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***  OXYGEN TRANSPORT 18-OCT-13 4N8T  ***

elNémo ID: 20102801013327754

Job options:

ID        	=	 20102801013327754
JOBID     	=	 OXYGEN TRANSPORT 18-OCT-13 4N8T
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    OXYGEN TRANSPORT                        18-OCT-13   4N8T              
TITLE     HUMAN HEMOGLOBIN NITRIC OXIDE ADDUCT                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: HEMOGLOBIN SUBUNIT ALPHA;                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 SYNONYM: ALPHA-GLOBIN, HEMOGLOBIN ALPHA CHAIN;                       
COMPND   5 MOL_ID: 2;                                                           
COMPND   6 MOLECULE: HEMOGLOBIN SUBUNIT BETA;                                   
COMPND   7 CHAIN: B;                                                            
COMPND   8 SYNONYM: BETA-GLOBIN, HEMOGLOBIN BETA CHAIN, LVV-HEMORPHIN-7,        
COMPND   9 SPINORPHIN                                                           
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   3 ORGANISM_COMMON: HUMAN;                                              
SOURCE   4 ORGANISM_TAXID: 9606;                                                
SOURCE   5 OTHER_DETAILS: BLOOD;                                                
SOURCE   6 MOL_ID: 2;                                                           
SOURCE   7 ORGANISM_SCIENTIFIC: HOMO SAPIENS;                                   
SOURCE   8 ORGANISM_COMMON: HUMAN;                                              
SOURCE   9 ORGANISM_TAXID: 9606;                                                
SOURCE  10 OTHER_DETAILS: BLOOD                                                 
KEYWDS    HUMAN HEMOGLOBIN, NITRIC OXIDE, OXYGEN TRANSPORT                      
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    J.YI,G.B.RICHTER-ADDO                                                 
REVDAT   1   08-OCT-14 4N8T    0                                                
JRNL        AUTH   J.YI,A.S.SOARES,G.B.RICHTER-ADDO                             
JRNL        TITL   CRYSTALLOGRAPHIC CHARACTERIZATION OF THE NITRIC OXIDE        
JRNL        TITL 2 DERIVATIVE OF R-STATE HUMAN HEMOGLOBIN.                      
JRNL        REF    NITRIC OXIDE                  V.  39    46 2014              
JRNL        REFN                   ISSN 1089-8603                               
JRNL        PMID   24769418                                                     
JRNL        DOI    10.1016/J.NIOX.2014.04.001                                   
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.90 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.7.0032                                      
REMARK   3   AUTHORS     : MURSHUDOV,VAGIN,DODSON                               
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.90                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.48                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 2.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 21891                          
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) : 0.203                           
REMARK   3   R VALUE            (WORKING SET) : 0.203                           
REMARK   3   FREE R VALUE                     : 0.252                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.100                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1185                            
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) : 1.90                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.95                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1561                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.00                       
REMARK   3   BIN R VALUE           (WORKING SET) : 0.2490                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 79                           
REMARK   3   BIN FREE R VALUE                    : 0.3380                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 2180                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 114                                     
REMARK   3   SOLVENT ATOMS            : 114                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : 32.70                          
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 34.78                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.02000                                              
REMARK   3    B22 (A**2) : 0.02000                                              
REMARK   3    B33 (A**2) : -0.04000                                             
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): 0.174         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.162         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.115         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 3.851         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.956                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.929                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  2373 ; 0.019 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  3250 ; 1.876 ; 2.006       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   286 ; 5.756 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    90 ;35.593 ;24.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   351 ;14.976 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     5 ;15.329 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   354 ; 0.147 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1809 ; 0.011 ; 0.021       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1146 ; 3.153 ; 3.267       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1427 ; 3.933 ; 4.872       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  1227 ; 4.037 ; 3.572       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  3811 ; 6.636 ;28.571       
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 USED IF PRESENT IN    
REMARK   3  THE INPUT                                                           
REMARK   4                                                                      
REMARK   4 4N8T COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 24-OCT-13.                  
REMARK 100 THE RCSB ID CODE IS RCSB082896.                                      
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 19-MAR-08                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 6.8                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : NSLS                               
REMARK 200  BEAMLINE                       : X29A                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.0809                             
REMARK 200  MONOCHROMATOR                  : ROSENBAUM-ROCK DOUBLE CRYSTAL      
REMARK 200                                   SAGITTAL FOCUSING MONOCHROMATOR    
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : CCD                                
REMARK 200  DETECTOR MANUFACTURER          : ADSC QUANTUM 315                   
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : D*TREK                             
REMARK 200  DATA SCALING SOFTWARE          : D*TREK                             
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 23142                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.900                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 24.500                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : 2.000                              
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 12.100                             
REMARK 200  R MERGE                    (I) : 0.07100                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 17.9000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.90                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.95                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
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: PHASER                                                
REMARK 200 STARTING MODEL: PDB ENTRY 1IRD                                       
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.70                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.22                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: SOLDIUM PHOSPHATE, POTASSIUM             
REMARK 280  PHOSPHATE, TOLUENE, HUMAN HEMOGLOBIN, PH 6.8, LIQUID DIFFUSION,     
REMARK 280  TEMPERATURE 295K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 41 21 2                        
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   -Y+1/2,X+1/2,Z+1/4                                      
REMARK 290       4555   Y+1/2,-X+1/2,Z+3/4                                      
REMARK 290       5555   -X+1/2,Y+1/2,-Z+1/4                                     
REMARK 290       6555   X+1/2,-Y+1/2,-Z+3/4                                     
REMARK 290       7555   Y,X,-Z                                                  
REMARK 290       8555   -Y,-X,-Z+1/2                                            
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       96.24950            
REMARK 290   SMTRY1   3  0.000000 -1.000000  0.000000       26.78350            
REMARK 290   SMTRY2   3  1.000000  0.000000  0.000000       26.78350            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       48.12475            
REMARK 290   SMTRY1   4  0.000000  1.000000  0.000000       26.78350            
REMARK 290   SMTRY2   4 -1.000000  0.000000  0.000000       26.78350            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000      144.37425            
REMARK 290   SMTRY1   5 -1.000000  0.000000  0.000000       26.78350            
REMARK 290   SMTRY2   5  0.000000  1.000000  0.000000       26.78350            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       48.12475            
REMARK 290   SMTRY1   6  1.000000  0.000000  0.000000       26.78350            
REMARK 290   SMTRY2   6  0.000000 -1.000000  0.000000       26.78350            
REMARK 290   SMTRY3   6  0.000000  0.000000 -1.000000      144.37425            
REMARK 290   SMTRY1   7  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   7  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000       96.24950            
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: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 6490 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 25110 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -31.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ARG A   141                                                      
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASP A  75       36.01   -144.95                                   
REMARK 500    TYR B  35       72.71   -119.30                                   
REMARK 500    CYS B  93      -73.94    -81.18                                   
REMARK 500    LYS B 120      -39.95    -33.06                                   
REMARK 500    LYS B 144       -5.60    -59.60                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM A 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1  NO A 206   N                                                      
REMARK 620 2 HEM A 201   NA   89.5                                              
REMARK 620 3 HEM A 201   NB   92.7  90.5                                        
REMARK 620 4 HEM A 201   NC   89.5 178.9  89.4                                  
REMARK 620 5 HEM A 201   ND   86.5  89.0 179.1  91.1                            
REMARK 620 6 HIS A  87   NE2 175.8  86.3  87.3  94.8  93.4                      
REMARK 620 7  NO A 206   O    16.5 103.0  83.2  75.9  96.1 166.7                
REMARK 620 N                    1     2     3     4     5     6                 
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                             HEM B 201  FE                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 HIS B  92   NE2                                                    
REMARK 620 2 HEM B 201   NA   88.9                                              
REMARK 620 3 HEM B 201   NB   89.4  88.3                                        
REMARK 620 4 HEM B 201   NC   92.7 178.0  90.6                                  
REMARK 620 5 HEM B 201   ND   92.3  91.0 178.2  90.1                            
REMARK 620 6  NO B 202   N   173.9  87.9  95.7  90.6  82.6                      
REMARK 620 N                    1     2     3     4     5                       
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM A 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBN A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBN A 203                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE MBN A 204                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO2 A 205                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO A 206                  
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC7                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE HEM B 201                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC8                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE NO B 202                  
DBREF  4N8T A    1   141  UNP    P69905   HBA_HUMAN        2    142             
DBREF  4N8T B    1   146  UNP    P68871   HBB_HUMAN        2    147             
SEQRES   1 A  141  VAL LEU SER PRO ALA ASP LYS THR ASN VAL LYS ALA ALA          
SEQRES   2 A  141  TRP GLY LYS VAL GLY ALA HIS ALA GLY GLU TYR GLY ALA          
SEQRES   3 A  141  GLU ALA LEU GLU ARG MET PHE LEU SER PHE PRO THR THR          
SEQRES   4 A  141  LYS THR TYR PHE PRO HIS PHE ASP LEU SER HIS GLY SER          
SEQRES   5 A  141  ALA GLN VAL LYS GLY HIS GLY LYS LYS VAL ALA ASP ALA          
SEQRES   6 A  141  LEU THR ASN ALA VAL ALA HIS VAL ASP ASP MET PRO ASN          
SEQRES   7 A  141  ALA LEU SER ALA LEU SER ASP LEU HIS ALA HIS LYS LEU          
SEQRES   8 A  141  ARG VAL ASP PRO VAL ASN PHE LYS LEU LEU SER HIS CYS          
SEQRES   9 A  141  LEU LEU VAL THR LEU ALA ALA HIS LEU PRO ALA GLU PHE          
SEQRES  10 A  141  THR PRO ALA VAL HIS ALA SER LEU ASP LYS PHE LEU ALA          
SEQRES  11 A  141  SER VAL SER THR VAL LEU THR SER LYS TYR ARG                  
SEQRES   1 B  146  VAL HIS LEU THR PRO GLU GLU LYS SER ALA VAL THR ALA          
SEQRES   2 B  146  LEU TRP GLY LYS VAL ASN VAL ASP GLU VAL GLY GLY GLU          
SEQRES   3 B  146  ALA LEU GLY ARG LEU LEU VAL VAL TYR PRO TRP THR GLN          
SEQRES   4 B  146  ARG PHE PHE GLU SER PHE GLY ASP LEU SER THR PRO ASP          
SEQRES   5 B  146  ALA VAL MET GLY ASN PRO LYS VAL LYS ALA HIS GLY LYS          
SEQRES   6 B  146  LYS VAL LEU GLY ALA PHE SER ASP GLY LEU ALA HIS LEU          
SEQRES   7 B  146  ASP ASN LEU LYS GLY THR PHE ALA THR LEU SER GLU LEU          
SEQRES   8 B  146  HIS CYS ASP LYS LEU HIS VAL ASP PRO GLU ASN PHE ARG          
SEQRES   9 B  146  LEU LEU GLY ASN VAL LEU VAL CYS VAL LEU ALA HIS HIS          
SEQRES  10 B  146  PHE GLY LYS GLU PHE THR PRO PRO VAL GLN ALA ALA TYR          
SEQRES  11 B  146  GLN LYS VAL VAL ALA GLY VAL ALA ASN ALA LEU ALA HIS          
SEQRES  12 B  146  LYS TYR HIS                                                  
HET    HEM  A 201      43                                                       
HET    MBN  A 202       7                                                       
HET    MBN  A 203       7                                                       
HET    MBN  A 204       7                                                       
HET    NO2  A 205       3                                                       
HET     NO  A 206       2                                                       
HET    HEM  B 201      43                                                       
HET     NO  B 202       2                                                       
HETNAM     HEM PROTOPORPHYRIN IX CONTAINING FE                                  
HETNAM     MBN TOLUENE                                                          
HETNAM     NO2 NITRITE ION                                                      
HETNAM      NO NITRIC OXIDE                                                     
HETSYN     HEM HEME                                                             
HETSYN      NO NITROGEN MONOXIDE                                                
FORMUL   3  HEM    2(C34 H32 FE N4 O4)                                          
FORMUL   4  MBN    3(C7 H8)                                                     
FORMUL   7  NO2    N O2 1-                                                      
FORMUL   8   NO    2(N O)                                                       
FORMUL  11  HOH   *114(H2 O)                                                    
HELIX    1   1 SER A    3  GLY A   18  1                                  16    
HELIX    2   2 HIS A   20  PHE A   36  1                                  17    
HELIX    3   3 PRO A   37  PHE A   43  5                                   7    
HELIX    4   4 SER A   52  HIS A   72  1                                  21    
HELIX    5   5 ASP A   75  LEU A   80  1                                   6    
HELIX    6   6 LEU A   80  LYS A   90  1                                  11    
HELIX    7   7 PRO A   95  LEU A  113  1                                  19    
HELIX    8   8 THR A  118  THR A  137  1                                  20    
HELIX    9   9 THR B    4  LYS B   17  1                                  14    
HELIX   10  10 GLU B   22  TYR B   35  1                                  14    
HELIX   11  11 PRO B   36  GLY B   46  5                                  11    
HELIX   12  12 THR B   50  ASN B   57  1                                   8    
HELIX   13  13 ASN B   57  HIS B   77  1                                  21    
HELIX   14  14 ASN B   80  ASP B   94  1                                  15    
HELIX   15  15 PRO B  100  GLY B  119  1                                  20    
HELIX   16  16 LYS B  120  PHE B  122  5                                   3    
HELIX   17  17 THR B  123  ALA B  142  1                                  20    
HELIX   18  18 HIS B  143  HIS B  146  5                                   4    
LINK        FE   HEM A 201                 N    NO A 206     1555   1555  1.78  
LINK         NE2 HIS A  87                FE   HEM A 201     1555   1555  1.96  
LINK         NE2 HIS B  92                FE   HEM B 201     1555   1555  1.99  
LINK        FE   HEM B 201                 N    NO B 202     1555   1555  2.13  
LINK        FE   HEM A 201                 O    NO A 206     1555   1555  2.78  
SITE     1 AC1 15 TYR A  42  PHE A  43  HIS A  45  PHE A  46                    
SITE     2 AC1 15 HIS A  58  LYS A  61  ALA A  65  HIS A  87                    
SITE     3 AC1 15 LEU A  91  VAL A  93  ASN A  97  PHE A  98                    
SITE     4 AC1 15 LEU A 101  LEU A 136   NO A 206                               
SITE     1 AC2  6 TRP A  14  LEU A  66  THR A  67  VAL A  70                    
SITE     2 AC2  6 LEU A 125  MBN A 204                                          
SITE     1 AC3  1 HIS A  50                                                     
SITE     1 AC4  6 ALA A  21  TYR A  24  LEU A  66  LEU A 105                    
SITE     2 AC4  6 LEU A 109  MBN A 202                                          
SITE     1 AC5  3 LYS A  99  HOH A 315  HOH A 331                               
SITE     1 AC6  3 HIS A  58  VAL A  62  HEM A 201                               
SITE     1 AC7 17 PRO A   4  THR B  38  PHE B  41  PHE B  42                    
SITE     2 AC7 17 HIS B  63  LYS B  66  LEU B  88  LEU B  91                    
SITE     3 AC7 17 HIS B  92  LEU B  96  VAL B  98  ASN B 102                    
SITE     4 AC7 17 PHE B 103  LEU B 106  LEU B 141   NO B 202                    
SITE     5 AC7 17 HOH B 337                                                     
SITE     1 AC8  3 HIS B  63  VAL B  67  HEM B 201                               
CRYST1   53.567   53.567  192.499  90.00  90.00  90.00 P 41 21 2     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      0.018668  0.000000  0.000000        0.00000                         
SCALE2      0.000000  0.018668  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.005195        0.00000                         
ATOM      1  N   VAL A   1       8.227  19.068   1.222  1.00 59.17           N  
ATOM      2  CA  VAL A   1       8.675  20.293   1.937  1.00 55.12           C  
ATOM      3  C   VAL A   1       7.757  20.596   3.144  1.00 57.64           C  
ATOM      4  O   VAL A   1       6.526  20.521   3.027  1.00 64.38           O  
ATOM      5  CB  VAL A   1       8.739  21.489   0.953  1.00 65.94           C  
ATOM      6  CG1 VAL A   1       9.867  21.301  -0.075  1.00 58.27           C  
ATOM      7  CG2 VAL A   1       7.379  21.716   0.257  1.00 68.11           C  
ATOM      8  N   LEU A   2       8.340  20.896   4.307  1.00 48.90           N  
ATOM      9  CA  LEU A   2       7.555  21.347   5.451  1.00 36.37           C  
ATOM     10  C   LEU A   2       7.467  22.864   5.376  1.00 39.33           C  
ATOM     11  O   LEU A   2       8.492  23.562   5.360  1.00 40.94           O  
ATOM     12  CB  LEU A   2       8.208  20.953   6.786  1.00 35.80           C  
ATOM     13  CG  LEU A   2       8.283  19.434   7.048  1.00 39.37           C  
ATOM     14  CD1 LEU A   2       8.989  19.088   8.347  1.00 40.33           C  
ATOM     15  CD2 LEU A   2       6.909  18.807   6.984  1.00 28.54           C  
ATOM     16  N   SER A   3       6.250  23.387   5.406  1.00 38.28           N  
ATOM     17  CA  SER A   3       6.040  24.838   5.393  1.00 32.64           C  
ATOM     18  C   SER A   3       6.345  25.478   6.750  1.00 37.67           C  
ATOM     19  O   SER A   3       6.433  24.790   7.787  1.00 31.30           O  
ATOM     20  CB  SER A   3       4.620  25.144   4.944  1.00 32.46           C  
ATOM     21  OG  SER A   3       3.631  24.727   5.904  1.00 34.86           O  
ATOM     22  N   PRO A   4       6.520  26.816   6.763  1.00 35.95           N  
ATOM     23  CA  PRO A   4       6.567  27.519   8.036  1.00 31.61           C  
ATOM     24  C   PRO A   4       5.368  27.189   8.951  1.00 29.86           C  
ATOM     25  O   PRO A   4       5.583  26.952  10.158  1.00 31.76           O  
ATOM     26  CB  PRO A   4       6.568  29.008   7.634  1.00 33.05           C  
ATOM     27  CG  PRO A   4       7.236  28.998   6.287  1.00 36.87           C  
ATOM     28  CD  PRO A   4       6.827  27.699   5.612  1.00 38.50           C  
ATOM     29  N   ALA A   5       4.159  27.157   8.399  1.00 29.62           N  
ATOM     30  CA  ALA A   5       2.989  26.879   9.228  1.00 34.21           C  
ATOM     31  C   ALA A   5       3.199  25.454   9.861  1.00 31.75           C  
ATOM     32  O   ALA A   5       3.098  25.296  11.073  1.00 31.72           O  
ATOM     33  CB  ALA A   5       1.700  26.946   8.424  1.00 31.79           C  
ATOM     34  N   ASP A   6       3.530  24.467   9.044  1.00 31.92           N  
ATOM     35  CA  ASP A   6       3.829  23.107   9.579  1.00 34.96           C  
ATOM     36  C   ASP A   6       4.937  23.080  10.652  1.00 33.09           C  
ATOM     37  O   ASP A   6       4.786  22.395  11.679  1.00 33.44           O  
ATOM     38  CB  ASP A   6       4.307  22.159   8.472  1.00 32.58           C  
ATOM     39  CG  ASP A   6       3.305  21.946   7.420  1.00 33.51           C  
ATOM     40  OD1 ASP A   6       2.093  21.844   7.709  1.00 29.15           O  
ATOM     41  OD2 ASP A   6       3.764  21.909   6.250  1.00 37.20           O  
ATOM     42  N   LYS A   7       6.077  23.764  10.403  1.00 30.63           N  
ATOM     43  CA  LYS A   7       7.153  23.815  11.409  1.00 31.65           C  
ATOM     44  C   LYS A   7       6.621  24.408  12.721  1.00 33.73           C  
ATOM     45  O   LYS A   7       6.917  23.907  13.802  1.00 32.34           O  
ATOM     46  CB  LYS A   7       8.381  24.601  10.928  1.00 35.72           C  
ATOM     47  CG  LYS A   7       9.015  23.983   9.709  1.00 42.61           C  
ATOM     48  CD  LYS A   7      10.224  24.775   9.242  1.00 45.53           C  
ATOM     49  CE  LYS A   7      10.619  24.258   7.867  1.00 52.90           C  
ATOM     50  NZ  LYS A   7      11.499  25.232   7.172  1.00 57.08           N  
ATOM     51  N   THR A   8       5.870  25.495  12.615  1.00 35.61           N  
ATOM     52  CA  THR A   8       5.213  26.087  13.785  1.00 39.53           C  
ATOM     53  C   THR A   8       4.255  25.112  14.504  1.00 38.96           C  
ATOM     54  O   THR A   8       4.301  24.984  15.737  1.00 33.88           O  
ATOM     55  CB  THR A   8       4.522  27.397  13.363  1.00 45.55           C  
ATOM     56  OG1 THR A   8       5.545  28.357  13.088  1.00 44.66           O  
ATOM     57  CG2 THR A   8       3.612  27.930  14.423  1.00 44.39           C  
ATOM     58  N   ASN A   9       3.405  24.428  13.731  1.00 38.30           N  
ATOM     59  CA  ASN A   9       2.427  23.478  14.299  1.00 31.47           C  
ATOM     60  C   ASN A   9       3.114  22.288  15.029  1.00 31.56           C  
ATOM     61  O   ASN A   9       2.650  21.851  16.074  1.00 30.77           O  
ATOM     62  CB  ASN A   9       1.515  22.941  13.215  1.00 30.33           C  
ATOM     63  CG  ASN A   9       0.434  23.937  12.778  1.00 39.20           C  
ATOM     64  OD1 ASN A   9       0.084  24.842  13.531  1.00 34.16           O  
ATOM     65  ND2 ASN A   9      -0.134  23.737  11.563  1.00 27.51           N  
ATOM     66  N   VAL A  10       4.204  21.757  14.469  1.00 30.06           N  
ATOM     67  CA  VAL A  10       4.879  20.586  15.035  1.00 27.29           C  
ATOM     68  C   VAL A  10       5.613  21.050  16.321  1.00 34.29           C  
ATOM     69  O   VAL A  10       5.541  20.375  17.334  1.00 26.86           O  
ATOM     70  CB  VAL A  10       5.866  20.054  13.997  1.00 27.19           C  
ATOM     71  CG1 VAL A  10       6.924  19.110  14.575  1.00 24.39           C  
ATOM     72  CG2 VAL A  10       5.109  19.496  12.765  1.00 23.65           C  
ATOM     73  N   LYS A  11       6.274  22.234  16.268  1.00 32.02           N  
ATOM     74  CA  LYS A  11       6.949  22.824  17.428  1.00 42.65           C  
ATOM     75  C   LYS A  11       5.979  23.049  18.562  1.00 40.94           C  
ATOM     76  O   LYS A  11       6.282  22.693  19.721  1.00 44.99           O  
ATOM     77  CB  LYS A  11       7.750  24.109  17.060  1.00 42.78           C  
ATOM     78  CG  LYS A  11       9.125  23.801  16.440  1.00 57.56           C  
ATOM     79  CD  LYS A  11       9.860  25.037  15.871  1.00 62.16           C  
ATOM     80  CE  LYS A  11      10.776  24.702  14.675  1.00 62.02           C  
ATOM     81  NZ  LYS A  11      11.847  23.649  14.888  1.00 46.13           N  
ATOM     82  N   ALA A  12       4.786  23.543  18.226  1.00 40.24           N  
ATOM     83  CA  ALA A  12       3.652  23.648  19.157  1.00 36.62           C  
ATOM     84  C   ALA A  12       3.296  22.384  19.914  1.00 42.11           C  
ATOM     85  O   ALA A  12       3.236  22.374  21.142  1.00 38.29           O  
ATOM     86  CB  ALA A  12       2.400  24.093  18.409  1.00 40.28           C  
ATOM     87  N   ALA A  13       3.014  21.317  19.165  1.00 38.30           N  
ATOM     88  CA  ALA A  13       2.556  20.067  19.740  1.00 34.60           C  
ATOM     89  C   ALA A  13       3.674  19.434  20.593  1.00 31.50           C  
ATOM     90  O   ALA A  13       3.412  18.895  21.668  1.00 26.26           O  
ATOM     91  CB  ALA A  13       2.102  19.136  18.601  1.00 34.53           C  
ATOM     92  N   TRP A  14       4.919  19.511  20.100  1.00 33.76           N  
ATOM     93  CA  TRP A  14       6.143  19.080  20.855  1.00 31.91           C  
ATOM     94  C   TRP A  14       6.154  19.744  22.215  1.00 35.74           C  
ATOM     95  O   TRP A  14       6.364  19.094  23.251  1.00 34.34           O  
