237  CB  SER A 411      33.286  15.722   2.027  1.00 35.10           C  
ATOM   3238  OG  SER A 411      32.946  15.371   0.698  1.00 37.21           O  
ATOM   3239  N   MET A 412      32.474  17.290   4.856  1.00 36.98           N  
ATOM   3240  CA  MET A 412      32.836  17.541   6.244  1.00 38.53           C  
ATOM   3241  C   MET A 412      31.623  17.261   7.116  1.00 37.34           C  
ATOM   3242  O   MET A 412      31.730  16.672   8.194  1.00 37.02           O  
ATOM   3243  CB  MET A 412      33.281  18.979   6.418  1.00 38.71           C  
ATOM   3244  CG  MET A 412      33.893  19.268   7.784  1.00 40.34           C  
ATOM   3245  SD  MET A 412      34.847  20.788   7.713  1.00 43.39           S  
ATOM   3246  CE  MET A 412      33.510  21.965   7.675  1.00 40.95           C  
ATOM   3247  N   ILE A 413      30.466  17.674   6.618  1.00 36.50           N  
ATOM   3248  CA  ILE A 413      29.212  17.403   7.266  1.00 35.72           C  
ATOM   3249  C   ILE A 413      29.079  15.888   7.486  1.00 36.82           C  
ATOM   3250  O   ILE A 413      28.717  15.436   8.582  1.00 37.45           O  
ATOM   3251  CB  ILE A 413      28.048  17.952   6.440  1.00 35.59           C  
ATOM   3252  CG1 ILE A 413      28.042  19.474   6.487  1.00 33.65           C  
ATOM   3253  CG2 ILE A 413      26.703  17.364   6.917  1.00 35.08           C  
ATOM   3254  CD1 ILE A 413      26.967  20.151   5.555  1.00 34.54           C  
ATOM   3255  N   THR A 414      29.413  15.119   6.455  1.00 35.93           N  
ATOM   3256  CA  THR A 414      29.243  13.675   6.431  1.00 35.85           C  
ATOM   3257  C   THR A 414      30.297  12.937   7.275  1.00 36.03           C  
ATOM   3258  O   THR A 414      29.978  12.082   8.103  1.00 36.37           O  
ATOM   3259  CB  THR A 414      29.314  13.188   4.956  1.00 35.75           C  
ATOM   3260  OG1 THR A 414      28.290  13.852   4.190  1.00 34.60           O  
ATOM   3261  CG2 THR A 414      29.149  11.690   4.861  1.00 35.85           C  
ATOM   3262  N   ALA A 415      31.560  13.274   7.049  1.00 35.48           N  
ATOM   3263  CA  ALA A 415      32.675  12.547   7.619  1.00 34.86           C  
ATOM   3264  C   ALA A 415      32.995  12.935   9.081  1.00 35.46           C  
ATOM   3265  O   ALA A 415      33.549  12.119   9.839  1.00 33.74           O  
ATOM   3266  CB  ALA A 415      33.897  12.755   6.737  1.00 33.73           C  
ATOM   3267  N   VAL A 416      32.682  14.191   9.436  1.00 35.81           N  
ATOM   3268  CA  VAL A 416      33.036  14.789  10.720  1.00 36.69           C  
ATOM   3269  C   VAL A 416      31.753  15.191  11.466  1.00 37.31           C  
ATOM   3270  O   VAL A 416      31.571  14.828  12.628  1.00 37.88           O  
ATOM   3271  CB  VAL A 416      33.976  16.021  10.544  1.00 37.01           C  
ATOM   3272  CG1 VAL A 416      34.268  16.710  11.895  1.00 37.50           C  
ATOM   3273  CG2 VAL A 416      35.284  15.611   9.892  1.00 37.92           C  
ATOM   3274  N   GLY A 417      30.862  15.916  10.791  1.00 37.01           N  
ATOM   3275  CA  GLY A 417      29.568  16.294  11.349  1.00 36.60           C  
ATOM   3276  C   GLY A 417      28.758  15.164  11.975  1.00 36.77           C  
ATOM   3277  O   GLY A 417      28.413  15.204  13.164  1.00 36.65           O  
ATOM   3278  N   ILE A 418      28.427  14.157  11.180  1.00 36.30           N  
ATOM   3279  CA  ILE A 418      27.640  13.046  11.681  1.00 35.89           C  
ATOM   3280  C   ILE A 418      28.315  12.380  12.897  1.00 35.96           C  
ATOM   3281  O   ILE A 418      27.707  12.341  13.950  1.00 35.92           O  
ATOM   3282  CB  ILE A 418      27.182  12.062  10.556  1.00 35.54           C  
ATOM   3283  CG1 ILE A 418      26.179  12.754   9.622  1.00 34.81           C  
ATOM   3284  CG2 ILE A 418      26.538  10.799  11.129  1.00 35.52           C  
ATOM   3285  CD1 ILE A 418      25.979  11.993   8.282  1.00 35.59           C  
ATOM   3286  N   PRO A 419      29.557  11.872  12.760  1.00 36.36           N  
ATOM   3287  CA  PRO A 419      30.216  11.248  13.930  1.00 36.69           C  
ATOM   3288  C   PRO A 419      30.485  12.169  15.137  1.00 36.75           C  
ATOM   3289  O   PRO A 419      30.488  11.695  16.258  1.00 37.00           O  
ATOM   3290  CB  PRO A 419      31.531  10.696  13.348  1.00 36.60           C  
ATOM   3291  CG  PRO A 419      31.273  10.562  11.886  1.00 35.98           C  
ATOM   3292  CD  PRO A 419      30.417  11.773  11.567  1.00 35.96           C  
ATOM   3293  N   GLU A 420      30.688  13.467  14.918  1.00 37.55           N  
ATOM   3294  CA  GLU A 420      30.805  14.416  16.021  1.00 37.03           C  
ATOM   3295  C   GLU A 420      29.484  14.521  16.768  1.00 37.07           C  
ATOM   3296  O   GLU A 420      29.471  14.355  17.983  1.00 37.68           O  
ATOM   3297  CB  GLU A 420      31.288  15.788  15.534  1.00 37.32           C  
ATOM   3298  CG  GLU A 420      31.627  16.861  16.609  1.00 38.35           C  
ATOM   3299  CD  GLU A 420      32.474  16.370  17.800  1.00 39.49           C  
ATOM   3300  OE1 GLU A 420      32.340  16.974  18.877  1.00 39.37           O  
ATOM   3301  OE2 GLU A 420      33.258  15.394  17.689  1.00 41.70           O  
ATOM   3302  N   VAL A 421      28.380  14.777  16.057  1.00 36.05           N  
ATOM   3303  CA  VAL A 421      27.064  14.938  16.689  1.00 34.67           C  
ATOM   3304  C   VAL A 421      26.628  13.665  17.430  1.00 35.00           C  
ATOM   3305  O   VAL A 421      26.033  13.709  18.515  1.00 34.83           O  
ATOM   3306  CB  VAL A 421      25.973  15.405  15.685  1.00 34.81           C  
ATOM   3307  CG1 VAL A 421      24.568  15.255  16.281  1.00 31.65           C  
ATOM   3308  CG2 VAL A 421      26.212  16.898  15.258  1.00 33.29           C  
ATOM   3309  N   MET A 422      26.956  12.521  16.866  1.00 35.09           N  
ATOM   3310  CA  MET A 422      26.648  11.273  17.551  1.00 35.20           C  
ATOM   3311  C   MET A 422      27.453  11.177  18.849  1.00 35.45           C  
ATOM   3312  O   MET A 422      26.895  10.885  19.881  1.00 35.18           O  
ATOM   3313  CB  MET A 422      26.841  10.075  16.634  1.00 34.39           C  
ATOM   3314  CG  MET A 422      25.847  10.087  15.474  1.00 34.53           C  
ATOM   3315  SD  MET A 422      25.930   8.587  14.419  1.00 35.42           S  
ATOM   3316  CE  MET A 422      25.725   7.249  15.583  1.00 37.69           C  
ATOM   3317  N   SER A 423      28.750  11.468  18.795  1.00 36.40           N  
ATOM   3318  CA  SER A 423      29.591  11.524  19.992  1.00 36.83           C  
ATOM   3319  C   SER A 423      28.996  12.460  21.066  1.00 37.22           C  
ATOM   3320  O   SER A 423      28.883  12.085  22.233  1.00 38.00           O  
ATOM   3321  CB  SER A 423      30.997  11.966  19.613  1.00 36.94           C  
ATOM   3322  OG  SER A 423      31.770  12.252  20.753  1.00 38.55           O  
ATOM   3323  N   ARG A 424      28.578  13.652  20.667  1.00 36.68           N  
ATOM   3324  CA  ARG A 424      28.029  14.604  21.616  1.00 36.90           C  
ATOM   3325  C   ARG A 424      26.739  14.092  22.219  1.00 37.56           C  
ATOM   3326  O   ARG A 424      26.428  14.373  23.374  1.00 37.90           O  
ATOM   3327  CB  ARG A 424      27.802  15.955  20.957  1.00 36.75           C  
ATOM   3328  CG  ARG A 424      29.056  16.521  20.404  1.00 36.26           C  
ATOM   3329  CD  ARG A 424      29.003  18.008  20.196  1.00 37.70           C  
ATOM   3330  NE  ARG A 424      30.350  18.464  19.873  1.00 39.74           N  
ATOM   3331  CZ  ARG A 424      30.839  19.671  20.129  1.00 44.77           C  
ATOM   3332  NH1 ARG A 424      30.102  20.591  20.728  1.00 45.96           N  
ATOM   3333  NH2 ARG A 424      32.083  19.961  19.782  1.00 46.53           N  
ATOM   3334  N   LEU A 425      25.999  13.329  21.429  1.00 37.77           N  
ATOM   3335  CA  LEU A 425      24.695  12.838  21.825  1.00 38.68           C  
ATOM   3336  C   LEU A 425      24.839  11.750  22.869  1.00 39.65           C  
ATOM   3337  O   LEU A 425      24.141  11.778  23.863  1.00 40.02           O  
ATOM   3338  CB  LEU A 425      23.925  12.322  20.615  1.00 38.17           C  
ATOM   3339  CG  LEU A 425      22.623  12.933  20.081  1.00 38.56           C  
ATOM   3340  CD1 LEU A 425      22.192  14.299  20.600  1.00 37.72           C  
ATOM   3341  CD2 LEU A 425      22.600  12.883  18.529  1.00 38.16           C  
ATOM   3342  N   GLU A 426      25.749  10.804  22.641  1.00 40.62           N  
ATOM   3343  CA  GLU A 426      26.005   9.743  23.604  1.00 41.92           C  
ATOM   3344  C   GLU A 426      26.595  10.275  24.918  1.00 41.88           C  
ATOM   3345  O   GLU A 426      26.216   9.818  25.979  1.00 42.53           O  
ATOM   3346  CB  GLU A 426      26.845   8.601  23.000  1.00 41.37           C  
ATOM   3347  CG  GLU A 426      28.299   8.916  22.670  1.00 42.87           C  
ATOM   3348  CD  GLU A 426      29.007   7.774  21.922  1.00 42.55           C  
ATOM   3349  OE1 GLU A 426      28.342   6.979  21.221  1.00 42.51           O  
ATOM   3350  OE2 GLU A 426      30.244   7.668  22.035  1.00 44.41           O  
ATOM   3351  N   VAL A 427      27.498  11.251  24.832  1.00 42.73           N  
ATOM   3352  CA  VAL A 427      28.022  11.955  26.010  1.00 42.63           C  
ATOM   3353  C   VAL A 427      26.909  12.657  26.807  1.00 43.54           C  
ATOM   3354  O   VAL A 427      26.890  12.596  28.034  1.00 43.61           O  
ATOM   3355  CB  VAL A 427      29.140  12.950  25.611  1.00 43.08           C  
ATOM   3356  CG1 VAL A 427      29.343  14.062  26.675  1.00 42.64           C  
ATOM   3357  CG2 VAL A 427      30.435  12.191  25.317  1.00 41.22           C  
ATOM   3358  N   VAL A 428      25.980  13.315  26.114  1.00 43.66           N  
ATOM   3359  CA  VAL A 428      24.868  13.986  26.778  1.00 44.09           C  
ATOM   3360  C   VAL A 428      23.896  13.023  27.493  1.00 43.97           C  
ATOM   3361  O   VAL A 428      23.524  13.258  28.648  1.00 43.83           O  
ATOM   3362  CB  VAL A 428      24.108  14.919  25.820  1.00 44.04           C  
ATOM   3363  CG1 VAL A 428      22.791  15.364  26.424  1.00 44.79           C  
ATOM   3364  CG2 VAL A 428      24.949  16.115  25.533  1.00 45.01           C  
ATOM   3365  N   PHE A 429      23.506  11.947  26.823  1.00 43.49           N  
ATOM   3366  CA  PHE A 429      22.597  10.977  27.413  1.00 43.03           C  
ATOM   3367  C   PHE A 429      23.242  10.161  28.530  1.00 42.96           C  
ATOM   3368  O   PHE A 429      22.550   9.733  29.454  1.00 42.75           O  
ATOM   3369  CB  PHE A 429      21.953  10.077  26.341  1.00 43.04           C  
ATOM   3370  CG  PHE A 429      20.826  10.742  25.609  1.00 42.63           C  
ATOM   3371  CD1 PHE A 429      21.059  11.427  24.418  1.00 42.10           C  
ATOM   3372  CD2 PHE A 429      19.537  10.726  26.132  1.00 41.96           C  
ATOM   3373  CE1 PHE A 429      20.015  12.072  23.755  1.00 41.59           C  
ATOM   3374  CE2 PHE A 429      18.493  11.364  25.486  1.00 42.19           C  
ATOM   3375  CZ  PHE A 429      18.721  12.034  24.292  1.00 42.48           C  
ATOM   3376  N   THR A 430      24.554   9.951  28.448  1.00 43.12           N  
ATOM   3377  CA  THR A 430      25.286   9.266  29.510  1.00 43.31           C  
ATOM   3378  C   THR A 430      25.362  10.134  30.770  1.00 43.37           C  
ATOM   3379  O   THR A 430      25.154   9.642  31.871  1.00 43.59           O  
ATOM   3380  CB  THR A 430      26.694   8.858  29.070  1.00 43.43           C  
ATOM   3381  OG1 THR A 430      26.600   7.945  27.971  1.00 43.50           O  
ATOM   3382  CG2 THR A 430      27.431   8.164  30.217  1.00 43.48           C  
ATOM   3383  N   ALA A 431      25.640  11.422  30.597  1.00 43.23           N  
ATOM   3384  CA  ALA A 431      25.652  12.365  31.699  1.00 43.55           C  
ATOM   3385  C   ALA A 431      24.267  12.571  32.327  1.00 44.56           C  
ATOM   3386  O   ALA A 431      24.156  12.803  33.535  1.00 45.15           O  
ATOM   3387  CB  ALA A 431      26.223  13.676  31.250  1.00 43.42           C  
ATOM   3388  N   LEU A 432      23.213  12.510  31.521  1.00 44.48           N  
ATOM   3389  CA  LEU A 432      21.856  12.557  32.060  1.00 44.86           C  
ATOM   3390  C   LEU A 432      21.603  11.332  32.926  1.00 45.07           C  
ATOM   3391  O   LEU A 432      20.948  11.426  33.953  1.00 45.56           O  
ATOM   3392  CB  LEU A 432      20.798  12.662  30.948  1.00 44.61           C  
ATOM   3393  CG  LEU A 432      20.605  14.016  30.251  1.00 45.11           C  
ATOM   3394  CD1 LEU A 432      19.689  13.836  29.036  1.00 45.94           C  
ATOM   3395  CD2 LEU A 432      20.057  15.118  31.163  1.00 43.87           C  
ATOM   3396  N   MET A 433      22.142  10.183  32.533  1.00 45.05           N  
ATOM   3397  CA  MET A 433      21.942   8.975  33.317  1.00 45.18           C  
ATOM   3398  C   MET A 433      22.707   9.051  34.646  1.00 45.04           C  
ATOM   3399  O   MET A 433      22.166   8.751  35.712  1.00 44.63           O  
ATOM   3400  CB  MET A 433      22.338   7.723  32.530  1.00 45.39           C  
ATOM   3401  CG  MET A 433      21.375   7.316  31.381  1.00 47.68           C  
ATOM   3402  SD  MET A 433      19.602   7.169  31.777  1.00 52.90           S  
ATOM   3403  CE  MET A 433      19.044   8.877  31.680  1.00 49.68           C  
ATOM   3404  N   ASN A 434      23.966   9.462  34.558  1.00 45.01           N  
ATOM   3405  CA  ASN A 434      24.870   9.496  35.695  1.00 44.68           C  
ATOM   3406  C   ASN A 434      24.364  10.400  36.799  1.00 45.12           C  
ATOM   3407  O   ASN A 434      24.358  10.012  37.973  1.00 45.55           O  
ATOM   3408  CB  ASN A 434      26.238   9.997  35.248  1.00 43.79           C  
ATOM   3409  CG  ASN A 434      27.019   8.952  34.514  1.00 42.87           C  
ATOM   3410  OD1 ASN A 434      26.664   7.751  34.511  1.00 38.59           O  
ATOM   3411  ND2 ASN A 434      28.113   9.389  33.886  1.00 39.38           N  
ATOM   3412  N   SER A 435      23.952  11.601  36.403  1.00 45.05           N  
ATOM   3413  CA  SER A 435      23.517  12.646  37.313  1.00 45.68           C  
ATOM   3414  C   SER A 435      22.234  12.303  38.065  1.00 46.01           C  
ATOM   3415  O   SER A 435      21.785  13.066  38.936  1.00 46.71           O  
ATOM   3416  CB  SER A 435      23.272  13.915  36.525  1.00 45.14           C  
ATOM   3417  OG  SER A 435      22.038  13.803  35.847  1.00 46.41           O  
ATOM   3418  N   LYS A 436      21.635  11.179  37.696  1.00 45.57           N  
ATOM   3419  CA  LYS A 436      20.386  10.742  38.268  1.00 45.23           C  
ATOM   3420  C   LYS A 436      20.556   9.422  38.987  1.00 44.96           C  
ATOM   3421  O   LYS A 436      19.581   8.854  39.478  1.00 45.34           O  
ATOM   3422  CB  LYS A 436      19.336  10.616  37.168  1.00 45.12           C  
ATOM   3423  CG  LYS A 436      18.339  11.725  37.172  1.00 45.68           C  
ATOM   3424  CD  LYS A 436      18.959  13.047  36.812  1.00 47.29           C  
ATOM   3425  CE  LYS A 436      17.942  14.168  36.955  1.00 47.52           C  
ATOM   3426  NZ  LYS A 436      17.194  14.347  35.684  1.00 48.25           N  
ATOM   3427  N   GLY A 437      21.794   8.934  39.034  1.00 44.80           N  
ATOM   3428  CA  GLY A 437      22.152   7.800  39.889  1.00 44.77           C  
