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

Should you encounter any unexpected behaviour,
please let us know.
elNémo will be down on october 27th, due to electrical maintenance.
Sorry for the inconvenience.


***  aa  ***

elNémo ID: 20100111574711308

Job options:

ID        	=	 20100111574711308
JOBID     	=	 aa
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 aa

HEADER    HYDROLASE                               19-MAY-14   4QEZ              
TITLE     CRYSTAL STRUCTURE OF 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE    
TITLE    2 NUCLEOSIDASE FROM BACILLUS ANTHRACIS                                 
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE;
COMPND   3 CHAIN: B, A, C;                                                      
COMPND   4 SYNONYM: MTA/SAH NUCLEOSIDASE, MTAN, 5'-METHYLTHIOADENOSINE          
COMPND   5 NUCLEOSIDASE, MTA NUCLEOSIDASE, S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE, 
COMPND   6 ADOHCY NUCLEOSIDASE, SAH NUCLEOSIDASE, SRH NUCLEOSIDASE;             
COMPND   7 EC: 3.2.2.9;                                                         
COMPND   8 ENGINEERED: YES                                                      
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: BACILLUS ANTHRACIS;                             
SOURCE   3 ORGANISM_COMMON: ANTHRAX, ANTHRAX BACTERIUM;                         
SOURCE   4 ORGANISM_TAXID: 1392;                                                
SOURCE   5 STRAIN: STERNE;                                                      
SOURCE   6 GENE: MTNN, BA_4602, GBAA_4602, BAS4270;                             
SOURCE   7 EXPRESSION_SYSTEM: ESCHERICHIA COLI;                                 
SOURCE   8 EXPRESSION_SYSTEM_TAXID: 562;                                        
SOURCE   9 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  10 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  11 EXPRESSION_SYSTEM_PLASMID: PET28(B)                                  
KEYWDS    AMINO-ACID BIOSYNTHESIS, METHIONINE BIOSYNTHESIS, HYDROLASE           
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    K.F.TARIQUE,S.DEVI,S.A.ABDUL REHMAN,S.GOURINATH                       
REVDAT   2   07-FEB-18 4QEZ    1       REMARK                                   
REVDAT   1   18-JUN-14 4QEZ    0                                                
JRNL        AUTH   K.F.TARIQUE,S.DEVI,S.A.ABDUL REHMAN,S.GOURINATH              
JRNL        TITL   CRYSTAL STRUCTURE OF                                         
JRNL        TITL 2 5'-METHYLTHIOADENOSINE/S-ADENOSYLHOMOCYSTEINE NUCLEOSIDASE   
JRNL        TITL 3 FROM BACILLUS ANTHRACIS                                      
JRNL        REF    TO BE PUBLISHED                                              
JRNL        REFN                                                                
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.70 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0049                                      
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) : 2.70                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 34.49                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 94.9                           
REMARK   3   NUMBER OF REFLECTIONS             : 15438                          
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) : 0.243                           
REMARK   3   R VALUE            (WORKING SET) : 0.241                           
REMARK   3   FREE R VALUE                     : 0.271                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 819                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.71                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.78                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 847                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 69.73                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3200                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 40                           
REMARK   3   BIN FREE R VALUE                    : 0.3940                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 5265                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 54                                      
REMARK   3   SOLVENT ATOMS            : 0                                       
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 60.04                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 1.01000                                              
REMARK   3    B22 (A**2) : -1.95000                                             
REMARK   3    B33 (A**2) : 1.03000                                              
REMARK   3    B12 (A**2) : 0.00000                                              
REMARK   3    B13 (A**2) : -0.60000                                             
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.446         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.362         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 40.202        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.916                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.895                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  5405 ; 0.006 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):  5222 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  7301 ; 1.176 ; 1.959       
REMARK   3   BOND ANGLES OTHERS          (DEGREES): 11995 ; 1.048 ; 3.000       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   679 ; 6.147 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):   246 ;34.796 ;25.041       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   931 ;16.528 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):    24 ;20.202 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   837 ; 0.073 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  6123 ; 0.004 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  1204 ; 0.002 ; 0.020       
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):  2734 ; 0.893 ; 5.544       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  2733 ; 0.893 ; 5.544       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  3407 ; 1.613 ; 8.313       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  3408 ; 1.613 ; 8.313       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  2568 ; 0.562 ; 5.667       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  2569 ; 0.562 ; 5.667       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  3767 ; 1.093 ; 8.465       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  5735 ; 2.634 ;43.119       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  5735 ; 2.634 ;43.119       
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   NCS TYPE: LOCAL                                                    
REMARK   3   NUMBER OF DIFFERENT NCS PAIRS  : 3                                 
REMARK   3  GROUP  CHAIN1    RANGE     CHAIN2     RANGE    COUNT RMS  WEIGHT    
REMARK   3    1     B     2    229       A     2    229   13212  0.11  0.05     
REMARK   3    2     B     2    237       C     2    237   13567  0.11  0.05     
REMARK   3    3     A     2    229       C     2    229   13228  0.11  0.05     
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 3                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   B     2        B   237                          
REMARK   3    ORIGIN FOR THE GROUP (A):  42.4780 -22.6610  10.7410              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0184 T22:   0.2773                                     
REMARK   3      T33:   0.1017 T12:  -0.0137                                     
REMARK   3      T13:  -0.0088 T23:  -0.0285                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.8701 L22:   2.4284                                     
REMARK   3      L33:   2.9467 L12:  -0.9789                                     
REMARK   3      L13:   0.7051 L23:   0.1690                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0583 S12:   0.0625 S13:  -0.0525                       
REMARK   3      S21:   0.1449 S22:  -0.0148 S23:  -0.2633                       
REMARK   3      S31:   0.1452 S32:   0.2719 S33:   0.0731                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 2                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     2        A   230                          
REMARK   3    ORIGIN FOR THE GROUP (A):  16.0590 -11.3760  10.2050              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0298 T22:   0.6377                                     
REMARK   3      T33:   0.1032 T12:   0.0850                                     
REMARK   3      T13:  -0.0335 T23:  -0.0871                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.2052 L22:   1.8068                                     
REMARK   3      L33:   2.7533 L12:  -1.0458                                     
REMARK   3      L13:   0.5309 L23:   0.3740                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.1373 S12:  -0.1452 S13:   0.1259                       
REMARK   3      S21:  -0.0183 S22:  -0.0106 S23:   0.0767                       
REMARK   3      S31:  -0.2503 S32:  -1.0067 S33:   0.1480                       
REMARK   3                                                                      
REMARK   3   TLS GROUP : 3                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 1                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   C     2        C   237                          
REMARK   3    ORIGIN FOR THE GROUP (A):  13.1200 -49.0390 -13.4320              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.1564 T22:   0.3634                                     
REMARK   3      T33:   0.2134 T12:   0.0173                                     
REMARK   3      T13:  -0.0061 T23:  -0.0078                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   2.7328 L22:   1.6222                                     
REMARK   3      L33:   4.0576 L12:   0.5194                                     
REMARK   3      L13:   1.8629 L23:   0.3448                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0702 S12:  -0.0537 S13:  -0.0298                       
REMARK   3      S21:   0.1113 S22:  -0.0477 S23:  -0.1895                       
REMARK   3      S31:   0.2510 S32:   0.2870 S33:  -0.0225                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.00                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 4QEZ COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 22-MAY-14.                  
REMARK 100 THE DEPOSITION ID IS D_1000085970.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 12-OCT-13                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8                                  
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : BRUKER AXS MICROSTAR               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54                               
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 16291                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.700                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : -3.000                             
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 95.4                               
REMARK 200  DATA REDUNDANCY                : 4.200                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : 0.08000                            
REMARK 200   FOR THE DATA SET  : 21.6400                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.70                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.80                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 75.0                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 2.40                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : 0.34000                            
REMARK 200   FOR SHELL         : 2.549                              
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: 3DP9                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 38.16                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 1.99                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 2M AMMONIUM SULFATE, 0.2M MGCL2, TRIS    
REMARK 280  PH 8.0, VAPOR DIFFUSION, HANGING DROP, TEMPERATURE 293K             
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: C 1 2 1                          
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -X,Y,-Z                                                 
REMARK 290       3555   X+1/2,Y+1/2,Z                                           
REMARK 290       4555   -X+1/2,Y+1/2,-Z                                         
REMARK 290                                                                      
REMARK 290     WHERE NNN -> OPERATOR NUMBER                                     
REMARK 290           MMM -> TRANSLATION VECTOR                                  
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY TRANSFORMATIONS                            
REMARK 290 THE FOLLOWING TRANSFORMATIONS OPERATE ON THE ATOM/HETATM             
REMARK 290 RECORDS IN THIS ENTRY TO PRODUCE CRYSTALLOGRAPHICALLY                
REMARK 290 RELATED MOLECULES.                                                   
REMARK 290   SMTRY1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   3  1.000000  0.000000  0.000000       90.63450            
REMARK 290   SMTRY2   3  0.000000  1.000000  0.000000       37.31750            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000       90.63450            
REMARK 290   SMTRY2   4  0.000000  1.000000  0.000000       37.31750            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1, 2                                                    
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: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4170 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 17340 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: B, A                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 2                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 4210 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 18220 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -1.0 KCAL/MOL                         
REMARK 350 APPLY THE FOLLOWING TO CHAINS: C                                     
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 -1.000000  0.000000  0.000000        4.28014            
REMARK 350   BIOMT2   2  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000 -1.000000      -46.49139            
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     MET B     1                                                      
REMARK 465     ALA B   135                                                      
REMARK 465     GLU B   136                                                      
REMARK 465     GLU B   137                                                      
REMARK 465     ASN B   138                                                      
REMARK 465     ILE B   139                                                      
REMARK 465     HIS B   238                                                      
REMARK 465     HIS B   239                                                      
REMARK 465     MET A     1                                                      
REMARK 465     GLN A   134                                                      
REMARK 465     ALA A   135                                                      
REMARK 465     GLU A   136                                                      
REMARK 465     GLU A   137                                                      
REMARK 465     ASN A   138                                                      
REMARK 465     ILE A   139                                                      
REMARK 465     LYS A   231                                                      
REMARK 465     LEU A   232                                                      
REMARK 465     GLU A   233                                                      
REMARK 465     HIS A   234                                                      
REMARK 465     HIS A   235                                                      
REMARK 465     HIS A   236                                                      
REMARK 465     HIS A   237                                                      
REMARK 465     HIS A   238                                                      
REMARK 465     HIS A   239                                                      
REMARK 465     MET C     1                                                      
REMARK 465     ALA C   135                                                      
REMARK 465     GLU C   136                                                      
REMARK 465     GLU C   137                                                      
REMARK 465     ASN C   138                                                      
REMARK 465     ILE C   139                                                      
REMARK 465     HIS C   238                                                      
REMARK 465     HIS C   239                                                      
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 B 150       38.09    -86.24                                   
REMARK 500    ASN B 168       81.08   -154.97                                   
REMARK 500    GLU B 173     -149.07   -155.37                                   
REMARK 500    GLU B 175      -34.74   -137.51                                   
REMARK 500    LYS B 202      -94.32    -90.04                                   
REMARK 500    GLU B 229       19.07    -65.91                                   
REMARK 500    HIS B 236      -80.64    -75.47                                   
REMARK 500    ASP A 150       38.19    -85.92                                   
REMARK 500    ASN A 168       80.06   -155.52                                   
REMARK 500    GLU A 173     -148.92   -156.07                                   
REMARK 500    GLU A 175      -34.90   -138.05                                   
REMARK 500    ASP C 150       37.76    -85.98                                   
REMARK 500    ASN C 168       80.63   -155.66                                   
REMARK 500    GLU C 173     -148.64   -156.05                                   
REMARK 500    GLU C 175      -34.76   -137.92                                   
REMARK 500    HIS C 234      -60.79   -108.06                                   
REMARK 500    HIS C 236      -79.68    -76.04                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: NON-CIS, NON-TRANS                                         
REMARK 500                                                                      
REMARK 500 THE FOLLOWING PEPTIDE BONDS DEVIATE SIGNIFICANTLY FROM BOTH          
REMARK 500 CIS AND TRANS CONFORMATION.  CIS BONDS, IF ANY, ARE LISTED           
REMARK 500 ON CISPEP RECORDS.  TRANS IS DEFINED AS 180 +/- 30 AND               
REMARK 500 CIS IS DEFINED AS 0 +/- 30 DEGREES.                                  