ATOM     96  CB  TRP A  14       7.477  19.466  20.074  0.50 26.54           C  
ATOM     97  CG  TRP A  14       8.673  19.533  21.000  0.50 25.77           C  
ATOM     98  CD1 TRP A  14       9.392  18.488  21.486  0.50 24.48           C  
ATOM     99  CD2 TRP A  14       9.171  20.709  21.670  0.50 25.96           C  
ATOM    100  NE1 TRP A  14      10.330  18.938  22.397  0.50 24.92           N  
ATOM    101  CE2 TRP A  14      10.203  20.299  22.524  0.50 25.31           C  
ATOM    102  CE3 TRP A  14       8.826  22.063  21.630  0.50 23.41           C  
ATOM    103  CZ2 TRP A  14      10.915  21.199  23.327  0.50 23.33           C  
ATOM    104  CZ3 TRP A  14       9.545  22.979  22.460  0.50 25.32           C  
ATOM    105  CH2 TRP A  14      10.564  22.527  23.276  0.50 24.00           C  
ATOM    106  N   GLY A  15       5.941  21.054  22.208  1.00 31.50           N  
ATOM    107  CA  GLY A  15       5.862  21.814  23.440  1.00 35.84           C  
ATOM    108  C   GLY A  15       4.832  21.396  24.446  1.00 34.65           C  
ATOM    109  O   GLY A  15       5.171  21.308  25.604  1.00 40.56           O  
ATOM    110  N   LYS A  16       3.580  21.179  24.030  1.00 34.54           N  
ATOM    111  CA  LYS A  16       2.548  20.591  24.899  1.00 39.76           C  
ATOM    112  C   LYS A  16       2.844  19.172  25.407  1.00 44.58           C  
ATOM    113  O   LYS A  16       2.505  18.821  26.551  1.00 41.63           O  
ATOM    114  CB  LYS A  16       1.193  20.562  24.193  1.00 40.15           C  
ATOM    115  CG  LYS A  16       0.764  21.944  23.695  1.00 57.32           C  
ATOM    116  CD  LYS A  16       1.046  23.042  24.717  1.00 59.56           C  
ATOM    117  CE  LYS A  16       0.094  24.217  24.587  1.00 65.72           C  
ATOM    118  NZ  LYS A  16       0.388  25.191  25.680  1.00 73.65           N  
ATOM    119  N   VAL A  17       3.404  18.323  24.539  1.00 42.19           N  
ATOM    120  CA  VAL A  17       3.839  16.970  24.960  1.00 38.02           C  
ATOM    121  C   VAL A  17       4.807  17.095  26.126  1.00 33.49           C  
ATOM    122  O   VAL A  17       4.822  16.262  27.067  1.00 33.05           O  
ATOM    123  CB  VAL A  17       4.502  16.226  23.767  1.00 38.62           C  
ATOM    124  CG1 VAL A  17       5.305  15.029  24.228  1.00 34.38           C  
ATOM    125  CG2 VAL A  17       3.410  15.815  22.794  1.00 34.83           C  
ATOM    126  N   GLY A  18       5.653  18.132  26.067  1.00 40.00           N  
ATOM    127  CA  GLY A  18       6.678  18.349  27.101  1.00 35.27           C  
ATOM    128  C   GLY A  18       7.408  17.074  27.483  1.00 39.81           C  
ATOM    129  O   GLY A  18       7.706  16.240  26.594  1.00 39.09           O  
ATOM    130  N   ALA A  19       7.671  16.895  28.784  1.00 30.21           N  
ATOM    131  CA  ALA A  19       8.357  15.729  29.275  1.00 34.59           C  
ATOM    132  C   ALA A  19       7.602  14.387  29.266  1.00 34.51           C  
ATOM    133  O   ALA A  19       8.149  13.394  29.716  1.00 35.63           O  
ATOM    134  CB  ALA A  19       8.959  15.993  30.652  1.00 34.06           C  
ATOM    135  N   HIS A  20       6.375  14.338  28.759  1.00 31.12           N  
ATOM    136  CA  HIS A  20       5.723  13.043  28.573  1.00 31.50           C  
ATOM    137  C   HIS A  20       6.239  12.330  27.273  1.00 36.88           C  
ATOM    138  O   HIS A  20       5.873  11.198  27.000  1.00 29.08           O  
ATOM    139  CB  HIS A  20       4.223  13.231  28.456  1.00 32.23           C  
ATOM    140  CG  HIS A  20       3.605  13.804  29.690  1.00 44.00           C  
ATOM    141  ND1 HIS A  20       3.382  13.052  30.826  1.00 44.24           N  
ATOM    142  CD2 HIS A  20       3.190  15.062  29.978  1.00 44.95           C  
ATOM    143  CE1 HIS A  20       2.850  13.825  31.758  1.00 44.36           C  
ATOM    144  NE2 HIS A  20       2.723  15.047  31.268  1.00 48.33           N  
ATOM    145  N   ALA A  21       7.069  13.004  26.468  1.00 34.13           N  
ATOM    146  CA  ALA A  21       7.422  12.424  25.174  1.00 34.33           C  
ATOM    147  C   ALA A  21       7.999  10.930  25.204  1.00 28.67           C  
ATOM    148  O   ALA A  21       7.557  10.105  24.405  1.00 30.79           O  
ATOM    149  CB  ALA A  21       8.318  13.385  24.402  1.00 38.07           C  
ATOM    150  N   GLY A  22       8.899  10.571  26.110  1.00 31.10           N  
ATOM    151  CA  GLY A  22       9.320   9.135  26.187  1.00 32.05           C  
ATOM    152  C   GLY A  22       8.196   8.137  26.494  1.00 29.37           C  
ATOM    153  O   GLY A  22       8.073   7.052  25.878  1.00 32.41           O  
ATOM    154  N   GLU A  23       7.395   8.467  27.514  1.00 30.85           N  
ATOM    155  CA  GLU A  23       6.146   7.722  27.849  1.00 28.05           C  
ATOM    156  C   GLU A  23       5.252   7.612  26.601  1.00 27.40           C  
ATOM    157  O   GLU A  23       4.631   6.574  26.357  1.00 27.20           O  
ATOM    158  CB  GLU A  23       5.362   8.469  28.964  1.00 32.06           C  
ATOM    159  CG  GLU A  23       4.017   7.841  29.429  1.00 36.21           C  
ATOM    160  CD  GLU A  23       3.032   8.833  30.073  0.50 38.24           C  
ATOM    161  OE1 GLU A  23       3.534   9.753  30.751  0.50 34.23           O  
ATOM    162  OE2 GLU A  23       1.764   8.711  29.901  0.50 34.15           O  
ATOM    163  N   TYR A  24       5.086   8.684  25.848  1.00 23.04           N  
ATOM    164  CA  TYR A  24       4.137   8.615  24.707  1.00 21.88           C  
ATOM    165  C   TYR A  24       4.770   7.757  23.582  1.00 22.98           C  
ATOM    166  O   TYR A  24       4.049   7.088  22.836  1.00 23.79           O  
ATOM    167  CB  TYR A  24       3.842  10.009  24.145  1.00 27.41           C  
ATOM    168  CG  TYR A  24       2.975  10.890  25.029  1.00 29.55           C  
ATOM    169  CD1 TYR A  24       2.664  12.197  24.645  1.00 32.27           C  
ATOM    170  CD2 TYR A  24       2.498  10.415  26.274  1.00 29.99           C  
ATOM    171  CE1 TYR A  24       1.873  13.017  25.452  1.00 33.11           C  
ATOM    172  CE2 TYR A  24       1.719  11.217  27.086  1.00 32.19           C  
ATOM    173  CZ  TYR A  24       1.408  12.519  26.694  1.00 35.33           C  
ATOM    174  OH  TYR A  24       0.565  13.266  27.551  1.00 29.19           O  
ATOM    175  N   GLY A  25       6.090   7.804  23.522  1.00 21.53           N  
ATOM    176  CA  GLY A  25       6.865   7.006  22.543  1.00 25.77           C  
ATOM    177  C   GLY A  25       6.661   5.526  22.868  1.00 25.05           C  
ATOM    178  O   GLY A  25       6.407   4.728  21.974  1.00 21.53           O  
ATOM    179  N   ALA A  26       6.704   5.175  24.157  1.00 22.48           N  
ATOM    180  CA  ALA A  26       6.454   3.784  24.586  1.00 22.61           C  
ATOM    181  C   ALA A  26       5.022   3.353  24.286  1.00 23.96           C  
ATOM    182  O   ALA A  26       4.713   2.247  23.822  1.00 24.88           O  
ATOM    183  CB  ALA A  26       6.804   3.682  26.114  1.00 22.58           C  
ATOM    184  N   GLU A  27       4.081   4.257  24.511  1.00 22.97           N  
ATOM    185  CA  GLU A  27       2.715   3.954  24.218  1.00 19.73           C  
ATOM    186  C   GLU A  27       2.459   3.757  22.700  1.00 20.29           C  
ATOM    187  O   GLU A  27       1.624   2.894  22.289  1.00 20.31           O  
ATOM    188  CB  GLU A  27       1.867   5.133  24.709  1.00 23.14           C  
ATOM    189  CG  GLU A  27       0.381   4.945  24.362  1.00 25.42           C  
ATOM    190  CD  GLU A  27      -0.541   6.040  24.899  1.00 26.61           C  
ATOM    191  OE1 GLU A  27      -0.171   6.726  25.854  1.00 32.58           O  
ATOM    192  OE2 GLU A  27      -1.641   6.237  24.363  1.00 28.43           O  
ATOM    193  N   ALA A  28       3.091   4.606  21.894  1.00 20.00           N  
ATOM    194  CA  ALA A  28       2.961   4.424  20.426  1.00 20.19           C  
ATOM    195  C   ALA A  28       3.517   3.028  20.035  1.00 20.81           C  
ATOM    196  O   ALA A  28       2.896   2.297  19.277  1.00 20.87           O  
ATOM    197  CB  ALA A  28       3.692   5.552  19.718  1.00 19.25           C  
ATOM    198  N   LEU A  29       4.667   2.659  20.539  1.00 21.45           N  
ATOM    199  CA  LEU A  29       5.231   1.308  20.224  1.00 22.87           C  
ATOM    200  C   LEU A  29       4.248   0.208  20.627  1.00 22.84           C  
ATOM    201  O   LEU A  29       3.972  -0.707  19.845  1.00 23.78           O  
ATOM    202  CB  LEU A  29       6.587   1.084  20.905  1.00 23.49           C  
ATOM    203  CG  LEU A  29       7.748   1.881  20.396  1.00 23.82           C  
ATOM    204  CD1 LEU A  29       8.905   1.846  21.421  1.00 19.55           C  
ATOM    205  CD2 LEU A  29       8.143   1.415  18.968  1.00 21.19           C  
ATOM    206  N   GLU A  30       3.635   0.297  21.810  1.00 25.06           N  
ATOM    207  CA  GLU A  30       2.662  -0.792  22.198  1.00 25.37           C  
ATOM    208  C   GLU A  30       1.449  -0.805  21.303  1.00 25.37           C  
ATOM    209  O   GLU A  30       0.873  -1.900  20.973  1.00 23.37           O  
ATOM    210  CB  GLU A  30       2.247  -0.721  23.708  1.00 27.91           C  
ATOM    211  CG  GLU A  30       1.099  -1.624  24.123  1.00 26.24           C  
ATOM    212  CD  GLU A  30       0.847  -1.567  25.651  1.00 36.20           C  
ATOM    213  OE1 GLU A  30       0.359  -0.553  26.199  1.00 34.73           O  
ATOM    214  OE2 GLU A  30       1.146  -2.551  26.319  1.00 41.10           O  
ATOM    215  N   ARG A  31       0.961   0.401  20.943  1.00 22.01           N  
ATOM    216  CA  ARG A  31      -0.161   0.516  20.029  1.00 20.30           C  
ATOM    217  C   ARG A  31       0.173  -0.184  18.700  1.00 22.40           C  
ATOM    218  O   ARG A  31      -0.684  -0.953  18.161  1.00 25.65           O  
ATOM    219  CB  ARG A  31      -0.536   2.024  19.748  1.00 19.94           C  
ATOM    220  CG  ARG A  31      -1.379   2.629  20.892  1.00 23.75           C  
ATOM    221  CD  ARG A  31      -1.576   4.162  20.606  1.00 22.75           C  
ATOM    222  NE  ARG A  31      -2.217   4.681  21.786  1.00 23.36           N  
ATOM    223  CZ  ARG A  31      -3.484   4.414  22.113  1.00 24.14           C  
ATOM    224  NH1 ARG A  31      -4.299   3.753  21.268  1.00 23.47           N  
ATOM    225  NH2 ARG A  31      -3.944   4.872  23.293  1.00 27.23           N  
ATOM    226  N   MET A  32       1.397   0.036  18.237  1.00 19.77           N  
ATOM    227  CA  MET A  32       1.849  -0.621  16.978  1.00 20.44           C  
ATOM    228  C   MET A  32       1.937  -2.176  17.085  1.00 20.64           C  
ATOM    229  O   MET A  32       1.553  -2.874  16.151  1.00 21.36           O  
ATOM    230  CB  MET A  32       3.202  -0.058  16.545  1.00 17.50           C  
ATOM    231  CG  MET A  32       3.690  -0.690  15.178  1.00 18.85           C  
ATOM    232  SD  MET A  32       5.378  -0.124  14.775  1.00 23.72           S  
ATOM    233  CE  MET A  32       6.461  -0.962  15.902  1.00 21.92           C  
ATOM    234  N   PHE A  33       2.537  -2.672  18.174  1.00 21.76           N  
ATOM    235  CA  PHE A  33       2.694  -4.115  18.353  1.00 24.22           C  
ATOM    236  C   PHE A  33       1.362  -4.825  18.472  1.00 23.35           C  
ATOM    237  O   PHE A  33       1.203  -5.918  17.935  1.00 26.46           O  
ATOM    238  CB  PHE A  33       3.507  -4.372  19.598  1.00 24.06           C  
ATOM    239  CG  PHE A  33       4.922  -3.884  19.514  1.00 25.41           C  
ATOM    240  CD1 PHE A  33       5.666  -4.012  18.341  1.00 24.59           C  
ATOM    241  CD2 PHE A  33       5.517  -3.290  20.637  1.00 22.95           C  
ATOM    242  CE1 PHE A  33       7.008  -3.621  18.282  1.00 24.45           C  
ATOM    243  CE2 PHE A  33       6.841  -2.845  20.556  1.00 23.34           C  
ATOM    244  CZ  PHE A  33       7.596  -3.031  19.397  1.00 25.58           C  
ATOM    245  N   LEU A  34       0.400  -4.226  19.186  1.00 22.81           N  
ATOM    246  CA  LEU A  34      -0.966  -4.766  19.294  1.00 23.18           C  
ATOM    247  C   LEU A  34      -1.755  -4.668  18.033  1.00 25.24           C  
ATOM    248  O   LEU A  34      -2.543  -5.606  17.685  1.00 23.16           O  
ATOM    249  CB  LEU A  34      -1.712  -4.103  20.494  1.00 21.59           C  
ATOM    250  CG  LEU A  34      -1.278  -4.368  21.955  1.00 27.34           C  
ATOM    251  CD1 LEU A  34      -2.306  -3.766  22.963  1.00 27.14           C  
ATOM    252  CD2 LEU A  34      -1.064  -5.880  22.223  1.00 29.31           C  
ATOM    253  N   SER A  35      -1.645  -3.509  17.334  1.00 20.85           N  
ATOM    254  CA  SER A  35      -2.456  -3.276  16.148  1.00 22.37           C  
ATOM    255  C   SER A  35      -1.933  -3.971  14.887  1.00 24.61           C  
ATOM    256  O   SER A  35      -2.727  -4.366  14.007  1.00 22.79           O  
ATOM    257  CB  SER A  35      -2.555  -1.793  15.855  1.00 25.91           C  
ATOM    258  OG  SER A  35      -3.462  -1.200  16.789  1.00 28.38           O  
ATOM    259  N   PHE A  36      -0.618  -4.107  14.787  1.00 24.11           N  
ATOM    260  CA  PHE A  36       0.060  -4.602  13.548  1.00 24.71           C  
ATOM    261  C   PHE A  36       1.108  -5.596  13.998  1.00 22.54           C  
ATOM    262  O   PHE A  36       2.315  -5.269  14.137  1.00 22.57           O  
ATOM    263  CB  PHE A  36       0.753  -3.393  12.816  1.00 25.10           C  
ATOM    264  CG  PHE A  36      -0.215  -2.267  12.522  1.00 22.29           C  
ATOM    265  CD1 PHE A  36      -0.100  -1.028  13.214  1.00 22.32           C  
ATOM    266  CD2 PHE A  36      -1.286  -2.467  11.640  1.00 26.78           C  
ATOM    267  CE1 PHE A  36      -1.005  -0.007  12.944  1.00 23.05           C  
ATOM    268  CE2 PHE A  36      -2.239  -1.447  11.421  1.00 26.90           C  
ATOM    269  CZ  PHE A  36      -2.066  -0.221  12.091  1.00 24.34           C  
ATOM    270  N   PRO A  37       0.663  -6.826  14.324  1.00 25.91           N  
ATOM    271  CA  PRO A  37       1.569  -7.783  14.944  1.00 24.85           C  
ATOM    272  C   PRO A  37       2.747  -8.140  14.152  1.00 26.67           C  
ATOM    273  O   PRO A  37       3.731  -8.538  14.757  1.00 24.10           O  
ATOM    274  CB  PRO A  37       0.688  -9.056  15.084  1.00 31.42           C  
ATOM    275  CG  PRO A  37      -0.650  -8.531  15.219  1.00 31.30           C  
ATOM    276  CD  PRO A  37      -0.712  -7.296  14.337  1.00 26.41           C  
ATOM    277  N   THR A  38       2.679  -8.061  12.809  1.00 25.40           N  
ATOM    278  CA  THR A  38       3.895  -8.301  11.999  1.00 28.75           C  
ATOM    279  C   THR A  38       5.080  -7.495  12.512  1.00 27.54           C  
ATOM    280  O   THR A  38       6.241  -7.934  12.358  1.00 25.08           O  
ATOM    281  CB  THR A  38       3.661  -7.937  10.506  1.00 31.39           C  
ATOM    282  OG1 THR A  38       3.133  -6.606  10.445  1.00 27.81           O  
ATOM    283  CG2 THR A  38       2.561  -8.863   9.935  1.00 27.95           C  
ATOM    284  N   THR A  39       4.846  -6.299  13.104  1.00 26.30           N  
ATOM    285  CA  THR A  39       6.015  -5.452  13.466  1.00 25.08           C  
ATOM    286  C   THR A  39       6.809  -6.068  14.625  1.00 23.23           C  
ATOM    287  O   THR A  39       8.010  -5.776  14.874  1.00 26.31           O  
ATOM    288  CB  THR A  39       5.570  -4.020  13.889  1.00 23.51           C  
ATOM    289  OG1 THR A  39       4.619  -4.163  14.947  1.00 22.01           O  
ATOM    290  CG2 THR A  39       4.874  -3.286  12.699  1.00 23.47           C  
ATOM    291  N   LYS A  40       6.124  -6.904  15.388  1.00 26.65           N  
ATOM    292  CA  LYS A  40       6.771  -7.555  16.551  1.00 26.68           C  
ATOM    293  C   LYS A  40       8.035  -8.345  16.205  1.00 28.38           C  
ATOM    294  O   LYS A  40       8.917  -8.476  17.037  1.00 28.03           O  
ATOM    295  CB  LYS A  40       5.780  -8.441  17.314  1.00 27.27           C  
ATOM    296  CG  LYS A  40       4.634  -7.764  18.044  1.00 29.83           C  
ATOM    297  CD  LYS A  40       4.012  -8.767  19.045  1.00 28.57           C  
ATOM    298  CE  LYS A  40       3.069  -9.698  18.330  1.00 31.99           C  
ATOM    299  NZ  LYS A  40       2.278 -10.529  19.274  1.00 33.48           N  
ATOM    300  N   THR A  41       8.163  -8.826  14.975  1.00 29.63           N  
ATOM    301  CA  THR A  41       9.282  -9.719  14.730  1.00 34.02           C  
ATOM    302  C   THR A  41      10.596  -8.973  14.684  1.00 36.46           C  
ATOM    303  O   THR A  41      11.649  -9.588  14.702  1.00 30.93           O  
ATOM    304  CB  THR A  41       9.083 -10.538  13.460  1.00 35.08           C  
ATOM    305  OG1 THR A  41       8.979  -9.654  12.323  1.00 34.27           O  
ATOM    306  CG2 THR A  41       7.819 -11.374  13.614  1.00 38.87           C  
ATOM    307  N   TYR A  42      10.561  -7.642  14.669  1.00 31.98           N  
ATOM    308  CA  TYR A  42      11.805  -6.915  14.722  1.00 29.99           C  
ATOM    309  C   TYR A  42      12.271  -6.807  16.129  1.00 26.45           C  
ATOM    310  O   TYR A  42      13.366  -6.389  16.351  1.00 27.39           O  
ATOM    311  CB  TYR A  42      11.677  -5.500  14.136  1.00 31.25           C  
ATOM    312  CG  TYR A  42      11.486  -5.450  12.699  1.00 30.27           C  
ATOM    313  CD1 TYR A  42      12.562  -5.223  11.845  1.00 30.29           C  
ATOM    314  CD2 TYR A  42      10.224  -5.602  12.181  1.00 34.00           C  
ATOM    315  CE1 TYR A  42      12.354  -5.180  10.474  1.00 30.27           C  
ATOM    316  CE2 TYR A  42       9.995  -5.587  10.846  1.00 32.58           C  
ATOM    317  CZ  TYR A  42      11.035  -5.367  10.009  1.00 28.02           C  
ATOM    318  OH  TYR A  42      10.699  -5.322   8.701  1.00 32.42           O  
ATOM    319  N   PHE A  43      11.479  -7.200  17.097  1.00 28.25           N  
ATOM    320  CA  PHE A  43      11.909  -7.052  18.463  1.00 30.12           C  
ATOM    321  C   PHE A  43      11.892  -8.425  19.132  1.00 36.08           C  
ATOM    322  O   PHE A  43      11.170  -8.614  20.129  1.00 35.25           O  
ATOM    323  CB  PHE A  43      10.997  -6.041  19.199  1.00 28.80           C  
ATOM    324  CG  PHE A  43      11.101  -4.634  18.621  1.00 31.78           C  
ATOM    325  CD1 PHE A  43      10.387  -4.297  17.464  1.00 32.38           C  
ATOM    326  CD2 PHE A  43      11.976  -3.680  19.197  1.00 33.32           C  
ATOM    327  CE1 PHE A  43      10.455  -3.015  16.928  1.00 34.40           C  
ATOM    328  CE2 PHE A  43      12.093  -2.379  18.639  1.00 31.99           C  
ATOM    329  CZ  PHE A  43      11.311  -2.058  17.509  1.00 29.57           C  
ATOM    330  N   PRO A  44      12.666  -9.398  18.565  1.00 40.32           N  
ATOM    331  CA  PRO A  44      12.430 -10.754  19.048  1.00 42.54           C  
ATOM    332  C   PRO A  44      12.950 -10.945  20.473  1.00 43.27           C  
ATOM    333  O   PRO A  44      12.363 -11.732  21.235  1.00 47.14           O  
ATOM    334  CB  PRO A  44      13.138 -11.637  17.997  1.00 46.23           C  
ATOM    335  CG  PRO A  44      14.188 -10.762  17.393  1.00 46.43           C  
ATOM    336  CD  PRO A  44      13.635  -9.358  17.444  1.00 41.81           C  
ATOM    337  N   HIS A  45      13.962 -10.156  20.849  1.00 41.20           N  
ATOM    338  CA  HIS A  45      14.575 -10.156  22.197  1.00 39.66           C  
ATOM    339  C   HIS A  45      14.007  -9.117  23.184  1.00 42.63           C  
ATOM    340  O   HIS A  45      14.652  -8.859  24.227  1.00 37.25           O  
ATOM    341  CB  HIS A  45      16.045  -9.804  22.080  1.00 40.43           C  
ATOM    342  CG  HIS A  45      16.286  -8.492  21.398  1.00 43.16           C  
ATOM    343  ND1 HIS A  45      15.864  -8.239  20.105  1.00 41.67           N  
ATOM    344  CD2 HIS A  45      16.911  -7.367  21.818  1.00 40.48           C  
ATOM    345  CE1 HIS A  45      16.185  -6.996  19.773  1.00 41.55           C  
ATOM    346  NE2 HIS A  45      16.829  -6.448  20.790  1.00 43.48           N  
ATOM    347  N   PHE A  46      12.860  -8.492  22.856  1.00 34.91           N  
ATOM    348  CA  PHE A  46      12.190  -7.604  23.800  1.00 30.24           C  
ATOM    349  C   PHE A  46      11.073  -8.443  24.403  1.00 29.26           C  
ATOM    350  O   PHE A  46      10.464  -9.305  23.714  1.00 28.01           O  
ATOM    351  CB  PHE A  46      11.546  -6.407  23.096  1.00 29.84           C  
ATOM    352  CG  PHE A  46      12.505  -5.266  22.796  1.00 34.25           C  
ATOM    353  CD1 PHE A  46      12.158  -3.934  23.106  1.00 33.46           C  
ATOM    354  CD2 PHE A  46      13.678  -5.478  22.109  1.00 33.87           C  
ATOM    355  CE1 PHE A  46      13.030  -2.885  22.849  1.00 28.92           C  
ATOM    356  CE2 PHE A  46      14.534  -4.414  21.834  1.00 37.83           C  
ATOM    357  CZ  PHE A  46      14.201  -3.119  22.208  1.00 33.52           C  
ATOM    358  N   ASP A  47      10.783  -8.194  25.671  1.00 25.18           N  
ATOM    359  CA  ASP A  47       9.476  -8.518  26.232  1.00 28.82           C  
ATOM    360  C   ASP A  47       8.557  -7.369  25.841  1.00 28.69           C  
ATOM    361  O   ASP A  47       8.861  -6.222  26.172  1.00 27.88           O  
ATOM    362  CB  ASP A  47       9.593  -8.660  27.742  1.00 33.93           C  
ATOM    363  CG  ASP A  47       8.251  -8.852  28.461  1.00 36.86           C  
ATOM    364  OD1 ASP A  47       8.245  -8.974  29.703  1.00 51.01           O  
ATOM    365  OD2 ASP A  47       7.209  -8.870  27.838  1.00 38.14           O  
ATOM    366  N   LEU A  48       7.486  -7.670  25.090  1.00 25.73           N  
ATOM    367  CA  LEU A  48       6.612  -6.670  24.510  1.00 29.54           C  
ATOM    368  C   LEU A  48       5.344  -6.554  25.348  1.00 31.32           C  
ATOM    369  O   LEU A  48       4.407  -5.863  24.958  1.00 30.82           O  
ATOM    370  CB  LEU A  48       6.288  -6.964  23.002  1.00 24.45           C  
ATOM    371  CG  LEU A  48       7.529  -6.894  22.062  1.00 26.03           C  
ATOM    372  CD1 LEU A  48       7.279  -7.233  20.596  1.00 25.43           C  
ATOM    373  CD2 LEU A  48       8.315  -5.571  22.197  1.00 22.02           C  
ATOM    374  N   SER A  49       5.321  -7.204  26.522  1.00 27.13           N  
ATOM    375  CA  SER A  49       4.164  -7.112  27.407  1.00 26.57           C  
ATOM    376  C   SER A  49       4.020  -5.698  27.928  1.00 29.33           C  
ATOM    377  O   SER A  49       5.010  -4.929  27.938  1.00 28.87           O  
ATOM    378  CB  SER A  49       4.269  -8.149  28.536  1.00 28.70           C  
ATOM    379  OG  SER A  49       5.421  -7.884  29.306  1.00 29.01           O  
ATOM    380  N   HIS A  50       2.803  -5.336  28.326  1.00 27.24           N  
ATOM    381  CA  HIS A  50       2.519  -4.039  28.958  1.00 30.80           C  
ATOM    382  C   HIS A  50       3.403  -3.781  30.174  1.00 33.41           C  
ATOM    383  O   HIS A  50       3.633  -4.700  30.991  1.00 33.80           O  
ATOM    384  CB  HIS A  50       1.036  -3.961  29.385  1.00 33.72           C  
ATOM    385  CG  HIS A  50       0.612  -2.585  29.815  1.00 37.41           C  
ATOM    386  ND1 HIS A  50       0.522  -1.519  28.937  1.00 37.12           N  
ATOM    387  CD2 HIS A  50       0.262  -2.089  31.036  1.00 40.46           C  
ATOM    388  CE1 HIS A  50       0.122  -0.440  29.589  1.00 40.79           C  
ATOM    389  NE2 HIS A  50      -0.036  -0.757  30.866  1.00 44.89           N  
ATOM    390  N   GLY A  51       3.959  -2.565  30.268  1.00 31.99           N  
ATOM    391  CA  GLY A  51       4.816  -2.171  31.405  1.00 30.82           C  
ATOM    392  C   GLY A  51       6.247  -2.639  31.220  1.00 28.84           C  
ATOM    393  O   GLY A  51       7.083  -2.573  32.104  1.00 31.09           O  
ATOM    394  N   SER A  52       6.554  -3.132  30.043  1.00 26.50           N  
ATOM    395  CA  SER A  52       7.892  -3.616  29.846  1.00 25.46           C  
ATOM    396  C   SER A  52       8.921  -2.507  29.895  1.00 30.51           C  
ATOM    397  O   SER A  52       8.839  -1.517  29.147  1.00 28.64           O  
ATOM    398  CB  SER A  52       8.004  -4.366  28.521  1.00 22.96           C  
ATOM    399  OG  SER A  52       9.397  -4.450  28.143  1.00 21.98           O  
ATOM    400  N   ALA A  53       9.967  -2.735  30.701  1.00 27.98           N  
ATOM    401  CA  ALA A  53      11.082  -1.790  30.834  1.00 26.79           C  
ATOM    402  C   ALA A  53      11.749  -1.621  29.470  1.00 29.72           C  
ATOM    403  O   ALA A  53      12.258  -0.565  29.162  1.00 23.33           O  
ATOM    404  CB  ALA A  53      12.084  -2.323  31.867  1.00 31.29           C  
ATOM    405  N   GLN A  54      11.768  -2.681  28.658  1.00 25.14           N  
ATOM    406  CA  GLN A  54      12.515  -2.561  27.431  1.00 25.89           C  
ATOM    407  C   GLN A  54      11.732  -1.715  26.419  1.00 25.00           C  
ATOM    408  O   GLN A  54      12.333  -0.968  25.641  1.00 25.35           O  
ATOM    409  CB  GLN A  54      12.786  -3.946  26.844  1.00 26.59           C  
ATOM    410  CG  GLN A  54      13.836  -4.693  27.656  1.00 33.04           C  
ATOM    411  CD  GLN A  54      13.495  -6.184  27.785  1.00 31.97           C  
ATOM    412  OE1 GLN A  54      12.507  -6.668  27.232  1.00 34.92           O  
ATOM    413  NE2 GLN A  54      14.235  -6.861  28.620  1.00 34.88           N  
ATOM    414  N   VAL A  55      10.411  -1.880  26.416  1.00 23.27           N  
ATOM    415  CA  VAL A  55       9.561  -1.026  25.577  1.00 24.12           C  
ATOM    416  C   VAL A  55       9.609   0.450  26.069  1.00 28.33           C  
ATOM    417  O   VAL A  55       9.761   1.416  25.262  1.00 26.04           O  
ATOM    418  CB  VAL A  55       8.132  -1.530  25.487  1.00 23.27           C  
ATOM    419  CG1 VAL A  55       7.335  -0.578  24.564  1.00 20.14           C  
ATOM    420  CG2 VAL A  55       8.089  -2.936  24.920  1.00 22.01           C  
ATOM    421  N   LYS A  56       9.558   0.646  27.384  1.00 26.47           N  
ATOM    422  CA  LYS A  56       9.774   2.003  27.939  1.00 30.75           C  
ATOM    423  C   LYS A  56      11.073   2.650  27.503  1.00 29.06           C  
ATOM    424  O   LYS A  56      11.045   3.816  27.082  1.00 25.48           O  
ATOM    425  CB  LYS A  56       9.785   2.029  29.473  1.00 32.70           C  
ATOM    426  CG  LYS A  56       8.436   1.851  30.093  1.00 41.26           C  
ATOM    427  CD  LYS A  56       8.554   2.158  31.594  1.00 49.27           C  
ATOM    428  CE  LYS A  56       7.199   2.056  32.286  1.00 56.49           C  
ATOM    429  NZ  LYS A  56       6.601   0.735  32.010  1.00 49.90           N  
ATOM    430  N   GLY A  57      12.183   1.900  27.560  1.00 25.02           N  
ATOM    431  CA  GLY A  57      13.465   2.476  27.309  1.00 25.86           C  
ATOM    432  C   GLY A  57      13.539   2.791  25.826  1.00 31.35           C  
ATOM    433  O   GLY A  57      14.109   3.831  25.411  1.00 28.22           O  
ATOM    434  N   HIS A  58      12.978   1.901  25.004  1.00 27.42           N  
ATOM    435  CA  HIS A  58      13.002   2.175  23.554  1.00 26.12           C  
ATOM    436  C   HIS A  58      12.130   3.370  23.136  1.00 24.94           C  
ATOM    437  O   HIS A  58      12.522   4.116  22.240  1.00 21.02           O  
ATOM    438  CB  HIS A  58      12.527   0.968  22.773  1.00 25.69           C  
ATOM    439  CG  HIS A  58      12.826   1.060  21.311  1.00 23.79           C  
ATOM    440  ND1 HIS A  58      14.122   1.078  20.826  1.00 24.88           N  
ATOM    441  CD2 HIS A  58      12.003   1.127  20.232  1.00 21.41           C  
ATOM    442  CE1 HIS A  58      14.087   1.113  19.501  1.00 22.93           C  
ATOM    443  NE2 HIS A  58      12.823   1.179  19.120  1.00 24.83           N  
ATOM    444  N   GLY A  59      10.951   3.492  23.748  1.00 26.04           N  