ATOM   3429  C   GLY A 437      22.450   6.477  39.216  1.00 44.80           C  
ATOM   3430  O   GLY A 437      22.866   5.520  39.876  1.00 44.83           O  
ATOM   3431  N   VAL A 438      22.271   6.423  37.898  1.00 44.72           N  
ATOM   3432  CA  VAL A 438      22.389   5.175  37.137  1.00 44.46           C  
ATOM   3433  C   VAL A 438      23.788   4.532  37.237  1.00 44.51           C  
ATOM   3434  O   VAL A 438      23.922   3.307  37.262  1.00 43.85           O  
ATOM   3435  CB  VAL A 438      21.970   5.420  35.660  1.00 44.56           C  
ATOM   3436  CG1 VAL A 438      21.892   4.120  34.878  1.00 43.77           C  
ATOM   3437  CG2 VAL A 438      20.641   6.132  35.634  1.00 44.45           C  
ATOM   3438  N   SER A 439      24.810   5.380  37.293  1.00 45.07           N  
ATOM   3439  CA  SER A 439      26.200   5.000  37.509  1.00 46.68           C  
ATOM   3440  C   SER A 439      26.404   4.151  38.772  1.00 47.41           C  
ATOM   3441  O   SER A 439      27.228   3.233  38.786  1.00 47.76           O  
ATOM   3442  CB  SER A 439      27.042   6.270  37.609  1.00 46.99           C  
ATOM   3443  OG  SER A 439      26.436   7.181  38.536  1.00 49.39           O  
ATOM   3444  N   LEU A 440      25.634   4.436  39.823  1.00 48.47           N  
ATOM   3445  CA  LEU A 440      25.763   3.719  41.108  1.00 48.93           C  
ATOM   3446  C   LEU A 440      25.389   2.239  41.035  1.00 49.16           C  
ATOM   3447  O   LEU A 440      25.876   1.423  41.820  1.00 49.61           O  
ATOM   3448  CB  LEU A 440      24.938   4.410  42.197  1.00 49.09           C  
ATOM   3449  CG  LEU A 440      25.138   5.917  42.345  1.00 49.33           C  
ATOM   3450  CD1 LEU A 440      24.296   6.413  43.499  1.00 50.40           C  
ATOM   3451  CD2 LEU A 440      26.621   6.292  42.524  1.00 49.49           C  
ATOM   3452  N   PHE A 441      24.532   1.885  40.089  1.00 49.28           N  
ATOM   3453  CA  PHE A 441      24.122   0.494  39.942  1.00 49.39           C  
ATOM   3454  C   PHE A 441      25.120  -0.302  39.129  1.00 48.77           C  
ATOM   3455  O   PHE A 441      25.880   0.258  38.334  1.00 48.26           O  
ATOM   3456  CB  PHE A 441      22.732   0.405  39.311  1.00 50.18           C  
ATOM   3457  CG  PHE A 441      21.620   0.544  40.301  1.00 52.39           C  
ATOM   3458  CD1 PHE A 441      21.290   1.799  40.829  1.00 54.60           C  
ATOM   3459  CD2 PHE A 441      20.910  -0.578  40.727  1.00 53.76           C  
ATOM   3460  CE1 PHE A 441      20.270   1.932  41.766  1.00 54.60           C  
ATOM   3461  CE2 PHE A 441      19.877  -0.454  41.650  1.00 54.14           C  
ATOM   3462  CZ  PHE A 441      19.555   0.807  42.172  1.00 54.20           C  
ATOM   3463  N   ASP A 442      25.116  -1.611  39.343  1.00 48.20           N  
ATOM   3464  CA  ASP A 442      25.926  -2.515  38.557  1.00 47.93           C  
ATOM   3465  C   ASP A 442      25.027  -3.141  37.510  1.00 47.14           C  
ATOM   3466  O   ASP A 442      24.334  -4.129  37.762  1.00 46.89           O  
ATOM   3467  CB  ASP A 442      26.584  -3.582  39.439  1.00 48.56           C  
ATOM   3468  CG  ASP A 442      27.377  -4.611  38.635  1.00 50.67           C  
ATOM   3469  OD1 ASP A 442      27.999  -4.249  37.603  1.00 51.93           O  
ATOM   3470  OD2 ASP A 442      27.369  -5.799  39.037  1.00 54.54           O  
ATOM   3471  N   ILE A 443      25.040  -2.536  36.329  1.00 46.39           N  
ATOM   3472  CA  ILE A 443      24.242  -2.985  35.199  1.00 45.02           C  
ATOM   3473  C   ILE A 443      25.008  -4.062  34.441  1.00 44.30           C  
ATOM   3474  O   ILE A 443      26.099  -3.828  33.950  1.00 44.68           O  
ATOM   3475  CB  ILE A 443      23.846  -1.775  34.328  1.00 44.89           C  
ATOM   3476  CG1 ILE A 443      22.851  -0.905  35.095  1.00 44.19           C  
ATOM   3477  CG2 ILE A 443      23.232  -2.229  33.039  1.00 44.29           C  
ATOM   3478  CD1 ILE A 443      22.733   0.505  34.577  1.00 45.02           C  
ATOM   3479  N   ILE A 444      24.436  -5.250  34.361  1.00 43.71           N  
ATOM   3480  CA  ILE A 444      25.175  -6.413  33.926  1.00 43.08           C  
ATOM   3481  C   ILE A 444      24.656  -6.915  32.573  1.00 43.12           C  
ATOM   3482  O   ILE A 444      23.475  -7.306  32.447  1.00 42.00           O  
ATOM   3483  CB  ILE A 444      25.075  -7.556  34.989  1.00 43.56           C  
ATOM   3484  CG1 ILE A 444      25.607  -7.098  36.354  1.00 43.54           C  
ATOM   3485  CG2 ILE A 444      25.776  -8.820  34.521  1.00 43.00           C  
ATOM   3486  CD1 ILE A 444      25.125  -7.978  37.520  1.00 43.24           C  
ATOM   3487  N   ASN A 445      25.549  -6.916  31.574  1.00 42.39           N  
ATOM   3488  CA  ASN A 445      25.246  -7.450  30.244  1.00 42.89           C  
ATOM   3489  C   ASN A 445      23.895  -6.923  29.732  1.00 41.51           C  
ATOM   3490  O   ASN A 445      23.015  -7.708  29.370  1.00 41.81           O  
ATOM   3491  CB  ASN A 445      25.323  -8.994  30.246  1.00 43.23           C  
ATOM   3492  CG  ASN A 445      24.982  -9.629  28.882  1.00 48.03           C  
ATOM   3493  OD1 ASN A 445      25.237  -9.050  27.815  1.00 52.85           O  
ATOM   3494  ND2 ASN A 445      24.397 -10.834  28.921  1.00 50.40           N  
ATOM   3495  N   PRO A 446      23.730  -5.583  29.702  1.00 40.35           N  
ATOM   3496  CA  PRO A 446      22.473  -5.066  29.216  1.00 40.12           C  
ATOM   3497  C   PRO A 446      22.458  -5.185  27.695  1.00 40.50           C  
ATOM   3498  O   PRO A 446      23.523  -5.068  27.072  1.00 40.58           O  
ATOM   3499  CB  PRO A 446      22.536  -3.598  29.612  1.00 39.78           C  
ATOM   3500  CG  PRO A 446      23.965  -3.266  29.607  1.00 39.02           C  
ATOM   3501  CD  PRO A 446      24.670  -4.497  30.047  1.00 39.68           C  
ATOM   3502  N   GLU A 447      21.281  -5.440  27.126  1.00 40.08           N  
ATOM   3503  CA  GLU A 447      21.075  -5.442  25.680  1.00 40.81           C  
ATOM   3504  C   GLU A 447      20.114  -4.324  25.313  1.00 40.23           C  
ATOM   3505  O   GLU A 447      19.065  -4.161  25.951  1.00 40.31           O  
ATOM   3506  CB  GLU A 447      20.450  -6.752  25.227  1.00 41.37           C  
ATOM   3507  CG  GLU A 447      21.204  -8.018  25.606  1.00 45.23           C  
ATOM   3508  CD  GLU A 447      20.321  -9.252  25.417  1.00 52.36           C  
ATOM   3509  OE1 GLU A 447      19.440  -9.499  26.298  1.00 52.87           O  
ATOM   3510  OE2 GLU A 447      20.493  -9.960  24.383  1.00 53.36           O  
ATOM   3511  N   ILE A 448      20.475  -3.549  24.295  1.00 39.24           N  
ATOM   3512  CA  ILE A 448      19.557  -2.577  23.698  1.00 38.62           C  
ATOM   3513  C   ILE A 448      19.140  -3.114  22.329  1.00 38.32           C  
ATOM   3514  O   ILE A 448      19.956  -3.222  21.414  1.00 38.26           O  
ATOM   3515  CB  ILE A 448      20.198  -1.171  23.580  1.00 38.47           C  
ATOM   3516  CG1 ILE A 448      20.745  -0.729  24.940  1.00 37.67           C  
ATOM   3517  CG2 ILE A 448      19.199  -0.180  22.967  1.00 38.47           C  
ATOM   3518  CD1 ILE A 448      21.393   0.620  24.980  1.00 37.25           C  
ATOM   3519  N   ILE A 449      17.866  -3.448  22.210  1.00 38.38           N  
ATOM   3520  CA  ILE A 449      17.334  -4.190  21.091  1.00 38.31           C  
ATOM   3521  C   ILE A 449      16.213  -3.415  20.417  1.00 38.72           C  
ATOM   3522  O   ILE A 449      15.191  -3.134  21.035  1.00 38.59           O  
ATOM   3523  CB  ILE A 449      16.746  -5.524  21.581  1.00 38.61           C  
ATOM   3524  CG1 ILE A 449      17.809  -6.387  22.260  1.00 37.99           C  
ATOM   3525  CG2 ILE A 449      15.993  -6.235  20.460  1.00 37.87           C  
ATOM   3526  CD1 ILE A 449      17.203  -7.550  23.028  1.00 40.78           C  
ATOM   3527  N   THR A 450      16.386  -3.097  19.137  1.00 38.45           N  
ATOM   3528  CA  THR A 450      15.359  -2.367  18.388  1.00 38.78           C  
ATOM   3529  C   THR A 450      14.490  -3.342  17.584  1.00 38.70           C  
ATOM   3530  O   THR A 450      14.977  -4.330  17.057  1.00 38.37           O  
ATOM   3531  CB  THR A 450      15.985  -1.345  17.458  1.00 38.59           C  
ATOM   3532  OG1 THR A 450      17.055  -1.977  16.739  1.00 39.55           O  
ATOM   3533  CG2 THR A 450      16.578  -0.204  18.260  1.00 38.59           C  
ATOM   3534  N   ARG A 451      13.202  -3.053  17.521  1.00 38.43           N  
ATOM   3535  CA  ARG A 451      12.248  -3.841  16.774  1.00 39.26           C  
ATOM   3536  C   ARG A 451      11.346  -2.860  16.073  1.00 39.23           C  
ATOM   3537  O   ARG A 451      11.460  -1.648  16.301  1.00 38.82           O  
ATOM   3538  CB  ARG A 451      11.427  -4.731  17.708  1.00 39.58           C  
ATOM   3539  CG  ARG A 451      12.244  -5.865  18.377  1.00 42.38           C  
ATOM   3540  CD  ARG A 451      12.430  -7.068  17.481  1.00 46.23           C  
ATOM   3541  NE  ARG A 451      13.464  -7.961  17.998  1.00 51.48           N  
ATOM   3542  CZ  ARG A 451      14.753  -7.928  17.648  1.00 54.63           C  
ATOM   3543  NH1 ARG A 451      15.195  -7.036  16.757  1.00 56.13           N  
ATOM   3544  NH2 ARG A 451      15.613  -8.794  18.192  1.00 55.90           N  
ATOM   3545  N   ASP A 452      10.455  -3.371  15.226  1.00 39.42           N  
ATOM   3546  CA  ASP A 452       9.547  -2.529  14.477  1.00 39.83           C  
ATOM   3547  C   ASP A 452       8.508  -1.928  15.412  1.00 39.48           C  
ATOM   3548  O   ASP A 452       7.559  -2.599  15.830  1.00 39.34           O  
ATOM   3549  CB  ASP A 452       8.873  -3.287  13.318  1.00 40.73           C  
ATOM   3550  CG  ASP A 452       7.922  -2.390  12.485  1.00 44.92           C  
ATOM   3551  OD1 ASP A 452       7.970  -1.125  12.591  1.00 48.15           O  
ATOM   3552  OD2 ASP A 452       7.119  -2.957  11.705  1.00 49.23           O  
ATOM   3553  N   GLY A 453       8.713  -0.663  15.752  1.00 38.05           N  
ATOM   3554  CA  GLY A 453       7.732   0.071  16.529  1.00 37.11           C  
ATOM   3555  C   GLY A 453       8.110   0.284  17.977  1.00 36.30           C  
ATOM   3556  O   GLY A 453       7.444   1.083  18.676  1.00 36.04           O  
ATOM   3557  N   PHE A 454       9.170  -0.401  18.424  1.00 34.73           N  
ATOM   3558  CA  PHE A 454       9.606  -0.325  19.830  1.00 34.18           C  
ATOM   3559  C   PHE A 454      11.087  -0.639  20.105  1.00 35.15           C  
ATOM   3560  O   PHE A 454      11.752  -1.366  19.340  1.00 34.26           O  
ATOM   3561  CB  PHE A 454       8.703  -1.188  20.719  1.00 33.81           C  
ATOM   3562  CG  PHE A 454       8.884  -2.688  20.537  1.00 31.36           C  
ATOM   3563  CD1 PHE A 454       9.883  -3.373  21.219  1.00 32.31           C  
ATOM   3564  CD2 PHE A 454       8.032  -3.402  19.713  1.00 32.17           C  
ATOM   3565  CE1 PHE A 454      10.052  -4.775  21.078  1.00 29.93           C  
ATOM   3566  CE2 PHE A 454       8.167  -4.793  19.565  1.00 32.95           C  
ATOM   3567  CZ  PHE A 454       9.183  -5.476  20.255  1.00 32.04           C  
ATOM   3568  N   LEU A 455      11.588  -0.085  21.210  1.00 35.38           N  
ATOM   3569  CA  LEU A 455      12.940  -0.351  21.683  1.00 36.05           C  
ATOM   3570  C   LEU A 455      12.896  -1.167  22.986  1.00 37.25           C  
ATOM   3571  O   LEU A 455      11.981  -0.997  23.806  1.00 37.20           O  
ATOM   3572  CB  LEU A 455      13.697   0.960  21.871  1.00 35.38           C  
ATOM   3573  CG  LEU A 455      15.116   0.862  22.418  1.00 35.01           C  
ATOM   3574  CD1 LEU A 455      16.101   1.618  21.543  1.00 35.02           C  
ATOM   3575  CD2 LEU A 455      15.183   1.354  23.860  1.00 36.94           C  
ATOM   3576  N   LEU A 456      13.882  -2.044  23.168  1.00 38.21           N  
ATOM   3577  CA  LEU A 456      13.926  -2.968  24.305  1.00 39.59           C  
ATOM   3578  C   LEU A 456      15.198  -2.839  25.089  1.00 40.12           C  
ATOM   3579  O   LEU A 456      16.281  -2.942  24.521  1.00 39.86           O  
ATOM   3580  CB  LEU A 456      13.854  -4.416  23.827  1.00 40.10           C  
ATOM   3581  CG  LEU A 456      12.524  -5.147  23.743  1.00 41.88           C  
ATOM   3582  CD1 LEU A 456      12.831  -6.583  23.352  1.00 43.01           C  
ATOM   3583  CD2 LEU A 456      11.809  -5.111  25.068  1.00 43.31           C  
ATOM   3584  N   LEU A 457      15.065  -2.624  26.396  1.00 40.62           N  
ATOM   3585  CA  LEU A 457      16.190  -2.726  27.321  1.00 41.46           C  
ATOM   3586  C   LEU A 457      16.052  -4.001  28.156  1.00 41.66           C  
ATOM   3587  O   LEU A 457      15.012  -4.234  28.765  1.00 41.92           O  
ATOM   3588  CB  LEU A 457      16.252  -1.522  28.249  1.00 41.05           C  
ATOM   3589  CG  LEU A 457      16.501  -0.129  27.689  1.00 41.61           C  
ATOM   3590  CD1 LEU A 457      16.897   0.806  28.846  1.00 39.89           C  
ATOM   3591  CD2 LEU A 457      17.576  -0.127  26.610  1.00 42.90           C  
ATOM   3592  N   GLN A 458      17.091  -4.831  28.164  1.00 41.90           N  
ATOM   3593  CA  GLN A 458      17.098  -6.051  28.969  1.00 42.13           C  
ATOM   3594  C   GLN A 458      18.415  -6.068  29.686  1.00 42.75           C  
ATOM   3595  O   GLN A 458      19.411  -5.687  29.098  1.00 42.92           O  
ATOM   3596  CB  GLN A 458      16.970  -7.292  28.092  1.00 41.96           C  
ATOM   3597  CG  GLN A 458      16.056  -7.089  26.898  1.00 41.97           C  
ATOM   3598  CD  GLN A 458      15.613  -8.376  26.251  1.00 41.40           C  
ATOM   3599  OE1 GLN A 458      16.354  -9.356  26.190  1.00 41.39           O  
ATOM   3600  NE2 GLN A 458      14.385  -8.384  25.770  1.00 40.92           N  
ATOM   3601  N   MET A 459      18.429  -6.512  30.946  1.00 43.09           N  
ATOM   3602  CA  MET A 459      19.636  -6.458  31.780  1.00 43.56           C  
ATOM   3603  C   MET A 459      19.512  -7.228  33.105  1.00 43.84           C  
ATOM   3604  O   MET A 459      18.416  -7.524  33.584  1.00 43.46           O  
ATOM   3605  CB  MET A 459      19.985  -5.006  32.106  1.00 42.96           C  
ATOM   3606  CG  MET A 459      18.997  -4.360  33.064  1.00 43.06           C  
ATOM   3607  SD  MET A 459      19.090  -2.568  33.129  1.00 45.02           S  
ATOM   3608  CE  MET A 459      18.312  -2.153  31.573  1.00 44.12           C  
ATOM   3609  N   ASP A 460      20.661  -7.547  33.684  1.00 44.37           N  
ATOM   3610  CA  ASP A 460      20.723  -7.922  35.074  1.00 45.02           C  
ATOM   3611  C   ASP A 460      21.307  -6.740  35.792  1.00 45.57           C  
ATOM   3612  O   ASP A 460      21.841  -5.826  35.156  1.00 44.86           O  
ATOM   3613  CB  ASP A 460      21.583  -9.155  35.268  1.00 44.84           C  
ATOM   3614  CG  ASP A 460      21.073 -10.337  34.482  1.00 46.01           C  
ATOM   3615  OD1 ASP A 460      19.848 -10.575  34.473  1.00 46.54           O  
ATOM   3616  OD2 ASP A 460      21.900 -11.042  33.868  1.00 49.64           O  
ATOM   3617  N   PHE A 461      21.175  -6.748  37.115  1.00 46.78           N  
ATOM   3618  CA  PHE A 461      21.747  -5.716  37.958  1.00 48.31           C  
ATOM   3619  C   PHE A 461      22.320  -6.290  39.259  1.00 49.61           C  
ATOM   3620  O   PHE A 461      21.978  -7.390  39.694  1.00 48.61           O  