REMARK 500                                 MODEL     OMEGA                      
REMARK 500 LEU B  230     LYS B  231                  -40.07                    
REMARK 500 LEU C  232     GLU C  233                  137.99                    
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE B 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS B 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC3                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE A 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC4                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS A 302                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC5                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE TRS C 301                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC6                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE ADE C 302                 
DBREF  4QEZ B    1   231  UNP    Q81LL4   MTNN_BACAN       1    231             
DBREF  4QEZ A    1   231  UNP    Q81LL4   MTNN_BACAN       1    231             
DBREF  4QEZ C    1   231  UNP    Q81LL4   MTNN_BACAN       1    231             
SEQADV 4QEZ LEU B  232  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ GLU B  233  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS B  234  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS B  235  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS B  236  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS B  237  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS B  238  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS B  239  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ LEU A  232  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ GLU A  233  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS A  234  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS A  235  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS A  236  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS A  237  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS A  238  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS A  239  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ LEU C  232  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ GLU C  233  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS C  234  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS C  235  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS C  236  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS C  237  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS C  238  UNP  Q81LL4              EXPRESSION TAG                 
SEQADV 4QEZ HIS C  239  UNP  Q81LL4              EXPRESSION TAG                 
SEQRES   1 B  239  MET ARG ILE ALA VAL ILE GLY ALA MET GLU GLU GLU VAL          
SEQRES   2 B  239  ARG ILE LEU ARG ASP LYS LEU GLU GLN ALA GLU THR GLU          
SEQRES   3 B  239  THR VAL ALA GLY CYS GLU PHE THR LYS GLY GLN LEU ALA          
SEQRES   4 B  239  GLY HIS GLU VAL ILE LEU LEU LYS SER GLY ILE GLY LYS          
SEQRES   5 B  239  VAL ASN ALA ALA MET SER THR THR ILE LEU LEU GLU ARG          
SEQRES   6 B  239  TYR LYS PRO GLU LYS VAL ILE ASN THR GLY SER ALA GLY          
SEQRES   7 B  239  GLY PHE HIS HIS SER LEU ASN VAL GLY ASP VAL VAL ILE          
SEQRES   8 B  239  SER THR GLU VAL ARG HIS HIS ASP VAL ASP VAL THR ALA          
SEQRES   9 B  239  PHE ASN TYR GLU TYR GLY GLN VAL PRO GLY MET PRO PRO          
SEQRES  10 B  239  GLY PHE LYS ALA ASP GLU ALA LEU VAL ALA LEU ALA GLU          
SEQRES  11 B  239  LYS CYS MET GLN ALA GLU GLU ASN ILE GLN VAL VAL LYS          
SEQRES  12 B  239  GLY MET ILE ALA THR GLY ASP SER PHE MET SER ASP PRO          
SEQRES  13 B  239  ASN ARG VAL ALA ALA ILE ARG ASP LYS PHE GLU ASN LEU          
SEQRES  14 B  239  TYR ALA VAL GLU MET GLU ALA ALA ALA VAL ALA GLN VAL          
SEQRES  15 B  239  CYS HIS GLN TYR GLU VAL PRO PHE VAL ILE ILE ARG ALA          
SEQRES  16 B  239  LEU SER ASP ILE ALA GLY LYS GLU SER ASN VAL SER PHE          
SEQRES  17 B  239  ASP GLN PHE LEU ASP GLN ALA ALA LEU HIS SER THR ASN          
SEQRES  18 B  239  PHE ILE VAL LYS VAL LEU GLU GLU LEU LYS LEU GLU HIS          
SEQRES  19 B  239  HIS HIS HIS HIS HIS                                          
SEQRES   1 A  239  MET ARG ILE ALA VAL ILE GLY ALA MET GLU GLU GLU VAL          
SEQRES   2 A  239  ARG ILE LEU ARG ASP LYS LEU GLU GLN ALA GLU THR GLU          
SEQRES   3 A  239  THR VAL ALA GLY CYS GLU PHE THR LYS GLY GLN LEU ALA          
SEQRES   4 A  239  GLY HIS GLU VAL ILE LEU LEU LYS SER GLY ILE GLY LYS          
SEQRES   5 A  239  VAL ASN ALA ALA MET SER THR THR ILE LEU LEU GLU ARG          
SEQRES   6 A  239  TYR LYS PRO GLU LYS VAL ILE ASN THR GLY SER ALA GLY          
SEQRES   7 A  239  GLY PHE HIS HIS SER LEU ASN VAL GLY ASP VAL VAL ILE          
SEQRES   8 A  239  SER THR GLU VAL ARG HIS HIS ASP VAL ASP VAL THR ALA          
SEQRES   9 A  239  PHE ASN TYR GLU TYR GLY GLN VAL PRO GLY MET PRO PRO          
SEQRES  10 A  239  GLY PHE LYS ALA ASP GLU ALA LEU VAL ALA LEU ALA GLU          
SEQRES  11 A  239  LYS CYS MET GLN ALA GLU GLU ASN ILE GLN VAL VAL LYS          
SEQRES  12 A  239  GLY MET ILE ALA THR GLY ASP SER PHE MET SER ASP PRO          
SEQRES  13 A  239  ASN ARG VAL ALA ALA ILE ARG ASP LYS PHE GLU ASN LEU          
SEQRES  14 A  239  TYR ALA VAL GLU MET GLU ALA ALA ALA VAL ALA GLN VAL          
SEQRES  15 A  239  CYS HIS GLN TYR GLU VAL PRO PHE VAL ILE ILE ARG ALA          
SEQRES  16 A  239  LEU SER ASP ILE ALA GLY LYS GLU SER ASN VAL SER PHE          
SEQRES  17 A  239  ASP GLN PHE LEU ASP GLN ALA ALA LEU HIS SER THR ASN          
SEQRES  18 A  239  PHE ILE VAL LYS VAL LEU GLU GLU LEU LYS LEU GLU HIS          
SEQRES  19 A  239  HIS HIS HIS HIS HIS                                          
SEQRES   1 C  239  MET ARG ILE ALA VAL ILE GLY ALA MET GLU GLU GLU VAL          
SEQRES   2 C  239  ARG ILE LEU ARG ASP LYS LEU GLU GLN ALA GLU THR GLU          
SEQRES   3 C  239  THR VAL ALA GLY CYS GLU PHE THR LYS GLY GLN LEU ALA          
SEQRES   4 C  239  GLY HIS GLU VAL ILE LEU LEU LYS SER GLY ILE GLY LYS          
SEQRES   5 C  239  VAL ASN ALA ALA MET SER THR THR ILE LEU LEU GLU ARG          
SEQRES   6 C  239  TYR LYS PRO GLU LYS VAL ILE ASN THR GLY SER ALA GLY          
SEQRES   7 C  239  GLY PHE HIS HIS SER LEU ASN VAL GLY ASP VAL VAL ILE          
SEQRES   8 C  239  SER THR GLU VAL ARG HIS HIS ASP VAL ASP VAL THR ALA          
SEQRES   9 C  239  PHE ASN TYR GLU TYR GLY GLN VAL PRO GLY MET PRO PRO          
SEQRES  10 C  239  GLY PHE LYS ALA ASP GLU ALA LEU VAL ALA LEU ALA GLU          
SEQRES  11 C  239  LYS CYS MET GLN ALA GLU GLU ASN ILE GLN VAL VAL LYS          
SEQRES  12 C  239  GLY MET ILE ALA THR GLY ASP SER PHE MET SER ASP PRO          
SEQRES  13 C  239  ASN ARG VAL ALA ALA ILE ARG ASP LYS PHE GLU ASN LEU          
SEQRES  14 C  239  TYR ALA VAL GLU MET GLU ALA ALA ALA VAL ALA GLN VAL          
SEQRES  15 C  239  CYS HIS GLN TYR GLU VAL PRO PHE VAL ILE ILE ARG ALA          
SEQRES  16 C  239  LEU SER ASP ILE ALA GLY LYS GLU SER ASN VAL SER PHE          
SEQRES  17 C  239  ASP GLN PHE LEU ASP GLN ALA ALA LEU HIS SER THR ASN          
SEQRES  18 C  239  PHE ILE VAL LYS VAL LEU GLU GLU LEU LYS LEU GLU HIS          
SEQRES  19 C  239  HIS HIS HIS HIS HIS                                          
HET    ADE  B 301      10                                                       
HET    TRS  B 302       8                                                       
HET    ADE  A 301      10                                                       
HET    TRS  A 302       8                                                       
HET    TRS  C 301       8                                                       
HET    ADE  C 302      10                                                       
HETNAM     ADE ADENINE                                                          
HETNAM     TRS 2-AMINO-2-HYDROXYMETHYL-PROPANE-1,3-DIOL                         
HETSYN     TRS TRIS BUFFER                                                      
FORMUL   4  ADE    3(C5 H5 N5)                                                  
FORMUL   5  TRS    3(C4 H12 N O3 1+)                                            
HELIX    1   1 MET B    9  LEU B   20  1                                  12
HELIX    2   2 GLY B   51  TYR B   66  1                                  16
HELIX    3   3 VAL B  102  ASN B  106  1                                   5
HELIX    4   4 ASP B  122  MET B  133  1                                  12
HELIX    5   5 ASP B  155  ASP B  164  1                                  10
HELIX    6   6 GLU B  175  GLU B  187  1                                  13
HELIX    7   7 GLU B  203  GLU B  229  1                                  27
HELIX    8   8 MET A    9  LEU A   20  1                                  12
HELIX    9   9 GLY A   51  TYR A   66  1                                  16
HELIX   10  10 VAL A  102  ASN A  106  1                                   5
HELIX   11  11 ASP A  122  CYS A  132  1                                  11
HELIX   12  12 ASP A  155  ASP A  164  1                                  10
HELIX   13  13 GLU A  175  GLU A  187  1                                  13
HELIX   14  14 GLU A  203  LEU A  230  1                                  28
HELIX   15  15 MET C    9  LEU C   20  1                                  12