ATOM    445  CA  GLY A  59      10.046   4.607  23.544  1.00 22.93           C  
ATOM    446  C   GLY A  59      10.766   5.928  23.706  1.00 25.68           C  
ATOM    447  O   GLY A  59      10.487   6.912  22.976  1.00 23.72           O  
ATOM    448  N   LYS A  60      11.702   5.971  24.663  1.00 25.59           N  
ATOM    449  CA  LYS A  60      12.379   7.200  24.989  1.00 26.87           C  
ATOM    450  C   LYS A  60      13.384   7.472  23.905  1.00 26.15           C  
ATOM    451  O   LYS A  60      13.602   8.613  23.501  1.00 24.03           O  
ATOM    452  CB  LYS A  60      13.113   7.121  26.375  1.00 26.87           C  
ATOM    453  CG  LYS A  60      13.899   8.394  26.637  1.00 33.01           C  
ATOM    454  CD  LYS A  60      13.041   9.691  26.569  1.00 37.46           C  
ATOM    455  CE  LYS A  60      13.770  10.842  27.267  1.00 48.93           C  
ATOM    456  NZ  LYS A  60      14.710  10.207  28.255  1.00 38.47           N  
ATOM    457  N   LYS A  61      13.984   6.411  23.401  1.00 21.85           N  
ATOM    458  CA  LYS A  61      14.969   6.607  22.306  1.00 26.65           C  
ATOM    459  C   LYS A  61      14.300   7.128  21.033  1.00 24.65           C  
ATOM    460  O   LYS A  61      14.886   7.999  20.360  1.00 22.87           O  
ATOM    461  CB  LYS A  61      15.753   5.312  22.063  1.00 27.59           C  
ATOM    462  CG  LYS A  61      16.680   5.008  23.244  1.00 35.33           C  
ATOM    463  CD  LYS A  61      17.608   3.858  22.968  1.00 43.40           C  
ATOM    464  CE  LYS A  61      18.701   3.735  24.057  1.00 54.62           C  
ATOM    465  NZ  LYS A  61      19.414   5.004  24.449  1.00 52.96           N  
ATOM    466  N   VAL A  62      13.100   6.607  20.721  1.00 21.96           N  
ATOM    467  CA  VAL A  62      12.341   7.003  19.517  1.00 21.66           C  
ATOM    468  C   VAL A  62      11.923   8.488  19.671  1.00 23.12           C  
ATOM    469  O   VAL A  62      12.113   9.284  18.753  1.00 21.64           O  
ATOM    470  CB  VAL A  62      11.093   6.080  19.311  1.00 22.92           C  
ATOM    471  CG1 VAL A  62      10.083   6.649  18.282  1.00 22.02           C  
ATOM    472  CG2 VAL A  62      11.525   4.636  18.958  1.00 23.81           C  
ATOM    473  N   ALA A  63      11.357   8.831  20.826  1.00 23.08           N  
ATOM    474  CA  ALA A  63      10.882  10.197  21.110  1.00 24.74           C  
ATOM    475  C   ALA A  63      12.062  11.150  21.084  1.00 23.57           C  
ATOM    476  O   ALA A  63      11.918  12.214  20.525  1.00 26.64           O  
ATOM    477  CB  ALA A  63      10.174  10.285  22.461  1.00 24.17           C  
ATOM    478  N   ASP A  64      13.224  10.764  21.632  1.00 23.55           N  
ATOM    479  CA  ASP A  64      14.430  11.584  21.494  1.00 28.25           C  
ATOM    480  C   ASP A  64      14.901  11.777  20.050  1.00 27.79           C  
ATOM    481  O   ASP A  64      15.398  12.821  19.746  1.00 23.95           O  
ATOM    482  CB  ASP A  64      15.640  11.023  22.242  1.00 31.01           C  
ATOM    483  CG  ASP A  64      15.513  11.146  23.749  1.00 36.86           C  
ATOM    484  OD1 ASP A  64      14.548  11.736  24.271  1.00 37.26           O  
ATOM    485  OD2 ASP A  64      16.401  10.583  24.400  1.00 42.52           O  
ATOM    486  N   ALA A  65      14.837  10.729  19.217  1.00 23.46           N  
ATOM    487  CA  ALA A  65      15.146  10.876  17.764  1.00 25.40           C  
ATOM    488  C   ALA A  65      14.201  11.886  17.103  1.00 21.38           C  
ATOM    489  O   ALA A  65      14.664  12.711  16.308  1.00 21.50           O  
ATOM    490  CB  ALA A  65      14.997   9.518  17.022  1.00 24.60           C  
ATOM    491  N   LEU A  66      12.892  11.751  17.368  1.00 20.07           N  
ATOM    492  CA  LEU A  66      11.908  12.623  16.745  1.00 23.04           C  
ATOM    493  C   LEU A  66      12.168  14.041  17.233  1.00 25.57           C  
ATOM    494  O   LEU A  66      12.018  14.960  16.472  1.00 22.55           O  
ATOM    495  CB  LEU A  66      10.493  12.202  17.078  1.00 23.10           C  
ATOM    496  CG  LEU A  66      10.067  10.909  16.424  1.00 23.19           C  
ATOM    497  CD1 LEU A  66       8.744  10.450  17.063  1.00 20.74           C  
ATOM    498  CD2 LEU A  66       9.980  11.129  14.884  1.00 23.07           C  
ATOM    499  N   THR A  67      12.566  14.187  18.512  1.00 23.78           N  
ATOM    500  CA  THR A  67      12.856  15.529  19.083  1.00 26.30           C  
ATOM    501  C   THR A  67      14.082  16.114  18.418  1.00 23.06           C  
ATOM    502  O   THR A  67      14.064  17.262  18.039  1.00 27.94           O  
ATOM    503  CB  THR A  67      12.993  15.472  20.649  1.00 27.47           C  
ATOM    504  OG1 THR A  67      11.729  15.050  21.150  1.00 34.11           O  
ATOM    505  CG2 THR A  67      13.249  16.828  21.222  1.00 32.49           C  
ATOM    506  N   ASN A  68      15.110  15.303  18.201  1.00 25.73           N  
ATOM    507  CA  ASN A  68      16.254  15.745  17.391  1.00 26.73           C  
ATOM    508  C   ASN A  68      15.848  16.132  15.982  1.00 25.75           C  
ATOM    509  O   ASN A  68      16.348  17.140  15.429  1.00 29.34           O  
ATOM    510  CB  ASN A  68      17.362  14.691  17.434  1.00 26.81           C  
ATOM    511  CG  ASN A  68      18.560  14.993  16.565  1.00 34.49           C  
ATOM    512  OD1 ASN A  68      18.820  14.213  15.669  1.00 39.33           O  
ATOM    513  ND2 ASN A  68      19.367  16.053  16.879  1.00 28.35           N  
ATOM    514  N   ALA A  69      14.923  15.382  15.378  1.00 22.56           N  
ATOM    515  CA  ALA A  69      14.453  15.782  14.053  1.00 24.71           C  
ATOM    516  C   ALA A  69      13.700  17.177  14.023  1.00 22.67           C  
ATOM    517  O   ALA A  69      13.934  17.999  13.146  1.00 28.08           O  
ATOM    518  CB  ALA A  69      13.593  14.687  13.411  1.00 22.73           C  
ATOM    519  N   VAL A  70      12.826  17.431  14.976  1.00 24.92           N  
ATOM    520  CA  VAL A  70      12.108  18.736  15.144  1.00 26.33           C  
ATOM    521  C   VAL A  70      13.158  19.840  15.332  1.00 26.52           C  
ATOM    522  O   VAL A  70      13.102  20.911  14.672  1.00 26.18           O  
ATOM    523  CB  VAL A  70      11.239  18.682  16.456  1.00 32.24           C  
ATOM    524  CG1 VAL A  70      10.769  20.060  16.978  1.00 32.53           C  
ATOM    525  CG2 VAL A  70      10.038  17.809  16.205  1.00 34.68           C  
ATOM    526  N   ALA A  71      14.144  19.579  16.184  1.00 24.49           N  
ATOM    527  CA  ALA A  71      15.137  20.599  16.525  1.00 29.17           C  
ATOM    528  C   ALA A  71      16.080  20.956  15.342  1.00 27.79           C  
ATOM    529  O   ALA A  71      16.771  22.011  15.373  1.00 27.18           O  
ATOM    530  CB  ALA A  71      15.960  20.136  17.735  1.00 26.84           C  
ATOM    531  N   HIS A  72      16.147  20.066  14.339  1.00 24.37           N  
ATOM    532  CA  HIS A  72      16.956  20.193  13.157  1.00 23.08           C  
ATOM    533  C   HIS A  72      16.161  19.915  11.911  1.00 28.40           C  
ATOM    534  O   HIS A  72      16.669  19.272  10.953  1.00 28.55           O  
ATOM    535  CB  HIS A  72      18.250  19.322  13.157  1.00 25.55           C  
ATOM    536  CG  HIS A  72      19.167  19.647  14.285  1.00 31.26           C  
ATOM    537  ND1 HIS A  72      20.116  20.653  14.214  1.00 33.38           N  
ATOM    538  CD2 HIS A  72      19.205  19.186  15.558  1.00 31.55           C  
ATOM    539  CE1 HIS A  72      20.758  20.734  15.369  1.00 29.14           C  
ATOM    540  NE2 HIS A  72      20.222  19.860  16.201  1.00 34.09           N  
ATOM    541  N   VAL A  73      14.992  20.519  11.890  1.00 28.89           N  
ATOM    542  CA  VAL A  73      13.940  20.280  10.903  1.00 27.38           C  
ATOM    543  C   VAL A  73      14.392  20.612   9.485  1.00 33.66           C  
ATOM    544  O   VAL A  73      13.936  19.974   8.499  1.00 33.03           O  
ATOM    545  CB  VAL A  73      12.646  21.032  11.317  1.00 28.16           C  
ATOM    546  CG1 VAL A  73      12.684  22.571  11.043  1.00 30.19           C  
ATOM    547  CG2 VAL A  73      11.386  20.373  10.712  1.00 32.02           C  
ATOM    548  N   ASP A  74      15.281  21.588   9.356  1.00 34.13           N  
ATOM    549  CA  ASP A  74      15.814  21.993   8.025  1.00 38.56           C  
ATOM    550  C   ASP A  74      17.025  21.180   7.548  1.00 43.00           C  
ATOM    551  O   ASP A  74      17.588  21.413   6.453  1.00 35.68           O  
ATOM    552  CB  ASP A  74      16.104  23.503   8.008  1.00 40.22           C  
ATOM    553  CG  ASP A  74      14.813  24.338   7.999  1.00 43.96           C  
ATOM    554  OD1 ASP A  74      14.693  25.322   8.765  1.00 40.00           O  
ATOM    555  OD2 ASP A  74      13.874  23.958   7.257  1.00 47.72           O  
ATOM    556  N   ASP A  75      17.424  20.211   8.367  1.00 39.43           N  
ATOM    557  CA  ASP A  75      18.637  19.447   8.121  1.00 34.58           C  
ATOM    558  C   ASP A  75      18.438  18.004   8.573  1.00 32.91           C  
ATOM    559  O   ASP A  75      19.396  17.326   9.045  1.00 34.76           O  
ATOM    560  CB  ASP A  75      19.790  20.148   8.856  1.00 38.12           C  
ATOM    561  CG  ASP A  75      21.173  19.639   8.486  1.00 44.12           C  
ATOM    562  OD1 ASP A  75      22.006  19.571   9.423  1.00 48.06           O  
ATOM    563  OD2 ASP A  75      21.465  19.321   7.305  1.00 45.09           O  
ATOM    564  N   MET A  76      17.226  17.514   8.376  1.00 32.45           N  
ATOM    565  CA  MET A  76      16.879  16.166   8.824  1.00 31.16           C  
ATOM    566  C   MET A  76      17.707  15.064   8.234  1.00 31.78           C  
ATOM    567  O   MET A  76      18.080  14.144   9.009  1.00 32.11           O  
ATOM    568  CB  MET A  76      15.417  15.877   8.646  1.00 36.38           C  
ATOM    569  CG  MET A  76      14.485  16.698   9.529  1.00 40.51           C  
ATOM    570  SD  MET A  76      12.913  15.802   9.670  1.00 48.45           S  
ATOM    571  CE  MET A  76      11.748  17.138   9.523  1.00 45.47           C  
ATOM    572  N   PRO A  77      18.015  15.109   6.873  1.00 31.52           N  
ATOM    573  CA  PRO A  77      18.831  14.010   6.350  1.00 32.63           C  
ATOM    574  C   PRO A  77      20.139  13.853   7.119  1.00 38.16           C  
ATOM    575  O   PRO A  77      20.519  12.733   7.471  1.00 38.39           O  
ATOM    576  CB  PRO A  77      19.074  14.414   4.873  1.00 32.55           C  
ATOM    577  CG  PRO A  77      17.913  15.267   4.491  1.00 29.99           C  
ATOM    578  CD  PRO A  77      17.643  16.054   5.787  1.00 31.59           C  
ATOM    579  N   ASN A  78      20.786  14.973   7.442  1.00 37.32           N  
ATOM    580  CA  ASN A  78      22.036  14.956   8.172  1.00 32.05           C  
ATOM    581  C   ASN A  78      21.849  14.566   9.654  1.00 33.64           C  
ATOM    582  O   ASN A  78      22.532  13.657  10.146  1.00 33.17           O  
ATOM    583  CB  ASN A  78      22.789  16.288   7.948  1.00 40.17           C  
ATOM    584  CG  ASN A  78      23.989  16.461   8.861  1.00 42.71           C  
ATOM    585  OD1 ASN A  78      24.951  15.670   8.853  1.00 46.91           O  
ATOM    586  ND2 ASN A  78      23.936  17.522   9.672  1.00 44.01           N  
ATOM    587  N   ALA A  79      20.851  15.145  10.331  1.00 32.48           N  
ATOM    588  CA  ALA A  79      20.604  14.780  11.745  1.00 37.14           C  
ATOM    589  C   ALA A  79      20.244  13.287  11.910  1.00 36.70           C  
ATOM    590  O   ALA A  79      20.670  12.634  12.872  1.00 34.91           O  
ATOM    591  CB  ALA A  79      19.504  15.665  12.336  1.00 35.83           C  
ATOM    592  N   LEU A  80      19.486  12.744  10.957  1.00 33.99           N  
ATOM    593  CA  LEU A  80      19.035  11.352  11.040  1.00 33.58           C  
ATOM    594  C   LEU A  80      19.883  10.334  10.252  1.00 35.20           C  
ATOM    595  O   LEU A  80      19.479   9.167  10.087  1.00 34.05           O  
ATOM    596  CB  LEU A  80      17.573  11.213  10.623  1.00 29.11           C  
ATOM    597  CG  LEU A  80      16.545  11.899  11.497  1.00 30.54           C  
ATOM    598  CD1 LEU A  80      15.182  11.755  10.915  1.00 27.48           C  
ATOM    599  CD2 LEU A  80      16.600  11.299  12.888  1.00 38.27           C  
ATOM    600  N   SER A  81      21.083  10.741   9.856  1.00 39.82           N  
ATOM    601  CA  SER A  81      21.918   9.893   8.986  1.00 33.90           C  
ATOM    602  C   SER A  81      22.273   8.508   9.544  1.00 32.00           C  
ATOM    603  O   SER A  81      22.133   7.472   8.870  0.50 25.02           O  
ATOM    604  CB  SER A  81      23.221  10.623   8.622  1.00 34.68           C  
ATOM    605  OG  SER A  81      23.756   9.903   7.519  1.00 45.66           O  
ATOM    606  N   ALA A  82      22.771   8.538  10.769  1.00 33.68           N  
ATOM    607  CA  ALA A  82      23.154   7.326  11.485  1.00 38.32           C  
ATOM    608  C   ALA A  82      21.953   6.424  11.692  1.00 32.83           C  
ATOM    609  O   ALA A  82      22.071   5.238  11.553  1.00 31.83           O  
ATOM    610  CB  ALA A  82      23.834   7.657  12.801  1.00 35.68           C  
ATOM    611  N   LEU A  83      20.791   6.995  12.016  1.00 28.30           N  
ATOM    612  CA  LEU A  83      19.595   6.175  12.175  1.00 27.25           C  
ATOM    613  C   LEU A  83      19.053   5.649  10.848  1.00 27.66           C  
ATOM    614  O   LEU A  83      18.535   4.562  10.817  1.00 27.70           O  
ATOM    615  CB  LEU A  83      18.456   6.952  12.873  1.00 30.77           C  
ATOM    616  CG  LEU A  83      18.655   7.260  14.351  1.00 39.85           C  
ATOM    617  CD1 LEU A  83      17.360   7.947  14.822  1.00 39.38           C  
ATOM    618  CD2 LEU A  83      18.956   5.997  15.184  1.00 35.96           C  
ATOM    619  N   SER A  84      19.167   6.386   9.752  1.00 28.58           N  
ATOM    620  CA  SER A  84      18.718   5.807   8.456  1.00 30.96           C  
ATOM    621  C   SER A  84      19.583   4.589   8.014  1.00 31.30           C  
ATOM    622  O   SER A  84      19.047   3.575   7.497  1.00 27.48           O  
ATOM    623  CB  SER A  84      18.549   6.879   7.376  1.00 33.47           C  
ATOM    624  OG  SER A  84      19.707   7.685   7.353  1.00 37.63           O  
ATOM    625  N   ASP A  85      20.879   4.675   8.310  1.00 30.23           N  
ATOM    626  CA  ASP A  85      21.866   3.568   8.173  1.00 30.92           C  
ATOM    627  C   ASP A  85      21.494   2.358   8.942  1.00 31.81           C  
ATOM    628  O   ASP A  85      21.376   1.258   8.402  1.00 28.68           O  
ATOM    629  CB  ASP A  85      23.229   3.990   8.715  1.00 34.54           C  
ATOM    630  CG  ASP A  85      23.972   4.923   7.777  1.00 40.80           C  
ATOM    631  OD1 ASP A  85      23.540   5.101   6.613  1.00 46.19           O  
ATOM    632  OD2 ASP A  85      24.982   5.506   8.234  1.00 53.13           O  
ATOM    633  N   LEU A  86      21.317   2.566  10.231  1.00 29.32           N  
ATOM    634  CA  LEU A  86      20.796   1.564  11.115  1.00 28.78           C  
ATOM    635  C   LEU A  86      19.554   0.826  10.602  1.00 29.18           C  
ATOM    636  O   LEU A  86      19.614  -0.436  10.491  1.00 26.95           O  
ATOM    637  CB  LEU A  86      20.573   2.157  12.529  1.00 29.41           C  
ATOM    638  CG  LEU A  86      20.020   1.119  13.514  1.00 35.60           C  
ATOM    639  CD1 LEU A  86      20.980  -0.052  13.681  1.00 33.64           C  
ATOM    640  CD2 LEU A  86      19.695   1.729  14.867  1.00 31.25           C  
ATOM    641  N   HIS A  87      18.464   1.571  10.290  1.00 28.43           N  
ATOM    642  CA  HIS A  87      17.154   0.945   9.991  1.00 27.65           C  
ATOM    643  C   HIS A  87      17.136   0.272   8.584  1.00 30.17           C  
ATOM    644  O   HIS A  87      16.574  -0.795   8.437  1.00 25.86           O  
ATOM    645  CB  HIS A  87      15.984   1.943  10.106  1.00 26.05           C  
ATOM    646  CG  HIS A  87      15.642   2.330  11.536  1.00 24.28           C  
ATOM    647  ND1 HIS A  87      16.363   3.270  12.235  1.00 23.25           N  
ATOM    648  CD2 HIS A  87      14.696   1.856  12.397  1.00 23.18           C  
ATOM    649  CE1 HIS A  87      15.854   3.392  13.462  1.00 25.66           C  
ATOM    650  NE2 HIS A  87      14.842   2.535  13.594  1.00 23.78           N  
ATOM    651  N   ALA A  88      17.714   0.936   7.592  1.00 30.63           N  
ATOM    652  CA  ALA A  88      17.841   0.323   6.232  1.00 34.46           C  
ATOM    653  C   ALA A  88      18.912  -0.780   6.126  1.00 37.58           C  
ATOM    654  O   ALA A  88      18.614  -1.917   5.719  1.00 39.64           O  
ATOM    655  CB  ALA A  88      18.100   1.410   5.217  1.00 30.99           C  
ATOM    656  N   HIS A  89      20.151  -0.475   6.511  1.00 40.87           N  
ATOM    657  CA  HIS A  89      21.262  -1.441   6.303  1.00 42.69           C  
ATOM    658  C   HIS A  89      21.263  -2.577   7.283  1.00 40.30           C  
ATOM    659  O   HIS A  89      21.370  -3.716   6.874  1.00 42.83           O  
ATOM    660  CB  HIS A  89      22.663  -0.807   6.296  1.00 49.63           C  
ATOM    661  CG  HIS A  89      22.830   0.290   5.303  1.00 56.31           C  
ATOM    662  ND1 HIS A  89      23.707   1.338   5.502  1.00 67.16           N  
ATOM    663  CD2 HIS A  89      22.214   0.531   4.123  1.00 58.30           C  
ATOM    664  CE1 HIS A  89      23.634   2.172   4.477  1.00 69.85           C  
ATOM    665  NE2 HIS A  89      22.727   1.710   3.632  1.00 67.82           N  
ATOM    666  N   LYS A  90      21.224  -2.293   8.587  1.00 42.97           N  
ATOM    667  CA  LYS A  90      21.354  -3.360   9.529  1.00 40.48           C  
ATOM    668  C   LYS A  90      20.041  -4.028   9.833  1.00 44.21           C  
ATOM    669  O   LYS A  90      19.942  -5.275   9.899  1.00 41.13           O  
ATOM    670  CB  LYS A  90      22.040  -2.904  10.828  1.00 47.50           C  
ATOM    671  CG  LYS A  90      22.104  -3.981  11.907  1.00 51.26           C  
ATOM    672  CD  LYS A  90      22.381  -3.344  13.264  1.00 61.63           C  
ATOM    673  CE  LYS A  90      23.368  -4.150  14.100  1.00 57.66           C  
ATOM    674  NZ  LYS A  90      22.657  -5.103  14.991  1.00 54.54           N  
ATOM    675  N   LEU A  91      19.011  -3.234  10.034  1.00 35.09           N  
ATOM    676  CA  LEU A  91      17.821  -3.836  10.576  1.00 32.60           C  
ATOM    677  C   LEU A  91      16.921  -4.283   9.434  1.00 31.19           C  
ATOM    678  O   LEU A  91      16.012  -5.072   9.638  1.00 35.95           O  
ATOM    679  CB  LEU A  91      17.046  -2.870  11.488  1.00 32.51           C  
ATOM    680  CG  LEU A  91      17.693  -2.508  12.834  1.00 37.25           C  
ATOM    681  CD1 LEU A  91      17.063  -1.241  13.396  1.00 33.89           C  
ATOM    682  CD2 LEU A  91      17.570  -3.681  13.816  1.00 35.75           C  
ATOM    683  N   ARG A  92      17.146  -3.708   8.279  1.00 28.08           N  
ATOM    684  CA  ARG A  92      16.333  -4.037   7.105  1.00 36.47           C  
ATOM    685  C   ARG A  92      14.859  -3.802   7.392  1.00 32.49           C  
ATOM    686  O   ARG A  92      14.005  -4.672   7.173  1.00 28.02           O  
ATOM    687  CB  ARG A  92      16.642  -5.485   6.655  1.00 37.56           C  
ATOM    688  CG  ARG A  92      18.074  -5.611   6.127  1.00 43.73           C  
ATOM    689  CD  ARG A  92      18.400  -7.093   5.851  1.00 56.43           C  
ATOM    690  NE  ARG A  92      19.781  -7.336   5.441  1.00 54.54           N  
ATOM    691  CZ  ARG A  92      20.354  -6.890   4.313  1.00 58.91           C  
ATOM    692  NH1 ARG A  92      19.700  -6.135   3.416  1.00 48.01           N  
ATOM    693  NH2 ARG A  92      21.629  -7.179   4.086  1.00 62.41           N  
ATOM    694  N   VAL A  93      14.544  -2.615   7.923  1.00 32.09           N  
ATOM    695  CA  VAL A  93      13.143  -2.364   8.218  1.00 27.25           C  
ATOM    696  C   VAL A  93      12.311  -2.129   6.954  1.00 27.45           C  
ATOM    697  O   VAL A  93      12.547  -1.231   6.193  1.00 25.85           O  
ATOM    698  CB  VAL A  93      12.894  -1.189   9.264  1.00 24.33           C  
ATOM    699  CG1 VAL A  93      11.408  -1.065   9.466  1.00 21.97           C  
ATOM    700  CG2 VAL A  93      13.475  -1.574  10.612  1.00 21.80           C  
ATOM    701  N   ASP A  94      11.254  -2.896   6.813  1.00 23.83           N  
ATOM    702  CA  ASP A  94      10.379  -2.803   5.674  1.00 26.58           C  
ATOM    703  C   ASP A  94       9.766  -1.377   5.696  1.00 26.28           C  
ATOM    704  O   ASP A  94       9.263  -0.967   6.748  1.00 23.43           O  
ATOM    705  CB  ASP A  94       9.303  -3.842   5.970  1.00 26.71           C  
ATOM    706  CG  ASP A  94       8.355  -4.051   4.884  1.00 29.68           C  
ATOM    707  OD1 ASP A  94       7.983  -3.094   4.199  1.00 30.29           O  
ATOM    708  OD2 ASP A  94       7.943  -5.225   4.737  1.00 28.71           O  
ATOM    709  N   PRO A  95       9.798  -0.625   4.566  1.00 25.05           N  
ATOM    710  CA  PRO A  95       9.251   0.742   4.529  1.00 25.84           C  
ATOM    711  C   PRO A  95       7.806   0.891   4.933  1.00 25.13           C  
ATOM    712  O   PRO A  95       7.463   1.935   5.468  1.00 22.13           O  
ATOM    713  CB  PRO A  95       9.378   1.175   3.037  1.00 32.28           C  
ATOM    714  CG  PRO A  95      10.373   0.217   2.459  1.00 27.28           C  
ATOM    715  CD  PRO A  95      10.385  -1.035   3.257  1.00 26.33           C  
ATOM    716  N   VAL A  96       6.966  -0.132   4.714  1.00 22.72           N  
ATOM    717  CA  VAL A  96       5.603  -0.105   5.139  1.00 20.90           C  
ATOM    718  C   VAL A  96       5.496   0.150   6.645  1.00 19.43           C  
ATOM    719  O   VAL A  96       4.535   0.777   7.129  1.00 24.69           O  
ATOM    720  CB  VAL A  96       4.907  -1.513   4.911  1.00 23.49           C  
ATOM    721  CG1 VAL A  96       3.489  -1.486   5.477  1.00 32.96           C  
ATOM    722  CG2 VAL A  96       4.811  -1.816   3.448  1.00 27.89           C  
ATOM    723  N   ASN A  97       6.488  -0.305   7.405  1.00 20.76           N  
ATOM    724  CA  ASN A  97       6.381  -0.246   8.911  1.00 19.86           C  
ATOM    725  C   ASN A  97       6.518   1.141   9.483  1.00 21.53           C  
ATOM    726  O   ASN A  97       5.982   1.420  10.574  1.00 18.35           O  
ATOM    727  CB  ASN A  97       7.396  -1.167   9.540  1.00 19.89           C  
ATOM    728  CG  ASN A  97       6.972  -2.653   9.377  1.00 22.20           C  
ATOM    729  OD1 ASN A  97       5.792  -2.979   9.300  1.00 22.82           O  
ATOM    730  ND2 ASN A  97       7.938  -3.509   9.273  1.00 22.66           N  
ATOM    731  N   PHE A  98       7.148   2.017   8.681  1.00 17.39           N  
ATOM    732  CA  PHE A  98       7.219   3.430   9.049  1.00 20.56           C  
ATOM    733  C   PHE A  98       5.884   4.099   9.068  1.00 21.60           C  
ATOM    734  O   PHE A  98       5.635   4.920   9.956  1.00 21.16           O  
ATOM    735  CB  PHE A  98       8.261   4.193   8.177  1.00 22.07           C  
ATOM    736  CG  PHE A  98       9.668   3.736   8.461  1.00 22.91           C  
ATOM    737  CD1 PHE A  98      10.388   4.260   9.545  1.00 24.42           C  
ATOM    738  CD2 PHE A  98      10.222   2.684   7.734  1.00 25.65           C  
ATOM    739  CE1 PHE A  98      11.645   3.754   9.863  1.00 29.06           C  
ATOM    740  CE2 PHE A  98      11.484   2.192   8.041  1.00 26.42           C  
ATOM    741  CZ  PHE A  98      12.198   2.728   9.089  1.00 27.91           C  
ATOM    742  N   LYS A  99       5.021   3.737   8.104  1.00 20.09           N  
ATOM    743  CA  LYS A  99       3.629   4.222   8.044  1.00 19.08           C  
ATOM    744  C   LYS A  99       2.798   3.770   9.267  1.00 20.66           C  
ATOM    745  O   LYS A  99       2.025   4.523   9.865  1.00 18.43           O  
ATOM    746  CB  LYS A  99       2.985   3.708   6.767  1.00 21.68           C  
ATOM    747  CG  LYS A  99       3.590   4.331   5.503  1.00 25.55           C  
ATOM    748  CD  LYS A  99       2.816   3.935   4.226  1.00 24.21           C  
ATOM    749  CE  LYS A  99       3.358   4.709   3.005  1.00 31.41           C  
ATOM    750  NZ  LYS A  99       2.547   4.374   1.743  1.00 31.22           N  
ATOM    751  N   LEU A 100       3.008   2.524   9.660  1.00 19.35           N  
ATOM    752  CA  LEU A 100       2.291   1.952  10.801  1.00 19.68           C  
ATOM    753  C   LEU A 100       2.739   2.652  12.096  1.00 17.33           C  
ATOM    754  O   LEU A 100       1.878   3.045  12.869  1.00 18.62           O  
ATOM    755  CB  LEU A 100       2.601   0.422  10.891  1.00 18.14           C  
ATOM    756  CG  LEU A 100       2.238  -0.370   9.600  1.00 20.49           C  
ATOM    757  CD1 LEU A 100       2.460  -1.915   9.794  1.00 19.96           C  
ATOM    758  CD2 LEU A 100       0.758  -0.136   9.178  1.00 23.84           C  
ATOM    759  N   LEU A 101       4.038   2.839  12.314  1.00 17.01           N  
ATOM    760  CA  LEU A 101       4.510   3.498  13.549  1.00 19.24           C  
ATOM    761  C   LEU A 101       4.084   4.994  13.514  1.00 22.43           C  
ATOM    762  O   LEU A 101       3.645   5.518  14.537  1.00 19.54           O  
ATOM    763  CB  LEU A 101       6.004   3.414  13.745  1.00 19.48           C  
ATOM    764  CG  LEU A 101       6.550   4.165  15.012  1.00 20.11           C  
ATOM    765  CD1 LEU A 101       5.881   3.718  16.326  1.00 20.08           C  
ATOM    766  CD2 LEU A 101       7.998   3.859  15.145  1.00 23.19           C  
ATOM    767  N   SER A 102       4.101   5.626  12.319  1.00 19.88           N  
ATOM    768  CA  SER A 102       3.675   7.043  12.213  1.00 21.22           C  
ATOM    769  C   SER A 102       2.221   7.182  12.625  1.00 22.36           C  
ATOM    770  O   SER A 102       1.846   8.129  13.337  1.00 19.85           O  
ATOM    771  CB  SER A 102       3.867   7.573  10.756  1.00 17.61           C  
ATOM    772  OG  SER A 102       5.302   7.631  10.514  1.00 18.23           O  
ATOM    773  N   HIS A 103       1.387   6.277  12.155  1.00 20.81           N  
ATOM    774  CA  HIS A 103      -0.018   6.316  12.448  1.00 22.40           C  
ATOM    775  C   HIS A 103      -0.242   6.167  13.986  1.00 22.77           C  
ATOM    776  O   HIS A 103      -1.106   6.843  14.574  1.00 22.08           O  
ATOM    777  CB  HIS A 103      -0.758   5.165  11.677  1.00 20.83           C  
ATOM    778  CG  HIS A 103      -2.158   4.922  12.157  1.00 21.33           C  
ATOM    779  ND1 HIS A 103      -3.195   5.850  12.021  1.00 21.92           N  
ATOM    780  CD2 HIS A 103      -2.696   3.864  12.814  1.00 22.94           C  
ATOM    781  CE1 HIS A 103      -4.299   5.378  12.576  1.00 22.02           C  
ATOM    782  NE2 HIS A 103      -4.032   4.160  13.036  1.00 21.30           N  
ATOM    783  N   CYS A 104       0.471   5.217  14.595  1.00 20.04           N  
ATOM    784  CA  CYS A 104       0.374   5.030  16.083  1.00 20.45           C  
ATOM    785  C   CYS A 104       0.941   6.217  16.890  1.00 19.07           C  
ATOM    786  O   CYS A 104       0.455   6.528  17.956  1.00 20.11           O  
ATOM    787  CB  CYS A 104       1.111   3.746  16.508  1.00 20.20           C  
ATOM    788  SG  CYS A 104       0.250   2.296  15.848  1.00 22.06           S  
ATOM    789  N   LEU A 105       1.981   6.849  16.405  1.00 19.63           N  
ATOM    790  CA  LEU A 105       2.450   8.085  17.019  1.00 21.05           C  
ATOM    791  C   LEU A 105       1.369   9.178  16.928  1.00 21.24           C  
ATOM    792  O   LEU A 105       1.154   9.915  17.920  1.00 20.45           O  
ATOM    793  CB  LEU A 105       3.721   8.589  16.331  1.00 19.06           C  