ATOM   3621  CB  PHE A 461      20.748  -4.562  38.218  1.00 48.17           C  
ATOM   3622  CG  PHE A 461      19.535  -4.956  39.031  1.00 49.50           C  
ATOM   3623  CD1 PHE A 461      18.411  -5.507  38.422  1.00 49.83           C  
ATOM   3624  CD2 PHE A 461      19.513  -4.762  40.411  1.00 50.73           C  
ATOM   3625  CE1 PHE A 461      17.298  -5.867  39.175  1.00 50.57           C  
ATOM   3626  CE2 PHE A 461      18.393  -5.121  41.172  1.00 50.74           C  
ATOM   3627  CZ  PHE A 461      17.291  -5.667  40.556  1.00 49.80           C  
ATOM   3628  N   GLY A 462      23.229  -5.531  39.842  1.00 51.94           N  
ATOM   3629  CA  GLY A 462      23.806  -5.858  41.118  1.00 55.38           C  
ATOM   3630  C   GLY A 462      23.349  -4.756  42.028  1.00 57.83           C  
ATOM   3631  O   GLY A 462      23.333  -3.580  41.640  1.00 57.76           O  
ATOM   3632  N   PHE A 463      22.968  -5.151  43.236  1.00 60.60           N  
ATOM   3633  CA  PHE A 463      22.434  -4.237  44.213  1.00 63.17           C  
ATOM   3634  C   PHE A 463      23.505  -3.939  45.253  1.00 64.89           C  
ATOM   3635  O   PHE A 463      23.813  -4.805  46.079  1.00 65.31           O  
ATOM   3636  CB  PHE A 463      21.192  -4.849  44.865  1.00 63.55           C  
ATOM   3637  CG  PHE A 463      20.253  -3.830  45.420  1.00 64.41           C  
ATOM   3638  CD1 PHE A 463      19.613  -2.925  44.572  1.00 64.14           C  
ATOM   3639  CD2 PHE A 463      20.018  -3.756  46.789  1.00 65.51           C  
ATOM   3640  CE1 PHE A 463      18.748  -1.966  45.077  1.00 65.06           C  
ATOM   3641  CE2 PHE A 463      19.152  -2.793  47.309  1.00 65.59           C  
ATOM   3642  CZ  PHE A 463      18.518  -1.895  46.451  1.00 64.86           C  
ATOM   3643  N   PRO A 464      24.098  -2.723  45.205  1.00 66.48           N  
ATOM   3644  CA  PRO A 464      25.104  -2.359  46.217  1.00 67.56           C  
ATOM   3645  C   PRO A 464      24.421  -2.258  47.586  1.00 68.36           C  
ATOM   3646  O   PRO A 464      23.697  -1.287  47.858  1.00 68.48           O  
ATOM   3647  CB  PRO A 464      25.628  -0.989  45.741  1.00 67.57           C  
ATOM   3648  CG  PRO A 464      25.158  -0.852  44.317  1.00 67.24           C  
ATOM   3649  CD  PRO A 464      23.869  -1.625  44.248  1.00 66.73           C  
ATOM   3650  N   GLU A 465      24.646  -3.278  48.415  1.00 69.08           N  
ATOM   3651  CA  GLU A 465      23.929  -3.477  49.679  1.00 70.03           C  
ATOM   3652  C   GLU A 465      23.953  -2.259  50.614  1.00 70.03           C  
ATOM   3653  O   GLU A 465      23.050  -2.084  51.432  1.00 70.14           O  
ATOM   3654  CB  GLU A 465      24.442  -4.761  50.361  1.00 70.36           C  
ATOM   3655  CG  GLU A 465      23.989  -5.005  51.803  1.00 71.95           C  
ATOM   3656  CD  GLU A 465      25.100  -4.780  52.822  1.00 74.40           C  
ATOM   3657  OE1 GLU A 465      24.888  -4.008  53.786  1.00 75.60           O  
ATOM   3658  OE2 GLU A 465      26.191  -5.379  52.665  1.00 75.31           O  
ATOM   3659  N   HIS A 466      24.962  -1.404  50.444  1.00 69.99           N  
ATOM   3660  CA  HIS A 466      25.104  -0.163  51.206  1.00 69.88           C  
ATOM   3661  C   HIS A 466      24.129   0.937  50.775  1.00 69.49           C  
ATOM   3662  O   HIS A 466      23.912   1.896  51.521  1.00 69.49           O  
ATOM   3663  CB  HIS A 466      26.547   0.359  51.111  1.00 70.30           C  
ATOM   3664  CG  HIS A 466      26.830   1.131  49.860  1.00 71.24           C  
ATOM   3665  ND1 HIS A 466      27.225   0.526  48.685  1.00 72.74           N  
ATOM   3666  CD2 HIS A 466      26.759   2.458  49.594  1.00 72.53           C  
ATOM   3667  CE1 HIS A 466      27.392   1.448  47.752  1.00 73.06           C  
ATOM   3668  NE2 HIS A 466      27.111   2.628  48.276  1.00 72.84           N  
ATOM   3669  N   LEU A 467      23.565   0.817  49.572  1.00 69.12           N  
ATOM   3670  CA  LEU A 467      22.620   1.818  49.057  1.00 68.59           C  
ATOM   3671  C   LEU A 467      21.275   1.749  49.768  1.00 68.03           C  
ATOM   3672  O   LEU A 467      20.639   2.772  49.996  1.00 67.88           O  
ATOM   3673  CB  LEU A 467      22.419   1.681  47.539  1.00 68.84           C  
ATOM   3674  CG  LEU A 467      23.394   2.376  46.575  1.00 69.41           C  
ATOM   3675  CD1 LEU A 467      23.084   1.981  45.128  1.00 69.24           C  
ATOM   3676  CD2 LEU A 467      23.398   3.912  46.736  1.00 69.02           C  
ATOM   3677  N   LEU A 468      20.843   0.539  50.115  1.00 67.75           N  
ATOM   3678  CA  LEU A 468      19.614   0.375  50.874  1.00 67.57           C  
ATOM   3679  C   LEU A 468      19.797   0.811  52.329  1.00 67.49           C  
ATOM   3680  O   LEU A 468      18.900   1.432  52.906  1.00 67.30           O  
ATOM   3681  CB  LEU A 468      19.088  -1.063  50.796  1.00 67.61           C  
ATOM   3682  CG  LEU A 468      17.665  -1.212  51.357  1.00 67.34           C  
ATOM   3683  CD1 LEU A 468      16.683  -0.327  50.608  1.00 66.87           C  
ATOM   3684  CD2 LEU A 468      17.203  -2.649  51.336  1.00 68.66           C  
ATOM   3685  N   VAL A 469      20.960   0.491  52.899  1.00 67.50           N  
ATOM   3686  CA  VAL A 469      21.322   0.908  54.264  1.00 67.80           C  
ATOM   3687  C   VAL A 469      21.236   2.423  54.434  1.00 67.98           C  
ATOM   3688  O   VAL A 469      20.608   2.910  55.372  1.00 67.91           O  
ATOM   3689  CB  VAL A 469      22.740   0.409  54.671  1.00 67.56           C  
ATOM   3690  CG1 VAL A 469      23.110   0.889  56.070  1.00 67.56           C  
ATOM   3691  CG2 VAL A 469      22.802  -1.097  54.627  1.00 67.41           C  
ATOM   3692  N   ASP A 470      21.856   3.154  53.513  1.00 68.60           N  
ATOM   3693  CA  ASP A 470      21.880   4.610  53.555  1.00 69.25           C  
ATOM   3694  C   ASP A 470      20.505   5.242  53.336  1.00 69.44           C  
ATOM   3695  O   ASP A 470      20.212   6.280  53.926  1.00 69.82           O  
ATOM   3696  CB  ASP A 470      22.887   5.165  52.541  1.00 69.53           C  
ATOM   3697  CG  ASP A 470      24.343   4.917  52.947  1.00 70.75           C  
ATOM   3698  OD1 ASP A 470      25.221   5.639  52.429  1.00 72.33           O  
ATOM   3699  OD2 ASP A 470      24.625   4.012  53.772  1.00 71.81           O  
ATOM   3700  N   PHE A 471      19.677   4.619  52.493  1.00 69.44           N  
ATOM   3701  CA  PHE A 471      18.317   5.101  52.203  1.00 69.20           C  
ATOM   3702  C   PHE A 471      17.404   4.995  53.419  1.00 69.79           C  
ATOM   3703  O   PHE A 471      16.732   5.956  53.776  1.00 69.75           O  
ATOM   3704  CB  PHE A 471      17.720   4.341  51.004  1.00 68.54           C  
ATOM   3705  CG  PHE A 471      16.240   4.550  50.815  1.00 67.06           C  
ATOM   3706  CD1 PHE A 471      15.332   3.544  51.148  1.00 66.14           C  
ATOM   3707  CD2 PHE A 471      15.751   5.741  50.295  1.00 65.69           C  
ATOM   3708  CE1 PHE A 471      13.966   3.728  50.977  1.00 64.76           C  
ATOM   3709  CE2 PHE A 471      14.381   5.931  50.121  1.00 65.26           C  
ATOM   3710  CZ  PHE A 471      13.492   4.923  50.462  1.00 65.07           C  
ATOM   3711  N   LEU A 472      17.378   3.810  54.028  1.00 70.73           N  
ATOM   3712  CA  LEU A 472      16.678   3.561  55.286  1.00 71.83           C  
ATOM   3713  C   LEU A 472      17.187   4.485  56.418  1.00 73.16           C  
ATOM   3714  O   LEU A 472      16.400   5.009  57.213  1.00 73.47           O  
ATOM   3715  CB  LEU A 472      16.833   2.087  55.674  1.00 71.20           C  
ATOM   3716  CG  LEU A 472      15.840   0.990  55.260  1.00 70.20           C  
ATOM   3717  CD1 LEU A 472      14.930   1.333  54.092  1.00 69.26           C  
ATOM   3718  CD2 LEU A 472      16.576  -0.315  54.994  1.00 69.23           C  
ATOM   3719  N   GLN A 473      18.503   4.681  56.476  1.00 74.65           N  
ATOM   3720  CA  GLN A 473      19.122   5.624  57.410  1.00 75.98           C  
ATOM   3721  C   GLN A 473      18.673   7.065  57.136  1.00 76.56           C  
ATOM   3722  O   GLN A 473      18.491   7.847  58.069  1.00 76.80           O  
ATOM   3723  CB  GLN A 473      20.654   5.508  57.349  1.00 76.06           C  
ATOM   3724  CG  GLN A 473      21.438   6.472  58.257  1.00 77.35           C  
ATOM   3725  CD  GLN A 473      21.189   6.245  59.745  1.00 78.99           C  
ATOM   3726  OE1 GLN A 473      21.061   5.105  60.204  1.00 79.40           O  
ATOM   3727  NE2 GLN A 473      21.126   7.336  60.508  1.00 79.29           N  
ATOM   3728  N   SER A 474      18.489   7.402  55.859  1.00 77.31           N  
ATOM   3729  CA  SER A 474      18.045   8.742  55.466  1.00 78.08           C  
ATOM   3730  C   SER A 474      16.552   8.985  55.731  1.00 78.50           C  
ATOM   3731  O   SER A 474      16.081  10.119  55.622  1.00 78.41           O  
ATOM   3732  CB  SER A 474      18.415   9.053  53.999  1.00 78.06           C  
ATOM   3733  OG  SER A 474      17.495   8.491  53.077  1.00 78.18           O  
ATOM   3734  N   LEU A 475      15.818   7.930  56.095  1.00 79.27           N  
ATOM   3735  CA  LEU A 475      14.385   8.063  56.410  1.00 80.11           C  
ATOM   3736  C   LEU A 475      14.133   8.931  57.649  1.00 80.66           C  
ATOM   3737  O   LEU A 475      13.031   9.460  57.829  1.00 80.80           O  
ATOM   3738  CB  LEU A 475      13.703   6.692  56.572  1.00 80.02           C  
ATOM   3739  CG  LEU A 475      13.502   5.776  55.356  1.00 79.71           C  
ATOM   3740  CD1 LEU A 475      12.605   4.631  55.755  1.00 79.25           C  
ATOM   3741  CD2 LEU A 475      12.916   6.506  54.157  1.00 78.96           C  
ATOM   3742  N   SER A 476      15.154   9.053  58.500  1.00 81.30           N  
ATOM   3743  CA  SER A 476      15.131   9.976  59.640  1.00 81.83           C  
ATOM   3744  C   SER A 476      15.866  11.281  59.290  1.00 81.96           C  
ATOM   3745  O   SER A 476      15.311  12.137  58.591  1.00 81.98           O  
ATOM   3746  CB  SER A 476      15.731   9.322  60.894  1.00 81.85           C  
ATOM   3747  OG  SER A 476      17.107   9.023  60.707  1.00 82.07           O  
ATOM   3748  OXT SER A 476      17.022  11.509  59.676  1.00 82.01           O  
TER    3749      SER A 476                                                      
HETATM 3750  C1  NAG B   1      27.595  32.523  -5.225  1.00 58.78           C  
HETATM 3751  C2  NAG B   1      27.403  34.036  -5.323  1.00 60.68           C  
HETATM 3752  C3  NAG B   1      26.965  34.490  -6.721  1.00 63.39           C  
HETATM 3753  C4  NAG B   1      27.590  33.735  -7.909  1.00 65.47           C  
HETATM 3754  C5  NAG B   1      28.051  32.311  -7.545  1.00 63.62           C  
HETATM 3755  C6  NAG B   1      29.159  31.872  -8.494  1.00 62.81           C  
HETATM 3756  C7  NAG B   1      26.602  35.601  -3.604  1.00 59.00           C  
HETATM 3757  C8  NAG B   1      25.344  36.293  -3.170  1.00 58.73           C  
HETATM 3758  N2  NAG B   1      26.434  34.513  -4.346  1.00 59.20           N  
HETATM 3759  O3  NAG B   1      27.280  35.865  -6.834  1.00 64.05           O  
HETATM 3760  O4  NAG B   1      26.659  33.645  -8.999  1.00 69.89           O  
HETATM 3761  O5  NAG B   1      28.537  32.179  -6.215  1.00 60.55           O  
HETATM 3762  O6  NAG B   1      29.239  30.464  -8.498  1.00 63.52           O  
HETATM 3763  O7  NAG B   1      27.707  36.039  -3.270  1.00 59.88           O  
HETATM 3764  C1  NDG B   2      26.658  34.666 -10.064  1.00 72.02           C  
HETATM 3765  C2  NDG B   2      27.285  34.175 -11.401  1.00 73.08           C  
HETATM 3766  C3  NDG B   2      28.714  34.699 -11.554  1.00 74.66           C  
HETATM 3767  C4  NDG B   2      28.659  36.219 -11.492  1.00 75.17           C  
HETATM 3768  C5  NDG B   2      28.278  36.570 -10.047  1.00 74.29           C  
HETATM 3769  C6  NDG B   2      28.303  38.082  -9.800  1.00 74.00           C  
HETATM 3770  C7  NDG B   2      26.227  31.991 -11.915  1.00 72.17           C  
HETATM 3771  C8  NDG B   2      26.542  30.657 -12.530  1.00 72.14           C  
HETATM 3772  O5  NDG B   2      27.001  36.018  -9.700  1.00 73.23           O  
HETATM 3773  O3  NDG B   2      29.311  34.274 -12.758  1.00 75.66           O  
HETATM 3774  O4  NDG B   2      29.894  36.784 -11.900  1.00 75.40           O  
HETATM 3775  O6  NDG B   2      27.043  38.657 -10.058  1.00 73.43           O  
HETATM 3776  O7  NDG B   2      25.056  32.330 -11.716  1.00 72.18           O  
HETATM 3777  N2  NDG B   2      27.287  32.731 -11.590  1.00 72.44           N  
HETATM 3778  C1  FUC B   3      28.836  29.359  -9.117  1.00 61.95           C  
HETATM 3779  C2  FUC B   3      29.403  27.980  -8.805  1.00 61.29           C  
HETATM 3780  C3  FUC B   3      28.780  27.428  -7.528  1.00 60.86           C  
HETATM 3781  C4  FUC B   3      27.260  27.463  -7.576  1.00 61.20           C  
HETATM 3782  C5  FUC B   3      26.770  28.864  -7.940  1.00 62.26           C  
HETATM 3783  C6  FUC B   3      25.248  28.906  -8.089  1.00 63.04           C  
HETATM 3784  O2  FUC B   3      30.821  28.071  -8.636  1.00 61.52           O  
HETATM 3785  O3  FUC B   3      29.198  26.077  -7.340  1.00 61.02           O  
HETATM 3786  O4  FUC B   3      26.793  26.501  -8.527  1.00 60.56           O  
HETATM 3787  O5  FUC B   3      27.403  29.322  -9.147  1.00 63.54           O  
HETATM 3788 CL    CL A 493       9.366  -9.721  94.840  1.00 35.33          CL  
HETATM 3789  O2  2OB A 485       9.149   2.915  38.598  1.00 47.97           O  
HETATM 3790  C48 2OB A 485       8.457   2.313  37.818  1.00 47.89           C  
HETATM 3791  O1  2OB A 485       7.932   1.007  38.205  1.00 49.63           O  
HETATM 3792  C3  2OB A 485       8.169   0.705  39.574  1.00 50.39           C  
HETATM 3793  C2  2OB A 485       6.812   0.458  40.221  1.00 50.92           C  
HETATM 3794  C4  2OB A 485       9.039  -0.543  39.642  1.00 51.40           C  
HETATM 3795  C5  2OB A 485       9.047  -1.109  41.049  1.00 51.57           C  
HETATM 3796  C10 2OB A 485       7.735  -1.380  41.759  1.00 51.76           C  
HETATM 3797  C9  2OB A 485       8.000  -1.678  43.241  1.00 51.94           C  
HETATM 3798  C11 2OB A 485       6.703  -2.022  44.008  1.00 51.99           C  
HETATM 3799  C12 2OB A 485       6.887  -2.515  45.451  1.00 52.10           C  
HETATM 3800  C13 2OB A 485       7.997  -3.549  45.603  1.00 51.75           C  
HETATM 3801  C18 2OB A 485       7.558  -4.882  44.974  1.00 50.85           C  
HETATM 3802  C17 2OB A 485       8.515  -3.755  47.042  1.00 51.35           C  
HETATM 3803  C20 2OB A 485       7.752  -4.713  47.979  1.00 49.14           C  
HETATM 3804  C22 2OB A 485       8.454  -4.759  49.342  1.00 47.61           C  
HETATM 3805  C23 2OB A 485       7.949  -5.839  50.290  1.00 46.67           C  
HETATM 3806  C24 2OB A 485       8.998  -6.071  51.370  1.00 45.85           C  
HETATM 3807  C25 2OB A 485       8.447  -6.548  52.705  1.00 45.11           C  
HETATM 3808  C27 2OB A 485       7.366  -7.591  52.574  1.00 42.19           C  
HETATM 3809  C26 2OB A 485       9.563  -7.128  53.561  1.00 44.97           C  
HETATM 3810  C21 2OB A 485       6.300  -4.287  48.148  1.00 46.88           C  
HETATM 3811  C16 2OB A 485       9.996  -4.144  46.900  1.00 51.80           C  
HETATM 3812  C15 2OB A 485      10.412  -3.824  45.457  1.00 52.24           C  