HELIX   16  16 GLY C   51  TYR C   66  1                                  16
HELIX   17  17 VAL C  102  ASN C  106  1                                   5
HELIX   18  18 ASP C  122  CYS C  132  1                                  11
HELIX   19  19 ASP C  155  ASP C  164  1                                  10
HELIX   20  20 GLU C  175  GLU C  187  1                                  13
HELIX   21  21 GLU C  203  LYS C  231  1                                  29
SHEET    1   1 1 ILE B   3  GLY B   7  0
SHEET    2   2 1 GLU B  21  VAL B  28  0
SHEET    3   3 1 CYS B  31  LEU B  38  0
SHEET    4   4 1 HIS B  41  LYS B  47  0
SHEET    5   5 1 LYS B  70  ASN B  73  0
SHEET    6   6 1 SER B  76  GLY B  79  0
SHEET    7   7 1 VAL B  89  HIS B  97  0
SHEET    8   8 1 PHE B 119  LYS B 120  0
SHEET    9   9 1 VAL B 141  THR B 148  0
SHEET   10  10 1 LEU B 169  GLU B 173  0
SHEET   11  11 1 PHE B 190  ILE B 199  0
SHEET   12  12 1 ILE A   3  GLY A   7  0
SHEET   13  13 1 GLU A  21  VAL A  28  0
SHEET   14  14 1 CYS A  31  LEU A  38  0
SHEET   15  15 1 HIS A  41  LYS A  47  0
SHEET   16  16 1 LYS A  70  ASN A  73  0
SHEET   17  17 1 SER A  76  GLY A  79  0
SHEET   18  18 1 VAL A  89  HIS A  97  0
SHEET   19  19 1 PHE A 119  LYS A 120  0
SHEET   20  20 1 VAL A 141  THR A 148  0
SHEET   21  21 1 LEU A 169  GLU A 173  0
SHEET   22  22 1 PHE A 190  ILE A 199  0
SHEET   23  23 1 ILE C   3  GLY C   7  0
SHEET   24  24 1 GLU C  21  VAL C  28  0
SHEET   25  25 1 CYS C  31  LEU C  38  0
SHEET   26  26 1 HIS C  41  LYS C  47  0
SHEET   27  27 1 LYS C  70  ASN C  73  0
SHEET   28  28 1 SER C  76  GLY C  79  0
SHEET   29  29 1 VAL C  89  HIS C  97  0
SHEET   30  30 1 PHE C 119  LYS C 120  0
SHEET   31  31 1 VAL C 141  THR C 148  0
SHEET   32  32 1 LEU C 169  GLU C 173  0
SHEET   33  33 1 PHE C 190  ILE C 199  0
SITE     1 AC1  9 ALA B  77  GLY B  78  PHE B 152  MET B 153                    
SITE     2 AC1  9 VAL B 172  GLU B 173  SER B 197  ASP B 198                    
SITE     3 AC1  9 TRS B 302                                                     
SITE     1 AC2  9 ALA B   8  GLU B  12  SER B  76  GLU B 173                    
SITE     2 AC2  9 MET B 174  GLU B 175  ARG B 194  ADE B 301                    
SITE     3 AC2  9 HIS C 236                                                     
SITE     1 AC3  9 ALA A  77  GLY A  78  PHE A 152  MET A 153                    
SITE     2 AC3  9 VAL A 172  GLU A 173  SER A 197  ASP A 198                    
SITE     3 AC3  9 TRS A 302                                                     
SITE     1 AC4 10 ALA A   8  GLU A  12  SER A  76  GLU A 173                    
SITE     2 AC4 10 MET A 174  GLU A 175  ARG A 194  PHE A 208                    
SITE     3 AC4 10 ADE A 301  HIS B 236                                          
SITE     1 AC5  9 ALA C   8  GLU C  12  SER C  76  GLU C 173                    
SITE     2 AC5  9 MET C 174  GLU C 175  ARG C 194  PHE C 208                    
SITE     3 AC5  9 ADE C 302                                                     
SITE     1 AC6 10 ALA C  77  GLY C  78  PHE C 152  MET C 153                    
SITE     2 AC6 10 VAL C 172  GLU C 173  SER C 197  ASP C 198                    
SITE     3 AC6 10 PHE C 208  TRS C 301                                          
CRYST1  181.269   74.635   46.688  90.00  95.26  90.00 C 1 2 1      12          
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      0.005517  0.000000  0.000508        0.00000                         
SCALE2      0.000000  0.013399  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.021509        0.00000                         
ATOM      1  N   ARG B   2      39.947 -31.716  25.650  1.00 57.89           N
ANISOU    1  N   ARG B   2     7869   8323   5804    489     16   1053       N
ATOM      2  CA  ARG B   2      41.083 -30.807  26.040  1.00 57.50           C
ANISOU    2  CA  ARG B   2     7779   8415   5653    648   -176    922       C
ATOM      3  C   ARG B   2      41.590 -29.927  24.874  1.00 55.11           C
ANISOU    3  C   ARG B   2     7276   8139   5526    603   -259    700       C
ATOM      4  O   ARG B   2      41.581 -28.695  24.978  1.00 54.21           O
ANISOU    4  O   ARG B   2     7077   8164   5354    599   -306    566       O
ATOM      5  CB  ARG B   2      42.229 -31.638  26.649  1.00 59.35           C
ANISOU    5  CB  ARG B   2     8138   8584   5828    829   -324   1024       C
ATOM      6  CG  ARG B   2      43.614 -31.008  26.623  1.00 58.97           C
ANISOU    6  CG  ARG B   2     7991   8626   5789    970   -548    871       C
ATOM      7  CD  ARG B   2      44.696 -32.049  26.845  1.00 60.70           C
ANISOU    7  CD  ARG B   2     8292   8743   6028   1141   -682    962       C
ATOM      8  NE  ARG B   2      45.957 -31.402  27.170  1.00 61.03           N
ANISOU    8  NE  ARG B   2     8241   8920   6026   1290   -905    837       N
ATOM      9  CZ  ARG B   2      46.269 -30.940  28.378  1.00 62.55           C
ANISOU    9  CZ  ARG B   2     8515   9262   5988   1416  -1027    847       C
ATOM     10  NH1 ARG B   2      45.401 -31.025  29.393  1.00 63.87           N
ANISOU   10  NH1 ARG B   2     8866   9480   5921   1425   -928    984       N
ATOM     11  NH2 ARG B   2      47.456 -30.377  28.569  1.00 62.98           N
ANISOU   11  NH2 ARG B   2     8457   9429   6043   1533  -1250    713       N
ATOM     12  N   ILE B   3      42.031 -30.549  23.778  1.00 54.39           N
ANISOU   12  N   ILE B   3     7116   7910   5638    576   -277    665       N
ATOM     13  CA  ILE B   3      42.396 -29.786  22.557  1.00 52.36           C
ANISOU   13  CA  ILE B   3     6671   7685   5540    519   -316    484       C
ATOM     14  C   ILE B   3      41.486 -30.081  21.369  1.00 51.19           C
ANISOU   14  C   ILE B   3     6461   7441   5547    367   -182    452       C
ATOM     15  O   ILE B   3      41.185 -31.232  21.065  1.00 51.96           O
ANISOU   15  O   ILE B   3     6632   7382   5729    337   -123    533       O
ATOM     16  CB  ILE B   3      43.873 -29.933  22.114  1.00 52.48           C
ANISOU   16  CB  ILE B   3     6599   7691   5649    637   -469    414       C
ATOM     17  CG1 ILE B   3      44.202 -28.805  21.128  1.00 50.69           C
ANISOU   17  CG1 ILE B   3     6176   7556   5530    566   -497    250       C
ATOM     18  CG2 ILE B   3      44.159 -31.269  21.455  1.00 53.14           C
ANISOU   18  CG2 ILE B   3     6724   7603   5864    679   -450    465       C
ATOM     19  CD1 ILE B   3      45.659 -28.637  20.734  1.00 50.92           C
ANISOU   19  CD1 ILE B   3     6066   7637   5645    660   -634    171       C
ATOM     20  N   ALA B   4      41.058 -29.029  20.693  1.00 49.54           N
ANISOU   20  N   ALA B   4     6125   7319   5379    276   -152    330       N
ATOM     21  CA  ALA B   4      40.190 -29.176  19.538  1.00 48.50           C
ANISOU   21  CA  ALA B   4     5924   7127   5378    144    -49    280       C
ATOM     22  C   ALA B   4      40.933 -28.848  18.249  1.00 47.28           C
ANISOU   22  C   ALA B   4     5637   6978   5349    151   -105    153       C
ATOM     23  O   ALA B   4      41.700 -27.885  18.181  1.00 46.68           O
ANISOU   23  O   ALA B   4     5472   7004   5261    190   -188     80       O
ATOM     24  CB  ALA B   4      38.975 -28.280  19.688  1.00 47.85           C
ANISOU   24  CB  ALA B   4     5801   7143   5235     47     42    251       C
ATOM     25  N   VAL B   5      40.692 -29.649  17.221  1.00 47.20           N
ANISOU   25  N   VAL B   5     5614   6860   5459    109    -58    126       N
ATOM     26  CA  VAL B   5      41.195 -29.330  15.891  1.00 46.21           C
ANISOU   26  CA  VAL B   5     5366   6767   5426    111    -79      7       C
ATOM     27  C   VAL B   5      40.016 -29.364  14.917  1.00 45.54           C
ANISOU   27  C   VAL B   5     5249   6652   5402    -11      8    -50       C
ATOM     28  O   VAL B   5      39.244 -30.329  14.880  1.00 46.33           O
ANISOU   28  O   VAL B   5     5422   6630   5552    -70     60    -15       O
ATOM     29  CB  VAL B   5      42.410 -30.163  15.452  1.00 47.03           C
ANISOU   29  CB  VAL B   5     5461   6812   5596    239   -144    -14       C
ATOM     30  CG1 VAL B   5      42.448 -31.466  16.203  1.00 48.69           C
ANISOU   30  CG1 VAL B   5     5825   6865   5808    305   -158     90       C
ATOM     31  CG2 VAL B   5      42.435 -30.369  13.942  1.00 46.57           C
ANISOU   31  CG2 VAL B   5     5324   6742   5629    227   -110   -124       C
ATOM     32  N   ILE B   6      39.887 -28.322  14.131  1.00 44.33           N
ANISOU   32  N   ILE B   6     4988   6604   5253    -51     12   -133       N
ATOM     33  CA  ILE B   6      38.744 -28.163  13.267  1.00 43.78           C
ANISOU   33  CA  ILE B   6     4878   6539   5219   -151     73   -193       C
ATOM     34  C   ILE B   6      39.129 -28.101  11.806  1.00 43.34           C
ANISOU   34  C   ILE B   6     4746   6511   5212   -130     62   -291       C
ATOM     35  O   ILE B   6      40.097 -27.495  11.449  1.00 42.99           O
ANISOU   35  O   ILE B   6     4635   6547   5154    -73     29   -311       O
ATOM     36  CB  ILE B   6      38.020 -26.891  13.607  1.00 42.98           C
ANISOU   36  CB  ILE B   6     4730   6545   5053   -205     92   -199       C
ATOM     37  CG1 ILE B   6      37.825 -26.807  15.091  1.00 43.57           C
ANISOU   37  CG1 ILE B   6     4879   6635   5042   -191    101   -113       C