ATOM    794  CG  LEU A 105       4.994   7.788  16.658  1.00 22.27           C  
ATOM    795  CD1 LEU A 105       6.113   8.132  15.651  1.00 20.42           C  
ATOM    796  CD2 LEU A 105       5.397   8.035  18.101  1.00 19.46           C  
ATOM    797  N   LEU A 106       0.686   9.284  15.787  1.00 23.19           N  
ATOM    798  CA  LEU A 106      -0.433  10.222  15.679  1.00 23.56           C  
ATOM    799  C   LEU A 106      -1.597   9.883  16.602  1.00 29.84           C  
ATOM    800  O   LEU A 106      -2.182  10.784  17.247  1.00 24.10           O  
ATOM    801  CB  LEU A 106      -0.996  10.325  14.248  1.00 23.02           C  
ATOM    802  CG  LEU A 106      -0.263  11.020  13.125  1.00 24.24           C  
ATOM    803  CD1 LEU A 106      -1.053  11.040  11.780  1.00 24.89           C  
ATOM    804  CD2 LEU A 106       0.160  12.438  13.549  1.00 25.35           C  
ATOM    805  N   VAL A 107      -1.977   8.604  16.649  1.00 24.45           N  
ATOM    806  CA  VAL A 107      -3.042   8.194  17.573  1.00 22.31           C  
ATOM    807  C   VAL A 107      -2.683   8.589  19.007  1.00 23.55           C  
ATOM    808  O   VAL A 107      -3.581   8.997  19.719  1.00 24.54           O  
ATOM    809  CB  VAL A 107      -3.354   6.639  17.439  1.00 23.25           C  
ATOM    810  CG1 VAL A 107      -4.292   6.100  18.530  1.00 23.89           C  
ATOM    811  CG2 VAL A 107      -3.871   6.320  16.025  1.00 21.07           C  
ATOM    812  N   THR A 108      -1.435   8.393  19.417  1.00 22.47           N  
ATOM    813  CA  THR A 108      -0.991   8.585  20.790  1.00 26.17           C  
ATOM    814  C   THR A 108      -1.112  10.114  21.143  1.00 26.91           C  
ATOM    815  O   THR A 108      -1.599  10.465  22.208  1.00 22.08           O  
ATOM    816  CB  THR A 108       0.471   8.120  20.943  1.00 22.66           C  
ATOM    817  OG1 THR A 108       0.571   6.669  20.718  1.00 25.00           O  
ATOM    818  CG2 THR A 108       0.999   8.395  22.345  1.00 23.46           C  
ATOM    819  N   LEU A 109      -0.653  10.961  20.223  1.00 23.07           N  
ATOM    820  CA  LEU A 109      -0.840  12.419  20.360  1.00 26.29           C  
ATOM    821  C   LEU A 109      -2.275  12.827  20.469  1.00 24.83           C  
ATOM    822  O   LEU A 109      -2.601  13.683  21.353  1.00 26.60           O  
ATOM    823  CB  LEU A 109      -0.184  13.155  19.193  1.00 27.47           C  
ATOM    824  CG  LEU A 109       1.365  13.031  19.156  1.00 31.48           C  
ATOM    825  CD1 LEU A 109       1.989  13.818  17.990  1.00 35.69           C  
ATOM    826  CD2 LEU A 109       1.995  13.467  20.478  1.00 34.88           C  
ATOM    827  N   ALA A 110      -3.128  12.246  19.626  1.00 24.01           N  
ATOM    828  CA  ALA A 110      -4.549  12.572  19.586  1.00 28.36           C  
ATOM    829  C   ALA A 110      -5.161  12.199  20.950  1.00 31.98           C  
ATOM    830  O   ALA A 110      -6.007  12.934  21.503  1.00 27.52           O  
ATOM    831  CB  ALA A 110      -5.262  11.875  18.421  1.00 27.42           C  
ATOM    832  N   ALA A 111      -4.732  11.052  21.492  1.00 26.03           N  
ATOM    833  CA  ALA A 111      -5.296  10.558  22.729  1.00 28.35           C  
ATOM    834  C   ALA A 111      -4.867  11.405  23.924  1.00 30.47           C  
ATOM    835  O   ALA A 111      -5.473  11.317  24.977  1.00 29.76           O  
ATOM    836  CB  ALA A 111      -4.865   9.067  22.959  1.00 24.84           C  
ATOM    837  N   HIS A 112      -3.746  12.078  23.809  1.00 29.97           N  
ATOM    838  CA  HIS A 112      -3.269  12.929  24.873  1.00 32.13           C  
ATOM    839  C   HIS A 112      -3.379  14.447  24.698  1.00 33.01           C  
ATOM    840  O   HIS A 112      -3.273  15.124  25.713  1.00 37.01           O  
ATOM    841  CB  HIS A 112      -1.808  12.623  25.218  1.00 30.15           C  
ATOM    842  CG  HIS A 112      -1.591  11.282  25.792  1.00 31.98           C  
ATOM    843  ND1 HIS A 112      -1.775  11.002  27.137  1.00 30.52           N  
ATOM    844  CD2 HIS A 112      -1.200  10.118  25.210  1.00 30.00           C  
ATOM    845  CE1 HIS A 112      -1.437   9.742  27.367  1.00 33.34           C  
ATOM    846  NE2 HIS A 112      -1.101   9.179  26.209  1.00 27.21           N  
ATOM    847  N   LEU A 113      -3.655  14.964  23.500  1.00 29.01           N  
ATOM    848  CA  LEU A 113      -3.763  16.443  23.233  1.00 34.82           C  
ATOM    849  C   LEU A 113      -5.087  16.880  22.663  1.00 35.78           C  
ATOM    850  O   LEU A 113      -5.185  17.311  21.505  1.00 41.88           O  
ATOM    851  CB  LEU A 113      -2.690  16.940  22.266  1.00 35.96           C  
ATOM    852  CG  LEU A 113      -1.245  16.495  22.527  1.00 41.74           C  
ATOM    853  CD1 LEU A 113      -0.403  16.897  21.292  1.00 41.93           C  
ATOM    854  CD2 LEU A 113      -0.607  16.970  23.846  1.00 43.40           C  
ATOM    855  N   PRO A 114      -6.138  16.783  23.459  1.00 34.92           N  
ATOM    856  CA  PRO A 114      -7.423  17.199  22.913  1.00 37.19           C  
ATOM    857  C   PRO A 114      -7.293  18.581  22.236  1.00 37.92           C  
ATOM    858  O   PRO A 114      -7.647  18.748  21.033  1.00 34.63           O  
ATOM    859  CB  PRO A 114      -8.329  17.254  24.161  1.00 36.43           C  
ATOM    860  CG  PRO A 114      -7.467  16.881  25.350  1.00 39.72           C  
ATOM    861  CD  PRO A 114      -6.237  16.224  24.807  1.00 34.80           C  
ATOM    862  N   ALA A 115      -6.722  19.542  22.960  1.00 37.74           N  
ATOM    863  CA  ALA A 115      -6.663  20.922  22.423  1.00 37.90           C  
ATOM    864  C   ALA A 115      -5.715  21.061  21.192  1.00 32.09           C  
ATOM    865  O   ALA A 115      -6.103  21.663  20.194  1.00 36.28           O  
ATOM    866  CB  ALA A 115      -6.312  21.926  23.525  1.00 32.39           C  
ATOM    867  N   GLU A 116      -4.529  20.455  21.241  1.00 31.14           N  
ATOM    868  CA  GLU A 116      -3.518  20.677  20.190  1.00 32.37           C  
ATOM    869  C   GLU A 116      -3.781  19.918  18.912  1.00 32.38           C  
ATOM    870  O   GLU A 116      -3.406  20.364  17.826  1.00 34.68           O  
ATOM    871  CB  GLU A 116      -2.113  20.388  20.696  1.00 37.73           C  
ATOM    872  CG  GLU A 116      -1.638  21.449  21.701  1.00 42.67           C  
ATOM    873  CD  GLU A 116      -2.370  21.371  23.029  1.00 49.36           C  
ATOM    874  OE1 GLU A 116      -2.585  20.232  23.537  1.00 54.96           O  
ATOM    875  OE2 GLU A 116      -2.709  22.439  23.588  0.50 46.52           O  
ATOM    876  N   PHE A 117      -4.515  18.812  18.995  1.00 27.69           N  
ATOM    877  CA  PHE A 117      -4.705  17.961  17.790  1.00 25.75           C  
ATOM    878  C   PHE A 117      -5.853  18.390  16.827  1.00 29.86           C  
ATOM    879  O   PHE A 117      -6.772  17.638  16.531  1.00 29.31           O  
ATOM    880  CB  PHE A 117      -4.796  16.479  18.252  1.00 22.73           C  
ATOM    881  CG  PHE A 117      -4.536  15.488  17.134  1.00 22.91           C  
ATOM    882  CD1 PHE A 117      -3.212  15.219  16.729  1.00 24.80           C  
ATOM    883  CD2 PHE A 117      -5.569  14.828  16.506  1.00 22.14           C  
ATOM    884  CE1 PHE A 117      -2.964  14.325  15.692  1.00 24.65           C  
ATOM    885  CE2 PHE A 117      -5.313  13.903  15.463  1.00 21.96           C  
ATOM    886  CZ  PHE A 117      -4.004  13.670  15.067  1.00 21.02           C  
ATOM    887  N   THR A 118      -5.818  19.651  16.354  1.00 28.86           N  
ATOM    888  CA  THR A 118      -6.820  20.138  15.446  1.00 29.41           C  
ATOM    889  C   THR A 118      -6.516  19.600  14.060  1.00 30.63           C  
ATOM    890  O   THR A 118      -5.411  19.081  13.847  1.00 27.46           O  
ATOM    891  CB  THR A 118      -6.648  21.653  15.251  1.00 33.02           C  
ATOM    892  OG1 THR A 118      -5.320  21.890  14.736  1.00 28.16           O  
ATOM    893  CG2 THR A 118      -6.788  22.359  16.605  1.00 31.62           C  
ATOM    894  N   PRO A 119      -7.469  19.760  13.104  1.00 31.02           N  
ATOM    895  CA  PRO A 119      -7.170  19.289  11.743  1.00 28.51           C  
ATOM    896  C   PRO A 119      -5.871  19.834  11.119  1.00 30.67           C  
ATOM    897  O   PRO A 119      -5.126  19.048  10.536  1.00 25.86           O  
ATOM    898  CB  PRO A 119      -8.441  19.608  10.969  1.00 28.28           C  
ATOM    899  CG  PRO A 119      -9.539  19.556  12.062  1.00 24.21           C  
ATOM    900  CD  PRO A 119      -8.897  20.199  13.228  1.00 27.71           C  
ATOM    901  N   ALA A 120      -5.543  21.128  11.301  1.00 26.33           N  
ATOM    902  CA  ALA A 120      -4.310  21.689  10.685  1.00 30.11           C  
ATOM    903  C   ALA A 120      -3.057  21.042  11.321  1.00 26.72           C  
ATOM    904  O   ALA A 120      -2.110  20.626  10.630  1.00 22.51           O  
ATOM    905  CB  ALA A 120      -4.265  23.238  10.788  1.00 27.19           C  
ATOM    906  N   VAL A 121      -3.142  20.824  12.628  1.00 25.88           N  
ATOM    907  CA  VAL A 121      -2.009  20.361  13.366  1.00 27.57           C  
ATOM    908  C   VAL A 121      -1.780  18.849  13.056  1.00 25.22           C  
ATOM    909  O   VAL A 121      -0.663  18.413  12.952  1.00 23.90           O  
ATOM    910  CB  VAL A 121      -2.203  20.644  14.876  1.00 27.03           C  
ATOM    911  CG1 VAL A 121      -1.141  19.908  15.686  1.00 30.94           C  
ATOM    912  CG2 VAL A 121      -1.997  22.132  15.131  1.00 32.86           C  
ATOM    913  N   HIS A 122      -2.867  18.112  12.919  1.00 22.69           N  
ATOM    914  CA  HIS A 122      -2.843  16.687  12.481  1.00 23.40           C  
ATOM    915  C   HIS A 122      -2.163  16.612  11.094  1.00 24.45           C  
ATOM    916  O   HIS A 122      -1.299  15.801  10.892  1.00 22.19           O  
ATOM    917  CB  HIS A 122      -4.287  16.246  12.480  1.00 21.85           C  
ATOM    918  CG  HIS A 122      -4.575  14.883  11.909  1.00 23.36           C  
ATOM    919  ND1 HIS A 122      -5.855  14.369  11.889  1.00 23.36           N  
ATOM    920  CD2 HIS A 122      -3.776  13.914  11.381  1.00 21.86           C  
ATOM    921  CE1 HIS A 122      -5.846  13.143  11.389  1.00 20.72           C  
ATOM    922  NE2 HIS A 122      -4.594  12.874  11.016  1.00 21.14           N  
ATOM    923  N   ALA A 123      -2.563  17.494  10.166  1.00 25.89           N  
ATOM    924  CA  ALA A 123      -1.923  17.575   8.857  1.00 24.65           C  
ATOM    925  C   ALA A 123      -0.463  17.839   8.988  1.00 22.60           C  
ATOM    926  O   ALA A 123       0.323  17.110   8.349  1.00 21.95           O  
ATOM    927  CB  ALA A 123      -2.583  18.602   7.931  1.00 22.48           C  
ATOM    928  N   SER A 124      -0.057  18.835   9.814  1.00 20.85           N  
ATOM    929  CA  SER A 124       1.344  19.162   9.912  1.00 20.99           C  
ATOM    930  C   SER A 124       2.154  17.989  10.513  1.00 24.96           C  
ATOM    931  O   SER A 124       3.258  17.734  10.088  1.00 25.14           O  
ATOM    932  CB  SER A 124       1.659  20.463  10.678  1.00 25.63           C  
ATOM    933  OG  SER A 124       0.846  21.507  10.185  1.00 27.08           O  
ATOM    934  N   LEU A 125       1.618  17.330  11.545  1.00 22.53           N  
ATOM    935  CA  LEU A 125       2.342  16.214  12.156  1.00 20.30           C  
ATOM    936  C   LEU A 125       2.444  15.029  11.236  1.00 20.40           C  
ATOM    937  O   LEU A 125       3.530  14.371  11.174  1.00 21.11           O  
ATOM    938  CB  LEU A 125       1.549  15.749  13.380  1.00 21.46           C  
ATOM    939  CG  LEU A 125       1.566  16.684  14.579  1.00 24.07           C  
ATOM    940  CD1 LEU A 125       0.515  16.326  15.590  1.00 23.82           C  
ATOM    941  CD2 LEU A 125       2.920  16.683  15.243  1.00 25.76           C  
ATOM    942  N   ASP A 126       1.351  14.745  10.518  1.00 19.29           N  
ATOM    943  CA  ASP A 126       1.454  13.712   9.459  1.00 22.03           C  
ATOM    944  C   ASP A 126       2.570  13.983   8.487  1.00 22.15           C  
ATOM    945  O   ASP A 126       3.327  13.072   8.139  1.00 22.28           O  
ATOM    946  CB  ASP A 126       0.145  13.526   8.706  1.00 23.13           C  
ATOM    947  CG  ASP A 126       0.209  12.356   7.691  1.00 28.55           C  
ATOM    948  OD1 ASP A 126       0.324  12.640   6.483  1.00 35.38           O  
ATOM    949  OD2 ASP A 126       0.194  11.207   8.123  1.00 34.73           O  
ATOM    950  N   LYS A 127       2.699  15.218   8.020  1.00 21.27           N  
ATOM    951  CA  LYS A 127       3.787  15.579   7.092  1.00 22.12           C  
ATOM    952  C   LYS A 127       5.140  15.460   7.715  1.00 20.51           C  
ATOM    953  O   LYS A 127       6.072  15.025   7.068  1.00 20.55           O  
ATOM    954  CB  LYS A 127       3.648  17.019   6.553  1.00 24.97           C  
ATOM    955  CG  LYS A 127       2.502  17.155   5.554  1.00 27.79           C  
ATOM    956  CD  LYS A 127       2.473  18.557   4.950  1.00 35.28           C  
ATOM    957  CE  LYS A 127       1.058  19.170   4.943  1.00 42.81           C  
ATOM    958  NZ  LYS A 127      -0.055  18.253   4.500  1.00 36.67           N  
ATOM    959  N   PHE A 128       5.260  15.862   8.977  1.00 21.41           N  
ATOM    960  CA  PHE A 128       6.543  15.718   9.711  1.00 20.79           C  
ATOM    961  C   PHE A 128       6.958  14.242   9.803  1.00 20.61           C  
ATOM    962  O   PHE A 128       8.077  13.883   9.527  1.00 19.46           O  
ATOM    963  CB  PHE A 128       6.406  16.354  11.134  1.00 22.14           C  
ATOM    964  CG  PHE A 128       7.564  16.031  12.060  1.00 23.04           C  
ATOM    965  CD1 PHE A 128       8.806  16.535  11.830  1.00 22.14           C  
ATOM    966  CD2 PHE A 128       7.383  15.151  13.129  1.00 25.32           C  
ATOM    967  CE1 PHE A 128       9.901  16.201  12.661  1.00 26.36           C  
ATOM    968  CE2 PHE A 128       8.434  14.838  13.963  1.00 24.20           C  
ATOM    969  CZ  PHE A 128       9.691  15.372  13.743  1.00 24.58           C  
ATOM    970  N   LEU A 129       6.009  13.386  10.196  1.00 20.50           N  
ATOM    971  CA  LEU A 129       6.369  11.955  10.383  1.00 19.88           C  
ATOM    972  C   LEU A 129       6.664  11.315   9.046  1.00 20.15           C  
ATOM    973  O   LEU A 129       7.594  10.501   8.916  1.00 20.91           O  
ATOM    974  CB  LEU A 129       5.221  11.223  11.106  1.00 21.44           C  
ATOM    975  CG  LEU A 129       5.019  11.683  12.584  1.00 21.53           C  
ATOM    976  CD1 LEU A 129       3.738  11.099  13.202  1.00 23.71           C  
ATOM    977  CD2 LEU A 129       6.298  11.445  13.422  1.00 20.99           C  
ATOM    978  N   ALA A 130       5.924  11.737   8.017  1.00 19.92           N  
ATOM    979  CA  ALA A 130       6.258  11.235   6.648  1.00 23.23           C  
ATOM    980  C   ALA A 130       7.659  11.697   6.191  1.00 21.13           C  
ATOM    981  O   ALA A 130       8.450  10.896   5.560  1.00 22.63           O  
ATOM    982  CB  ALA A 130       5.199  11.697   5.634  1.00 23.51           C  
ATOM    983  N   SER A 131       8.027  12.944   6.510  1.00 20.90           N  
ATOM    984  CA  SER A 131       9.416  13.377   6.217  1.00 23.03           C  
ATOM    985  C   SER A 131      10.474  12.587   6.987  1.00 22.89           C  
ATOM    986  O   SER A 131      11.522  12.262   6.422  1.00 23.02           O  
ATOM    987  CB  SER A 131       9.676  14.844   6.555  1.00 26.26           C  
ATOM    988  OG  SER A 131       8.704  15.671   5.917  1.00 39.41           O  
ATOM    989  N   VAL A 132      10.236  12.334   8.281  1.00 22.21           N  
ATOM    990  CA  VAL A 132      11.162  11.510   9.016  1.00 20.93           C  
ATOM    991  C   VAL A 132      11.231  10.116   8.397  1.00 22.49           C  
ATOM    992  O   VAL A 132      12.365   9.585   8.241  1.00 24.98           O  
ATOM    993  CB  VAL A 132      10.738  11.387  10.487  1.00 23.87           C  
ATOM    994  CG1 VAL A 132      11.528  10.295  11.253  1.00 21.72           C  
ATOM    995  CG2 VAL A 132      10.831  12.783  11.173  1.00 21.03           C  
ATOM    996  N   SER A 133      10.068   9.503   8.124  1.00 21.75           N  
ATOM    997  CA  SER A 133      10.003   8.220   7.414  1.00 21.11           C  
ATOM    998  C   SER A 133      10.812   8.176   6.060  1.00 21.55           C  
ATOM    999  O   SER A 133      11.542   7.207   5.791  1.00 23.04           O  
ATOM   1000  CB  SER A 133       8.557   7.786   7.212  1.00 21.26           C  
ATOM   1001  OG  SER A 133       7.943   7.593   8.555  1.00 22.41           O  
ATOM   1002  N   THR A 134      10.686   9.215   5.264  1.00 23.47           N  
ATOM   1003  CA  THR A 134      11.446   9.362   4.004  1.00 27.49           C  
ATOM   1004  C   THR A 134      12.941   9.315   4.279  1.00 26.78           C  
ATOM   1005  O   THR A 134      13.662   8.505   3.660  1.00 25.75           O  
ATOM   1006  CB  THR A 134      11.027  10.631   3.273  1.00 24.21           C  
ATOM   1007  OG1 THR A 134       9.668  10.500   2.925  1.00 28.99           O  
ATOM   1008  CG2 THR A 134      11.864  10.947   1.960  1.00 28.04           C  
ATOM   1009  N   VAL A 135      13.414  10.118   5.257  1.00 24.81           N  
ATOM   1010  CA  VAL A 135      14.801  10.034   5.661  1.00 22.54           C  
ATOM   1011  C   VAL A 135      15.234   8.663   6.114  1.00 25.89           C  
ATOM   1012  O   VAL A 135      16.283   8.162   5.683  1.00 26.80           O  
ATOM   1013  CB  VAL A 135      15.205  11.078   6.731  1.00 23.45           C  
ATOM   1014  CG1 VAL A 135      16.676  10.842   7.125  1.00 24.77           C  
ATOM   1015  CG2 VAL A 135      14.942  12.485   6.138  1.00 23.99           C  
ATOM   1016  N   LEU A 136      14.451   8.063   7.001  1.00 25.69           N  
ATOM   1017  CA  LEU A 136      14.807   6.780   7.572  1.00 28.66           C  
ATOM   1018  C   LEU A 136      14.793   5.620   6.536  1.00 25.62           C  
ATOM   1019  O   LEU A 136      15.428   4.598   6.735  1.00 27.43           O  
ATOM   1020  CB  LEU A 136      13.891   6.480   8.774  1.00 25.82           C  
ATOM   1021  CG  LEU A 136      14.288   7.411   9.952  1.00 29.57           C  
ATOM   1022  CD1 LEU A 136      13.413   7.128  11.161  1.00 28.38           C  
ATOM   1023  CD2 LEU A 136      15.735   7.154  10.379  1.00 32.65           C  
ATOM   1024  N   THR A 137      14.117   5.799   5.424  1.00 29.07           N  
ATOM   1025  CA  THR A 137      14.146   4.736   4.408  1.00 31.57           C  
ATOM   1026  C   THR A 137      14.985   5.125   3.185  1.00 32.48           C  
ATOM   1027  O   THR A 137      14.848   4.514   2.122  1.00 31.67           O  
ATOM   1028  CB  THR A 137      12.762   4.474   3.877  1.00 30.40           C  
ATOM   1029  OG1 THR A 137      12.228   5.719   3.411  1.00 30.80           O  
ATOM   1030  CG2 THR A 137      11.831   3.835   4.939  1.00 33.48           C  
ATOM   1031  N   SER A 138      15.841   6.119   3.319  1.00 36.19           N  
ATOM   1032  CA  SER A 138      16.445   6.704   2.122  1.00 42.31           C  
ATOM   1033  C   SER A 138      17.669   5.897   1.724  1.00 39.93           C  
ATOM   1034  O   SER A 138      18.161   6.004   0.610  1.00 47.70           O  
ATOM   1035  CB  SER A 138      16.815   8.161   2.357  1.00 38.32           C  
ATOM   1036  OG  SER A 138      17.699   8.260   3.449  1.00 38.45           O  
ATOM   1037  N   LYS A 139      18.131   5.075   2.642  1.00 41.30           N  
ATOM   1038  CA  LYS A 139      19.410   4.414   2.507  1.00 46.95           C  
ATOM   1039  C   LYS A 139      19.449   2.911   2.111  1.00 50.80           C  
ATOM   1040  O   LYS A 139      20.483   2.293   2.356  1.00 52.58           O  
ATOM   1041  CB  LYS A 139      20.258   4.627   3.790  1.00 48.79           C  
ATOM   1042  CG  LYS A 139      20.380   6.077   4.279  1.00 55.28           C  
ATOM   1043  CD  LYS A 139      21.516   6.865   3.629  1.00 50.95           C  
ATOM   1044  CE  LYS A 139      21.691   8.239   4.280  1.00 48.51           C  
ATOM   1045  NZ  LYS A 139      22.486   8.195   5.535  1.00 48.31           N  
ATOM   1046  N   TYR A 140      18.405   2.319   1.501  1.00 51.71           N  
ATOM   1047  CA  TYR A 140      18.480   0.848   1.167  1.00 58.70           C  
ATOM   1048  C   TYR A 140      19.543   0.512   0.090  1.00 68.25           C  
ATOM   1049  O   TYR A 140      19.722   1.276  -0.863  1.00 72.78           O  
ATOM   1050  CB  TYR A 140      17.119   0.192   0.772  1.00 46.71           C  
ATOM   1051  CG  TYR A 140      16.062   0.208   1.852  1.00 36.13           C  
ATOM   1052  CD1 TYR A 140      15.007   1.103   1.771  1.00 34.73           C  
ATOM   1053  CD2 TYR A 140      16.152  -0.631   2.989  1.00 32.80           C  
ATOM   1054  CE1 TYR A 140      14.047   1.153   2.751  1.00 33.89           C  
ATOM   1055  CE2 TYR A 140      15.200  -0.558   4.014  1.00 31.40           C  
ATOM   1056  CZ  TYR A 140      14.153   0.327   3.867  1.00 33.05           C  
ATOM   1057  OH  TYR A 140      13.214   0.428   4.857  1.00 42.33           O  
TER    1058      TYR A 140                                                      
ATOM   1059  N   VAL B   1     -14.136 -10.358   8.944  1.00 47.47           N  
ATOM   1060  CA  VAL B   1     -13.030 -10.415   9.949  1.00 53.77           C  
ATOM   1061  C   VAL B   1     -13.557 -11.050  11.246  1.00 51.77           C  
ATOM   1062  O   VAL B   1     -14.729 -10.869  11.629  1.00 52.40           O  
ATOM   1063  CB  VAL B   1     -12.427  -8.998  10.192  1.00 58.52           C  
ATOM   1064  CG1 VAL B   1     -13.452  -8.086  10.841  1.00 55.87           C  
ATOM   1065  CG2 VAL B   1     -11.136  -9.054  11.021  1.00 59.97           C  
ATOM   1066  N   HIS B   2     -12.695 -11.806  11.901  1.00 48.55           N  
ATOM   1067  CA  HIS B   2     -13.032 -12.390  13.194  1.00 55.54           C  
ATOM   1068  C   HIS B   2     -12.442 -11.555  14.343  1.00 50.55           C  
ATOM   1069  O   HIS B   2     -11.218 -11.459  14.513  1.00 50.78           O  
ATOM   1070  CB  HIS B   2     -12.579 -13.865  13.268  1.00 53.88           C  
ATOM   1071  CG  HIS B   2     -13.203 -14.747  12.229  0.50 52.08           C  
ATOM   1072  ND1 HIS B   2     -14.534 -15.118  12.266  0.50 51.98           N  
ATOM   1073  CD2 HIS B   2     -12.677 -15.335  11.126  0.50 50.22           C  
ATOM   1074  CE1 HIS B   2     -14.800 -15.890  11.226  0.50 53.74           C  
ATOM   1075  NE2 HIS B   2     -13.691 -16.038  10.520  0.50 51.81           N  
ATOM   1076  N   LEU B   3     -13.313 -10.909  15.114  1.00 45.91           N  
ATOM   1077  CA  LEU B   3     -12.868 -10.301  16.356  1.00 40.36           C  
ATOM   1078  C   LEU B   3     -13.123 -11.312  17.487  1.00 43.48           C  
ATOM   1079  O   LEU B   3     -14.116 -12.034  17.442  1.00 46.75           O  
ATOM   1080  CB  LEU B   3     -13.649  -9.034  16.613  1.00 40.35           C  
ATOM   1081  CG  LEU B   3     -13.011  -7.759  16.060  1.00 40.72           C  
ATOM   1082  CD1 LEU B   3     -12.690  -7.889  14.581  1.00 39.20           C  
ATOM   1083  CD2 LEU B   3     -14.017  -6.675  16.319  1.00 38.60           C  
ATOM   1084  N   THR B   4     -12.220 -11.390  18.465  1.00 45.48           N  
ATOM   1085  CA  THR B   4     -12.499 -12.128  19.700  1.00 41.38           C  
ATOM   1086  C   THR B   4     -13.701 -11.473  20.409  1.00 40.97           C  
ATOM   1087  O   THR B   4     -14.091 -10.333  20.071  1.00 40.45           O  
ATOM   1088  CB  THR B   4     -11.334 -12.121  20.681  1.00 40.14           C  
ATOM   1089  OG1 THR B   4     -11.160 -10.780  21.165  1.00 41.00           O  
ATOM   1090  CG2 THR B   4     -10.032 -12.739  20.081  1.00 39.72           C  
ATOM   1091  N   PRO B   5     -14.334 -12.199  21.382  1.00 35.77           N  
ATOM   1092  CA  PRO B   5     -15.414 -11.527  22.135  1.00 31.40           C  
ATOM   1093  C   PRO B   5     -14.899 -10.294  22.936  1.00 30.54           C  
ATOM   1094  O   PRO B   5     -15.592  -9.284  22.983  1.00 33.87           O  
ATOM   1095  CB  PRO B   5     -15.977 -12.651  23.039  1.00 36.21           C  
ATOM   1096  CG  PRO B   5     -15.626 -13.931  22.303  1.00 30.18           C  
ATOM   1097  CD  PRO B   5     -14.334 -13.675  21.538  1.00 32.16           C  
ATOM   1098  N   GLU B   6     -13.670 -10.352  23.488  1.00 32.49           N  
ATOM   1099  CA  GLU B   6     -13.018  -9.178  24.057  1.00 35.18           C  
ATOM   1100  C   GLU B   6     -12.784  -8.025  23.029  1.00 31.78           C  
ATOM   1101  O   GLU B   6     -12.938  -6.879  23.365  1.00 33.72           O  
ATOM   1102  CB  GLU B   6     -11.757  -9.548  24.817  1.00 43.24           C  
ATOM   1103  CG  GLU B   6     -11.947  -9.498  26.333  1.00 54.87           C  
ATOM   1104  CD  GLU B   6     -11.261 -10.621  27.118  1.00 67.53           C  
ATOM   1105  OE1 GLU B   6     -11.909 -11.155  28.071  1.00 71.02           O  
ATOM   1106  OE2 GLU B   6     -10.089 -10.964  26.802  1.00 68.75           O  
ATOM   1107  N   GLU B   7     -12.467  -8.336  21.786  1.00 35.15           N  
ATOM   1108  CA  GLU B   7     -12.356  -7.290  20.747  1.00 33.65           C  
ATOM   1109  C   GLU B   7     -13.711  -6.744  20.421  1.00 34.75           C  
ATOM   1110  O   GLU B   7     -13.906  -5.495  20.306  1.00 36.61           O  
ATOM   1111  CB  GLU B   7     -11.697  -7.881  19.482  1.00 37.29           C  
ATOM   1112  CG  GLU B   7     -10.189  -7.955  19.606  1.00 39.66           C  
ATOM   1113  CD  GLU B   7      -9.519  -8.887  18.614  1.00 41.04           C  
ATOM   1114  OE1 GLU B   7      -8.281  -8.949  18.638  1.00 55.67           O  
ATOM   1115  OE2 GLU B   7     -10.175  -9.553  17.786  1.00 37.47           O  
ATOM   1116  N   LYS B   8     -14.678  -7.659  20.266  1.00 33.02           N  
ATOM   1117  CA  LYS B   8     -16.021  -7.237  19.955  1.00 31.68           C  
ATOM   1118  C   LYS B   8     -16.501  -6.326  21.049  1.00 34.87           C  
ATOM   1119  O   LYS B   8     -17.121  -5.286  20.799  1.00 33.59           O  
ATOM   1120  CB  LYS B   8     -16.977  -8.405  19.811  1.00 35.78           C  
ATOM   1121  CG  LYS B   8     -16.966  -9.069  18.439  1.00 42.50           C  
ATOM   1122  CD  LYS B   8     -17.567 -10.459  18.608  1.00 48.82           C  
ATOM   1123  CE  LYS B   8     -17.427 -11.353  17.389  1.00 51.84           C  
ATOM   1124  NZ  LYS B   8     -18.723 -12.076  17.312  1.00 52.39           N  
ATOM   1125  N   SER B   9     -16.160  -6.692  22.273  1.00 39.19           N  
ATOM   1126  CA  SER B   9     -16.652  -5.965  23.426  1.00 43.25           C  
ATOM   1127  C   SER B   9     -16.100  -4.520  23.419  1.00 45.46           C  
ATOM   1128  O   SER B   9     -16.840  -3.539  23.607  1.00 43.86           O  
ATOM   1129  CB  SER B   9     -16.216  -6.697  24.689  1.00 40.43           C  
ATOM   1130  OG  SER B   9     -16.586  -5.931  25.810  1.00 44.69           O  
ATOM   1131  N   ALA B  10     -14.808  -4.416  23.132  1.00 43.83           N  
ATOM   1132  CA  ALA B  10     -14.105  -3.133  23.075  1.00 42.49           C  
ATOM   1133  C   ALA B  10     -14.720  -2.193  22.043  1.00 41.12           C  
ATOM   1134  O   ALA B  10     -14.927  -1.016  22.309  1.00 47.57           O  
ATOM   1135  CB  ALA B  10     -12.627  -3.368  22.821  1.00 42.66           C  
ATOM   1136  N   VAL B  11     -15.087  -2.746  20.899  1.00 37.01           N  
ATOM   1137  CA  VAL B  11     -15.569  -1.991  19.770  1.00 38.49           C  
ATOM   1138  C   VAL B  11     -16.943  -1.454  20.079  1.00 36.77           C  
ATOM   1139  O   VAL B  11     -17.167  -0.220  20.033  1.00 35.90           O  
ATOM   1140  CB  VAL B  11     -15.532  -2.839  18.460  1.00 39.45           C  
ATOM   1141  CG1 VAL B  11     -16.317  -2.152  17.356  1.00 39.39           C  
ATOM   1142  CG2 VAL B  11     -14.084  -3.031  18.027  1.00 38.52           C  
