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***  trail run   ***

elNémo ID: 19112215255517168

Job options:

ID        	=	 19112215255517168
JOBID     	=	 trail run 
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 trail run 

HEADER    TRANSPORT PROTEIN                       02-MAY-09   3HAP              
TITLE     CRYSTAL STRUCTURE OF BACTERIORHODOPSIN MUTANT L111A CRYSTALLIZED FROM 
TITLE    2 BICELLES                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: BACTERIORHODOPSIN;                                         
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: BR;                                                         
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 MUTATION: YES                                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HALOBACTERIUM SALINARUM;                        
SOURCE   3 ORGANISM_COMMON: HALOBACTERIUM HALOBIUM;                             
SOURCE   4 ORGANISM_TAXID: 2242;                                                
SOURCE   5 GENE: BOP, VNG_1467G;                                                
SOURCE   6 EXPRESSION_SYSTEM: HALOBACTERIUM SALINARUM;                          
SOURCE   7 EXPRESSION_SYSTEM_TAXID: 2242;                                       
SOURCE   8 EXPRESSION_SYSTEM_STRAIN: L33                                        
KEYWDS    BACTERIORHODOPSIN, PACKING FORCE, VAN DER WAALS, EVOLUTIONARY         
KEYWDS   2 CONSTRAINT, MEMBRANE PROTEIN, INTEGRAL MEMBRANE PROTEIN, HELICAL     
KEYWDS   3 MEMBRANE PROTEIN, PROTON TRANSPORT, CELL MEMBRANE, CHROMOPHORE,      
KEYWDS   4 HYDROGEN ION TRANSPORT, ION TRANSPORT, MEMBRANE, PHOTORECEPTOR       
KEYWDS   5 PROTEIN, PYRROLIDONE CARBOXYLIC ACID, RECEPTOR, RETINAL PROTEIN,     
KEYWDS   6 SENSORY TRANSDUCTION, TRANSMEMBRANE, TRANSPORT, TRANSPORT PROTEIN    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    N.H.JOH,D.YANG,J.U.BOWIE                                              
REVDAT   2   01-NOV-17 3HAP    1       REMARK                                   
REVDAT   1   22-SEP-09 3HAP    0                                                
JRNL        AUTH   N.H.JOH,A.OBERAI,D.YANG,J.P.WHITELEGGE,J.U.BOWIE             
JRNL        TITL   SIMILAR ENERGETIC CONTRIBUTIONS OF PACKING IN THE CORE OF    
JRNL        TITL 2 MEMBRANE AND WATER-SOLUBLE PROTEINS.                         
JRNL        REF    J.AM.CHEM.SOC.                V. 131 10846 2009              
JRNL        REFN                   ISSN 0002-7863                               
JRNL        PMID   19603754                                                     
JRNL        DOI    10.1021/JA904711K                                            
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.60 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0019                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD WITH PHASES                
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.60                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 21.74                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 93.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 36725                          
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) : 0.169                           
REMARK   3   R VALUE            (WORKING SET) : 0.167                           
REMARK   3   FREE R VALUE                     : 0.192                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 7.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 2871                            
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) : 1.60                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.64                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 2041                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 78.22                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2330                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 178                          
REMARK   3   BIN FREE R VALUE                    : 0.2910                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1745                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 215                                     
REMARK   3   SOLVENT ATOMS            : 154                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 19.59                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.00000                                              
REMARK   3    B22 (A**2) : 0.00000                                              
REMARK   3    B33 (A**2) : 0.00000                                              
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): 0.085         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.084         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.046         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 2.843         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.961                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.948                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2202 ; 0.010 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2994 ; 2.007 ; 2.056       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   289 ; 3.822 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    66 ;29.753 ;21.818       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   346 ;12.296 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    11 ;12.682 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   350 ; 0.177 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1506 ; 0.006 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  1109 ; 0.208 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1496 ; 0.320 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):   138 ; 0.123 ; 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 ; 0.185 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     8 ; 0.149 ; 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):  1255 ; 0.605 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  2008 ; 0.938 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1087 ; 1.553 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   951 ; 2.157 ; 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 3HAP COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 06-MAY-09.                  
REMARK 100 THE DEPOSITION ID IS D_1000052903.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 17-JAN-09                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 4.0                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : ALS                                
REMARK 200  BEAMLINE                       : 8.2.2                              
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.9998                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO                              
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 36787                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.600                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 93.9                               
REMARK 200  DATA REDUNDANCY                : 6.300                              
REMARK 200  R MERGE                    (I) : 0.05000                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 22.4310                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.60                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.66                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 78.4                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 4.10                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.38200                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: NULL                                                  
REMARK 200 STARTING MODEL: NULL                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 54.99                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.73                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 400UL 4M NAPI, 30UL 6M 1,6-HEXANEDIOL,   
REMARK 280  35UL 100% TRIETHYLENE GLYCOL, 535 UL H2O, PH 4.0, HANGING DROP,     
REMARK 280  BICELLE METHOD, TEMPERATURE 310K                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 2 2 21                         
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,-Y,Z+1/2                                             
REMARK 290       3555   -X,Y,-Z+1/2                                             
REMARK 290       4555   X,-Y,-Z                                                 
REMARK 290       5555   X+1/2,Y+1/2,Z                                           
REMARK 290       6555   -X+1/2,-Y+1/2,Z+1/2                                     
REMARK 290       7555   -X+1/2,Y+1/2,-Z+1/2                                     
REMARK 290       8555   X+1/2,-Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       64.01350            
REMARK 290   SMTRY1   3 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000 -1.000000       64.01350            
REMARK 290   SMTRY1   4  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000       22.47550            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       51.06750            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   6 -1.000000  0.000000  0.000000       22.47550            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       51.06750            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       64.01350            
REMARK 290   SMTRY1   7 -1.000000  0.000000  0.000000       22.47550            
REMARK 290   SMTRY2   7  0.000000  1.000000  0.000000       51.06750            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       64.01350            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000       22.47550            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000       51.06750            
REMARK 290   SMTRY3   8  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                                     
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 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 382  LIES ON A SPECIAL POSITION.                          
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     GLN A     1                                                      
REMARK 465     ALA A     2                                                      
REMARK 465     GLN A     3                                                      
REMARK 465     ILE A     4                                                      
REMARK 465     THR A     5                                                      
REMARK 465     GLU A   232                                                      
REMARK 465     ALA A   233                                                      
REMARK 465     GLU A   234                                                      
REMARK 465     ALA A   235                                                      
REMARK 465     PRO A   236                                                      
REMARK 465     GLU A   237                                                      
REMARK 465     PRO A   238                                                      
REMARK 465     SER A   239                                                      
REMARK 465     ALA A   240                                                      
REMARK 465     GLY A   241                                                      
REMARK 465     ASP A   242                                                      
REMARK 465     GLY A   243                                                      
REMARK 465     ALA A   244                                                      
REMARK 465     ALA A   245                                                      
REMARK 465     ALA A   246                                                      
REMARK 465     THR A   247                                                      
REMARK 465     SER A   248                                                      
REMARK 465     ASP A   249                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     GLY A 231    O                                                   
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   NZ   LYS A   216     C14  RET A   301              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    PHE A 154      -60.93    -95.05                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 610                                                                      
REMARK 610 MISSING HETEROATOM                                                   
REMARK 610 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 610 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 610 I=INSERTION CODE):                                                   
REMARK 610   M RES C SSEQI                                                      
REMARK 610     CPS A  501                                                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE RET A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 402                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 403                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 405                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D10 A 406                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE R16 A 411                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE CPS A 501                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D10 A 250                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC9                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 251                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 254                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 255                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D12 A 256                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: BC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE D10 A 257                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3HAN   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HAO   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HAQ   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HAR   RELATED DB: PDB                                   
REMARK 900 RELATED ID: 3HAS   RELATED DB: PDB                                   
DBREF  3HAP A    1   249  UNP    P02945   BACR_HALSA      14    262             
SEQADV 3HAP ALA A  111  UNP  P02945    LEU   124 ENGINEERED                     
SEQRES   1 A  249  GLN ALA GLN ILE THR GLY ARG PRO GLU TRP ILE TRP LEU          
SEQRES   2 A  249  ALA LEU GLY THR ALA LEU MET GLY LEU GLY THR LEU TYR          
SEQRES   3 A  249  PHE LEU VAL LYS GLY MET GLY VAL SER ASP PRO ASP ALA          
SEQRES   4 A  249  LYS LYS PHE TYR ALA ILE THR THR LEU VAL PRO ALA ILE          
SEQRES   5 A  249  ALA PHE THR MET TYR LEU SER MET LEU LEU GLY TYR GLY          
SEQRES   6 A  249  LEU THR MET VAL PRO PHE GLY GLY GLU GLN ASN PRO ILE          
SEQRES   7 A  249  TYR TRP ALA ARG TYR ALA ASP TRP LEU PHE THR THR PRO          
SEQRES   8 A  249  LEU LEU LEU LEU ASP LEU ALA LEU LEU VAL ASP ALA ASP          
SEQRES   9 A  249  GLN GLY THR ILE LEU ALA ALA VAL GLY ALA ASP GLY ILE          
SEQRES  10 A  249  MET ILE GLY THR GLY LEU VAL GLY ALA LEU THR LYS VAL          
SEQRES  11 A  249  TYR SER TYR ARG PHE VAL TRP TRP ALA ILE SER THR ALA          
SEQRES  12 A  249  ALA MET LEU TYR ILE LEU TYR VAL LEU PHE PHE GLY PHE          
SEQRES  13 A  249  THR SER LYS ALA GLU SER MET ARG PRO GLU VAL ALA SER          
SEQRES  14 A  249  THR PHE LYS VAL LEU ARG ASN VAL THR VAL VAL LEU TRP          
SEQRES  15 A  249  SER ALA TYR PRO VAL VAL TRP LEU ILE GLY SER GLU GLY          
SEQRES  16 A  249  ALA GLY ILE VAL PRO LEU ASN ILE GLU THR LEU LEU PHE          
SEQRES  17 A  249  MET VAL LEU ASP VAL SER ALA LYS VAL GLY PHE GLY LEU          
SEQRES  18 A  249  ILE LEU LEU ARG SER ARG ALA ILE PHE GLY GLU ALA GLU          
SEQRES  19 A  249  ALA PRO GLU PRO SER ALA GLY ASP GLY ALA ALA ALA THR          
SEQRES  20 A  249  SER ASP                                                      
HET    RET  A 301      20                                                       
HET    D12  A 402      12                                                       
HET    D12  A 403      12                                                       
HET    D12  A 405      12                                                       
HET    D10  A 406      10                                                       
HET    D10  A 409      10                                                       
HET    R16  A 411      16                                                       
HET    CPS  A 501      27                                                       
HET    D10  A 250      10                                                       
HET    D12  A 251      12                                                       
HET    HP6  A 401       7                                                       
HET    D12  A 252      12                                                       
HET    DD9  A 253       9                                                       
HET    D12  A 254      12                                                       
HET    D12  A 255      12                                                       
HET    D12  A 256      12                                                       
HET    D10  A 257      10                                                       
HETNAM     RET RETINAL                                                          
HETNAM     D12 DODECANE                                                         
HETNAM     D10 DECANE                                                           
HETNAM     R16 HEXADECANE                                                       
HETNAM     CPS 3-[(3-CHOLAMIDOPROPYL)DIMETHYLAMMONIO]-1-                        
HETNAM   2 CPS  PROPANESULFONATE                                                
HETNAM     HP6 HEPTANE                                                          
HETNAM     DD9 NONANE                                                           
HETSYN     CPS CHAPS                                                            
FORMUL   2  RET    C20 H28 O                                                    
FORMUL   3  D12    8(C12 H26)                                                   
FORMUL   6  D10    4(C10 H22)                                                   
FORMUL   8  R16    C16 H34                                                      
FORMUL   9  CPS    C32 H58 N2 O7 S                                              
FORMUL  12  HP6    C7 H16                                                       
FORMUL  14  DD9    C9 H20                                                       
FORMUL  19  HOH   *154(H2 O)                                                    
HELIX    1   1 GLU A    9  VAL A   34  1                                  26    
HELIX    2   2 ASP A   36  LEU A   62  1                                  27    
HELIX    3   3 TRP A   80  ASP A  102  1                                  23    
HELIX    4   4 ASP A  104  THR A  128  1                                  25    
HELIX    5   5 VAL A  130  PHE A  154  1                                  25    
HELIX    6   6 PHE A  154  GLU A  161  1                                   8    
HELIX    7   7 ARG A  164  GLY A  192  1                                  29    
HELIX    8   8 PRO A  200  ARG A  225  1                                  26    
HELIX    9   9 SER A  226  PHE A  230  5                                   5    
SHEET    1   A 2 LEU A  66  PHE A  71  0                                        
SHEET    2   A 2 GLU A  74  TYR A  79 -1  O  ILE A  78   N  THR A  67           
LINK         NZ  LYS A 216                 C15 RET A 301     1555   1555  1.27  
SITE     1 AC1 12 TRP A  86  THR A  90  TRP A 138  SER A 141                    
SITE     2 AC1 12 THR A 142  TRP A 182  TYR A 185  PRO A 186                    
SITE     3 AC1 12 TRP A 189  ASP A 212  ALA A 215  LYS A 216                    
SITE     1 AC2  1 D12 A 403                                                     
SITE     1 AC3  1 D12 A 402                                                     
SITE     1 AC4  1 ASN A 176                                                     
SITE     1 AC5  5 THR A  17  ALA A  44  D12 A 251  D12 A 256                    
SITE     2 AC5  5 CPS A 501                                                     
SITE     1 AC6  1 VAL A 136                                                     
SITE     1 AC7  9 GLY A   6  LYS A  41  LEU A  61  GLN A 105                    
SITE     2 AC7  9 ILE A 108  HOH A 298  HOH A 329  HOH A 351                    
SITE     3 AC7  9 D10 A 406                                                     
SITE     1 AC8  1 LEU A  25                                                     
SITE     1 AC9  2 LEU A  15  D10 A 406                                          
SITE     1 BC1  1 HOH A 375                                                     
SITE     1 BC2  1 ALA A 110                                                     
SITE     1 BC3  3 LEU A  28  LEU A  48  D10 A 406                               
SITE     1 BC4  1 ILE A 203                                                     
CRYST1   44.951  102.135  128.027  90.00  90.00  90.00 C 2 2 21      8          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.022246  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.009791  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.007811        0.00000                         
ATOM      1  N   GLY A   6       8.055  19.701 -18.547  1.00 29.81           N  
ATOM      2  CA  GLY A   6       7.290  18.523 -19.046  1.00 29.21           C  
ATOM      3  C   GLY A   6       7.904  17.176 -18.698  1.00 28.38           C  
ATOM      4  O   GLY A   6       7.377  16.138 -19.105  1.00 29.49           O  
ATOM      5  N   ARG A   7       9.005  17.193 -17.942  1.00 27.33           N  
ATOM      6  CA AARG A   7       9.706  15.965 -17.547  0.60 26.38           C  
ATOM      7  CA BARG A   7       9.713  15.972 -17.544  0.40 26.23           C  
ATOM      8  C   ARG A   7       8.882  15.190 -16.519  1.00 25.47           C  
ATOM      9  O   ARG A   7       8.373  15.778 -15.576  1.00 25.28           O  
ATOM     10  CB AARG A   7      11.088  16.299 -16.979  0.60 26.31           C  
ATOM     11  CB BARG A   7      11.087  16.336 -16.972  0.40 26.24           C  
ATOM     12  CG AARG A   7      12.023  17.009 -17.962  0.60 26.83           C  
ATOM     13  CG BARG A   7      11.956  17.158 -17.932  0.40 26.46           C  
ATOM     14  CD AARG A   7      13.468  17.004 -17.468  0.60 26.99           C  
ATOM     15  CD BARG A   7      12.918  18.090 -17.200  0.40 26.48           C  
ATOM     16  NE AARG A   7      14.049  15.659 -17.468  0.60 27.77           N  
ATOM     17  NE BARG A   7      13.428  19.129 -18.096  0.40 27.18           N  
ATOM     18  CZ AARG A   7      14.715  15.126 -18.488  0.60 29.35           C  
ATOM     19  CZ BARG A   7      14.091  20.216 -17.708  0.40 26.67           C  
ATOM     20  NH1AARG A   7      14.901  15.812 -19.612  0.60 28.94           N  
ATOM     21  NH1BARG A   7      14.344  20.433 -16.423  0.40 26.52           N  
ATOM     22  NH2AARG A   7      15.198  13.899 -18.386  0.60 30.34           N  
ATOM     23  NH2BARG A   7      14.502  21.095 -18.612  0.40 27.16           N  
ATOM     24  N   PRO A   8       8.743  13.853 -16.703  1.00 24.28           N  
ATOM     25  CA  PRO A   8       7.810  13.114 -15.834  1.00 23.09           C  
ATOM     26  C   PRO A   8       8.108  13.196 -14.336  1.00 22.22           C  
ATOM     27  O   PRO A   8       7.193  13.052 -13.520  1.00 22.59           O  
ATOM     28  CB  PRO A   8       7.931  11.660 -16.315  1.00 23.38           C  
ATOM     29  CG  PRO A   8       9.176  11.596 -17.116  1.00 23.79           C  
ATOM     30  CD  PRO A   8       9.392  12.965 -17.690  1.00 24.06           C  
ATOM     31  N   GLU A   9       9.371  13.420 -13.988  1.00 20.27           N  
ATOM     32  CA  GLU A   9       9.765  13.539 -12.575  1.00 19.04           C  
ATOM     33  C   GLU A   9       9.319  14.864 -11.930  1.00 18.62           C  
ATOM     34  O   GLU A   9       9.462  15.039 -10.717  1.00 18.50           O  
ATOM     35  CB  GLU A   9      11.282  13.368 -12.423  1.00 18.58           C  
ATOM     36  CG  GLU A   9      12.130  14.493 -13.004  1.00 18.70           C  
ATOM     37  CD  GLU A   9      12.482  14.299 -14.477  1.00 19.12           C  
ATOM     38  OE1 GLU A   9      11.849  13.456 -15.153  1.00 19.77           O  
ATOM     39  OE2 GLU A   9      13.385  15.016 -14.962  1.00 20.63           O  
ATOM     40  N   TRP A  10       8.782  15.793 -12.726  1.00 18.04           N  
ATOM     41  CA  TRP A  10       8.399  17.114 -12.206  1.00 17.59           C  
ATOM     42  C   TRP A  10       7.427  17.015 -11.026  1.00 16.90           C  
ATOM     43  O   TRP A  10       7.498  17.817 -10.098  1.00 16.58           O  
ATOM     44  CB  TRP A  10       7.838  18.041 -13.306  1.00 18.77           C  
ATOM     45  CG  TRP A  10       6.387  17.818 -13.639  1.00 19.88           C  
ATOM     46  CD1 TRP A  10       5.893  17.108 -14.695  1.00 21.52           C  
ATOM     47  CD2 TRP A  10       5.242  18.325 -12.927  1.00 20.20           C  
ATOM     48  NE1 TRP A  10       4.520  17.128 -14.680  1.00 22.64           N  
ATOM     49  CE2 TRP A  10       4.092  17.868 -13.609  1.00 22.08           C  
ATOM     50  CE3 TRP A  10       5.078  19.117 -11.780  1.00 19.79           C  
ATOM     51  CZ2 TRP A  10       2.787  18.173 -13.180  1.00 21.20           C  
ATOM     52  CZ3 TRP A  10       3.783  19.411 -11.347  1.00 20.99           C  
ATOM     53  CH2 TRP A  10       2.655  18.941 -12.051  1.00 21.18           C  
ATOM     54  N   ILE A  11       6.548  16.012 -11.039  1.00 16.31           N  
ATOM     55  CA  ILE A  11       5.559  15.875  -9.970  1.00 16.64           C  
ATOM     56  C   ILE A  11       6.224  15.657  -8.601  1.00 16.06           C  
ATOM     57  O   ILE A  11       5.761  16.192  -7.588  1.00 15.55           O  
ATOM     58  CB  ILE A  11       4.490  14.793 -10.288  1.00 17.68           C  
ATOM     59  CG1 ILE A  11       3.389  14.781  -9.222  1.00 19.70           C  
ATOM     60  CG2 ILE A  11       5.106  13.423 -10.438  1.00 18.72           C  
ATOM     61  CD1 ILE A  11       2.530  16.053  -9.205  1.00 21.38           C  
ATOM     62  N   TRP A  12       7.328  14.909  -8.590  1.00 15.50           N  
ATOM     63  CA  TRP A  12       8.033  14.644  -7.327  1.00 15.34           C  
ATOM     64  C   TRP A  12       8.889  15.834  -6.893  1.00 14.98           C  
ATOM     65  O   TRP A  12       9.066  16.090  -5.688  1.00 14.73           O  
ATOM     66  CB  TRP A  12       8.848  13.350  -7.426  1.00 15.58           C  
ATOM     67  CG  TRP A  12       8.004  12.188  -7.905  1.00 16.15           C  
ATOM     68  CD1 TRP A  12       8.216  11.431  -9.026  1.00 16.65           C  
ATOM     69  CD2 TRP A  12       6.794  11.695  -7.312  1.00 16.70           C  
ATOM     70  NE1 TRP A  12       7.230  10.477  -9.150  1.00 17.71           N  
ATOM     71  CE2 TRP A  12       6.339  10.622  -8.122  1.00 17.66           C  
ATOM     72  CE3 TRP A  12       6.061  12.040  -6.170  1.00 17.69           C  
ATOM     73  CZ2 TRP A  12       5.177   9.894  -7.825  1.00 18.33           C  
ATOM     74  CZ3 TRP A  12       4.894  11.316  -5.877  1.00 18.27           C  
ATOM     75  CH2 TRP A  12       4.477  10.250  -6.699  1.00 18.10           C  
ATOM     76  N   LEU A  13       9.387  16.583  -7.873  1.00 14.85           N  
ATOM     77  CA  LEU A  13      10.066  17.850  -7.588  1.00 14.34           C  