ATOM     38  CG2 ILE B   6      36.718 -26.852  12.928  1.00 42.76           C
ANISOU   38  CG2 ILE B   6     4662   6525   5060   -296    148   -247       C
ATOM     39  CD1 ILE B   6      37.098 -25.629  15.507  1.00 43.13           C
ANISOU   39  CD1 ILE B   6     4790   6680   4916   -215    118   -137       C
ATOM     40  N   GLY B   7      38.341 -28.719  10.959  1.00 43.61           N
ANISOU   40  N   GLY B   7     4786   6486   5298   -181     90   -353       N
ATOM     41  CA  GLY B   7      38.612 -28.688   9.552  1.00 43.47           C
ANISOU   41  CA  GLY B   7     4711   6512   5292   -145     81   -455       C
ATOM     42  C   GLY B   7      37.340 -28.799   8.783  1.00 43.51           C
ANISOU   42  C   GLY B   7     4702   6507   5322   -231     98   -530       C
ATOM     43  O   GLY B   7      36.431 -29.411   9.224  1.00 44.11           O
ANISOU   43  O   GLY B   7     4818   6494   5450   -314    114   -513       O
ATOM     44  N   ALA B   8      37.302 -28.223   7.608  1.00 43.13           N
ANISOU   44  N   ALA B   8     4593   6560   5236   -211     91   -606       N
ATOM     45  CA  ALA B   8      36.084 -28.068   6.878  1.00 43.17           C
ANISOU   45  CA  ALA B   8     4565   6593   5244   -280     85   -681       C
ATOM     46  C   ALA B   8      35.671 -29.246   6.043  1.00 44.38           C
ANISOU   46  C   ALA B   8     4754   6654   5454   -286     52   -798       C
ATOM     47  O   ALA B   8      34.520 -29.571   5.992  1.00 44.91           O
ANISOU   47  O   ALA B   8     4808   6677   5579   -383     38   -840       O
ATOM     48  CB  ALA B   8      36.199 -26.899   6.032  1.00 42.50           C
ANISOU   48  CB  ALA B   8     4418   6653   5078   -245     81   -696       C
ATOM     49  N   MET B   9      36.606 -29.867   5.352  1.00 45.03           N
ANISOU   49  N   MET B   9     4870   6714   5524   -178     34   -864       N
ATOM     50  CA  MET B   9      36.264 -30.889   4.396  1.00 46.37           C
ANISOU   50  CA  MET B   9     5085   6804   5732   -159    -17  -1012       C
ATOM     51  C   MET B   9      36.721 -32.191   4.909  1.00 47.58           C
ANISOU   51  C   MET B   9     5336   6759   5983   -129    -37  -1016       C
ATOM     52  O   MET B   9      37.362 -32.240   5.909  1.00 47.29           O
ANISOU   52  O   MET B   9     5327   6679   5963   -107    -10   -899       O
ATOM     53  CB  MET B   9      36.914 -30.594   3.065  1.00 46.61           C
ANISOU   53  CB  MET B   9     5089   6975   5646    -28    -23  -1108       C
ATOM     54  CG  MET B   9      36.546 -29.292   2.510  1.00 45.70           C
ANISOU   54  CG  MET B   9     4896   7041   5425    -44     -6  -1080       C
ATOM     55  SD  MET B   9      37.519 -28.791   1.171  1.00 46.09           S
ANISOU   55  SD  MET B   9     4917   7280   5317    106     27  -1117       S
ATOM     56  CE  MET B   9      36.932 -29.811  -0.103  1.00 47.86           C
ANISOU   56  CE  MET B   9     5200   7482   5502    172    -51  -1335       C
ATOM     57  N   GLU B  10      36.396 -33.260   4.224  1.00 49.11           N
ANISOU   57  N   GLU B  10     5595   6823   6244   -121    -99  -1156       N
ATOM     58  CA  GLU B  10      36.740 -34.561   4.725  1.00 50.60           C
ANISOU   58  CA  GLU B  10     5901   6776   6549    -97   -131  -1157       C
ATOM     59  C   GLU B  10      38.204 -34.838   4.534  1.00 50.96           C
ANISOU   59  C   GLU B  10     5978   6842   6542    109   -129  -1178       C
ATOM     60  O   GLU B  10      38.841 -35.484   5.327  1.00 51.60           O
ANISOU   60  O   GLU B  10     6134   6789   6684    166   -135  -1103       O
ATOM     61  CB  GLU B  10      35.885 -35.631   4.057  1.00 52.50           C
ANISOU   61  CB  GLU B  10     6207   6837   6904   -165   -218  -1317       C
ATOM     62  CG  GLU B  10      36.425 -37.014   4.196  1.00 54.47           C
ANISOU   62  CG  GLU B  10     6603   6827   7267    -89   -276  -1366       C
ATOM     63  CD  GLU B  10      35.940 -37.683   5.423  1.00 55.28           C
ANISOU   63  CD  GLU B  10     6782   6703   7519   -238   -263  -1211       C
ATOM     64  OE1 GLU B  10      35.248 -37.050   6.196  1.00 54.25           O
ANISOU   64  OE1 GLU B  10     6580   6647   7386   -387   -196  -1068       O
ATOM     65  OE2 GLU B  10      36.253 -38.853   5.632  1.00 57.17           O
ANISOU   65  OE2 GLU B  10     7160   6686   7874   -198   -318  -1225       O
ATOM     66  N   GLU B  11      38.734 -34.331   3.453  1.00 50.75           N
ANISOU   66  N   GLU B  11     5887   7002   6394    230   -116  -1275       N
ATOM     67  CA  GLU B  11      40.113 -34.528   3.142  1.00 51.34           C
ANISOU   67  CA  GLU B  11     5952   7145   6410    432    -97  -1305       C
ATOM     68  C   GLU B  11      40.997 -33.869   4.151  1.00 50.23           C
ANISOU   68  C   GLU B  11     5744   7086   6253    451    -44  -1131       C
ATOM     69  O   GLU B  11      42.079 -34.318   4.397  1.00 51.01           O
ANISOU   69  O   GLU B  11     5848   7169   6364    596    -48  -1121       O
ATOM     70  CB  GLU B  11      40.380 -33.974   1.763  1.00 51.49           C
ANISOU   70  CB  GLU B  11     5898   7387   6279    534    -68  -1418       C
ATOM     71  CG  GLU B  11      39.740 -34.795   0.719  1.00 53.11           C
ANISOU   71  CG  GLU B  11     6184   7512   6481    570   -145  -1629       C
ATOM     72  CD  GLU B  11      38.503 -34.183   0.147  1.00 52.56           C
ANISOU   72  CD  GLU B  11     6081   7522   6366    436   -173  -1671       C
ATOM     73  OE1 GLU B  11      37.721 -33.597   0.889  1.00 51.24           O
ANISOU   73  OE1 GLU B  11     5873   7340   6256    265   -162  -1549       O
ATOM     74  OE2 GLU B  11      38.296 -34.304  -1.066  1.00 53.66           O
ANISOU   74  OE2 GLU B  11     6236   7750   6404    519   -214  -1838       O
ATOM     75  N   GLU B  12      40.519 -32.796   4.737  1.00 48.59           N
ANISOU   75  N   GLU B  12     5473   6970   6020    315     -9  -1007       N
ATOM     76  CA  GLU B  12      41.277 -32.049   5.750  1.00 47.62           C
ANISOU   76  CA  GLU B  12     5287   6926   5880    317     19   -856       C
ATOM     77  C   GLU B  12      41.228 -32.654   7.163  1.00 47.93           C
ANISOU   77  C   GLU B  12     5418   6793   5998    284    -11   -746       C
ATOM     78  O   GLU B  12      42.053 -32.302   7.999  1.00 47.64           O
ANISOU   78  O   GLU B  12     5349   6808   5946    332    -15   -648       O
ATOM     79  CB  GLU B  12      40.781 -30.607   5.818  1.00 46.02           C
ANISOU   79  CB  GLU B  12     4998   6875   5614    199     56   -782       C
ATOM     80  CG  GLU B  12      40.873 -29.857   4.494  1.00 45.85           C
ANISOU   80  CG  GLU B  12     4894   7032   5496    231     91   -845       C
ATOM     81  CD  GLU B  12      40.080 -28.565   4.488  1.00 44.59           C
ANISOU   81  CD  GLU B  12     4685   6965   5291    111    107   -784       C
ATOM     82  OE1 GLU B  12      38.966 -28.532   5.049  1.00 44.10           O
ANISOU   82  OE1 GLU B  12     4661   6825   5270      3     86   -769       O
ATOM     83  OE2 GLU B  12      40.575 -27.585   3.902  1.00 44.30           O
ANISOU   83  OE2 GLU B  12     4571   7081   5181    131    143   -746       O
ATOM     84  N   VAL B  13      40.281 -33.559   7.426  1.00 48.73           N
ANISOU   84  N   VAL B  13     5632   6698   6184    199    -35   -757       N
ATOM     85  CA  VAL B  13      40.185 -34.217   8.741  1.00 49.41           C
ANISOU   85  CA  VAL B  13     5826   6614   6335    164    -49   -626       C
ATOM     86  C   VAL B  13      40.475 -35.720   8.727  1.00 51.50           C
ANISOU   86  C   VAL B  13     6231   6634   6702    253   -106   -664       C
ATOM     87  O   VAL B  13      40.941 -36.263   9.728  1.00 52.35           O
ANISOU   87  O   VAL B  13     6429   6626   6838    308   -130   -548       O
ATOM     88  CB  VAL B  13      38.814 -33.976   9.405  1.00 49.00           C
ANISOU   88  CB  VAL B  13     5790   6522   6306    -35     -9   -542       C
ATOM     89  CG1 VAL B  13      38.574 -32.479   9.577  1.00 47.17           C
ANISOU   89  CG1 VAL B  13     5439   6510   5975    -92     34   -502       C
ATOM     90  CG2 VAL B  13      37.677 -34.631   8.620  1.00 49.91           C
ANISOU   90  CG2 VAL B  13     5929   6519   6514   -149    -24   -649       C
ATOM     91  N   ARG B  14      40.210 -36.392   7.606  1.00 52.54           N
ANISOU   91  N   ARG B  14     6396   6682   6886    279   -142   -832       N
ATOM     92  CA  ARG B  14      40.370 -37.847   7.529  1.00 54.83           C
ANISOU   92  CA  ARG B  14     6840   6697   7294    358   -213   -893       C
ATOM     93  C   ARG B  14      41.758 -38.310   7.976  1.00 55.75           C
ANISOU   93  C   ARG B  14     7000   6781   7402    582   -248   -852       C
ATOM     94  O   ARG B  14      41.891 -39.370   8.586  1.00 57.53           O
ANISOU   94  O   ARG B  14     7378   6755   7724    628   -302   -794       O
ATOM     95  CB  ARG B  14      40.077 -38.365   6.113  1.00 55.92           C
ANISOU   95  CB  ARG B  14     6996   6790   7461    399   -264  -1126       C
ATOM     96  CG  ARG B  14      41.089 -37.947   5.061  1.00 55.69           C
ANISOU   96  CG  ARG B  14     6871   6983   7306    606   -249  -1263       C
ATOM     97  CD  ARG B  14      40.662 -38.423   3.688  1.00 56.96           C