HETATM 3813  C14 2OB A 485       9.248  -2.977  44.946  1.00 52.54           C  
HETATM 3814  C8  2OB A 485       9.111  -2.723  43.438  1.00 52.87           C  
HETATM 3815  C7  2OB A 485      10.439  -2.314  42.786  1.00 52.60           C  
HETATM 3816  C6  2OB A 485      10.235  -1.339  41.639  1.00 52.22           C  
HETATM 3817  C19 2OB A 485       7.005  -2.545  41.077  1.00 50.45           C  
HETATM 3818  C1  2OB A 485       6.896  -0.109  41.639  1.00 51.15           C  
HETATM 3819  C47 2OB A 485       8.168   2.939  36.480  1.00 47.65           C  
HETATM 3820  C46 2OB A 485       9.269   2.606  35.486  1.00 48.16           C  
HETATM 3821  C45 2OB A 485       9.337   3.633  34.358  1.00 47.99           C  
HETATM 3822  C44 2OB A 485      10.446   3.264  33.382  1.00 47.77           C  
HETATM 3823  C43 2OB A 485      11.603   4.257  33.405  1.00 49.08           C  
HETATM 3824  C42 2OB A 485      12.824   3.558  32.833  1.00 50.22           C  
HETATM 3825  C41 2OB A 485      14.128   4.313  33.049  1.00 52.52           C  
HETATM 3826  C40 2OB A 485      14.997   4.123  31.817  1.00 54.69           C  
HETATM 3827  C39 2OB A 485      16.316   3.878  31.793  1.00 55.85           C  
HETATM 3828  C38 2OB A 485      17.206   3.736  33.006  1.00 56.70           C  
HETATM 3829  C37 2OB A 485      17.625   2.274  33.090  1.00 58.17           C  
HETATM 3830  C36 2OB A 485      18.622   2.066  34.218  1.00 58.80           C  
HETATM 3831  C35 2OB A 485      18.122   1.005  35.185  1.00 59.23           C  
HETATM 3832  C34 2OB A 485      19.017   0.975  36.408  1.00 59.48           C  
HETATM 3833  C33 2OB A 485      18.295   0.336  37.579  1.00 60.18           C  
HETATM 3834  C32 2OB A 485      18.834  -1.064  37.812  1.00 61.26           C  
HETATM 3835  C31 2OB A 485      18.006  -1.751  38.868  1.00 63.08           C  
HETATM 3836  O2  2OB A 486      22.541   9.742  16.934  1.00 35.45           O  
HETATM 3837  C48 2OB A 486      21.458  10.061  16.500  1.00 34.48           C  
HETATM 3838  O1  2OB A 486      20.264   9.608  17.161  1.00 37.37           O  
HETATM 3839  C3  2OB A 486      20.475   8.886  18.365  1.00 36.50           C  
HETATM 3840  C2  2OB A 486      20.234   9.852  19.523  1.00 37.20           C  
HETATM 3841  C4  2OB A 486      19.432   7.774  18.335  1.00 37.05           C  
HETATM 3842  C5  2OB A 486      19.214   7.165  19.700  1.00 37.79           C  
HETATM 3843  C10 2OB A 486      19.093   8.056  20.929  1.00 38.50           C  
HETATM 3844  C9  2OB A 486      19.323   7.246  22.216  1.00 39.66           C  
HETATM 3845  C11 2OB A 486      18.839   7.985  23.479  1.00 41.09           C  
HETATM 3846  C12 2OB A 486      19.307   7.232  24.729  1.00 41.14           C  
HETATM 3847  C13 2OB A 486      18.700   5.834  24.740  1.00 42.44           C  
HETATM 3848  C18 2OB A 486      17.167   5.905  24.775  1.00 43.28           C  
HETATM 3849  C17 2OB A 486      19.172   4.859  25.821  1.00 45.07           C  
HETATM 3850  C20 2OB A 486      18.832   5.098  27.317  1.00 45.72           C  
HETATM 3851  C22 2OB A 486      19.891   4.460  28.199  1.00 48.32           C  
HETATM 3852  C23 2OB A 486      19.424   3.136  28.781  1.00 49.41           C  
HETATM 3853  C24 2OB A 486      20.638   2.253  29.074  1.00 49.08           C  
HETATM 3854  C25 2OB A 486      20.656   1.830  30.535  1.00 47.23           C  
HETATM 3855  C27 2OB A 486      21.178   0.409  30.672  1.00 47.02           C  
HETATM 3856  C26 2OB A 486      21.503   2.808  31.330  1.00 46.08           C  
HETATM 3857  C21 2OB A 486      18.767   6.549  27.781  1.00 46.28           C  
HETATM 3858  C16 2OB A 486      18.653   3.517  25.265  1.00 44.68           C  
HETATM 3859  C15 2OB A 486      18.587   3.682  23.738  1.00 43.54           C  
HETATM 3860  C14 2OB A 486      19.157   5.078  23.503  1.00 41.65           C  
HETATM 3861  C8  2OB A 486      18.833   5.786  22.175  1.00 40.90           C  
HETATM 3862  C7  2OB A 486      19.449   5.054  20.993  1.00 40.94           C  
HETATM 3863  C6  2OB A 486      19.150   5.827  19.740  1.00 38.34           C  
HETATM 3864  C19 2OB A 486      17.733   8.782  20.910  1.00 39.28           C  
HETATM 3865  C1  2OB A 486      20.187   9.123  20.868  1.00 36.95           C  
HETATM 3866  C47 2OB A 486      21.265  10.927  15.292  1.00 34.52           C  
HETATM 3867  C46 2OB A 486      22.553  11.313  14.588  1.00 32.87           C  
HETATM 3868  C45 2OB A 486      22.268  12.687  13.965  1.00 32.81           C  
HETATM 3869  C44 2OB A 486      23.597  13.246  13.499  1.00 32.93           C  
HETATM 3870  C43 2OB A 486      23.428  13.858  12.142  1.00 36.35           C  
HETATM 3871  C42 2OB A 486      23.147  15.330  12.273  1.00 38.07           C  
HETATM 3872  C41 2OB A 486      24.484  16.029  12.095  1.00 40.28           C  
HETATM 3873  C40 2OB A 486      24.191  17.198  11.204  1.00 39.74           C  
HETATM 3874  C39 2OB A 486      25.130  18.031  10.801  1.00 41.45           C  
HETATM 3875  C38 2OB A 486      26.563  17.913  11.221  1.00 42.40           C  
HETATM 3876  C37 2OB A 486      27.188  19.241  10.840  1.00 44.07           C  
HETATM 3877  C36 2OB A 486      28.194  19.648  11.895  1.00 46.84           C  
HETATM 3878  C35 2OB A 486      29.201  20.598  11.278  1.00 49.50           C  
HETATM 3879  C34 2OB A 486      30.395  19.801  10.795  1.00 50.90           C  
HETATM 3880  C33 2OB A 486      31.661  20.604  10.986  1.00 51.83           C  
HETATM 3881  C32 2OB A 486      32.504  19.931  12.052  1.00 54.46           C  
HETATM 3882  C31 2OB A 486      33.953  20.306  11.843  1.00 55.76           C  
HETATM 3883  C1  PCW A 487      21.493   7.442  45.969  1.00 90.16           C  
HETATM 3884  C2  PCW A 487      20.232   7.176  45.140  1.00 86.57           C  
HETATM 3885  C3  PCW A 487      20.576   6.565  43.777  1.00 86.41           C  
HETATM 3886  C4  PCW A 487      20.724  11.160  44.624  1.00 98.81           C  
HETATM 3887  C5  PCW A 487      21.542  10.317  43.639  1.00 99.16           C  
HETATM 3888  C6  PCW A 487      22.413  11.934  42.105  1.00 99.45           C  
HETATM 3889  C7  PCW A 487      23.655   9.956  42.565  1.00 99.36           C  
HETATM 3890  C8  PCW A 487      23.524  11.653  44.231  1.00 99.33           C  
HETATM 3891  C11 PCW A 487      19.412   5.388  41.884  1.00 85.29           C  
HETATM 3892  C12 PCW A 487      18.139   5.031  41.150  1.00 83.20           C  
HETATM 3893  C13 PCW A 487      17.391   3.933  41.904  1.00 80.83           C  
HETATM 3894  C14 PCW A 487      15.926   3.816  41.487  1.00 78.28           C  
HETATM 3895  C15 PCW A 487      15.695   2.844  40.335  1.00 75.67           C  
HETATM 3896  C16 PCW A 487      15.756   3.574  38.996  1.00 73.90           C  
HETATM 3897  C17 PCW A 487      14.401   3.665  38.302  1.00 71.41           C  
HETATM 3898  C18 PCW A 487      14.335   2.697  37.128  1.00 68.82           C  
HETATM 3899  C19 PCW A 487      12.968   2.059  37.118  1.00 66.98           C  
HETATM 3900  C20 PCW A 487      12.743   0.814  37.531  1.00 64.88           C  
HETATM 3901  C21 PCW A 487      13.840  -0.077  38.044  1.00 63.62           C  
HETATM 3902  C22 PCW A 487      13.201  -1.288  38.701  1.00 63.21           C  
HETATM 3903  C23 PCW A 487      14.264  -2.104  39.426  1.00 63.51           C  
HETATM 3904  C24 PCW A 487      13.954  -2.227  40.906  1.00 63.64           C  
HETATM 3905  C25 PCW A 487      15.196  -2.598  41.700  1.00 64.71           C  
HETATM 3906  C26 PCW A 487      16.075  -1.395  42.018  1.00 66.01           C  
HETATM 3907  C27 PCW A 487      15.339  -0.333  42.822  1.00 67.15           C  
HETATM 3908  C28 PCW A 487      16.328   0.635  43.437  1.00 68.45           C  
HETATM 3909  C31 PCW A 487      19.288   5.009  46.036  1.00 78.84           C  
HETATM 3910  C32 PCW A 487      18.255   4.337  46.900  1.00 75.11           C  
HETATM 3911  C33 PCW A 487      18.393   2.823  46.825  1.00 70.75           C  
HETATM 3912  C34 PCW A 487      17.429   2.158  47.795  1.00 66.86           C  
HETATM 3913  C35 PCW A 487      15.984   2.280  47.316  1.00 63.52           C  
HETATM 3914  C36 PCW A 487      15.366   0.900  47.140  1.00 59.78           C  
HETATM 3915  C37 PCW A 487      13.863   0.981  46.915  1.00 56.69           C  
HETATM 3916  C38 PCW A 487      13.248  -0.384  46.612  1.00 54.32           C  
HETATM 3917  C39 PCW A 487      14.325  -1.362  46.207  1.00 53.51           C  
HETATM 3918  C40 PCW A 487      14.467  -2.572  46.757  1.00 52.23           C  
HETATM 3919  C41 PCW A 487      13.544  -3.083  47.833  1.00 49.80           C  
HETATM 3920  C42 PCW A 487      14.288  -4.003  48.783  1.00 47.03           C  
HETATM 3921  C43 PCW A 487      13.236  -4.783  49.561  1.00 46.37           C  
HETATM 3922  C44 PCW A 487      13.509  -6.275  49.511  1.00 44.47           C  
HETATM 3923  C45 PCW A 487      12.212  -7.060  49.567  1.00 43.84           C  
HETATM 3924  C46 PCW A 487      12.141  -7.954  48.348  1.00 42.67           C  
HETATM 3925  C47 PCW A 487      10.925  -8.852  48.391  1.00 43.27           C  
HETATM 3926  C48 PCW A 487      10.577  -9.252  46.973  1.00 44.72           C  
HETATM 3927  N   PCW A 487      22.775  10.974  43.155  1.00 99.34           N  
HETATM 3928  O2  PCW A 487      19.257   6.470  45.940  1.00 82.69           O  
HETATM 3929  O3  PCW A 487      19.374   6.232  43.075  1.00 86.10           O  
HETATM 3930  O11 PCW A 487      20.488   4.969  41.478  1.00 86.39           O  
HETATM 3931  O31 PCW A 487      20.117   4.334  45.448  1.00 79.11           O  
HETATM 3932  O1P PCW A 487      18.749   8.714  47.381  1.00 96.31           O  
HETATM 3933  O2P PCW A 487      20.465  10.842  47.830  1.00 97.39           O  
HETATM 3934  O3P PCW A 487      21.474   8.747  46.570  1.00 94.48           O  
HETATM 3935  O4P PCW A 487      19.816  10.316  45.337  1.00 97.92           O  
HETATM 3936  P   PCW A 487      20.146   9.669  46.791  1.00 97.49           P  
HETATM 3937  C1  PCW A 488      22.140  18.306  24.284  1.00 76.94           C  
HETATM 3938  C2  PCW A 488      21.677  18.052  22.856  1.00 72.29           C  
HETATM 3939  C3  PCW A 488      22.599  17.010  22.219  1.00 70.97           C  
HETATM 3940  C4  PCW A 488      22.377  22.662  23.479  1.00 85.77           C  
HETATM 3941  C5  PCW A 488      21.605  23.850  22.891  1.00 85.87           C  
HETATM 3942  C6  PCW A 488      20.956  24.999  24.941  1.00 86.05           C  
HETATM 3943  C7  PCW A 488      21.041  26.168  22.858  1.00 85.93           C  
HETATM 3944  C8  PCW A 488      23.072  25.530  23.925  1.00 86.23           C  
HETATM 3945  C11 PCW A 488      24.384  17.926  20.630  1.00 67.54           C  
HETATM 3946  C12 PCW A 488      23.821  17.316  19.369  1.00 64.11           C  
HETATM 3947  C13 PCW A 488      22.622  18.107  18.880  1.00 61.93           C  
HETATM 3948  C14 PCW A 488      23.043  19.144  17.858  1.00 58.45           C  
HETATM 3949  C15 PCW A 488      22.740  18.621  16.467  1.00 56.84           C  
HETATM 3950  C16 PCW A 488      21.582  19.377  15.846  1.00 54.47           C  
HETATM 3951  C17 PCW A 488      21.007  18.588  14.682  1.00 55.05           C  
HETATM 3952  C18 PCW A 488      20.930  17.093  14.964  1.00 55.50           C  
HETATM 3953  C19 PCW A 488      19.554  16.579  14.637  1.00 55.84           C  
HETATM 3954  C20 PCW A 488      18.948  15.604  15.314  1.00 55.99           C  
HETATM 3955  C21 PCW A 488      19.576  14.897  16.487  1.00 56.26           C  
HETATM 3956  C22 PCW A 488      18.821  13.608  16.754  1.00 56.58           C  
HETATM 3957  C23 PCW A 488      17.642  13.856  17.672  1.00 57.28           C  
HETATM 3958  C24 PCW A 488      17.788  13.085  18.974  1.00 58.34           C  
HETATM 3959  C25 PCW A 488      17.653  14.039  20.154  1.00 58.33           C  
HETATM 3960  C26 PCW A 488      16.302  13.880  20.843  1.00 58.32           C  
HETATM 3961  C27 PCW A 488      16.215  12.511  21.501  1.00 59.36           C  
HETATM 3962  C28 PCW A 488      14.895  11.848  21.182  1.00 58.44           C  
HETATM 3963  C31 PCW A 488      19.637  16.694  23.494  1.00 67.02           C  
HETATM 3964  C32 PCW A 488      18.133  16.546  23.434  1.00 64.59           C  
HETATM 3965  C33 PCW A 488      17.617  15.450  24.362  1.00 62.00           C  
HETATM 3966  C34 PCW A 488      17.584  15.928  25.810  1.00 60.07           C  
HETATM 3967  C35 PCW A 488      16.372  15.404  26.566  1.00 57.71           C  
HETATM 3968  C36 PCW A 488      16.531  15.753  28.041  1.00 57.25           C  
HETATM 3969  C37 PCW A 488      15.452  15.133  28.925  1.00 55.57           C  
HETATM 3970  C38 PCW A 488      15.943  13.850  29.584  1.00 54.48           C  
HETATM 3971  C39 PCW A 488      14.885  12.828  29.283  1.00 54.35           C  
HETATM 3972  C40 PCW A 488      15.129  11.545  29.084  1.00 53.97           C  
HETATM 3973  C41 PCW A 488      16.515  10.979  29.143  1.00 55.88           C  
HETATM 3974  C42 PCW A 488      16.602   9.801  28.181  1.00 58.37           C  
HETATM 3975  C43 PCW A 488      15.250   9.155  27.905  1.00 59.24           C  
HETATM 3976  C44 PCW A 488      15.342   7.668  28.224  1.00 62.42           C  
HETATM 3977  C45 PCW A 488      14.715   6.794  27.138  1.00 63.62           C  
HETATM 3978  C46 PCW A 488      13.237   7.120  26.921  1.00 64.98           C  
HETATM 3979  C47 PCW A 488      12.841   7.029  25.453  1.00 65.72           C  
HETATM 3980  C48 PCW A 488      12.719   8.413  24.858  1.00 65.88           C  
HETATM 3981  N   PCW A 488      21.680  25.114  23.660  1.00 86.07           N  
HETATM 3982  O2  PCW A 488      20.256  17.842  22.823  1.00 69.83           O  
HETATM 3983  O3  PCW A 488      23.797  17.741  21.949  1.00 68.47           O  
HETATM 3984  O11 PCW A 488      25.397  18.596  20.564  1.00 70.32           O  
HETATM 3985  O31 PCW A 488      20.303  15.863  24.085  1.00 68.87           O  
HETATM 3986  O1P PCW A 488      20.688  20.062  26.286  1.00 83.35           O  
HETATM 3987  O2P PCW A 488      23.221  21.256  26.228  1.00 85.65           O  
HETATM 3988  O3P PCW A 488      22.671  19.622  24.303  1.00 82.02           O  
HETATM 3989  O4P PCW A 488      21.490  21.854  24.262  1.00 85.53           O  
HETATM 3990  P   PCW A 488      22.032  20.721  25.294  1.00 85.49           P  
HETATM 3991  N1  EPE A 489      19.291  -0.485  81.953  1.00 79.57           N  
HETATM 3992  C2  EPE A 489      19.681  -0.482  83.380  1.00 80.14           C  
HETATM 3993  C3  EPE A 489      19.156   0.769  84.079  1.00 80.71           C  
HETATM 3994  N4  EPE A 489      17.692   0.855  83.939  1.00 81.03           N  
HETATM 3995  C5  EPE A 489      17.301   0.881  82.515  1.00 80.96           C  
HETATM 3996  C6  EPE A 489      17.828  -0.360  81.791  1.00 80.05           C  
HETATM 3997  C7  EPE A 489      17.236   2.097  84.585  1.00 82.10           C  
HETATM 3998  C8  EPE A 489      16.560   1.796  85.922  1.00 82.68           C  
HETATM 3999  O8  EPE A 489      15.319   1.131  85.667  1.00 82.66           O  
HETATM 4000  C9  EPE A 489      19.724  -1.740  81.317  1.00 78.48           C  
HETATM 4001  C10 EPE A 489      21.212  -1.983  81.565  1.00 77.46           C  
HETATM 4002  S   EPE A 489      21.886  -2.952  80.389  1.00 76.56           S  
HETATM 4003  O1S EPE A 489      21.638  -2.334  79.058  1.00 77.26           O  
HETATM 4004  O2S EPE A 489      21.317  -4.326  80.451  1.00 75.11           O  