ATOM     78  C   LEU A  13       9.080  18.851  -6.984  1.00 14.71           C  
ATOM     79  O   LEU A  13       9.407  19.551  -6.023  1.00 14.67           O  
ATOM     80  CB  LEU A  13      10.703  18.419  -8.848  1.00 14.59           C  
ATOM     81  CG  LEU A  13      11.820  17.571  -9.460  1.00 14.16           C  
ATOM     82  CD1 LEU A  13      12.315  18.173 -10.773  1.00 15.45           C  
ATOM     83  CD2 LEU A  13      12.961  17.403  -8.458  1.00 15.24           C  
ATOM     84  N   ALA A  14       7.863  18.890  -7.527  1.00 14.82           N  
ATOM     85  CA  ALA A  14       6.803  19.753  -6.991  1.00 14.85           C  
ATOM     86  C   ALA A  14       6.409  19.361  -5.571  1.00 14.67           C  
ATOM     87  O   ALA A  14       6.311  20.220  -4.695  1.00 14.83           O  
ATOM     88  CB  ALA A  14       5.574  19.731  -7.910  1.00 15.01           C  
ATOM     89  N   LEU A  15       6.188  18.069  -5.325  1.00 14.58           N  
ATOM     90  CA ALEU A  15       5.828  17.612  -3.987  0.70 14.41           C  
ATOM     91  CA BLEU A  15       5.828  17.628  -3.982  0.30 14.43           C  
ATOM     92  C   LEU A  15       6.973  17.861  -2.997  1.00 14.29           C  
ATOM     93  O   LEU A  15       6.745  18.262  -1.854  1.00 14.68           O  
ATOM     94  CB ALEU A  15       5.435  16.134  -4.014  0.70 14.80           C  
ATOM     95  CB BLEU A  15       5.370  16.167  -3.981  0.30 14.67           C  
ATOM     96  CG ALEU A  15       4.905  15.502  -2.726  0.70 14.42           C  
ATOM     97  CG BLEU A  15       4.010  15.908  -4.642  0.30 14.73           C  
ATOM     98  CD1ALEU A  15       3.834  16.363  -2.052  0.70 16.14           C  
ATOM     99  CD1BLEU A  15       3.715  14.423  -4.673  0.30 15.39           C  
ATOM    100  CD2ALEU A  15       4.392  14.097  -3.000  0.70 14.67           C  
ATOM    101  CD2BLEU A  15       2.892  16.648  -3.917  0.30 15.33           C  
ATOM    102  N   GLY A  16       8.206  17.633  -3.447  1.00 13.65           N  
ATOM    103  CA  GLY A  16       9.387  17.914  -2.612  1.00 13.16           C  
ATOM    104  C   GLY A  16       9.445  19.387  -2.228  1.00 13.12           C  
ATOM    105  O   GLY A  16       9.689  19.722  -1.063  1.00 13.14           O  
ATOM    106  N   THR A  17       9.214  20.259  -3.212  1.00 12.97           N  
ATOM    107  CA ATHR A  17       9.208  21.700  -2.973  0.80 12.59           C  
ATOM    108  CA BTHR A  17       9.198  21.709  -2.967  0.20 13.09           C  
ATOM    109  C   THR A  17       8.173  22.058  -1.899  1.00 12.96           C  
ATOM    110  O   THR A  17       8.458  22.824  -0.966  1.00 13.21           O  
ATOM    111  CB ATHR A  17       8.908  22.468  -4.296  0.80 12.21           C  
ATOM    112  CB BTHR A  17       8.843  22.533  -4.233  0.20 12.99           C  
ATOM    113  OG1ATHR A  17       9.943  22.182  -5.245  0.80 11.69           O  
ATOM    114  OG1BTHR A  17       7.610  22.065  -4.780  0.20 13.97           O  
ATOM    115  CG2ATHR A  17       8.911  23.967  -4.042  0.80 12.61           C  
ATOM    116  CG2BTHR A  17       9.922  22.434  -5.279  0.20 12.96           C  
ATOM    117  N   ALA A  18       6.968  21.498  -2.036  1.00 13.20           N  
ATOM    118  CA  ALA A  18       5.889  21.739  -1.079  1.00 13.07           C  
ATOM    119  C   ALA A  18       6.255  21.284   0.330  1.00 12.81           C  
ATOM    120  O   ALA A  18       6.067  22.025   1.289  1.00 13.53           O  
ATOM    121  CB  ALA A  18       4.624  21.048  -1.528  1.00 13.39           C  
ATOM    122  N   LEU A  19       6.767  20.059   0.455  1.00 12.57           N  
ATOM    123  CA  LEU A  19       7.063  19.494   1.769  1.00 12.07           C  
ATOM    124  C   LEU A  19       8.241  20.198   2.449  1.00 11.91           C  
ATOM    125  O   LEU A  19       8.204  20.453   3.657  1.00 12.62           O  
ATOM    126  CB  LEU A  19       7.295  17.980   1.649  1.00 12.48           C  
ATOM    127  CG  LEU A  19       6.055  17.202   1.194  1.00 13.27           C  
ATOM    128  CD1 LEU A  19       6.404  15.754   0.855  1.00 13.48           C  
ATOM    129  CD2 LEU A  19       4.954  17.271   2.256  1.00 16.42           C  
ATOM    130  N   MET A  20       9.276  20.537   1.678  1.00 11.88           N  
ATOM    131  CA  MET A  20      10.400  21.307   2.250  1.00 11.69           C  
ATOM    132  C   MET A  20       9.954  22.718   2.644  1.00 11.76           C  
ATOM    133  O   MET A  20      10.363  23.238   3.685  1.00 12.05           O  
ATOM    134  CB  MET A  20      11.572  21.386   1.270  1.00 12.08           C  
ATOM    135  CG  MET A  20      12.177  20.043   0.919  1.00 12.16           C  
ATOM    136  SD  MET A  20      12.826  19.206   2.376  1.00 12.65           S  
ATOM    137  CE  MET A  20      13.599  17.826   1.545  1.00 13.95           C  
ATOM    138  N   GLY A  21       9.129  23.338   1.799  1.00 12.28           N  
ATOM    139  CA  GLY A  21       8.625  24.686   2.108  1.00 12.03           C  
ATOM    140  C   GLY A  21       7.773  24.729   3.366  1.00 12.34           C  
ATOM    141  O   GLY A  21       7.994  25.561   4.259  1.00 12.63           O  
ATOM    142  N   LEU A  22       6.819  23.810   3.459  1.00 12.74           N  
ATOM    143  CA  LEU A  22       5.946  23.736   4.636  1.00 12.76           C  
ATOM    144  C   LEU A  22       6.746  23.399   5.904  1.00 12.75           C  
ATOM    145  O   LEU A  22       6.514  23.988   6.956  1.00 13.42           O  
ATOM    146  CB  LEU A  22       4.821  22.712   4.427  1.00 13.49           C  
ATOM    147  CG  LEU A  22       3.797  23.091   3.360  1.00 14.36           C  
ATOM    148  CD1 LEU A  22       3.010  21.856   2.901  1.00 17.11           C  
ATOM    149  CD2 LEU A  22       2.886  24.232   3.874  1.00 15.71           C  
ATOM    150  N   GLY A  23       7.688  22.463   5.790  1.00 12.88           N  
ATOM    151  CA  GLY A  23       8.573  22.115   6.909  1.00 12.67           C  
ATOM    152  C   GLY A  23       9.354  23.321   7.394  1.00 12.38           C  
ATOM    153  O   GLY A  23       9.381  23.606   8.599  1.00 13.33           O  
ATOM    154  N   THR A  24       9.938  24.063   6.455  1.00 12.49           N  
ATOM    155  CA  THR A  24      10.708  25.268   6.787  1.00 12.29           C  
ATOM    156  C   THR A  24       9.853  26.286   7.547  1.00 12.77           C  
ATOM    157  O   THR A  24      10.283  26.836   8.580  1.00 13.16           O  
ATOM    158  CB  THR A  24      11.293  25.949   5.513  1.00 12.44           C  
ATOM    159  OG1 THR A  24      12.103  25.013   4.784  1.00 12.79           O  
ATOM    160  CG2 THR A  24      12.152  27.158   5.903  1.00 11.80           C  
ATOM    161  N   LEU A  25       8.660  26.553   7.006  1.00 12.72           N  
ATOM    162  CA ALEU A  25       7.756  27.545   7.593  0.60 13.77           C  
ATOM    163  CA BLEU A  25       7.752  27.534   7.571  0.40 13.41           C  
ATOM    164  C   LEU A  25       7.369  27.159   9.011  1.00 13.52           C  
ATOM    165  O   LEU A  25       7.393  27.991   9.913  1.00 13.62           O  
ATOM    166  CB ALEU A  25       6.501  27.739   6.739  0.60 14.60           C  
ATOM    167  CB BLEU A  25       6.530  27.638   6.662  0.40 13.77           C  
ATOM    168  CG ALEU A  25       6.669  28.435   5.391  0.60 14.61           C  
ATOM    169  CG BLEU A  25       5.491  28.705   6.944  0.40 13.22           C  
ATOM    170  CD1ALEU A  25       5.320  28.952   4.937  0.60 16.39           C  
ATOM    171  CD1BLEU A  25       5.124  29.375   5.640  0.40 13.78           C  
ATOM    172  CD2ALEU A  25       7.680  29.584   5.426  0.60 17.11           C  
ATOM    173  CD2BLEU A  25       4.302  28.033   7.569  0.40 13.03           C  
ATOM    174  N   TYR A  26       7.034  25.886   9.216  1.00 13.53           N  
ATOM    175  CA  TYR A  26       6.630  25.411  10.532  1.00 13.84           C  
ATOM    176  C   TYR A  26       7.782  25.523  11.541  1.00 12.79           C  
ATOM    177  O   TYR A  26       7.591  25.974  12.683  1.00 12.61           O  
ATOM    178  CB  TYR A  26       6.122  23.972  10.431  1.00 14.44           C  
ATOM    179  CG  TYR A  26       5.694  23.395  11.752  1.00 16.78           C  
ATOM    180  CD1 TYR A  26       4.571  23.892  12.421  1.00 18.55           C  
ATOM    181  CD2 TYR A  26       6.427  22.368  12.349  1.00 17.48           C  
ATOM    182  CE1 TYR A  26       4.174  23.360  13.639  1.00 20.17           C  
ATOM    183  CE2 TYR A  26       6.045  21.837  13.581  1.00 18.50           C  
ATOM    184  CZ  TYR A  26       4.929  22.334  14.213  1.00 19.82           C  
ATOM    185  OH  TYR A  26       4.568  21.801  15.426  1.00 21.62           O  
ATOM    186  N   PHE A  27       8.987  25.125  11.116  1.00 12.25           N  
ATOM    187  CA  PHE A  27      10.157  25.194  12.005  1.00 12.01           C  
ATOM    188  C   PHE A  27      10.495  26.639  12.362  1.00 12.30           C  
ATOM    189  O   PHE A  27      10.876  26.927  13.492  1.00 12.72           O  
ATOM    190  CB  PHE A  27      11.400  24.513  11.409  1.00 11.77           C  
ATOM    191  CG  PHE A  27      11.272  23.017  11.177  1.00 11.26           C  
ATOM    192  CD1 PHE A  27      10.249  22.256  11.750  1.00 12.60           C  
ATOM    193  CD2 PHE A  27      12.226  22.368  10.397  1.00 11.60           C  
ATOM    194  CE1 PHE A  27      10.170  20.863  11.526  1.00 11.00           C  
ATOM    195  CE2 PHE A  27      12.160  20.990  10.162  1.00 12.81           C  
ATOM    196  CZ  PHE A  27      11.125  20.232  10.717  1.00 11.50           C  
ATOM    197  N   LEU A  28      10.354  27.530  11.382  1.00 12.55           N  
ATOM    198  CA ALEU A  28      10.587  28.952  11.610  0.70 12.83           C  
ATOM    199  CA BLEU A  28      10.567  28.963  11.581  0.30 12.96           C  
ATOM    200  C   LEU A  28       9.586  29.530  12.618  1.00 13.17           C  
ATOM    201  O   LEU A  28       9.969  30.256  13.528  1.00 13.06           O  
ATOM    202  CB ALEU A  28      10.528  29.719  10.294  0.70 13.20           C  
ATOM    203  CB BLEU A  28      10.409  29.689  10.241  0.30 13.22           C  
ATOM    204  CG ALEU A  28      10.728  31.228  10.433  0.70 12.77           C  
ATOM    205  CG BLEU A  28      11.114  31.025   9.993  0.30 13.61           C  
ATOM    206  CD1ALEU A  28      12.187  31.553  10.775  0.70 13.34           C  
ATOM    207  CD1BLEU A  28      11.125  31.323   8.509  0.30 13.77           C  
ATOM    208  CD2ALEU A  28      10.298  31.933   9.154  0.70 13.33           C  
ATOM    209  CD2BLEU A  28      10.459  32.165  10.752  0.30 14.87           C  
ATOM    210  N   VAL A  29       8.309  29.207  12.468  1.00 13.02           N  
ATOM    211  CA  VAL A  29       7.295  29.710  13.394  1.00 13.55           C  
ATOM    212  C   VAL A  29       7.580  29.235  14.810  1.00 14.36           C  
ATOM    213  O   VAL A  29       7.609  30.031  15.752  1.00 15.05           O  
ATOM    214  CB  VAL A  29       5.885  29.317  12.940  1.00 13.60           C  
ATOM    215  CG1 VAL A  29       4.852  29.643  14.032  1.00 14.12           C  
ATOM    216  CG2 VAL A  29       5.567  30.032  11.625  1.00 13.10           C  
ATOM    217  N   LYS A  30       7.831  27.933  14.954  1.00 14.07           N  
ATOM    218  CA  LYS A  30       8.150  27.384  16.276  1.00 15.46           C  
ATOM    219  C   LYS A  30       9.434  27.972  16.846  1.00 15.37           C  
ATOM    220  O   LYS A  30       9.476  28.333  18.027  1.00 16.09           O  
ATOM    221  CB  LYS A  30       8.230  25.860  16.218  1.00 15.96           C  
ATOM    222  CG  LYS A  30       6.912  25.213  15.848  1.00 19.63           C  
ATOM    223  CD  LYS A  30       5.816  25.601  16.848  1.00 26.19           C  
ATOM    224  CE  LYS A  30       4.430  25.333  16.303  1.00 29.19           C  
ATOM    225  NZ  LYS A  30       3.409  25.395  17.394  1.00 32.53           N  
ATOM    226  N   GLY A  31      10.458  28.104  16.002  1.00 15.15           N  
ATOM    227  CA  GLY A  31      11.776  28.591  16.430  1.00 15.77           C  
ATOM    228  C   GLY A  31      11.790  30.041  16.862  1.00 16.56           C  
ATOM    229  O   GLY A  31      12.453  30.407  17.839  1.00 16.79           O  
ATOM    230  N   MET A  32      11.049  30.867  16.137  1.00 16.40           N  
ATOM    231  CA AMET A  32      10.952  32.301  16.440  0.50 17.27           C  
ATOM    232  CA BMET A  32      11.003  32.281  16.478  0.50 17.47           C  
ATOM    233  C   MET A  32      10.242  32.523  17.773  1.00 17.94           C  
ATOM    234  O   MET A  32      10.426  33.560  18.418  1.00 18.74           O  
ATOM    235  CB AMET A  32      10.221  33.056  15.321  0.50 17.04           C  
ATOM    236  CB BMET A  32      10.447  33.094  15.321  0.50 17.09           C  
ATOM    237  CG AMET A  32      11.009  33.218  14.014  0.50 17.60           C  
ATOM    238  CG BMET A  32      11.422  33.124  14.166  0.50 17.59           C  
ATOM    239  SD AMET A  32      12.465  34.284  14.117  0.50 20.12           S  
ATOM    240  SD BMET A  32      11.065  34.389  12.968  0.50 18.44           S  
ATOM    241  CE AMET A  32      11.701  35.904  14.201  0.50 19.32           C  
ATOM    242  CE BMET A  32      11.380  35.883  13.911  0.50 18.12           C  
ATOM    243  N   GLY A  33       9.419  31.554  18.168  1.00 18.51           N  
ATOM    244  CA  GLY A  33       8.688  31.623  19.430  1.00 20.11           C  
ATOM    245  C   GLY A  33       9.515  31.324  20.675  1.00 21.55           C  
ATOM    246  O   GLY A  33       9.256  31.886  21.740  1.00 22.05           O  
ATOM    247  N   VAL A  34      10.521  30.462  20.544  1.00 21.78           N  
ATOM    248  CA AVAL A  34      11.294  30.028  21.718  0.60 22.28           C  
ATOM    249  CA BVAL A  34      11.335  29.992  21.674  0.40 22.21           C  
ATOM    250  C   VAL A  34      12.312  31.068  22.172  1.00 22.71           C  
ATOM    251  O   VAL A  34      12.844  31.840  21.369  1.00 23.26           O  
ATOM    252  CB AVAL A  34      11.983  28.638  21.525  0.60 22.32           C  
ATOM    253  CB BVAL A  34      12.094  28.689  21.275  0.40 22.07           C  
ATOM    254  CG1AVAL A  34      10.961  27.579  21.127  0.60 21.73           C  
ATOM    255  CG1BVAL A  34      13.129  28.288  22.316  0.40 22.01           C  
ATOM    256  CG2AVAL A  34      13.124  28.713  20.525  0.60 22.89           C  
ATOM    257  CG2BVAL A  34      11.105  27.556  21.048  0.40 21.80           C  
ATOM    258  N   SER A  35      12.558  31.102  23.485  1.00 23.29           N  
ATOM    259  CA ASER A  35      13.491  32.066  24.065  0.50 23.63           C  
ATOM    260  CA BSER A  35      13.486  32.066  24.077  0.50 23.77           C  
ATOM    261  C   SER A  35      14.806  31.439  24.531  1.00 23.83           C  
ATOM    262  O   SER A  35      15.835  32.116  24.588  1.00 24.19           O  
ATOM    263  CB ASER A  35      12.825  32.831  25.214  0.50 23.75           C  
ATOM    264  CB BSER A  35      12.821  32.790  25.250  0.50 23.91           C  
ATOM    265  OG ASER A  35      12.155  31.951  26.099  0.50 23.56           O  
ATOM    266  OG BSER A  35      11.768  33.621  24.798  0.50 24.61           O  
ATOM    267  N   ASP A  36      14.780  30.146  24.852  1.00 23.82           N  
ATOM    268  CA  ASP A  36      15.981  29.448  25.334  1.00 23.93           C  
ATOM    269  C   ASP A  36      17.124  29.517  24.317  1.00 24.11           C  
ATOM    270  O   ASP A  36      16.951  29.094  23.178  1.00 23.30           O  
ATOM    271  CB  ASP A  36      15.661  27.989  25.661  1.00 24.13           C  
ATOM    272  CG  ASP A  36      16.858  27.245  26.234  1.00 25.06           C  
ATOM    273  OD1 ASP A  36      17.171  27.464  27.419  1.00 27.73           O  
ATOM    274  OD2 ASP A  36      17.486  26.442  25.511  1.00 24.32           O  
ATOM    275  N   PRO A  37      18.290  30.061  24.719  1.00 24.23           N  
ATOM    276  CA  PRO A  37      19.431  30.181  23.796  1.00 24.37           C  
ATOM    277  C   PRO A  37      19.881  28.857  23.158  1.00 23.97           C  
ATOM    278  O   PRO A  37      20.120  28.817  21.945  1.00 24.14           O  
ATOM    279  CB  PRO A  37      20.536  30.785  24.676  1.00 24.90           C  
ATOM    280  CG  PRO A  37      19.790  31.502  25.759  1.00 25.03           C  
ATOM    281  CD  PRO A  37      18.597  30.639  26.044  1.00 24.58           C  
ATOM    282  N   ASP A  38      19.980  27.786  23.947  1.00 23.62           N  
ATOM    283  CA  ASP A  38      20.357  26.483  23.384  1.00 23.18           C  
ATOM    284  C   ASP A  38      19.337  26.008  22.357  1.00 22.07           C  
ATOM    285  O   ASP A  38      19.705  25.581  21.253  1.00 21.89           O  
ATOM    286  CB  ASP A  38      20.535  25.424  24.473  1.00 23.78           C  
ATOM    287  CG  ASP A  38      21.911  25.481  25.122  1.00 26.96           C  
ATOM    288  OD1 ASP A  38      22.687  26.412  24.813  1.00 29.66           O  
ATOM    289  OD2 ASP A  38      22.216  24.578  25.931  1.00 30.95           O  
ATOM    290  N   ALA A  39      18.055  26.083  22.702  1.00 20.24           N  
ATOM    291  CA  ALA A  39      17.024  25.615  21.770  1.00 19.40           C  
ATOM    292  C   ALA A  39      17.039  26.427  20.481  1.00 19.06           C  
ATOM    293  O   ALA A  39      16.804  25.887  19.394  1.00 18.77           O  
ATOM    294  CB  ALA A  39      15.651  25.637  22.414  1.00 19.37           C  
ATOM    295  N   LYS A  40      17.330  27.721  20.598  1.00 18.65           N  
ATOM    296  CA  LYS A  40      17.362  28.610  19.429  1.00 19.62           C  
ATOM    297  C   LYS A  40      18.423  28.170  18.416  1.00 18.48           C  
ATOM    298  O   LYS A  40      18.188  28.254  17.205  1.00 18.67           O  
ATOM    299  CB  LYS A  40      17.596  30.065  19.851  1.00 19.33           C  
ATOM    300  CG  LYS A  40      16.347  30.725  20.433  1.00 21.96           C  
ATOM    301  CD  LYS A  40      16.519  32.229  20.675  1.00 22.87           C  
ATOM    302  CE  LYS A  40      17.531  32.542  21.762  1.00 29.16           C  
ATOM    303  NZ  LYS A  40      17.439  33.965  22.230  1.00 31.89           N  
ATOM    304  N   LYS A  41      19.573  27.703  18.915  1.00 17.94           N  
ATOM    305  CA ALYS A  41      20.648  27.213  18.063  0.50 17.34           C  
ATOM    306  CA BLYS A  41      20.658  27.202  18.067  0.50 17.60           C  
ATOM    307  C   LYS A  41      20.175  26.015  17.235  1.00 16.50           C  
ATOM    308  O   LYS A  41      20.375  25.971  16.020  1.00 16.77           O  
ATOM    309  CB ALYS A  41      21.852  26.828  18.916  0.50 17.76           C  
ATOM    310  CB BLYS A  41      21.869  26.781  18.910  0.50 17.80           C  
ATOM    311  CG ALYS A  41      23.149  26.737  18.157  0.50 18.37           C  
ATOM    312  CG BLYS A  41      22.619  27.922  19.579  0.50 18.43           C  
ATOM    313  CD ALYS A  41      24.273  26.378  19.115  0.50 20.40           C  
ATOM    314  CD BLYS A  41      23.796  27.395  20.400  0.50 18.95           C  
ATOM    315  CE ALYS A  41      25.622  26.475  18.435  0.50 22.20           C  
ATOM    316  CE BLYS A  41      24.609  28.524  21.018  0.50 20.73           C  
ATOM    317  NZ ALYS A  41      26.736  26.589  19.413  0.50 22.07           N  
ATOM    318  NZ BLYS A  41      25.322  29.331  19.986  0.50 21.64           N  
ATOM    319  N   PHE A  42      19.516  25.056  17.886  1.00 15.14           N  
ATOM    320  CA  PHE A  42      18.995  23.886  17.171  1.00 13.39           C  
ATOM    321  C   PHE A  42      17.941  24.309  16.155  1.00 13.20           C  
ATOM    322  O   PHE A  42      17.889  23.776  15.047  1.00 12.45           O  
ATOM    323  CB  PHE A  42      18.400  22.865  18.147  1.00 13.40           C  
ATOM    324  CG  PHE A  42      19.440  22.102  18.917  1.00 12.83           C  
ATOM    325  CD1 PHE A  42      20.151  21.080  18.303  1.00 12.52           C  
ATOM    326  CD2 PHE A  42      19.710  22.408  20.256  1.00 14.18           C  
ATOM    327  CE1 PHE A  42      21.124  20.375  19.003  1.00 12.97           C  
ATOM    328  CE2 PHE A  42      20.675  21.700  20.977  1.00 13.60           C  
ATOM    329  CZ  PHE A  42      21.379  20.676  20.354  1.00 13.93           C  
ATOM    330  N   TYR A  43      17.100  25.265  16.539  1.00 13.19           N  
ATOM    331  CA  TYR A  43      16.082  25.760  15.597  1.00 13.45           C  
ATOM    332  C   TYR A  43      16.706  26.440  14.387  1.00 13.76           C  
ATOM    333  O   TYR A  43      16.263  26.231  13.257  1.00 14.09           O  
ATOM    334  CB  TYR A  43      15.073  26.692  16.280  1.00 13.49           C  
ATOM    335  CG  TYR A  43      13.882  25.963  16.871  1.00 13.62           C  
ATOM    336  CD1 TYR A  43      12.837  25.514  16.061  1.00 13.65           C  
ATOM    337  CD2 TYR A  43      13.794  25.732  18.245  1.00 15.62           C  
ATOM    338  CE1 TYR A  43      11.730  24.860  16.605  1.00 14.18           C  
ATOM    339  CE2 TYR A  43      12.694  25.069  18.785  1.00 14.61           C  
ATOM    340  CZ  TYR A  43      11.678  24.643  17.962  1.00 14.73           C  
ATOM    341  OH  TYR A  43      10.595  23.990  18.516  1.00 17.26           O  
ATOM    342  N   ALA A  44      17.740  27.244  14.615  1.00 14.05           N  
ATOM    343  CA  ALA A  44      18.394  27.939  13.501  1.00 13.99           C  
ATOM    344  C   ALA A  44      18.994  26.943  12.502  1.00 14.49           C  
ATOM    345  O   ALA A  44      18.727  27.006  11.297  1.00 14.58           O  
ATOM    346  CB  ALA A  44      19.462  28.900  14.018  1.00 14.89           C  
ATOM    347  N   ILE A  45      19.760  25.985  13.020  1.00 13.91           N  
ATOM    348  CA  ILE A  45      20.406  24.985  12.150  1.00 13.71           C  
ATOM    349  C   ILE A  45      19.356  24.179  11.401  1.00 13.33           C  
ATOM    350  O   ILE A  45      19.447  23.957  10.183  1.00 13.99           O  
ATOM    351  CB  ILE A  45      21.269  24.034  12.989  1.00 13.91           C  
ATOM    352  CG1 ILE A  45      22.447  24.811  13.591  1.00 14.78           C  
ATOM    353  CG2 ILE A  45      21.706  22.819  12.163  1.00 13.80           C  
ATOM    354  CD1 ILE A  45      23.171  24.081  14.724  1.00 17.57           C  
ATOM    355  N   THR A  46      18.343  23.744  12.145  1.00 13.37           N  
ATOM    356  CA  THR A  46      17.343  22.801  11.645  1.00 13.22           C  
ATOM    357  C   THR A  46      16.325  23.447  10.693  1.00 13.55           C  
ATOM    358  O   THR A  46      15.713  22.763   9.858  1.00 15.09           O  
ATOM    359  CB  THR A  46      16.642  22.080  12.816  1.00 13.41           C  
ATOM    360  OG1 THR A  46      17.645  21.498  13.660  1.00 12.83           O  
ATOM    361  CG2 THR A  46      15.736  20.932  12.308  1.00 13.71           C  
ATOM    362  N   THR A  47      16.142  24.759  10.817  1.00 13.25           N  
ATOM    363  CA  THR A  47      15.255  25.476   9.899  1.00 12.78           C  
ATOM    364  C   THR A  47      15.985  25.736   8.574  1.00 12.49           C  
ATOM    365  O   THR A  47      15.377  25.700   7.496  1.00 12.91           O  
ATOM    366  CB  THR A  47      14.745  26.780  10.544  1.00 11.91           C  
ATOM    367  OG1 THR A  47      14.092  26.467  11.788  1.00 13.66           O  
ATOM    368  CG2 THR A  47      13.768  27.529   9.618  1.00 12.09           C  
ATOM    369  N   LEU A  48      17.290  26.001   8.672  1.00 12.00           N  
ATOM    370  CA ALEU A  48      18.093  26.254   7.486  0.80 12.28           C  
ATOM    371  CA BLEU A  48      18.145  26.233   7.495  0.20 12.24           C  
ATOM    372  C   LEU A  48      18.141  25.041   6.543  1.00 12.32           C  
ATOM    373  O   LEU A  48      18.187  25.197   5.312  1.00 12.37           O  
ATOM    374  CB ALEU A  48      19.497  26.686   7.909  0.80 12.91           C  
ATOM    375  CB BLEU A  48      19.598  26.512   7.913  0.20 12.45           C  
ATOM    376  CG ALEU A  48      20.440  27.096   6.783  0.80 13.08           C  
ATOM    377  CG BLEU A  48      20.291  27.886   7.827  0.20 12.65           C  
ATOM    378  CD1ALEU A  48      19.840  28.215   5.926  0.80 13.60           C  
ATOM    379  CD1BLEU A  48      19.619  28.873   6.868  0.20 12.15           C  
ATOM    380  CD2ALEU A  48      21.782  27.530   7.372  0.80 13.44           C  
ATOM    381  CD2BLEU A  48      20.511  28.509   9.197  0.20 13.49           C  
ATOM    382  N   VAL A  49      18.110  23.843   7.117  1.00 11.66           N  
ATOM    383  CA  VAL A  49      18.210  22.612   6.341  1.00 11.74           C  
ATOM    384  C   VAL A  49      17.106  22.480   5.269  1.00 11.89           C  
ATOM    385  O   VAL A  49      17.426  22.441   4.081  1.00 12.13           O  
ATOM    386  CB  VAL A  49      18.321  21.384   7.269  1.00 11.68           C  
ATOM    387  CG1 VAL A  49      18.096  20.109   6.493  1.00 12.12           C  
ATOM    388  CG2 VAL A  49      19.708  21.383   7.958  1.00 11.77           C  
ATOM    389  N   PRO A  50      15.815  22.430   5.668  1.00 11.73           N  
ATOM    390  CA  PRO A  50      14.766  22.370   4.644  1.00 11.45           C  
ATOM    391  C   PRO A  50      14.641  23.669   3.837  1.00 11.14           C  
ATOM    392  O   PRO A  50      14.154  23.649   2.709  1.00 11.59           O  
ATOM    393  CB  PRO A  50      13.496  22.063   5.453  1.00 11.53           C  
ATOM    394  CG  PRO A  50      13.765  22.607   6.796  1.00 11.62           C  
ATOM    395  CD  PRO A  50      15.246  22.359   7.028  1.00 11.93           C  
ATOM    396  N   ALA A  51      15.107  24.789   4.391  1.00 11.43           N  
ATOM    397  CA  ALA A  51      15.115  26.036   3.599  1.00 12.27           C  
ATOM    398  C   ALA A  51      16.012  25.923   2.356  1.00 12.01           C  
ATOM    399  O   ALA A  51      15.627  26.317   1.244  1.00 12.52           O  
ATOM    400  CB  ALA A  51      15.513  27.223   4.461  1.00 12.05           C  
ATOM    401  N   ILE A  52      17.205  25.361   2.539  1.00 12.06           N  
ATOM    402  CA  ILE A  52      18.140  25.150   1.430  1.00 11.87           C  
ATOM    403  C   ILE A  52      17.562  24.116   0.465  1.00 11.71           C  
ATOM    404  O   ILE A  52      17.582  24.315  -0.742  1.00 12.24           O  
ATOM    405  CB  ILE A  52      19.531  24.709   1.957  1.00 12.25           C  
ATOM    406  CG1 ILE A  52      20.184  25.849   2.771  1.00 12.39           C  
ATOM    407  CG2 ILE A  52      20.428  24.230   0.806  1.00 12.66           C  
ATOM    408  CD1 ILE A  52      21.395  25.391   3.630  1.00 13.19           C  
ATOM    409  N   ALA A  53      17.021  23.023   1.006  1.00 11.45           N  
ATOM    410  CA  ALA A  53      16.408  22.001   0.148  1.00 11.69           C  
ATOM    411  C   ALA A  53      15.239  22.561  -0.662  1.00 12.03           C  
ATOM    412  O   ALA A  53      15.087  22.236  -1.848  1.00 12.49           O  
ATOM    413  CB  ALA A  53      15.958  20.792   0.974  1.00 12.79           C  
ATOM    414  N   PHE A  54      14.423  23.410  -0.039  1.00 12.85           N  
ATOM    415  CA  PHE A  54      13.331  24.073  -0.760  1.00 13.18           C  
ATOM    416  C   PHE A  54      13.869  24.851  -1.966  1.00 13.32           C  
ATOM    417  O   PHE A  54      13.345  24.740  -3.080  1.00 12.69           O  
ATOM    418  CB  PHE A  54      12.565  24.995   0.187  1.00 13.78           C  
ATOM    419  CG  PHE A  54      11.615  25.982  -0.525  1.00 14.37           C  
ATOM    420  CD1 PHE A  54      10.329  25.575  -0.893  1.00 13.34           C  
ATOM    421  CD2 PHE A  54      12.005  27.294  -0.774  1.00 16.44           C  
ATOM    422  CE1 PHE A  54       9.428  26.460  -1.485  1.00 14.26           C  
ATOM    423  CE2 PHE A  54      11.113  28.192  -1.399  1.00 15.11           C  
ATOM    424  CZ  PHE A  54       9.831  27.763  -1.757  1.00 14.49           C  