ANISOU   97  CD  ARG B  14     7064   7118   7460    648   -302  -1500       C
ATOM     98  NE  ARG B  14      41.538 -37.933   2.625  1.00 56.88           N
ANISOU   98  NE  ARG B  14     6954   7365   7295    840   -261  -1616       N
ATOM     99  CZ  ARG B  14      41.239 -37.966   1.328  1.00 57.66           C
ANISOU   99  CZ  ARG B  14     7046   7552   7309    896   -282  -1812       C
ATOM    100  NH1 ARG B  14      40.089 -38.481   0.909  1.00 58.55           N
ANISOU  100  NH1 ARG B  14     7243   7509   7496    774   -369  -1936       N
ATOM    101  NH2 ARG B  14      42.099 -37.485   0.438  1.00 57.79           N
ANISOU  101  NH2 ARG B  14     6968   7827   7162   1075   -218  -1882       N
ATOM    102  N   ILE B  15      42.782 -37.516   7.672  1.00 54.80           N
ANISOU  102  N   ILE B  15     6738   6909   7173    718   -219   -876       N
ATOM    103  CA  ILE B  15      44.155 -37.867   8.012  1.00 55.82           C
ANISOU  103  CA  ILE B  15     6859   7056   7294    944   -256   -856       C
ATOM    104  C   ILE B  15      44.296 -37.918   9.526  1.00 55.84           C
ANISOU  104  C   ILE B  15     6930   6977   7311    916   -281   -651       C
ATOM    105  O   ILE B  15      44.732 -38.926  10.073  1.00 57.67           O
ANISOU  105  O   ILE B  15     7294   7010   7607   1040   -350   -606       O
ATOM    106  CB  ILE B  15      45.184 -36.878   7.412  1.00 54.91           C
ANISOU  106  CB  ILE B  15     6537   7257   7071   1056   -206   -902       C
ATOM    107  CG1 ILE B  15      44.862 -36.623   5.924  1.00 54.76           C
ANISOU  107  CG1 ILE B  15     6453   7360   6993   1056   -158  -1073       C
ATOM    108  CG2 ILE B  15      46.606 -37.395   7.633  1.00 56.47           C
ANISOU  108  CG2 ILE B  15     6699   7478   7281   1310   -251   -912       C
ATOM    109  CD1 ILE B  15      46.062 -36.439   5.005  1.00 55.55           C
ANISOU  109  CD1 ILE B  15     6411   7682   7012   1265   -116  -1175       C
ATOM    110  N   LEU B  16      43.916 -36.835  10.195  1.00 54.05           N
ANISOU  110  N   LEU B  16     6625   6899   7012    768   -233   -533       N
ATOM    111  CA  LEU B  16      43.873 -36.806  11.658  1.00 54.15           C
ANISOU  111  CA  LEU B  16     6716   6858   7003    729   -252   -343       C
ATOM    112  C   LEU B  16      43.013 -37.919  12.242  1.00 55.71           C
ANISOU  112  C   LEU B  16     7116   6763   7287    643   -262   -249       C
ATOM    113  O   LEU B  16      43.422 -38.598  13.187  1.00 57.19           O
ANISOU  113  O   LEU B  16     7432   6812   7486    732   -313   -121       O
ATOM    114  CB  LEU B  16      43.302 -35.464  12.150  1.00 52.14           C
ANISOU  114  CB  LEU B  16     6363   6793   6657    565   -192   -268       C
ATOM    115  CG  LEU B  16      44.297 -34.308  12.337  1.00 51.06           C
ANISOU  115  CG  LEU B  16     6063   6903   6435    633   -209   -263       C
ATOM    116  CD1 LEU B  16      43.748 -32.975  11.826  1.00 49.15           C
ANISOU  116  CD1 LEU B  16     5691   6843   6141    491   -145   -303       C
ATOM    117  CD2 LEU B  16      44.729 -34.186  13.793  1.00 51.52           C
ANISOU  117  CD2 LEU B  16     6173   6970   6432    679   -265   -120       C
ATOM    118  N   ARG B  17      41.823 -38.104  11.682  1.00 55.61           N
ANISOU  118  N   ARG B  17     7129   6657   7341    467   -220   -304       N
ATOM    119  CA  ARG B  17      40.855 -39.036  12.258  1.00 57.19           C
ANISOU  119  CA  ARG B  17     7493   6593   7643    324   -211   -194       C
ATOM    120  C   ARG B  17      41.366 -40.473  12.338  1.00 59.84           C
ANISOU  120  C   ARG B  17     8016   6626   8095    460   -298   -186       C
ATOM    121  O   ARG B  17      41.026 -41.200  13.269  1.00 61.51           O
ANISOU  121  O   ARG B  17     8386   6625   8358    400   -300     -9       O
ATOM    122  CB  ARG B  17      39.529 -38.998  11.489  1.00 56.90           C
ANISOU  122  CB  ARG B  17     7415   6522   7683    111   -169   -289       C
ATOM    123  CG  ARG B  17      38.385 -39.708  12.206  1.00 58.46           C
ANISOU  123  CG  ARG B  17     7725   6500   7987    -97   -130   -143       C
ATOM    124  CD  ARG B  17      37.041 -39.476  11.532  1.00 58.12           C
ANISOU  124  CD  ARG B  17     7585   6482   8014   -320    -90   -234       C
ATOM    125  NE  ARG B  17      37.093 -39.840  10.117  1.00 58.50           N
ANISOU  125  NE  ARG B  17     7616   6476   8135   -267   -172   -481       N
ATOM    126  CZ  ARG B  17      36.774 -39.049   9.092  1.00 57.05           C
ANISOU  126  CZ  ARG B  17     7287   6496   7892   -284   -171   -647       C
ATOM    127  NH1 ARG B  17      36.330 -37.805   9.272  1.00 55.00           N
ANISOU  127  NH1 ARG B  17     6882   6494   7522   -362    -96   -599       N
ATOM    128  NH2 ARG B  17      36.889 -39.524   7.860  1.00 57.89           N
ANISOU  128  NH2 ARG B  17     7410   6542   8044   -209   -254   -868       N
ATOM    129  N   ASP B  18      42.193 -40.872  11.374  1.00 60.50           N
ANISOU  129  N   ASP B  18     8085   6691   8210    655   -366   -370       N
ATOM    130  CA  ASP B  18      42.789 -42.204  11.379  1.00 63.19           C
ANISOU  130  CA  ASP B  18     8604   6745   8660    832   -465   -392       C
ATOM    131  C   ASP B  18      43.878 -42.362  12.444  1.00 64.00           C
ANISOU  131  C   ASP B  18     8761   6854   8703   1032   -515   -237       C
ATOM    132  O   ASP B  18      44.100 -43.467  12.931  1.00 66.48           O
ANISOU  132  O   ASP B  18     9271   6884   9104   1129   -590   -153       O
ATOM    133  CB  ASP B  18      43.330 -42.555   9.988  1.00 63.86           C
ANISOU  133  CB  ASP B  18     8648   6837   8777   1009   -517   -662       C
ATOM    134  CG  ASP B  18      42.213 -42.854   8.991  1.00 64.22           C
ANISOU  134  CG  ASP B  18     8719   6766   8914    839   -520   -824       C
ATOM    135  OD1 ASP B  18      41.068 -42.379   9.209  1.00 63.10           O
ANISOU  135  OD1 ASP B  18     8536   6656   8783    575   -457   -748       O
ATOM    136  OD2 ASP B  18      42.470 -43.558   7.991  1.00 65.78           O
ANISOU  136  OD2 ASP B  18     8973   6851   9171    978   -592  -1040       O
ATOM    137  N   LYS B  19      44.548 -41.267  12.802  1.00 62.18           N
ANISOU  137  N   LYS B  19     8362   6935   8330   1092   -489   -200       N
ATOM    138  CA  LYS B  19      45.566 -41.277  13.867  1.00 62.94           C
ANISOU  138  CA  LYS B  19     8481   7080   8352   1274   -555    -60       C
ATOM    139  C   LYS B  19      44.954 -41.311  15.273  1.00 63.35           C
ANISOU  139  C   LYS B  19     8672   7048   8350   1145   -533    194       C
ATOM    140  O   LYS B  19      45.623 -41.692  16.230  1.00 64.83           O
ANISOU  140  O   LYS B  19     8960   7183   8490   1299   -608    334       O
ATOM    141  CB  LYS B  19      46.478 -40.054  13.762  1.00 61.12           C
ANISOU  141  CB  LYS B  19     8008   7211   8004   1358   -547   -120       C
ATOM    142  CG  LYS B  19      47.342 -40.014  12.515  1.00 61.21           C
ANISOU  142  CG  LYS B  19     7865   7353   8040   1529   -557   -333       C
ATOM    143  CD  LYS B  19      48.109 -38.701  12.418  1.00 59.51           C
ANISOU  143  CD  LYS B  19     7392   7492   7727   1546   -528   -362       C
ATOM    144  CE  LYS B  19      49.156 -38.674  11.288  1.00 60.10           C
ANISOU  144  CE  LYS B  19     7289   7735   7811   1740   -521   -539       C
ATOM    145  NZ  LYS B  19      50.013 -39.880  11.063  1.00 62.75           N
ANISOU  145  NZ  LYS B  19     7694   7934   8216   2028   -603   -621       N
ATOM    146  N   LEU B  20      43.694 -40.900  15.398  1.00 62.25           N
ANISOU  146  N   LEU B  20     8531   6918   8203    879   -429    255       N
ATOM    147  CA  LEU B  20      43.016 -40.908  16.689  1.00 62.83           C
ANISOU  147  CA  LEU B  20     8723   6944   8207    750   -377    497       C
ATOM    148  C   LEU B  20      42.833 -42.349  17.158  1.00 65.94           C
ANISOU  148  C   LEU B  20     9373   6971   8711    770   -417    647       C
ATOM    149  O   LEU B  20      42.586 -43.252  16.356  1.00 67.28           O
ANISOU  149  O   LEU B  20     9624   6888   9052    751   -448    548       O
ATOM    150  CB  LEU B  20      41.641 -40.230  16.600  1.00 61.34           C
ANISOU  150  CB  LEU B  20     8454   6846   8006    467   -245    510       C
ATOM    151  CG  LEU B  20      41.504 -38.707  16.540  1.00 58.58           C
ANISOU  151  CG  LEU B  20     7899   6834   7526    401   -188    442       C
ATOM    152  CD1 LEU B  20      40.044 -38.266  16.594  1.00 57.82           C
ANISOU  152  CD1 LEU B  20     7757   6781   7431    144    -63    481       C
ATOM    153  CD2 LEU B  20      42.286 -38.026  17.646  1.00 58.26           C
ANISOU  153  CD2 LEU B  20     7845   6979   7314    527   -227    546       C
ATOM    154  N   GLU B  21      42.968 -42.548  18.464  1.00 67.32           N
ANISOU  154  N   GLU B  21     9686   7112   8782    815   -424    887       N
ATOM    155  CA  GLU B  21      42.700 -43.835  19.092  1.00 70.50           C
ANISOU  155  CA  GLU B  21    10353   7166   9269    808   -444   1094       C
ATOM    156  C   GLU B  21      41.582 -43.678  20.098  1.00 71.03           C
ANISOU  156  C   GLU B  21    10490   7245   9253    574   -304   1342       C