ATOM   1143  N   THR B  12     -17.845  -2.355  20.465  1.00 35.83           N  
ATOM   1144  CA  THR B  12     -19.253  -1.952  20.634  1.00 37.50           C  
ATOM   1145  C   THR B  12     -19.422  -1.050  21.854  1.00 33.39           C  
ATOM   1146  O   THR B  12     -20.166  -0.103  21.778  1.00 37.66           O  
ATOM   1147  CB  THR B  12     -20.253  -3.146  20.665  1.00 39.39           C  
ATOM   1148  OG1 THR B  12     -19.810  -4.055  21.639  1.00 44.37           O  
ATOM   1149  CG2 THR B  12     -20.282  -3.910  19.350  1.00 41.03           C  
ATOM   1150  N   ALA B  13     -18.730  -1.300  22.955  1.00 34.79           N  
ATOM   1151  CA  ALA B  13     -18.873  -0.407  24.101  1.00 37.31           C  
ATOM   1152  C   ALA B  13     -18.498   1.058  23.712  1.00 35.49           C  
ATOM   1153  O   ALA B  13     -19.245   2.039  23.985  1.00 31.17           O  
ATOM   1154  CB  ALA B  13     -18.046  -0.897  25.285  1.00 38.99           C  
ATOM   1155  N   LEU B  14     -17.348   1.228  23.058  1.00 28.39           N  
ATOM   1156  CA  LEU B  14     -16.987   2.573  22.617  1.00 29.83           C  
ATOM   1157  C   LEU B  14     -17.975   3.134  21.626  1.00 28.61           C  
ATOM   1158  O   LEU B  14     -18.300   4.336  21.648  1.00 33.10           O  
ATOM   1159  CB  LEU B  14     -15.598   2.551  21.986  1.00 32.73           C  
ATOM   1160  CG  LEU B  14     -14.917   3.921  21.959  1.00 42.09           C  
ATOM   1161  CD1 LEU B  14     -14.437   4.271  23.355  1.00 45.99           C  
ATOM   1162  CD2 LEU B  14     -13.754   3.899  20.980  1.00 41.03           C  
ATOM   1163  N   TRP B  15     -18.428   2.305  20.693  1.00 34.48           N  
ATOM   1164  CA  TRP B  15     -19.232   2.830  19.581  1.00 34.14           C  
ATOM   1165  C   TRP B  15     -20.567   3.416  20.018  1.00 38.37           C  
ATOM   1166  O   TRP B  15     -21.042   4.375  19.403  1.00 42.77           O  
ATOM   1167  CB  TRP B  15     -19.465   1.786  18.521  1.00 35.10           C  
ATOM   1168  CG  TRP B  15     -19.837   2.382  17.168  1.00 40.54           C  
ATOM   1169  CD1 TRP B  15     -21.065   2.331  16.557  1.00 39.89           C  
ATOM   1170  CD2 TRP B  15     -18.962   3.057  16.226  1.00 41.83           C  
ATOM   1171  NE1 TRP B  15     -21.022   2.951  15.333  1.00 38.56           N  
ATOM   1172  CE2 TRP B  15     -19.752   3.408  15.104  1.00 40.84           C  
ATOM   1173  CE3 TRP B  15     -17.607   3.402  16.231  1.00 38.07           C  
ATOM   1174  CZ2 TRP B  15     -19.230   4.077  14.000  1.00 41.99           C  
ATOM   1175  CZ3 TRP B  15     -17.087   4.080  15.125  1.00 41.58           C  
ATOM   1176  CH2 TRP B  15     -17.896   4.383  14.011  1.00 36.89           C  
ATOM   1177  N   GLY B  16     -21.181   2.834  21.061  1.00 38.61           N  
ATOM   1178  CA  GLY B  16     -22.442   3.359  21.585  1.00 35.86           C  
ATOM   1179  C   GLY B  16     -22.244   4.757  22.109  1.00 35.49           C  
ATOM   1180  O   GLY B  16     -23.183   5.486  22.237  1.00 43.12           O  
ATOM   1181  N   LYS B  17     -21.012   5.157  22.405  1.00 35.84           N  
ATOM   1182  CA  LYS B  17     -20.786   6.502  22.873  1.00 33.78           C  
ATOM   1183  C   LYS B  17     -20.486   7.535  21.793  1.00 32.62           C  
ATOM   1184  O   LYS B  17     -20.291   8.721  22.082  1.00 34.24           O  
ATOM   1185  CB  LYS B  17     -19.675   6.525  23.923  1.00 40.86           C  
ATOM   1186  CG  LYS B  17     -20.056   5.808  25.210  1.00 42.57           C  
ATOM   1187  CD  LYS B  17     -19.064   6.104  26.311  1.00 46.86           C  
ATOM   1188  CE  LYS B  17     -18.968   4.896  27.222  1.00 48.95           C  
ATOM   1189  NZ  LYS B  17     -17.698   4.988  27.963  1.00 56.66           N  
ATOM   1190  N   VAL B  18     -20.409   7.081  20.552  1.00 35.43           N  
ATOM   1191  CA  VAL B  18     -20.004   7.956  19.438  1.00 34.18           C  
ATOM   1192  C   VAL B  18     -21.114   8.909  19.027  1.00 34.18           C  
ATOM   1193  O   VAL B  18     -22.242   8.440  18.856  1.00 34.82           O  
ATOM   1194  CB  VAL B  18     -19.559   7.096  18.208  1.00 33.25           C  
ATOM   1195  CG1 VAL B  18     -19.465   7.947  16.914  1.00 29.59           C  
ATOM   1196  CG2 VAL B  18     -18.251   6.396  18.535  1.00 31.33           C  
ATOM   1197  N   ASN B  19     -20.808  10.214  18.837  1.00 33.30           N  
ATOM   1198  CA  ASN B  19     -21.804  11.157  18.221  1.00 35.23           C  
ATOM   1199  C   ASN B  19     -21.904  10.946  16.737  1.00 35.43           C  
ATOM   1200  O   ASN B  19     -21.079  11.456  15.953  1.00 32.02           O  
ATOM   1201  CB  ASN B  19     -21.426  12.625  18.511  1.00 36.76           C  
ATOM   1202  CG  ASN B  19     -22.540  13.630  18.123  1.00 39.88           C  
ATOM   1203  OD1 ASN B  19     -23.238  13.477  17.122  1.00 38.08           O  
ATOM   1204  ND2 ASN B  19     -22.695  14.671  18.946  1.00 38.55           N  
ATOM   1205  N   VAL B  20     -22.915  10.192  16.315  1.00 38.39           N  
ATOM   1206  CA  VAL B  20     -23.052   9.847  14.910  1.00 34.26           C  
ATOM   1207  C   VAL B  20     -23.405  11.033  13.981  1.00 34.31           C  
ATOM   1208  O   VAL B  20     -23.266  10.947  12.786  1.00 32.74           O  
ATOM   1209  CB  VAL B  20     -24.069   8.695  14.719  1.00 41.27           C  
ATOM   1210  CG1 VAL B  20     -23.770   7.574  15.716  1.00 42.79           C  
ATOM   1211  CG2 VAL B  20     -25.502   9.217  14.902  1.00 40.34           C  
ATOM   1212  N   ASP B  21     -23.827  12.163  14.526  1.00 38.35           N  
ATOM   1213  CA  ASP B  21     -24.059  13.293  13.666  1.00 36.28           C  
ATOM   1214  C   ASP B  21     -22.759  14.084  13.409  1.00 37.22           C  
ATOM   1215  O   ASP B  21     -22.716  14.933  12.535  1.00 36.36           O  
ATOM   1216  CB  ASP B  21     -25.195  14.159  14.239  1.00 41.86           C  
ATOM   1217  CG  ASP B  21     -26.553  13.437  14.168  1.00 42.99           C  
ATOM   1218  OD1 ASP B  21     -26.882  12.842  13.128  1.00 44.55           O  
ATOM   1219  OD2 ASP B  21     -27.295  13.476  15.134  1.00 45.89           O  
ATOM   1220  N   GLU B  22     -21.712  13.770  14.170  1.00 32.88           N  
ATOM   1221  CA  GLU B  22     -20.477  14.559  14.171  1.00 35.78           C  
ATOM   1222  C   GLU B  22     -19.210  13.822  13.692  1.00 32.52           C  
ATOM   1223  O   GLU B  22     -18.371  14.379  12.979  1.00 30.96           O  
ATOM   1224  CB  GLU B  22     -20.229  15.114  15.594  1.00 44.47           C  
ATOM   1225  CG  GLU B  22     -21.300  16.093  16.057  1.00 47.39           C  
ATOM   1226  CD  GLU B  22     -21.632  17.114  14.981  1.00 57.60           C  
ATOM   1227  OE1 GLU B  22     -20.706  17.564  14.247  1.00 61.02           O  
ATOM   1228  OE2 GLU B  22     -22.833  17.462  14.853  1.00 67.88           O  
ATOM   1229  N   VAL B  23     -19.038  12.605  14.186  1.00 29.64           N  
ATOM   1230  CA  VAL B  23     -17.741  11.923  14.024  1.00 27.39           C  
ATOM   1231  C   VAL B  23     -17.413  11.634  12.565  1.00 29.73           C  
ATOM   1232  O   VAL B  23     -16.249  11.795  12.155  1.00 30.08           O  
ATOM   1233  CB  VAL B  23     -17.667  10.671  14.927  0.50 20.87           C  
ATOM   1234  CG1 VAL B  23     -16.532   9.752  14.508  0.50 19.45           C  
ATOM   1235  CG2 VAL B  23     -17.444  11.142  16.360  0.50 18.02           C  
ATOM   1236  N   GLY B  24     -18.389  11.163  11.803  1.00 30.16           N  
ATOM   1237  CA  GLY B  24     -18.266  11.068  10.332  1.00 32.07           C  
ATOM   1238  C   GLY B  24     -17.727  12.317   9.632  1.00 36.70           C  
ATOM   1239  O   GLY B  24     -16.822  12.251   8.744  1.00 34.82           O  
ATOM   1240  N   GLY B  25     -18.264  13.483   9.963  1.00 32.78           N  
ATOM   1241  CA  GLY B  25     -17.838  14.663   9.225  1.00 30.05           C  
ATOM   1242  C   GLY B  25     -16.474  15.081   9.708  1.00 30.32           C  
ATOM   1243  O   GLY B  25     -15.720  15.739   8.989  1.00 30.66           O  
ATOM   1244  N   GLU B  26     -16.164  14.753  10.952  1.00 29.38           N  
ATOM   1245  CA  GLU B  26     -14.845  15.076  11.465  1.00 31.81           C  
ATOM   1246  C   GLU B  26     -13.807  14.191  10.716  1.00 27.35           C  
ATOM   1247  O   GLU B  26     -12.754  14.686  10.321  1.00 25.98           O  
ATOM   1248  CB  GLU B  26     -14.770  14.909  13.002  1.00 36.39           C  
ATOM   1249  CG  GLU B  26     -13.385  15.233  13.602  1.00 36.31           C  
ATOM   1250  CD  GLU B  26     -13.146  16.716  13.836  1.00 47.31           C  
ATOM   1251  OE1 GLU B  26     -11.985  17.127  14.173  1.00 46.30           O  
ATOM   1252  OE2 GLU B  26     -14.125  17.497  13.683  1.00 54.36           O  
ATOM   1253  N   ALA B  27     -14.144  12.951  10.474  1.00 26.22           N  
ATOM   1254  CA  ALA B  27     -13.170  12.034   9.816  1.00 31.55           C  
ATOM   1255  C   ALA B  27     -13.002  12.367   8.316  1.00 31.16           C  
ATOM   1256  O   ALA B  27     -11.886  12.349   7.772  1.00 31.58           O  
ATOM   1257  CB  ALA B  27     -13.612  10.612   9.983  1.00 26.67           C  
ATOM   1258  N   LEU B  28     -14.106  12.671   7.642  1.00 30.49           N  
ATOM   1259  CA  LEU B  28     -14.040  13.117   6.239  1.00 28.40           C  
ATOM   1260  C   LEU B  28     -13.295  14.434   6.044  1.00 30.77           C  
ATOM   1261  O   LEU B  28     -12.439  14.527   5.103  1.00 29.92           O  
ATOM   1262  CB  LEU B  28     -15.410  13.207   5.581  1.00 30.38           C  
ATOM   1263  CG  LEU B  28     -15.354  13.775   4.145  1.00 27.59           C  
ATOM   1264  CD1 LEU B  28     -14.455  12.977   3.179  1.00 35.23           C  
ATOM   1265  CD2 LEU B  28     -16.780  13.885   3.576  1.00 31.27           C  
ATOM   1266  N   GLY B  29     -13.674  15.456   6.849  1.00 26.61           N  
ATOM   1267  CA  GLY B  29     -12.959  16.721   6.957  1.00 29.55           C  
ATOM   1268  C   GLY B  29     -11.468  16.481   7.086  1.00 31.29           C  
ATOM   1269  O   GLY B  29     -10.670  16.974   6.272  1.00 26.76           O  
ATOM   1270  N   ARG B  30     -11.066  15.673   8.086  1.00 28.49           N  
ATOM   1271  CA  ARG B  30      -9.638  15.519   8.324  1.00 24.14           C  
ATOM   1272  C   ARG B  30      -8.962  14.800   7.134  1.00 24.80           C  
ATOM   1273  O   ARG B  30      -7.848  15.171   6.757  1.00 24.52           O  
ATOM   1274  CB  ARG B  30      -9.405  14.787   9.646  1.00 25.70           C  
ATOM   1275  CG  ARG B  30      -9.407  15.736  10.851  1.00 24.96           C  
ATOM   1276  CD  ARG B  30      -9.407  14.935  12.148  1.00 27.08           C  
ATOM   1277  NE  ARG B  30      -9.697  15.793  13.294  1.00 22.03           N  
ATOM   1278  CZ  ARG B  30      -8.749  16.374  14.039  1.00 25.92           C  
ATOM   1279  NH1 ARG B  30      -7.465  16.191  13.785  1.00 24.89           N  
ATOM   1280  NH2 ARG B  30      -9.084  17.174  15.059  1.00 30.08           N  
ATOM   1281  N   LEU B  31      -9.650  13.812   6.541  1.00 22.83           N  
ATOM   1282  CA  LEU B  31      -9.110  13.087   5.327  1.00 25.29           C  
ATOM   1283  C   LEU B  31      -8.752  14.113   4.223  1.00 27.37           C  
ATOM   1284  O   LEU B  31      -7.612  14.153   3.667  1.00 28.34           O  
ATOM   1285  CB  LEU B  31     -10.131  12.096   4.811  1.00 21.08           C  
ATOM   1286  CG  LEU B  31      -9.608  11.352   3.550  1.00 26.40           C  
ATOM   1287  CD1 LEU B  31      -8.816  10.064   3.919  1.00 23.90           C  
ATOM   1288  CD2 LEU B  31     -10.754  11.036   2.622  1.00 29.18           C  
ATOM   1289  N   LEU B  32      -9.697  15.030   3.995  1.00 25.98           N  
ATOM   1290  CA  LEU B  32      -9.528  16.031   2.939  1.00 28.18           C  
ATOM   1291  C   LEU B  32      -8.452  17.007   3.255  1.00 29.59           C  
ATOM   1292  O   LEU B  32      -7.824  17.598   2.339  1.00 32.16           O  
ATOM   1293  CB  LEU B  32     -10.853  16.826   2.725  1.00 31.19           C  
ATOM   1294  CG  LEU B  32     -12.050  16.070   2.241  1.00 32.54           C  
ATOM   1295  CD1 LEU B  32     -13.274  17.006   2.394  1.00 35.63           C  
ATOM   1296  CD2 LEU B  32     -11.919  15.637   0.793  1.00 28.51           C  
ATOM   1297  N   VAL B  33      -8.283  17.292   4.534  1.00 28.45           N  
ATOM   1298  CA  VAL B  33      -7.261  18.257   4.917  1.00 28.05           C  
ATOM   1299  C   VAL B  33      -5.886  17.587   4.913  1.00 30.26           C  
ATOM   1300  O   VAL B  33      -4.900  18.224   4.527  1.00 28.78           O  
ATOM   1301  CB  VAL B  33      -7.507  18.896   6.295  1.00 25.13           C  
ATOM   1302  CG1 VAL B  33      -6.295  19.644   6.784  1.00 25.87           C  
ATOM   1303  CG2 VAL B  33      -8.679  19.892   6.196  1.00 30.16           C  
ATOM   1304  N   VAL B  34      -5.807  16.342   5.412  1.00 27.13           N  
ATOM   1305  CA  VAL B  34      -4.484  15.710   5.690  1.00 24.78           C  
ATOM   1306  C   VAL B  34      -3.929  15.075   4.365  1.00 24.07           C  
ATOM   1307  O   VAL B  34      -2.709  14.998   4.143  1.00 26.58           O  
ATOM   1308  CB  VAL B  34      -4.612  14.629   6.842  1.00 22.67           C  
ATOM   1309  CG1 VAL B  34      -3.313  13.772   7.013  1.00 23.18           C  
ATOM   1310  CG2 VAL B  34      -4.988  15.324   8.162  1.00 24.55           C  
ATOM   1311  N   TYR B  35      -4.835  14.544   3.587  1.00 25.07           N  
ATOM   1312  CA  TYR B  35      -4.540  13.848   2.299  1.00 26.27           C  
ATOM   1313  C   TYR B  35      -5.270  14.628   1.179  1.00 27.08           C  
ATOM   1314  O   TYR B  35      -6.256  14.156   0.651  1.00 25.99           O  
ATOM   1315  CB  TYR B  35      -4.985  12.402   2.338  1.00 26.15           C  
ATOM   1316  CG  TYR B  35      -4.406  11.703   3.570  1.00 25.17           C  
ATOM   1317  CD1 TYR B  35      -3.055  11.480   3.687  1.00 24.03           C  
ATOM   1318  CD2 TYR B  35      -5.225  11.289   4.606  1.00 25.12           C  
ATOM   1319  CE1 TYR B  35      -2.506  10.839   4.804  1.00 26.77           C  
ATOM   1320  CE2 TYR B  35      -4.703  10.621   5.715  1.00 27.16           C  
ATOM   1321  CZ  TYR B  35      -3.360  10.441   5.847  1.00 24.78           C  
ATOM   1322  OH  TYR B  35      -2.827   9.844   6.967  1.00 26.56           O  
ATOM   1323  N   PRO B  36      -4.756  15.826   0.836  1.00 28.99           N  
ATOM   1324  CA  PRO B  36      -5.612  16.717   0.033  1.00 35.25           C  
ATOM   1325  C   PRO B  36      -5.870  16.280  -1.384  1.00 33.80           C  
ATOM   1326  O   PRO B  36      -6.675  16.919  -2.081  1.00 34.16           O  
ATOM   1327  CB  PRO B  36      -4.895  18.070   0.120  1.00 31.61           C  
ATOM   1328  CG  PRO B  36      -3.476  17.691   0.232  1.00 32.04           C  
ATOM   1329  CD  PRO B  36      -3.473  16.479   1.150  1.00 31.17           C  
ATOM   1330  N   TRP B  37      -5.228  15.195  -1.819  1.00 31.92           N  
ATOM   1331  CA  TRP B  37      -5.521  14.692  -3.142  1.00 30.17           C  
ATOM   1332  C   TRP B  37      -6.897  14.161  -3.154  1.00 32.89           C  
ATOM   1333  O   TRP B  37      -7.487  14.065  -4.215  1.00 31.05           O  
ATOM   1334  CB  TRP B  37      -4.541  13.599  -3.646  1.00 33.01           C  
ATOM   1335  CG  TRP B  37      -4.402  12.410  -2.764  1.00 27.94           C  
ATOM   1336  CD1 TRP B  37      -5.143  11.274  -2.784  1.00 24.69           C  
ATOM   1337  CD2 TRP B  37      -3.439  12.271  -1.717  1.00 26.79           C  
ATOM   1338  NE1 TRP B  37      -4.684  10.408  -1.778  1.00 24.16           N  
ATOM   1339  CE2 TRP B  37      -3.618  10.989  -1.141  1.00 26.21           C  
ATOM   1340  CE3 TRP B  37      -2.391  13.082  -1.255  1.00 25.84           C  
ATOM   1341  CZ2 TRP B  37      -2.821  10.514  -0.046  1.00 23.66           C  
ATOM   1342  CZ3 TRP B  37      -1.570  12.600  -0.149  1.00 30.32           C  
ATOM   1343  CH2 TRP B  37      -1.796  11.311   0.405  1.00 27.19           C  
ATOM   1344  N   THR B  38      -7.421  13.770  -1.978  1.00 29.59           N  
ATOM   1345  CA  THR B  38      -8.765  13.219  -1.924  1.00 27.69           C  
ATOM   1346  C   THR B  38      -9.803  14.319  -2.255  1.00 25.99           C  
ATOM   1347  O   THR B  38     -10.901  13.978  -2.558  1.00 29.93           O  
ATOM   1348  CB  THR B  38      -9.140  12.665  -0.522  1.00 27.56           C  
ATOM   1349  OG1 THR B  38      -8.730  13.614   0.422  1.00 28.33           O  
ATOM   1350  CG2 THR B  38      -8.399  11.359  -0.227  1.00 25.39           C  
ATOM   1351  N   GLN B  39      -9.433  15.585  -2.183  1.00 29.62           N  
ATOM   1352  CA  GLN B  39     -10.330  16.696  -2.566  1.00 32.27           C  
ATOM   1353  C   GLN B  39     -10.619  16.627  -4.041  1.00 36.82           C  
ATOM   1354  O   GLN B  39     -11.633  17.138  -4.505  1.00 36.04           O  
ATOM   1355  CB  GLN B  39      -9.713  18.032  -2.262  1.00 34.64           C  
ATOM   1356  CG  GLN B  39      -9.477  18.255  -0.778  1.00 39.32           C  
ATOM   1357  CD  GLN B  39      -8.827  19.568  -0.592  1.00 41.22           C  
ATOM   1358  OE1 GLN B  39      -8.981  20.433  -1.476  1.00 43.72           O  
ATOM   1359  NE2 GLN B  39      -8.104  19.765   0.524  1.00 35.83           N  
ATOM   1360  N   ARG B  40      -9.770  15.944  -4.798  1.00 39.30           N  
ATOM   1361  CA  ARG B  40     -10.184  15.600  -6.163  1.00 40.02           C  
ATOM   1362  C   ARG B  40     -11.608  15.107  -6.337  1.00 39.07           C  
ATOM   1363  O   ARG B  40     -12.215  15.451  -7.336  1.00 40.81           O  
ATOM   1364  CB  ARG B  40      -9.321  14.519  -6.763  1.00 42.11           C  
ATOM   1365  CG  ARG B  40      -9.108  14.782  -8.219  1.00 44.54           C  
ATOM   1366  CD  ARG B  40      -7.983  13.920  -8.693  1.00 48.54           C  
ATOM   1367  NE  ARG B  40      -8.501  12.683  -9.232  1.00 52.44           N  
ATOM   1368  CZ  ARG B  40      -8.856  12.522 -10.500  1.00 58.98           C  
ATOM   1369  NH1 ARG B  40      -8.779  13.549 -11.364  1.00 60.98           N  
ATOM   1370  NH2 ARG B  40      -9.278  11.326 -10.903  1.00 59.45           N  
ATOM   1371  N   PHE B  41     -12.088  14.227  -5.454  1.00 34.79           N  
ATOM   1372  CA  PHE B  41     -13.371  13.553  -5.638  1.00 36.02           C  
ATOM   1373  C   PHE B  41     -14.548  14.395  -5.062  1.00 40.10           C  
ATOM   1374  O   PHE B  41     -15.705  13.927  -5.039  1.00 40.33           O  
ATOM   1375  CB  PHE B  41     -13.385  12.171  -4.993  1.00 40.75           C  
ATOM   1376  CG  PHE B  41     -12.500  11.162  -5.676  1.00 43.51           C  
ATOM   1377  CD1 PHE B  41     -11.195  10.925  -5.206  1.00 45.63           C  
ATOM   1378  CD2 PHE B  41     -12.960  10.447  -6.783  1.00 43.60           C  
ATOM   1379  CE1 PHE B  41     -10.366  10.007  -5.849  1.00 42.23           C  
ATOM   1380  CE2 PHE B  41     -12.134   9.512  -7.426  1.00 45.02           C  
ATOM   1381  CZ  PHE B  41     -10.844   9.303  -6.949  1.00 40.25           C  
ATOM   1382  N   PHE B  42     -14.234  15.587  -4.537  1.00 38.40           N  
ATOM   1383  CA  PHE B  42     -15.259  16.401  -3.843  1.00 42.69           C  
ATOM   1384  C   PHE B  42     -15.285  17.837  -4.349  1.00 45.46           C  
ATOM   1385  O   PHE B  42     -15.667  18.753  -3.630  1.00 38.98           O  
ATOM   1386  CB  PHE B  42     -15.087  16.329  -2.308  1.00 41.32           C  
ATOM   1387  CG  PHE B  42     -15.229  14.930  -1.773  1.00 42.22           C  
ATOM   1388  CD1 PHE B  42     -14.105  14.170  -1.456  1.00 37.83           C  
ATOM   1389  CD2 PHE B  42     -16.495  14.324  -1.674  1.00 43.30           C  
ATOM   1390  CE1 PHE B  42     -14.251  12.863  -1.004  1.00 31.97           C  
ATOM   1391  CE2 PHE B  42     -16.633  13.003  -1.238  1.00 37.11           C  
ATOM   1392  CZ  PHE B  42     -15.513  12.273  -0.906  1.00 35.86           C  
ATOM   1393  N   GLU B  43     -14.918  18.023  -5.613  1.00 50.76           N  
ATOM   1394  CA  GLU B  43     -14.910  19.372  -6.230  1.00 58.71           C  
ATOM   1395  C   GLU B  43     -16.247  20.151  -6.025  1.00 57.31           C  
ATOM   1396  O   GLU B  43     -16.252  21.357  -5.770  1.00 61.84           O  
ATOM   1397  CB  GLU B  43     -14.520  19.261  -7.719  1.00 59.69           C  
ATOM   1398  CG  GLU B  43     -15.540  18.533  -8.608  0.50 62.29           C  
ATOM   1399  CD  GLU B  43     -15.434  17.002  -8.602  0.50 60.23           C  
ATOM   1400  OE1 GLU B  43     -14.693  16.422  -7.785  0.50 59.10           O  
ATOM   1401  OE2 GLU B  43     -16.116  16.360  -9.424  0.50 59.83           O  
ATOM   1402  N   SER B  44     -17.362  19.433  -6.095  1.00 50.47           N  
ATOM   1403  CA  SER B  44     -18.685  20.000  -5.957  1.00 52.23           C  
ATOM   1404  C   SER B  44     -19.105  20.456  -4.515  1.00 54.79           C  
ATOM   1405  O   SER B  44     -20.148  21.089  -4.354  1.00 51.54           O  
ATOM   1406  CB  SER B  44     -19.677  18.978  -6.495  1.00 48.15           C  
ATOM   1407  OG  SER B  44     -19.744  17.880  -5.603  1.00 53.33           O  
ATOM   1408  N   PHE B  45     -18.314  20.126  -3.486  1.00 49.04           N  
ATOM   1409  CA  PHE B  45     -18.637  20.459  -2.112  1.00 46.96           C  
ATOM   1410  C   PHE B  45     -18.370  21.951  -1.814  1.00 54.25           C  
ATOM   1411  O   PHE B  45     -18.845  22.491  -0.793  1.00 52.04           O  
ATOM   1412  CB  PHE B  45     -17.835  19.542  -1.151  1.00 48.05           C  
ATOM   1413  CG  PHE B  45     -18.466  18.185  -0.895  1.00 41.05           C  
ATOM   1414  CD1 PHE B  45     -18.232  17.523   0.294  1.00 48.59           C  
ATOM   1415  CD2 PHE B  45     -19.274  17.573  -1.828  1.00 44.97           C  
ATOM   1416  CE1 PHE B  45     -18.784  16.263   0.562  1.00 42.43           C  
ATOM   1417  CE2 PHE B  45     -19.831  16.326  -1.576  1.00 43.98           C  
ATOM   1418  CZ  PHE B  45     -19.593  15.675  -0.376  1.00 39.76           C  
ATOM   1419  N   GLY B  46     -17.593  22.609  -2.678  1.00 48.08           N  
ATOM   1420  CA  GLY B  46     -17.409  24.049  -2.578  1.00 52.06           C  
ATOM   1421  C   GLY B  46     -16.124  24.455  -1.894  1.00 46.76           C  
ATOM   1422  O   GLY B  46     -15.080  23.903  -2.209  1.00 55.67           O  
ATOM   1423  N   ASP B  47     -16.192  25.409  -0.953  1.00 42.90           N  
ATOM   1424  CA  ASP B  47     -14.969  25.986  -0.385  1.00 45.22           C  
ATOM   1425  C   ASP B  47     -14.214  24.942   0.429  1.00 41.93           C  
ATOM   1426  O   ASP B  47     -14.683  24.494   1.526  1.00 38.18           O  
ATOM   1427  CB  ASP B  47     -15.227  27.207   0.490  1.00 44.83           C  
ATOM   1428  CG  ASP B  47     -13.925  27.929   0.867  1.00 48.61           C  
ATOM   1429  OD1 ASP B  47     -14.001  28.986   1.499  1.00 50.47           O  
ATOM   1430  OD2 ASP B  47     -12.817  27.442   0.527  1.00 48.60           O  
ATOM   1431  N   LEU B  48     -13.069  24.550  -0.117  1.00 41.47           N  
ATOM   1432  CA  LEU B  48     -12.143  23.650   0.579  1.00 41.28           C  
ATOM   1433  C   LEU B  48     -10.768  24.289   0.702  1.00 49.50           C  
ATOM   1434  O   LEU B  48      -9.772  23.598   0.886  1.00 53.25           O  
ATOM   1435  CB  LEU B  48     -12.072  22.287  -0.107  1.00 40.11           C  
ATOM   1436  CG  LEU B  48     -13.418  21.572  -0.257  1.00 39.19           C  
ATOM   1437  CD1 LEU B  48     -13.324  20.343  -1.151  1.00 42.17           C  
ATOM   1438  CD2 LEU B  48     -14.049  21.218   1.078  1.00 42.15           C  
ATOM   1439  N   SER B  49     -10.722  25.614   0.635  1.00 48.51           N  
ATOM   1440  CA  SER B  49      -9.440  26.326   0.548  1.00 54.03           C  
ATOM   1441  C   SER B  49      -8.667  26.395   1.885  1.00 50.78           C  
ATOM   1442  O   SER B  49      -7.519  26.831   1.920  1.00 52.87           O  
ATOM   1443  CB  SER B  49      -9.670  27.745  -0.006  1.00 50.53           C  
ATOM   1444  OG  SER B  49     -10.482  28.499   0.893  1.00 53.34           O  
ATOM   1445  N   THR B  50      -9.293  25.968   2.979  1.00 47.13           N  
ATOM   1446  CA  THR B  50      -8.687  26.097   4.285  1.00 46.74           C  
ATOM   1447  C   THR B  50      -9.069  24.882   5.135  1.00 44.99           C  
ATOM   1448  O   THR B  50     -10.053  24.180   4.824  1.00 44.54           O  
ATOM   1449  CB  THR B  50      -9.098  27.436   4.988  1.00 44.52           C  
ATOM   1450  OG1 THR B  50      -8.265  27.689   6.124  1.00 51.58           O  
ATOM   1451  CG2 THR B  50     -10.433  27.368   5.501  1.00 39.04           C  
ATOM   1452  N   PRO B  51      -8.292  24.633   6.200  1.00 40.13           N  
ATOM   1453  CA  PRO B  51      -8.793  23.644   7.173  1.00 39.42           C  
ATOM   1454  C   PRO B  51     -10.166  24.044   7.750  1.00 42.66           C  
ATOM   1455  O   PRO B  51     -11.109  23.247   7.646  1.00 38.03           O  
ATOM   1456  CB  PRO B  51      -7.692  23.616   8.238  1.00 37.44           C  
ATOM   1457  CG  PRO B  51      -6.425  23.985   7.461  1.00 40.35           C  
ATOM   1458  CD  PRO B  51      -6.892  25.032   6.470  1.00 41.14           C  
ATOM   1459  N   ASP B  52     -10.284  25.251   8.345  1.00 44.32           N  
ATOM   1460  CA  ASP B  52     -11.607  25.740   8.895  1.00 44.76           C  
ATOM   1461  C   ASP B  52     -12.720  25.650   7.854  1.00 43.33           C  
ATOM   1462  O   ASP B  52     -13.818  25.219   8.170  1.00 44.35           O  
ATOM   1463  CB  ASP B  52     -11.564  27.184   9.462  1.00 43.41           C  
ATOM   1464  CG  ASP B  52     -10.675  27.318  10.686  1.00 54.48           C  
ATOM   1465  OD1 ASP B  52     -10.347  26.268  11.304  1.00 55.44           O  
ATOM   1466  OD2 ASP B  52     -10.309  28.474  11.037  1.00 46.53           O  
ATOM   1467  N   ALA B  53     -12.410  26.009   6.609  1.00 44.90           N  
ATOM   1468  CA  ALA B  53     -13.367  25.959   5.509  1.00 43.13           C  
ATOM   1469  C   ALA B  53     -13.874  24.539   5.336  1.00 45.81           C  
ATOM   1470  O   ALA B  53     -15.095  24.309   5.224  1.00 40.94           O  
ATOM   1471  CB  ALA B  53     -12.719  26.468   4.216  1.00 46.91           C  
ATOM   1472  N   VAL B  54     -12.945  23.571   5.319  1.00 38.18           N  
ATOM   1473  CA  VAL B  54     -13.364  22.153   5.294  1.00 38.96           C  
ATOM   1474  C   VAL B  54     -14.263  21.671   6.444  1.00 35.02           C  
ATOM   1475  O   VAL B  54     -15.296  21.008   6.206  1.00 33.23           O  
ATOM   1476  CB  VAL B  54     -12.117  21.192   5.165  1.00 36.36           C  
ATOM   1477  CG1 VAL B  54     -12.563  19.778   4.871  1.00 31.36           C  
ATOM   1478  CG2 VAL B  54     -11.220  21.659   4.005  1.00 33.20           C  
ATOM   1479  N   MET B  55     -13.808  21.893   7.675  1.00 40.24           N  
ATOM   1480  CA  MET B  55     -14.477  21.323   8.843  1.00 41.19           C  
ATOM   1481  C   MET B  55     -15.844  21.978   9.013  1.00 43.57           C  
ATOM   1482  O   MET B  55     -16.816  21.302   9.315  1.00 43.65           O  
ATOM   1483  CB  MET B  55     -13.612  21.448  10.103  1.00 34.91           C  
ATOM   1484  CG  MET B  55     -12.178  20.932   9.865  1.00 36.15           C  
ATOM   1485  SD  MET B  55     -12.040  19.247   9.189  1.00 38.07           S  
ATOM   1486  CE  MET B  55     -12.799  18.296  10.530  1.00 36.41           C  
ATOM   1487  N   GLY B  56     -15.900  23.276   8.714  1.00 46.44           N  
ATOM   1488  CA  GLY B  56     -17.136  24.058   8.788  1.00 53.95           C  
ATOM   1489  C   GLY B  56     -18.054  23.930   7.590  1.00 51.94           C  
ATOM   1490  O   GLY B  56     -19.174  24.425   7.624  1.00 50.78           O  