HETATM 4005  O3S EPE A 489      23.345  -2.983  80.612  1.00 75.67           O  
HETATM 4006  OH2 1PE A 490       7.786   6.256  89.045  1.00 74.97           O  
HETATM 4007  C12 1PE A 490       8.896   6.252  89.956  1.00 75.52           C  
HETATM 4008  C22 1PE A 490       9.729   4.982  89.801  1.00 75.46           C  
HETATM 4009  OH3 1PE A 490      11.092   5.317  89.505  1.00 75.73           O  
HETATM 4010  C13 1PE A 490      12.606   4.783  87.660  1.00 74.88           C  
HETATM 4011  C23 1PE A 490      11.814   4.254  88.862  1.00 75.56           C  
HETATM 4012  OH4 1PE A 490      12.484   3.920  86.523  1.00 73.32           O  
HETATM 4013  C14 1PE A 490      11.958   4.108  84.151  1.00 71.05           C  
HETATM 4014  C24 1PE A 490      12.840   4.583  85.306  1.00 71.92           C  
HETATM 4015  OH5 1PE A 490      10.696   4.782  84.195  1.00 70.33           O  
HETATM 4016  C15 1PE A 490       8.525   4.694  83.150  1.00 68.19           C  
HETATM 4017  C25 1PE A 490      10.028   4.803  82.936  1.00 68.68           C  
HETATM 4018  OH6 1PE A 490       8.002   5.933  83.616  1.00 67.52           O  
HETATM 4019  C16 1PE A 490       6.666   6.137  85.601  1.00 67.62           C  
HETATM 4020  C26 1PE A 490       6.670   5.799  84.111  1.00 67.53           C  
HETATM 4021  OH7 1PE A 490       5.326   6.217  86.096  1.00 66.47           O  
HETATM 4022  OH2 1PE A 491      -8.573  -9.321 109.578  1.00 79.27           O  
HETATM 4023  C12 1PE A 491      -7.757  -9.772 108.493  1.00 78.58           C  
HETATM 4024  C22 1PE A 491      -7.281  -8.563 107.704  1.00 78.10           C  
HETATM 4025  OH3 1PE A 491      -5.872  -8.444 107.867  1.00 77.71           O  
HETATM 4026  C13 1PE A 491      -4.004  -6.931 108.048  1.00 76.79           C  
HETATM 4027  C23 1PE A 491      -5.433  -7.123 107.552  1.00 77.59           C  
HETATM 4028  OH4 1PE A 491      -3.907  -5.698 108.762  1.00 76.60           O  
HETATM 4029  C14 1PE A 491      -1.828  -5.136 109.896  1.00 75.74           C  
HETATM 4030  C24 1PE A 491      -2.630  -5.074 108.595  1.00 76.27           C  
HETATM 4031  OH5 1PE A 491      -0.423  -5.039 109.662  1.00 74.30           O  
HETATM 4032  C15 1PE A 491       1.733  -6.090 109.679  1.00 72.50           C  
HETATM 4033  C25 1PE A 491       0.228  -6.304 109.531  1.00 73.58           C  
HETATM 4034  OH6 1PE A 491       2.476  -7.189 109.129  1.00 70.60           O  
HETATM 4035  C16 1PE A 491       4.172  -5.704 108.197  1.00 65.30           C  
HETATM 4036  C26 1PE A 491       3.225  -6.872 107.948  1.00 67.32           C  
HETATM 4037  OH7 1PE A 491       3.744  -4.529 107.500  1.00 62.61           O  
HETATM 4038  O1  PG4 A 492      -4.718  -4.262  34.001  1.00 69.66           O  
HETATM 4039  C1  PG4 A 492      -5.835  -4.240  34.901  1.00 69.31           C  
HETATM 4040  C2  PG4 A 492      -6.642  -2.970  34.675  1.00 69.24           C  
HETATM 4041  O2  PG4 A 492      -6.566  -2.160  35.849  1.00 69.46           O  
HETATM 4042  C3  PG4 A 492      -7.825  -1.561  36.166  1.00 69.58           C  
HETATM 4043  C4  PG4 A 492      -7.734  -0.049  35.973  1.00 69.48           C  
HETATM 4044  O3  PG4 A 492      -6.873   0.496  36.974  1.00 68.55           O  
HETATM 4045  C5  PG4 A 492      -7.341   1.758  37.440  1.00 68.12           C  
HETATM 4046  C6  PG4 A 492      -6.262   2.804  37.195  1.00 66.94           C  
HETATM 4047  O4  PG4 A 492      -5.816   2.725  35.849  1.00 65.98           O  
HETATM 4048  C7  PG4 A 492      -5.438   4.004  35.347  1.00 66.22           C  
HETATM 4049  C8  PG4 A 492      -6.221   4.310  34.074  1.00 66.46           C  
HETATM 4050  O5  PG4 A 492      -7.154   5.362  34.338  1.00 65.64           O  
HETATM 4051  O   HOH A 494      19.533  12.023  11.676  1.00 27.03           O  
HETATM 4052  O   HOH A 495       4.128  10.549  20.719  1.00 27.07           O  
HETATM 4053  O   HOH A 496      10.372  26.330  18.142  1.00 27.04           O  
HETATM 4054  O   HOH A 497      12.432  25.776  18.054  1.00 27.50           O  
HETATM 4055  O   HOH A 498      28.123  25.872  -4.573  1.00 28.32           O  
HETATM 4056  O   HOH A 499      -2.691 -14.165  77.384  1.00 30.00           O  
HETATM 4057  O   HOH A 500       2.937   6.734  24.757  1.00 29.80           O  
HETATM 4058  O   HOH A 501      25.486   6.048   3.160  1.00 29.56           O  
HETATM 4059  O   HOH A 502      16.002  22.745  18.847  1.00 31.27           O  
HETATM 4060  O   HOH A 503       4.362   8.777  24.291  1.00 31.16           O  
HETATM 4061  O   HOH A 504       2.597  10.193  23.305  1.00 30.75           O  
HETATM 4062  O   HOH A 505      -3.811 -11.924  76.979  1.00 30.96           O  
HETATM 4063  O   HOH A 506       4.229  13.097  20.447  1.00 32.06           O  
HETATM 4064  O   HOH A 507       4.150   4.974  53.315  1.00 35.36           O  
HETATM 4065  O   HOH A 508      24.700  -2.797  25.471  1.00 32.47           O  
HETATM 4066  O   HOH A 509       2.121  -2.652  51.642  1.00 31.51           O  
HETATM 4067  O   HOH A 510      25.732   5.373  32.872  1.00 31.94           O  
HETATM 4068  O   HOH A 511      -0.870   0.722  94.094  1.00 32.62           O  
HETATM 4069  O   HOH A 512      19.275 -10.146  60.836  1.00 33.45           O  
HETATM 4070  O   HOH A 513      20.823  -1.457  19.363  1.00 33.22           O  
HETATM 4071  O   HOH A 514       0.124  -1.323  35.122  1.00 34.22           O  
HETATM 4072  O   HOH A 515      38.278  30.263   9.256  1.00 33.04           O  
HETATM 4073  O   HOH A 516       0.624   2.368  54.235  1.00 34.21           O  
HETATM 4074  O   HOH A 517      -1.097 -12.915  88.630  1.00 34.07           O  
HETATM 4075  O   HOH A 518      38.153  22.876  -1.409  1.00 32.99           O  
HETATM 4076  O   HOH A 519       1.016   8.103  23.527  1.00 33.39           O  
HETATM 4077  O   HOH A 520      26.769   0.270  35.459  1.00 33.33           O  
HETATM 4078  O   HOH A 521       1.965  -9.543  31.501  1.00 33.45           O  
HETATM 4079  O   HOH A 522      -1.503 -13.599  93.174  1.00 33.53           O  
HETATM 4080  O   HOH A 523       6.995  -7.638  95.184  1.00 33.40           O  
HETATM 4081  O   HOH A 524       0.925   2.397  92.852  1.00 34.19           O  
HETATM 4082  O   HOH A 525       4.861   1.368  19.476  1.00 33.65           O  
HETATM 4083  O   HOH A 526       1.721  -1.606  99.935  1.00 35.75           O  
HETATM 4084  O   HOH A 527       2.261  12.810  24.238  1.00 35.42           O  
HETATM 4085  O   HOH A 528      -1.711  -3.007  61.175  1.00 34.62           O  
HETATM 4086  O   HOH A 529      29.883   7.379  32.605  1.00 34.12           O  
HETATM 4087  O   HOH A 530      -1.129  -7.119  76.730  1.00 34.75           O  
HETATM 4088  O   HOH A 531       5.157   3.560  97.735  1.00 36.22           O  
HETATM 4089  O   HOH A 532       8.862  28.459  18.067  1.00 34.00           O  
HETATM 4090  O   HOH A 533      12.041 -14.060  85.364  1.00 34.70           O  
HETATM 4091  O   HOH A 534      -7.910 -13.762  97.033  1.00 35.02           O  
HETATM 4092  O   HOH A 535      32.962  16.675  21.431  1.00 35.11           O  
HETATM 4093  O   HOH A 536       8.389   1.463  12.870  1.00 33.65           O  
HETATM 4094  O   HOH A 537      12.079   7.872  11.168  1.00 33.98           O  
HETATM 4095  O   HOH A 538       7.018 -15.587  80.517  1.00 34.99           O  
HETATM 4096  O   HOH A 539      35.107  10.000   9.606  1.00 35.48           O  
HETATM 4097  O   HOH A 540      -2.407  -2.614  46.612  1.00 37.08           O  
HETATM 4098  O   HOH A 541       4.302  17.748  25.939  1.00 35.44           O  
HETATM 4099  O   HOH A 542      31.131  -2.830  31.110  1.00 34.74           O  
HETATM 4100  O   HOH A 543      -0.570   0.209  18.964  1.00 38.64           O  
HETATM 4101  O   HOH A 544       1.648   4.627  53.517  1.00 36.41           O  
HETATM 4102  O   HOH A 545      -2.900  -5.169  61.024  1.00 35.63           O  
HETATM 4103  O   HOH A 546       3.945  14.518  23.095  1.00 35.77           O  
HETATM 4104  O   HOH A 547      -5.805  -8.506  78.101  1.00 33.46           O  
HETATM 4105  O   HOH A 548       7.086  18.443  34.086  1.00 35.36           O  
HETATM 4106  O   HOH A 549      16.899  23.462  16.617  1.00 36.83           O  
HETATM 4107  O   HOH A 550      28.745   7.455  18.361  1.00 36.52           O  
HETATM 4108  O   HOH A 551       7.678  20.607  32.570  1.00 37.56           O  
HETATM 4109  O   HOH A 552       3.718  25.754  35.084  1.00 36.36           O  
HETATM 4110  O   HOH A 553       8.243  20.164  18.964  1.00 35.86           O  
HETATM 4111  O   HOH A 554       2.875 -15.947  88.908  1.00 38.00           O  
HETATM 4112  O   HOH A 555       7.871 -17.535  42.447  1.00 36.39           O  
HETATM 4113  O   HOH A 556      10.121  11.834  16.079  1.00 37.90           O  
HETATM 4114  O   HOH A 557      -2.879  -3.188  74.881  1.00 38.15           O  
HETATM 4115  O   HOH A 558      12.592  -9.963  25.279  1.00 37.12           O  
HETATM 4116  O   HOH A 559      -0.753  -9.479  31.238  1.00 35.42           O  
HETATM 4117  O   HOH A 560      31.294  31.528  -0.223  1.00 38.32           O  
HETATM 4118  O   HOH A 561      30.681  10.263  28.689  1.00 37.25           O  
HETATM 4119  O   HOH A 562      -1.383   5.770  47.159  1.00 36.92           O  
HETATM 4120  O   HOH A 563       7.353   2.950  71.614  1.00 37.63           O  
HETATM 4121  O   HOH A 564      17.466  13.042  33.086  1.00 38.64           O  
HETATM 4122  O   HOH A 565      -4.418   5.153  38.761  1.00 38.05           O  
HETATM 4123  O   HOH A 566       8.086   2.583  74.085  1.00 39.84           O  
HETATM 4124  O   HOH A 567      -1.568   0.893  99.381  1.00 38.52           O  
HETATM 4125  O   HOH A 568      31.834  14.361  22.241  1.00 37.92           O  
HETATM 4126  O   HOH A 569      25.783  19.232  -1.126  1.00 37.42           O  
HETATM 4127  O   HOH A 570      -6.146  -6.354  67.782  1.00 38.05           O  
HETATM 4128  O   HOH A 571      27.614  -4.801  27.838  1.00 38.26           O  
HETATM 4129  O   HOH A 572       1.894 -17.795  49.420  1.00 38.44           O  
HETATM 4130  O   HOH A 573      14.158  -3.129   9.692  1.00 37.49           O  
HETATM 4131  O   HOH A 574      27.848  16.849  24.387  1.00 38.87           O  
HETATM 4132  O   HOH A 575       9.214  16.592  11.839  1.00 38.32           O  
HETATM 4133  O   HOH A 576      20.508  23.918  -4.010  1.00 38.37           O  
HETATM 4134  O   HOH A 577       9.267   7.551  49.073  1.00 40.66           O  
HETATM 4135  O   HOH A 578      12.391   0.473  70.332  1.00 38.53           O  
HETATM 4136  O   HOH A 579      31.672   8.587  31.124  1.00 39.15           O  
HETATM 4137  O   HOH A 580       0.486   0.146  98.796  1.00 40.74           O  
HETATM 4138  O   HOH A 581      28.505  -0.403  33.284  1.00 39.82           O  
HETATM 4139  O   HOH A 582       6.878  -3.967  98.532  1.00 38.44           O  
HETATM 4140  O   HOH A 583      -2.482 -13.942  90.721  1.00 37.74           O  
HETATM 4141  O   HOH A 584       8.585  23.145  33.707  1.00 39.36           O  
HETATM 4142  O   HOH A 585      -4.733  -6.194  63.233  1.00 38.56           O  
HETATM 4143  O   HOH A 586      -2.017  -7.694  43.537  1.00 38.21           O  
HETATM 4144  O   HOH A 587      22.731  26.558  11.600  1.00 40.08           O  
HETATM 4145  O   HOH A 588      13.478  14.611   7.645  1.00 39.24           O  
HETATM 4146  O   HOH A 589      15.210  23.035  30.146  1.00 39.58           O  
HETATM 4147  O   HOH A 590      30.640   9.097  17.190  1.00 39.72           O  
HETATM 4148  O   HOH A 591      26.301  14.280  37.846  1.00 39.67           O  
HETATM 4149  O   HOH A 592       5.152  -9.040  50.506  1.00 40.06           O  
HETATM 4150  O   HOH A 593      25.666   2.468  35.556  1.00 40.83           O  
HETATM 4151  O   HOH A 594      17.687  22.753  31.262  1.00 39.84           O  
HETATM 4152  O   HOH A 595       6.446 -16.776  50.318  1.00 40.74           O  
HETATM 4153  O   HOH A 596      14.348  17.605  11.969  1.00 40.79           O  
HETATM 4154  O   HOH A 597       1.226  -2.564  74.264  1.00 38.31           O  
HETATM 4155  O   HOH A 598       2.949  -0.989  97.196  1.00 38.99           O  
HETATM 4156  O   HOH A 599       6.383  23.305  17.179  1.00 38.54           O  
HETATM 4157  O   HOH A 600      -0.565  -4.740  74.870  1.00 40.57           O  
HETATM 4158  O   HOH A 601      37.609  23.566  21.987  1.00 41.36           O  
HETATM 4159  O   HOH A 602       6.501   1.477  76.212  1.00 39.55           O  
HETATM 4160  O   HOH A 603       3.972   5.334  38.010  1.00 41.41           O  
HETATM 4161  O   HOH A 604      -1.941  -9.493  38.069  1.00 41.68           O  
HETATM 4162  O   HOH A 605      -4.472  -6.326  71.595  1.00 40.88           O  
HETATM 4163  O   HOH A 606      20.369  -6.068  66.745  1.00 41.12           O  
HETATM 4164  O   HOH A 607      26.512  19.860  22.460  1.00 42.01           O  
HETATM 4165  O   HOH A 608      -5.275 -14.029  90.333  1.00 41.13           O  
HETATM 4166  O   HOH A 609       7.066  20.553  16.871  1.00 39.58           O  
HETATM 4167  O   HOH A 610      10.326 -20.521  62.611  1.00 40.87           O  
HETATM 4168  O   HOH A 611      13.080 -17.407  47.844  1.00 41.57           O  
HETATM 4169  O   HOH A 612       7.233   2.200  90.976  1.00 40.40           O  
HETATM 4170  O   HOH A 613      -1.037  -1.105  74.127  1.00 39.63           O  
HETATM 4171  O   HOH A 614      23.352  -8.071  44.192  1.00 41.70           O  
HETATM 4172  O   HOH A 615      26.659  24.603  21.184  1.00 41.66           O  
HETATM 4173  O   HOH A 616      37.340   8.790  17.854  1.00 43.00           O  
HETATM 4174  O   HOH A 617      16.392  19.387  35.993  1.00 40.57           O  
HETATM 4175  O   HOH A 618       2.920  15.191  26.001  1.00 44.44           O  
HETATM 4176  O   HOH A 619      15.795  -3.673  87.917  1.00 42.17           O  
HETATM 4177  O   HOH A 620      -5.618   0.806  45.342  1.00 42.74           O  
HETATM 4178  O   HOH A 621       3.597  -4.487  51.837  1.00 41.98           O  
HETATM 4179  O   HOH A 622      39.932  23.440   1.254  1.00 42.00           O  
HETATM 4180  O   HOH A 623      -2.930  -1.291  78.752  1.00 42.30           O  
HETATM 4181  O   HOH A 624       4.108  -1.126  19.590  1.00 42.19           O  
HETATM 4182  O   HOH A 625       7.683  27.156  24.918  1.00 42.29           O  
HETATM 4183  O   HOH A 626      -3.266  -9.631 100.774  1.00 42.47           O  
HETATM 4184  O   HOH A 627      15.156  -2.378  80.998  1.00 42.83           O  
HETATM 4185  O   HOH A 628      16.280   4.049   6.132  1.00 42.79           O  
HETATM 4186  O   HOH A 629      23.251  -3.475  23.031  1.00 43.08           O  
HETATM 4187  O   HOH A 630      30.881  -1.380  34.287  1.00 41.82           O  
HETATM 4188  O   HOH A 631       2.735   6.489  49.597  1.00 41.91           O  
HETATM 4189  O   HOH A 632      -1.717  -2.232  58.142  1.00 42.02           O  
HETATM 4190  O   HOH A 633      35.876  18.874  20.299  1.00 43.88           O  
HETATM 4191  O   HOH A 634      32.417  25.741  -9.849  1.00 40.87           O  
HETATM 4192  O   HOH A 635       6.047 -18.239  75.195  1.00 44.47           O  
HETATM 4193  O   HOH A 636      -5.742 -11.867  88.496  1.00 42.44           O  
HETATM 4194  O   HOH A 637      17.484  24.559  27.562  1.00 43.57           O  
HETATM 4195  O   HOH A 638       8.582  14.697  35.569  1.00 43.87           O  
HETATM 4196  O   HOH A 639      25.795  -6.522  27.116  1.00 43.25           O  
HETATM 4197  O   HOH A 640      16.979 -10.309  92.709  1.00 45.27           O  