ATOM    425  N   THR A  55      14.926  25.622  -1.750  1.00 12.93           N  
ATOM    426  CA ATHR A  55      15.460  26.445  -2.840  0.60 13.29           C  
ATOM    427  CA BTHR A  55      15.503  26.446  -2.811  0.40 12.93           C  
ATOM    428  C   THR A  55      15.970  25.584  -3.988  1.00 13.11           C  
ATOM    429  O   THR A  55      15.792  25.941  -5.159  1.00 12.75           O  
ATOM    430  CB ATHR A  55      16.562  27.428  -2.388  0.60 13.33           C  
ATOM    431  CB BTHR A  55      16.665  27.298  -2.261  0.40 12.87           C  
ATOM    432  OG1ATHR A  55      17.736  26.707  -1.994  0.60 14.54           O  
ATOM    433  OG1BTHR A  55      16.181  28.136  -1.202  0.40 13.09           O  
ATOM    434  CG2ATHR A  55      16.077  28.317  -1.244  0.60 13.60           C  
ATOM    435  CG2BTHR A  55      17.267  28.170  -3.351  0.40 12.24           C  
ATOM    436  N   MET A  56      16.565  24.436  -3.675  1.00 12.75           N  
ATOM    437  CA AMET A  56      17.098  23.582  -4.731  0.60 13.18           C  
ATOM    438  CA BMET A  56      17.102  23.571  -4.726  0.40 12.99           C  
ATOM    439  C   MET A  56      16.010  22.762  -5.423  1.00 12.99           C  
ATOM    440  O   MET A  56      16.050  22.580  -6.654  1.00 13.04           O  
ATOM    441  CB AMET A  56      18.239  22.712  -4.205  0.60 13.37           C  
ATOM    442  CB BMET A  56      18.215  22.675  -4.183  0.40 13.10           C  
ATOM    443  CG AMET A  56      19.439  23.528  -3.679  0.60 14.50           C  
ATOM    444  CG BMET A  56      19.436  23.458  -3.701  0.40 13.19           C  
ATOM    445  SD AMET A  56      20.033  24.875  -4.748  0.60 19.20           S  
ATOM    446  SD BMET A  56      20.326  24.341  -5.007  0.40 14.04           S  
ATOM    447  CE AMET A  56      20.340  24.032  -6.289  0.60 17.69           C  
ATOM    448  CE BMET A  56      21.315  25.450  -4.002  0.40 14.71           C  
ATOM    449  N   TYR A  57      15.034  22.272  -4.648  1.00 12.97           N  
ATOM    450  CA  TYR A  57      13.881  21.589  -5.242  1.00 13.14           C  
ATOM    451  C   TYR A  57      13.148  22.551  -6.185  1.00 13.23           C  
ATOM    452  O   TYR A  57      12.751  22.182  -7.293  1.00 13.82           O  
ATOM    453  CB  TYR A  57      12.937  21.029  -4.163  1.00 13.13           C  
ATOM    454  CG  TYR A  57      13.268  19.595  -3.847  1.00 12.74           C  
ATOM    455  CD1 TYR A  57      12.670  18.558  -4.567  1.00 11.40           C  
ATOM    456  CD2 TYR A  57      14.190  19.269  -2.849  1.00 12.91           C  
ATOM    457  CE1 TYR A  57      12.981  17.210  -4.292  1.00 12.29           C  
ATOM    458  CE2 TYR A  57      14.514  17.931  -2.572  1.00 12.19           C  
ATOM    459  CZ  TYR A  57      13.905  16.914  -3.301  1.00 13.79           C  
ATOM    460  OH  TYR A  57      14.216  15.594  -3.064  1.00 12.86           O  
ATOM    461  N   LEU A  58      12.986  23.788  -5.728  1.00 13.20           N  
ATOM    462  CA  LEU A  58      12.300  24.787  -6.529  1.00 13.91           C  
ATOM    463  C   LEU A  58      13.071  25.069  -7.813  1.00 13.69           C  
ATOM    464  O   LEU A  58      12.481  25.127  -8.892  1.00 13.61           O  
ATOM    465  CB  LEU A  58      12.071  26.058  -5.706  1.00 13.37           C  
ATOM    466  CG  LEU A  58      11.338  27.201  -6.407  1.00 15.68           C  
ATOM    467  CD1 LEU A  58      10.011  26.738  -6.993  1.00 16.41           C  
ATOM    468  CD2 LEU A  58      11.153  28.345  -5.393  1.00 15.71           C  
ATOM    469  N   SER A  59      14.388  25.219  -7.691  1.00 13.56           N  
ATOM    470  CA ASER A  59      15.260  25.448  -8.849  0.70 13.60           C  
ATOM    471  CA BSER A  59      15.240  25.456  -8.859  0.30 13.80           C  
ATOM    472  C   SER A  59      15.103  24.314  -9.866  1.00 13.45           C  
ATOM    473  O   SER A  59      14.920  24.553 -11.067  1.00 13.88           O  
ATOM    474  CB ASER A  59      16.720  25.572  -8.400  0.70 13.76           C  
ATOM    475  CB BSER A  59      16.702  25.638  -8.449  0.30 13.90           C  
ATOM    476  OG ASER A  59      16.930  26.787  -7.691  0.70 13.82           O  
ATOM    477  OG BSER A  59      17.249  24.428  -7.970  0.30 14.92           O  
ATOM    478  N   MET A  60      15.157  23.069  -9.380  1.00 14.04           N  
ATOM    479  CA  MET A  60      14.997  21.905 -10.267  1.00 14.22           C  
ATOM    480  C   MET A  60      13.606  21.847 -10.905  1.00 14.32           C  
ATOM    481  O   MET A  60      13.465  21.524 -12.090  1.00 15.18           O  
ATOM    482  CB  MET A  60      15.309  20.600  -9.533  1.00 14.64           C  
ATOM    483  CG  MET A  60      16.779  20.497  -9.154  1.00 13.25           C  
ATOM    484  SD  MET A  60      17.227  18.865  -8.512  1.00 15.74           S  
ATOM    485  CE  MET A  60      16.606  18.976  -6.827  1.00 16.49           C  
ATOM    486  N   LEU A  61      12.581  22.167 -10.119  1.00 14.64           N  
ATOM    487  CA  LEU A  61      11.214  22.204 -10.621  1.00 15.17           C  
ATOM    488  C   LEU A  61      11.123  23.154 -11.820  1.00 15.49           C  
ATOM    489  O   LEU A  61      10.465  22.835 -12.815  1.00 16.61           O  
ATOM    490  CB  LEU A  61      10.238  22.629  -9.501  1.00 14.90           C  
ATOM    491  CG  LEU A  61       8.752  22.778  -9.857  1.00 14.87           C  
ATOM    492  CD1 LEU A  61       8.156  21.486 -10.422  1.00 15.43           C  
ATOM    493  CD2 LEU A  61       7.953  23.259  -8.640  1.00 15.14           C  
ATOM    494  N   LEU A  62      11.802  24.297 -11.717  1.00 15.48           N  
ATOM    495  CA  LEU A  62      11.770  25.340 -12.753  1.00 16.37           C  
ATOM    496  C   LEU A  62      12.805  25.125 -13.858  1.00 16.93           C  
ATOM    497  O   LEU A  62      13.017  26.016 -14.691  1.00 17.26           O  
ATOM    498  CB  LEU A  62      11.928  26.721 -12.122  1.00 16.35           C  
ATOM    499  CG  LEU A  62      10.771  27.173 -11.229  1.00 17.50           C  
ATOM    500  CD1 LEU A  62      11.133  28.479 -10.540  1.00 18.23           C  
ATOM    501  CD2 LEU A  62       9.460  27.318 -12.008  1.00 20.12           C  
ATOM    502  N   GLY A  63      13.449  23.960 -13.854  1.00 16.82           N  
ATOM    503  CA  GLY A  63      14.282  23.539 -14.993  1.00 17.15           C  
ATOM    504  C   GLY A  63      15.770  23.833 -14.881  1.00 17.47           C  
ATOM    505  O   GLY A  63      16.515  23.688 -15.866  1.00 18.38           O  
ATOM    506  N   TYR A  64      16.216  24.241 -13.695  1.00 17.41           N  
ATOM    507  CA  TYR A  64      17.632  24.493 -13.453  1.00 18.00           C  
ATOM    508  C   TYR A  64      18.279  23.304 -12.755  1.00 18.09           C  
ATOM    509  O   TYR A  64      17.579  22.410 -12.283  1.00 17.63           O  
ATOM    510  CB  TYR A  64      17.831  25.762 -12.621  1.00 18.31           C  
ATOM    511  CG  TYR A  64      17.504  26.995 -13.399  1.00 19.09           C  
ATOM    512  CD1 TYR A  64      16.195  27.448 -13.486  1.00 19.03           C  
ATOM    513  CD2 TYR A  64      18.498  27.687 -14.084  1.00 19.76           C  
ATOM    514  CE1 TYR A  64      15.875  28.573 -14.221  1.00 20.01           C  
ATOM    515  CE2 TYR A  64      18.196  28.821 -14.829  1.00 21.11           C  
ATOM    516  CZ  TYR A  64      16.878  29.258 -14.888  1.00 21.79           C  
ATOM    517  OH  TYR A  64      16.554  30.373 -15.619  1.00 21.26           O  
ATOM    518  N   GLY A  65      19.611  23.305 -12.703  1.00 18.49           N  
ATOM    519  CA  GLY A  65      20.374  22.258 -12.016  1.00 18.88           C  
ATOM    520  C   GLY A  65      20.334  20.894 -12.686  1.00 19.21           C  
ATOM    521  O   GLY A  65      20.523  19.873 -12.027  1.00 18.40           O  
ATOM    522  N   LEU A  66      20.087  20.880 -13.994  1.00 19.48           N  
ATOM    523  CA  LEU A  66      20.055  19.656 -14.786  1.00 20.81           C  
ATOM    524  C   LEU A  66      21.007  19.812 -15.954  1.00 21.02           C  
ATOM    525  O   LEU A  66      20.969  20.809 -16.670  1.00 21.11           O  
ATOM    526  CB  LEU A  66      18.641  19.396 -15.309  1.00 20.73           C  
ATOM    527  CG  LEU A  66      18.389  18.208 -16.245  1.00 21.99           C  
ATOM    528  CD1 LEU A  66      18.690  16.870 -15.585  1.00 22.95           C  
ATOM    529  CD2 LEU A  66      16.949  18.234 -16.748  1.00 22.44           C  
ATOM    530  N   THR A  67      21.871  18.826 -16.139  1.00 21.47           N  
ATOM    531  CA  THR A  67      22.772  18.833 -17.284  1.00 21.58           C  
ATOM    532  C   THR A  67      22.795  17.457 -17.929  1.00 21.98           C  
ATOM    533  O   THR A  67      22.443  16.468 -17.292  1.00 22.06           O  
ATOM    534  CB  THR A  67      24.184  19.300 -16.882  1.00 22.07           C  
ATOM    535  OG1 THR A  67      24.946  19.582 -18.066  1.00 22.34           O  
ATOM    536  CG2 THR A  67      24.915  18.247 -16.020  1.00 22.27           C  
ATOM    537  N   MET A  68      23.197  17.400 -19.197  1.00 21.39           N  
ATOM    538  CA  MET A  68      23.331  16.134 -19.911  1.00 21.69           C  
ATOM    539  C   MET A  68      24.788  15.699 -19.832  1.00 20.91           C  
ATOM    540  O   MET A  68      25.702  16.506 -20.039  1.00 21.45           O  
ATOM    541  CB  MET A  68      22.880  16.268 -21.377  1.00 22.58           C  
ATOM    542  CG  MET A  68      21.408  16.693 -21.566  1.00 25.57           C  
ATOM    543  SD  MET A  68      20.143  15.644 -20.783  1.00 32.16           S  
ATOM    544  CE  MET A  68      20.256  14.148 -21.746  1.00 30.65           C  
ATOM    545  N   VAL A  69      25.007  14.434 -19.487  1.00 19.48           N  
ATOM    546  CA  VAL A  69      26.353  13.890 -19.429  1.00 18.02           C  
ATOM    547  C   VAL A  69      26.441  12.666 -20.339  1.00 17.85           C  
ATOM    548  O   VAL A  69      25.647  11.738 -20.202  1.00 17.73           O  
ATOM    549  CB  VAL A  69      26.730  13.481 -17.992  1.00 17.56           C  
ATOM    550  CG1 VAL A  69      28.144  12.936 -17.956  1.00 18.27           C  
ATOM    551  CG2 VAL A  69      26.569  14.659 -17.021  1.00 17.00           C  
ATOM    552  N   PRO A  70      27.406  12.659 -21.277  1.00 17.65           N  
ATOM    553  CA  PRO A  70      27.544  11.478 -22.123  1.00 17.66           C  
ATOM    554  C   PRO A  70      28.281  10.345 -21.415  1.00 17.75           C  
ATOM    555  O   PRO A  70      29.390  10.541 -20.924  1.00 18.00           O  
ATOM    556  CB  PRO A  70      28.373  12.001 -23.300  1.00 17.57           C  
ATOM    557  CG  PRO A  70      29.233  13.055 -22.692  1.00 17.81           C  
ATOM    558  CD  PRO A  70      28.386  13.711 -21.622  1.00 17.35           C  
ATOM    559  N   PHE A  71      27.657   9.170 -21.353  1.00 17.96           N  
ATOM    560  CA  PHE A  71      28.349   7.951 -20.922  1.00 18.07           C  
ATOM    561  C   PHE A  71      27.557   6.723 -21.349  1.00 18.91           C  
ATOM    562  O   PHE A  71      26.340   6.797 -21.535  1.00 18.96           O  
ATOM    563  CB  PHE A  71      28.645   7.944 -19.410  1.00 17.18           C  
ATOM    564  CG  PHE A  71      27.424   8.000 -18.519  1.00 16.75           C  
ATOM    565  CD1 PHE A  71      26.792   6.827 -18.112  1.00 15.55           C  
ATOM    566  CD2 PHE A  71      26.952   9.217 -18.029  1.00 16.34           C  
ATOM    567  CE1 PHE A  71      25.686   6.867 -17.258  1.00 16.26           C  
ATOM    568  CE2 PHE A  71      25.859   9.262 -17.171  1.00 14.73           C  
ATOM    569  CZ  PHE A  71      25.220   8.079 -16.790  1.00 15.31           C  
ATOM    570  N   GLY A  72      28.260   5.611 -21.531  1.00 20.36           N  
ATOM    571  CA  GLY A  72      27.633   4.383 -21.996  1.00 21.99           C  
ATOM    572  C   GLY A  72      26.996   4.551 -23.364  1.00 23.46           C  
ATOM    573  O   GLY A  72      26.025   3.868 -23.685  1.00 24.03           O  
ATOM    574  N   GLY A  73      27.540   5.470 -24.162  1.00 24.14           N  
ATOM    575  CA  GLY A  73      27.082   5.675 -25.537  1.00 25.61           C  
ATOM    576  C   GLY A  73      25.827   6.513 -25.704  1.00 26.68           C  
ATOM    577  O   GLY A  73      25.283   6.607 -26.809  1.00 26.94           O  
ATOM    578  N   GLU A  74      25.359   7.127 -24.616  1.00 26.95           N  
ATOM    579  CA  GLU A  74      24.155   7.950 -24.675  1.00 27.78           C  
ATOM    580  C   GLU A  74      24.267   9.210 -23.827  1.00 26.80           C  
ATOM    581  O   GLU A  74      25.184   9.339 -23.018  1.00 26.37           O  
ATOM    582  CB  GLU A  74      22.908   7.143 -24.298  1.00 27.83           C  
ATOM    583  CG  GLU A  74      22.837   6.663 -22.856  1.00 29.95           C  
ATOM    584  CD  GLU A  74      21.523   5.944 -22.525  1.00 30.87           C  
ATOM    585  OE1 GLU A  74      20.710   5.712 -23.448  1.00 35.16           O  
ATOM    586  OE2 GLU A  74      21.310   5.614 -21.333  1.00 34.72           O  
ATOM    587  N   GLN A  75      23.349  10.146 -24.063  1.00 26.58           N  
ATOM    588  CA  GLN A  75      23.271  11.397 -23.309  1.00 26.19           C  
ATOM    589  C   GLN A  75      22.335  11.194 -22.138  1.00 25.32           C  
ATOM    590  O   GLN A  75      21.158  10.868 -22.321  1.00 25.76           O  
ATOM    591  CB  GLN A  75      22.758  12.535 -24.193  1.00 26.82           C  
ATOM    592  CG  GLN A  75      23.705  12.936 -25.327  1.00 29.13           C  
ATOM    593  CD  GLN A  75      24.966  13.627 -24.839  1.00 32.35           C  
ATOM    594  OE1 GLN A  75      25.041  14.092 -23.699  1.00 35.70           O  
ATOM    595  NE2 GLN A  75      25.966  13.706 -25.711  1.00 34.72           N  
ATOM    596  N   ASN A  76      22.860  11.403 -20.935  1.00 23.59           N  
ATOM    597  CA  ASN A  76      22.142  11.070 -19.712  1.00 22.88           C  
ATOM    598  C   ASN A  76      21.807  12.322 -18.907  1.00 22.18           C  
ATOM    599  O   ASN A  76      22.693  13.128 -18.644  1.00 21.08           O  
ATOM    600  CB  ASN A  76      22.998  10.135 -18.873  1.00 22.79           C  
ATOM    601  CG  ASN A  76      23.422   8.886 -19.636  1.00 24.20           C  
ATOM    602  OD1 ASN A  76      24.539   8.796 -20.161  1.00 24.50           O  
ATOM    603  ND2 ASN A  76      22.531   7.911 -19.689  1.00 25.05           N  
ATOM    604  N   PRO A  77      20.529  12.484 -18.513  1.00 21.90           N  
ATOM    605  CA  PRO A  77      20.122  13.646 -17.715  1.00 21.35           C  
ATOM    606  C   PRO A  77      20.544  13.517 -16.248  1.00 20.30           C  
ATOM    607  O   PRO A  77      20.131  12.582 -15.563  1.00 21.44           O  
ATOM    608  CB  PRO A  77      18.591  13.642 -17.843  1.00 21.44           C  
ATOM    609  CG  PRO A  77      18.231  12.217 -18.070  1.00 22.12           C  
ATOM    610  CD  PRO A  77      19.393  11.591 -18.818  1.00 22.33           C  
ATOM    611  N   ILE A  78      21.360  14.457 -15.777  1.00 18.56           N  
ATOM    612  CA  ILE A  78      21.900  14.400 -14.419  1.00 16.98           C  
ATOM    613  C   ILE A  78      21.531  15.676 -13.675  1.00 16.74           C  
ATOM    614  O   ILE A  78      21.905  16.778 -14.085  1.00 15.81           O  
ATOM    615  CB  ILE A  78      23.444  14.251 -14.433  1.00 16.95           C  
ATOM    616  CG1 ILE A  78      23.855  12.967 -15.179  1.00 16.66           C  
ATOM    617  CG2 ILE A  78      24.029  14.323 -12.993  1.00 17.26           C  
ATOM    618  CD1 ILE A  78      23.484  11.666 -14.462  1.00 15.15           C  
ATOM    619  N   TYR A  79      20.790  15.514 -12.580  1.00 16.43           N  
ATOM    620  CA  TYR A  79      20.457  16.631 -11.690  1.00 16.64           C  
ATOM    621  C   TYR A  79      21.628  16.945 -10.769  1.00 16.71           C  
ATOM    622  O   TYR A  79      21.853  16.246  -9.775  1.00 17.72           O  
ATOM    623  CB  TYR A  79      19.207  16.317 -10.861  1.00 16.88           C  
ATOM    624  CG  TYR A  79      17.910  16.508 -11.627  1.00 16.17           C  
ATOM    625  CD1 TYR A  79      17.440  17.789 -11.921  1.00 16.20           C  
ATOM    626  CD2 TYR A  79      17.150  15.411 -12.052  1.00 17.59           C  
ATOM    627  CE1 TYR A  79      16.247  17.986 -12.621  1.00 16.35           C  
ATOM    628  CE2 TYR A  79      15.948  15.596 -12.748  1.00 19.24           C  
ATOM    629  CZ  TYR A  79      15.509  16.883 -13.034  1.00 17.54           C  
ATOM    630  OH  TYR A  79      14.335  17.089 -13.739  1.00 17.79           O  
ATOM    631  N   TRP A  80      22.380  17.984 -11.109  1.00 16.01           N  
ATOM    632  CA  TRP A  80      23.509  18.383 -10.269  1.00 15.88           C  
ATOM    633  C   TRP A  80      23.092  19.268  -9.090  1.00 15.44           C  
ATOM    634  O   TRP A  80      23.835  19.390  -8.117  1.00 14.57           O  
ATOM    635  CB  TRP A  80      24.643  19.015 -11.097  1.00 17.11           C  
ATOM    636  CG  TRP A  80      24.264  20.273 -11.820  1.00 17.37           C  
ATOM    637  CD1 TRP A  80      23.765  20.373 -13.092  1.00 19.18           C  
ATOM    638  CD2 TRP A  80      24.368  21.615 -11.322  1.00 18.76           C  
ATOM    639  NE1 TRP A  80      23.558  21.691 -13.412  1.00 20.05           N  
ATOM    640  CE2 TRP A  80      23.908  22.475 -12.345  1.00 19.69           C  
ATOM    641  CE3 TRP A  80      24.796  22.170 -10.112  1.00 19.97           C  
ATOM    642  CZ2 TRP A  80      23.876  23.866 -12.198  1.00 20.04           C  
ATOM    643  CZ3 TRP A  80      24.757  23.564  -9.966  1.00 20.85           C  
ATOM    644  CH2 TRP A  80      24.301  24.386 -11.009  1.00 20.17           C  
ATOM    645  N   ALA A  81      21.904  19.869  -9.153  1.00 15.34           N  
ATOM    646  CA  ALA A  81      21.445  20.756  -8.073  1.00 15.24           C  
ATOM    647  C   ALA A  81      21.337  20.036  -6.724  1.00 14.84           C  
ATOM    648  O   ALA A  81      21.448  20.661  -5.653  1.00 14.87           O  
ATOM    649  CB  ALA A  81      20.107  21.384  -8.427  1.00 16.42           C  
ATOM    650  N   ARG A  82      21.108  18.729  -6.774  1.00 14.23           N  
ATOM    651  CA  ARG A  82      21.003  17.906  -5.564  1.00 13.33           C  
ATOM    652  C   ARG A  82      22.266  18.083  -4.715  1.00 13.23           C  
ATOM    653  O   ARG A  82      22.202  18.136  -3.490  1.00 12.88           O  
ATOM    654  CB  ARG A  82      20.872  16.419  -5.916  1.00 13.81           C  
ATOM    655  CG  ARG A  82      19.665  16.055  -6.745  1.00 14.31           C  
ATOM    656  CD  ARG A  82      19.395  14.561  -6.591  1.00 14.34           C  
ATOM    657  NE  ARG A  82      18.410  14.102  -7.575  1.00 15.48           N  
ATOM    658  CZ  ARG A  82      17.095  14.162  -7.388  1.00 17.84           C  
ATOM    659  NH1 ARG A  82      16.601  14.673  -6.274  1.00 20.05           N  
ATOM    660  NH2 ARG A  82      16.277  13.700  -8.329  1.00 19.85           N  
ATOM    661  N   TYR A  83      23.418  18.153  -5.386  1.00 12.93           N  
ATOM    662  CA  TYR A  83      24.715  18.248  -4.693  1.00 13.28           C  
ATOM    663  C   TYR A  83      24.930  19.610  -4.068  1.00 13.00           C  
ATOM    664  O   TYR A  83      25.612  19.725  -3.046  1.00 13.49           O  
ATOM    665  CB  TYR A  83      25.881  17.851  -5.623  1.00 12.87           C  
ATOM    666  CG  TYR A  83      25.659  16.467  -6.197  1.00 12.64           C  
ATOM    667  CD1 TYR A  83      26.148  15.335  -5.558  1.00 13.72           C  
ATOM    668  CD2 TYR A  83      24.887  16.296  -7.345  1.00 13.10           C  
ATOM    669  CE1 TYR A  83      25.904  14.060  -6.092  1.00 12.84           C  
ATOM    670  CE2 TYR A  83      24.631  15.044  -7.871  1.00 13.23           C  
ATOM    671  CZ  TYR A  83      25.140  13.933  -7.241  1.00 13.20           C  
ATOM    672  OH  TYR A  83      24.879  12.684  -7.768  1.00 15.38           O  
ATOM    673  N   ALA A  84      24.331  20.642  -4.659  1.00 12.93           N  
ATOM    674  CA  ALA A  84      24.416  21.976  -4.092  1.00 13.02           C  
ATOM    675  C   ALA A  84      23.622  22.048  -2.788  1.00 13.52           C  
ATOM    676  O   ALA A  84      24.050  22.701  -1.833  1.00 14.85           O  
ATOM    677  CB  ALA A  84      23.942  23.024  -5.101  1.00 13.52           C  
ATOM    678  N   ASP A  85      22.496  21.339  -2.752  1.00 12.55           N  
ATOM    679  CA  ASP A  85      21.679  21.172  -1.541  1.00 12.38           C  
ATOM    680  C   ASP A  85      22.497  20.387  -0.522  1.00 11.39           C  
ATOM    681  O   ASP A  85      22.852  20.900   0.554  1.00 11.72           O  
ATOM    682  CB  ASP A  85      20.399  20.423  -1.961  1.00 12.89           C  
ATOM    683  CG  ASP A  85      19.532  19.946  -0.807  1.00 14.12           C  
ATOM    684  OD1 ASP A  85      19.996  19.835   0.350  1.00 14.92           O  
ATOM    685  OD2 ASP A  85      18.350  19.641  -1.104  1.00 13.69           O  
ATOM    686  N   TRP A  86      22.888  19.178  -0.895  1.00 11.32           N  
ATOM    687  CA  TRP A  86      23.523  18.270   0.060  1.00 11.20           C  
ATOM    688  C   TRP A  86      24.872  18.762   0.613  1.00 10.98           C  
ATOM    689  O   TRP A  86      25.231  18.453   1.765  1.00 11.39           O  
ATOM    690  CB  TRP A  86      23.699  16.902  -0.585  1.00 11.79           C  
ATOM    691  CG  TRP A  86      22.439  16.224  -1.005  1.00 12.18           C  
ATOM    692  CD1 TRP A  86      21.169  16.431  -0.528  1.00 11.99           C  
ATOM    693  CD2 TRP A  86      22.351  15.152  -1.943  1.00 12.70           C  
ATOM    694  NE1 TRP A  86      20.281  15.574  -1.165  1.00 12.69           N  
ATOM    695  CE2 TRP A  86      20.987  14.774  -2.029  1.00 12.40           C  
ATOM    696  CE3 TRP A  86      23.290  14.496  -2.753  1.00 12.12           C  
ATOM    697  CZ2 TRP A  86      20.540  13.751  -2.889  1.00 13.12           C  
ATOM    698  CZ3 TRP A  86      22.842  13.493  -3.612  1.00 13.75           C  
ATOM    699  CH2 TRP A  86      21.480  13.125  -3.660  1.00 12.49           C  
ATOM    700  N   LEU A  87      25.621  19.512  -0.193  1.00 10.96           N  
ATOM    701  CA ALEU A  87      26.890  20.056   0.280  0.80 10.56           C  
ATOM    702  CA BLEU A  87      26.887  20.104   0.254  0.20 11.07           C  
ATOM    703  C   LEU A  87      26.716  20.837   1.579  1.00 10.54           C  
ATOM    704  O   LEU A  87      27.594  20.775   2.455  1.00 11.68           O  
ATOM    705  CB ALEU A  87      27.535  20.960  -0.776  0.80 10.32           C  
ATOM    706  CB BLEU A  87      27.450  21.077  -0.794  0.20 11.14           C  
ATOM    707  CG ALEU A  87      28.891  21.583  -0.415  0.80  8.99           C  
ATOM    708  CG BLEU A  87      28.542  20.614  -1.768  0.20 12.30           C  
ATOM    709  CD1ALEU A  87      29.993  20.545  -0.265  0.80 11.82           C  
ATOM    710  CD1BLEU A  87      28.727  21.628  -2.884  0.20 13.39           C  
ATOM    711  CD2ALEU A  87      29.272  22.626  -1.480  0.80 10.92           C  
ATOM    712  CD2BLEU A  87      29.872  20.352  -1.054  0.20 12.67           C  
ATOM    713  N   PHE A  88      25.587  21.538   1.719  1.00 10.43           N  
ATOM    714  CA  PHE A  88      25.347  22.327   2.934  1.00 11.14           C  
ATOM    715  C   PHE A  88      24.432  21.633   3.954  1.00 11.73           C  
ATOM    716  O   PHE A  88      24.647  21.747   5.175  1.00 12.82           O  
ATOM    717  CB  PHE A  88      24.808  23.702   2.557  1.00 12.14           C  
ATOM    718  CG  PHE A  88      25.723  24.464   1.638  1.00 12.50           C  
ATOM    719  CD1 PHE A  88      26.870  25.079   2.128  1.00 15.07           C  
ATOM    720  CD2 PHE A  88      25.446  24.541   0.275  1.00 14.74           C  
ATOM    721  CE1 PHE A  88      27.725  25.768   1.262  1.00 14.66           C  
ATOM    722  CE2 PHE A  88      26.304  25.242  -0.623  1.00 18.00           C  
ATOM    723  CZ  PHE A  88      27.438  25.882  -0.108  1.00 19.55           C  
ATOM    724  N   THR A  89      23.416  20.923   3.475  1.00 11.00           N  
ATOM    725  CA  THR A  89      22.433  20.342   4.400  1.00 11.09           C  
ATOM    726  C   THR A  89      22.962  19.136   5.168  1.00 11.30           C  
ATOM    727  O   THR A  89      22.642  18.955   6.338  1.00 11.73           O  
ATOM    728  CB  THR A  89      21.121  19.976   3.694  1.00 10.72           C  
ATOM    729  OG1 THR A  89      21.390  19.094   2.605  1.00 11.47           O  
ATOM    730  CG2 THR A  89      20.432  21.247   3.144  1.00 12.06           C  
ATOM    731  N   THR A  90      23.777  18.309   4.520  1.00 11.64           N  
ATOM    732  CA  THR A  90      24.290  17.145   5.235  1.00 11.88           C  
ATOM    733  C   THR A  90      25.219  17.501   6.416  1.00 12.01           C  
ATOM    734  O   THR A  90      25.049  16.941   7.507  1.00 12.21           O  
ATOM    735  CB  THR A  90      24.858  16.040   4.291  1.00 11.92           C  
ATOM    736  OG1 THR A  90      25.887  16.558   3.422  1.00 11.30           O  
ATOM    737  CG2 THR A  90      23.731  15.471   3.455  1.00 11.56           C  
ATOM    738  N   PRO A  91      26.184  18.433   6.230  1.00 11.73           N  
ATOM    739  CA  PRO A  91      26.954  18.823   7.435  1.00 11.88           C  
ATOM    740  C   PRO A  91      26.117  19.548   8.503  1.00 11.18           C  
ATOM    741  O   PRO A  91      26.447  19.445   9.689  1.00 10.93           O  
ATOM    742  CB  PRO A  91      28.060  19.747   6.913  1.00 13.12           C  
ATOM    743  CG  PRO A  91      27.814  19.954   5.493  1.00 13.22           C  
ATOM    744  CD  PRO A  91      26.676  19.100   5.006  1.00 12.35           C  
ATOM    745  N   LEU A  92      25.087  20.300   8.099  1.00 10.88           N  
ATOM    746  CA  LEU A  92      24.194  20.926   9.079  1.00 11.66           C  
ATOM    747  C   LEU A  92      23.494  19.869   9.938  1.00 11.74           C  
ATOM    748  O   LEU A  92      23.397  20.011  11.160  1.00 11.51           O  
ATOM    749  CB  LEU A  92      23.184  21.862   8.405  1.00 12.02           C  
ATOM    750  CG  LEU A  92      23.784  23.182   7.906  1.00 13.29           C  
ATOM    751  CD1 LEU A  92      22.780  23.866   6.989  1.00 13.41           C  
ATOM    752  CD2 LEU A  92      24.153  24.120   9.072  1.00 14.56           C  
ATOM    753  N   LEU A  93      23.046  18.783   9.300  1.00 11.06           N  
ATOM    754  CA  LEU A  93      22.439  17.674  10.045  1.00 11.11           C  
ATOM    755  C   LEU A  93      23.446  17.063  11.023  1.00 11.22           C  
ATOM    756  O   LEU A  93      23.116  16.775  12.172  1.00 11.19           O  
ATOM    757  CB  LEU A  93      21.906  16.613   9.089  1.00 10.76           C  
ATOM    758  CG  LEU A  93      20.638  17.082   8.358  1.00 10.54           C  
ATOM    759  CD1 LEU A  93      20.255  16.154   7.203  1.00 12.98           C  
ATOM    760  CD2 LEU A  93      19.449  17.256   9.322  1.00 12.82           C  
ATOM    761  N   LEU A  94      24.678  16.871  10.556  1.00 11.92           N  
ATOM    762  CA  LEU A  94      25.746  16.352  11.431  1.00 12.25           C  
ATOM    763  C   LEU A  94      26.021  17.274  12.609  1.00 12.60           C  
ATOM    764  O   LEU A  94      26.223  16.807  13.727  1.00 12.84           O  
ATOM    765  CB  LEU A  94      27.036  16.103  10.647  1.00 12.79           C  
ATOM    766  CG  LEU A  94      26.942  15.033   9.556  1.00 13.09           C  
ATOM    767  CD1 LEU A  94      28.281  14.918   8.847  1.00 14.29           C  
ATOM    768  CD2 LEU A  94      26.518  13.660  10.117  1.00 14.77           C  
ATOM    769  N   LEU A  95      26.019  18.578  12.349  1.00 12.29           N  
ATOM    770  CA ALEU A  95      26.209  19.570  13.405  0.60 12.55           C  