ATOM   1491  N   ASN B  57     -17.584  23.262   6.531  1.00 50.81           N  
ATOM   1492  CA  ASN B  57     -18.373  23.067   5.315  1.00 45.56           C  
ATOM   1493  C   ASN B  57     -19.569  22.132   5.578  1.00 46.24           C  
ATOM   1494  O   ASN B  57     -19.371  20.967   5.960  1.00 35.09           O  
ATOM   1495  CB  ASN B  57     -17.459  22.519   4.214  1.00 46.35           C  
ATOM   1496  CG  ASN B  57     -18.107  22.498   2.833  1.00 48.76           C  
ATOM   1497  OD1 ASN B  57     -19.131  21.850   2.590  1.00 41.19           O  
ATOM   1498  ND2 ASN B  57     -17.440  23.145   1.888  1.00 48.58           N  
ATOM   1499  N   PRO B  58     -20.825  22.630   5.370  1.00 42.86           N  
ATOM   1500  CA  PRO B  58     -22.060  21.815   5.621  1.00 39.75           C  
ATOM   1501  C   PRO B  58     -22.153  20.535   4.806  1.00 35.49           C  
ATOM   1502  O   PRO B  58     -22.758  19.556   5.244  1.00 41.38           O  
ATOM   1503  CB  PRO B  58     -23.200  22.770   5.197  1.00 39.20           C  
ATOM   1504  CG  PRO B  58     -22.584  24.153   5.342  1.00 45.36           C  
ATOM   1505  CD  PRO B  58     -21.176  23.974   4.853  1.00 43.05           C  
ATOM   1506  N   LYS B  59     -21.607  20.551   3.600  1.00 41.34           N  
ATOM   1507  CA  LYS B  59     -21.605  19.366   2.742  1.00 40.99           C  
ATOM   1508  C   LYS B  59     -20.664  18.243   3.269  1.00 41.40           C  
ATOM   1509  O   LYS B  59     -21.009  17.065   3.322  1.00 43.50           O  
ATOM   1510  CB  LYS B  59     -21.199  19.809   1.367  1.00 41.28           C  
ATOM   1511  CG  LYS B  59     -22.233  20.752   0.752  1.00 47.45           C  
ATOM   1512  CD  LYS B  59     -21.906  21.035  -0.714  1.00 50.37           C  
ATOM   1513  CE  LYS B  59     -23.072  21.700  -1.436  1.00 57.96           C  
ATOM   1514  NZ  LYS B  59     -22.838  21.813  -2.911  1.00 55.55           N  
ATOM   1515  N   VAL B  60     -19.489  18.642   3.709  1.00 44.68           N  
ATOM   1516  CA  VAL B  60     -18.537  17.720   4.376  1.00 40.58           C  
ATOM   1517  C   VAL B  60     -19.281  17.036   5.564  1.00 40.34           C  
ATOM   1518  O   VAL B  60     -19.372  15.820   5.632  1.00 37.92           O  
ATOM   1519  CB  VAL B  60     -17.235  18.507   4.715  1.00 45.07           C  
ATOM   1520  CG1 VAL B  60     -16.296  17.731   5.633  1.00 39.43           C  
ATOM   1521  CG2 VAL B  60     -16.504  18.945   3.418  1.00 42.28           C  
ATOM   1522  N   LYS B  61     -19.910  17.812   6.462  1.00 44.55           N  
ATOM   1523  CA  LYS B  61     -20.649  17.187   7.590  1.00 41.34           C  
ATOM   1524  C   LYS B  61     -21.785  16.286   7.099  1.00 42.70           C  
ATOM   1525  O   LYS B  61     -21.946  15.132   7.550  1.00 44.95           O  
ATOM   1526  CB  LYS B  61     -21.154  18.230   8.612  1.00 39.64           C  
ATOM   1527  CG  LYS B  61     -22.178  17.597   9.550  1.00 46.08           C  
ATOM   1528  CD  LYS B  61     -22.463  18.463  10.767  1.00 52.82           C  
ATOM   1529  CE  LYS B  61     -23.662  17.925  11.522  1.00 54.28           C  
ATOM   1530  NZ  LYS B  61     -23.781  18.721  12.770  1.00 51.88           N  
ATOM   1531  N   ALA B  62     -22.567  16.795   6.142  1.00 43.77           N  
ATOM   1532  CA  ALA B  62     -23.683  16.044   5.595  1.00 42.23           C  
ATOM   1533  C   ALA B  62     -23.161  14.696   5.060  1.00 38.94           C  
ATOM   1534  O   ALA B  62     -23.646  13.638   5.429  1.00 41.44           O  
ATOM   1535  CB  ALA B  62     -24.352  16.859   4.494  1.00 44.11           C  
ATOM   1536  N   HIS B  63     -22.116  14.732   4.235  1.00 35.33           N  
ATOM   1537  CA  HIS B  63     -21.720  13.497   3.608  1.00 38.53           C  
ATOM   1538  C   HIS B  63     -20.998  12.568   4.603  1.00 34.74           C  
ATOM   1539  O   HIS B  63     -21.167  11.357   4.524  1.00 31.20           O  
ATOM   1540  CB  HIS B  63     -20.915  13.751   2.334  1.00 40.24           C  
ATOM   1541  CG  HIS B  63     -20.460  12.503   1.650  1.00 40.21           C  
ATOM   1542  ND1 HIS B  63     -21.327  11.664   0.992  1.00 42.16           N  
ATOM   1543  CD2 HIS B  63     -19.224  11.953   1.514  1.00 39.43           C  
ATOM   1544  CE1 HIS B  63     -20.655  10.629   0.510  1.00 48.19           C  
ATOM   1545  NE2 HIS B  63     -19.376  10.789   0.803  1.00 41.70           N  
ATOM   1546  N   GLY B  64     -20.256  13.133   5.571  1.00 29.81           N  
ATOM   1547  CA  GLY B  64     -19.547  12.278   6.462  1.00 34.90           C  
ATOM   1548  C   GLY B  64     -20.508  11.480   7.317  1.00 39.09           C  
ATOM   1549  O   GLY B  64     -20.175  10.422   7.874  1.00 36.11           O  
ATOM   1550  N   LYS B  65     -21.728  12.000   7.439  1.00 38.47           N  
ATOM   1551  CA  LYS B  65     -22.704  11.354   8.282  1.00 37.45           C  
ATOM   1552  C   LYS B  65     -23.105  10.056   7.638  1.00 33.83           C  
ATOM   1553  O   LYS B  65     -23.304   9.007   8.328  1.00 31.90           O  
ATOM   1554  CB  LYS B  65     -23.918  12.304   8.414  1.00 44.77           C  
ATOM   1555  CG  LYS B  65     -25.019  11.870   9.354  1.00 44.80           C  
ATOM   1556  CD  LYS B  65     -26.080  12.989   9.477  1.00 43.26           C  
ATOM   1557  CE  LYS B  65     -27.346  12.353  10.000  1.00 44.88           C  
ATOM   1558  NZ  LYS B  65     -28.380  13.299  10.496  1.00 45.81           N  
ATOM   1559  N   LYS B  66     -23.222  10.093   6.302  1.00 33.93           N  
ATOM   1560  CA  LYS B  66     -23.562   8.866   5.524  1.00 34.77           C  
ATOM   1561  C   LYS B  66     -22.414   7.880   5.567  1.00 33.80           C  
ATOM   1562  O   LYS B  66     -22.603   6.685   5.714  1.00 32.38           O  
ATOM   1563  CB  LYS B  66     -23.756   9.203   4.070  1.00 38.97           C  
ATOM   1564  CG  LYS B  66     -25.078   9.819   3.765  1.00 45.89           C  
ATOM   1565  CD  LYS B  66     -25.545   9.275   2.425  1.00 55.57           C  
ATOM   1566  CE  LYS B  66     -25.469  10.400   1.420  1.00 59.52           C  
ATOM   1567  NZ  LYS B  66     -26.008  11.601   2.137  1.00 53.87           N  
ATOM   1568  N   VAL B  67     -21.203   8.402   5.393  1.00 36.34           N  
ATOM   1569  CA  VAL B  67     -20.028   7.520   5.555  1.00 31.41           C  
ATOM   1570  C   VAL B  67     -20.091   6.784   6.911  1.00 25.79           C  
ATOM   1571  O   VAL B  67     -19.841   5.570   6.977  1.00 28.58           O  
ATOM   1572  CB  VAL B  67     -18.699   8.325   5.389  1.00 29.03           C  
ATOM   1573  CG1 VAL B  67     -17.498   7.439   5.750  1.00 26.68           C  
ATOM   1574  CG2 VAL B  67     -18.590   8.859   3.963  1.00 29.84           C  
ATOM   1575  N   LEU B  68     -20.398   7.497   7.998  1.00 30.01           N  
ATOM   1576  CA  LEU B  68     -20.339   6.885   9.354  1.00 31.98           C  
ATOM   1577  C   LEU B  68     -21.447   5.873   9.499  1.00 30.58           C  
ATOM   1578  O   LEU B  68     -21.288   4.871  10.195  1.00 32.87           O  
ATOM   1579  CB  LEU B  68     -20.467   7.922  10.522  1.00 36.14           C  
ATOM   1580  CG  LEU B  68     -19.923   7.448  11.903  1.00 37.27           C  
ATOM   1581  CD1 LEU B  68     -18.418   7.401  11.934  1.00 33.94           C  
ATOM   1582  CD2 LEU B  68     -20.391   8.345  13.058  1.00 38.73           C  
ATOM   1583  N   GLY B  69     -22.602   6.193   8.908  1.00 39.38           N  
ATOM   1584  CA  GLY B  69     -23.700   5.226   8.750  1.00 37.76           C  
ATOM   1585  C   GLY B  69     -23.262   3.915   8.118  1.00 37.12           C  
ATOM   1586  O   GLY B  69     -23.635   2.808   8.582  1.00 30.74           O  
ATOM   1587  N   ALA B  70     -22.458   4.015   7.052  1.00 36.60           N  
ATOM   1588  CA  ALA B  70     -21.928   2.785   6.448  1.00 36.34           C  
ATOM   1589  C   ALA B  70     -20.981   2.055   7.406  1.00 37.13           C  
ATOM   1590  O   ALA B  70     -20.995   0.844   7.445  1.00 37.13           O  
ATOM   1591  CB  ALA B  70     -21.254   3.044   5.094  1.00 31.96           C  
ATOM   1592  N   PHE B  71     -20.146   2.777   8.167  1.00 36.32           N  
ATOM   1593  CA  PHE B  71     -19.282   2.091   9.114  1.00 34.92           C  
ATOM   1594  C   PHE B  71     -20.172   1.405  10.149  1.00 38.65           C  
ATOM   1595  O   PHE B  71     -19.960   0.245  10.463  1.00 33.79           O  
ATOM   1596  CB  PHE B  71     -18.300   3.033   9.810  1.00 37.23           C  
ATOM   1597  CG  PHE B  71     -16.952   3.184   9.114  1.00 43.09           C  
ATOM   1598  CD1 PHE B  71     -16.679   4.311   8.314  1.00 42.36           C  
ATOM   1599  CD2 PHE B  71     -15.933   2.217   9.277  1.00 43.43           C  
ATOM   1600  CE1 PHE B  71     -15.422   4.447   7.672  1.00 43.98           C  
ATOM   1601  CE2 PHE B  71     -14.701   2.356   8.627  1.00 42.98           C  
ATOM   1602  CZ  PHE B  71     -14.439   3.476   7.847  1.00 42.53           C  
ATOM   1603  N   SER B  72     -21.171   2.130  10.682  1.00 37.96           N  
ATOM   1604  CA  SER B  72     -22.036   1.517  11.727  1.00 39.35           C  
ATOM   1605  C   SER B  72     -22.615   0.223  11.192  1.00 40.31           C  
ATOM   1606  O   SER B  72     -22.618  -0.826  11.871  1.00 40.33           O  
ATOM   1607  CB  SER B  72     -23.142   2.485  12.194  1.00 38.16           C  
ATOM   1608  OG  SER B  72     -22.562   3.622  12.850  1.00 40.49           O  
ATOM   1609  N   ASP B  73     -23.013   0.270   9.936  1.00 46.11           N  
ATOM   1610  CA  ASP B  73     -23.531  -0.924   9.274  1.00 48.16           C  
ATOM   1611  C   ASP B  73     -22.574  -2.136   9.272  1.00 51.22           C  
ATOM   1612  O   ASP B  73     -23.003  -3.233   9.571  1.00 47.26           O  
ATOM   1613  CB  ASP B  73     -23.981  -0.565   7.857  1.00 56.33           C  
ATOM   1614  CG  ASP B  73     -25.007  -1.557   7.292  1.00 57.91           C  
ATOM   1615  OD1 ASP B  73     -25.690  -2.272   8.055  1.00 60.85           O  
ATOM   1616  OD2 ASP B  73     -25.141  -1.619   6.067  1.00 52.05           O  
ATOM   1617  N   GLY B  74     -21.280  -1.956   8.957  1.00 48.71           N  
ATOM   1618  CA  GLY B  74     -20.332  -3.096   9.050  1.00 46.90           C  
ATOM   1619  C   GLY B  74     -20.054  -3.617  10.473  1.00 50.09           C  
ATOM   1620  O   GLY B  74     -19.655  -4.798  10.707  1.00 44.85           O  
ATOM   1621  N   LEU B  75     -20.222  -2.719  11.435  1.00 48.73           N  
ATOM   1622  CA  LEU B  75     -20.017  -3.072  12.834  1.00 50.23           C  
ATOM   1623  C   LEU B  75     -21.111  -4.022  13.252  1.00 49.18           C  
ATOM   1624  O   LEU B  75     -20.874  -4.912  14.047  1.00 52.59           O  
ATOM   1625  CB  LEU B  75     -19.993  -1.832  13.726  1.00 50.45           C  
ATOM   1626  CG  LEU B  75     -18.698  -1.001  13.669  1.00 55.25           C  
ATOM   1627  CD1 LEU B  75     -18.846   0.310  14.425  1.00 61.92           C  
ATOM   1628  CD2 LEU B  75     -17.523  -1.748  14.249  1.00 49.89           C  
ATOM   1629  N   ALA B  76     -22.311  -3.838  12.703  1.00 48.96           N  
ATOM   1630  CA  ALA B  76     -23.358  -4.843  12.890  1.00 51.17           C  
ATOM   1631  C   ALA B  76     -23.130  -6.165  12.076  1.00 49.45           C  
ATOM   1632  O   ALA B  76     -23.623  -7.217  12.469  1.00 46.73           O  
ATOM   1633  CB  ALA B  76     -24.749  -4.238  12.650  1.00 42.55           C  
ATOM   1634  N   HIS B  77     -22.376  -6.125  10.967  1.00 45.57           N  
ATOM   1635  CA  HIS B  77     -22.178  -7.320  10.151  1.00 45.82           C  
ATOM   1636  C   HIS B  77     -20.715  -7.727   9.993  1.00 45.12           C  
ATOM   1637  O   HIS B  77     -20.241  -7.963   8.874  1.00 50.54           O  
ATOM   1638  CB  HIS B  77     -22.877  -7.176   8.794  1.00 46.71           C  
ATOM   1639  CG  HIS B  77     -24.295  -6.687   8.890  1.00 54.43           C  
ATOM   1640  ND1 HIS B  77     -24.617  -5.376   9.179  1.00 55.32           N  
ATOM   1641  CD2 HIS B  77     -25.475  -7.339   8.752  1.00 60.48           C  
ATOM   1642  CE1 HIS B  77     -25.932  -5.244   9.222  1.00 59.68           C  
ATOM   1643  NE2 HIS B  77     -26.476  -6.418   8.961  1.00 58.82           N  
ATOM   1644  N   LEU B  78     -19.995  -7.789  11.113  1.00 48.05           N  
ATOM   1645  CA  LEU B  78     -18.559  -8.180  11.121  1.00 53.62           C  
ATOM   1646  C   LEU B  78     -18.206  -9.431  10.299  1.00 55.04           C  
ATOM   1647  O   LEU B  78     -17.156  -9.474   9.615  1.00 57.13           O  
ATOM   1648  CB  LEU B  78     -18.023  -8.356  12.550  1.00 50.76           C  
ATOM   1649  CG  LEU B  78     -17.175  -7.255  13.196  1.00 53.93           C  
ATOM   1650  CD1 LEU B  78     -16.584  -6.334  12.136  1.00 55.77           C  
ATOM   1651  CD2 LEU B  78     -17.992  -6.471  14.213  1.00 57.55           C  
ATOM   1652  N   ASP B  79     -19.068 -10.447  10.364  1.00 52.32           N  
ATOM   1653  CA  ASP B  79     -18.835 -11.697   9.620  1.00 50.36           C  
ATOM   1654  C   ASP B  79     -19.379 -11.630   8.165  1.00 55.35           C  
ATOM   1655  O   ASP B  79     -19.148 -12.542   7.370  1.00 47.97           O  
ATOM   1656  CB  ASP B  79     -19.436 -12.884  10.387  1.00 58.56           C  
ATOM   1657  CG  ASP B  79     -18.928 -12.987  11.843  0.50 56.09           C  
ATOM   1658  OD1 ASP B  79     -17.704 -12.857  12.091  0.50 57.36           O  
ATOM   1659  OD2 ASP B  79     -19.759 -13.225  12.745  0.50 53.53           O  
ATOM   1660  N   ASN B  80     -20.083 -10.548   7.798  1.00 53.01           N  
ATOM   1661  CA  ASN B  80     -20.471 -10.374   6.386  1.00 56.08           C  
ATOM   1662  C   ASN B  80     -20.160  -8.999   5.831  1.00 57.62           C  
ATOM   1663  O   ASN B  80     -21.084  -8.255   5.488  1.00 50.78           O  
ATOM   1664  CB  ASN B  80     -21.949 -10.676   6.150  1.00 62.57           C  
ATOM   1665  CG  ASN B  80     -22.278 -10.800   4.669  1.00 74.29           C  
ATOM   1666  OD1 ASN B  80     -21.449 -11.269   3.876  1.00 71.77           O  
ATOM   1667  ND2 ASN B  80     -23.478 -10.353   4.278  1.00 74.11           N  
ATOM   1668  N   LEU B  81     -18.868  -8.658   5.756  1.00 54.07           N  
ATOM   1669  CA  LEU B  81     -18.479  -7.337   5.275  1.00 50.08           C  
ATOM   1670  C   LEU B  81     -18.573  -7.319   3.771  1.00 51.13           C  
ATOM   1671  O   LEU B  81     -19.006  -6.328   3.202  1.00 51.82           O  
ATOM   1672  CB  LEU B  81     -17.088  -6.947   5.761  1.00 47.43           C  
ATOM   1673  CG  LEU B  81     -17.070  -6.721   7.282  1.00 46.66           C  
ATOM   1674  CD1 LEU B  81     -15.652  -6.502   7.781  1.00 42.96           C  
ATOM   1675  CD2 LEU B  81     -17.959  -5.565   7.711  1.00 41.21           C  
ATOM   1676  N   LYS B  82     -18.218  -8.431   3.129  1.00 47.96           N  
ATOM   1677  CA  LYS B  82     -18.229  -8.473   1.677  1.00 53.27           C  
ATOM   1678  C   LYS B  82     -19.629  -8.165   1.177  1.00 51.92           C  
ATOM   1679  O   LYS B  82     -19.830  -7.221   0.400  1.00 45.74           O  
ATOM   1680  CB  LYS B  82     -17.702  -9.804   1.133  1.00 56.16           C  
ATOM   1681  CG  LYS B  82     -17.359  -9.738  -0.356  1.00 60.06           C  
ATOM   1682  CD  LYS B  82     -16.805 -11.060  -0.881  1.00 67.27           C  
ATOM   1683  CE  LYS B  82     -17.885 -11.948  -1.508  1.00 71.94           C  
ATOM   1684  NZ  LYS B  82     -17.996 -11.865  -3.003  1.00 74.12           N  
ATOM   1685  N   GLY B  83     -20.597  -8.921   1.703  1.00 54.47           N  
ATOM   1686  CA  GLY B  83     -22.019  -8.690   1.442  1.00 48.35           C  
ATOM   1687  C   GLY B  83     -22.497  -7.283   1.738  1.00 51.59           C  
ATOM   1688  O   GLY B  83     -23.069  -6.617   0.867  1.00 48.16           O  
ATOM   1689  N   THR B  84     -22.279  -6.824   2.969  1.00 49.31           N  
ATOM   1690  CA  THR B  84     -22.752  -5.498   3.369  1.00 48.24           C  
ATOM   1691  C   THR B  84     -22.280  -4.420   2.379  1.00 48.37           C  
ATOM   1692  O   THR B  84     -23.072  -3.565   1.936  1.00 43.26           O  
ATOM   1693  CB  THR B  84     -22.277  -5.163   4.802  1.00 49.25           C  
ATOM   1694  OG1 THR B  84     -22.803  -6.127   5.712  1.00 54.80           O  
ATOM   1695  CG2 THR B  84     -22.764  -3.775   5.237  1.00 56.33           C  
ATOM   1696  N   PHE B  85     -20.991  -4.469   2.022  1.00 43.52           N  
ATOM   1697  CA  PHE B  85     -20.355  -3.372   1.236  1.00 41.72           C  
ATOM   1698  C   PHE B  85     -20.406  -3.469  -0.294  1.00 48.30           C  
ATOM   1699  O   PHE B  85     -19.847  -2.582  -0.966  1.00 55.12           O  
ATOM   1700  CB  PHE B  85     -18.905  -3.091   1.728  1.00 38.49           C  
ATOM   1701  CG  PHE B  85     -18.867  -2.361   3.037  1.00 36.79           C  
ATOM   1702  CD1 PHE B  85     -18.692  -3.059   4.239  1.00 36.12           C  
ATOM   1703  CD2 PHE B  85     -19.084  -0.967   3.072  1.00 41.28           C  
ATOM   1704  CE1 PHE B  85     -18.724  -2.387   5.442  1.00 41.50           C  
ATOM   1705  CE2 PHE B  85     -19.136  -0.280   4.283  1.00 37.28           C  
ATOM   1706  CZ  PHE B  85     -18.966  -0.992   5.458  1.00 40.55           C  
ATOM   1707  N   ALA B  86     -21.087  -4.484  -0.847  1.00 51.36           N  
ATOM   1708  CA  ALA B  86     -21.057  -4.759  -2.322  1.00 46.50           C  
ATOM   1709  C   ALA B  86     -21.417  -3.553  -3.205  1.00 48.60           C  
ATOM   1710  O   ALA B  86     -20.624  -3.099  -4.053  1.00 40.77           O  
ATOM   1711  CB  ALA B  86     -21.907  -5.965  -2.678  1.00 46.88           C  
ATOM   1712  N   THR B  87     -22.612  -3.018  -2.986  1.00 44.13           N  
ATOM   1713  CA  THR B  87     -23.074  -1.804  -3.634  1.00 42.79           C  
ATOM   1714  C   THR B  87     -22.142  -0.600  -3.480  1.00 42.72           C  
ATOM   1715  O   THR B  87     -21.924   0.195  -4.416  1.00 36.47           O  
ATOM   1716  CB  THR B  87     -24.424  -1.462  -2.966  1.00 53.37           C  
ATOM   1717  OG1 THR B  87     -25.321  -2.561  -3.191  1.00 50.80           O  
ATOM   1718  CG2 THR B  87     -24.990  -0.133  -3.443  1.00 45.75           C  
ATOM   1719  N   LEU B  88     -21.582  -0.433  -2.287  1.00 37.41           N  
ATOM   1720  CA  LEU B  88     -20.697   0.736  -2.134  1.00 42.50           C  
ATOM   1721  C   LEU B  88     -19.366   0.494  -2.894  1.00 38.15           C  
ATOM   1722  O   LEU B  88     -18.721   1.454  -3.331  1.00 40.53           O  
ATOM   1723  CB  LEU B  88     -20.459   1.065  -0.653  1.00 37.64           C  
ATOM   1724  CG  LEU B  88     -21.608   1.870  -0.016  1.00 37.27           C  
ATOM   1725  CD1 LEU B  88     -21.542   1.789   1.520  1.00 39.42           C  
ATOM   1726  CD2 LEU B  88     -21.584   3.304  -0.472  1.00 36.15           C  
ATOM   1727  N   SER B  89     -18.972  -0.779  -2.989  1.00 35.12           N  
ATOM   1728  CA  SER B  89     -17.736  -1.188  -3.673  1.00 41.81           C  
ATOM   1729  C   SER B  89     -17.913  -0.943  -5.139  1.00 40.74           C  
ATOM   1730  O   SER B  89     -17.088  -0.270  -5.768  1.00 38.70           O  
ATOM   1731  CB  SER B  89     -17.414  -2.669  -3.438  1.00 41.43           C  
ATOM   1732  OG  SER B  89     -16.135  -3.018  -3.978  1.00 42.58           O  
ATOM   1733  N   GLU B  90     -19.008  -1.470  -5.682  1.00 48.24           N  
ATOM   1734  CA  GLU B  90     -19.399  -1.131  -7.055  1.00 46.72           C  
ATOM   1735  C   GLU B  90     -19.299   0.375  -7.331  1.00 41.66           C  
ATOM   1736  O   GLU B  90     -18.697   0.789  -8.322  1.00 42.51           O  
ATOM   1737  CB  GLU B  90     -20.789  -1.664  -7.359  1.00 50.24           C  
ATOM   1738  CG  GLU B  90     -21.038  -1.868  -8.849  1.00 62.40           C  
ATOM   1739  CD  GLU B  90     -21.668  -3.230  -9.148  1.00 71.35           C  
ATOM   1740  OE1 GLU B  90     -22.434  -3.760  -8.299  1.00 71.19           O  
ATOM   1741  OE2 GLU B  90     -21.382  -3.792 -10.232  1.00 84.36           O  
ATOM   1742  N   LEU B  91     -19.815   1.208  -6.425  1.00 39.56           N  
ATOM   1743  CA  LEU B  91     -19.837   2.643  -6.613  1.00 41.30           C  
ATOM   1744  C   LEU B  91     -18.414   3.331  -6.616  1.00 36.72           C  
ATOM   1745  O   LEU B  91     -18.104   4.197  -7.465  1.00 34.06           O  
ATOM   1746  CB  LEU B  91     -20.765   3.289  -5.513  1.00 38.58           C  
ATOM   1747  CG  LEU B  91     -20.553   4.797  -5.319  1.00 36.38           C  
ATOM   1748  CD1 LEU B  91     -20.880   5.613  -6.575  1.00 36.79           C  
ATOM   1749  CD2 LEU B  91     -21.236   5.354  -4.066  1.00 39.55           C  
ATOM   1750  N   HIS B  92     -17.616   3.013  -5.595  1.00 38.69           N  
ATOM   1751  CA  HIS B  92     -16.315   3.687  -5.378  1.00 36.79           C  
ATOM   1752  C   HIS B  92     -15.241   3.122  -6.364  1.00 39.43           C  
ATOM   1753  O   HIS B  92     -14.337   3.868  -6.833  1.00 35.87           O  
ATOM   1754  CB  HIS B  92     -15.833   3.461  -3.945  1.00 35.26           C  
ATOM   1755  CG  HIS B  92     -16.583   4.240  -2.905  1.00 32.65           C  
ATOM   1756  ND1 HIS B  92     -17.782   3.811  -2.388  1.00 36.85           N  
ATOM   1757  CD2 HIS B  92     -16.277   5.385  -2.246  1.00 33.29           C  
ATOM   1758  CE1 HIS B  92     -18.200   4.669  -1.477  1.00 35.74           C  
ATOM   1759  NE2 HIS B  92     -17.313   5.637  -1.370  1.00 30.63           N  
ATOM   1760  N   CYS B  93     -15.379   1.827  -6.658  1.00 31.94           N  
ATOM   1761  CA  CYS B  93     -14.523   1.107  -7.581  1.00 40.58           C  
ATOM   1762  C   CYS B  93     -14.906   1.315  -9.063  1.00 41.52           C  
ATOM   1763  O   CYS B  93     -14.198   2.050  -9.767  1.00 42.56           O  
ATOM   1764  CB  CYS B  93     -14.443  -0.397  -7.218  1.00 38.17           C  
ATOM   1765  SG  CYS B  93     -13.831  -0.783  -5.521  1.00 50.28           S  
ATOM   1766  N   ASP B  94     -16.013   0.695  -9.529  1.00 47.00           N  
ATOM   1767  CA  ASP B  94     -16.529   0.887 -10.952  1.00 46.71           C  
ATOM   1768  C   ASP B  94     -16.970   2.302 -11.383  1.00 43.67           C  
ATOM   1769  O   ASP B  94     -16.740   2.715 -12.502  1.00 44.48           O  
ATOM   1770  CB  ASP B  94     -17.645  -0.104 -11.308  1.00 45.90           C  
ATOM   1771  CG  ASP B  94     -17.223  -1.565 -11.138  1.00 56.23           C  
ATOM   1772  OD1 ASP B  94     -16.028  -1.889 -11.382  1.00 49.25           O  
ATOM   1773  OD2 ASP B  94     -18.082  -2.392 -10.737  1.00 56.39           O  
ATOM   1774  N   LYS B  95     -17.613   3.066 -10.530  1.00 43.99           N  
ATOM   1775  CA  LYS B  95     -18.043   4.387 -10.980  1.00 49.91           C  
ATOM   1776  C   LYS B  95     -17.087   5.531 -10.633  1.00 47.74           C  
ATOM   1777  O   LYS B  95     -16.747   6.373 -11.487  1.00 49.68           O  
ATOM   1778  CB  LYS B  95     -19.460   4.688 -10.466  1.00 53.52           C  
ATOM   1779  CG  LYS B  95     -20.484   3.611 -10.812  1.00 59.48           C  
ATOM   1780  CD  LYS B  95     -21.079   3.763 -12.226  1.00 64.78           C  
ATOM   1781  CE  LYS B  95     -22.482   3.149 -12.290  1.00 67.04           C  
ATOM   1782  NZ  LYS B  95     -23.439   3.686 -11.247  1.00 57.19           N  
ATOM   1783  N   LEU B  96     -16.662   5.584  -9.375  1.00 43.88           N  
ATOM   1784  CA  LEU B  96     -15.794   6.658  -8.925  1.00 43.44           C  
ATOM   1785  C   LEU B  96     -14.279   6.400  -9.213  1.00 38.09           C  
ATOM   1786  O   LEU B  96     -13.529   7.325  -9.380  1.00 37.06           O  
ATOM   1787  CB  LEU B  96     -16.038   6.912  -7.434  1.00 42.53           C  
ATOM   1788  CG  LEU B  96     -17.441   7.436  -7.082  1.00 42.52           C  
ATOM   1789  CD1 LEU B  96     -17.644   7.414  -5.584  1.00 40.85           C  
ATOM   1790  CD2 LEU B  96     -17.635   8.827  -7.667  1.00 39.19           C  
ATOM   1791  N   HIS B  97     -13.859   5.145  -9.261  1.00 36.99           N  
ATOM   1792  CA  HIS B  97     -12.422   4.817  -9.379  1.00 41.89           C  
ATOM   1793  C   HIS B  97     -11.525   5.537  -8.312  1.00 36.99           C  
ATOM   1794  O   HIS B  97     -10.536   6.211  -8.648  1.00 40.25           O  
ATOM   1795  CB  HIS B  97     -11.896   5.093 -10.807  1.00 41.71           C  
ATOM   1796  CG  HIS B  97     -12.846   4.736 -11.915  1.00 46.92           C  
ATOM   1797  ND1 HIS B  97     -12.954   3.454 -12.428  1.00 48.83           N  
ATOM   1798  CD2 HIS B  97     -13.711   5.508 -12.625  1.00 45.64           C  
ATOM   1799  CE1 HIS B  97     -13.850   3.457 -13.405  1.00 49.70           C  
ATOM   1800  NE2 HIS B  97     -14.304   4.695 -13.558  1.00 47.38           N  
ATOM   1801  N   VAL B  98     -11.910   5.435  -7.044  1.00 30.68           N  
ATOM   1802  CA  VAL B  98     -11.104   5.929  -5.933  1.00 28.04           C  
ATOM   1803  C   VAL B  98     -10.065   4.813  -5.746  1.00 28.44           C  
ATOM   1804  O   VAL B  98     -10.430   3.665  -5.715  1.00 27.75           O  
ATOM   1805  CB  VAL B  98     -11.979   6.132  -4.632  1.00 31.70           C  
ATOM   1806  CG1 VAL B  98     -11.100   6.347  -3.428  1.00 27.12           C  
ATOM   1807  CG2 VAL B  98     -12.909   7.347  -4.726  1.00 31.69           C  
ATOM   1808  N   ASP B  99      -8.758   5.141  -5.661  1.00 32.98           N  
ATOM   1809  CA  ASP B  99      -7.793   4.087  -5.311  1.00 26.00           C  
ATOM   1810  C   ASP B  99      -8.062   3.593  -3.900  1.00 26.81           C  
ATOM   1811  O   ASP B  99      -8.218   4.421  -3.041  1.00 28.00           O  
ATOM   1812  CB  ASP B  99      -6.354   4.604  -5.403  1.00 27.97           C  
ATOM   1813  CG  ASP B  99      -5.359   3.469  -5.306  1.00 29.43           C  
ATOM   1814  OD1 ASP B  99      -4.872   3.094  -6.395  1.00 31.21           O  
ATOM   1815  OD2 ASP B  99      -5.164   2.858  -4.205  1.00 24.05           O  
ATOM   1816  N   PRO B 100      -8.080   2.249  -3.670  1.00 24.95           N  
ATOM   1817  CA  PRO B 100      -8.393   1.598  -2.391  1.00 29.61           C  
ATOM   1818  C   PRO B 100      -7.458   1.954  -1.262  1.00 30.30           C  
ATOM   1819  O   PRO B 100      -7.860   1.920  -0.092  1.00 25.42           O  
ATOM   1820  CB  PRO B 100      -8.287   0.096  -2.672  1.00 28.93           C  
ATOM   1821  CG  PRO B 100      -7.829  -0.058  -4.082  1.00 28.65           C  
ATOM   1822  CD  PRO B 100      -7.648   1.296  -4.707  1.00 25.84           C  
ATOM   1823  N   GLU B 101      -6.226   2.345  -1.580  1.00 27.25           N  
ATOM   1824  CA  GLU B 101      -5.333   2.860  -0.501  1.00 25.34           C  
ATOM   1825  C   GLU B 101      -6.092   3.938   0.297  1.00 25.06           C  
ATOM   1826  O   GLU B 101      -5.910   4.099   1.524  1.00 25.67           O  
ATOM   1827  CB  GLU B 101      -4.054   3.461  -1.126  1.00 25.80           C  
ATOM   1828  CG  GLU B 101      -3.072   3.964  -0.079  1.00 30.02           C  
ATOM   1829  CD  GLU B 101      -2.601   2.906   0.901  1.00 31.42           C  
ATOM   1830  OE1 GLU B 101      -1.926   3.359   1.819  1.00 34.70           O  
ATOM   1831  OE2 GLU B 101      -2.879   1.661   0.788  1.00 35.96           O  
ATOM   1832  N   ASN B 102      -6.937   4.691  -0.379  1.00 23.75           N  
ATOM   1833  CA  ASN B 102      -7.629   5.762   0.337  1.00 25.49           C  
ATOM   1834  C   ASN B 102      -8.665   5.284   1.349  1.00 22.74           C  
ATOM   1835  O   ASN B 102      -8.998   6.032   2.269  1.00 26.54           O  
ATOM   1836  CB  ASN B 102      -8.194   6.821  -0.650  1.00 27.43           C  
ATOM   1837  CG  ASN B 102      -7.101   7.444  -1.486  1.00 24.99           C  
ATOM   1838  OD1 ASN B 102      -6.180   8.068  -0.968  1.00 27.67           O  
ATOM   1839  ND2 ASN B 102      -7.198   7.291  -2.795  1.00 26.97           N  