ATOM    157  O   GLU B  21      41.355 -42.584  20.603  1.00 69.19           O
ANISOU  157  O   GLU B  21    10130   7313   8845    516   -229   1369       O
ATOM    158  CB  GLU B  21      43.955 -44.352  19.765  1.00 72.39           C
ANISOU  158  CB  GLU B  21    10720   7343   9442   1115   -585   1185       C
ATOM    159  CG  GLU B  21      45.061 -44.543  18.748  1.00 72.21           C
ANISOU  159  CG  GLU B  21    10603   7328   9507   1361   -708    935       C
ATOM    160  CD  GLU B  21      46.402 -44.838  19.357  1.00 73.80           C
ANISOU  160  CD  GLU B  21    10857   7552   9632   1690   -856    987       C
ATOM    161  OE1 GLU B  21      46.670 -44.332  20.469  1.00 73.77           O
ANISOU  161  OE1 GLU B  21    10860   7721   9446   1737   -873   1149       O
ATOM    162  OE2 GLU B  21      47.185 -45.555  18.694  1.00 75.21           O
ANISOU  162  OE2 GLU B  21    11059   7590   9926   1913   -963    848       O
ATOM    163  N   GLN B  22      40.882 -44.771  20.378  1.00 73.79           N
ANISOU  163  N   GLN B  22    11039   7265   9732    440   -266   1521       N
ATOM    164  CA  GLN B  22      39.696 -44.716  21.225  1.00 74.71           C
ANISOU  164  CA  GLN B  22    11202   7389   9794    184   -102   1764       C
ATOM    165  C   GLN B  22      38.673 -43.767  20.573  1.00 72.13           C
ANISOU  165  C   GLN B  22    10631   7286   9488    -55     21   1607       C
ATOM    166  O   GLN B  22      37.998 -42.998  21.251  1.00 71.34           O
ANISOU  166  O   GLN B  22    10449   7419   9239   -177    153   1715       O
ATOM    167  CB  GLN B  22      40.067 -44.268  22.681  1.00 75.23           C
ANISOU  167  CB  GLN B  22    11347   7659   9580    306    -74   2002       C
ATOM    168  CG  GLN B  22      39.107 -44.765  23.772  1.00 77.94           C
ANISOU  168  CG  GLN B  22    11853   7896   9864    122     78   2345       C
ATOM    169  CD  GLN B  22      37.709 -44.163  23.683  1.00 76.93           C
ANISOU  169  CD  GLN B  22    11557   7924   9747   -190    277   2351       C
ATOM    170  OE1 GLN B  22      36.718 -44.886  23.694  1.00 79.08           O
ANISOU  170  OE1 GLN B  22    11890   7982  10175   -435    387   2500       O
ATOM    171  NE2 GLN B  22      37.627 -42.834  23.606  1.00 73.89           N
ANISOU  171  NE2 GLN B  22    10954   7911   9209   -179    318   2192       N
ATOM    172  N   ALA B  23      38.552 -43.841  19.249  1.00 71.06           N
ANISOU  172  N   ALA B  23    10388   7082   9529   -102    -30   1347       N
ATOM    173  CA  ALA B  23      37.727 -42.894  18.502  1.00 68.57           C
ANISOU  173  CA  ALA B  23     9837   6993   9223   -278     51   1170       C
ATOM    174  C   ALA B  23      36.241 -43.163  18.735  1.00 69.94           C
ANISOU  174  C   ALA B  23     9995   7081   9498   -596    193   1305       C
ATOM    175  O   ALA B  23      35.772 -44.292  18.607  1.00 72.62           O
ANISOU  175  O   ALA B  23    10464   7089  10038   -731    183   1382       O
ATOM    176  CB  ALA B  23      38.057 -42.945  17.015  1.00 67.42           C
ANISOU  176  CB  ALA B  23     9598   6808   9212   -214    -52    861       C
ATOM    177  N   GLU B  24      35.515 -42.102  19.069  1.00 68.29           N
ANISOU  177  N   GLU B  24     9616   7174   9156   -714    321   1327       N
ATOM    178  CA  GLU B  24      34.088 -42.166  19.356  1.00 69.51           C
ANISOU  178  CA  GLU B  24     9698   7333   9379  -1004    478   1452       C
ATOM    179  C   GLU B  24      33.426 -40.966  18.671  1.00 66.77           C
ANISOU  179  C   GLU B  24     9087   7286   8996  -1086    526   1246       C
ATOM    180  O   GLU B  24      33.479 -39.854  19.184  1.00 64.99           O
ANISOU  180  O   GLU B  24     8765   7364   8564  -1012    586   1253       O
ATOM    181  CB  GLU B  24      33.856 -42.143  20.873  1.00 71.16           C
ANISOU  181  CB  GLU B  24    10006   7626   9404  -1025    617   1772       C
ATOM    182  CG  GLU B  24      32.356 -42.093  21.287  1.00 72.62           C
ANISOU  182  CG  GLU B  24    10078   7886   9628  -1320    820   1924       C
ATOM    183  CD  GLU B  24      31.820 -43.370  21.950  1.00 76.71           C
ANISOU  183  CD  GLU B  24    10771   8101  10276  -1506    910   2230       C
ATOM    184  OE1 GLU B  24      32.446 -44.445  21.821  1.00 78.55           O
ANISOU  184  OE1 GLU B  24    11218   7986  10644  -1445    791   2284       O
ATOM    185  OE2 GLU B  24      30.744 -43.304  22.601  1.00 78.37           O
ANISOU  185  OE2 GLU B  24    10901   8417  10458  -1717   1106   2423       O
ATOM    186  N   THR B  25      32.813 -41.206  17.511  1.00 66.70           N
ANISOU  186  N   THR B  25     8975   7181   9188  -1226    483   1056       N
ATOM    187  CA  THR B  25      32.213 -40.143  16.695  1.00 64.34           C
ANISOU  187  CA  THR B  25     8437   7140   8868  -1282    497    845       C
ATOM    188  C   THR B  25      30.731 -39.929  16.980  1.00 65.31           C
ANISOU  188  C   THR B  25     8403   7369   9044  -1542    646    929       C
ATOM    189  O   THR B  25      29.985 -40.880  17.200  1.00 68.10           O
ANISOU  189  O   THR B  25     8795   7510   9568  -1753    701   1062       O
ATOM    190  CB  THR B  25      32.380 -40.438  15.193  1.00 63.78           C
ANISOU  190  CB  THR B  25     8328   6952   8955  -1261    353    566       C
ATOM    191  OG1 THR B  25      33.758 -40.721  14.908  1.00 63.29           O
ANISOU  191  OG1 THR B  25     8397   6798   8853  -1011    229    488       O
ATOM    192  CG2 THR B  25      31.934 -39.250  14.354  1.00 61.29           C
ANISOU  192  CG2 THR B  25     7789   6922   8576  -1269    353    361       C
ATOM    193  N   GLU B  26      30.317 -38.667  16.960  1.00 63.21           N
ANISOU  193  N   GLU B  26     7951   7426   8640  -1523    707    849       N
ATOM    194  CA  GLU B  26      28.941 -38.293  17.223  1.00 64.01           C
ANISOU  194  CA  GLU B  26     7865   7689   8766  -1726    850    904       C
ATOM    195  C   GLU B  26      28.573 -37.068  16.391  1.00 61.49           C
ANISOU  195  C   GLU B  26     7335   7634   8394  -1681    816    673       C
ATOM    196  O   GLU B  26      29.400 -36.167  16.229  1.00 59.04           O
ANISOU  196  O   GLU B  26     7034   7470   7927  -1478    751    571       O
ATOM    197  CB  GLU B  26      28.788 -38.025  18.715  1.00 64.99           C
ANISOU  197  CB  GLU B  26     8034   7960   8698  -1712   1018   1162       C
ATOM    198  CG  GLU B  26      27.357 -37.883  19.200  1.00 66.75           C
ANISOU  198  CG  GLU B  26     8078   8333   8949  -1929   1206   1278       C
ATOM    199  CD  GLU B  26      27.119 -38.579  20.531  1.00 69.75           C
ANISOU  199  CD  GLU B  26     8581   8655   9267  -2017   1374   1610       C
ATOM    200  OE1 GLU B  26      27.298 -39.816  20.591  1.00 72.08           O
ANISOU  200  OE1 GLU B  26     9038   8629   9720  -2121   1349   1749       O
ATOM    201  OE2 GLU B  26      26.741 -37.907  21.513  1.00 70.07           O
ANISOU  201  OE2 GLU B  26     8567   8962   9097  -1978   1533   1735       O
ATOM    202  N   THR B  27      27.354 -37.052  15.842  1.00 62.34           N
ANISOU  202  N   THR B  27     7251   7791   8644  -1872    847    594       N
ATOM    203  CA  THR B  27      26.907 -35.974  14.943  1.00 60.35           C
ANISOU  203  CA  THR B  27     6802   7767   8361  -1830    795    374       C
ATOM    204  C   THR B  27      25.909 -35.048  15.629  1.00 60.43           C
ANISOU  204  C   THR B  27     6627   8066   8269  -1875    946    441       C
ATOM    205  O   THR B  27      24.944 -35.510  16.233  1.00 62.83           O
ANISOU  205  O   THR B  27     6842   8378   8654  -2063   1082    586       O
ATOM    206  CB  THR B  27      26.233 -36.525  13.661  1.00 61.29           C
ANISOU  206  CB  THR B  27     6816   7766   8705  -1976    681    185       C
ATOM    207  OG1 THR B  27      27.119 -37.428  12.985  1.00 61.56           O
ANISOU  207  OG1 THR B  27     7027   7529   8833  -1918    538     97       O
ATOM    208  CG2 THR B  27      25.871 -35.390  12.706  1.00 59.31           C
ANISOU  208  CG2 THR B  27     6389   7755   8393  -1895    610    -33       C
ATOM    209  N   VAL B  28      26.139 -33.744  15.504  1.00 58.06           N
ANISOU  209  N   VAL B  28     6263   7999   7799  -1700    923    332       N
ATOM    210  CA  VAL B  28      25.260 -32.723  16.064  1.00 58.02           C
ANISOU  210  CA  VAL B  28     6088   8277   7682  -1688   1043    351       C
ATOM    211  C   VAL B  28      24.989 -31.688  14.981  1.00 56.19           C
ANISOU  211  C   VAL B  28     5711   8193   7443  -1604    935    124       C
ATOM    212  O   VAL B  28      25.922 -31.090  14.454  1.00 54.02           O
ANISOU  212  O   VAL B  28     5524   7918   7084  -1439    821     19       O
ATOM    213  CB  VAL B  28      25.916 -32.030  17.279  1.00 57.27           C
ANISOU  213  CB  VAL B  28     6108   8311   7340  -1515   1120    469       C
ATOM    214  CG1 VAL B  28      24.928 -31.101  17.968  1.00 57.85           C
ANISOU  214  CG1 VAL B  28     6017   8667   7295  -1496   1261    491       C
ATOM    215  CG2 VAL B  28      26.453 -33.064  18.261  1.00 58.96           C
ANISOU  215  CG2 VAL B  28     6515   8358   7528  -1550   1188    694       C
ATOM    216  N   ALA B  29      23.722 -31.491  14.638  1.00 57.31           N