ATOM    771  CA BLEU A  95      26.210  19.571  13.402  0.40 12.93           C  
ATOM    772  C   LEU A  95      25.108  19.465  14.462  1.00 12.89           C  
ATOM    773  O   LEU A  95      25.385  19.552  15.665  1.00 12.97           O  
ATOM    774  CB ALEU A  95      26.253  20.983  12.820  0.60 12.32           C  
ATOM    775  CB BLEU A  95      26.281  20.980  12.799  0.40 13.08           C  
ATOM    776  CG ALEU A  95      26.551  22.085  13.846  0.60 11.85           C  
ATOM    777  CG BLEU A  95      27.648  21.403  12.238  0.40 14.71           C  
ATOM    778  CD1ALEU A  95      27.867  21.820  14.605  0.60 12.38           C  
ATOM    779  CD1BLEU A  95      27.493  22.472  11.168  0.40 15.91           C  
ATOM    780  CD2ALEU A  95      26.574  23.447  13.171  0.60 13.04           C  
ATOM    781  CD2BLEU A  95      28.583  21.881  13.349  0.40 16.07           C  
ATOM    782  N   ASP A  96      23.855  19.274  14.023  1.00 12.64           N  
ATOM    783  CA  ASP A  96      22.730  19.047  14.973  1.00 12.63           C  
ATOM    784  C   ASP A  96      23.070  17.869  15.890  1.00 12.80           C  
ATOM    785  O   ASP A  96      22.928  17.951  17.117  1.00 12.94           O  
ATOM    786  CB  ASP A  96      21.425  18.722  14.225  1.00 13.03           C  
ATOM    787  CG  ASP A  96      20.477  19.927  14.077  1.00 13.42           C  
ATOM    788  OD1 ASP A  96      20.643  20.964  14.770  1.00 12.79           O  
ATOM    789  OD2 ASP A  96      19.525  19.800  13.265  1.00 12.38           O  
ATOM    790  N   LEU A  97      23.526  16.769  15.292  1.00 12.31           N  
ATOM    791  CA  LEU A  97      23.866  15.586  16.084  1.00 12.37           C  
ATOM    792  C   LEU A  97      25.036  15.864  17.014  1.00 12.86           C  
ATOM    793  O   LEU A  97      25.031  15.452  18.181  1.00 13.31           O  
ATOM    794  CB  LEU A  97      24.186  14.401  15.159  1.00 11.94           C  
ATOM    795  CG  LEU A  97      22.998  13.881  14.337  1.00 13.10           C  
ATOM    796  CD1 LEU A  97      23.452  12.810  13.350  1.00 14.33           C  
ATOM    797  CD2 LEU A  97      21.884  13.348  15.240  1.00 14.47           C  
ATOM    798  N   ALA A  98      26.028  16.592  16.501  1.00 12.81           N  
ATOM    799  CA  ALA A  98      27.242  16.887  17.264  1.00 13.32           C  
ATOM    800  C   ALA A  98      26.923  17.744  18.478  1.00 13.79           C  
ATOM    801  O   ALA A  98      27.476  17.538  19.572  1.00 14.35           O  
ATOM    802  CB  ALA A  98      28.251  17.592  16.375  1.00 13.41           C  
ATOM    803  N   LEU A  99      26.027  18.702  18.298  1.00 13.65           N  
ATOM    804  CA  LEU A  99      25.682  19.592  19.402  1.00 14.96           C  
ATOM    805  C   LEU A  99      24.899  18.855  20.469  1.00 15.18           C  
ATOM    806  O   LEU A  99      25.038  19.149  21.658  1.00 15.37           O  
ATOM    807  CB  LEU A  99      24.870  20.781  18.894  1.00 15.51           C  
ATOM    808  CG  LEU A  99      25.676  21.775  18.069  1.00 16.82           C  
ATOM    809  CD1 LEU A  99      24.741  22.835  17.521  1.00 19.34           C  
ATOM    810  CD2 LEU A  99      26.812  22.418  18.888  1.00 19.83           C  
ATOM    811  N   LEU A 100      24.080  17.898  20.048  1.00 15.13           N  
ATOM    812  CA ALEU A 100      23.272  17.137  20.983  0.60 15.99           C  
ATOM    813  CA BLEU A 100      23.281  17.114  20.991  0.40 15.50           C  
ATOM    814  C   LEU A 100      24.159  16.364  21.963  1.00 16.00           C  
ATOM    815  O   LEU A 100      23.837  16.272  23.145  1.00 17.16           O  
ATOM    816  CB ALEU A 100      22.355  16.187  20.207  0.60 16.73           C  
ATOM    817  CB BLEU A 100      22.405  16.091  20.273  0.40 15.75           C  
ATOM    818  CG ALEU A 100      21.002  15.787  20.787  0.60 16.69           C  
ATOM    819  CG BLEU A 100      21.019  16.518  19.816  0.40 13.66           C  
ATOM    820  CD1ALEU A 100      20.182  16.974  21.308  0.60 15.71           C  
ATOM    821  CD1BLEU A 100      20.439  15.376  19.009  0.40 12.38           C  
ATOM    822  CD2ALEU A 100      20.232  15.044  19.723  0.60 14.87           C  
ATOM    823  CD2BLEU A 100      20.092  16.891  20.975  0.40 13.60           C  
ATOM    824  N   VAL A 101      25.274  15.826  21.463  1.00 15.76           N  
ATOM    825  CA  VAL A 101      26.139  14.944  22.264  1.00 16.03           C  
ATOM    826  C   VAL A 101      27.403  15.614  22.797  1.00 16.41           C  
ATOM    827  O   VAL A 101      28.251  14.959  23.400  1.00 17.01           O  
ATOM    828  CB  VAL A 101      26.522  13.656  21.481  1.00 16.15           C  
ATOM    829  CG1 VAL A 101      25.267  12.953  21.019  1.00 16.74           C  
ATOM    830  CG2 VAL A 101      27.453  13.965  20.295  1.00 15.41           C  
ATOM    831  N   ASP A 102      27.514  16.921  22.558  1.00 17.03           N  
ATOM    832  CA AASP A 102      28.720  17.666  22.949  0.60 17.64           C  
ATOM    833  CA BASP A 102      28.709  17.702  22.886  0.40 17.32           C  
ATOM    834  C   ASP A 102      29.973  17.043  22.328  1.00 17.65           C  
ATOM    835  O   ASP A 102      30.969  16.833  23.024  1.00 17.98           O  
ATOM    836  CB AASP A 102      28.879  17.690  24.482  0.60 18.18           C  
ATOM    837  CB BASP A 102      28.816  17.957  24.393  0.40 17.57           C  
ATOM    838  CG AASP A 102      27.952  18.682  25.166  0.60 20.31           C  
ATOM    839  CG BASP A 102      29.942  18.908  24.739  0.40 17.98           C  
ATOM    840  OD1AASP A 102      27.219  19.419  24.478  0.60 22.04           O  
ATOM    841  OD1BASP A 102      30.258  19.790  23.914  0.40 18.17           O  
ATOM    842  OD2AASP A 102      27.962  18.729  26.417  0.60 23.27           O  
ATOM    843  OD2BASP A 102      30.517  18.756  25.833  0.40 19.08           O  
ATOM    844  N   ALA A 103      29.922  16.723  21.035  1.00 17.26           N  
ATOM    845  CA  ALA A 103      31.061  16.116  20.344  1.00 17.78           C  
ATOM    846  C   ALA A 103      32.257  17.063  20.333  1.00 18.26           C  
ATOM    847  O   ALA A 103      32.082  18.287  20.359  1.00 18.32           O  
ATOM    848  CB  ALA A 103      30.674  15.722  18.923  1.00 17.56           C  
ATOM    849  N   ASP A 104      33.461  16.487  20.297  1.00 18.81           N  
ATOM    850  CA  ASP A 104      34.700  17.268  20.266  1.00 19.54           C  
ATOM    851  C   ASP A 104      34.804  18.075  18.977  1.00 18.92           C  
ATOM    852  O   ASP A 104      34.364  17.622  17.916  1.00 18.48           O  
ATOM    853  CB  ASP A 104      35.931  16.356  20.373  1.00 20.01           C  
ATOM    854  CG  ASP A 104      36.025  15.634  21.715  1.00 23.26           C  
ATOM    855  OD1 ASP A 104      35.325  16.004  22.683  1.00 24.41           O  
ATOM    856  OD2 ASP A 104      36.823  14.677  21.793  1.00 25.83           O  
ATOM    857  N   GLN A 105      35.406  19.256  19.079  1.00 18.72           N  
ATOM    858  CA  GLN A 105      35.642  20.100  17.907  1.00 18.49           C  
ATOM    859  C   GLN A 105      36.331  19.342  16.759  1.00 17.16           C  
ATOM    860  O   GLN A 105      35.916  19.440  15.601  1.00 16.14           O  
ATOM    861  CB  GLN A 105      36.463  21.329  18.310  1.00 18.91           C  
ATOM    862  CG  GLN A 105      36.477  22.427  17.248  1.00 20.57           C  
ATOM    863  CD  GLN A 105      37.329  23.630  17.648  1.00 21.75           C  
ATOM    864  OE1 GLN A 105      37.260  24.693  17.017  1.00 25.67           O  
ATOM    865  NE2 GLN A 105      38.146  23.463  18.690  1.00 24.14           N  
ATOM    866  N   GLY A 106      37.380  18.588  17.078  1.00 16.10           N  
ATOM    867  CA  GLY A 106      38.106  17.807  16.074  1.00 16.01           C  
ATOM    868  C   GLY A 106      37.258  16.740  15.398  1.00 15.93           C  
ATOM    869  O   GLY A 106      37.386  16.492  14.194  1.00 15.46           O  
ATOM    870  N   THR A 107      36.372  16.114  16.173  1.00 15.81           N  
ATOM    871  CA ATHR A 107      35.462  15.100  15.641  0.80 16.22           C  
ATOM    872  CA BTHR A 107      35.489  15.096  15.609  0.20 15.89           C  
ATOM    873  C   THR A 107      34.508  15.736  14.633  1.00 15.77           C  
ATOM    874  O   THR A 107      34.202  15.155  13.582  1.00 16.53           O  
ATOM    875  CB ATHR A 107      34.635  14.451  16.765  0.80 16.29           C  
ATOM    876  CB BTHR A 107      34.732  14.291  16.686  0.20 15.87           C  
ATOM    877  OG1ATHR A 107      35.508  13.940  17.783  0.80 16.14           O  
ATOM    878  OG1BTHR A 107      33.992  15.180  17.531  0.20 15.72           O  
ATOM    879  CG2ATHR A 107      33.782  13.321  16.214  0.80 16.57           C  
ATOM    880  CG2BTHR A 107      35.708  13.467  17.523  0.20 15.78           C  
ATOM    881  N   ILE A 108      34.030  16.932  14.970  1.00 15.46           N  
ATOM    882  CA  ILE A 108      33.146  17.684  14.078  1.00 15.72           C  
ATOM    883  C   ILE A 108      33.887  18.051  12.796  1.00 15.43           C  
ATOM    884  O   ILE A 108      33.361  17.860  11.704  1.00 15.20           O  
ATOM    885  CB  ILE A 108      32.585  18.961  14.744  1.00 15.66           C  
ATOM    886  CG1 ILE A 108      31.737  18.584  15.966  1.00 16.78           C  
ATOM    887  CG2 ILE A 108      31.768  19.803  13.724  1.00 16.91           C  
ATOM    888  CD1 ILE A 108      31.304  19.765  16.813  1.00 15.93           C  
ATOM    889  N   LEU A 109      35.098  18.596  12.923  1.00 14.88           N  
ATOM    890  CA  LEU A 109      35.877  18.957  11.726  1.00 15.60           C  
ATOM    891  C   LEU A 109      36.082  17.747  10.801  1.00 15.41           C  
ATOM    892  O   LEU A 109      35.940  17.849   9.572  1.00 15.67           O  
ATOM    893  CB  LEU A 109      37.235  19.557  12.118  1.00 15.65           C  
ATOM    894  CG  LEU A 109      38.078  20.042  10.931  1.00 17.36           C  
ATOM    895  CD1 LEU A 109      37.405  21.210  10.226  1.00 19.40           C  
ATOM    896  CD2 LEU A 109      39.482  20.441  11.392  1.00 17.60           C  
ATOM    897  N   ALA A 110      36.415  16.605  11.394  1.00 14.45           N  
ATOM    898  CA  ALA A 110      36.673  15.388  10.621  1.00 15.11           C  
ATOM    899  C   ALA A 110      35.412  14.874   9.916  1.00 14.43           C  
ATOM    900  O   ALA A 110      35.463  14.500   8.740  1.00 14.76           O  
ATOM    901  CB  ALA A 110      37.245  14.292  11.525  1.00 15.34           C  
ATOM    902  N   ALA A 111      34.289  14.859  10.633  1.00 14.02           N  
ATOM    903  CA  ALA A 111      33.011  14.431  10.057  1.00 14.15           C  
ATOM    904  C   ALA A 111      32.548  15.358   8.931  1.00 13.94           C  
ATOM    905  O   ALA A 111      32.136  14.887   7.878  1.00 14.23           O  
ATOM    906  CB  ALA A 111      31.931  14.343  11.126  1.00 13.92           C  
ATOM    907  N   VAL A 112      32.602  16.663   9.174  1.00 14.10           N  
ATOM    908  CA  VAL A 112      32.222  17.655   8.160  1.00 14.05           C  
ATOM    909  C   VAL A 112      33.181  17.587   6.950  1.00 14.45           C  
ATOM    910  O   VAL A 112      32.743  17.689   5.799  1.00 14.42           O  
ATOM    911  CB  VAL A 112      32.112  19.076   8.785  1.00 14.38           C  
ATOM    912  CG1 VAL A 112      31.953  20.151   7.711  1.00 14.91           C  
ATOM    913  CG2 VAL A 112      30.945  19.108   9.797  1.00 13.95           C  
ATOM    914  N   GLY A 113      34.478  17.389   7.207  1.00 14.16           N  
ATOM    915  CA  GLY A 113      35.458  17.176   6.130  1.00 14.01           C  
ATOM    916  C   GLY A 113      35.116  15.953   5.283  1.00 14.23           C  
ATOM    917  O   GLY A 113      35.113  16.016   4.044  1.00 15.06           O  
ATOM    918  N   ALA A 114      34.827  14.834   5.950  1.00 13.76           N  
ATOM    919  CA  ALA A 114      34.414  13.611   5.250  1.00 12.82           C  
ATOM    920  C   ALA A 114      33.139  13.843   4.431  1.00 13.23           C  
ATOM    921  O   ALA A 114      32.990  13.305   3.332  1.00 12.72           O  
ATOM    922  CB  ALA A 114      34.186  12.464   6.249  1.00 14.03           C  
ATOM    923  N   ASP A 115      32.224  14.627   4.991  1.00 12.75           N  
ATOM    924  CA  ASP A 115      30.956  14.949   4.326  1.00 12.67           C  
ATOM    925  C   ASP A 115      31.218  15.726   3.017  1.00 12.34           C  
ATOM    926  O   ASP A 115      30.612  15.435   1.976  1.00 12.04           O  
ATOM    927  CB  ASP A 115      30.058  15.724   5.293  1.00 13.27           C  
ATOM    928  CG  ASP A 115      28.610  15.737   4.857  1.00 15.45           C  
ATOM    929  OD1 ASP A 115      28.346  16.089   3.697  1.00 16.62           O  
ATOM    930  OD2 ASP A 115      27.734  15.423   5.672  1.00 19.50           O  
ATOM    931  N   GLY A 116      32.111  16.719   3.075  1.00 12.37           N  
ATOM    932  CA  GLY A 116      32.509  17.464   1.863  1.00 12.79           C  
ATOM    933  C   GLY A 116      33.117  16.550   0.809  1.00 12.85           C  
ATOM    934  O   GLY A 116      32.801  16.660  -0.382  1.00 13.89           O  
ATOM    935  N   ILE A 117      33.983  15.636   1.240  1.00 12.90           N  
ATOM    936  CA  ILE A 117      34.545  14.644   0.329  1.00 13.70           C  
ATOM    937  C   ILE A 117      33.432  13.793  -0.288  1.00 12.94           C  
ATOM    938  O   ILE A 117      33.450  13.538  -1.493  1.00 13.54           O  
ATOM    939  CB  ILE A 117      35.591  13.731   1.035  1.00 14.30           C  
ATOM    940  CG1 ILE A 117      36.849  14.544   1.381  1.00 14.59           C  
ATOM    941  CG2 ILE A 117      35.948  12.541   0.152  1.00 14.46           C  
ATOM    942  CD1 ILE A 117      37.767  13.853   2.396  1.00 16.58           C  
ATOM    943  N   MET A 118      32.486  13.347   0.545  1.00 12.18           N  
ATOM    944  CA  MET A 118      31.369  12.507   0.099  1.00 11.63           C  
ATOM    945  C   MET A 118      30.578  13.209  -0.985  1.00 11.48           C  
ATOM    946  O   MET A 118      30.321  12.647  -2.051  1.00 11.78           O  
ATOM    947  CB  MET A 118      30.472  12.149   1.297  1.00 11.19           C  
ATOM    948  CG  MET A 118      29.237  11.335   0.930  1.00 11.82           C  
ATOM    949  SD  MET A 118      28.196  11.073   2.391  1.00 11.99           S  
ATOM    950  CE  MET A 118      27.375  12.674   2.474  1.00 13.60           C  
ATOM    951  N   ILE A 119      30.211  14.459  -0.732  1.00 10.95           N  
ATOM    952  CA  ILE A 119      29.405  15.180  -1.701  1.00 12.31           C  
ATOM    953  C   ILE A 119      30.215  15.556  -2.950  1.00 12.34           C  
ATOM    954  O   ILE A 119      29.734  15.395  -4.070  1.00 13.25           O  
ATOM    955  CB  ILE A 119      28.716  16.420  -1.056  1.00 12.34           C  
ATOM    956  CG1 ILE A 119      27.757  15.985   0.068  1.00 13.49           C  
ATOM    957  CG2 ILE A 119      27.972  17.184  -2.097  1.00 13.11           C  
ATOM    958  CD1 ILE A 119      26.744  14.859  -0.321  1.00 11.99           C  
ATOM    959  N   GLY A 120      31.439  16.056  -2.760  1.00 12.07           N  
ATOM    960  CA  GLY A 120      32.288  16.465  -3.891  1.00 12.52           C  
ATOM    961  C   GLY A 120      32.590  15.309  -4.827  1.00 12.17           C  
ATOM    962  O   GLY A 120      32.425  15.424  -6.053  1.00 12.16           O  
ATOM    963  N   THR A 121      33.011  14.175  -4.266  1.00 12.66           N  
ATOM    964  CA  THR A 121      33.308  12.999  -5.107  1.00 12.08           C  
ATOM    965  C   THR A 121      32.041  12.412  -5.750  1.00 12.16           C  
ATOM    966  O   THR A 121      32.092  11.930  -6.885  1.00 12.37           O  
ATOM    967  CB  THR A 121      34.109  11.894  -4.357  1.00 12.76           C  
ATOM    968  OG1 THR A 121      33.399  11.487  -3.170  1.00 12.62           O  
ATOM    969  CG2 THR A 121      35.503  12.412  -3.961  1.00 12.96           C  
ATOM    970  N   GLY A 122      30.911  12.450  -5.036  1.00 11.63           N  
ATOM    971  CA  GLY A 122      29.619  12.038  -5.617  1.00 11.78           C  
ATOM    972  C   GLY A 122      29.306  12.884  -6.850  1.00 11.54           C  
ATOM    973  O   GLY A 122      28.897  12.350  -7.888  1.00 12.55           O  
ATOM    974  N   LEU A 123      29.544  14.194  -6.757  1.00 11.56           N  
ATOM    975  CA  LEU A 123      29.276  15.093  -7.888  1.00 11.19           C  
ATOM    976  C   LEU A 123      30.240  14.816  -9.049  1.00 11.74           C  
ATOM    977  O   LEU A 123      29.830  14.740 -10.223  1.00 12.69           O  
ATOM    978  CB  LEU A 123      29.363  16.566  -7.453  1.00 10.81           C  
ATOM    979  CG  LEU A 123      29.128  17.571  -8.590  1.00 11.00           C  
ATOM    980  CD1 LEU A 123      27.771  17.340  -9.289  1.00 13.04           C  
ATOM    981  CD2 LEU A 123      29.202  18.978  -8.017  1.00 12.13           C  
ATOM    982  N   VAL A 124      31.524  14.658  -8.726  1.00 12.25           N  
ATOM    983  CA  VAL A 124      32.507  14.308  -9.759  1.00 11.96           C  
ATOM    984  C   VAL A 124      32.079  13.016 -10.469  1.00 12.11           C  
ATOM    985  O   VAL A 124      32.048  12.966 -11.709  1.00 12.68           O  
ATOM    986  CB  VAL A 124      33.935  14.195  -9.194  1.00 12.44           C  
ATOM    987  CG1 VAL A 124      34.902  13.671 -10.273  1.00 12.79           C  
ATOM    988  CG2 VAL A 124      34.405  15.556  -8.698  1.00 12.86           C  
ATOM    989  N   GLY A 125      31.730  11.990  -9.695  1.00 12.63           N  
ATOM    990  CA  GLY A 125      31.208  10.740 -10.283  1.00 13.14           C  
ATOM    991  C   GLY A 125      30.003  10.983 -11.187  1.00 13.01           C  
ATOM    992  O   GLY A 125      29.921  10.431 -12.294  1.00 13.92           O  
ATOM    993  N   ALA A 126      29.076  11.826 -10.732  1.00 12.87           N  
ATOM    994  CA  ALA A 126      27.837  12.091 -11.468  1.00 13.22           C  
ATOM    995  C   ALA A 126      28.098  12.747 -12.826  1.00 13.36           C  
ATOM    996  O   ALA A 126      27.269  12.657 -13.734  1.00 12.99           O  
ATOM    997  CB  ALA A 126      26.886  12.961 -10.628  1.00 12.63           C  
ATOM    998  N   LEU A 127      29.252  13.407 -12.941  1.00 13.65           N  
ATOM    999  CA  LEU A 127      29.606  14.190 -14.138  1.00 13.87           C  
ATOM   1000  C   LEU A 127      30.639  13.520 -15.026  1.00 13.72           C  
ATOM   1001  O   LEU A 127      31.021  14.077 -16.064  1.00 13.41           O  
ATOM   1002  CB  LEU A 127      30.147  15.555 -13.725  1.00 14.57           C  
ATOM   1003  CG  LEU A 127      29.242  16.439 -12.871  1.00 14.74           C  
ATOM   1004  CD1 LEU A 127      29.997  17.690 -12.425  1.00 15.75           C  
ATOM   1005  CD2 LEU A 127      27.963  16.792 -13.617  1.00 16.10           C  
ATOM   1006  N   THR A 128      31.086  12.335 -14.624  1.00 13.07           N  
ATOM   1007  CA  THR A 128      32.205  11.677 -15.278  1.00 13.43           C  
ATOM   1008  C   THR A 128      31.760  10.975 -16.555  1.00 13.83           C  
ATOM   1009  O   THR A 128      30.740  10.293 -16.572  1.00 13.41           O  
ATOM   1010  CB  THR A 128      32.918  10.722 -14.280  1.00 13.36           C  
ATOM   1011  OG1 THR A 128      33.675  11.510 -13.355  1.00 13.46           O  
ATOM   1012  CG2 THR A 128      33.878   9.787 -14.994  1.00 14.23           C  
ATOM   1013  N   LYS A 129      32.537  11.161 -17.627  1.00 13.95           N  
ATOM   1014  CA  LYS A 129      32.144  10.660 -18.949  1.00 15.35           C  
ATOM   1015  C   LYS A 129      32.546   9.210 -19.245  1.00 15.78           C  
ATOM   1016  O   LYS A 129      31.943   8.573 -20.116  1.00 17.42           O  
ATOM   1017  CB  LYS A 129      32.615  11.604 -20.069  1.00 15.01           C  
ATOM   1018  CG  LYS A 129      32.046  13.003 -19.961  1.00 16.07           C  
ATOM   1019  CD  LYS A 129      32.722  13.976 -20.940  1.00 17.74           C  
ATOM   1020  CE  LYS A 129      32.122  15.356 -20.813  1.00 21.15           C  
ATOM   1021  NZ  LYS A 129      32.793  16.344 -21.728  1.00 25.01           N  
ATOM   1022  N   VAL A 130      33.556   8.703 -18.543  1.00 15.54           N  
ATOM   1023  CA  VAL A 130      33.991   7.310 -18.696  1.00 15.96           C  
ATOM   1024  C   VAL A 130      33.191   6.464 -17.716  1.00 15.81           C  
ATOM   1025  O   VAL A 130      33.314   6.654 -16.512  1.00 15.23           O  
ATOM   1026  CB  VAL A 130      35.504   7.142 -18.399  1.00 16.28           C  
ATOM   1027  CG1 VAL A 130      35.899   5.673 -18.476  1.00 17.42           C  
ATOM   1028  CG2 VAL A 130      36.353   7.988 -19.360  1.00 18.04           C  
ATOM   1029  N   TYR A 131      32.381   5.537 -18.229  1.00 15.95           N  
ATOM   1030  CA  TYR A 131      31.391   4.828 -17.392  1.00 15.77           C  
ATOM   1031  C   TYR A 131      32.014   4.161 -16.177  1.00 16.15           C  
ATOM   1032  O   TYR A 131      31.515   4.319 -15.053  1.00 16.41           O  
ATOM   1033  CB  TYR A 131      30.634   3.774 -18.215  1.00 15.86           C  
ATOM   1034  CG  TYR A 131      29.184   3.538 -17.825  1.00 14.38           C  
ATOM   1035  CD1 TYR A 131      28.706   3.820 -16.530  1.00 13.37           C  
ATOM   1036  CD2 TYR A 131      28.284   3.037 -18.762  1.00 15.43           C  
ATOM   1037  CE1 TYR A 131      27.360   3.592 -16.197  1.00 13.61           C  
ATOM   1038  CE2 TYR A 131      26.957   2.821 -18.455  1.00 15.77           C  
ATOM   1039  CZ  TYR A 131      26.489   3.104 -17.173  1.00 15.70           C  
ATOM   1040  OH  TYR A 131      25.156   2.882 -16.894  1.00 15.41           O  
ATOM   1041  N   SER A 132      33.094   3.410 -16.393  1.00 16.22           N  
ATOM   1042  CA ASER A 132      33.740   2.671 -15.310  0.50 16.45           C  
ATOM   1043  CA BSER A 132      33.738   2.667 -15.309  0.50 16.40           C  
ATOM   1044  C   SER A 132      34.219   3.600 -14.205  1.00 16.45           C  
ATOM   1045  O   SER A 132      34.119   3.264 -13.034  1.00 16.67           O  
ATOM   1046  CB ASER A 132      34.900   1.831 -15.839  0.50 16.68           C  
ATOM   1047  CB BSER A 132      34.901   1.820 -15.830  0.50 16.62           C  
ATOM   1048  OG ASER A 132      34.413   0.828 -16.709  0.50 17.53           O  
ATOM   1049  OG BSER A 132      35.816   2.613 -16.558  0.50 17.19           O  
ATOM   1050  N   TYR A 133      34.718   4.781 -14.590  1.00 16.18           N  
ATOM   1051  CA  TYR A 133      35.239   5.753 -13.625  1.00 16.80           C  
ATOM   1052  C   TYR A 133      34.137   6.404 -12.788  1.00 15.48           C  
ATOM   1053  O   TYR A 133      34.395   6.826 -11.664  1.00 15.38           O  
ATOM   1054  CB  TYR A 133      36.077   6.848 -14.304  1.00 18.59           C  
ATOM   1055  CG  TYR A 133      37.315   6.367 -15.028  1.00 22.16           C  
ATOM   1056  CD1 TYR A 133      37.820   5.084 -14.830  1.00 24.37           C  
ATOM   1057  CD2 TYR A 133      37.996   7.219 -15.903  1.00 24.15           C  
ATOM   1058  CE1 TYR A 133      38.962   4.649 -15.505  1.00 26.27           C  
ATOM   1059  CE2 TYR A 133      39.135   6.799 -16.572  1.00 26.39           C  
ATOM   1060  CZ  TYR A 133      39.608   5.513 -16.367  1.00 25.12           C  
ATOM   1061  OH  TYR A 133      40.740   5.103 -17.040  1.00 27.27           O  
ATOM   1062  N   ARG A 134      32.917   6.501 -13.322  1.00 13.71           N  
ATOM   1063  CA  ARG A 134      31.797   7.006 -12.504  1.00 13.11           C  
ATOM   1064  C   ARG A 134      31.722   6.205 -11.211  1.00 12.82           C  
ATOM   1065  O   ARG A 134      31.485   6.763 -10.137  1.00 13.35           O  
ATOM   1066  CB  ARG A 134      30.464   6.907 -13.244  1.00 12.93           C  
ATOM   1067  CG  ARG A 134      30.435   7.742 -14.525  1.00 13.76           C  
ATOM   1068  CD  ARG A 134      29.109   7.594 -15.286  1.00 12.75           C  
ATOM   1069  NE  ARG A 134      27.971   8.122 -14.532  1.00 13.09           N  
ATOM   1070  CZ  ARG A 134      27.639   9.416 -14.484  1.00 12.84           C  
ATOM   1071  NH1 ARG A 134      28.354  10.328 -15.163  1.00 12.96           N  
ATOM   1072  NH2 ARG A 134      26.585   9.809 -13.776  1.00 13.02           N  
ATOM   1073  N   PHE A 135      31.958   4.902 -11.317  1.00 12.33           N  
ATOM   1074  CA  PHE A 135      31.840   4.021 -10.138  1.00 12.90           C  
ATOM   1075  C   PHE A 135      33.039   4.087  -9.187  1.00 13.38           C  
ATOM   1076  O   PHE A 135      32.909   3.793  -7.991  1.00 13.59           O  
ATOM   1077  CB  PHE A 135      31.509   2.582 -10.554  1.00 12.68           C  
ATOM   1078  CG  PHE A 135      30.182   2.459 -11.275  1.00 12.80           C  
ATOM   1079  CD1 PHE A 135      28.981   2.627 -10.575  1.00 13.15           C  
ATOM   1080  CD2 PHE A 135      30.129   2.168 -12.633  1.00 14.22           C  
ATOM   1081  CE1 PHE A 135      27.753   2.518 -11.228  1.00 13.26           C  
ATOM   1082  CE2 PHE A 135      28.896   2.063 -13.309  1.00 16.01           C  
ATOM   1083  CZ  PHE A 135      27.709   2.238 -12.599  1.00 14.33           C  
ATOM   1084  N   VAL A 136      34.201   4.490  -9.704  1.00 13.94           N  
ATOM   1085  CA  VAL A 136      35.358   4.741  -8.836  1.00 14.03           C  
ATOM   1086  C   VAL A 136      35.014   5.898  -7.895  1.00 13.54           C  
ATOM   1087  O   VAL A 136      35.185   5.781  -6.685  1.00 13.63           O  
ATOM   1088  CB  VAL A 136      36.648   5.104  -9.636  1.00 14.61           C  
ATOM   1089  CG1 VAL A 136      37.767   5.508  -8.689  1.00 15.21           C  
ATOM   1090  CG2 VAL A 136      37.091   3.929 -10.476  1.00 14.99           C  
ATOM   1091  N   TRP A 137      34.500   6.998  -8.452  1.00 13.21           N  
ATOM   1092  CA  TRP A 137      34.099   8.150  -7.634  1.00 12.47           C  
ATOM   1093  C   TRP A 137      32.968   7.796  -6.666  1.00 12.34           C  
ATOM   1094  O   TRP A 137      33.007   8.175  -5.490  1.00 12.49           O  
ATOM   1095  CB  TRP A 137      33.721   9.337  -8.517  1.00 13.97           C  
ATOM   1096  CG  TRP A 137      34.903   9.858  -9.276  1.00 14.11           C  
ATOM   1097  CD1 TRP A 137      35.164   9.696 -10.612  1.00 15.25           C  
ATOM   1098  CD2 TRP A 137      35.989  10.633  -8.744  1.00 14.99           C  
ATOM   1099  NE1 TRP A 137      36.350  10.335 -10.940  1.00 14.56           N  
ATOM   1100  CE2 TRP A 137      36.879  10.899  -9.812  1.00 14.83           C  
ATOM   1101  CE3 TRP A 137      36.310  11.109  -7.460  1.00 16.60           C  
ATOM   1102  CZ2 TRP A 137      38.055  11.646  -9.643  1.00 15.14           C  
ATOM   1103  CZ3 TRP A 137      37.483  11.852  -7.294  1.00 16.63           C  
ATOM   1104  CH2 TRP A 137      38.342  12.105  -8.382  1.00 15.78           C  
ATOM   1105  N   TRP A 138      31.985   7.041  -7.154  1.00 11.32           N  
ATOM   1106  CA  TRP A 138      30.911   6.522  -6.289  1.00 11.75           C  
ATOM   1107  C   TRP A 138      31.471   5.723  -5.092  1.00 11.86           C  
ATOM   1108  O   TRP A 138      31.006   5.870  -3.948  1.00 11.64           O  
ATOM   1109  CB  TRP A 138      29.940   5.669  -7.123  1.00 11.92           C  
ATOM   1110  CG  TRP A 138      28.917   4.935  -6.287  1.00 11.81           C  
ATOM   1111  CD1 TRP A 138      27.673   5.381  -5.929  1.00 11.51           C  
ATOM   1112  CD2 TRP A 138      29.054   3.635  -5.701  1.00 12.83           C  
ATOM   1113  NE1 TRP A 138      27.030   4.443  -5.153  1.00 11.65           N  
ATOM   1114  CE2 TRP A 138      27.859   3.362  -5.000  1.00 12.11           C  
ATOM   1115  CE3 TRP A 138      30.077   2.673  -5.701  1.00 12.80           C  
ATOM   1116  CZ2 TRP A 138      27.667   2.173  -4.290  1.00 11.75           C  
ATOM   1117  CZ3 TRP A 138      29.886   1.500  -5.007  1.00 12.81           C  