ATOM   1840  N   PHE B 103      -9.199   4.088   1.146  1.00 26.26           N  
ATOM   1841  CA  PHE B 103     -10.117   3.436   2.074  1.00 25.35           C  
ATOM   1842  C   PHE B 103      -9.339   3.169   3.391  1.00 29.09           C  
ATOM   1843  O   PHE B 103      -9.843   3.439   4.498  1.00 26.89           O  
ATOM   1844  CB  PHE B 103     -10.669   2.068   1.503  1.00 23.45           C  
ATOM   1845  CG  PHE B 103     -11.379   2.169   0.181  1.00 28.54           C  
ATOM   1846  CD1 PHE B 103     -11.951   3.371  -0.234  1.00 27.94           C  
ATOM   1847  CD2 PHE B 103     -11.497   1.055  -0.655  1.00 27.38           C  
ATOM   1848  CE1 PHE B 103     -12.563   3.470  -1.479  1.00 31.04           C  
ATOM   1849  CE2 PHE B 103     -12.120   1.159  -1.894  1.00 28.05           C  
ATOM   1850  CZ  PHE B 103     -12.652   2.375  -2.295  1.00 25.11           C  
ATOM   1851  N   ARG B 104      -8.130   2.624   3.277  1.00 27.57           N  
ATOM   1852  CA  ARG B 104      -7.264   2.397   4.445  1.00 25.45           C  
ATOM   1853  C   ARG B 104      -6.936   3.715   5.081  1.00 23.25           C  
ATOM   1854  O   ARG B 104      -6.925   3.845   6.297  1.00 23.36           O  
ATOM   1855  CB  ARG B 104      -5.976   1.670   4.038  1.00 31.62           C  
ATOM   1856  CG  ARG B 104      -5.002   1.396   5.212  1.00 35.99           C  
ATOM   1857  CD  ARG B 104      -3.620   0.806   4.777  1.00 42.44           C  
ATOM   1858  NE  ARG B 104      -2.678   1.878   4.376  1.00 42.78           N  
ATOM   1859  CZ  ARG B 104      -2.011   2.658   5.229  1.00 46.38           C  
ATOM   1860  NH1 ARG B 104      -2.125   2.496   6.559  1.00 44.04           N  
ATOM   1861  NH2 ARG B 104      -1.210   3.608   4.763  1.00 51.23           N  
ATOM   1862  N   LEU B 105      -6.695   4.741   4.281  1.00 22.42           N  
ATOM   1863  CA  LEU B 105      -6.440   6.027   4.876  1.00 21.09           C  
ATOM   1864  C   LEU B 105      -7.661   6.589   5.725  1.00 22.10           C  
ATOM   1865  O   LEU B 105      -7.474   7.066   6.830  1.00 19.52           O  
ATOM   1866  CB  LEU B 105      -6.016   7.030   3.815  1.00 20.22           C  
ATOM   1867  CG  LEU B 105      -4.613   6.712   3.224  1.00 19.16           C  
ATOM   1868  CD1 LEU B 105      -4.299   7.781   2.191  1.00 22.01           C  
ATOM   1869  CD2 LEU B 105      -3.592   6.658   4.363  1.00 23.63           C  
ATOM   1870  N   LEU B 106      -8.851   6.540   5.180  1.00 25.05           N  
ATOM   1871  CA  LEU B 106     -10.002   7.102   5.874  1.00 25.04           C  
ATOM   1872  C   LEU B 106     -10.193   6.289   7.165  1.00 29.05           C  
ATOM   1873  O   LEU B 106     -10.491   6.877   8.223  1.00 30.35           O  
ATOM   1874  CB  LEU B 106     -11.242   7.057   4.964  1.00 27.46           C  
ATOM   1875  CG  LEU B 106     -12.586   7.574   5.575  1.00 25.46           C  
ATOM   1876  CD1 LEU B 106     -12.353   8.949   6.164  1.00 24.15           C  
ATOM   1877  CD2 LEU B 106     -13.695   7.661   4.507  1.00 22.79           C  
ATOM   1878  N   GLY B 107     -10.040   4.948   7.084  1.00 25.31           N  
ATOM   1879  CA  GLY B 107     -10.090   4.095   8.292  1.00 25.68           C  
ATOM   1880  C   GLY B 107      -9.153   4.580   9.366  1.00 24.32           C  
ATOM   1881  O   GLY B 107      -9.527   4.699  10.538  1.00 22.83           O  
ATOM   1882  N   ASN B 108      -7.878   4.805   9.007  1.00 22.65           N  
ATOM   1883  CA  ASN B 108      -6.916   5.309   9.957  1.00 23.33           C  
ATOM   1884  C   ASN B 108      -7.247   6.702  10.471  1.00 25.05           C  
ATOM   1885  O   ASN B 108      -7.043   7.009  11.637  1.00 23.55           O  
ATOM   1886  CB  ASN B 108      -5.565   5.321   9.283  1.00 23.98           C  
ATOM   1887  CG  ASN B 108      -4.946   3.967   9.280  1.00 27.48           C  
ATOM   1888  OD1 ASN B 108      -5.521   3.005   9.848  1.00 27.75           O  
ATOM   1889  ND2 ASN B 108      -3.789   3.864   8.666  1.00 31.38           N  
ATOM   1890  N   VAL B 109      -7.803   7.547   9.602  1.00 23.49           N  
ATOM   1891  CA  VAL B 109      -8.193   8.907  10.092  1.00 21.48           C  
ATOM   1892  C   VAL B 109      -9.320   8.770  11.118  1.00 24.29           C  
ATOM   1893  O   VAL B 109      -9.310   9.458  12.135  1.00 23.85           O  
ATOM   1894  CB  VAL B 109      -8.587   9.860   8.922  1.00 23.93           C  
ATOM   1895  CG1 VAL B 109      -9.184  11.182   9.462  1.00 23.37           C  
ATOM   1896  CG2 VAL B 109      -7.359  10.177   8.053  1.00 22.98           C  
ATOM   1897  N   LEU B 110     -10.248   7.855  10.855  1.00 22.62           N  
ATOM   1898  CA  LEU B 110     -11.328   7.637  11.824  1.00 27.39           C  
ATOM   1899  C   LEU B 110     -10.743   7.167  13.145  1.00 27.53           C  
ATOM   1900  O   LEU B 110     -11.137   7.698  14.207  1.00 27.55           O  
ATOM   1901  CB  LEU B 110     -12.317   6.580  11.295  1.00 24.48           C  
ATOM   1902  CG  LEU B 110     -13.422   6.125  12.257  1.00 23.75           C  
ATOM   1903  CD1 LEU B 110     -14.336   7.333  12.513  1.00 24.51           C  
ATOM   1904  CD2 LEU B 110     -14.155   4.951  11.619  1.00 24.33           C  
ATOM   1905  N   VAL B 111      -9.781   6.219  13.113  1.00 23.28           N  
ATOM   1906  CA  VAL B 111      -9.156   5.811  14.334  1.00 24.18           C  
ATOM   1907  C   VAL B 111      -8.592   7.034  15.093  1.00 25.77           C  
ATOM   1908  O   VAL B 111      -8.723   7.111  16.351  1.00 21.92           O  
ATOM   1909  CB  VAL B 111      -8.076   4.708  14.081  1.00 26.68           C  
ATOM   1910  CG1 VAL B 111      -7.169   4.518  15.282  1.00 20.67           C  
ATOM   1911  CG2 VAL B 111      -8.735   3.376  13.659  1.00 23.48           C  
ATOM   1912  N   CYS B 112      -7.910   7.938  14.371  1.00 23.48           N  
ATOM   1913  CA  CYS B 112      -7.369   9.163  14.979  1.00 24.04           C  
ATOM   1914  C   CYS B 112      -8.463  10.038  15.640  1.00 23.35           C  
ATOM   1915  O   CYS B 112      -8.257  10.631  16.702  1.00 23.08           O  
ATOM   1916  CB  CYS B 112      -6.580  10.022  13.959  1.00 23.47           C  
ATOM   1917  SG  CYS B 112      -5.003   9.307  13.439  1.00 25.09           S  
ATOM   1918  N   VAL B 113      -9.577  10.158  14.976  1.00 24.13           N  
ATOM   1919  CA  VAL B 113     -10.753  10.927  15.532  1.00 23.72           C  
ATOM   1920  C   VAL B 113     -11.278  10.267  16.812  1.00 25.47           C  
ATOM   1921  O   VAL B 113     -11.595  10.969  17.755  1.00 27.74           O  
ATOM   1922  CB  VAL B 113     -11.896  10.969  14.500  1.00 23.78           C  
ATOM   1923  CG1 VAL B 113     -13.204  11.600  15.084  1.00 22.95           C  
ATOM   1924  CG2 VAL B 113     -11.435  11.796  13.270  1.00 24.37           C  
ATOM   1925  N   LEU B 114     -11.366   8.917  16.835  1.00 24.99           N  
ATOM   1926  CA  LEU B 114     -11.831   8.211  17.990  1.00 25.53           C  
ATOM   1927  C   LEU B 114     -10.841   8.461  19.143  1.00 26.32           C  
ATOM   1928  O   LEU B 114     -11.236   8.767  20.268  1.00 31.76           O  
ATOM   1929  CB  LEU B 114     -11.971   6.724  17.621  1.00 26.55           C  
ATOM   1930  CG  LEU B 114     -13.088   6.325  16.660  1.00 28.75           C  
ATOM   1931  CD1 LEU B 114     -12.989   4.829  16.314  1.00 32.38           C  
ATOM   1932  CD2 LEU B 114     -14.528   6.716  17.141  1.00 29.68           C  
ATOM   1933  N   ALA B 115      -9.532   8.367  18.872  1.00 27.69           N  
ATOM   1934  CA  ALA B 115      -8.545   8.586  19.882  1.00 24.95           C  
ATOM   1935  C   ALA B 115      -8.687  10.057  20.480  1.00 28.49           C  
ATOM   1936  O   ALA B 115      -8.618  10.275  21.713  1.00 23.82           O  
ATOM   1937  CB  ALA B 115      -7.147   8.362  19.312  1.00 23.85           C  
ATOM   1938  N   HIS B 116      -8.799  11.027  19.582  1.00 28.61           N  
ATOM   1939  CA  HIS B 116      -9.048  12.427  19.919  1.00 30.62           C  
ATOM   1940  C   HIS B 116     -10.319  12.544  20.829  1.00 27.88           C  
ATOM   1941  O   HIS B 116     -10.258  13.137  21.902  1.00 35.16           O  
ATOM   1942  CB  HIS B 116      -9.266  13.255  18.641  1.00 28.82           C  
ATOM   1943  CG  HIS B 116      -9.247  14.748  18.863  1.00 35.80           C  
ATOM   1944  ND1 HIS B 116     -10.022  15.615  18.115  1.00 38.99           N  
ATOM   1945  CD2 HIS B 116      -8.513  15.529  19.705  1.00 33.47           C  
ATOM   1946  CE1 HIS B 116      -9.805  16.863  18.524  1.00 38.90           C  
ATOM   1947  NE2 HIS B 116      -8.883  16.839  19.472  1.00 34.24           N  
ATOM   1948  N   HIS B 117     -11.416  11.975  20.403  1.00 27.31           N  
ATOM   1949  CA AHIS B 117     -12.701  12.102  21.141  0.50 30.31           C  
ATOM   1950  CA BHIS B 117     -12.670  12.123  21.143  0.50 31.11           C  
ATOM   1951  C   HIS B 117     -12.675  11.366  22.487  1.00 32.49           C  
ATOM   1952  O   HIS B 117     -13.284  11.819  23.497  1.00 32.52           O  
ATOM   1953  CB AHIS B 117     -13.891  11.637  20.282  0.50 29.09           C  
ATOM   1954  CB BHIS B 117     -13.828  11.771  20.210  0.50 31.25           C  
ATOM   1955  CG AHIS B 117     -15.232  11.890  20.910  0.50 32.49           C  
ATOM   1956  CG BHIS B 117     -14.005  12.770  19.107  0.50 35.46           C  
ATOM   1957  ND1AHIS B 117     -15.927  13.067  20.738  0.50 33.16           N  
ATOM   1958  ND1BHIS B 117     -15.135  12.835  18.321  0.50 38.98           N  
ATOM   1959  CD2AHIS B 117     -15.994  11.121  21.726  0.50 32.13           C  
ATOM   1960  CD2BHIS B 117     -13.207  13.786  18.697  0.50 39.30           C  
ATOM   1961  CE1AHIS B 117     -17.060  13.012  21.420  0.50 34.31           C  
ATOM   1962  CE1BHIS B 117     -15.019  13.835  17.464  0.50 37.65           C  
ATOM   1963  NE2AHIS B 117     -17.126  11.837  22.023  0.50 33.09           N  
ATOM   1964  NE2BHIS B 117     -13.860  14.432  17.678  0.50 39.57           N  
ATOM   1965  N   PHE B 118     -11.992  10.226  22.527  1.00 31.10           N  
ATOM   1966  CA  PHE B 118     -12.058   9.369  23.696  1.00 29.36           C  
ATOM   1967  C   PHE B 118     -10.836   9.373  24.580  1.00 29.71           C  
ATOM   1968  O   PHE B 118     -10.882   8.848  25.659  1.00 34.30           O  
ATOM   1969  CB  PHE B 118     -12.470   7.938  23.311  1.00 30.87           C  
ATOM   1970  CG  PHE B 118     -13.896   7.814  22.838  1.00 34.00           C  
ATOM   1971  CD1 PHE B 118     -14.193   7.493  21.512  1.00 33.50           C  
ATOM   1972  CD2 PHE B 118     -14.962   7.969  23.739  1.00 34.70           C  
ATOM   1973  CE1 PHE B 118     -15.527   7.350  21.087  1.00 43.31           C  
ATOM   1974  CE2 PHE B 118     -16.303   7.826  23.331  1.00 33.95           C  
ATOM   1975  CZ  PHE B 118     -16.595   7.524  21.993  1.00 34.35           C  
ATOM   1976  N   GLY B 119      -9.710   9.924  24.143  1.00 26.82           N  
ATOM   1977  CA  GLY B 119      -8.566  10.025  25.028  1.00 29.44           C  
ATOM   1978  C   GLY B 119      -8.083   8.692  25.579  1.00 32.92           C  
ATOM   1979  O   GLY B 119      -8.051   7.690  24.857  1.00 28.41           O  
ATOM   1980  N   LYS B 120      -7.684   8.710  26.861  1.00 37.22           N  
ATOM   1981  CA  LYS B 120      -7.388   7.527  27.725  1.00 37.71           C  
ATOM   1982  C   LYS B 120      -8.237   6.314  27.433  1.00 29.89           C  
ATOM   1983  O   LYS B 120      -7.752   5.206  27.433  1.00 30.76           O  
ATOM   1984  CB  LYS B 120      -7.660   7.915  29.195  1.00 43.11           C  
ATOM   1985  CG  LYS B 120      -6.529   7.621  30.151  1.00 57.52           C  
ATOM   1986  CD  LYS B 120      -6.938   7.913  31.604  1.00 62.79           C  
ATOM   1987  CE  LYS B 120      -5.716   7.900  32.526  1.00 67.74           C  
ATOM   1988  NZ  LYS B 120      -4.848   6.705  32.285  1.00 64.10           N  
ATOM   1989  N   GLU B 121      -9.523   6.518  27.164  1.00 29.55           N  
ATOM   1990  CA  GLU B 121     -10.451   5.419  26.973  1.00 32.25           C  
ATOM   1991  C   GLU B 121     -10.151   4.658  25.677  1.00 35.99           C  
ATOM   1992  O   GLU B 121     -10.508   3.471  25.507  1.00 28.69           O  
ATOM   1993  CB  GLU B 121     -11.878   5.956  26.955  1.00 38.78           C  
ATOM   1994  CG  GLU B 121     -12.961   4.884  27.024  1.00 49.41           C  
ATOM   1995  CD  GLU B 121     -14.403   5.442  27.146  1.00 56.54           C  
ATOM   1996  OE1 GLU B 121     -14.610   6.675  27.354  1.00 48.76           O  
ATOM   1997  OE2 GLU B 121     -15.355   4.619  27.016  1.00 61.49           O  
ATOM   1998  N   PHE B 122      -9.472   5.334  24.741  1.00 29.10           N  
ATOM   1999  CA  PHE B 122      -9.121   4.640  23.482  1.00 28.00           C  
ATOM   2000  C   PHE B 122      -7.786   3.978  23.718  1.00 27.47           C  
ATOM   2001  O   PHE B 122      -6.729   4.473  23.232  1.00 25.12           O  
ATOM   2002  CB  PHE B 122      -8.961   5.645  22.335  1.00 25.88           C  
ATOM   2003  CG  PHE B 122      -8.997   5.008  20.973  1.00 26.80           C  
ATOM   2004  CD1 PHE B 122     -10.151   4.369  20.542  1.00 24.64           C  
ATOM   2005  CD2 PHE B 122      -7.846   4.985  20.163  1.00 25.53           C  
ATOM   2006  CE1 PHE B 122     -10.204   3.768  19.268  1.00 26.19           C  
ATOM   2007  CE2 PHE B 122      -7.892   4.386  18.904  1.00 22.35           C  
ATOM   2008  CZ  PHE B 122      -9.052   3.784  18.475  1.00 25.26           C  
ATOM   2009  N   THR B 123      -7.811   2.869  24.453  1.00 24.58           N  
ATOM   2010  CA  THR B 123      -6.597   2.236  24.946  1.00 24.81           C  
ATOM   2011  C   THR B 123      -5.868   1.457  23.776  1.00 23.79           C  
ATOM   2012  O   THR B 123      -6.456   1.217  22.729  1.00 26.76           O  
ATOM   2013  CB  THR B 123      -6.944   1.188  26.069  1.00 28.96           C  
ATOM   2014  OG1 THR B 123      -7.822   0.205  25.475  1.00 27.54           O  
ATOM   2015  CG2 THR B 123      -7.674   1.819  27.309  1.00 22.84           C  
ATOM   2016  N   PRO B 124      -4.583   1.059  23.952  1.00 25.85           N  
ATOM   2017  CA  PRO B 124      -3.931   0.319  22.828  1.00 26.11           C  
ATOM   2018  C   PRO B 124      -4.681  -0.953  22.384  1.00 25.74           C  
ATOM   2019  O   PRO B 124      -4.835  -1.189  21.184  1.00 21.95           O  
ATOM   2020  CB  PRO B 124      -2.519   0.042  23.366  1.00 24.73           C  
ATOM   2021  CG  PRO B 124      -2.304   1.197  24.313  1.00 25.63           C  
ATOM   2022  CD  PRO B 124      -3.620   1.297  25.043  1.00 27.41           C  
ATOM   2023  N   PRO B 125      -5.218  -1.779  23.340  1.00 29.12           N  
ATOM   2024  CA  PRO B 125      -6.114  -2.899  22.897  1.00 25.18           C  
ATOM   2025  C   PRO B 125      -7.394  -2.475  22.202  1.00 26.46           C  
ATOM   2026  O   PRO B 125      -7.891  -3.168  21.272  1.00 25.51           O  
ATOM   2027  CB  PRO B 125      -6.546  -3.521  24.245  1.00 30.68           C  
ATOM   2028  CG  PRO B 125      -5.323  -3.326  25.092  1.00 30.81           C  
ATOM   2029  CD  PRO B 125      -4.960  -1.855  24.797  1.00 30.02           C  
ATOM   2030  N   VAL B 126      -7.980  -1.366  22.661  1.00 24.00           N  
ATOM   2031  CA  VAL B 126      -9.162  -0.898  21.966  1.00 23.78           C  
ATOM   2032  C   VAL B 126      -8.816  -0.449  20.520  1.00 23.24           C  
ATOM   2033  O   VAL B 126      -9.609  -0.664  19.600  1.00 22.54           O  
ATOM   2034  CB  VAL B 126      -9.887   0.251  22.683  1.00 25.03           C  
ATOM   2035  CG1 VAL B 126     -11.021   0.746  21.777  1.00 28.00           C  
ATOM   2036  CG2 VAL B 126     -10.391  -0.196  24.091  1.00 25.63           C  
ATOM   2037  N   GLN B 127      -7.689   0.222  20.371  1.00 22.89           N  
ATOM   2038  CA  GLN B 127      -7.233   0.595  19.007  1.00 22.21           C  
ATOM   2039  C   GLN B 127      -7.054  -0.641  18.143  1.00 22.98           C  
ATOM   2040  O   GLN B 127      -7.589  -0.713  17.052  1.00 25.04           O  
ATOM   2041  CB  GLN B 127      -5.916   1.315  19.073  1.00 21.38           C  
ATOM   2042  CG  GLN B 127      -5.376   1.570  17.655  1.00 23.35           C  
ATOM   2043  CD  GLN B 127      -4.104   2.311  17.637  1.00 24.43           C  
ATOM   2044  OE1 GLN B 127      -3.564   2.687  18.661  1.00 23.45           O  
ATOM   2045  NE2 GLN B 127      -3.590   2.519  16.438  1.00 25.16           N  
ATOM   2046  N   ALA B 128      -6.298  -1.621  18.632  1.00 22.33           N  
ATOM   2047  CA  ALA B 128      -6.080  -2.906  17.880  1.00 21.93           C  
ATOM   2048  C   ALA B 128      -7.322  -3.514  17.342  1.00 24.89           C  
ATOM   2049  O   ALA B 128      -7.369  -3.852  16.166  1.00 25.16           O  
ATOM   2050  CB  ALA B 128      -5.276  -3.891  18.735  1.00 20.59           C  
ATOM   2051  N   ALA B 129      -8.404  -3.528  18.146  1.00 26.32           N  
ATOM   2052  CA  ALA B 129      -9.656  -4.084  17.701  1.00 28.47           C  
ATOM   2053  C   ALA B 129     -10.263  -3.198  16.593  1.00 28.51           C  
ATOM   2054  O   ALA B 129     -10.700  -3.714  15.559  1.00 29.89           O  
ATOM   2055  CB  ALA B 129     -10.678  -4.232  18.876  1.00 27.71           C  
ATOM   2056  N   TYR B 130     -10.318  -1.884  16.812  1.00 25.34           N  
ATOM   2057  CA  TYR B 130     -10.749  -0.968  15.717  1.00 23.61           C  
ATOM   2058  C   TYR B 130      -9.871  -1.089  14.465  1.00 24.36           C  
ATOM   2059  O   TYR B 130     -10.381  -0.929  13.384  1.00 24.00           O  
ATOM   2060  CB  TYR B 130     -10.789   0.493  16.182  1.00 25.89           C  
ATOM   2061  CG  TYR B 130     -12.132   0.813  16.770  1.00 26.94           C  
ATOM   2062  CD1 TYR B 130     -13.195   1.259  15.971  1.00 28.79           C  
ATOM   2063  CD2 TYR B 130     -12.361   0.619  18.134  1.00 32.77           C  
ATOM   2064  CE1 TYR B 130     -14.444   1.502  16.521  1.00 29.19           C  
ATOM   2065  CE2 TYR B 130     -13.588   0.893  18.691  1.00 31.15           C  
ATOM   2066  CZ  TYR B 130     -14.611   1.283  17.891  1.00 29.17           C  
ATOM   2067  OH  TYR B 130     -15.783   1.542  18.498  1.00 32.68           O  
ATOM   2068  N   GLN B 131      -8.572  -1.396  14.588  1.00 23.80           N  
ATOM   2069  CA  GLN B 131      -7.766  -1.539  13.320  1.00 23.93           C  
ATOM   2070  C   GLN B 131      -8.269  -2.773  12.521  1.00 28.44           C  
ATOM   2071  O   GLN B 131      -8.331  -2.768  11.264  1.00 27.58           O  
ATOM   2072  CB  GLN B 131      -6.234  -1.623  13.613  1.00 23.28           C  
ATOM   2073  CG  GLN B 131      -5.663  -0.389  14.350  1.00 23.97           C  
ATOM   2074  CD  GLN B 131      -5.462   0.882  13.481  1.00 23.79           C  
ATOM   2075  OE1 GLN B 131      -5.143   1.926  14.034  1.00 26.24           O  
ATOM   2076  NE2 GLN B 131      -5.697   0.805  12.125  1.00 22.70           N  
ATOM   2077  N   LYS B 132      -8.594  -3.858  13.223  1.00 30.88           N  
ATOM   2078  CA  LYS B 132      -9.092  -5.059  12.504  1.00 28.14           C  
ATOM   2079  C   LYS B 132     -10.361  -4.674  11.804  1.00 26.10           C  
ATOM   2080  O   LYS B 132     -10.611  -4.995  10.655  1.00 28.77           O  
ATOM   2081  CB  LYS B 132      -9.411  -6.237  13.479  1.00 32.06           C  
ATOM   2082  CG  LYS B 132      -8.227  -6.828  14.131  1.00 36.99           C  
ATOM   2083  CD  LYS B 132      -8.493  -8.193  14.686  1.00 44.02           C  
ATOM   2084  CE  LYS B 132      -7.251  -8.657  15.432  1.00 42.74           C  
ATOM   2085  NZ  LYS B 132      -7.625  -9.926  16.113  1.00 52.87           N  
ATOM   2086  N   VAL B 133     -11.180  -3.904  12.479  1.00 28.07           N  
ATOM   2087  CA  VAL B 133     -12.416  -3.437  11.866  1.00 28.59           C  
ATOM   2088  C   VAL B 133     -12.235  -2.542  10.609  1.00 28.98           C  
ATOM   2089  O   VAL B 133     -12.879  -2.764   9.583  1.00 30.98           O  
ATOM   2090  CB  VAL B 133     -13.315  -2.678  12.874  1.00 32.18           C  
ATOM   2091  CG1 VAL B 133     -14.498  -2.086  12.115  1.00 36.47           C  
ATOM   2092  CG2 VAL B 133     -13.803  -3.609  13.987  1.00 31.90           C  
ATOM   2093  N   VAL B 134     -11.409  -1.514  10.680  1.00 30.58           N  
ATOM   2094  CA  VAL B 134     -11.373  -0.600   9.544  1.00 30.61           C  
ATOM   2095  C   VAL B 134     -10.588  -1.265   8.440  1.00 30.18           C  
ATOM   2096  O   VAL B 134     -10.839  -0.995   7.279  1.00 31.09           O  
ATOM   2097  CB  VAL B 134     -10.802   0.802   9.889  1.00 31.13           C  
ATOM   2098  CG1 VAL B 134     -11.654   1.539  10.957  1.00 31.32           C  
ATOM   2099  CG2 VAL B 134      -9.342   0.712  10.309  1.00 31.19           C  
ATOM   2100  N   ALA B 135      -9.679  -2.177   8.790  1.00 32.94           N  
ATOM   2101  CA  ALA B 135      -9.061  -3.024   7.777  1.00 30.43           C  
ATOM   2102  C   ALA B 135     -10.108  -3.869   7.062  1.00 33.57           C  
ATOM   2103  O   ALA B 135     -10.068  -3.999   5.835  1.00 31.47           O  
ATOM   2104  CB  ALA B 135      -7.918  -3.878   8.352  1.00 30.03           C  
ATOM   2105  N   GLY B 136     -11.053  -4.450   7.809  1.00 30.64           N  
ATOM   2106  CA  GLY B 136     -12.039  -5.321   7.172  1.00 30.21           C  
ATOM   2107  C   GLY B 136     -12.971  -4.548   6.235  1.00 30.98           C  
ATOM   2108  O   GLY B 136     -13.295  -5.017   5.157  1.00 29.95           O  
ATOM   2109  N   VAL B 137     -13.390  -3.356   6.629  1.00 30.49           N  
ATOM   2110  CA  VAL B 137     -14.237  -2.505   5.774  1.00 31.26           C  
ATOM   2111  C   VAL B 137     -13.552  -1.998   4.480  1.00 29.07           C  
ATOM   2112  O   VAL B 137     -14.123  -2.054   3.392  1.00 28.13           O  
ATOM   2113  CB  VAL B 137     -14.699  -1.294   6.622  1.00 32.13           C  
ATOM   2114  CG1 VAL B 137     -15.308  -0.210   5.752  1.00 30.07           C  
ATOM   2115  CG2 VAL B 137     -15.676  -1.786   7.703  1.00 30.40           C  
ATOM   2116  N   ALA B 138     -12.314  -1.506   4.628  1.00 28.14           N  
ATOM   2117  CA  ALA B 138     -11.492  -1.100   3.463  1.00 31.24           C  
ATOM   2118  C   ALA B 138     -11.445  -2.279   2.459  1.00 28.91           C  
ATOM   2119  O   ALA B 138     -11.613  -2.097   1.256  1.00 29.02           O  
ATOM   2120  CB  ALA B 138     -10.064  -0.759   3.908  1.00 23.06           C  
ATOM   2121  N   ASN B 139     -11.164  -3.471   2.976  1.00 29.76           N  
ATOM   2122  CA  ASN B 139     -10.962  -4.632   2.110  1.00 32.06           C  
ATOM   2123  C   ASN B 139     -12.259  -5.028   1.389  1.00 34.90           C  
ATOM   2124  O   ASN B 139     -12.224  -5.385   0.208  1.00 33.73           O  
ATOM   2125  CB  ASN B 139     -10.372  -5.800   2.927  1.00 36.50           C  
ATOM   2126  CG  ASN B 139     -10.237  -7.092   2.123  1.00 44.01           C  
ATOM   2127  OD1 ASN B 139      -9.414  -7.205   1.199  1.00 48.57           O  
ATOM   2128  ND2 ASN B 139     -11.018  -8.094   2.501  1.00 45.04           N  
ATOM   2129  N   ALA B 140     -13.401  -4.898   2.086  1.00 34.11           N  
ATOM   2130  CA  ALA B 140     -14.697  -5.201   1.510  1.00 32.64           C  
ATOM   2131  C   ALA B 140     -15.109  -4.137   0.505  1.00 33.34           C  
ATOM   2132  O   ALA B 140     -15.598  -4.458  -0.611  1.00 30.00           O  
ATOM   2133  CB  ALA B 140     -15.742  -5.362   2.606  1.00 28.69           C  
ATOM   2134  N   LEU B 141     -14.827  -2.877   0.819  1.00 33.12           N  
ATOM   2135  CA  LEU B 141     -15.104  -1.791  -0.141  1.00 33.21           C  
ATOM   2136  C   LEU B 141     -14.236  -1.958  -1.380  1.00 33.97           C  
ATOM   2137  O   LEU B 141     -14.586  -1.506  -2.464  1.00 35.30           O  
ATOM   2138  CB  LEU B 141     -14.815  -0.426   0.494  1.00 35.73           C  
ATOM   2139  CG  LEU B 141     -15.533   0.811  -0.047  1.00 40.60           C  
ATOM   2140  CD1 LEU B 141     -17.063   0.654  -0.136  1.00 36.17           C  
ATOM   2141  CD2 LEU B 141     -15.162   2.028   0.779  1.00 38.31           C  
ATOM   2142  N   ALA B 142     -13.091  -2.619  -1.249  1.00 35.07           N  
ATOM   2143  CA  ALA B 142     -12.228  -2.753  -2.419  1.00 34.04           C  
ATOM   2144  C   ALA B 142     -12.490  -4.059  -3.214  1.00 36.18           C  
ATOM   2145  O   ALA B 142     -11.762  -4.366  -4.175  1.00 34.27           O  
ATOM   2146  CB  ALA B 142     -10.753  -2.675  -1.996  1.00 35.51           C  
ATOM   2147  N   HIS B 143     -13.481  -4.857  -2.820  1.00 39.01           N  
ATOM   2148  CA  HIS B 143     -13.661  -6.167  -3.475  1.00 36.84           C  
ATOM   2149  C   HIS B 143     -13.903  -6.052  -5.012  1.00 37.80           C  
ATOM   2150  O   HIS B 143     -13.405  -6.880  -5.761  1.00 37.69           O  
ATOM   2151  CB  HIS B 143     -14.777  -6.984  -2.815  1.00 45.61           C  
ATOM   2152  CG  HIS B 143     -14.977  -8.353  -3.406  1.00 44.77           C  
ATOM   2153  ND1 HIS B 143     -14.256  -9.456  -2.998  1.00 50.57           N  
ATOM   2154  CD2 HIS B 143     -15.845  -8.801  -4.349  1.00 47.73           C  
ATOM   2155  CE1 HIS B 143     -14.648 -10.518  -3.684  1.00 49.61           C  
ATOM   2156  NE2 HIS B 143     -15.615 -10.147  -4.510  1.00 45.22           N  
ATOM   2157  N   LYS B 144     -14.647  -5.042  -5.464  1.00 39.69           N  
ATOM   2158  CA  LYS B 144     -14.842  -4.789  -6.911  1.00 47.18           C  
ATOM   2159  C   LYS B 144     -13.564  -4.520  -7.724  1.00 51.17           C  
ATOM   2160  O   LYS B 144     -13.623  -4.394  -8.939  1.00 51.93           O  
ATOM   2161  CB  LYS B 144     -15.920  -3.725  -7.154  1.00 50.15           C  
ATOM   2162  CG  LYS B 144     -17.335  -4.229  -6.899  1.00 51.96           C  
ATOM   2163  CD  LYS B 144     -17.644  -5.545  -7.621  1.00 55.49           C  
ATOM   2164  CE  LYS B 144     -18.010  -5.353  -9.090  1.00 56.26           C  
ATOM   2165  NZ  LYS B 144     -18.429  -6.661  -9.683  1.00 54.42           N  
ATOM   2166  N   TYR B 145     -12.421  -4.426  -7.029  1.00 55.58           N  
ATOM   2167  CA  TYR B 145     -11.071  -4.438  -7.632  1.00 56.02           C  
ATOM   2168  C   TYR B 145     -10.345  -5.800  -7.593  1.00 59.73           C  
ATOM   2169  O   TYR B 145      -9.421  -5.996  -8.366  1.00 70.16           O  
ATOM   2170  CB  TYR B 145     -10.153  -3.438  -6.914  1.00 44.96           C  
ATOM   2171  CG  TYR B 145     -10.466  -1.964  -7.091  1.00 43.19           C  
ATOM   2172  CD1 TYR B 145     -10.527  -1.390  -8.355  1.00 42.66           C  
ATOM   2173  CD2 TYR B 145     -10.673  -1.144  -5.986  1.00 41.74           C  
ATOM   2174  CE1 TYR B 145     -10.787  -0.042  -8.516  1.00 42.57           C  
ATOM   2175  CE2 TYR B 145     -10.929   0.218  -6.128  1.00 38.39           C  
ATOM   2176  CZ  TYR B 145     -10.988   0.758  -7.395  1.00 39.74           C  
ATOM   2177  OH  TYR B 145     -11.222   2.103  -7.549  1.00 40.97           O  
ATOM   2178  N   HIS B 146     -10.704  -6.715  -6.690  1.00 56.50           N  
ATOM   2179  CA  HIS B 146      -9.951  -7.993  -6.568  1.00 58.25           C  
ATOM   2180  C   HIS B 146     -10.362  -9.059  -7.575  1.00 67.54           C  
ATOM   2181  O   HIS B 146     -11.069  -8.800  -8.560  1.00 67.68           O  
ATOM   2182  CB  HIS B 146     -10.005  -8.586  -5.149  1.00 56.74           C  
ATOM   2183  CG  HIS B 146      -9.786  -7.579  -4.060  1.00 62.21           C  
ATOM   2184  ND1 HIS B 146     -10.288  -7.746  -2.782  1.00 68.42           N  
ATOM   2185  CD2 HIS B 146      -9.159  -6.379  -4.066  1.00 56.05           C  
ATOM   2186  CE1 HIS B 146      -9.952  -6.705  -2.039  1.00 60.16           C  
ATOM   2187  NE2 HIS B 146      -9.261  -5.863  -2.794  1.00 69.71           N  
ATOM   2188  OXT HIS B 146      -9.965 -10.218  -7.413  1.00 73.35           O  