HETATM 4198  O   HOH A 641      17.675 -16.007  53.473  1.00 43.27           O  
HETATM 4199  O   HOH A 642       4.177 -18.449  58.653  1.00 46.83           O  
HETATM 4200  O   HOH A 643      27.501   0.457  19.913  1.00 45.08           O  
HETATM 4201  O   HOH A 644      35.254  23.832  -8.703  1.00 44.77           O  
HETATM 4202  O   HOH A 645      14.074  25.596  29.032  1.00 46.00           O  
HETATM 4203  O   HOH A 646      26.411  14.317  34.834  1.00 43.37           O  
HETATM 4204  O   HOH A 647      -7.806 -13.225  87.126  1.00 44.79           O  
HETATM 4205  O   HOH A 648      14.659  17.420  36.351  1.00 43.72           O  
HETATM 4206  O   HOH A 649       4.294 -18.205  49.913  1.00 44.40           O  
HETATM 4207  O   HOH A 650      27.336  -2.162  32.019  1.00 42.68           O  
HETATM 4208  O   HOH A 651      17.066  26.975  28.750  1.00 42.96           O  
HETATM 4209  O   HOH A 652       5.021   3.098  90.837  1.00 45.19           O  
HETATM 4210  O   HOH A 653       8.467  20.233  14.222  1.00 43.75           O  
HETATM 4211  O   HOH A 654      30.511   4.220  19.109  1.00 45.91           O  
HETATM 4212  O   HOH A 655      26.375  27.604  -4.168  1.00 44.72           O  
HETATM 4213  O   HOH A 656      -5.409  -8.150 100.465  1.00 45.48           O  
HETATM 4214  O   HOH A 657      15.551 -12.625  27.533  1.00 43.72           O  
HETATM 4215  O   HOH A 658      20.716  27.137   1.990  1.00 45.73           O  
HETATM 4216  O   HOH A 659      30.258  16.308  24.403  1.00 44.98           O  
HETATM 4217  O   HOH A 660      17.834 -16.149  89.965  1.00 44.45           O  
HETATM 4218  O   HOH A 661       0.080 -17.893  56.193  1.00 46.32           O  
HETATM 4219  O   HOH A 662      -2.457  -0.339  71.743  1.00 45.43           O  
HETATM 4220  O   HOH A 663       4.038  11.025  36.250  1.00 45.74           O  
HETATM 4221  O   HOH A 664       2.081  13.597  35.597  1.00 46.10           O  
HETATM 4222  O   HOH A 665      12.641  21.297   6.865  1.00 44.42           O  
HETATM 4223  O   HOH A 666      -2.754  -4.668  81.348  1.00 44.54           O  
HETATM 4224  O   HOH A 667      18.641  19.535  -4.598  1.00 44.37           O  
HETATM 4225  O   HOH A 668       2.965   2.951  17.370  1.00 46.07           O  
HETATM 4226  O   HOH A 669      32.876   8.101  19.009  1.00 46.88           O  
HETATM 4227  O   HOH A 670      15.068  26.344  33.465  1.00 45.13           O  
HETATM 4228  O   HOH A 671      -1.631  -5.132  57.681  1.00 48.54           O  
HETATM 4229  O   HOH A 672      -3.093  -9.534  32.795  1.00 46.97           O  
HETATM 4230  O   HOH A 673      -6.376  -6.095  78.220  1.00 44.56           O  
HETATM 4231  O   HOH A 674      14.117  11.233  42.803  1.00 46.01           O  
HETATM 4232  O   HOH A 675      -0.496  12.594  29.632  1.00 47.19           O  
HETATM 4233  O   HOH A 676      17.211 -10.813  53.968  1.00 46.75           O  
HETATM 4234  O   HOH A 677      19.593  -0.816  57.546  1.00 47.14           O  
HETATM 4235  O   HOH A 678      -2.415  -5.243  97.264  1.00 46.27           O  
HETATM 4236  O   HOH A 679      -7.022 -10.114  98.860  1.00 47.28           O  
HETATM 4237  O   HOH A 680      -6.767  -2.447 102.527  1.00 45.41           O  
HETATM 4238  O   HOH A 681      19.682 -15.789  43.724  1.00 47.26           O  
HETATM 4239  O   HOH A 682      11.661  -3.512  10.765  1.00 46.64           O  
HETATM 4240  O   HOH A 683      -0.205   2.071  86.070  1.00 46.20           O  
HETATM 4241  O   HOH A 684      -1.381 -12.639  35.877  1.00 45.55           O  
HETATM 4242  O   HOH A 685      18.683  -4.657  17.812  1.00 47.76           O  
HETATM 4243  O   HOH A 686      -7.010   4.541  39.863  1.00 47.56           O  
HETATM 4244  O   HOH A 687      30.523  32.125 -15.268  1.00 47.58           O  
HETATM 4245  O   HOH A 688      -7.054   2.261  97.768  1.00 47.88           O  
HETATM 4246  O   HOH A 689       2.131   0.772  88.243  1.00 48.46           O  
HETATM 4247  O   HOH A 690      35.388  21.226  20.076  1.00 46.78           O  
HETATM 4248  O   HOH A 691      28.362  -6.387  32.256  1.00 46.95           O  
HETATM 4249  O   HOH A 692      17.826 -13.530  52.637  1.00 48.76           O  
HETATM 4250  O   HOH A 693      33.474  40.880  -7.449  1.00 46.58           O  
HETATM 4251  O   HOH A 694      37.595  10.162  10.760  1.00 48.58           O  
HETATM 4252  O   HOH A 695      -4.446  -6.519  43.753  1.00 47.85           O  
HETATM 4253  O   HOH A 696       7.702 -20.121  75.228  1.00 47.80           O  
HETATM 4254  O   HOH A 697       8.975  18.146  35.550  1.00 48.47           O  
HETATM 4255  O   HOH A 698      24.968  -2.811  16.863  1.00 49.98           O  
HETATM 4256  O   HOH A 699       6.805  27.458  22.076  1.00 49.14           O  
HETATM 4257  O   HOH A 700       6.627   6.243  12.614  1.00 46.26           O  
HETATM 4258  O   HOH A 701       6.302 -18.064  57.211  1.00 47.88           O  
HETATM 4259  O   HOH A 702      14.088   4.081   6.778  1.00 46.78           O  
HETATM 4260  O   HOH A 703      30.077   1.675  19.348  1.00 49.25           O  
HETATM 4261  O   HOH A 704       2.758   4.667  76.025  1.00 47.78           O  
HETATM 4262  O   HOH A 705      17.550  -1.618  58.830  1.00 47.33           O  
HETATM 4263  O   HOH A 706      40.453   9.356   9.455  1.00 48.93           O  
HETATM 4264  O   HOH A 707      -3.575  -2.832  68.265  1.00 49.69           O  
HETATM 4265  O   HOH A 708      16.857 -16.457  34.539  1.00 47.97           O  
HETATM 4266  O   HOH A 709      16.877 -15.399  64.299  1.00 51.22           O  
HETATM 4267  O   HOH A 710      -7.984  -7.732  50.226  1.00 46.81           O  
HETATM 4268  O   HOH A 711      11.572  18.547  34.978  1.00 47.50           O  
HETATM 4269  O   HOH A 712      -4.557  -6.672  65.907  1.00 48.17           O  
HETATM 4270  O   HOH A 713       1.084 -18.452  41.132  1.00 49.22           O  
HETATM 4271  O   HOH A 714      13.995  27.075  25.580  1.00 46.84           O  
HETATM 4272  O   HOH A 715       9.838 -23.097  51.237  1.00 48.91           O  
HETATM 4273  O   HOH A 716       3.770  15.442  36.764  1.00 48.89           O  
HETATM 4274  O   HOH A 717      16.435  -4.663  80.884  1.00 49.85           O  
HETATM 4275  O   HOH A 718      16.016  20.004   4.950  1.00 49.13           O  
HETATM 4276  O   HOH A 719      18.348 -11.177  27.055  1.00 47.11           O  
HETATM 4277  O   HOH A 720       5.039   4.658  92.971  1.00 48.98           O  
HETATM 4278  O   HOH A 721      21.183  15.950  35.763  1.00 48.61           O  
HETATM 4279  O   HOH A 722      17.742 -16.308  39.755  1.00 49.02           O  
HETATM 4280  O   HOH A 723      14.275  27.271  18.914  1.00 48.88           O  
HETATM 4281  O   HOH A 724      -1.721   0.114  65.058  1.00 49.68           O  
HETATM 4282  O   HOH A 725      23.494  15.910  32.565  1.00 49.80           O  
HETATM 4283  O   HOH A 726       3.390 -19.025  42.354  1.00 51.45           O  
HETATM 4284  O   HOH A 727      13.015 -15.546  28.415  1.00 48.93           O  
HETATM 4285  O   HOH A 728       6.958   8.564  50.649  1.00 46.17           O  
HETATM 4286  O   HOH A 729      21.659  -7.993  65.901  1.00 51.70           O  
HETATM 4287  O   HOH A 730      28.822  -4.080  30.524  1.00 50.48           O  
HETATM 4288  O   HOH A 731      -2.119  11.205  33.117  1.00 52.05           O  
HETATM 4289  O   HOH A 732      31.920   0.601  21.706  1.00 51.31           O  
HETATM 4290  O   HOH A 733      16.563 -14.597  47.766  1.00 49.57           O  
HETATM 4291  O   HOH A 734      33.207  -3.097  26.649  1.00 47.09           O  
HETATM 4292  O   HOH A 735       9.347   7.311  74.014  1.00 50.16           O  
HETATM 4293  O   HOH A 736      33.256   1.123  34.895  1.00 50.86           O  
HETATM 4294  O   HOH A 737      17.738 -10.734  20.667  1.00 49.10           O  
HETATM 4295  O   HOH A 738       8.488 -20.936  51.564  1.00 50.00           O  
HETATM 4296  O   HOH A 739      23.766 -12.812  30.487  1.00 48.05           O  
HETATM 4297  O   HOH A 740      34.232   5.217  21.724  1.00 50.51           O  
HETATM 4298  O   HOH A 741      -5.485  -4.151 110.262  1.00 52.69           O  
HETATM 4299  O   HOH A 742      25.946  -0.472  13.131  1.00 50.65           O  
HETATM 4300  O   HOH A 743      -7.077  -0.961  47.245  1.00 48.75           O  
HETATM 4301  O   HOH A 744      14.515 -14.133  70.756  1.00 52.51           O  
HETATM 4302  O   HOH A 745      31.921   5.858  20.404  1.00 50.40           O  
HETATM 4303  O   HOH A 746      36.771  25.852  -9.302  1.00 49.17           O  
HETATM 4304  O   HOH A 747       3.225 -18.083  71.493  1.00 50.54           O  
HETATM 4305  O   HOH A 748       0.802   1.337  96.518  1.00 49.33           O  
HETATM 4306  O   HOH A 749      22.526  21.034  -4.073  1.00 51.62           O  
HETATM 4307  O   HOH A 750      25.227  22.328  21.738  1.00 51.88           O  
HETATM 4308  O   HOH A 751      -1.446  -2.150  67.244  1.00 51.40           O  
HETATM 4309  O   HOH A 752      36.587  18.798  -2.585  1.00 50.16           O  
HETATM 4310  O   HOH A 753       9.102  22.776  36.398  1.00 50.80           O  
HETATM 4311  O   HOH A 754      12.057  -1.068  93.520  1.00 50.88           O  
HETATM 4312  O   HOH A 755      -0.686 -16.761  61.288  1.00 50.48           O  
HETATM 4313  O   HOH A 756      26.432  38.941  -5.390  1.00 52.78           O  
HETATM 4314  O   HOH A 757      25.658  20.292  26.396  1.00 53.98           O  
HETATM 4315  O   HOH A 758      38.006  21.115  22.728  1.00 50.80           O  
HETATM 4316  O   HOH A 759      28.952  12.021  29.758  1.00 49.09           O  
HETATM 4317  O   HOH A 760       7.105  12.072  39.570  1.00 50.88           O  
HETATM 4318  O   HOH A 761      22.316 -12.734  27.862  1.00 53.63           O  
HETATM 4319  O   HOH A 762      -8.585  -1.587  86.376  1.00 51.04           O  
HETATM 4320  O   HOH A 763       0.231 -10.540  23.707  1.00 51.71           O  
HETATM 4321  O   HOH A 764      29.450  -0.563  39.812  1.00 52.35           O  
HETATM 4322  O   HOH A 765      15.246  15.323  37.570  1.00 50.68           O  
HETATM 4323  O   HOH A 766      -4.232   8.551  26.360  1.00 52.37           O  
HETATM 4324  O   HOH A 767      27.998  32.766 -15.776  1.00 50.35           O  
HETATM 4325  O   HOH A 768      -4.177 -11.432  24.079  1.00 52.62           O  
HETATM 4326  O   HOH A 769      41.572  38.905   1.879  1.00 53.04           O  
HETATM 4327  O   HOH A 770      -2.433  -7.690  40.659  1.00 52.98           O  
HETATM 4328  O   HOH A 771      35.195   7.276  18.049  1.00 54.57           O  
HETATM 4329  O   HOH A 772      43.414  33.934   4.008  1.00 52.03           O  
HETATM 4330  O   HOH A 773      11.049 -14.362  24.659  1.00 52.95           O  
HETATM 4331  O   HOH A 774      15.977  24.417  34.654  1.00 50.38           O  
HETATM 4332  O   HOH A 775      -3.002   6.961  16.947  1.00 53.31           O  
HETATM 4333  O   HOH A 776      33.786   3.929  34.944  1.00 53.86           O  
HETATM 4334  O   HOH A 777      25.042  35.743 -17.919  1.00 51.16           O  
HETATM 4335  O   HOH A 778      10.046  14.601   4.157  1.00 52.48           O  
HETATM 4336  O   HOH A 779      -1.893 -14.819  47.912  1.00 51.96           O  
HETATM 4337  O   HOH A 780      28.527  11.947  33.966  1.00 53.53           O  
HETATM 4338  O   HOH A 781      26.672  -7.864  41.092  1.00 52.00           O  
HETATM 4339  O   HOH A 782      13.514   0.412  77.575  1.00 52.41           O  
HETATM 4340  O   HOH A 783      20.525  26.345  -4.520  1.00 49.64           O  
HETATM 4341  O   HOH A 784      -4.599  -6.584  36.476  1.00 50.68           O  
HETATM 4342  O   HOH A 785      15.194  -6.530  90.421  1.00 52.21           O  
HETATM 4343  O   HOH A 786      -2.271   3.427 106.475  1.00 52.06           O  
HETATM 4344  O   HOH A 787       0.885   4.542  85.407  1.00 52.82           O  
HETATM 4345  O   HOH A 788      -6.211 -11.322  36.192  1.00 54.42           O  
HETATM 4346  O   HOH A 789      29.740  19.679  -6.221  1.00 55.62           O  
HETATM 4347  O   HOH A 790      27.817  12.103  38.115  1.00 51.01           O  
HETATM 4348  O   HOH A 791       6.184 -13.313  28.414  1.00 54.19           O  
HETATM 4349  O   HOH A 792      40.523  32.201   7.011  1.00 51.91           O  
HETATM 4350  O   HOH A 793       2.390   9.840  38.602  1.00 52.01           O  
HETATM 4351  O   HOH A 794      -6.310 -14.339  54.652  1.00 51.73           O  
HETATM 4352  O   HOH A 795      -0.124   8.717  19.509  1.00 53.51           O  
HETATM 4353  O   HOH A 796       4.227   4.512  15.727  1.00 53.29           O  
HETATM 4354  O   HOH A 797      18.518 -14.119  40.970  1.00 53.81           O  
HETATM 4355  O   HOH A 798      17.183   9.029   1.976  1.00 54.85           O  
HETATM 4356  O   HOH A 799      35.753  16.478  19.224  1.00 53.49           O  
HETATM 4357  O   HOH A 800      30.228   7.126  25.475  1.00 54.83           O  
HETATM 4358  O   HOH A 801      42.757  23.104  -3.917  1.00 54.16           O  
HETATM 4359  O   HOH A 802      14.233  28.488   3.784  1.00 52.58           O  
HETATM 4360  O   HOH A 803      -4.316   2.946  92.605  1.00 52.77           O  
HETATM 4361  O   HOH A 804      39.792  37.925   9.489  1.00 54.77           O  
HETATM 4362  O   HOH A 805      11.480   9.648   8.496  1.00 53.24           O  
HETATM 4363  O   HOH A 806      -5.595   5.303  24.613  1.00 53.64           O  
HETATM 4364  O   HOH A 807      10.195  -6.857  14.970  1.00 54.11           O  
HETATM 4365  O   HOH A 808      -7.845  -0.537  95.344  1.00 56.12           O  
HETATM 4366  O   HOH A 809      25.938   1.573  54.220  1.00 55.52           O  
HETATM 4367  O   HOH A 810      15.125  -1.053   6.081  1.00 55.51           O  
HETATM 4368  O   HOH A 811       2.764 -19.151  83.684  1.00 57.49           O  
HETATM 4369  O   HOH A 812      -6.256  -4.691  84.163  1.00 55.11           O  
HETATM 4370  O   HOH A 813      23.576  33.553  -5.082  1.00 52.48           O  
HETATM 4371  O   HOH A 814       3.336 -13.320  29.175  1.00 56.39           O  
HETATM 4372  O   HOH A 815      24.152  23.254  -5.799  1.00 53.11           O  
HETATM 4373  O   HOH A 816      47.567  24.837  -1.487  1.00 55.30           O  
HETATM 4374  O   HOH A 817      -2.531  -2.873  33.007  1.00 53.56           O  
HETATM 4375  O   HOH A 818      29.866  34.530 -16.079  1.00 55.52           O  
HETATM 4376  O   HOH A 819      -6.648 -12.165  56.199  1.00 55.39           O  
HETATM 4377  O   HOH A 820       2.393   2.663  86.588  1.00 54.79           O  
HETATM 4378  O   HOH A 821      34.906  44.115   1.394  1.00 56.43           O  
HETATM 4379  O   HOH A 822      19.737  -2.282  16.973  1.00 57.77           O  
HETATM 4380  O   HOH A 823      -4.110  -6.946  58.445  1.00 53.01           O  
HETATM 4381  O   HOH A 824      29.103  23.536  21.057  1.00 55.54           O  
HETATM 4382  O   HOH A 825      -5.729  -4.726  29.166  1.00 56.15           O  
HETATM 4383  O   HOH A 826      21.511  18.214  32.339  1.00 54.75           O  
HETATM 4384  O   HOH A 827      27.902  38.468 -14.421  1.00 53.89           O  
HETATM 4385  O   HOH A 828       2.919  -4.839  21.193  1.00 56.33           O  
HETATM 4386  O   HOH A 829      17.561  11.738   3.199  1.00 53.53           O  
HETATM 4387  O   HOH A 830      23.276  33.049  -1.964  1.00 55.25           O  
HETATM 4388  O   HOH A 831       2.203   4.667  47.914  1.00 56.80           O  
HETATM 4389  O   HOH A 832      15.019 -16.470  70.084  1.00 57.42           O  