ATOM   1118  CH2 TRP A 138      28.683   1.250  -4.321  1.00 12.93           C  
ATOM   1119  N   ALA A 139      32.470   4.878  -5.348  1.00 11.85           N  
ATOM   1120  CA  ALA A 139      33.075   4.065  -4.284  1.00 12.01           C  
ATOM   1121  C   ALA A 139      33.822   4.920  -3.259  1.00 12.34           C  
ATOM   1122  O   ALA A 139      33.741   4.685  -2.055  1.00 12.93           O  
ATOM   1123  CB  ALA A 139      34.020   3.025  -4.890  1.00 12.66           C  
ATOM   1124  N   ILE A 140      34.536   5.931  -3.731  1.00 12.58           N  
ATOM   1125  CA  ILE A 140      35.223   6.841  -2.821  1.00 12.56           C  
ATOM   1126  C   ILE A 140      34.210   7.582  -1.937  1.00 12.63           C  
ATOM   1127  O   ILE A 140      34.373   7.705  -0.715  1.00 12.49           O  
ATOM   1128  CB  ILE A 140      36.093   7.829  -3.609  1.00 12.67           C  
ATOM   1129  CG1 ILE A 140      37.209   7.060  -4.304  1.00 14.35           C  
ATOM   1130  CG2 ILE A 140      36.676   8.902  -2.680  1.00 13.09           C  
ATOM   1131  CD1 ILE A 140      37.946   7.891  -5.339  1.00 15.76           C  
ATOM   1132  N   SER A 141      33.157   8.064  -2.571  1.00 11.79           N  
ATOM   1133  CA  SER A 141      32.102   8.800  -1.867  1.00 11.75           C  
ATOM   1134  C   SER A 141      31.417   7.907  -0.818  1.00 11.83           C  
ATOM   1135  O   SER A 141      31.144   8.329   0.311  1.00 11.25           O  
ATOM   1136  CB  SER A 141      31.094   9.288  -2.892  1.00 11.91           C  
ATOM   1137  OG  SER A 141      30.025   9.952  -2.257  1.00 12.30           O  
ATOM   1138  N   THR A 142      31.143   6.661  -1.210  1.00 11.85           N  
ATOM   1139  CA ATHR A 142      30.532   5.700  -0.305  0.80 11.58           C  
ATOM   1140  CA BTHR A 142      30.515   5.720  -0.285  0.20 11.79           C  
ATOM   1141  C   THR A 142      31.443   5.414   0.897  1.00 11.72           C  
ATOM   1142  O   THR A 142      30.983   5.342   2.037  1.00 11.30           O  
ATOM   1143  CB ATHR A 142      30.138   4.431  -1.093  0.80 11.55           C  
ATOM   1144  CB BTHR A 142      29.966   4.432  -0.985  0.20 11.86           C  
ATOM   1145  OG1ATHR A 142      29.133   4.802  -2.050  0.80 10.44           O  
ATOM   1146  OG1BTHR A 142      29.010   3.784  -0.133  0.20 11.78           O  
ATOM   1147  CG2ATHR A 142      29.586   3.317  -0.168  0.80 10.96           C  
ATOM   1148  CG2BTHR A 142      31.072   3.452  -1.331  0.20 11.85           C  
ATOM   1149  N   ALA A 143      32.749   5.270   0.643  1.00 11.87           N  
ATOM   1150  CA  ALA A 143      33.704   5.086   1.746  1.00 12.01           C  
ATOM   1151  C   ALA A 143      33.670   6.273   2.724  1.00 12.09           C  
ATOM   1152  O   ALA A 143      33.709   6.080   3.947  1.00 12.19           O  
ATOM   1153  CB  ALA A 143      35.118   4.886   1.221  1.00 12.79           C  
ATOM   1154  N   ALA A 144      33.609   7.493   2.190  1.00 12.10           N  
ATOM   1155  CA  ALA A 144      33.509   8.682   3.041  1.00 12.23           C  
ATOM   1156  C   ALA A 144      32.207   8.655   3.862  1.00 11.34           C  
ATOM   1157  O   ALA A 144      32.207   8.946   5.075  1.00 11.38           O  
ATOM   1158  CB  ALA A 144      33.595   9.942   2.207  1.00 11.40           C  
ATOM   1159  N   MET A 145      31.098   8.260   3.230  1.00 11.21           N  
ATOM   1160  CA AMET A 145      29.826   8.153   3.954  0.80 10.86           C  
ATOM   1161  CA BMET A 145      29.826   8.143   3.931  0.20 11.10           C  
ATOM   1162  C   MET A 145      29.948   7.137   5.078  1.00 10.74           C  
ATOM   1163  O   MET A 145      29.484   7.372   6.192  1.00 10.36           O  
ATOM   1164  CB AMET A 145      28.666   7.724   3.043  0.80 10.60           C  
ATOM   1165  CB BMET A 145      28.729   7.717   2.950  0.20 11.39           C  
ATOM   1166  CG AMET A 145      27.311   7.729   3.758  0.80 11.57           C  
ATOM   1167  CG BMET A 145      27.314   7.879   3.469  0.20 12.94           C  
ATOM   1168  SD AMET A 145      26.111   6.649   2.970  0.80 11.98           S  
ATOM   1169  SD BMET A 145      26.769   6.447   4.397  0.20 16.34           S  
ATOM   1170  CE AMET A 145      26.866   5.063   3.283  0.80 13.92           C  
ATOM   1171  CE BMET A 145      26.629   5.219   3.105  0.20 15.50           C  
ATOM   1172  N   LEU A 146      30.559   5.995   4.790  1.00 10.19           N  
ATOM   1173  CA  LEU A 146      30.664   4.960   5.818  1.00 11.00           C  
ATOM   1174  C   LEU A 146      31.537   5.397   6.999  1.00 11.20           C  
ATOM   1175  O   LEU A 146      31.280   5.018   8.154  1.00 12.07           O  
ATOM   1176  CB  LEU A 146      31.150   3.639   5.212  1.00 11.45           C  
ATOM   1177  CG  LEU A 146      30.099   3.047   4.272  1.00 11.70           C  
ATOM   1178  CD1 LEU A 146      30.725   1.981   3.352  1.00 12.95           C  
ATOM   1179  CD2 LEU A 146      28.904   2.446   5.037  1.00 14.68           C  
ATOM   1180  N   TYR A 147      32.558   6.201   6.719  1.00 11.94           N  
ATOM   1181  CA  TYR A 147      33.340   6.819   7.784  1.00 12.43           C  
ATOM   1182  C   TYR A 147      32.405   7.623   8.689  1.00 11.90           C  
ATOM   1183  O   TYR A 147      32.450   7.507   9.906  1.00 11.64           O  
ATOM   1184  CB  TYR A 147      34.439   7.733   7.205  1.00 13.67           C  
ATOM   1185  CG  TYR A 147      35.109   8.560   8.277  1.00 15.05           C  
ATOM   1186  CD1 TYR A 147      36.080   7.998   9.116  1.00 17.18           C  
ATOM   1187  CD2 TYR A 147      34.710   9.876   8.507  1.00 15.42           C  
ATOM   1188  CE1 TYR A 147      36.665   8.755  10.133  1.00 18.17           C  
ATOM   1189  CE2 TYR A 147      35.291  10.639   9.516  1.00 16.95           C  
ATOM   1190  CZ  TYR A 147      36.267  10.064  10.317  1.00 17.30           C  
ATOM   1191  OH  TYR A 147      36.835  10.813  11.326  1.00 19.09           O  
ATOM   1192  N   ILE A 148      31.554   8.434   8.077  1.00 11.57           N  
ATOM   1193  CA  ILE A 148      30.640   9.271   8.847  1.00 11.17           C  
ATOM   1194  C   ILE A 148      29.684   8.412   9.679  1.00 10.91           C  
ATOM   1195  O   ILE A 148      29.478   8.665  10.874  1.00 11.22           O  
ATOM   1196  CB  ILE A 148      29.849  10.204   7.917  1.00 10.96           C  
ATOM   1197  CG1 ILE A 148      30.789  11.224   7.262  1.00 11.24           C  
ATOM   1198  CG2 ILE A 148      28.697  10.885   8.669  1.00 12.00           C  
ATOM   1199  CD1 ILE A 148      30.137  11.983   6.098  1.00 12.92           C  
ATOM   1200  N   LEU A 149      29.101   7.382   9.070  1.00 10.61           N  
ATOM   1201  CA  LEU A 149      28.152   6.543   9.813  1.00 11.03           C  
ATOM   1202  C   LEU A 149      28.856   5.818  10.959  1.00 10.49           C  
ATOM   1203  O   LEU A 149      28.297   5.661  12.031  1.00 11.74           O  
ATOM   1204  CB  LEU A 149      27.414   5.563   8.890  1.00 11.06           C  
ATOM   1205  CG  LEU A 149      26.586   6.252   7.797  1.00 12.17           C  
ATOM   1206  CD1 LEU A 149      25.775   5.183   7.075  1.00 13.60           C  
ATOM   1207  CD2 LEU A 149      25.675   7.357   8.359  1.00 13.15           C  
ATOM   1208  N   TYR A 150      30.097   5.399  10.718  1.00 10.09           N  
ATOM   1209  CA  TYR A 150      30.885   4.744  11.769  1.00 11.31           C  
ATOM   1210  C   TYR A 150      31.086   5.693  12.945  1.00 11.13           C  
ATOM   1211  O   TYR A 150      30.865   5.326  14.106  1.00 12.08           O  
ATOM   1212  CB  TYR A 150      32.238   4.262  11.232  1.00 11.78           C  
ATOM   1213  CG  TYR A 150      33.013   3.490  12.280  1.00 12.14           C  
ATOM   1214  CD1 TYR A 150      33.034   2.091  12.273  1.00 13.55           C  
ATOM   1215  CD2 TYR A 150      33.713   4.168  13.285  1.00 13.60           C  
ATOM   1216  CE1 TYR A 150      33.750   1.381  13.261  1.00 15.69           C  
ATOM   1217  CE2 TYR A 150      34.416   3.471  14.265  1.00 14.35           C  
ATOM   1218  CZ  TYR A 150      34.429   2.093  14.241  1.00 16.57           C  
ATOM   1219  OH  TYR A 150      35.134   1.437  15.227  1.00 17.59           O  
ATOM   1220  N   VAL A 151      31.491   6.927  12.657  1.00 11.63           N  
ATOM   1221  CA AVAL A 151      31.738   7.934  13.694  0.60 12.30           C  
ATOM   1222  CA BVAL A 151      31.746   7.845  13.755  0.40 12.12           C  
ATOM   1223  C   VAL A 151      30.450   8.240  14.462  1.00 12.23           C  
ATOM   1224  O   VAL A 151      30.456   8.389  15.680  1.00 12.62           O  
ATOM   1225  CB AVAL A 151      32.298   9.231  13.069  0.60 12.28           C  
ATOM   1226  CB BVAL A 151      32.608   9.058  13.354  0.40 12.25           C  
ATOM   1227  CG1AVAL A 151      32.375  10.355  14.091  0.60 13.56           C  
ATOM   1228  CG1BVAL A 151      34.001   8.591  12.931  0.40 12.30           C  
ATOM   1229  CG2AVAL A 151      33.684   8.982  12.480  0.60 13.44           C  
ATOM   1230  CG2BVAL A 151      31.956   9.869  12.257  0.40 13.04           C  
ATOM   1231  N   LEU A 152      29.340   8.347  13.724  1.00 12.51           N  
ATOM   1232  CA  LEU A 152      28.045   8.612  14.371  1.00 12.75           C  
ATOM   1233  C   LEU A 152      27.660   7.452  15.277  1.00 13.37           C  
ATOM   1234  O   LEU A 152      27.241   7.646  16.422  1.00 13.83           O  
ATOM   1235  CB  LEU A 152      26.936   8.814  13.343  1.00 13.51           C  
ATOM   1236  CG  LEU A 152      26.956  10.091  12.518  1.00 15.51           C  
ATOM   1237  CD1 LEU A 152      25.709  10.090  11.643  1.00 16.40           C  
ATOM   1238  CD2 LEU A 152      26.981  11.331  13.395  1.00 17.29           C  
ATOM   1239  N   PHE A 153      27.828   6.232  14.770  1.00 13.20           N  
ATOM   1240  CA  PHE A 153      27.359   5.065  15.497  1.00 13.64           C  
ATOM   1241  C   PHE A 153      28.210   4.758  16.716  1.00 14.20           C  
ATOM   1242  O   PHE A 153      27.678   4.405  17.766  1.00 15.37           O  
ATOM   1243  CB  PHE A 153      27.278   3.830  14.587  1.00 13.67           C  
ATOM   1244  CG  PHE A 153      26.545   2.666  15.218  1.00 14.80           C  
ATOM   1245  CD1 PHE A 153      27.238   1.529  15.627  1.00 15.06           C  
ATOM   1246  CD2 PHE A 153      25.171   2.717  15.395  1.00 16.07           C  
ATOM   1247  CE1 PHE A 153      26.560   0.446  16.228  1.00 18.29           C  
ATOM   1248  CE2 PHE A 153      24.489   1.645  15.993  1.00 16.88           C  
ATOM   1249  CZ  PHE A 153      25.190   0.510  16.391  1.00 16.48           C  
ATOM   1250  N   PHE A 154      29.528   4.864  16.575  1.00 13.89           N  
ATOM   1251  CA  PHE A 154      30.433   4.534  17.668  1.00 14.68           C  
ATOM   1252  C   PHE A 154      30.813   5.773  18.460  1.00 15.11           C  
ATOM   1253  O   PHE A 154      30.482   5.874  19.646  1.00 15.99           O  
ATOM   1254  CB  PHE A 154      31.650   3.771  17.131  1.00 15.17           C  
ATOM   1255  CG  PHE A 154      31.333   2.352  16.740  1.00 15.00           C  
ATOM   1256  CD1 PHE A 154      31.230   1.364  17.715  1.00 17.60           C  
ATOM   1257  CD2 PHE A 154      31.136   2.006  15.408  1.00 16.39           C  
ATOM   1258  CE1 PHE A 154      30.912   0.048  17.365  1.00 17.52           C  
ATOM   1259  CE2 PHE A 154      30.831   0.696  15.043  1.00 15.94           C  
ATOM   1260  CZ  PHE A 154      30.720  -0.285  16.027  1.00 17.73           C  
ATOM   1261  N   GLY A 155      31.447   6.736  17.798  1.00 14.87           N  
ATOM   1262  CA  GLY A 155      31.962   7.940  18.480  1.00 14.40           C  
ATOM   1263  C   GLY A 155      30.895   8.825  19.106  1.00 13.76           C  
ATOM   1264  O   GLY A 155      30.974   9.188  20.299  1.00 14.12           O  
ATOM   1265  N   PHE A 156      29.892   9.198  18.319  1.00 13.70           N  
ATOM   1266  CA  PHE A 156      28.861  10.097  18.842  1.00 13.26           C  
ATOM   1267  C   PHE A 156      28.037   9.394  19.920  1.00 12.84           C  
ATOM   1268  O   PHE A 156      27.629  10.022  20.898  1.00 13.03           O  
ATOM   1269  CB  PHE A 156      27.940  10.634  17.734  1.00 13.24           C  
ATOM   1270  CG  PHE A 156      28.532  11.765  16.906  1.00 14.42           C  
ATOM   1271  CD1 PHE A 156      29.851  11.735  16.463  1.00 15.48           C  
ATOM   1272  CD2 PHE A 156      27.715  12.818  16.497  1.00 14.18           C  
ATOM   1273  CE1 PHE A 156      30.363  12.773  15.655  1.00 17.07           C  
ATOM   1274  CE2 PHE A 156      28.216  13.862  15.683  1.00 15.70           C  
ATOM   1275  CZ  PHE A 156      29.548  13.834  15.274  1.00 14.30           C  
ATOM   1276  N   THR A 157      27.801   8.093  19.756  1.00 12.41           N  
ATOM   1277  CA  THR A 157      27.035   7.354  20.750  1.00 13.13           C  
ATOM   1278  C   THR A 157      27.793   7.305  22.064  1.00 13.38           C  
ATOM   1279  O   THR A 157      27.194   7.517  23.119  1.00 14.45           O  
ATOM   1280  CB  THR A 157      26.656   5.951  20.272  1.00 12.62           C  
ATOM   1281  OG1 THR A 157      25.897   6.077  19.062  1.00 12.80           O  
ATOM   1282  CG2 THR A 157      25.807   5.239  21.323  1.00 14.46           C  
ATOM   1283  N   SER A 158      29.108   7.102  21.996  1.00 13.95           N  
ATOM   1284  CA ASER A 158      29.937   7.106  23.206  0.60 14.11           C  
ATOM   1285  CA BSER A 158      29.937   7.109  23.201  0.40 14.29           C  
ATOM   1286  C   SER A 158      29.807   8.439  23.942  1.00 14.46           C  
ATOM   1287  O   SER A 158      29.654   8.466  25.171  1.00 14.33           O  
ATOM   1288  CB ASER A 158      31.404   6.843  22.875  0.60 14.54           C  
ATOM   1289  CB BSER A 158      31.394   6.824  22.847  0.40 14.61           C  
ATOM   1290  OG ASER A 158      32.156   6.728  24.074  0.60 15.23           O  
ATOM   1291  OG BSER A 158      31.554   5.459  22.510  0.40 16.00           O  
ATOM   1292  N   LYS A 159      29.856   9.543  23.194  1.00 14.70           N  
ATOM   1293  CA  LYS A 159      29.645  10.889  23.765  1.00 14.98           C  
ATOM   1294  C   LYS A 159      28.237  11.063  24.344  1.00 15.23           C  
ATOM   1295  O   LYS A 159      28.058  11.674  25.394  1.00 15.17           O  
ATOM   1296  CB  LYS A 159      29.904  11.969  22.705  1.00 15.55           C  
ATOM   1297  CG  LYS A 159      31.372  12.168  22.388  1.00 17.70           C  
ATOM   1298  CD  LYS A 159      32.032  12.911  23.549  1.00 20.83           C  
ATOM   1299  CE  LYS A 159      33.499  13.171  23.291  1.00 24.77           C  
ATOM   1300  NZ  LYS A 159      34.098  13.906  24.447  1.00 26.58           N  
ATOM   1301  N   ALA A 160      27.236  10.526  23.652  1.00 14.58           N  
ATOM   1302  CA  ALA A 160      25.851  10.614  24.102  1.00 15.52           C  
ATOM   1303  C   ALA A 160      25.644   9.974  25.466  1.00 16.65           C  
ATOM   1304  O   ALA A 160      24.825  10.454  26.254  1.00 16.42           O  
ATOM   1305  CB  ALA A 160      24.918   9.990  23.068  1.00 15.49           C  
ATOM   1306  N   GLU A 161      26.420   8.928  25.746  1.00 17.28           N  
ATOM   1307  CA AGLU A 161      26.245   8.189  26.993  0.35 17.59           C  
ATOM   1308  CA BGLU A 161      26.294   8.175  26.995  0.35 17.68           C  
ATOM   1309  CA CGLU A 161      26.313   8.163  26.994  0.30 17.63           C  
ATOM   1310  C   GLU A 161      26.634   9.002  28.229  1.00 17.50           C  
ATOM   1311  O   GLU A 161      26.306   8.612  29.357  1.00 18.33           O  
ATOM   1312  CB AGLU A 161      26.971   6.837  26.955  0.35 18.14           C  
ATOM   1313  CB BGLU A 161      27.155   6.913  26.950  0.35 18.30           C  
ATOM   1314  CB CGLU A 161      27.229   6.929  26.968  0.30 18.19           C  
ATOM   1315  CG AGLU A 161      26.545   5.916  25.804  0.35 19.04           C  
ATOM   1316  CG BGLU A 161      26.459   5.745  26.279  0.35 19.65           C  
ATOM   1317  CG CGLU A 161      26.934   5.907  25.863  0.30 19.37           C  
ATOM   1318  CD AGLU A 161      25.058   5.990  25.484  0.35 19.58           C  
ATOM   1319  CD BGLU A 161      27.417   4.687  25.772  0.35 20.91           C  
ATOM   1320  CD CGLU A 161      25.587   5.205  26.006  0.30 20.95           C  
ATOM   1321  OE1AGLU A 161      24.233   5.617  26.348  0.35 21.16           O  
ATOM   1322  OE1BGLU A 161      28.594   4.665  26.200  0.35 21.57           O  
ATOM   1323  OE1CGLU A 161      24.986   5.240  27.106  0.30 22.09           O  
ATOM   1324  OE2AGLU A 161      24.715   6.419  24.359  0.35 20.61           O  
ATOM   1325  OE2BGLU A 161      26.985   3.873  24.932  0.35 22.61           O  
ATOM   1326  OE2CGLU A 161      25.132   4.603  25.009  0.30 21.21           O  
ATOM   1327  N   SER A 162      27.300  10.141  28.021  1.00 16.49           N  
ATOM   1328  CA ASER A 162      27.642  11.044  29.123  0.80 16.12           C  
ATOM   1329  CA BSER A 162      27.641  11.036  29.131  0.20 15.73           C  
ATOM   1330  C   SER A 162      26.573  12.106  29.366  1.00 15.36           C  
ATOM   1331  O   SER A 162      26.638  12.851  30.345  1.00 15.04           O  
ATOM   1332  CB ASER A 162      28.995  11.707  28.867  0.80 16.88           C  
ATOM   1333  CB BSER A 162      29.008  11.686  28.907  0.20 15.95           C  
ATOM   1334  OG ASER A 162      30.025  10.741  28.992  0.80 19.61           O  
ATOM   1335  OG BSER A 162      29.012  12.463  27.728  0.20 15.67           O  
ATOM   1336  N   MET A 163      25.595  12.172  28.468  1.00 14.32           N  
ATOM   1337  CA  MET A 163      24.500  13.140  28.578  1.00 14.59           C  
ATOM   1338  C   MET A 163      23.353  12.572  29.412  1.00 14.45           C  
ATOM   1339  O   MET A 163      23.342  11.369  29.707  1.00 14.19           O  
ATOM   1340  CB  MET A 163      23.984  13.505  27.170  1.00 14.89           C  
ATOM   1341  CG  MET A 163      25.069  14.000  26.204  1.00 17.86           C  
ATOM   1342  SD  MET A 163      25.916  15.509  26.773  1.00 25.34           S  
ATOM   1343  CE  MET A 163      24.696  16.729  26.383  1.00 25.89           C  
ATOM   1344  N   ARG A 164      22.395  13.428  29.795  1.00 14.84           N  
ATOM   1345  CA AARG A 164      21.162  12.970  30.443  0.60 15.75           C  
ATOM   1346  CA BARG A 164      21.188  12.944  30.459  0.40 15.49           C  
ATOM   1347  C   ARG A 164      20.510  11.912  29.555  1.00 15.74           C  
ATOM   1348  O   ARG A 164      20.553  12.040  28.332  1.00 15.04           O  
ATOM   1349  CB AARG A 164      20.161  14.117  30.609  0.60 15.89           C  
ATOM   1350  CB BARG A 164      20.222  14.089  30.777  0.40 15.56           C  
ATOM   1351  CG AARG A 164      20.615  15.267  31.476  0.60 17.48           C  
ATOM   1352  CG BARG A 164      20.593  14.898  32.006  0.40 16.44           C  
ATOM   1353  CD AARG A 164      19.482  16.274  31.669  0.60 18.09           C  
ATOM   1354  CD BARG A 164      19.516  15.912  32.367  0.40 17.06           C  
ATOM   1355  NE AARG A 164      19.186  17.079  30.481  0.60 23.72           N  
ATOM   1356  NE BARG A 164      19.953  16.828  33.422  0.40 20.11           N  
ATOM   1357  CZ AARG A 164      18.084  16.966  29.739  0.60 23.72           C  
ATOM   1358  CZ BARG A 164      19.256  17.872  33.864  0.40 21.50           C  
ATOM   1359  NH1AARG A 164      17.150  16.072  30.044  0.60 25.21           N  
ATOM   1360  NH1BARG A 164      18.068  18.164  33.347  0.40 22.05           N  
ATOM   1361  NH2AARG A 164      17.911  17.755  28.691  0.60 25.17           N  
ATOM   1362  NH2BARG A 164      19.753  18.636  34.826  0.40 22.83           N  
ATOM   1363  N   PRO A 165      19.911  10.867  30.155  1.00 15.79           N  
ATOM   1364  CA  PRO A 165      19.244   9.859  29.328  1.00 15.92           C  
ATOM   1365  C   PRO A 165      18.262  10.407  28.295  1.00 16.20           C  
ATOM   1366  O   PRO A 165      18.189   9.836  27.192  1.00 16.59           O  
ATOM   1367  CB  PRO A 165      18.542   8.969  30.356  1.00 16.54           C  
ATOM   1368  CG  PRO A 165      19.434   9.045  31.527  1.00 17.02           C  
ATOM   1369  CD  PRO A 165      19.872  10.486  31.584  1.00 15.98           C  
ATOM   1370  N   GLU A 166      17.550  11.494  28.599  1.00 15.95           N  
ATOM   1371  CA AGLU A 166      16.599  12.027  27.623  0.60 16.12           C  
ATOM   1372  CA BGLU A 166      16.602  12.107  27.652  0.40 16.50           C  
ATOM   1373  C   GLU A 166      17.306  12.592  26.384  1.00 16.14           C  
ATOM   1374  O   GLU A 166      16.772  12.492  25.270  1.00 15.76           O  
ATOM   1375  CB AGLU A 166      15.629  13.030  28.259  0.60 16.45           C  
ATOM   1376  CB BGLU A 166      15.836  13.270  28.308  0.40 16.61           C  
ATOM   1377  CG AGLU A 166      14.533  13.529  27.311  0.60 17.99           C  
ATOM   1378  CG BGLU A 166      16.715  14.439  28.772  0.40 17.80           C  
ATOM   1379  CD AGLU A 166      15.037  14.616  26.383  0.60 18.24           C  
ATOM   1380  CD BGLU A 166      15.930  15.668  29.202  0.40 18.44           C  
ATOM   1381  OE1AGLU A 166      15.971  15.341  26.793  0.60 18.87           O  
ATOM   1382  OE1BGLU A 166      14.866  15.517  29.848  0.40 21.34           O  
ATOM   1383  OE2AGLU A 166      14.520  14.728  25.242  0.60 20.68           O  
ATOM   1384  OE2BGLU A 166      16.392  16.792  28.904  0.40 21.49           O  
ATOM   1385  N   VAL A 167      18.498  13.151  26.569  1.00 14.81           N  
ATOM   1386  CA  VAL A 167      19.308  13.669  25.467  1.00 14.16           C  
ATOM   1387  C   VAL A 167      19.884  12.480  24.695  1.00 13.58           C  
ATOM   1388  O   VAL A 167      19.825  12.436  23.452  1.00 13.35           O  
ATOM   1389  CB  VAL A 167      20.446  14.603  25.977  1.00 14.44           C  
ATOM   1390  CG1 VAL A 167      21.398  14.964  24.845  1.00 15.16           C  
ATOM   1391  CG2 VAL A 167      19.857  15.859  26.575  1.00 14.69           C  
ATOM   1392  N   ALA A 168      20.430  11.500  25.417  1.00 13.69           N  
ATOM   1393  CA  ALA A 168      20.969  10.303  24.756  1.00 13.69           C  
ATOM   1394  C   ALA A 168      19.894   9.592  23.927  1.00 13.60           C  
ATOM   1395  O   ALA A 168      20.165   9.132  22.806  1.00 13.80           O  
ATOM   1396  CB  ALA A 168      21.549   9.340  25.785  1.00 13.99           C  
ATOM   1397  N   SER A 169      18.678   9.525  24.466  1.00 13.65           N  
ATOM   1398  CA ASER A 169      17.558   8.838  23.813  0.50 14.02           C  
ATOM   1399  CA BSER A 169      17.592   8.821  23.785  0.50 13.72           C  
ATOM   1400  C   SER A 169      17.163   9.517  22.505  1.00 13.34           C  
ATOM   1401  O   SER A 169      16.946   8.856  21.487  1.00 13.96           O  
ATOM   1402  CB ASER A 169      16.346   8.791  24.750  0.50 14.38           C  
ATOM   1403  CB BSER A 169      16.403   8.632  24.719  0.50 14.14           C  
ATOM   1404  OG ASER A 169      15.321   7.987  24.197  0.50 16.41           O  
ATOM   1405  OG BSER A 169      16.756   7.717  25.730  0.50 14.08           O  
ATOM   1406  N   THR A 170      17.045  10.841  22.552  1.00 13.03           N  
ATOM   1407  CA  THR A 170      16.719  11.634  21.361  1.00 12.68           C  
ATOM   1408  C   THR A 170      17.842  11.481  20.337  1.00 12.10           C  
ATOM   1409  O   THR A 170      17.572  11.244  19.134  1.00 12.01           O  
ATOM   1410  CB  THR A 170      16.497  13.118  21.730  1.00 13.76           C  
ATOM   1411  OG1 THR A 170      15.381  13.207  22.627  1.00 14.43           O  
ATOM   1412  CG2 THR A 170      16.201  13.967  20.488  1.00 13.31           C  
ATOM   1413  N   PHE A 171      19.090  11.558  20.806  1.00 11.68           N  
ATOM   1414  CA  PHE A 171      20.216  11.331  19.894  1.00 11.28           C  
ATOM   1415  C   PHE A 171      20.103   9.964  19.216  1.00 11.51           C  
ATOM   1416  O   PHE A 171      20.323   9.855  18.007  1.00 11.84           O  
ATOM   1417  CB  PHE A 171      21.591  11.429  20.574  1.00 11.51           C  
ATOM   1418  CG  PHE A 171      22.692  10.852  19.712  1.00 10.63           C  
ATOM   1419  CD1 PHE A 171      23.159  11.554  18.608  1.00 12.07           C  
ATOM   1420  CD2 PHE A 171      23.181   9.568  19.955  1.00 12.11           C  
ATOM   1421  CE1 PHE A 171      24.131  11.010  17.781  1.00 12.35           C  
ATOM   1422  CE2 PHE A 171      24.155   9.018  19.149  1.00 12.63           C  
ATOM   1423  CZ  PHE A 171      24.615   9.735  18.045  1.00 12.51           C  
ATOM   1424  N   LYS A 172      19.784   8.917  19.984  1.00 11.54           N  
ATOM   1425  CA  LYS A 172      19.757   7.568  19.389  1.00 11.93           C  
ATOM   1426  C   LYS A 172      18.681   7.437  18.320  1.00 11.59           C  
ATOM   1427  O   LYS A 172      18.912   6.812  17.281  1.00 11.58           O  
ATOM   1428  CB  LYS A 172      19.622   6.482  20.459  1.00 12.35           C  
ATOM   1429  CG  LYS A 172      20.868   6.340  21.299  1.00 15.34           C  
ATOM   1430  CD  LYS A 172      20.627   5.328  22.406  1.00 19.53           C  
ATOM   1431  CE  LYS A 172      21.815   5.269  23.346  1.00 24.57           C  
ATOM   1432  NZ  LYS A 172      21.613   4.248  24.422  1.00 27.11           N  
ATOM   1433  N   VAL A 173      17.527   8.060  18.538  1.00 11.22           N  
ATOM   1434  CA  VAL A 173      16.468   8.033  17.517  1.00 11.21           C  
ATOM   1435  C   VAL A 173      16.973   8.719  16.238  1.00 11.02           C  
ATOM   1436  O   VAL A 173      16.860   8.185  15.131  1.00 11.63           O  
ATOM   1437  CB  VAL A 173      15.173   8.703  18.004  1.00 11.13           C  
ATOM   1438  CG1 VAL A 173      14.160   8.836  16.842  1.00 13.18           C  
ATOM   1439  CG2 VAL A 173      14.575   7.907  19.163  1.00 12.89           C  
ATOM   1440  N   LEU A 174      17.551   9.908  16.401  1.00 10.31           N  
ATOM   1441  CA  LEU A 174      17.996  10.690  15.241  1.00 10.62           C  
ATOM   1442  C   LEU A 174      19.169  10.000  14.544  1.00 10.58           C  
ATOM   1443  O   LEU A 174      19.276  10.020  13.295  1.00 11.65           O  
ATOM   1444  CB  LEU A 174      18.392  12.091  15.683  1.00 10.88           C  
ATOM   1445  CG  LEU A 174      17.208  12.915  16.187  1.00 10.27           C  
ATOM   1446  CD1 LEU A 174      17.736  14.160  16.911  1.00 12.09           C  
ATOM   1447  CD2 LEU A 174      16.292  13.302  15.026  1.00 12.84           C  
ATOM   1448  N   ARG A 175      20.046   9.392  15.338  1.00 10.72           N  
ATOM   1449  CA  ARG A 175      21.176   8.629  14.799  1.00 10.39           C  
ATOM   1450  C   ARG A 175      20.637   7.498  13.926  1.00 10.52           C  
ATOM   1451  O   ARG A 175      21.107   7.268  12.804  1.00 11.47           O  
ATOM   1452  CB  ARG A 175      21.977   8.019  15.949  1.00 10.91           C  
ATOM   1453  CG  ARG A 175      23.138   7.103  15.514  1.00 11.26           C  
ATOM   1454  CD  ARG A 175      23.552   6.209  16.713  1.00 13.33           C  
ATOM   1455  NE  ARG A 175      22.516   5.206  16.962  1.00 13.43           N  
ATOM   1456  CZ  ARG A 175      22.513   4.340  17.977  1.00 16.93           C  
ATOM   1457  NH1 ARG A 175      23.492   4.337  18.880  1.00 16.79           N  
ATOM   1458  NH2 ARG A 175      21.520   3.458  18.084  1.00 17.89           N  
ATOM   1459  N   ASN A 176      19.640   6.796  14.451  1.00 10.41           N  
ATOM   1460  CA  ASN A 176      19.060   5.651  13.749  1.00 10.50           C  
ATOM   1461  C   ASN A 176      18.374   6.046  12.449  1.00 10.49           C  
ATOM   1462  O   ASN A 176      18.544   5.392  11.416  1.00 11.45           O  
ATOM   1463  CB  ASN A 176      18.069   4.923  14.654  1.00 10.93           C  