ANISOU  216  N   ALA B  29     5629   8465   7679  -1717    971     60       N
ATOM    217  CA  ALA B  29      23.325 -30.544  13.590  1.00 56.00           C
ANISOU  217  CA  ALA B  29     5321   8444   7511  -1634    861   -144       C
ATOM    218  C   ALA B  29      24.022 -30.813  12.249  1.00 54.77           C
ANISOU  218  C   ALA B  29     5252   8138   7421  -1591    674   -305       C
ATOM    219  O   ALA B  29      24.392 -29.882  11.522  1.00 52.93           O
ANISOU  219  O   ALA B  29     5021   7994   7094  -1437    576   -431       O
ATOM    220  CB  ALA B  29      23.580 -29.117  14.054  1.00 54.27           C
ANISOU  220  CB  ALA B  29     5108   8429   7084  -1425    886   -163       C
ATOM    221  N   GLY B  30      24.202 -32.093  11.932  1.00 56.07           N
ANISOU  221  N   GLY B  30     5496   8069   7740  -1722    628   -296       N
ATOM    222  CA  GLY B  30      24.904 -32.502  10.720  1.00 55.34           C
ANISOU  222  CA  GLY B  30     5502   7828   7696  -1667    461   -453       C
ATOM    223  C   GLY B  30      26.417 -32.305  10.744  1.00 53.40           C
ANISOU  223  C   GLY B  30     5459   7516   7314  -1477    420   -436       C
ATOM    224  O   GLY B  30      27.073 -32.451   9.711  1.00 52.70           O
ANISOU  224  O   GLY B  30     5439   7357   7226  -1391    298   -571       O
ATOM    225  N   CYS B  31      26.975 -31.987  11.913  1.00 52.80           N
ANISOU  225  N   CYS B  31     5471   7476   7116  -1405    519   -277       N
ATOM    226  CA  CYS B  31      28.415 -31.793  12.073  1.00 51.25           C
ANISOU  226  CA  CYS B  31     5440   7232   6801  -1233    478   -252       C
ATOM    227  C   CYS B  31      29.036 -32.979  12.798  1.00 52.57           C
ANISOU  227  C   CYS B  31     5773   7183   7018  -1265    505   -112       C
ATOM    228  O   CYS B  31      28.568 -33.387  13.862  1.00 54.04           O
ANISOU  228  O   CYS B  31     5976   7345   7214  -1361    617     56       O
ATOM    229  CB  CYS B  31      28.697 -30.509  12.847  1.00 49.79           C
ANISOU  229  CB  CYS B  31     5244   7240   6435  -1106    531   -197       C
ATOM    230  SG  CYS B  31      28.312 -29.004  11.925  1.00 48.15           S
ANISOU  230  SG  CYS B  31     4897   7241   6156  -1013    468   -355       S
ATOM    231  N   GLU B  32      30.092 -33.528  12.208  1.00 52.23           N
ANISOU  231  N   GLU B  32     5854   6992   7001  -1169    405   -176       N
ATOM    232  CA  GLU B  32      30.809 -34.671  12.768  1.00 53.57           C
ANISOU  232  CA  GLU B  32     6198   6934   7222  -1158    399    -62       C
ATOM    233  C   GLU B  32      31.742 -34.218  13.905  1.00 52.77           C
ANISOU  233  C   GLU B  32     6192   6905   6954  -1017    440     81       C
ATOM    234  O   GLU B  32      32.494 -33.263  13.750  1.00 50.91           O
ANISOU  234  O   GLU B  32     5934   6814   6597   -871    400     18       O
ATOM    235  CB  GLU B  32      31.623 -35.336  11.659  1.00 53.60           C
ANISOU  235  CB  GLU B  32     6285   6782   7300  -1066    269   -215       C
ATOM    236  CG  GLU B  32      32.063 -36.762  11.940  1.00 55.70           C
ANISOU  236  CG  GLU B  32     6725   6751   7688  -1079    235   -143       C
ATOM    237  CD  GLU B  32      33.190 -37.205  11.021  1.00 55.51           C
ANISOU  237  CD  GLU B  32     6792   6624   7676   -902    114   -294       C
ATOM    238  OE1 GLU B  32      34.361 -36.805  11.268  1.00 54.34           O
ANISOU  238  OE1 GLU B  32     6686   6556   7404   -715    101   -268       O
ATOM    239  OE2 GLU B  32      32.899 -37.960  10.062  1.00 56.77           O
ANISOU  239  OE2 GLU B  32     6972   6631   7969   -947     30   -448       O
ATOM    240  N   PHE B  33      31.664 -34.888  15.051  1.00 54.43           N
ANISOU  240  N   PHE B  33     6507   7016   7159  -1067    517    279       N
ATOM    241  CA  PHE B  33      32.598 -34.668  16.159  1.00 54.22           C
ANISOU  241  CA  PHE B  33     6598   7033   6972   -921    530    415       C
ATOM    242  C   PHE B  33      33.244 -35.988  16.519  1.00 56.11           C
ANISOU  242  C   PHE B  33     7025   7010   7283   -893    492    534       C
ATOM    243  O   PHE B  33      32.605 -36.829  17.153  1.00 58.34           O
ANISOU  243  O   PHE B  33     7379   7155   7632  -1027    572    701       O
ATOM    244  CB  PHE B  33      31.868 -34.155  17.390  1.00 54.85           C
ANISOU  244  CB  PHE B  33     6647   7274   6920   -973    667    570       C
ATOM    245  CG  PHE B  33      31.398 -32.740  17.275  1.00 53.13           C
ANISOU  245  CG  PHE B  33     6272   7317   6597   -944    694    463       C
ATOM    246  CD1 PHE B  33      30.150 -32.450  16.745  1.00 53.27           C
ANISOU  246  CD1 PHE B  33     6123   7421   6697  -1079    751    390       C
ATOM    247  CD2 PHE B  33      32.191 -31.701  17.723  1.00 51.67           C
ANISOU  247  CD2 PHE B  33     6107   7282   6242   -778    650    434       C
ATOM    248  CE1 PHE B  33      29.704 -31.142  16.655  1.00 51.93           C
ANISOU  248  CE1 PHE B  33     5821   7478   6432  -1028    767    293       C
ATOM    249  CE2 PHE B  33      31.752 -30.396  17.635  1.00 50.37           C
ANISOU  249  CE2 PHE B  33     5821   7323   5995   -745    664    335       C
ATOM    250  CZ  PHE B  33      30.504 -30.114  17.100  1.00 50.48           C
ANISOU  250  CZ  PHE B  33     5681   7417   6083   -860    725    268       C
ATOM    251  N   THR B  34      34.489 -36.194  16.101  1.00 55.49           N
ANISOU  251  N   THR B  34     7025   6859   7202   -719    373    455       N
ATOM    252  CA  THR B  34      35.218 -37.398  16.496  1.00 57.40           C
ANISOU  252  CA  THR B  34     7457   6853   7499   -643    320    564       C
ATOM    253  C   THR B  34      36.118 -37.077  17.676  1.00 57.36           C
ANISOU  253  C   THR B  34     7541   6943   7311   -478    310    705       C
ATOM    254  O   THR B  34      36.842 -36.082  17.666  1.00 55.55           O
ANISOU  254  O   THR B  34     7235   6912   6959   -346    262    621       O
ATOM    255  CB  THR B  34      36.043 -37.994  15.341  1.00 57.36           C
ANISOU  255  CB  THR B  34     7486   6699   7610   -527    190    387       C
ATOM    256  OG1 THR B  34      35.199 -38.198  14.200  1.00 57.42           O
ANISOU  256  OG1 THR B  34     7409   6647   7761   -666    180    226       O
ATOM    257  CG2 THR B  34      36.648 -39.337  15.756  1.00 59.80           C
ANISOU  257  CG2 THR B  34     8004   6714   8002   -448    130    499       C
ATOM    258  N   LYS B  35      36.064 -37.935  18.689  1.00 59.67           N
ANISOU  258  N   LYS B  35     7999   7084   7588   -492    348    925       N
ATOM    259  CA  LYS B  35      36.754 -37.710  19.951  1.00 60.19           C
ANISOU  259  CA  LYS B  35     8168   7244   7456   -343    340   1085       C
ATOM    260  C   LYS B  35      37.640 -38.911  20.256  1.00 62.29           C
ANISOU  260  C   LYS B  35     8640   7257   7772   -208    245   1197       C
ATOM    261  O   LYS B  35      37.156 -40.041  20.304  1.00 64.60           O
ANISOU  261  O   LYS B  35     9060   7284   8201   -315    277   1320       O
ATOM    262  CB  LYS B  35      35.710 -37.501  21.046  1.00 61.34           C
ANISOU  262  CB  LYS B  35     8329   7497   7482   -475    501   1281       C
ATOM    263  CG  LYS B  35      36.247 -37.432  22.465  1.00 62.60           C
ANISOU  263  CG  LYS B  35     8632   7743   7411   -331    505   1475       C
ATOM    264  CD  LYS B  35      35.104 -37.319  23.427  1.00 64.11           C
ANISOU  264  CD  LYS B  35     8831   8045   7485   -470    692   1667       C
ATOM    265  CE  LYS B  35      35.478 -36.952  24.852  1.00 65.21           C
ANISOU  265  CE  LYS B  35     9087   8357   7332   -317    713   1828       C
ATOM    266  NZ  LYS B  35      34.231 -36.751  25.655  1.00 66.72           N
ANISOU  266  NZ  LYS B  35     9249   8701   7402   -459    928   1990       N
ATOM    267  N   GLY B  36      38.932 -38.659  20.466  1.00 61.75           N
ANISOU  267  N   GLY B  36     8595   7264   7605     27    120   1154       N
ATOM    268  CA  GLY B  36      39.895 -39.723  20.740  1.00 63.80           C
ANISOU  268  CA  GLY B  36     9034   7306   7901    206      6   1241       C
ATOM    269  C   GLY B  36      41.210 -39.217  21.320  1.00 63.42           C
ANISOU  269  C   GLY B  36     8980   7425   7690    459   -119   1227       C
ATOM    270  O   GLY B  36      41.295 -38.086  21.807  1.00 61.98           O
ANISOU  270  O   GLY B  36     8696   7512   7343    477   -109   1200       O
ATOM    271  N   GLN B  37      42.233 -40.067  21.262  1.00 64.93           N
ANISOU  271  N   GLN B  37     9278   7452   7941    660   -250   1236       N
ATOM    272  CA  GLN B  37      43.546 -39.774  21.838  1.00 65.17           C
ANISOU  272  CA  GLN B  37     9301   7621   7841    916   -392   1231       C
ATOM    273  C   GLN B  37      44.612 -39.634  20.759  1.00 64.10           C
ANISOU  273  C   GLN B  37     9007   7536   7813   1069   -502    997       C
ATOM    274  O   GLN B  37      44.699 -40.472  19.865  1.00 64.83           O
ANISOU  274  O   GLN B  37     9133   7424   8076   1098   -522    911       O
ATOM    275  CB  GLN B  37      43.959 -40.894  22.799  1.00 68.37           C
ANISOU  275  CB  GLN B  37     9957   7817   8202   1070   -466   1459       C