HETATM 4390  O   HOH A 833      -7.143   0.500  41.518  1.00 56.13           O  
HETATM 4391  O   HOH A 834      28.875  18.049  -4.359  1.00 56.70           O  
HETATM 4392  O   HOH A 835       8.565   3.051  95.133  1.00 56.00           O  
HETATM 4393  O   HOH A 836      16.953   2.751   4.123  1.00 56.65           O  
HETATM 4394  O   HOH A 837       5.232   6.029  76.656  1.00 55.67           O  
HETATM 4395  O   HOH A 838      -6.345  -1.747 105.475  1.00 57.56           O  
HETATM 4396  O   HOH A 839      -4.375  -2.992  57.075  1.00 56.19           O  
HETATM 4397  O   HOH A 840      19.935   5.150   7.351  1.00 55.25           O  
HETATM 4398  O   HOH A 841      -9.987  -7.064  89.442  1.00 57.38           O  
HETATM 4399  O   HOH A 842      14.930 -22.584  64.372  1.00 57.33           O  
HETATM 4400  O   HOH A 843      16.647  29.185  10.359  1.00 52.83           O  
HETATM 4401  O   HOH A 844      15.106   0.174  79.663  1.00 56.73           O  
HETATM 4402  O   HOH A 845      24.185  19.094  -3.799  1.00 55.37           O  
HETATM 4403  O   HOH A 846      29.047  37.003   4.481  1.00 59.04           O  
HETATM 4404  O   HOH A 847      27.181  -4.674  21.621  1.00 58.09           O  
HETATM 4405  O   HOH A 848      30.273   3.374  47.508  1.00 59.78           O  
HETATM 4406  O   HOH A 849      36.009  36.217  -4.747  1.00 61.48           O  
HETATM 4407  O   HOH A 850      -0.085 -19.407  37.789  1.00 59.65           O  
HETATM 4408  O   HOH A 851      36.141  10.460  19.080  1.00 56.94           O  
HETATM 4409  O   HOH A 852       9.578   4.790  74.966  1.00 58.14           O  
HETATM 4410  O   HOH A 853      16.872   6.449  60.172  1.00 59.05           O  
HETATM 4411  O   HOH A 854      -4.354  -7.309  33.157  1.00 58.96           O  
HETATM 4412  O   HOH A 855      -7.456 -10.468  95.572  1.00 57.60           O  
HETATM 4413  O   HOH A 856       9.917 -13.701  22.298  1.00 61.44           O  
HETATM 4414  O   HOH A 857      20.305   1.703  57.789  1.00 61.05           O  
HETATM 4415  O   HOH A 858       4.319   5.061  72.750  1.00 60.41           O  
HETATM 4416  O   HOH A 859      30.034  38.400   7.003  1.00 62.27           O  
HETATM 4417  O   HOH A 860      17.496  -6.156  15.920  1.00 58.36           O  
HETATM 4418  O   HOH A 861      14.823   2.684  61.919  1.00 59.88           O  
HETATM 4419  O   HOH A 862      18.975 -13.044  34.992  1.00 60.89           O  
HETATM 4420  O   HOH A 863      -3.184   5.913  87.197  1.00 59.07           O  
HETATM 4421  O   HOH A 864      13.875   1.770   7.189  1.00 63.71           O  
HETATM 4422  O   HOH A 865      20.996 -13.716  44.598  1.00 61.80           O  
HETATM 4423  O   HOH A 866      25.952  21.170  -7.178  1.00 63.93           O  
HETATM 4424  O   HOH A 867       3.938 -20.593  61.048  1.00 64.26           O  
HETATM 4425  O   HOH A 868      31.405  24.185 -11.819  1.00 62.46           O  
HETATM 4426  O   HOH A 869      33.453  -1.107  22.832  1.00 66.12           O  
HETATM 4427  O   HOH A 870      24.735  13.380  41.160  1.00 61.43           O  
HETATM 4428  O   HOH A 871      46.452  23.841  13.318  1.00 66.07           O  
HETATM 4429  O   HOH A 872      17.923  -5.045  77.678  1.00 64.17           O  
HETATM 4430  O   HOH A 873      30.426   0.993  50.220  1.00 62.81           O  
HETATM 4431  O   HOH A 874      -2.771  -1.477  30.549  1.00 63.00           O  
HETATM 4432  O   HOH A 875      -2.939 -13.652  51.060  1.00 63.60           O  
HETATM 4433  O   HOH A 876      33.828  37.676   6.843  1.00 63.05           O  
HETATM 4434  O   HOH A 877      21.306   4.943  48.921  1.00 63.21           O  
HETATM 4435  O   HOH A 878      19.811  -7.284  73.271  1.00 65.69           O  
HETATM 4436  O   HOH A 879      13.330 -18.598  40.668  1.00 67.62           O  
HETATM 4437  O   HOH A 880       9.729  24.372  12.111  1.00 70.73           O  
HETATM 4438  O   HOH A 881      -4.966   3.339 105.200  1.00 71.13           O  
HETATM 4439  O   HOH A 882      22.649  -8.120  52.597  1.00 70.27           O  
HETATM 4440  O   HOH A 883       1.569 -17.508  59.941  1.00 50.78           O  
HETATM 4441  O   HOH A 884      14.713   4.270  82.111  1.00 52.52           O  
HETATM 4442  O   HOH A 885      12.779  15.842  10.377  1.00 56.42           O  
HETATM 4443  O   HOH A 886      18.086  27.356  22.118  1.00 65.07           O  
HETATM 4444  O   HOH A 887      27.057  -4.212  43.554  1.00 48.10           O  
HETATM 4445  O   HOH A 888      18.806  -1.858   5.326  1.00 42.20           O  
HETATM 4446  O   HOH A 889      20.823  -7.587  57.180  1.00 53.37           O  
HETATM 4447  O   HOH A 890      17.323  -2.636  67.063  1.00 58.88           O  
HETATM 4448  O   HOH A 891      29.296  40.703 -14.485  1.00 51.83           O  
HETATM 4449  O   HOH A 892      15.705   9.622  50.638  1.00 52.61           O  
HETATM 4450  O   HOH A 893      -4.999 -18.417  79.955  1.00 48.52           O  
HETATM 4451  O   HOH A 894      25.935  18.355  -5.597  1.00 51.41           O  
HETATM 4452  O   HOH A 895      34.911   1.853  27.325  1.00 53.60           O  
HETATM 4453  O   HOH A 896       6.663   2.737  11.210  1.00 64.10           O  
HETATM 4454  O   HOH A 897      13.911  -9.873  14.627  1.00 64.56           O  
HETATM 4455  O   HOH A 898      14.127  26.948  14.714  1.00 57.72           O  
HETATM 4456  O   HOH A 899      18.720 -17.357  32.983  1.00 55.11           O  
HETATM 4457  O   HOH A 900      40.832  10.979  18.346  1.00 49.09           O  
HETATM 4458  O   HOH A 901       4.643   7.516  54.623  1.00 41.02           O  
HETATM 4459  O   HOH A 902      21.436  28.103  15.784  1.00 62.25           O  
HETATM 4460  O   HOH A 903      25.275  33.153 -15.361  1.00 58.52           O  
HETATM 4461  O   HOH A 904      17.844  25.617  25.051  1.00 46.13           O  
HETATM 4462  O   HOH A 905       5.024   6.855  50.658  1.00 45.94           O  
HETATM 4463  O   HOH A 906       7.547  24.838  15.554  1.00 46.85           O  
HETATM 4464  O   HOH A 907      -0.779 -16.081  74.882  1.00 42.15           O  
HETATM 4465  O   HOH A 908      22.827  14.901  43.293  1.00 68.48           O  
HETATM 4466  O   HOH A 909      19.389  12.891  41.542  1.00 53.27           O  
CONECT 1086 1434                                                                
CONECT 1434 1086                                                                
CONECT 3124 3750                                                                
CONECT 3750 3124 3751 3761                                                      
CONECT 3751 3750 3752 3758                                                      
CONECT 3752 3751 3753 3759                                                      
CONECT 3753 3752 3754 3760                                                      
CONECT 3754 3753 3755 3761                                                      
CONECT 3755 3754 3762                                                           
CONECT 3756 3757 3758 3763                                                      
CONECT 3757 3756                                                                
CONECT 3758 3751 3756                                                           
CONECT 3759 3752                                                                
CONECT 3760 3753 3764                                                           
CONECT 3761 3750 3754                                                           
CONECT 3762 3755 3778                                                           
CONECT 3763 3756                                                                
CONECT 3764 3760 3765 3772                                                      
CONECT 3765 3764 3766 3777                                                      
CONECT 3766 3765 3767 3773                                                      
CONECT 3767 3766 3768 3774                                                      
CONECT 3768 3767 3769 3772                                                      
CONECT 3769 3768 3775                                                           
CONECT 3770 3771 3776 3777                                                      
CONECT 3771 3770                                                                
CONECT 3772 3764 3768                                                           
CONECT 3773 3766                                                                
CONECT 3774 3767                                                                
CONECT 3775 3769                                                                
CONECT 3776 3770                                                                
CONECT 3777 3765 3770                                                           
CONECT 3778 3762 3779 3787                                                      
CONECT 3779 3778 3780 3784                                                      
CONECT 3780 3779 3781 3785                                                      
CONECT 3781 3780 3782 3786                                                      
CONECT 3782 3781 3783 3787                                                      
CONECT 3783 3782                                                                
CONECT 3784 3779                                                                
CONECT 3785 3780                                                                
CONECT 3786 3781                                                                
CONECT 3787 3778 3782                                                           
CONECT 3789 3790                                                                
CONECT 3790 3789 3791 3819                                                      
CONECT 3791 3790 3792                                                           
CONECT 3792 3791 3793 3794                                                      
CONECT 3793 3792 3818                                                           
CONECT 3794 3792 3795                                                           
CONECT 3795 3794 3796 3816                                                      
CONECT 3796 3795 3797 3817 3818                                                 
CONECT 3797 3796 3798 3814                                                      
CONECT 3798 3797 3799                                                           
CONECT 3799 3798 3800                                                           
CONECT 3800 3799 3801 3802 3813                                                 
CONECT 3801 3800                                                                
CONECT 3802 3800 3803 3811                                                      
CONECT 3803 3802 3804 3810                                                      
CONECT 3804 3803 3805                                                           
CONECT 3805 3804 3806                                                           
CONECT 3806 3805 3807                                                           
CONECT 3807 3806 3808 3809                                                      
CONECT 3808 3807                                                                
CONECT 3809 3807                                                                
CONECT 3810 3803                                                                
CONECT 3811 3802 3812                                                           
CONECT 3812 3811 3813                                                           
CONECT 3813 3800 3812 3814                                                      
CONECT 3814 3797 3813 3815                                                      
CONECT 3815 3814 3816                                                           
CONECT 3816 3795 3815                                                           
CONECT 3817 3796                                                                
CONECT 3818 3793 3796                                                           
CONECT 3819 3790 3820                                                           
CONECT 3820 3819 3821                                                           
CONECT 3821 3820 3822                                                           
CONECT 3822 3821 3823                                                           
CONECT 3823 3822 3824                                                           
CONECT 3824 3823 3825                                                           
CONECT 3825 3824 3826                                                           
CONECT 3826 3825 3827                                                           
CONECT 3827 3826 3828                                                           
CONECT 3828 3827 3829                                                           
CONECT 3829 3828 3830                                                           
CONECT 3830 3829 3831                                                           
CONECT 3831 3830 3832                                                           
CONECT 3832 3831 3833                                                           
CONECT 3833 3832 3834                                                           
CONECT 3834 3833 3835                                                           
CONECT 3835 3834                                                                
CONECT 3836 3837                                                                
CONECT 3837 3836 3838 3866                                                      
CONECT 3838 3837 3839                                                           
CONECT 3839 3838 3840 3841                                                      
CONECT 3840 3839 3865                                                           
CONECT 3841 3839 3842                                                           
CONECT 3842 3841 3843 3863                                                      
CONECT 3843 3842 3844 3864 3865                                                 
CONECT 3844 3843 3845 3861                                                      
CONECT 3845 3844 3846                                                           
CONECT 3846 3845 3847                                                           
CONECT 3847 3846 3848 3849 3860                                                 
CONECT 3848 3847                                                                
CONECT 3849 3847 3850 3858                                                      
CONECT 3850 3849 3851 3857                                                      
CONECT 3851 3850 3852                                                           
CONECT 3852 3851 3853                                                           
CONECT 3853 3852 3854                                                           
CONECT 3854 3853 3855 3856                                                      
CONECT 3855 3854                                                                
CONECT 3856 3854                                                                
CONECT 3857 3850                                                                
CONECT 3858 3849 3859                                                           
CONECT 3859 3858 3860                                                           
CONECT 3860 3847 3859 3861                                                      
CONECT 3861 3844 3860 3862                                                      
CONECT 3862 3861 3863                                                           