ATOM   1464  CG  ASN A 176      18.755   4.156  15.762  1.00 12.05           C  
ATOM   1465  OD1 ASN A 176      19.992   4.125  15.836  1.00 12.76           O  
ATOM   1466  ND2 ASN A 176      17.960   3.535  16.637  1.00 14.83           N  
ATOM   1467  N   VAL A 177      17.632   7.147  12.491  1.00 10.35           N  
ATOM   1468  CA  VAL A 177      16.996   7.696  11.292  1.00 11.10           C  
ATOM   1469  C   VAL A 177      18.067   8.056  10.265  1.00 11.31           C  
ATOM   1470  O   VAL A 177      17.940   7.748   9.079  1.00 12.01           O  
ATOM   1471  CB  VAL A 177      16.170   8.951  11.676  1.00 11.24           C  
ATOM   1472  CG1 VAL A 177      15.800   9.806  10.452  1.00 13.04           C  
ATOM   1473  CG2 VAL A 177      14.922   8.527  12.470  1.00 11.80           C  
ATOM   1474  N   THR A 178      19.135   8.704  10.728  1.00 11.59           N  
ATOM   1475  CA  THR A 178      20.248   9.092   9.857  1.00 11.95           C  
ATOM   1476  C   THR A 178      20.939   7.879   9.210  1.00 11.76           C  
ATOM   1477  O   THR A 178      21.121   7.839   7.992  1.00 12.04           O  
ATOM   1478  CB  THR A 178      21.248   9.966  10.649  1.00 12.42           C  
ATOM   1479  OG1 THR A 178      20.573  11.161  11.060  1.00 11.93           O  
ATOM   1480  CG2 THR A 178      22.490  10.340   9.812  1.00 12.24           C  
ATOM   1481  N   VAL A 179      21.258   6.858  10.000  1.00 11.38           N  
ATOM   1482  CA  VAL A 179      21.929   5.678   9.429  1.00 10.69           C  
ATOM   1483  C   VAL A 179      21.047   4.990   8.388  1.00 10.76           C  
ATOM   1484  O   VAL A 179      21.513   4.659   7.291  1.00 11.01           O  
ATOM   1485  CB  VAL A 179      22.316   4.674  10.535  1.00 10.71           C  
ATOM   1486  CG1 VAL A 179      22.726   3.327   9.924  1.00 11.52           C  
ATOM   1487  CG2 VAL A 179      23.447   5.277  11.372  1.00 10.83           C  
ATOM   1488  N   VAL A 180      19.763   4.831   8.706  1.00 11.08           N  
ATOM   1489  CA  VAL A 180      18.870   4.119   7.775  1.00 10.98           C  
ATOM   1490  C   VAL A 180      18.689   4.927   6.480  1.00 10.76           C  
ATOM   1491  O   VAL A 180      18.792   4.380   5.374  1.00 12.02           O  
ATOM   1492  CB  VAL A 180      17.510   3.805   8.399  1.00 11.41           C  
ATOM   1493  CG1 VAL A 180      16.531   3.290   7.320  1.00 13.07           C  
ATOM   1494  CG2 VAL A 180      17.648   2.788   9.536  1.00 11.14           C  
ATOM   1495  N   LEU A 181      18.436   6.227   6.601  1.00  9.89           N  
ATOM   1496  CA  LEU A 181      18.153   7.012   5.397  1.00  9.80           C  
ATOM   1497  C   LEU A 181      19.404   7.256   4.559  1.00 10.36           C  
ATOM   1498  O   LEU A 181      19.385   7.077   3.328  1.00 10.35           O  
ATOM   1499  CB  LEU A 181      17.494   8.343   5.785  1.00 10.33           C  
ATOM   1500  CG  LEU A 181      16.120   8.194   6.443  1.00 10.66           C  
ATOM   1501  CD1 LEU A 181      15.646   9.548   6.943  1.00 13.27           C  
ATOM   1502  CD2 LEU A 181      15.111   7.624   5.448  1.00 12.80           C  
ATOM   1503  N   TRP A 182      20.497   7.647   5.215  1.00 10.69           N  
ATOM   1504  CA  TRP A 182      21.727   7.982   4.472  1.00 10.59           C  
ATOM   1505  C   TRP A 182      22.256   6.748   3.733  1.00 10.79           C  
ATOM   1506  O   TRP A 182      22.699   6.863   2.577  1.00 11.62           O  
ATOM   1507  CB  TRP A 182      22.811   8.544   5.396  1.00 11.44           C  
ATOM   1508  CG  TRP A 182      22.568   9.946   5.898  1.00 10.49           C  
ATOM   1509  CD1 TRP A 182      21.382  10.494   6.311  1.00 11.58           C  
ATOM   1510  CD2 TRP A 182      23.575  10.950   6.115  1.00 10.12           C  
ATOM   1511  NE1 TRP A 182      21.584  11.799   6.740  1.00 10.91           N  
ATOM   1512  CE2 TRP A 182      22.921  12.098   6.637  1.00 11.81           C  
ATOM   1513  CE3 TRP A 182      24.963  10.997   5.899  1.00 12.60           C  
ATOM   1514  CZ2 TRP A 182      23.619  13.276   6.961  1.00 11.94           C  
ATOM   1515  CZ3 TRP A 182      25.661  12.189   6.219  1.00 12.30           C  
ATOM   1516  CH2 TRP A 182      24.972  13.305   6.736  1.00 11.81           C  
ATOM   1517  N   SER A 183      22.159   5.573   4.364  1.00 10.67           N  
ATOM   1518  CA  SER A 183      22.755   4.361   3.764  1.00 11.64           C  
ATOM   1519  C   SER A 183      22.051   3.988   2.446  1.00 11.61           C  
ATOM   1520  O   SER A 183      22.604   3.222   1.643  1.00 11.95           O  
ATOM   1521  CB  SER A 183      22.719   3.185   4.748  1.00 12.52           C  
ATOM   1522  OG  SER A 183      21.399   2.732   4.939  1.00 14.91           O  
ATOM   1523  N   ALA A 184      20.843   4.517   2.238  1.00 10.52           N  
ATOM   1524  CA  ALA A 184      20.077   4.208   1.007  1.00 11.20           C  
ATOM   1525  C   ALA A 184      20.539   5.021  -0.194  1.00 11.18           C  
ATOM   1526  O   ALA A 184      20.388   4.581  -1.344  1.00 10.86           O  
ATOM   1527  CB  ALA A 184      18.589   4.406   1.234  1.00 11.22           C  
ATOM   1528  N   TYR A 185      21.077   6.214   0.063  1.00 10.48           N  
ATOM   1529  CA  TYR A 185      21.451   7.112  -1.041  1.00 10.36           C  
ATOM   1530  C   TYR A 185      22.452   6.485  -2.019  1.00 10.80           C  
ATOM   1531  O   TYR A 185      22.247   6.560  -3.228  1.00 10.62           O  
ATOM   1532  CB  TYR A 185      21.989   8.453  -0.524  1.00 11.10           C  
ATOM   1533  CG  TYR A 185      20.926   9.393  -0.013  1.00 10.22           C  
ATOM   1534  CD1 TYR A 185      20.383   9.230   1.262  1.00 11.46           C  
ATOM   1535  CD2 TYR A 185      20.486  10.466  -0.789  1.00 11.43           C  
ATOM   1536  CE1 TYR A 185      19.424  10.104   1.749  1.00 11.16           C  
ATOM   1537  CE2 TYR A 185      19.521  11.354  -0.308  1.00 12.00           C  
ATOM   1538  CZ  TYR A 185      18.993  11.162   0.962  1.00 10.89           C  
ATOM   1539  OH  TYR A 185      18.025  12.029   1.460  1.00 12.21           O  
ATOM   1540  N   PRO A 186      23.545   5.881  -1.525  1.00 10.41           N  
ATOM   1541  CA  PRO A 186      24.476   5.285  -2.504  1.00 10.81           C  
ATOM   1542  C   PRO A 186      23.840   4.193  -3.355  1.00 10.98           C  
ATOM   1543  O   PRO A 186      24.234   4.024  -4.516  1.00 11.36           O  
ATOM   1544  CB  PRO A 186      25.613   4.690  -1.642  1.00 10.70           C  
ATOM   1545  CG  PRO A 186      25.137   4.768  -0.215  1.00 10.59           C  
ATOM   1546  CD  PRO A 186      24.056   5.826  -0.144  1.00 11.23           C  
ATOM   1547  N   VAL A 187      22.871   3.465  -2.796  1.00 10.74           N  
ATOM   1548  CA  VAL A 187      22.173   2.399  -3.553  1.00 11.13           C  
ATOM   1549  C   VAL A 187      21.269   3.019  -4.625  1.00 11.23           C  
ATOM   1550  O   VAL A 187      21.276   2.583  -5.788  1.00 11.77           O  
ATOM   1551  CB  VAL A 187      21.383   1.467  -2.613  1.00 11.83           C  
ATOM   1552  CG1 VAL A 187      20.601   0.412  -3.422  1.00 13.14           C  
ATOM   1553  CG2 VAL A 187      22.354   0.790  -1.673  1.00 12.61           C  
ATOM   1554  N   VAL A 188      20.543   4.079  -4.287  1.00 11.18           N  
ATOM   1555  CA  VAL A 188      19.701   4.747  -5.296  1.00 10.84           C  
ATOM   1556  C   VAL A 188      20.585   5.261  -6.449  1.00 11.24           C  
ATOM   1557  O   VAL A 188      20.265   5.073  -7.618  1.00 11.99           O  
ATOM   1558  CB  VAL A 188      18.859   5.877  -4.652  1.00 11.80           C  
ATOM   1559  CG1 VAL A 188      18.048   6.624  -5.697  1.00 12.04           C  
ATOM   1560  CG2 VAL A 188      17.945   5.270  -3.582  1.00 11.80           C  
ATOM   1561  N   TRP A 189      21.720   5.862  -6.112  1.00 11.42           N  
ATOM   1562  CA  TRP A 189      22.635   6.395  -7.135  1.00 11.69           C  
ATOM   1563  C   TRP A 189      23.165   5.253  -8.010  1.00 11.65           C  
ATOM   1564  O   TRP A 189      23.159   5.342  -9.245  1.00 11.69           O  
ATOM   1565  CB  TRP A 189      23.777   7.083  -6.419  1.00 12.32           C  
ATOM   1566  CG  TRP A 189      24.659   8.016  -7.205  1.00 12.92           C  
ATOM   1567  CD1 TRP A 189      24.663   9.380  -7.131  1.00 14.22           C  
ATOM   1568  CD2 TRP A 189      25.719   7.658  -8.114  1.00 12.23           C  
ATOM   1569  NE1 TRP A 189      25.645   9.898  -7.945  1.00 14.10           N  
ATOM   1570  CE2 TRP A 189      26.312   8.864  -8.555  1.00 13.83           C  
ATOM   1571  CE3 TRP A 189      26.217   6.442  -8.603  1.00 14.05           C  
ATOM   1572  CZ2 TRP A 189      27.395   8.886  -9.443  1.00 13.34           C  
ATOM   1573  CZ3 TRP A 189      27.291   6.466  -9.497  1.00 13.37           C  
ATOM   1574  CH2 TRP A 189      27.855   7.680  -9.918  1.00 13.61           C  
ATOM   1575  N   LEU A 190      23.581   4.158  -7.364  1.00 10.86           N  
ATOM   1576  CA  LEU A 190      24.156   3.010  -8.070  1.00 11.78           C  
ATOM   1577  C   LEU A 190      23.194   2.426  -9.097  1.00 11.41           C  
ATOM   1578  O   LEU A 190      23.611   2.062 -10.204  1.00 11.71           O  
ATOM   1579  CB  LEU A 190      24.540   1.923  -7.056  1.00 11.96           C  
ATOM   1580  CG  LEU A 190      25.257   0.672  -7.572  1.00 13.39           C  
ATOM   1581  CD1 LEU A 190      26.662   1.050  -8.032  1.00 16.09           C  
ATOM   1582  CD2 LEU A 190      25.336  -0.402  -6.480  1.00 13.87           C  
ATOM   1583  N   ILE A 191      21.918   2.319  -8.733  1.00 10.98           N  
ATOM   1584  CA  ILE A 191      20.937   1.630  -9.598  1.00 11.74           C  
ATOM   1585  C   ILE A 191      20.167   2.583 -10.511  1.00 12.22           C  
ATOM   1586  O   ILE A 191      19.458   2.136 -11.413  1.00 12.03           O  
ATOM   1587  CB  ILE A 191      19.921   0.774  -8.779  1.00 12.00           C  
ATOM   1588  CG1 ILE A 191      19.008   1.671  -7.923  1.00 12.03           C  
ATOM   1589  CG2 ILE A 191      20.660  -0.238  -7.927  1.00 12.67           C  
ATOM   1590  CD1 ILE A 191      17.980   0.892  -7.049  1.00 11.90           C  
ATOM   1591  N   GLY A 192      20.297   3.883 -10.251  1.00 12.31           N  
ATOM   1592  CA  GLY A 192      19.473   4.891 -10.926  1.00 12.50           C  
ATOM   1593  C   GLY A 192      20.165   5.583 -12.083  1.00 13.54           C  
ATOM   1594  O   GLY A 192      21.101   5.046 -12.666  1.00 12.82           O  
ATOM   1595  N   SER A 193      19.711   6.808 -12.367  1.00 13.52           N  
ATOM   1596  CA ASER A 193      20.142   7.580 -13.543  0.60 14.29           C  
ATOM   1597  CA BSER A 193      20.147   7.568 -13.547  0.40 14.43           C  
ATOM   1598  C   SER A 193      21.648   7.840 -13.620  1.00 14.21           C  
ATOM   1599  O   SER A 193      22.218   7.986 -14.731  1.00 15.07           O  
ATOM   1600  CB ASER A 193      19.405   8.926 -13.564  0.60 14.35           C  
ATOM   1601  CB BSER A 193      19.398   8.899 -13.598  0.40 14.53           C  
ATOM   1602  OG ASER A 193      19.828   9.758 -12.499  0.60 15.16           O  
ATOM   1603  OG BSER A 193      18.005   8.671 -13.568  0.40 16.38           O  
ATOM   1604  N   GLU A 194      22.276   7.947 -12.453  1.00 14.00           N  
ATOM   1605  CA  GLU A 194      23.680   8.303 -12.353  1.00 14.42           C  
ATOM   1606  C   GLU A 194      24.589   7.102 -12.508  1.00 13.94           C  
ATOM   1607  O   GLU A 194      25.764   7.251 -12.826  1.00 14.11           O  
ATOM   1608  CB  GLU A 194      23.964   8.979 -11.006  1.00 14.59           C  
ATOM   1609  CG  GLU A 194      23.145  10.244 -10.730  1.00 17.43           C  
ATOM   1610  CD  GLU A 194      21.812   9.960 -10.017  1.00 19.42           C  
ATOM   1611  OE1 GLU A 194      21.370   8.787  -9.972  1.00 20.75           O  
ATOM   1612  OE2 GLU A 194      21.196  10.916  -9.499  1.00 22.14           O  
ATOM   1613  N   GLY A 195      24.044   5.913 -12.241  1.00 13.49           N  
ATOM   1614  CA  GLY A 195      24.836   4.694 -12.227  1.00 13.46           C  
ATOM   1615  C   GLY A 195      24.416   3.739 -13.316  1.00 12.75           C  
ATOM   1616  O   GLY A 195      24.643   4.005 -14.502  1.00 13.51           O  
ATOM   1617  N   ALA A 196      23.800   2.628 -12.912  1.00 12.39           N  
ATOM   1618  CA  ALA A 196      23.472   1.535 -13.833  1.00 12.25           C  
ATOM   1619  C   ALA A 196      22.291   1.825 -14.774  1.00 12.47           C  
ATOM   1620  O   ALA A 196      22.112   1.114 -15.786  1.00 13.07           O  
ATOM   1621  CB  ALA A 196      23.214   0.248 -13.045  1.00 12.31           C  
ATOM   1622  N   GLY A 197      21.490   2.840 -14.439  1.00 12.27           N  
ATOM   1623  CA  GLY A 197      20.369   3.277 -15.290  1.00 13.15           C  
ATOM   1624  C   GLY A 197      19.218   2.294 -15.342  1.00 12.85           C  
ATOM   1625  O   GLY A 197      18.474   2.237 -16.333  1.00 14.40           O  
ATOM   1626  N   ILE A 198      19.080   1.513 -14.274  1.00 12.86           N  
ATOM   1627  CA  ILE A 198      18.028   0.520 -14.174  1.00 12.95           C  
ATOM   1628  C   ILE A 198      16.739   1.176 -13.714  1.00 13.59           C  
ATOM   1629  O   ILE A 198      15.695   0.976 -14.314  1.00 14.43           O  
ATOM   1630  CB  ILE A 198      18.410  -0.583 -13.178  1.00 12.88           C  
ATOM   1631  CG1 ILE A 198      19.689  -1.293 -13.646  1.00 12.52           C  
ATOM   1632  CG2 ILE A 198      17.259  -1.570 -12.992  1.00 12.13           C  
ATOM   1633  CD1 ILE A 198      20.314  -2.235 -12.599  1.00 13.29           C  
ATOM   1634  N   VAL A 199      16.816   1.959 -12.639  1.00 13.76           N  
ATOM   1635  CA  VAL A 199      15.646   2.677 -12.137  1.00 13.93           C  
ATOM   1636  C   VAL A 199      15.540   3.987 -12.906  1.00 14.43           C  
ATOM   1637  O   VAL A 199      16.508   4.748 -12.964  1.00 13.67           O  
ATOM   1638  CB  VAL A 199      15.762   2.931 -10.617  1.00 14.31           C  
ATOM   1639  CG1 VAL A 199      14.567   3.755 -10.100  1.00 14.82           C  
ATOM   1640  CG2 VAL A 199      15.855   1.594  -9.877  1.00 14.11           C  
ATOM   1641  N   PRO A 200      14.379   4.227 -13.543  1.00 15.11           N  
ATOM   1642  CA  PRO A 200      14.201   5.448 -14.334  1.00 15.37           C  
ATOM   1643  C   PRO A 200      14.197   6.702 -13.478  1.00 15.91           C  
ATOM   1644  O   PRO A 200      13.913   6.644 -12.272  1.00 16.13           O  
ATOM   1645  CB  PRO A 200      12.836   5.251 -15.013  1.00 16.26           C  
ATOM   1646  CG  PRO A 200      12.157   4.224 -14.225  1.00 16.56           C  
ATOM   1647  CD  PRO A 200      13.185   3.359 -13.581  1.00 15.09           C  
ATOM   1648  N   LEU A 201      14.512   7.815 -14.125  1.00 15.92           N  
ATOM   1649  CA  LEU A 201      14.683   9.091 -13.431  1.00 16.14           C  
ATOM   1650  C   LEU A 201      13.433   9.521 -12.657  1.00 16.39           C  
ATOM   1651  O   LEU A 201      13.550  10.103 -11.573  1.00 15.20           O  
ATOM   1652  CB  LEU A 201      15.134  10.165 -14.425  1.00 16.68           C  
ATOM   1653  CG  LEU A 201      15.468  11.556 -13.888  1.00 16.42           C  
ATOM   1654  CD1 LEU A 201      16.525  11.498 -12.784  1.00 16.67           C  
ATOM   1655  CD2 LEU A 201      15.903  12.458 -15.051  1.00 16.79           C  
ATOM   1656  N   ASN A 202      12.239   9.226 -13.173  1.00 16.46           N  
ATOM   1657  CA  ASN A 202      11.031   9.617 -12.448  1.00 16.68           C  
ATOM   1658  C   ASN A 202      10.914   8.906 -11.103  1.00 16.12           C  
ATOM   1659  O   ASN A 202      10.623   9.544 -10.086  1.00 16.31           O  
ATOM   1660  CB  ASN A 202       9.754   9.506 -13.301  1.00 17.77           C  
ATOM   1661  CG  ASN A 202       9.397   8.072 -13.673  1.00 20.32           C  
ATOM   1662  OD1 ASN A 202      10.263   7.222 -13.862  1.00 22.68           O  
ATOM   1663  ND2 ASN A 202       8.094   7.808 -13.800  1.00 25.20           N  
ATOM   1664  N   ILE A 203      11.196   7.598 -11.087  1.00 15.39           N  
ATOM   1665  CA AILE A 203      11.138   6.819  -9.853  0.60 15.17           C  
ATOM   1666  CA BILE A 203      11.134   6.820  -9.851  0.40 15.14           C  
ATOM   1667  C   ILE A 203      12.300   7.193  -8.927  1.00 14.93           C  
ATOM   1668  O   ILE A 203      12.134   7.307  -7.708  1.00 14.71           O  
ATOM   1669  CB AILE A 203      11.122   5.288 -10.136  0.60 15.30           C  
ATOM   1670  CB BILE A 203      11.117   5.291 -10.120  0.40 15.24           C  
ATOM   1671  CG1AILE A 203       9.867   4.904 -10.940  0.60 15.67           C  
ATOM   1672  CG1BILE A 203      10.004   4.929 -11.116  0.40 15.31           C  
ATOM   1673  CG2AILE A 203      11.242   4.490  -8.830  0.60 15.77           C  
ATOM   1674  CG2BILE A 203      10.976   4.516  -8.803  0.40 15.66           C  
ATOM   1675  CD1AILE A 203       8.561   5.354 -10.303  0.60 14.87           C  
ATOM   1676  CD1BILE A 203       9.940   3.459 -11.460  0.40 15.10           C  
ATOM   1677  N   GLU A 204      13.482   7.393  -9.501  1.00 14.52           N  
ATOM   1678  CA  GLU A 204      14.620   7.837  -8.701  1.00 14.13           C  
ATOM   1679  C   GLU A 204      14.316   9.147  -7.975  1.00 13.62           C  
ATOM   1680  O   GLU A 204      14.649   9.327  -6.801  1.00 13.23           O  
ATOM   1681  CB  GLU A 204      15.827   8.037  -9.582  1.00 14.66           C  
ATOM   1682  CG  GLU A 204      17.003   8.563  -8.819  1.00 17.09           C  
ATOM   1683  CD  GLU A 204      18.254   8.443  -9.597  1.00 18.60           C  
ATOM   1684  OE1 GLU A 204      18.190   8.615 -10.831  1.00 21.67           O  
ATOM   1685  OE2 GLU A 204      19.286   8.150  -8.969  1.00 22.04           O  
ATOM   1686  N   THR A 205      13.687  10.071  -8.692  1.00 13.14           N  
ATOM   1687  CA  THR A 205      13.342  11.372  -8.100  1.00 12.44           C  
ATOM   1688  C   THR A 205      12.332  11.194  -6.944  1.00 12.88           C  
ATOM   1689  O   THR A 205      12.443  11.872  -5.917  1.00 12.23           O  
ATOM   1690  CB  THR A 205      12.835  12.347  -9.183  1.00 12.93           C  
ATOM   1691  OG1 THR A 205      13.846  12.466 -10.200  1.00 12.83           O  
ATOM   1692  CG2 THR A 205      12.558  13.723  -8.583  1.00 13.37           C  
ATOM   1693  N   LEU A 206      11.362  10.293  -7.110  1.00 12.83           N  
ATOM   1694  CA  LEU A 206      10.454   9.915  -6.021  1.00 13.47           C  
ATOM   1695  C   LEU A 206      11.240   9.387  -4.814  1.00 12.83           C  
ATOM   1696  O   LEU A 206      10.999   9.796  -3.670  1.00 12.86           O  
ATOM   1697  CB  LEU A 206       9.473   8.846  -6.504  1.00 13.63           C  
ATOM   1698  CG  LEU A 206       8.620   8.113  -5.467  1.00 13.95           C  
ATOM   1699  CD1 LEU A 206       7.753   9.078  -4.659  1.00 15.22           C  
ATOM   1700  CD2 LEU A 206       7.767   7.032  -6.147  1.00 15.18           C  
ATOM   1701  N   LEU A 207      12.171   8.471  -5.061  1.00 12.69           N  
ATOM   1702  CA  LEU A 207      12.952   7.893  -3.969  1.00 11.84           C  
ATOM   1703  C   LEU A 207      13.779   8.945  -3.242  1.00 11.77           C  
ATOM   1704  O   LEU A 207      13.741   9.011  -1.997  1.00 12.07           O  
ATOM   1705  CB  LEU A 207      13.862   6.764  -4.461  1.00 12.13           C  
ATOM   1706  CG  LEU A 207      13.135   5.553  -5.067  1.00 11.86           C  
ATOM   1707  CD1 LEU A 207      14.139   4.573  -5.690  1.00 13.98           C  
ATOM   1708  CD2 LEU A 207      12.265   4.844  -4.025  1.00 15.60           C  
ATOM   1709  N   PHE A 208      14.511   9.781  -3.989  1.00 11.30           N  
ATOM   1710  CA  PHE A 208      15.276  10.850  -3.319  1.00 12.04           C  
ATOM   1711  C   PHE A 208      14.361  11.831  -2.568  1.00 12.41           C  
ATOM   1712  O   PHE A 208      14.757  12.365  -1.538  1.00 12.40           O  
ATOM   1713  CB  PHE A 208      16.160  11.647  -4.285  1.00 12.18           C  
ATOM   1714  CG  PHE A 208      17.450  10.961  -4.676  1.00 11.93           C  
ATOM   1715  CD1 PHE A 208      18.248  10.331  -3.730  1.00 12.20           C  
ATOM   1716  CD2 PHE A 208      17.884  10.991  -6.002  1.00 12.19           C  
ATOM   1717  CE1 PHE A 208      19.452   9.720  -4.093  1.00 12.83           C  
ATOM   1718  CE2 PHE A 208      19.093  10.387  -6.371  1.00 13.98           C  
ATOM   1719  CZ  PHE A 208      19.878   9.758  -5.419  1.00 13.08           C  
ATOM   1720  N   MET A 209      13.163  12.098  -3.090  1.00 12.14           N  
ATOM   1721  CA AMET A 209      12.240  13.006  -2.408  0.50 12.17           C  
ATOM   1722  CA BMET A 209      12.201  12.993  -2.410  0.50 12.57           C  
ATOM   1723  C   MET A 209      11.819  12.423  -1.054  1.00 12.31           C  
ATOM   1724  O   MET A 209      11.847  13.124  -0.038  1.00 12.28           O  
ATOM   1725  CB AMET A 209      11.040  13.334  -3.303  0.50 12.38           C  
ATOM   1726  CB BMET A 209      10.931  13.205  -3.246  0.50 12.42           C  
ATOM   1727  CG AMET A 209      10.114  14.405  -2.741  0.50 12.95           C  
ATOM   1728  CG BMET A 209       9.913  14.166  -2.596  0.50 12.79           C  
ATOM   1729  SD AMET A 209       8.860  13.669  -1.689  0.50 15.71           S  
ATOM   1730  SD BMET A 209       8.229  13.915  -3.192  0.50 14.73           S  
ATOM   1731  CE AMET A 209       7.833  12.829  -2.909  0.50 15.03           C  
ATOM   1732  CE BMET A 209       7.679  12.559  -2.154  0.50 15.65           C  
ATOM   1733  N   VAL A 210      11.463  11.139  -1.032  1.00 12.19           N  
ATOM   1734  CA  VAL A 210      11.079  10.496   0.224  1.00 12.62           C  
ATOM   1735  C   VAL A 210      12.247  10.530   1.195  1.00 11.62           C  
ATOM   1736  O   VAL A 210      12.081  10.881   2.366  1.00 12.52           O  
ATOM   1737  CB  VAL A 210      10.608   9.039  -0.018  1.00 13.42           C  
ATOM   1738  CG1 VAL A 210      10.403   8.296   1.294  1.00 15.38           C  
ATOM   1739  CG2 VAL A 210       9.304   9.049  -0.834  1.00 14.29           C  
ATOM   1740  N   LEU A 211      13.427  10.158   0.711  1.00 11.52           N  
ATOM   1741  CA  LEU A 211      14.623  10.133   1.577  1.00 10.99           C  
ATOM   1742  C   LEU A 211      14.929  11.540   2.098  1.00 11.10           C  
ATOM   1743  O   LEU A 211      15.123  11.720   3.296  1.00 11.08           O  
ATOM   1744  CB  LEU A 211      15.834   9.580   0.820  1.00 11.12           C  
ATOM   1745  CG  LEU A 211      15.756   8.090   0.492  1.00 10.84           C  
ATOM   1746  CD1 LEU A 211      16.895   7.758  -0.475  1.00 12.83           C  
ATOM   1747  CD2 LEU A 211      15.871   7.234   1.757  1.00 12.73           C  
ATOM   1748  N   ASP A 212      14.947  12.520   1.196  1.00 10.92           N  
ATOM   1749  CA  ASP A 212      15.289  13.903   1.547  1.00 10.88           C  
ATOM   1750  C   ASP A 212      14.309  14.468   2.578  1.00 10.58           C  
ATOM   1751  O   ASP A 212      14.718  15.065   3.573  1.00 11.80           O  
ATOM   1752  CB  ASP A 212      15.221  14.803   0.308  1.00 10.89           C  
ATOM   1753  CG  ASP A 212      16.437  14.669  -0.628  1.00 13.28           C  
ATOM   1754  OD1 ASP A 212      17.464  14.040  -0.288  1.00 13.36           O  
ATOM   1755  OD2 ASP A 212      16.365  15.263  -1.724  1.00 13.84           O  
ATOM   1756  N   VAL A 213      13.011  14.322   2.309  1.00 11.11           N  
ATOM   1757  CA  VAL A 213      11.986  14.869   3.219  1.00 11.26           C  
ATOM   1758  C   VAL A 213      12.068  14.191   4.593  1.00 10.87           C  
ATOM   1759  O   VAL A 213      12.024  14.862   5.638  1.00 12.11           O  
ATOM   1760  CB  VAL A 213      10.572  14.773   2.600  1.00 11.23           C  
ATOM   1761  CG1 VAL A 213       9.494  15.158   3.620  1.00 12.43           C  
ATOM   1762  CG2 VAL A 213      10.481  15.638   1.327  1.00 11.84           C  
ATOM   1763  N   SER A 214      12.223  12.872   4.599  1.00 10.68           N  
ATOM   1764  CA  SER A 214      12.394  12.131   5.859  1.00 10.85           C  
ATOM   1765  C   SER A 214      13.644  12.582   6.638  1.00 11.01           C  
ATOM   1766  O   SER A 214      13.589  12.756   7.857  1.00 11.25           O  
ATOM   1767  CB  SER A 214      12.464  10.634   5.566  1.00 11.59           C  
ATOM   1768  OG  SER A 214      11.267  10.202   4.956  1.00 12.82           O  
ATOM   1769  N   ALA A 215      14.749  12.774   5.916  1.00 10.87           N  
ATOM   1770  CA  ALA A 215      16.048  13.090   6.513  1.00 11.54           C  
ATOM   1771  C   ALA A 215      16.164  14.522   7.030  1.00 11.45           C  
ATOM   1772  O   ALA A 215      17.079  14.832   7.806  1.00 12.03           O  
ATOM   1773  CB  ALA A 215      17.178  12.794   5.501  1.00 11.86           C  
ATOM   1774  N   LYS A 216      15.261  15.389   6.569  1.00 11.82           N  
ATOM   1775  CA  LYS A 216      15.287  16.826   6.914  1.00 11.76           C  
ATOM   1776  C   LYS A 216      14.059  17.220   7.743  1.00 12.26           C  
ATOM   1777  O   LYS A 216      14.189  17.694   8.881  1.00 12.73           O  
ATOM   1778  CB  LYS A 216      15.373  17.685   5.635  1.00 12.14           C  
ATOM   1779  CG  LYS A 216      16.611  17.396   4.836  1.00 12.61           C  
ATOM   1780  CD  LYS A 216      16.763  18.336   3.644  1.00 14.51           C  
ATOM   1781  CE  LYS A 216      18.143  18.178   3.024  1.00 15.75           C  
ATOM   1782  NZ  LYS A 216      18.325  16.872   2.325  1.00 17.45           N  
ATOM   1783  N   VAL A 217      12.868  17.016   7.176  1.00 11.82           N  
ATOM   1784  CA  VAL A 217      11.631  17.392   7.872  1.00 11.95           C  
ATOM   1785  C   VAL A 217      11.293  16.360   8.946  1.00 11.79           C  
ATOM   1786  O   VAL A 217      10.928  16.731  10.063  1.00 12.20           O  
ATOM   1787  CB  VAL A 217      10.459  17.647   6.899  1.00 12.00           C  
ATOM   1788  CG1 VAL A 217       9.192  18.098   7.667  1.00 11.95           C  
ATOM   1789  CG2 VAL A 217      10.853  18.729   5.886  1.00 12.86           C  
ATOM   1790  N   GLY A 218      11.409  15.070   8.619  1.00 11.47           N  
ATOM   1791  CA  GLY A 218      11.188  14.014   9.624  1.00 11.43           C  
ATOM   1792  C   GLY A 218      12.158  14.135  10.783  1.00 11.14           C  
ATOM   1793  O   GLY A 218      11.763  14.210  11.947  1.00 12.04           O  
ATOM   1794  N   PHE A 219      13.442  14.179  10.453  1.00 10.63           N  
ATOM   1795  CA  PHE A 219      14.509  14.411  11.436  1.00 10.39           C  
ATOM   1796  C   PHE A 219      14.214  15.656  12.271  1.00 10.45           C  
ATOM   1797  O   PHE A 219      14.259  15.617  13.506  1.00 10.83           O  
ATOM   1798  CB  PHE A 219      15.809  14.587  10.645  1.00 10.51           C  
ATOM   1799  CG  PHE A 219      17.050  14.828  11.464  1.00 10.75           C  
ATOM   1800  CD1 PHE A 219      17.328  16.087  11.988  1.00 10.75           C  
ATOM   1801  CD2 PHE A 219      18.001  13.811  11.621  1.00 11.55           C  
ATOM   1802  CE1 PHE A 219      18.507  16.336  12.721  1.00 10.88           C  
ATOM   1803  CE2 PHE A 219      19.209  14.047  12.318  1.00 10.85           C  
ATOM   1804  CZ  PHE A 219      19.466  15.319  12.876  1.00 10.38           C  
ATOM   1805  N   GLY A 220      13.911  16.766  11.604  1.00 10.10           N  
ATOM   1806  CA  GLY A 220      13.662  18.031  12.302  1.00 11.63           C  
ATOM   1807  C   GLY A 220      12.469  17.959  13.232  1.00 12.20           C  
ATOM   1808  O   GLY A 220      12.497  18.503  14.335  1.00 13.17           O  
ATOM   1809  N   LEU A 221      11.400  17.290  12.802  1.00 12.75           N  
ATOM   1810  CA  LEU A 221      10.225  17.135  13.680  1.00 13.54           C  