TER    2189      HIS B 146                                                      
HETATM 2190  CHA HEM A 201      16.410   1.201  16.837  1.00 25.26           C  
HETATM 2191  CHB HEM A 201      14.217   5.418  16.105  1.00 26.14           C  
HETATM 2192  CHC HEM A 201      11.025   3.358  13.154  1.00 22.43           C  
HETATM 2193  CHD HEM A 201      12.738  -0.984  14.508  1.00 20.78           C  
HETATM 2194  C1A HEM A 201      16.087   2.536  16.860  1.00 24.32           C  
HETATM 2195  C2A HEM A 201      16.810   3.552  17.572  1.00 24.97           C  
HETATM 2196  C3A HEM A 201      16.160   4.747  17.377  1.00 26.83           C  
HETATM 2197  C4A HEM A 201      15.064   4.469  16.526  1.00 25.03           C  
HETATM 2198  CMA HEM A 201      16.511   6.138  17.971  1.00 22.80           C  
HETATM 2199  CAA HEM A 201      18.072   3.333  18.428  1.00 25.12           C  
HETATM 2200  CBA HEM A 201      17.876   2.596  19.726  1.00 37.42           C  
HETATM 2201  CGA HEM A 201      19.273   2.539  20.375  1.00 47.05           C  
HETATM 2202  O1A HEM A 201      19.506   1.767  21.341  1.00 47.41           O  
HETATM 2203  O2A HEM A 201      20.228   3.241  19.929  1.00 49.02           O  
HETATM 2204  C1B HEM A 201      13.196   5.265  15.192  1.00 25.56           C  
HETATM 2205  C2B HEM A 201      12.340   6.342  14.742  1.00 22.20           C  
HETATM 2206  C3B HEM A 201      11.423   5.751  13.940  1.00 21.70           C  
HETATM 2207  C4B HEM A 201      11.745   4.280  13.908  1.00 22.39           C  
HETATM 2208  CMB HEM A 201      12.407   7.869  14.963  1.00 22.36           C  
HETATM 2209  CAB HEM A 201      10.364   6.352  13.090  1.00 22.89           C  
HETATM 2210  CBB HEM A 201       9.592   7.392  13.424  1.00 22.66           C  
HETATM 2211  C1C HEM A 201      11.189   1.968  13.267  1.00 22.92           C  
HETATM 2212  C2C HEM A 201      10.343   0.980  12.753  1.00 21.93           C  
HETATM 2213  C3C HEM A 201      10.844  -0.269  13.139  1.00 21.89           C  
HETATM 2214  C4C HEM A 201      11.998  -0.010  13.869  1.00 20.36           C  
HETATM 2215  CMC HEM A 201       9.151   1.239  11.889  1.00 22.76           C  
HETATM 2216  CAC HEM A 201      10.283  -1.622  12.783  1.00 21.69           C  
HETATM 2217  CBC HEM A 201       8.972  -1.917  13.012  1.00 24.51           C  
HETATM 2218  C1D HEM A 201      13.850  -0.709  15.281  1.00 22.02           C  
HETATM 2219  C2D HEM A 201      14.671  -1.819  15.850  1.00 22.76           C  
HETATM 2220  C3D HEM A 201      15.686  -1.209  16.501  1.00 24.68           C  
HETATM 2221  C4D HEM A 201      15.488   0.257  16.301  1.00 23.23           C  
HETATM 2222  CMD HEM A 201      14.400  -3.340  15.737  1.00 21.20           C  
HETATM 2223  CAD HEM A 201      16.819  -1.929  17.254  1.00 26.82           C  
HETATM 2224  CBD HEM A 201      16.219  -2.120  18.662  1.00 31.47           C  
HETATM 2225  CGD HEM A 201      17.111  -2.912  19.610  1.00 36.14           C  
HETATM 2226  O1D HEM A 201      17.364  -2.424  20.688  1.00 33.26           O  
HETATM 2227  O2D HEM A 201      17.525  -4.093  19.437  1.00 37.38           O  
HETATM 2228  NA  HEM A 201      15.009   3.112  16.225  1.00 24.81           N  
HETATM 2229  NB  HEM A 201      12.801   4.093  14.655  1.00 21.93           N  
HETATM 2230  NC  HEM A 201      12.163   1.354  13.956  1.00 23.33           N  
HETATM 2231  ND  HEM A 201      14.393   0.497  15.541  1.00 23.92           N  
HETATM 2232 FE   HEM A 201      13.619   2.246  15.093  1.00 23.08          FE  
HETATM 2233  C   MBN A 202       5.394  16.497  17.942  1.00 47.64           C  
HETATM 2234  C1  MBN A 202       6.668  16.042  18.553  1.00 50.82           C  
HETATM 2235  C2  MBN A 202       6.694  15.670  19.887  1.00 46.51           C  
HETATM 2236  C3  MBN A 202       7.876  15.281  20.462  1.00 44.69           C  
HETATM 2237  C4  MBN A 202       9.016  15.242  19.722  1.00 45.48           C  
HETATM 2238  C5  MBN A 202       8.988  15.588  18.378  1.00 46.75           C  
HETATM 2239  C6  MBN A 202       7.817  15.991  17.767  1.00 47.88           C  
HETATM 2240  C   MBN A 203      -0.519   2.644  31.696  0.50 43.70           C  
HETATM 2241  C1  MBN A 203      -1.113   1.686  32.699  0.50 46.77           C  
HETATM 2242  C2  MBN A 203      -0.299   1.108  33.665  0.50 45.96           C  
HETATM 2243  C3  MBN A 203      -0.835   0.229  34.589  0.50 47.04           C  
HETATM 2244  C4  MBN A 203      -2.189  -0.077  34.558  0.50 47.62           C  
HETATM 2245  C5  MBN A 203      -3.007   0.500  33.596  0.50 48.57           C  
HETATM 2246  C6  MBN A 203      -2.467   1.381  32.666  0.50 46.86           C  
HETATM 2247  C   MBN A 204       4.391  12.098  17.532  1.00 49.87           C  
HETATM 2248  C1  MBN A 204       5.189  11.857  18.792  1.00 44.41           C  
HETATM 2249  C2  MBN A 204       6.442  12.464  18.942  1.00 49.19           C  
HETATM 2250  C3  MBN A 204       7.220  12.221  20.079  1.00 52.72           C  
HETATM 2251  C4  MBN A 204       6.729  11.373  21.065  1.00 47.44           C  
HETATM 2252  C5  MBN A 204       5.474  10.779  20.920  1.00 44.69           C  
HETATM 2253  C6  MBN A 204       4.687  11.004  19.782  1.00 47.56           C  
HETATM 2254  N   NO2 A 205       6.434   4.020   0.454  0.50 35.05           N  
HETATM 2255  O1  NO2 A 205       6.613   3.270   1.412  0.50 31.30           O  
HETATM 2256  O2  NO2 A 205       5.103   4.360   0.204  0.50 39.58           O  
HETATM 2257  N    NO A 206      12.595   2.041  16.535  1.00 21.04           N  
HETATM 2258  O    NO A 206      11.445   2.056  16.808  1.00 35.33           O  
HETATM 2259  CHA HEM B 201     -20.166   8.327  -1.539  1.00 34.08           C  
HETATM 2260  CHB HEM B 201     -19.055   5.376   2.180  1.00 33.13           C  
HETATM 2261  CHC HEM B 201     -14.321   6.039   1.237  1.00 35.00           C  
HETATM 2262  CHD HEM B 201     -15.449   9.144  -2.355  1.00 35.89           C  
HETATM 2263  C1A HEM B 201     -20.220   7.471  -0.474  1.00 34.06           C  
HETATM 2264  C2A HEM B 201     -21.452   7.136   0.155  1.00 34.69           C  
HETATM 2265  C3A HEM B 201     -21.169   6.298   1.245  1.00 30.07           C  
HETATM 2266  C4A HEM B 201     -19.747   6.155   1.260  1.00 32.45           C  
HETATM 2267  CMA HEM B 201     -22.042   5.595   2.274  1.00 34.57           C  
HETATM 2268  CAA HEM B 201     -22.735   7.685  -0.394  1.00 32.08           C  
HETATM 2269  CBA HEM B 201     -23.291   6.643  -1.368  1.00 40.29           C  
HETATM 2270  CGA HEM B 201     -24.772   6.883  -1.639  1.00 47.86           C  
HETATM 2271  O1A HEM B 201     -25.252   8.055  -1.648  1.00 36.84           O  
HETATM 2272  O2A HEM B 201     -25.524   5.886  -1.834  1.00 47.84           O  
HETATM 2273  C1B HEM B 201     -17.673   5.274   2.241  1.00 34.34           C  
HETATM 2274  C2B HEM B 201     -16.967   4.445   3.185  1.00 35.87           C  
HETATM 2275  C3B HEM B 201     -15.603   4.620   2.937  1.00 36.40           C  
HETATM 2276  C4B HEM B 201     -15.508   5.572   1.794  1.00 36.42           C  
HETATM 2277  CMB HEM B 201     -17.551   3.534   4.266  1.00 30.64           C  
HETATM 2278  CAB HEM B 201     -14.525   3.906   3.653  1.00 36.12           C  
HETATM 2279  CBB HEM B 201     -13.336   4.373   3.951  1.00 52.23           C  
HETATM 2280  C1C HEM B 201     -14.188   6.983   0.223  1.00 37.96           C  
HETATM 2281  C2C HEM B 201     -12.989   7.617  -0.184  1.00 38.93           C  
HETATM 2282  C3C HEM B 201     -13.314   8.487  -1.237  1.00 34.26           C  
HETATM 2283  C4C HEM B 201     -14.732   8.404  -1.431  1.00 38.10           C  
HETATM 2284  CMC HEM B 201     -11.649   7.337   0.455  1.00 30.13           C  
HETATM 2285  CAC HEM B 201     -12.426   9.410  -1.983  1.00 37.72           C  
HETATM 2286  CBC HEM B 201     -11.305   9.877  -1.426  1.00 34.28           C  
HETATM 2287  C1D HEM B 201     -16.845   9.109  -2.365  1.00 38.31           C  
HETATM 2288  C2D HEM B 201     -17.583   9.949  -3.309  1.00 37.69           C  
HETATM 2289  C3D HEM B 201     -18.901   9.729  -3.085  1.00 35.75           C  
HETATM 2290  C4D HEM B 201     -18.945   8.765  -1.997  1.00 38.90           C  
HETATM 2291  CMD HEM B 201     -16.930  10.858  -4.324  1.00 36.19           C  
HETATM 2292  CAD HEM B 201     -20.097  10.359  -3.791  1.00 40.57           C  
HETATM 2293  CBD HEM B 201     -20.463   9.491  -4.994  1.00 50.32           C  
HETATM 2294  CGD HEM B 201     -21.863   9.722  -5.558  1.00 58.17           C  
HETATM 2295  O1D HEM B 201     -22.873   9.788  -4.794  1.00 56.08           O  
HETATM 2296  O2D HEM B 201     -22.005   9.805  -6.812  1.00 54.64           O  
HETATM 2297  NA  HEM B 201     -19.194   6.915   0.268  1.00 32.64           N  
HETATM 2298  NB  HEM B 201     -16.788   5.911   1.446  1.00 36.30           N  
HETATM 2299  NC  HEM B 201     -15.217   7.526  -0.498  1.00 40.32           N  
HETATM 2300  ND  HEM B 201     -17.693   8.427  -1.552  1.00 37.30           N  
HETATM 2301 FE   HEM B 201     -17.249   7.204  -0.141  1.00 36.71          FE  
HETATM 2302  N    NO B 202     -17.342   8.973   1.046  0.80 32.97           N  
HETATM 2303  O    NO B 202     -16.413   9.453   1.639  0.80 39.40           O  
HETATM 2304  O   HOH A 301      -2.772   7.990  10.360  1.00 22.92           O  
HETATM 2305  O   HOH A 302       7.283  -3.312   1.546  1.00 27.64           O  
HETATM 2306  O   HOH A 303      -7.848  13.328  23.363  1.00 29.81           O  
HETATM 2307  O   HOH A 304       0.481  -6.542  11.267  1.00 31.31           O  
HETATM 2308  O   HOH A 305       4.418  -5.283   8.678  1.00 24.92           O  
HETATM 2309  O   HOH A 306       5.371   7.286   7.359  1.00 28.98           O  
HETATM 2310  O   HOH A 307      -7.341  23.236  12.034  1.00 31.61           O  
HETATM 2311  O   HOH A 308      -0.276   8.507   9.874  1.00 24.61           O  
HETATM 2312  O   HOH A 309       8.284  10.737  29.385  1.00 34.11           O  
HETATM 2313  O   HOH A 310       6.318  -0.145  28.609  1.00 39.61           O  
HETATM 2314  O   HOH A 311       8.022  16.928  23.664  1.00 36.53           O  
HETATM 2315  O   HOH A 312       4.330  -2.764  25.904  1.00 30.66           O  
HETATM 2316  O   HOH A 313       1.151   6.550   8.322  1.00 26.16           O  
HETATM 2317  O   HOH A 314       7.806  -7.291   6.249  1.00 26.76           O  
HETATM 2318  O   HOH A 315       7.582   4.298   4.043  1.00 29.04           O  
HETATM 2319  O   HOH A 316      -4.746   9.316  26.899  1.00 25.77           O  
HETATM 2320  O   HOH A 317       2.710  10.180   8.657  1.00 32.30           O  
HETATM 2321  O   HOH A 318      -1.709  22.027   8.180  1.00 32.16           O  
HETATM 2322  O   HOH A 319       3.812   0.342  29.223  1.00 50.18           O  
HETATM 2323  O   HOH A 320       3.361   8.357   7.351  1.00 32.08           O  
HETATM 2324  O   HOH A 321       3.892   4.741  28.157  1.00 29.72           O  
HETATM 2325  O   HOH A 322       6.716   6.209   4.774  1.00 38.77           O  
HETATM 2326  O   HOH A 323       7.150  -6.321   8.801  1.00 31.29           O  
HETATM 2327  O   HOH A 324      16.519   0.414  22.318  1.00 36.23           O  
HETATM 2328  O   HOH A 325      14.911  18.518   6.434  1.00 35.93           O  
HETATM 2329  O   HOH A 326      17.479   8.424  20.306  1.00 35.03           O  
HETATM 2330  O   HOH A 327       1.618 -12.317  17.052  1.00 46.67           O  
HETATM 2331  O   HOH A 328       3.322  28.361   5.848  1.00 39.93           O  
HETATM 2332  O   HOH A 329      16.834  14.558  21.338  1.00 39.51           O  
HETATM 2333  O   HOH A 330      -4.752  24.558  14.835  1.00 28.52           O  
HETATM 2334  O   HOH A 331       5.549   1.136   1.674  1.00 33.79           O  
HETATM 2335  O   HOH A 332      -3.435   6.919  26.360  1.00 29.30           O  
HETATM 2336  O   HOH A 333      12.031  13.848  23.978  1.00 54.42           O  
HETATM 2337  O   HOH A 334       0.282  -8.396  18.906  1.00 37.07           O  
HETATM 2338  O   HOH A 335      17.338  24.006  13.325  1.00 38.59           O  
HETATM 2339  O   HOH A 336      16.299   4.772  26.711  1.00 30.89           O  
HETATM 2340  O   HOH A 337      -3.199  13.022  28.825  1.00 47.16           O  
HETATM 2341  O   HOH A 338       0.885  -4.961  25.435  1.00 45.48           O  
HETATM 2342  O   HOH A 339       8.923 -10.713  18.874  1.00 36.17           O  
HETATM 2343  O   HOH A 340      -0.279  12.610  29.755  1.00 42.81           O  
HETATM 2344  O   HOH A 341      -2.132  -1.887  26.746  1.00 37.11           O  
HETATM 2345  O   HOH A 342      -4.408  -3.839   9.880  1.00 47.64           O  
HETATM 2346  O   HOH A 343       5.918  -1.849  35.007  1.00 49.48           O  
HETATM 2347  O   HOH A 344       9.487 -10.496  21.420  1.00 39.71           O  
HETATM 2348  O   HOH A 345      -8.772  20.299  18.989  1.00 48.35           O  
HETATM 2349  O   HOH A 346      15.641  -6.607  14.469  1.00 41.71           O  
HETATM 2350  O   HOH A 347       1.085  27.786  12.066  1.00 41.22           O  
HETATM 2351  O   HOH A 348       1.355  25.582   5.103  1.00 50.22           O  
HETATM 2352  O   HOH A 349      -1.604  26.014  10.730  1.00 43.23           O  
HETATM 2353  O   HOH A 350       0.705   2.011  26.674  1.00 38.91           O  
HETATM 2354  O   HOH A 351      14.986  -0.761  25.823  1.00 42.86           O  
HETATM 2355  O   HOH A 352       7.093 -10.273  24.279  1.00 35.10           O  
HETATM 2356  O   HOH A 353      20.367  17.565   6.019  1.00 32.31           O  
HETATM 2357  O   HOH A 354      20.024  10.394   6.331  1.00 41.48           O  
HETATM 2358  O   HOH A 355      23.371  10.860  12.332  1.00 42.61           O  
HETATM 2359  O   HOH A 356      20.820   9.771  13.322  1.00 34.35           O  
HETATM 2360  O   HOH A 357      13.522   8.104   0.849  1.00 43.23           O  
HETATM 2361  O   HOH A 358       5.781  18.233   3.225  1.00 55.83           O  
HETATM 2362  O   HOH A 359      -3.257  -5.738  11.648  1.00 54.13           O  
HETATM 2363  O   HOH A 360       2.810  -6.966  31.728  1.00 39.44           O  
HETATM 2364  O   HOH A 361      21.804  13.366  15.365  1.00 33.77           O  
HETATM 2365  O   HOH A 362      19.845  22.469  11.922  1.00 45.68           O  
HETATM 2366  O   HOH A 363       3.302   1.853  27.506  1.00 47.84           O  
HETATM 2367  O   HOH B 301     -21.061  14.553  10.275  1.00 30.46           O  
HETATM 2368  O   HOH B 302     -21.202  11.792  11.211  1.00 39.01           O  
HETATM 2369  O   HOH B 303      -3.839  10.428   9.630  1.00 24.78           O  
HETATM 2370  O   HOH B 304      -3.927   0.729  -7.066  1.00 38.06           O  
HETATM 2371  O   HOH B 305      -5.032   4.650  26.624  1.00 27.82           O  
HETATM 2372  O   HOH B 306     -14.622  14.239  24.257  1.00 35.03           O  
HETATM 2373  O   HOH B 307     -18.827  17.077  11.898  1.00 45.66           O  
HETATM 2374  O   HOH B 308      -1.031   6.938  -0.146  1.00 27.37           O  
HETATM 2375  O   HOH B 309     -13.351  -7.414   4.696  1.00 33.97           O  
HETATM 2376  O   HOH B 310      -3.869   0.616  -3.827  1.00 31.89           O  
HETATM 2377  O   HOH B 311      -9.956  23.350  11.364  1.00 35.59           O  
HETATM 2378  O   HOH B 312      -2.880   5.994   7.524  1.00 41.19           O  
HETATM 2379  O   HOH B 313      -5.948  -1.469  10.334  1.00 28.09           O  
HETATM 2380  O   HOH B 314      -3.178   0.607   8.228  1.00 45.19           O  
HETATM 2381  O   HOH B 315     -25.153  10.428  18.463  1.00 35.49           O  
HETATM 2382  O   HOH B 316     -23.048  -1.473  -0.236  1.00 42.97           O  
HETATM 2383  O   HOH B 317     -22.891  16.897   1.293  1.00 52.50           O  
HETATM 2384  O   HOH B 318     -24.241  -4.320  -0.830  1.00 49.34           O  
HETATM 2385  O   HOH B 319     -18.460  11.536  19.630  1.00 49.33           O  
HETATM 2386  O   HOH B 320      -0.587   5.825   6.372  1.00 32.42           O  
HETATM 2387  O   HOH B 321      -6.855  -1.170  -7.767  1.00 40.79           O  
HETATM 2388  O   HOH B 322      -8.640  -1.637  27.062  1.00 37.76           O  
HETATM 2389  O   HOH B 323     -13.046   9.543  27.241  1.00 46.02           O  
HETATM 2390  O   HOH B 324     -16.124 -11.025  14.205  1.00 53.91           O  
HETATM 2391  O   HOH B 325       2.706   0.793   1.405  1.00 37.69           O  
HETATM 2392  O   HOH B 326     -11.998   0.848 -11.792  1.00 48.17           O  
HETATM 2393  O   HOH B 327      -8.913   7.569 -10.106  1.00 44.29           O  
HETATM 2394  O   HOH B 328     -11.505 -10.903  -1.088  1.00 55.76           O  
HETATM 2395  O   HOH B 329       0.149   7.190   4.266  1.00 40.34           O  
HETATM 2396  O   HOH B 330     -14.420   0.107  24.726  1.00 40.57           O  
HETATM 2397  O   HOH B 331      -3.969  -0.433  -1.552  1.00 43.84           O  
HETATM 2398  O   HOH B 332     -17.261  16.541  -6.622  1.00 58.36           O  
HETATM 2399  O   HOH B 333      -7.219  -6.000  21.283  1.00 34.41           O  
HETATM 2400  O   HOH B 334     -29.686  13.888  13.544  1.00 40.73           O  
HETATM 2401  O   HOH B 335       0.265   1.660   2.122  1.00 41.94           O  
HETATM 2402  O   HOH B 336     -16.850  18.582  10.539  1.00 49.72           O  
HETATM 2403  O   HOH B 337     -24.805   3.823  -3.194  1.00 42.71           O  
HETATM 2404  O   HOH B 338      -5.396  -5.185  14.636  1.00 36.76           O  
HETATM 2405  O   HOH B 339      -0.480   5.030   1.990  1.00 39.75           O  
HETATM 2406  O   HOH B 340     -11.258  19.188  15.894  1.00 49.10           O  
HETATM 2407  O   HOH B 341     -12.651  19.987  14.321  1.00 42.80           O  
HETATM 2408  O   HOH B 342      -0.721  15.745   5.503  1.00 40.34           O  
HETATM 2409  O   HOH B 343      -0.568   9.186   6.827  1.00 40.17           O  
HETATM 2410  O   HOH B 344      -9.134 -10.830  22.569  1.00 54.10           O  
HETATM 2411  O   HOH B 345     -15.781  17.189  15.800  1.00 41.76           O  
HETATM 2412  O   HOH B 346      -7.129  15.743 -11.332  1.00 43.12           O  
HETATM 2413  O   HOH B 347     -24.442  19.650   7.310  1.00 39.19           O  
HETATM 2414  O   HOH B 348     -23.714   8.953  10.947  1.00 39.25           O  
HETATM 2415  O   HOH B 349     -23.693  -0.486  14.217  1.00 53.97           O  
HETATM 2416  O   HOH B 350      -7.117   1.786   8.120  1.00 34.18           O  
HETATM 2417  O   HOH B 351     -23.730   0.821  -6.695  1.00 43.15           O  
CONECT  650 2232                                                                
CONECT 1759 2301                                                                
CONECT 2190 2194 2221                                                           
CONECT 2191 2197 2204                                                           
CONECT 2192 2207 2211                                                           
CONECT 2193 2214 2218                                                           
CONECT 2194 2190 2195 2228                                                      
CONECT 2195 2194 2196 2199                                                      
CONECT 2196 2195 2197 2198                                                      
CONECT 2197 2191 2196 2228                                                      
CONECT 2198 2196                                                                
CONECT 2199 2195 2200                                                           
CONECT 2200 2199 2201                                                           
CONECT 2201 2200 2202 2203                                                      
CONECT 2202 2201                                                                
CONECT 2203 2201                                                                
CONECT 2204 2191 2205 2229                                                      
CONECT 2205 2204 2206 2208                                                      
CONECT 2206 2205 2207 2209                                                      
CONECT 2207 2192 2206 2229                                                      
CONECT 2208 2205                                                                
CONECT 2209 2206 2210                                                           
CONECT 2210 2209                                                                
CONECT 2211 2192 2212 2230                                                      
CONECT 2212 2211 2213 2215                                                      
CONECT 2213 2212 2214 2216                                                      
CONECT 2214 2193 2213 2230                                                      
CONECT 2215 2212                                                                
CONECT 2216 2213 2217                                                           
CONECT 2217 2216                                                                
CONECT 2218 2193 2219 2231                                                      
CONECT 2219 2218 2220 2222                                                      
CONECT 2220 2219 2221 2223                                                      
CONECT 2221 2190 2220 2231                                                      
CONECT 2222 2219                                                                
CONECT 2223 2220 2224                                                           
CONECT 2224 2223 2225                                                           
CONECT 2225 2224 2226 2227                                                      
CONECT 2226 2225                                                                
CONECT 2227 2225                                                                
CONECT 2228 2194 2197 2232                                                      
CONECT 2229 2204 2207 2232                                                      
CONECT 2230 2211 2214 2232                                                      
CONECT 2231 2218 2221 2232                                                      
CONECT 2232  650 2228 2229 2230                                                 
CONECT 2232 2231 2257 2258                                                      
CONECT 2233 2234                                                                
CONECT 2234 2233 2235 2239                                                      
CONECT 2235 2234 2236                                                           
CONECT 2236 2235 2237                                                           
CONECT 2237 2236 2238                                                           
CONECT 2238 2237 2239                                                           
CONECT 2239 2234 2238                                                           
CONECT 2240 2241                                                                
CONECT 2241 2240 2242 2246                                                      
CONECT 2242 2241 2243                                                           
CONECT 2243 2242 2244                                                           
CONECT 2244 2243 2245                                                           
CONECT 2245 2244 2246                                                           
CONECT 2246 2241 2245                                                           
CONECT 2247 2248                                                                
CONECT 2248 2247 2249 2253                                                      
CONECT 2249 2248 2250                                                           
CONECT 2250 2249 2251                                                           
CONECT 2251 2250 2252                                                           
CONECT 2252 2251 2253                                                           
CONECT 2253 2248 2252                                                           
CONECT 2254 2255 2256                                                           
CONECT 2255 2254                                                                
CONECT 2256 2254                                                                
CONECT 2257 2232 2258                                                           
CONECT 2258 2232 2257                                                           
CONECT 2259 2263 2290                                                           
CONECT 2260 2266 2273                                                           
CONECT 2261 2276 2280                                                           
CONECT 2262 2283 2287                                                           
CONECT 2263 2259 2264 2297                                                      
CONECT 2264 2263 2265 2268                                                      
CONECT 2265 2264 2266 2267                                                      
CONECT 2266 2260 2265 2297                                                      
CONECT 2267 2265                                                                
CONECT 2268 2264 2269                                                           
CONECT 2269 2268 2270                                                           
CONECT 2270 2269 2271 2272                                                      
CONECT 2271 2270                                                                
CONECT 2272 2270                                                                
CONECT 2273 2260 2274 2298                                                      
CONECT 2274 2273 2275 2277                                                      
CONECT 2275 2274 2276 2278                                                      
CONECT 2276 2261 2275 2298                                                      
CONECT 2277 2274                                                                
CONECT 2278 2275 2279                                                           
CONECT 2279 2278                                                                
CONECT 2280 2261 2281 2299                                                      
CONECT 2281 2280 2282 2284                                                      
CONECT 2282 2281 2283 2285                                                      
CONECT 2283 2262 2282 2299                                                      
CONECT 2284 2281                                                                
CONECT 2285 2282 2286                                                           
CONECT 2286 2285                                                                
CONECT 2287 2262 2288 2300                                                      
CONECT 2288 2287 2289 2291                                                      
CONECT 2289 2288 2290 2292                                                      
CONECT 2290 2259 2289 2300                                                      
CONECT 2291 2288                                                                
CONECT 2292 2289 2293                                                           
CONECT 2293 2292 2294                                                           
CONECT 2294 2293 2295 2296                                                      
CONECT 2295 2294                                                                
CONECT 2296 2294                                                                
CONECT 2297 2263 2266 2301                                                      
CONECT 2298 2273 2276 2301                                                      
CONECT 2299 2280 2283 2301                                                      
CONECT 2300 2287 2290 2301                                                      
CONECT 2301 1759 2297 2298 2299                                                 
CONECT 2301 2300 2302                                                           
CONECT 2302 2301 2303                                                           
CONECT 2303 2302                                                                
MASTER      349    0    8   18    0    0   17    6 2408    2  118   23          
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.