CONECT 3863 3842 3862                                                           
CONECT 3864 3843                                                                
CONECT 3865 3840 3843                                                           
CONECT 3866 3837 3867                                                           
CONECT 3867 3866 3868                                                           
CONECT 3868 3867 3869                                                           
CONECT 3869 3868 3870                                                           
CONECT 3870 3869 3871                                                           
CONECT 3871 3870 3872                                                           
CONECT 3872 3871 3873                                                           
CONECT 3873 3872 3874                                                           
CONECT 3874 3873 3875                                                           
CONECT 3875 3874 3876                                                           
CONECT 3876 3875 3877                                                           
CONECT 3877 3876 3878                                                           
CONECT 3878 3877 3879                                                           
CONECT 3879 3878 3880                                                           
CONECT 3880 3879 3881                                                           
CONECT 3881 3880 3882                                                           
CONECT 3882 3881                                                                
CONECT 3883 3884 3934                                                           
CONECT 3884 3883 3885 3928                                                      
CONECT 3885 3884 3929                                                           
CONECT 3886 3887 3935                                                           
CONECT 3887 3886 3927                                                           
CONECT 3888 3927                                                                
CONECT 3889 3927                                                                
CONECT 3890 3927                                                                
CONECT 3891 3892 3929 3930                                                      
CONECT 3892 3891 3893                                                           
CONECT 3893 3892 3894                                                           
CONECT 3894 3893 3895                                                           
CONECT 3895 3894 3896                                                           
CONECT 3896 3895 3897                                                           
CONECT 3897 3896 3898                                                           
CONECT 3898 3897 3899                                                           
CONECT 3899 3898 3900                                                           
CONECT 3900 3899 3901                                                           
CONECT 3901 3900 3902                                                           
CONECT 3902 3901 3903                                                           
CONECT 3903 3902 3904                                                           
CONECT 3904 3903 3905                                                           
CONECT 3905 3904 3906                                                           
CONECT 3906 3905 3907                                                           
CONECT 3907 3906 3908                                                           
CONECT 3908 3907                                                                
CONECT 3909 3910 3928 3931                                                      
CONECT 3910 3909 3911                                                           
CONECT 3911 3910 3912                                                           
CONECT 3912 3911 3913                                                           
CONECT 3913 3912 3914                                                           
CONECT 3914 3913 3915                                                           
CONECT 3915 3914 3916                                                           
CONECT 3916 3915 3917                                                           
CONECT 3917 3916 3918                                                           
CONECT 3918 3917 3919                                                           
CONECT 3919 3918 3920                                                           
CONECT 3920 3919 3921                                                           
CONECT 3921 3920 3922                                                           
CONECT 3922 3921 3923                                                           
CONECT 3923 3922 3924                                                           
CONECT 3924 3923 3925                                                           
CONECT 3925 3924 3926                                                           
CONECT 3926 3925                                                                
CONECT 3927 3887 3888 3889 3890                                                 
CONECT 3928 3884 3909                                                           
CONECT 3929 3885 3891                                                           
CONECT 3930 3891                                                                
CONECT 3931 3909                                                                
CONECT 3932 3936                                                                
CONECT 3933 3936                                                                
CONECT 3934 3883 3936                                                           
CONECT 3935 3886 3936                                                           
CONECT 3936 3932 3933 3934 3935                                                 
CONECT 3937 3938 3988                                                           
CONECT 3938 3937 3939 3982                                                      
CONECT 3939 3938 3983                                                           
CONECT 3940 3941 3989                                                           
CONECT 3941 3940 3981                                                           
CONECT 3942 3981                                                                
CONECT 3943 3981                                                                
CONECT 3944 3981                                                                
CONECT 3945 3946 3983 3984                                                      
CONECT 3946 3945 3947                                                           
CONECT 3947 3946 3948                                                           
CONECT 3948 3947 3949                                                           
CONECT 3949 3948 3950                                                           
CONECT 3950 3949 3951                                                           
CONECT 3951 3950 3952                                                           
CONECT 3952 3951 3953                                                           
CONECT 3953 3952 3954                                                           
CONECT 3954 3953 3955                                                           
CONECT 3955 3954 3956                                                           
CONECT 3956 3955 3957                                                           
CONECT 3957 3956 3958                                                           
CONECT 3958 3957 3959                                                           
CONECT 3959 3958 3960                                                           
CONECT 3960 3959 3961                                                           
CONECT 3961 3960 3962                                                           
CONECT 3962 3961                                                                
CONECT 3963 3964 3982 3985                                                      
CONECT 3964 3963 3965                                                           
CONECT 3965 3964 3966                                                           
CONECT 3966 3965 3967                                                           
CONECT 3967 3966 3968                                                           
CONECT 3968 3967 3969                                                           
CONECT 3969 3968 3970                                                           
CONECT 3970 3969 3971                                                           
CONECT 3971 3970 3972                                                           
CONECT 3972 3971 3973                                                           
CONECT 3973 3972 3974                                                           
CONECT 3974 3973 3975                                                           
CONECT 3975 3974 3976                                                           
CONECT 3976 3975 3977                                                           
CONECT 3977 3976 3978                                                           
CONECT 3978 3977 3979                                                           
CONECT 3979 3978 3980                                                           
CONECT 3980 3979                                                                
CONECT 3981 3941 3942 3943 3944                                                 
CONECT 3982 3938 3963                                                           
CONECT 3983 3939 3945                                                           
CONECT 3984 3945                                                                
CONECT 3985 3963                                                                
CONECT 3986 3990                                                                
CONECT 3987 3990                                                                
CONECT 3988 3937 3990                                                           
CONECT 3989 3940 3990                                                           
CONECT 3990 3986 3987 3988 3989                                                 
CONECT 3991 3992 3996 4000                                                      
CONECT 3992 3991 3993                                                           
CONECT 3993 3992 3994                                                           
CONECT 3994 3993 3995 3997                                                      
CONECT 3995 3994 3996                                                           
CONECT 3996 3991 3995                                                           
CONECT 3997 3994 3998                                                           
CONECT 3998 3997 3999                                                           
CONECT 3999 3998                                                                
CONECT 4000 3991 4001                                                           
CONECT 4001 4000 4002                                                           
CONECT 4002 4001 4003 4004 4005                                                 
CONECT 4003 4002                                                                
CONECT 4004 4002                                                                
CONECT 4005 4002                                                                
CONECT 4006 4007                                                                
CONECT 4007 4006 4008                                                           
CONECT 4008 4007 4009                                                           
CONECT 4009 4008 4011                                                           
CONECT 4010 4011 4012                                                           
CONECT 4011 4009 4010                                                           
CONECT 4012 4010 4014                                                           
CONECT 4013 4014 4015                                                           
CONECT 4014 4012 4013                                                           
CONECT 4015 4013 4017                                                           
CONECT 4016 4017 4018                                                           
CONECT 4017 4015 4016                                                           
CONECT 4018 4016 4020                                                           
CONECT 4019 4020 4021                                                           
CONECT 4020 4018 4019                                                           
CONECT 4021 4019                                                                
CONECT 4022 4023                                                                
CONECT 4023 4022 4024                                                           
CONECT 4024 4023 4025                                                           
CONECT 4025 4024 4027                                                           
CONECT 4026 4027 4028                                                           
CONECT 4027 4025 4026                                                           
CONECT 4028 4026 4030                                                           
CONECT 4029 4030 4031                                                           
CONECT 4030 4028 4029                                                           
CONECT 4031 4029 4033                                                           
CONECT 4032 4033 4034                                                           
CONECT 4033 4031 4032                                                           
CONECT 4034 4032 4036                                                           
CONECT 4035 4036 4037                                                           
CONECT 4036 4034 4035                                                           
CONECT 4037 4035                                                                
CONECT 4038 4039                                                                
CONECT 4039 4038 4040                                                           
CONECT 4040 4039 4041                                                           
CONECT 4041 4040 4042                                                           
CONECT 4042 4041 4043                                                           
CONECT 4043 4042 4044                                                           
CONECT 4044 4043 4045                                                           
CONECT 4045 4044 4046                                                           
CONECT 4046 4045 4047                                                           
CONECT 4047 4046 4048                                                           
CONECT 4048 4047 4049                                                           
CONECT 4049 4048 4050                                                           
CONECT 4050 4049                                                                
MASTER      297    0   12   16   24    0    0    6 4429    1  303   37          
END                                                                             



If you find results from this site helpful for your research, please cite one of our papers:

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.