ATOM   1811  C   LEU A 221      10.578  16.382  14.955  1.00 13.61           C  
ATOM   1812  O   LEU A 221      10.157  16.767  16.043  1.00 14.66           O  
ATOM   1813  CB  LEU A 221       9.077  16.430  12.954  1.00 13.68           C  
ATOM   1814  CG  LEU A 221       8.332  17.346  11.972  1.00 14.49           C  
ATOM   1815  CD1 LEU A 221       7.535  16.476  11.006  1.00 14.14           C  
ATOM   1816  CD2 LEU A 221       7.441  18.411  12.663  1.00 15.16           C  
ATOM   1817  N   ILE A 222      11.353  15.312  14.815  1.00 13.09           N  
ATOM   1818  CA  ILE A 222      11.779  14.541  15.987  1.00 13.39           C  
ATOM   1819  C   ILE A 222      12.638  15.399  16.925  1.00 13.63           C  
ATOM   1820  O   ILE A 222      12.401  15.456  18.129  1.00 14.11           O  
ATOM   1821  CB  ILE A 222      12.565  13.271  15.579  1.00 13.41           C  
ATOM   1822  CG1 ILE A 222      11.676  12.331  14.760  1.00 13.50           C  
ATOM   1823  CG2 ILE A 222      13.101  12.559  16.833  1.00 14.02           C  
ATOM   1824  CD1 ILE A 222      12.452  11.256  13.957  1.00 13.96           C  
ATOM   1825  N   LEU A 223      13.631  16.071  16.358  1.00 12.95           N  
ATOM   1826  CA  LEU A 223      14.530  16.905  17.143  1.00 12.31           C  
ATOM   1827  C   LEU A 223      13.800  18.050  17.837  1.00 12.53           C  
ATOM   1828  O   LEU A 223      13.954  18.258  19.046  1.00 13.35           O  
ATOM   1829  CB  LEU A 223      15.647  17.469  16.245  1.00 12.24           C  
ATOM   1830  CG  LEU A 223      16.665  18.370  16.962  1.00 11.91           C  
ATOM   1831  CD1 LEU A 223      17.432  17.660  18.101  1.00 13.44           C  
ATOM   1832  CD2 LEU A 223      17.633  18.945  15.933  1.00 12.79           C  
ATOM   1833  N   LEU A 224      13.005  18.785  17.070  1.00 12.75           N  
ATOM   1834  CA  LEU A 224      12.478  20.059  17.567  1.00 13.83           C  
ATOM   1835  C   LEU A 224      11.300  19.899  18.535  1.00 15.92           C  
ATOM   1836  O   LEU A 224      10.956  20.852  19.249  1.00 16.90           O  
ATOM   1837  CB  LEU A 224      12.161  21.010  16.406  1.00 12.93           C  
ATOM   1838  CG  LEU A 224      13.379  21.403  15.550  1.00 11.72           C  
ATOM   1839  CD1 LEU A 224      12.961  22.269  14.369  1.00 13.06           C  
ATOM   1840  CD2 LEU A 224      14.425  22.124  16.387  1.00 11.01           C  
ATOM   1841  N   ARG A 225      10.712  18.700  18.585  1.00 16.61           N  
ATOM   1842  CA AARG A 225       9.645  18.404  19.548  0.50 17.80           C  
ATOM   1843  CA BARG A 225       9.647  18.412  19.555  0.50 17.96           C  
ATOM   1844  C   ARG A 225      10.194  17.843  20.868  1.00 17.92           C  
ATOM   1845  O   ARG A 225       9.439  17.629  21.831  1.00 18.37           O  
ATOM   1846  CB AARG A 225       8.608  17.460  18.922  0.50 17.80           C  
ATOM   1847  CB BARG A 225       8.583  17.485  18.951  0.50 17.98           C  
ATOM   1848  CG AARG A 225       7.828  18.098  17.768  0.50 18.63           C  
ATOM   1849  CG BARG A 225       8.993  16.033  18.773  0.50 19.26           C  
ATOM   1850  CD AARG A 225       6.732  17.195  17.198  0.50 19.63           C  
ATOM   1851  CD BARG A 225       7.790  15.191  18.334  0.50 20.11           C  
ATOM   1852  NE AARG A 225       5.420  17.513  17.767  0.50 24.34           N  
ATOM   1853  NE BARG A 225       8.168  14.004  17.565  0.50 25.25           N  
ATOM   1854  CZ AARG A 225       4.901  16.947  18.854  0.50 25.75           C  
ATOM   1855  CZ BARG A 225       7.777  13.750  16.317  0.50 25.94           C  
ATOM   1856  NH1AARG A 225       5.569  16.010  19.518  0.50 27.35           N  
ATOM   1857  NH1BARG A 225       8.176  12.638  15.714  0.50 27.40           N  
ATOM   1858  NH2AARG A 225       3.703  17.320  19.281  0.50 27.11           N  
ATOM   1859  NH2BARG A 225       6.981  14.595  15.668  0.50 27.41           N  
ATOM   1860  N   SER A 226      11.507  17.612  20.916  1.00 17.36           N  
ATOM   1861  CA ASER A 226      12.154  17.015  22.089  0.70 17.16           C  
ATOM   1862  CA BSER A 226      12.131  17.015  22.097  0.30 17.48           C  
ATOM   1863  C   SER A 226      12.561  18.041  23.143  1.00 17.49           C  
ATOM   1864  O   SER A 226      12.842  19.197  22.823  1.00 17.79           O  
ATOM   1865  CB ASER A 226      13.386  16.205  21.663  0.70 17.09           C  
ATOM   1866  CB BSER A 226      13.327  16.150  21.693  0.30 17.42           C  
ATOM   1867  OG ASER A 226      14.508  17.043  21.417  0.70 14.87           O  
ATOM   1868  OG BSER A 226      13.966  15.605  22.835  0.30 16.98           O  
ATOM   1869  N   ARG A 227      12.611  17.601  24.401  1.00 17.80           N  
ATOM   1870  CA AARG A 227      13.117  18.442  25.480  0.70 18.74           C  
ATOM   1871  CA BARG A 227      13.119  18.427  25.494  0.30 18.06           C  
ATOM   1872  C   ARG A 227      14.641  18.514  25.432  1.00 18.28           C  
ATOM   1873  O   ARG A 227      15.246  19.381  26.057  1.00 18.55           O  
ATOM   1874  CB AARG A 227      12.625  17.935  26.846  0.70 19.47           C  
ATOM   1875  CB BARG A 227      12.696  17.855  26.850  0.30 18.26           C  
ATOM   1876  CG AARG A 227      12.163  16.470  26.862  0.70 22.50           C  
ATOM   1877  CG BARG A 227      11.196  17.870  27.116  0.30 18.01           C  
ATOM   1878  CD AARG A 227      10.955  16.243  25.928  0.70 26.98           C  
ATOM   1879  CD BARG A 227      10.854  17.022  28.338  0.30 20.02           C  
ATOM   1880  NE AARG A 227      10.602  14.835  25.739  0.70 30.04           N  
ATOM   1881  NE BARG A 227      11.065  15.599  28.078  0.30 20.94           N  
ATOM   1882  CZ AARG A 227      11.217  13.990  24.915  0.70 30.62           C  
ATOM   1883  CZ BARG A 227      11.015  14.638  28.997  0.30 21.31           C  
ATOM   1884  NH1AARG A 227      12.254  14.377  24.192  0.70 32.83           N  
ATOM   1885  NH1BARG A 227      10.755  14.924  30.267  0.30 22.45           N  
ATOM   1886  NH2AARG A 227      10.797  12.739  24.824  0.70 32.76           N  
ATOM   1887  NH2BARG A 227      11.227  13.380  28.640  0.30 21.81           N  
ATOM   1888  N   ALA A 228      15.248  17.610  24.662  1.00 18.16           N  
ATOM   1889  CA  ALA A 228      16.713  17.507  24.570  1.00 18.32           C  
ATOM   1890  C   ALA A 228      17.409  18.775  24.086  1.00 18.48           C  
ATOM   1891  O   ALA A 228      18.593  18.982  24.379  1.00 19.33           O  
ATOM   1892  CB  ALA A 228      17.106  16.333  23.679  1.00 18.12           C  
ATOM   1893  N   ILE A 229      16.691  19.611  23.334  1.00 18.61           N  
ATOM   1894  CA  ILE A 229      17.294  20.809  22.754  1.00 18.43           C  
ATOM   1895  C   ILE A 229      17.395  21.988  23.737  1.00 19.18           C  
ATOM   1896  O   ILE A 229      18.069  22.982  23.448  1.00 18.28           O  
ATOM   1897  CB  ILE A 229      16.559  21.255  21.460  1.00 18.01           C  
ATOM   1898  CG1 ILE A 229      15.109  21.639  21.761  1.00 18.27           C  
ATOM   1899  CG2 ILE A 229      16.644  20.168  20.385  1.00 18.35           C  
ATOM   1900  CD1 ILE A 229      14.426  22.379  20.616  1.00 18.03           C  
ATOM   1901  N   PHE A 230      16.747  21.856  24.897  1.00 20.58           N  
ATOM   1902  CA  PHE A 230      16.714  22.933  25.892  1.00 22.47           C  
ATOM   1903  C   PHE A 230      17.877  22.934  26.881  1.00 23.98           C  
ATOM   1904  O   PHE A 230      18.269  21.882  27.377  1.00 25.12           O  
ATOM   1905  CB  PHE A 230      15.372  22.938  26.621  1.00 22.48           C  
ATOM   1906  CG  PHE A 230      14.258  23.481  25.782  1.00 22.21           C  
ATOM   1907  CD1 PHE A 230      13.543  22.646  24.930  1.00 22.72           C  
ATOM   1908  CD2 PHE A 230      13.971  24.837  25.789  1.00 23.68           C  
ATOM   1909  CE1 PHE A 230      12.532  23.151  24.130  1.00 24.45           C  
ATOM   1910  CE2 PHE A 230      12.964  25.353  24.990  1.00 24.87           C  
ATOM   1911  CZ  PHE A 230      12.241  24.512  24.160  1.00 23.97           C  
ATOM   1912  N   GLY A 231      18.417  24.127  27.140  1.00 25.16           N  
ATOM   1913  CA  GLY A 231      19.501  24.306  28.109  1.00 26.52           C  
ATOM   1914  C   GLY A 231      18.971  24.364  29.528  1.00 27.34           C  
TER    1915      GLY A 231                                                      
HETATM 1916  C1  RET A 301      26.245  10.459  -3.065  1.00 15.09           C  
HETATM 1917  C2  RET A 301      26.589   9.853  -4.410  1.00 16.79           C  
HETATM 1918  C3  RET A 301      26.977   8.394  -4.328  1.00 15.38           C  
HETATM 1919  C4  RET A 301      27.740   8.012  -3.047  1.00 13.94           C  
HETATM 1920  C5  RET A 301      27.016   8.505  -1.812  1.00 13.07           C  
HETATM 1921  C6  RET A 301      26.255   9.613  -1.798  1.00 13.29           C  
HETATM 1922  C7  RET A 301      25.606   9.973  -0.491  1.00 13.22           C  
HETATM 1923  C8  RET A 301      24.590  10.820  -0.340  1.00 13.25           C  
HETATM 1924  C9  RET A 301      23.932  11.134   0.940  1.00 12.72           C  
HETATM 1925  C10 RET A 301      23.027  12.129   0.941  1.00 12.83           C  
HETATM 1926  C11 RET A 301      22.248  12.602   2.082  1.00 13.11           C  
HETATM 1927  C12 RET A 301      21.297  13.485   1.804  1.00 14.80           C  
HETATM 1928  C13 RET A 301      20.428  14.121   2.785  1.00 15.77           C  
HETATM 1929  C14 RET A 301      19.720  15.183   2.313  1.00 20.39           C  
HETATM 1930  C15 RET A 301      18.827  16.002   3.100  1.00 20.88           C  
HETATM 1931  C16 RET A 301      26.039  11.991  -2.959  1.00 14.76           C  
HETATM 1932  C17 RET A 301      24.749  10.253  -3.381  1.00 13.98           C  
HETATM 1933  C18 RET A 301      27.182   7.652  -0.584  1.00 16.37           C  
HETATM 1934  C19 RET A 301      24.230  10.318   2.171  1.00 12.70           C  
HETATM 1935  C20 RET A 301      20.386  13.630   4.203  1.00 17.18           C  
HETATM 1936  C1  D12 A 402      41.570   3.068  12.804  1.00 52.90           C  
HETATM 1937  C2  D12 A 402      40.792   3.063  11.505  1.00 53.22           C  
HETATM 1938  C3  D12 A 402      41.262   1.949  10.574  1.00 53.34           C  
HETATM 1939  C4  D12 A 402      40.809   2.208   9.139  1.00 53.51           C  
HETATM 1940  C5  D12 A 402      40.907   0.948   8.281  1.00 53.47           C  
HETATM 1941  C6  D12 A 402      39.544   0.298   8.167  1.00 53.31           C  
HETATM 1942  C7  D12 A 402      39.174  -0.236   7.083  1.00 53.15           C  
HETATM 1943  C8  D12 A 402      38.831  -0.902   6.132  1.00 52.89           C  
HETATM 1944  C9  D12 A 402      38.468  -1.742   5.356  1.00 53.24           C  
HETATM 1945  C10 D12 A 402      38.161  -2.766   4.663  1.00 53.15           C  
HETATM 1946  C11 D12 A 402      38.074  -2.651   3.382  1.00 53.30           C  
HETATM 1947  C12 D12 A 402      37.877  -2.834   2.119  1.00 53.40           C  
HETATM 1948  C1  D12 A 403      34.251  -0.194  -2.536  1.00 37.03           C  
HETATM 1949  C2  D12 A 403      35.292  -0.873  -3.403  1.00 36.63           C  
HETATM 1950  C3  D12 A 403      34.649  -1.696  -4.513  1.00 36.60           C  
HETATM 1951  C4  D12 A 403      35.605  -2.744  -5.066  1.00 37.14           C  
HETATM 1952  C5  D12 A 403      35.177  -3.227  -6.449  1.00 37.09           C  
HETATM 1953  C6  D12 A 403      36.416  -3.481  -7.277  1.00 36.90           C  
HETATM 1954  C7  D12 A 403      36.335  -3.892  -8.485  1.00 36.64           C  
HETATM 1955  C8  D12 A 403      36.525  -4.204  -9.627  1.00 37.58           C  
HETATM 1956  C9  D12 A 403      36.899  -4.385 -10.749  1.00 38.56           C  
HETATM 1957  C10 D12 A 403      37.353  -4.351 -11.937  1.00 39.55           C  
HETATM 1958  C11 D12 A 403      37.452  -5.413 -12.621  1.00 40.12           C  
HETATM 1959  C12 D12 A 403      37.576  -6.370 -13.444  1.00 40.88           C  
HETATM 1960  C1  D12 A 405      11.439  -4.640  -3.682  1.00 43.15           C  
HETATM 1961  C2  D12 A 405      12.541  -4.711  -4.718  1.00 42.97           C  
HETATM 1962  C3  D12 A 405      12.005  -5.012  -6.116  1.00 42.60           C  
HETATM 1963  C4  D12 A 405      12.915  -4.405  -7.187  1.00 42.49           C  
HETATM 1964  C5  D12 A 405      12.744  -5.050  -8.564  1.00 41.27           C  
HETATM 1965  C6  D12 A 405      13.780  -4.466  -9.505  1.00 40.71           C  
HETATM 1966  C7  D12 A 405      13.737  -4.639 -10.770  1.00 41.02           C  
HETATM 1967  C8  D12 A 405      13.926  -4.577 -11.965  1.00 40.88           C  
HETATM 1968  C9  D12 A 405      13.982  -4.772 -13.150  1.00 40.93           C  
HETATM 1969  C10 D12 A 405      13.915  -5.206 -14.353  1.00 41.05           C  
HETATM 1970  C11 D12 A 405      14.249  -4.456 -15.348  1.00 40.93           C  
HETATM 1971  C12 D12 A 405      14.571  -3.876 -16.449  1.00 38.93           C  
HETATM 1972  C1  D10 A 406       3.041  23.442  -5.054  1.00 38.67           C  
HETATM 1973  C2  D10 A 406       4.347  23.472  -5.809  1.00 38.24           C  
HETATM 1974  C3  D10 A 406       4.115  24.174  -7.140  1.00 38.34           C  
HETATM 1975  C4  D10 A 406       4.072  23.187  -8.300  1.00 37.46           C  
HETATM 1976  C5  D10 A 406       2.690  23.135  -8.938  1.00 35.88           C  
HETATM 1977  C6  D10 A 406       2.769  23.172 -10.458  1.00 34.17           C  
HETATM 1978  C7  D10 A 406       1.425  22.798 -11.075  1.00 33.90           C  
HETATM 1979  C8  D10 A 406       1.503  22.830 -12.595  1.00 34.09           C  
HETATM 1980  C9  D10 A 406       0.532  21.826 -13.202  1.00 34.22           C  
HETATM 1981  C10 D10 A 406       0.705  21.778 -14.703  1.00 33.89           C  
HETATM 1982  C1  D10 A 409      41.202   6.796  -2.991  1.00 43.21           C  
HETATM 1983  C2  D10 A 409      41.388   5.535  -3.801  1.00 43.21           C  
HETATM 1984  C3  D10 A 409      41.186   5.838  -5.281  1.00 43.49           C  
HETATM 1985  C4  D10 A 409      41.951   4.851  -6.157  1.00 43.37           C  
HETATM 1986  C5  D10 A 409      41.044   4.221  -7.207  1.00 43.81           C  
HETATM 1987  C6  D10 A 409      41.806   3.918  -8.492  1.00 43.69           C  
HETATM 1988  C7  D10 A 409      40.960   3.101  -9.465  1.00 43.57           C  
HETATM 1989  C8  D10 A 409      41.767   2.721 -10.700  1.00 43.69           C  
HETATM 1990  C9  D10 A 409      40.862   2.332 -11.863  1.00 43.78           C  
HETATM 1991  C10 D10 A 409      41.663   2.279 -13.143  1.00 43.77           C  
HETATM 1992  C27 R16 A 411      38.883  -0.272  15.553  1.00 41.74           C  
HETATM 1993  C28 R16 A 411      38.443  -0.240  14.366  1.00 41.70           C  
HETATM 1994  C29 R16 A 411      37.913  -0.176  13.303  1.00 41.18           C  
HETATM 1995  C30 R16 A 411      37.269  -0.122  12.297  1.00 40.78           C  
HETATM 1996  C31 R16 A 411      36.655  -0.205  11.277  1.00 38.83           C  
HETATM 1997  C32 R16 A 411      36.031  -0.390  10.279  1.00 37.15           C  
HETATM 1998  C33 R16 A 411      35.362  -0.398   9.271  1.00 35.71           C  
HETATM 1999  C34 R16 A 411      34.436  -0.284   8.468  1.00 33.04           C  
HETATM 2000  C35 R16 A 411      33.345   0.045   8.031  1.00 31.51           C  
HETATM 2001  C36 R16 A 411      32.218   0.452   7.938  1.00 29.12           C  
HETATM 2002  C37 R16 A 411      31.112   0.862   8.199  1.00 28.13           C  
HETATM 2003  C38 R16 A 411      29.312   1.465   9.624  1.00 26.21           C  
HETATM 2004  C39 R16 A 411      30.162   1.242   8.827  1.00 27.52           C  
HETATM 2005  C40 R16 A 411      28.418   1.592  10.390  1.00 25.90           C  
HETATM 2006  C41 R16 A 411      27.431   1.699  11.038  1.00 26.47           C  
HETATM 2007  C42 R16 A 411      26.307   1.748  11.603  1.00 27.13           C  
HETATM 2008  C1  CPS A 501       4.398  23.223 -15.080  1.00 45.53           C  
HETATM 2009  C2  CPS A 501       5.907  23.190 -14.800  1.00 45.09           C  
HETATM 2010  C3  CPS A 501       6.158  25.339 -16.241  1.00 43.69           C  
HETATM 2011  C4  CPS A 501       6.966  26.098 -17.306  1.00 43.44           C  
HETATM 2012  C5  CPS A 501       8.476  26.076 -17.027  1.00 43.75           C  
HETATM 2013  C6  CPS A 501       8.914  24.620 -16.879  1.00 43.78           C  
HETATM 2014  C7  CPS A 501      10.442  24.615 -16.968  1.00 43.66           C  
HETATM 2015  C8  CPS A 501      10.746  25.784 -17.906  1.00 44.02           C  
HETATM 2016  C9  CPS A 501       9.411  26.508 -18.172  1.00 44.20           C  
HETATM 2017  C10 CPS A 501       8.762  26.905 -15.760  1.00 43.17           C  
HETATM 2018  C11 CPS A 501       6.124  23.906 -13.463  1.00 44.47           C  
HETATM 2019  C12 CPS A 501       3.901  22.261 -16.164  1.00 45.94           C  
HETATM 2020  C13 CPS A 501       4.387  20.825 -15.988  1.00 45.96           C  
HETATM 2021  C14 CPS A 501       5.902  20.801 -15.813  1.00 45.42           C  
HETATM 2022  C15 CPS A 501       6.399  21.730 -14.691  1.00 45.06           C  
HETATM 2023  C16 CPS A 501       7.928  21.599 -14.585  1.00 44.73           C  
HETATM 2024  C17 CPS A 501       8.724  22.416 -15.611  1.00 44.50           C  
HETATM 2025  C18 CPS A 501       8.219  23.860 -15.736  1.00 44.28           C  
HETATM 2026  C19 CPS A 501       6.683  23.919 -15.931  1.00 44.29           C  
HETATM 2027  C20 CPS A 501       9.554  28.015 -18.463  1.00 44.92           C  
HETATM 2028  C21 CPS A 501       8.272  28.595 -19.058  1.00 44.64           C  
HETATM 2029  C22 CPS A 501      10.766  28.371 -19.338  1.00 45.74           C  
HETATM 2030  C23 CPS A 501      10.546  28.189 -20.843  1.00 46.64           C  
HETATM 2031  C24 CPS A 501      11.875  28.102 -21.559  1.00 46.74           C  
HETATM 2032  O2  CPS A 501       4.043  20.078 -17.163  1.00 46.75           O  
HETATM 2033  O3  CPS A 501       8.703  21.765 -16.893  1.00 44.39           O  
HETATM 2034  O4  CPS A 501       6.679  25.538 -18.595  1.00 42.37           O  
HETATM 2035  C1  D10 A 250      10.571  30.598   3.395  1.00 54.51           C  
HETATM 2036  C2  D10 A 250      11.643  30.157   2.425  1.00 54.81           C  
HETATM 2037  C3  D10 A 250      12.099  31.353   1.594  1.00 54.46           C  
HETATM 2038  C4  D10 A 250      13.397  31.065   0.843  1.00 54.40           C  
HETATM 2039  C5  D10 A 250      13.765  32.228  -0.074  1.00 53.96           C  
HETATM 2040  C6  D10 A 250      14.676  31.794  -1.221  1.00 53.77           C  
HETATM 2041  C7  D10 A 250      13.910  31.675  -2.536  1.00 53.38           C  
HETATM 2042  C8  D10 A 250      14.850  31.430  -3.712  1.00 53.07           C  
HETATM 2043  C9  D10 A 250      14.346  30.289  -4.592  1.00 52.86           C  
HETATM 2044  C10 D10 A 250      15.010  30.352  -5.947  1.00 52.55           C  
HETATM 2045  C1  D12 A 251      -1.525  21.822   3.503  1.00 51.02           C  
HETATM 2046  C2  D12 A 251      -1.707  22.166   2.039  1.00 51.12           C  
HETATM 2047  C3  D12 A 251      -0.468  22.841   1.458  1.00 51.02           C  
HETATM 2048  C4  D12 A 251      -0.445  22.717  -0.061  1.00 50.83           C  
HETATM 2049  C5  D12 A 251       0.977  22.795  -0.614  1.00 51.00           C  
HETATM 2050  C6  D12 A 251       0.932  22.938  -2.121  1.00 50.92           C  
HETATM 2051  C7  D12 A 251       1.021  21.925  -2.871  1.00 51.37           C  
HETATM 2052  C8  D12 A 251       1.215  21.076  -3.702  1.00 51.73           C  
HETATM 2053  C9  D12 A 251       1.552  20.392  -4.629  1.00 51.88           C  
HETATM 2054  C10 D12 A 251       2.115  19.695  -5.523  1.00 51.99           C  
HETATM 2055  C11 D12 A 251       1.489  19.347  -6.560  1.00 52.11           C  
HETATM 2056  C12 D12 A 251       0.952  19.027  -7.660  1.00 51.76           C  
HETATM 2057  C20 HP6 A 401       7.909  -1.872  -4.163  1.00 42.90           C  
HETATM 2058  C21 HP6 A 401       8.582  -1.943  -5.519  1.00 43.62           C  
HETATM 2059  C22 HP6 A 401       7.793  -2.831  -6.476  1.00 43.42           C  
HETATM 2060  C23 HP6 A 401       8.451  -2.890  -7.801  1.00 43.67           C  
HETATM 2061  C24 HP6 A 401       8.845  -3.089  -8.918  1.00 43.63           C  
HETATM 2062  C25 HP6 A 401       9.038  -3.288 -10.080  1.00 42.94           C  
HETATM 2063  C26 HP6 A 401       9.089  -3.535 -11.320  1.00 42.54           C  
HETATM 2064  C1  D12 A 252      38.901  -1.831  -2.492  1.00 54.39           C  
HETATM 2065  C2  D12 A 252      38.960  -3.261  -2.987  1.00 54.23           C  
HETATM 2066  C3  D12 A 252      39.489  -3.339  -4.417  1.00 53.97           C  
HETATM 2067  C4  D12 A 252      39.447  -4.775  -4.928  1.00 54.18           C  
HETATM 2068  C5  D12 A 252      39.775  -4.856  -6.416  1.00 54.12           C  
HETATM 2069  C6  D12 A 252      39.581  -6.277  -6.896  1.00 54.09           C  
HETATM 2070  C7  D12 A 252      40.007  -6.616  -8.031  1.00 54.36           C  
HETATM 2071  C8  D12 A 252      40.483  -6.924  -9.076  1.00 54.76           C  
HETATM 2072  C9  D12 A 252      40.945  -7.002 -10.203  1.00 55.27           C  
HETATM 2073  C10 D12 A 252      41.360  -6.718 -11.384  1.00 55.68           C  
HETATM 2074  C11 D12 A 252      41.509  -7.652 -12.237  1.00 56.00           C  
HETATM 2075  C12 D12 A 252      41.697  -8.408 -13.254  1.00 55.73           C  
HETATM 2076  C1  DD9 A 253      39.750  13.286  -2.526  1.00 41.22           C  
HETATM 2077  C2  DD9 A 253      40.038  11.901  -3.059  1.00 40.71           C  
HETATM 2078  C3  DD9 A 253      40.915  12.007  -4.304  1.00 40.00           C  
HETATM 2079  C4  DD9 A 253      41.135  10.640  -4.941  1.00 39.85           C  
HETATM 2080  C5  DD9 A 253      41.321  10.753  -6.451  1.00 39.24           C  
HETATM 2081  C6  DD9 A 253      41.266   9.383  -7.121  1.00 38.41           C  
HETATM 2082  C7  DD9 A 253      41.043   9.507  -8.622  1.00 38.23           C  
HETATM 2083  C8  DD9 A 253      40.404   8.247  -9.190  1.00 37.86           C  
HETATM 2084  C9  DD9 A 253      40.461   8.245 -10.701  1.00 37.96           C  
HETATM 2085  C1  D12 A 254      12.841   0.109  -6.094  1.00 47.75           C  
HETATM 2086  C2  D12 A 254      12.242   0.480  -7.433  1.00 48.10           C  
HETATM 2087  C3  D12 A 254      12.853  -0.347  -8.558  1.00 48.33           C  
HETATM 2088  C4  D12 A 254      11.906  -0.449  -9.747  1.00 48.80           C  
HETATM 2089  C5  D12 A 254      12.489   0.228 -10.982  1.00 49.72           C  
HETATM 2090  C6  D12 A 254      12.596  -0.786 -12.096  1.00 50.48           C  
HETATM 2091  C7  D12 A 254      12.220  -0.477 -13.256  1.00 51.45           C  
HETATM 2092  C8  D12 A 254      11.851  -0.058 -14.303  1.00 52.31           C  
HETATM 2093  C9  D12 A 254      11.446   0.459 -15.295  1.00 52.83           C  
HETATM 2094  C10 D12 A 254      10.903   1.002 -16.298  1.00 53.04           C  
HETATM 2095  C11 D12 A 254      11.612   1.564 -17.171  1.00 53.20           C  
HETATM 2096  C12 D12 A 254      12.301   2.093 -18.077  1.00 53.05           C  
HETATM 2097  C1  D12 A 255      40.031  16.624   8.304  1.00 54.59           C  
HETATM 2098  C2  D12 A 255      39.692  16.065   6.938  1.00 54.94           C  
HETATM 2099  C3  D12 A 255      38.558  15.048   7.017  1.00 55.22           C  
HETATM 2100  C4  D12 A 255      39.042  13.642   6.672  1.00 55.55           C  
HETATM 2101  C5  D12 A 255      38.530  12.620   7.689  1.00 55.87           C  
HETATM 2102  C6  D12 A 255      39.147  11.261   7.430  1.00 55.96           C  
HETATM 2103  C7  D12 A 255      38.686  10.522   6.508  1.00 56.07           C  
HETATM 2104  C8  D12 A 255      38.181  10.003   5.547  1.00 56.17           C  
HETATM 2105  C9  D12 A 255      37.811   9.727   4.425  1.00 56.13           C  
HETATM 2106  C10 D12 A 255      37.138   9.543   3.360  1.00 55.77           C  
HETATM 2107  C11 D12 A 255      37.493   8.667   2.525  1.00 55.60           C  
HETATM 2108  C12 D12 A 255      37.774   7.856   1.594  1.00 55.28           C  
HETATM 2109  C1  D12 A 256      21.717  32.652  14.561  1.00 53.71           C  
HETATM 2110  C2  D12 A 256      20.459  32.935  13.763  1.00 53.32           C  
HETATM 2111  C3  D12 A 256      20.754  33.112  12.277  1.00 53.35           C  
HETATM 2112  C4  D12 A 256      20.441  31.841  11.490  1.00 53.35           C  
HETATM 2113  C5  D12 A 256      19.208  32.013  10.608  1.00 53.49           C  
HETATM 2114  C6  D12 A 256      18.346  30.766  10.650  1.00 53.36           C  
HETATM 2115  C7  D12 A 256      17.510  30.555   9.717  1.00 52.99           C  
HETATM 2116  C8  D12 A 256      16.645  30.532   8.886  1.00 52.34           C  
HETATM 2117  C9  D12 A 256      15.932  30.433   7.922  1.00 52.13           C  
HETATM 2118  C10 D12 A 256      15.161  30.051   6.972  1.00 51.93           C  
HETATM 2119  C11 D12 A 256      14.266  30.856   6.495  1.00 51.79           C  
HETATM 2120  C12 D12 A 256      13.347  31.399   5.738  1.00 51.95           C  
HETATM 2121  C1  D10 A 257       9.319   4.695  -0.813  1.00 47.88           C  
HETATM 2122  C2  D10 A 257       8.175   4.381  -1.750  1.00 48.16           C  
HETATM 2123  C3  D10 A 257       8.685   4.373  -3.185  1.00 47.92           C  
HETATM 2124  C4  D10 A 257       8.113   3.202  -3.974  1.00 47.85           C  
HETATM 2125  C5  D10 A 257       8.496   3.307  -5.445  1.00 47.83           C  
HETATM 2126  C6  D10 A 257       8.397   1.957  -6.145  1.00 47.95           C  
HETATM 2127  C7  D10 A 257       7.746   2.100  -7.515  1.00 47.96           C  
HETATM 2128  C8  D10 A 257       8.567   1.395  -8.588  1.00 48.48           C  
HETATM 2129  C9  D10 A 257       7.702   0.447  -9.409  1.00 48.72           C  
HETATM 2130  C10 D10 A 257       7.615   0.946 -10.833  1.00 48.90           C  
HETATM 2131  O   HOH A 258      13.941  14.186  -5.655  1.00 14.79           O  
HETATM 2132  O   HOH A 259      19.287  12.804   8.421  1.00 14.79           O  
HETATM 2133  O   HOH A 260      17.811  15.956  -3.931  1.00 16.86           O  
HETATM 2134  O   HOH A 261      11.955   8.880 -16.119  1.00 21.30           O  
HETATM 2135  O   HOH A 262      28.017  12.561  32.659  1.00 18.44           O  
HETATM 2136  O   HOH A 263      17.747   5.663 -15.256  1.00 23.88           O  
HETATM 2137  O   HOH A 264      17.737  18.814  -3.635  1.00 16.59           O  
HETATM 2138  O   HOH A 265      17.244  17.474  -0.159  1.00 19.95           O  
HETATM 2139  O   HOH A 266      23.007   8.727  29.495  1.00 25.79           O  
HETATM 2140  O   HOH A 267      22.235  16.251  34.663  1.00 20.22           O  
HETATM 2141  O   HOH A 268      16.205   6.104  21.846  1.00 22.20           O  
HETATM 2142  O   HOH A 269      31.216   6.100 -21.072  1.00 22.50           O  
HETATM 2143  O   HOH A 270      30.264  16.287 -17.477  1.00 19.61           O  
HETATM 2144  O   HOH A 271      34.887  12.833 -17.395  1.00 24.87           O  
HETATM 2145  O   HOH A 272      29.553  18.798   2.559  1.00 20.73           O  
HETATM 2146  O   HOH A 273      31.242   9.562 -22.905  1.00 23.18           O  
HETATM 2147  O   HOH A 274      19.894  12.675 -12.258  1.00 24.89           O  
HETATM 2148  O   HOH A 275      33.844  13.554  19.993  1.00 23.22           O  
HETATM 2149  O   HOH A 276      14.784   7.647 -16.956  1.00 24.07           O  
HETATM 2150  O   HOH A 277      11.164  13.604  19.758  1.00 24.95           O  
HETATM 2151  O   HOH A 278      29.351  14.120  25.808  1.00 22.52           O  
HETATM 2152  O   HOH A 279      28.651  16.668 -19.778  1.00 24.29           O  
HETATM 2153  O   HOH A 280      11.075  21.083  21.845  1.00 23.21           O  
HETATM 2154  O   HOH A 281      35.000  12.415  13.177  1.00 25.88           O  
HETATM 2155  O   HOH A 282      10.637  23.872  21.207  1.00 27.16           O  
HETATM 2156  O   HOH A 283      18.494  12.414  -9.911  1.00 23.32           O  
HETATM 2157  O   HOH A 284      29.547   7.689 -24.294  1.00 28.60           O  
HETATM 2158  O   HOH A 285      23.186  18.500  24.709  1.00 26.89           O  
HETATM 2159  O   HOH A 286      19.133  22.911 -16.147  1.00 30.45           O  
HETATM 2160  O   HOH A 287       6.489  32.420  16.577  1.00 22.09           O  
HETATM 2161  O   HOH A 288      38.985  18.311  19.496  1.00 28.06           O  
HETATM 2162  O   HOH A 289      12.604  11.426 -16.877  1.00 28.51           O  
HETATM 2163  O   HOH A 290      36.147  12.267 -14.052  1.00 31.33           O  
HETATM 2164  O   HOH A 291      33.853   2.540 -19.163  1.00 24.40           O  
HETATM 2165  O   HOH A 292       7.584  27.801  19.813  1.00 29.98           O  
HETATM 2166  O   HOH A 293      13.184  19.560 -14.088  1.00 24.69           O  
HETATM 2167  O   HOH A 294      29.655   3.414  21.080  1.00 37.26           O  
HETATM 2168  O   HOH A 295      21.047  13.782  -9.307  0.60 19.71           O  
HETATM 2169  O   HOH A 296      11.949  28.996  25.434  1.00 38.15           O  
HETATM 2170  O   HOH A 297      35.531   2.669  17.559  1.00 37.31           O  
HETATM 2171  O   HOH A 298      29.695  19.778  20.143  1.00 37.03           O  
HETATM 2172  O   HOH A 299      22.664   5.589 -16.014  1.00 28.54           O  
HETATM 2173  O   HOH A 300      33.390   9.390  24.453  1.00 39.27           O  
HETATM 2174  O   HOH A 302      16.191  19.692   9.314  1.00 27.43           O  
HETATM 2175  O   HOH A 303      21.304  31.065  20.635  1.00 34.97           O  
HETATM 2176  O   HOH A 304       6.528   8.826 -11.378  1.00 30.07           O  
HETATM 2177  O   HOH A 305      18.867   2.681 -18.977  1.00 48.64           O  
HETATM 2178  O   HOH A 306      31.678  19.886   3.986  1.00 27.88           O  
HETATM 2179  O   HOH A 307      23.007  22.890 -15.883  1.00 33.61           O  
HETATM 2180  O   HOH A 308      18.892   6.891  27.227  1.00 29.70           O  
HETATM 2181  O   HOH A 309      13.755  32.619  18.970  1.00 29.61           O  
HETATM 2182  O   HOH A 310      31.294  10.133  26.924  1.00 37.69           O  
HETATM 2183  O   HOH A 311      32.921  11.179  19.017  1.00 41.90           O  
HETATM 2184  O   HOH A 312      20.663   9.461 -16.630  1.00 36.31           O  
HETATM 2185  O   HOH A 313      19.024   1.275  18.298  1.00 31.96           O  
HETATM 2186  O   HOH A 314      37.788  10.234 -13.452  1.00 37.22           O  
HETATM 2187  O   HOH A 315      19.319  19.386  26.965  1.00 44.82           O  
HETATM 2188  O   HOH A 316      18.762   1.900   4.435  1.00 31.57           O  
HETATM 2189  O   HOH A 317       5.378  15.094 -17.698  1.00 41.69           O  
HETATM 2190  O   HOH A 318      19.933  27.668  27.112  1.00 45.03           O  
HETATM 2191  O   HOH A 319      33.697   9.176  21.639  1.00 35.19           O  
HETATM 2192  O   HOH A 320      13.108   9.614  22.563  1.00 40.51           O  
HETATM 2193  O   HOH A 321      21.266   0.241 -18.224  1.00 41.96           O  
HETATM 2194  O   HOH A 322      27.488   1.987  19.777  1.00 42.55           O  
HETATM 2195  O   HOH A 323      37.909   9.502  13.425  1.00 39.87           O  
HETATM 2196  O   HOH A 324      35.996  20.224  21.639  1.00 33.10           O  
HETATM 2197  O   HOH A 325      32.050  15.196 -24.393  1.00 40.91           O  
HETATM 2198  O   HOH A 326      12.349  35.540  18.120  1.00 39.16           O  
HETATM 2199  O   HOH A 327      23.415   2.390  21.028  1.00 40.53           O  
HETATM 2200  O   HOH A 328      25.415   6.107  30.316  1.00 42.32           O  
HETATM 2201  O   HOH A 329      10.032  19.470 -16.412  1.00 42.14           O  
HETATM 2202  O   HOH A 330      13.981  11.251  24.840  1.00 42.15           O  
HETATM 2203  O   HOH A 331      22.169   5.185 -18.474  1.00 33.03           O  
HETATM 2204  O   HOH A 332      34.314   6.866  16.268  1.00 28.50           O  
HETATM 2205  O   HOH A 333      37.025  13.330  24.297  1.00 51.60           O  
HETATM 2206  O   HOH A 334      37.625   1.625 -19.057  1.00 49.92           O  
HETATM 2207  O   HOH A 335      34.800   9.575  17.170  1.00 36.17           O  
HETATM 2208  O   HOH A 336      34.846   5.175  18.238  1.00 36.13           O  
HETATM 2209  O   HOH A 337       8.025  22.346  17.829  1.00 50.95           O  
HETATM 2210  O   HOH A 338      10.707  20.008 -13.913  1.00 30.29           O  
HETATM 2211  O   HOH A 339      27.519  19.147 -18.502  1.00 35.70           O  
HETATM 2212  O   HOH A 340      22.374  18.355  27.593  1.00 34.46           O  
HETATM 2213  O   HOH A 341      17.762   8.318 -16.497  1.00 36.39           O  
HETATM 2214  O   HOH A 342      36.249  10.965  15.031  1.00 34.00           O  
HETATM 2215  O   HOH A 343       8.657  19.618  15.635  1.00 34.33           O  
HETATM 2216  O   HOH A 344      25.522   2.058  23.164  1.00 45.82           O  
HETATM 2217  O   HOH A 345      26.455  25.627  21.809  1.00 54.17           O  
HETATM 2218  O   HOH A 346      16.744   4.832  24.078  1.00 40.11           O  
HETATM 2219  O   HOH A 347       6.003  10.505 -13.358  1.00 44.56           O  
HETATM 2220  O   HOH A 348      28.926  21.610  21.793  1.00 32.63           O  
HETATM 2221  O   HOH A 349      16.750   0.221 -18.140  1.00 43.98           O  
HETATM 2222  O   HOH A 350      10.149   7.408 -17.326  1.00 39.88           O  
HETATM 2223  O   HOH A 351       6.614  26.484 -21.192  1.00 38.19           O  
HETATM 2224  O   HOH A 352      21.253  19.889  24.161  1.00 46.59           O  
HETATM 2225  O   HOH A 353      16.258   9.454 -18.229  1.00 39.98           O  
HETATM 2226  O   HOH A 354      22.744  22.105  24.135  1.00 43.82           O  
HETATM 2227  O   HOH A 355      34.006   8.396 -22.599  1.00 41.76           O  
HETATM 2228  O   HOH A 356      21.327  20.647  28.308  1.00 53.86           O  
HETATM 2229  O   HOH A 357      20.828   2.004  22.946  1.00 59.36           O  
HETATM 2230  O   HOH A 358      13.328  11.624  20.669  1.00 49.86           O  
HETATM 2231  O   HOH A 359      26.481  21.128  22.669  1.00 42.86           O  
HETATM 2232  O   HOH A 360      35.740  16.062 -20.776  1.00 37.32           O  
HETATM 2233  O   HOH A 361       9.435  32.050  24.509  1.00 48.88           O  
HETATM 2234  O   HOH A 362       9.556  11.852  18.124  1.00 49.37           O  
HETATM 2235  O   HOH A 363      13.474   6.361  22.244  1.00 44.19           O  
HETATM 2236  O   HOH A 364      16.484  15.703  33.597  1.00 51.40           O  
HETATM 2237  O   HOH A 365      33.015  16.442  24.633  1.00 52.36           O  
HETATM 2238  O   HOH A 366      14.553   5.447 -18.371  1.00 35.65           O  
HETATM 2239  O   HOH A 367      11.512   5.353  19.801  1.00 57.19           O  
HETATM 2240  O   HOH A 368      10.630   9.443  18.719  1.00 58.02           O  
HETATM 2241  O   HOH A 369      16.296   4.471  19.661  1.00 32.97           O  
HETATM 2242  O   HOH A 370       8.235  12.308  12.959  1.00 45.78           O  
HETATM 2243  O   HOH A 371      15.483  20.940 -13.797  1.00 37.57           O  
HETATM 2244  O   HOH A 372      24.125   4.643 -20.508  1.00 58.44           O  
HETATM 2245  O   HOH A 373       9.236   5.201 -16.011  1.00 51.94           O  
HETATM 2246  O   HOH A 374      14.949  -0.633 -16.287  1.00 50.24           O  
HETATM 2247  O   HOH A 375      11.090   4.907 -18.052  1.00 46.84           O  
HETATM 2248  O   HOH A 376      14.533  11.423 -18.771  1.00 45.39           O  
HETATM 2249  O   HOH A 377      23.126  19.754 -21.098  1.00 45.32           O  
HETATM 2250  O   HOH A 378      19.332   7.786 -20.650  1.00 53.15           O  
HETATM 2251  O   HOH A 379      16.136  13.148 -21.204  1.00 53.07           O  
HETATM 2252  O   HOH A 380      21.270  25.125 -14.718  1.00 36.90           O  
HETATM 2253  O   HOH A 381      18.861  31.529 -16.925  1.00 35.28           O  
HETATM 2254  O   HOH A 382      22.477   7.594  32.008  0.50 36.54           O  
HETATM 2255  O   HOH A 383      33.149   4.595 -21.335  1.00 41.53           O  
HETATM 2256  O   HOH A 384      31.872  11.672 -24.707  1.00 40.59           O  
HETATM 2257  O   HOH A 385      25.225   0.973  19.945  1.00 51.53           O  
HETATM 2258  O   HOH A 386      21.545   6.788  28.427  1.00 42.61           O  
HETATM 2259  O   HOH A 387       0.742  22.931  14.948  1.00 59.63           O  
HETATM 2260  O   HOH A 388      37.799  14.417 -12.723  1.00 46.35           O  
HETATM 2261  O   HOH A 389      30.961   4.024 -22.812  1.00 68.55           O  
HETATM 2262  O   HOH A 390      30.250  10.540  32.425  1.00 48.05           O  
HETATM 2263  O   HOH A 391       8.817  24.931  22.837  1.00 46.01           O  
HETATM 2264  O   HOH A 392      36.168  10.839 -17.669  1.00 48.70           O  
HETATM 2265  O   HOH A 393      24.446  23.804  22.404  1.00 53.83           O  
HETATM 2266  O   HOH A 394      30.834   1.721 -21.383  1.00 52.50           O  
HETATM 2267  O   HOH A 395       5.183  28.589  18.648  1.00 47.47           O  
HETATM 2268  O   HOH A 396       9.603  14.095  21.984  1.00 45.04           O  
HETATM 2269  O   HOH A 397      28.899   3.080  23.460  1.00 52.73           O  
HETATM 2270  O   HOH A 398      35.750  10.329 -22.286  1.00 48.86           O  
HETATM 2271  O   HOH A 399      38.189  16.456 -11.046  1.00 47.76           O  
HETATM 2272  O   HOH A 400      21.418  27.147 -16.545  1.00 54.02           O  
HETATM 2273  O   HOH A 404      19.564  32.398 -14.516  1.00 57.73           O  
HETATM 2274  O   HOH A 407       7.378  25.183  20.389  1.00 48.22           O  
HETATM 2275  O   HOH A 408      14.580   8.999  28.149  1.00 55.79           O  
HETATM 2276  O   HOH A 410      -0.605  22.817  12.640  1.00 71.40           O  
HETATM 2277  O   HOH A 412       1.093  25.382  15.439  1.00 48.02           O  
HETATM 2278  O   HOH A 413      27.435   9.955 -26.701  1.00 57.65           O  
HETATM 2279  O   HOH A 414      22.662  13.238  -9.534  0.40 13.91           O  
HETATM 2280  O   HOH A 415       1.854  17.092 -17.317  1.00 38.95           O  
HETATM 2281  O   HOH A 416      39.443  13.337  14.747  1.00 55.77           O  
HETATM 2282  O   HOH A 417       3.031  28.146  17.397  1.00 49.42           O  
HETATM 2283  O   HOH A 418      15.165   2.537 -16.654  1.00 44.71           O  
HETATM 2284  O   HOH A 419      16.911   4.089 -17.449  1.00 41.50           O  
CONECT 1782 1930                                                                
CONECT 1916 1917 1921 1931 1932                                                 
CONECT 1917 1916 1918                                                           
CONECT 1918 1917 1919                                                           
CONECT 1919 1918 1920                                                           
CONECT 1920 1919 1921 1933                                                      
CONECT 1921 1916 1920 1922                                                      
CONECT 1922 1921 1923                                                           
CONECT 1923 1922 1924                                                           
CONECT 1924 1923 1925 1934                                                      
CONECT 1925 1924 1926                                                           
CONECT 1926 1925 1927                                                           
CONECT 1927 1926 1928                                                           
CONECT 1928 1927 1929 1935                                                      
CONECT 1929 1928 1930                                                           
CONECT 1930 1782 1929                                                           
CONECT 1931 1916                                                                
CONECT 1932 1916                                                                
CONECT 1933 1920                                                                
CONECT 1934 1924                                                                
CONECT 1935 1928                                                                
CONECT 1936 1937                                                                
CONECT 1937 1936 1938                                                           
CONECT 1938 1937 1939                                                           
CONECT 1939 1938 1940                                                           
CONECT 1940 1939 1941                                                           
CONECT 1941 1940 1942                                                           
CONECT 1942 1941 1943                                                           
CONECT 1943 1942 1944                                                           
CONECT 1944 1943 1945                                                           
CONECT 1945 1944 1946                                                           
CONECT 1946 1945 1947                                                           
CONECT 1947 1946                                                                
CONECT 1948 1949                                                                
CONECT 1949 1948 1950                                                           
CONECT 1950 1949 1951                                                           
CONECT 1951 1950 1952                                                           
CONECT 1952 1951 1953                                                           
CONECT 1953 1952 1954                                                           
CONECT 1954 1953 1955                                                           
CONECT 1955 1954 1956                                                           
CONECT 1956 1955 1957                                                           
CONECT 1957 1956 1958                                                           
CONECT 1958 1957 1959                                                           
CONECT 1959 1958                                                                
CONECT 1960 1961                                                                
CONECT 1961 1960 1962                                                           
CONECT 1962 1961 1963                                                           
CONECT 1963 1962 1964                                                           
CONECT 1964 1963 1965                                                           
CONECT 1965 1964 1966                                                           
CONECT 1966 1965 1967                                                           
CONECT 1967 1966 1968                                                           
CONECT 1968 1967 1969                                                           
CONECT 1969 1968 1970                                                           
CONECT 1970 1969 1971                                                           
CONECT 1971 1970                                                                
CONECT 1972 1973                                                                
CONECT 1973 1972 1974                                                           
CONECT 1974 1973 1975                                                           
CONECT 1975 1974 1976                                                           
CONECT 1976 1975 1977                                                           
CONECT 1977 1976 1978                                                           
CONECT 1978 1977 1979                                                           
CONECT 1979 1978 1980                                                           
CONECT 1980 1979 1981                                                           
CONECT 1981 1980                                                                
CONECT 1982 1983                                                                
CONECT 1983 1982 1984                                                           
CONECT 1984 1983 1985                                                           
CONECT 1985 1984 1986                                                           
CONECT 1986 1985 1987                                                           
CONECT 1987 1986 1988                                                           
CONECT 1988 1987 1989                                                           
CONECT 1989 1988 1990                                                           
CONECT 1990 1989 1991                                                           
CONECT 1991 1990                                                                
CONECT 1992 1993                                                                
CONECT 1993 1992 1994                                                           
CONECT 1994 1993 1995                                                           
CONECT 1995 1994 1996                                                           
CONECT 1996 1995 1997                                                           
CONECT 1997 1996 1998                                                           
CONECT 1998 1997 1999                                                           
CONECT 1999 1998 2000                                                           
CONECT 2000 1999 2001                                                           
CONECT 2001 2000 2002                                                           
CONECT 2002 2001 2003                                                           
CONECT 2003 2002 2004                                                           
CONECT 2004 2003 2005                                                           
CONECT 2005 2004 2006                                                           
CONECT 2006 2005 2007                                                           
CONECT 2007 2006                                                                
CONECT 2008 2009 2019                                                           
CONECT 2009 2008 2018 2022 2026                                                 
CONECT 2010 2011 2026                                                           
CONECT 2011 2010 2012 2034                                                      
CONECT 2012 2011 2013 2016 2017                                                 
CONECT 2013 2012 2014 2025                                                      
CONECT 2014 2013 2015                                                           
CONECT 2015 2014 2016                                                           
CONECT 2016 2012 2015 2027                                                      
CONECT 2017 2012                                                                
CONECT 2018 2009                                                                
CONECT 2019 2008 2020                                                           
CONECT 2020 2019 2021 2032                                                      
CONECT 2021 2020 2022                                                           
CONECT 2022 2009 2021 2023                                                      
CONECT 2023 2022 2024                                                           
CONECT 2024 2023 2025 2033                                                      
CONECT 2025 2013 2024 2026                                                      
CONECT 2026 2009 2010 2025                                                      
CONECT 2027 2016 2028 2029                                                      
CONECT 2028 2027                                                                
CONECT 2029 2027 2030                                                           
CONECT 2030 2029 2031                                                           
CONECT 2031 2030                                                                
CONECT 2032 2020                                                                
CONECT 2033 2024                                                                
CONECT 2034 2011                                                                
CONECT 2035 2036                                                                
CONECT 2036 2035 2037                                                           
CONECT 2037 2036 2038                                                           
CONECT 2038 2037 2039                                                           
CONECT 2039 2038 2040                                                           
CONECT 2040 2039 2041                                                           
CONECT 2041 2040 2042                                                           
CONECT 2042 2041 2043                                                           
CONECT 2043 2042 2044                                                           
CONECT 2044 2043                                                                
CONECT 2045 2046                                                                
CONECT 2046 2045 2047                                                           
CONECT 2047 2046 2048                                                           
CONECT 2048 2047 2049                                                           
CONECT 2049 2048 2050                                                           
CONECT 2050 2049 2051                                                           
CONECT 2051 2050 2052                                                           
CONECT 2052 2051 2053                                                           
CONECT 2053 2052 2054                                                           
CONECT 2054 2053 2055                                                           
CONECT 2055 2054 2056                                                           
CONECT 2056 2055                                                                
CONECT 2057 2058                                                                
CONECT 2058 2057 2059                                                           
CONECT 2059 2058 2060                                                           
CONECT 2060 2059 2061                                                           
CONECT 2061 2060 2062                                                           
CONECT 2062 2061 2063                                                           
CONECT 2063 2062                                                                
CONECT 2064 2065                                                                
CONECT 2065 2064 2066                                                           
CONECT 2066 2065 2067                                                           
CONECT 2067 2066 2068                                                           
CONECT 2068 2067 2069                                                           
CONECT 2069 2068 2070                                                           
CONECT 2070 2069 2071                                                           
CONECT 2071 2070 2072                                                           
CONECT 2072 2071 2073                                                           
CONECT 2073 2072 2074                                                           
CONECT 2074 2073 2075                                                           
CONECT 2075 2074                                                                
CONECT 2076 2077                                                                
CONECT 2077 2076 2078                                                           
CONECT 2078 2077 2079                                                           
CONECT 2079 2078 2080                                                           
CONECT 2080 2079 2081                                                           
CONECT 2081 2080 2082                                                           
CONECT 2082 2081 2083                                                           
CONECT 2083 2082 2084                                                           
CONECT 2084 2083                                                                
CONECT 2085 2086                                                                
CONECT 2086 2085 2087                                                           
CONECT 2087 2086 2088                                                           
CONECT 2088 2087 2089                                                           
CONECT 2089 2088 2090                                                           
CONECT 2090 2089 2091                                                           
CONECT 2091 2090 2092                                                           
CONECT 2092 2091 2093                                                           
CONECT 2093 2092 2094                                                           
CONECT 2094 2093 2095                                                           
CONECT 2095 2094 2096                                                           
CONECT 2096 2095                                                                
CONECT 2097 2098                                                                
CONECT 2098 2097 2099                                                           
CONECT 2099 2098 2100                                                           
CONECT 2100 2099 2101                                                           
CONECT 2101 2100 2102                                                           
CONECT 2102 2101 2103                                                           
CONECT 2103 2102 2104                                                           
CONECT 2104 2103 2105                                                           
CONECT 2105 2104 2106                                                           
CONECT 2106 2105 2107                                                           
CONECT 2107 2106 2108                                                           
CONECT 2108 2107                                                                
CONECT 2109 2110                                                                
CONECT 2110 2109 2111                                                           
CONECT 2111 2110 2112                                                           
CONECT 2112 2111 2113                                                           
CONECT 2113 2112 2114                                                           
CONECT 2114 2113 2115                                                           
CONECT 2115 2114 2116                                                           
CONECT 2116 2115 2117                                                           
CONECT 2117 2116 2118                                                           
CONECT 2118 2117 2119                                                           
CONECT 2119 2118 2120                                                           
CONECT 2120 2119                                                                
CONECT 2121 2122                                                                
CONECT 2122 2121 2123                                                           
CONECT 2123 2122 2124                                                           
CONECT 2124 2123 2125                                                           
CONECT 2125 2124 2126                                                           
CONECT 2126 2125 2127                                                           
CONECT 2127 2126 2128                                                           
CONECT 2128 2127 2129                                                           
CONECT 2129 2128 2130                                                           
CONECT 2130 2129                                                                
MASTER      390    0   17    9    2    0   18    6 2114    1  216   20          
END                                                                             



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