ATOM    276  CG  GLN B  37      42.939 -41.230  23.881  1.00 70.15           C
ANISOU  276  CG  GLN B  37    10366   7968   8318    926   -340   1737       C
ATOM    277  CD  GLN B  37      42.547 -40.021  24.714  1.00 68.89           C
ANISOU  277  CD  GLN B  37    10123   8130   7922    867   -265   1770       C
ATOM    278  OE1 GLN B  37      43.358 -39.120  24.949  1.00 67.67           O
ANISOU  278  OE1 GLN B  37     9855   8217   7640   1010   -370   1655       O
ATOM    279  NE2 GLN B  37      41.296 -39.991  25.158  1.00 69.42           N
ANISOU  279  NE2 GLN B  37    10236   8203   7938    655    -87   1918       N
ATOM    280  N   LEU B  38      45.415 -38.575  20.849  1.00 62.66           N
ANISOU  280  N   LEU B  38     8649   7627   7531   1163   -570    892       N
ATOM    281  CA  LEU B  38      46.566 -38.383  19.963  1.00 62.06           C
ANISOU  281  CA  LEU B  38     8398   7645   7536   1321   -665    699       C
ATOM    282  C   LEU B  38      47.653 -37.575  20.675  1.00 62.00           C
ANISOU  282  C   LEU B  38     8274   7883   7401   1473   -789    685       C
ATOM    283  O   LEU B  38      47.355 -36.589  21.344  1.00 61.01           O
ANISOU  283  O   LEU B  38     8105   7933   7141   1382   -773    714       O
ATOM    284  CB  LEU B  38      46.148 -37.680  18.669  1.00 59.70           C
ANISOU  284  CB  LEU B  38     7911   7447   7325   1170   -574    509       C
ATOM    285  CG  LEU B  38      47.241 -37.526  17.599  1.00 59.31           C
ANISOU  285  CG  LEU B  38     7673   7503   7357   1315   -631    319       C
ATOM    286  CD1 LEU B  38      47.658 -38.890  17.069  1.00 61.37           C
ANISOU  286  CD1 LEU B  38     8046   7530   7743   1483   -683    281       C
ATOM    287  CD2 LEU B  38      46.785 -36.624  16.453  1.00 57.04           C
ANISOU  287  CD2 LEU B  38     7208   7357   7106   1157   -533    166       C
ATOM    288  N   ALA B  39      48.907 -38.015  20.539  1.00 63.37           N
ANISOU  288  N   ALA B  39     8393   8063   7621   1711   -923    630       N
ATOM    289  CA  ALA B  39      50.051 -37.384  21.205  1.00 63.87           C
ANISOU  289  CA  ALA B  39     8328   8349   7591   1870  -1073    608       C
ATOM    290  C   ALA B  39      49.773 -37.138  22.694  1.00 64.75           C
ANISOU  290  C   ALA B  39     8591   8510   7502   1873  -1123    777       C
ATOM    291  O   ALA B  39      50.092 -36.074  23.230  1.00 64.08           O
ANISOU  291  O   ALA B  39     8389   8652   7308   1858  -1190    732       O
ATOM    292  CB  ALA B  39      50.407 -36.082  20.505  1.00 61.71           C
ANISOU  292  CB  ALA B  39     7768   8331   7350   1773  -1053    434       C
ATOM    293  N   GLY B  40      49.161 -38.126  23.345  1.00 66.50           N
ANISOU  293  N   GLY B  40     9081   8513   7672   1888  -1090    972       N
ATOM    294  CA  GLY B  40      48.729 -38.016  24.737  1.00 67.68           C
ANISOU  294  CA  GLY B  40     9410   8701   7604   1885  -1099   1163       C
ATOM    295  C   GLY B  40      47.844 -36.818  25.039  1.00 65.72           C
ANISOU  295  C   GLY B  40     9097   8639   7235   1676   -990   1137       C
ATOM    296  O   GLY B  40      47.898 -36.270  26.135  1.00 66.41           O
ANISOU  296  O   GLY B  40     9236   8881   7114   1725  -1049   1200       O
ATOM    297  N   HIS B  41      47.029 -36.405  24.071  1.00 63.49           N
ANISOU  297  N   HIS B  41     8706   8346   7072   1461   -841   1033       N
ATOM    298  CA  HIS B  41      46.040 -35.356  24.285  1.00 61.82           C
ANISOU  298  CA  HIS B  41     8446   8279   6763   1267   -723   1011       C
ATOM    299  C   HIS B  41      44.663 -35.942  24.056  1.00 61.82           C
ANISOU  299  C   HIS B  41     8560   8111   6818   1074   -532   1120       C
ATOM    300  O   HIS B  41      44.513 -36.874  23.264  1.00 62.20           O
ANISOU  300  O   HIS B  41     8647   7945   7042   1042   -496   1122       O
ATOM    301  CB  HIS B  41      46.247 -34.193  23.313  1.00 59.28           C
ANISOU  301  CB  HIS B  41     7871   8116   6537   1176   -723    788       C
ATOM    302  CG  HIS B  41      47.528 -33.452  23.515  1.00 59.33           C
ANISOU  302  CG  HIS B  41     7724   8305   6513   1313   -900    674       C
ATOM    303  ND1 HIS B  41      47.794 -32.724  24.654  1.00 60.03           N
ANISOU  303  ND1 HIS B  41     7836   8555   6418   1376  -1006    688       N
ATOM    304  CD2 HIS B  41      48.606 -33.300  22.712  1.00 59.00           C
ANISOU  304  CD2 HIS B  41     7489   8321   6607   1391   -989    538       C
ATOM    305  CE1 HIS B  41      48.986 -32.165  24.551  1.00 60.15           C
ANISOU  305  CE1 HIS B  41     7674   8704   6476   1472  -1169    563       C
ATOM    306  NE2 HIS B  41      49.501 -32.500  23.382  1.00 59.54           N
ANISOU  306  NE2 HIS B  41     7454   8575   6595   1479  -1150    480       N
ATOM    307  N   GLU B  42      43.659 -35.404  24.744  1.00 61.65           N
ANISOU  307  N   GLU B  42     8583   8188   6652    949   -416   1200       N
ATOM    308  CA  GLU B  42      42.273 -35.688  24.379  1.00 61.33           C
ANISOU  308  CA  GLU B  42     8568   8046   6688    727   -223   1262       C
ATOM    309  C   GLU B  42      41.913 -34.711  23.291  1.00 58.60           C
ANISOU  309  C   GLU B  42     8006   7809   6451    596   -179   1048       C
ATOM    310  O   GLU B  42      41.853 -33.507  23.531  1.00 57.32           O
ANISOU  310  O   GLU B  42     7742   7855   6183    584   -188    955       O
ATOM    311  CB  GLU B  42      41.314 -35.549  25.556  1.00 62.62           C
ANISOU  311  CB  GLU B  42     8849   8296   6649    658    -96   1445       C
ATOM    312  CG  GLU B  42      41.338 -36.793  26.424  1.00 65.73           C
ANISOU  312  CG  GLU B  42     9485   8513   6974    727    -83   1712       C
ATOM    313  CD  GLU B  42      40.671 -36.630  27.777  1.00 67.57           C
ANISOU  313  CD  GLU B  42     9850   8882   6940    721     26   1916       C
ATOM    314  OE1 GLU B  42      40.340 -35.484  28.166  1.00 66.49           O
ANISOU  314  OE1 GLU B  42     9620   8998   6643    710     62   1823       O
ATOM    315  OE2 GLU B  42      40.483 -37.669  28.453  1.00 70.35           O
ANISOU  315  OE2 GLU B  42    10409   9080   7239    737     78   2175       O
ATOM    316  N   VAL B  43      41.690 -35.236  22.094  1.00 57.94           N
ANISOU  316  N   VAL B  43     7868   7574   6574    510   -144    966       N
ATOM    317  CA  VAL B  43      41.540 -34.407  20.913  1.00 55.57           C
ANISOU  317  CA  VAL B  43     7372   7367   6376    422   -126    762       C
ATOM    318  C   VAL B  43      40.116 -34.518  20.387  1.00 55.15           C
ANISOU  318  C   VAL B  43     7294   7253   6407    208     22    763       C
ATOM    319  O   VAL B  43      39.649 -35.609  20.077  1.00 56.40           O
ANISOU  319  O   VAL B  43     7539   7201   6690    135     66    826       O
ATOM    320  CB  VAL B  43      42.555 -34.800  19.820  1.00 55.26           C
ANISOU  320  CB  VAL B  43     7258   7254   6483    528   -222    626       C
ATOM    321  CG1 VAL B  43      42.309 -34.027  18.533  1.00 53.13           C
ANISOU  321  CG1 VAL B  43     6807   7076   6304    430   -184    442       C
ATOM    322  CG2 VAL B  43      43.974 -34.549  20.319  1.00 55.74           C
ANISOU  322  CG2 VAL B  43     7288   7419   6471    734   -373    609       C
ATOM    323  N   ILE B  44      39.433 -33.380  20.298  1.00 53.60           N
ANISOU  323  N   ILE B  44     6976   7235   6154    111     86    687       N
ATOM    324  CA  ILE B  44      38.110 -33.312  19.688  1.00 53.08           C
ANISOU  324  CA  ILE B  44     6838   7155   6174    -78    209    654       C
ATOM    325  C   ILE B  44      38.260 -32.834  18.242  1.00 51.22           C
ANISOU  325  C   ILE B  44     6454   6948   6060   -102    169    453       C
ATOM    326  O   ILE B  44      38.587 -31.677  17.981  1.00 49.66           O
ANISOU  326  O   ILE B  44     6145   6914   5809    -66    131    346       O
ATOM    327  CB  ILE B  44      37.157 -32.376  20.466  1.00 52.85           C
ANISOU  327  CB  ILE B  44     6765   7312   6002   -149    311    693       C
ATOM    328  CG1 ILE B  44      36.935 -32.896  21.895  1.00 55.04           C
ANISOU  328  CG1 ILE B  44     7198   7585   6129   -122    376    909       C
ATOM    329  CG2 ILE B  44      35.821 -32.241  19.734  1.00 52.34           C
ANISOU  329  CG2 ILE B  44     6587   7259   6043   -330    422    637       C
ATOM    330  CD1 ILE B  44      37.864 -32.288  22.928  1.00 55.27           C
ANISOU  330  CD1 ILE B  44     7293   7753   5955     59    279    929       C
ATOM    331  N   LEU B  45      38.032 -33.753  17.315  1.00 51.72           N
ANISOU  331  N   LEU B  45     6531   6841   6280   -159    171    406       N
ATOM    332  CA  LEU B  45      38.158 -33.483  15.897  1.00 50.43           C
ANISOU  332  CA  LEU B  45     6251   6699   6212   -165    136    223       C
ATOM    333  C   LEU B  45      36.797 -33.127  15.333  1.00 49.88           C
ANISOU  333  C   LEU B  45     6088   6673   6190   -337    216    165       C
ATOM    334  O   LEU B  45      35.830 -33.863  15.517  1.00 51.19           O
ANISOU  334  O   LEU B  45     6296   6723   6432   -469    281    234       O
ATOM    335  CB  LEU B  45      38.718 -34.721  15.203  1.00 51.63           C
ANISOU  335  CB  LEU B  45     6482   6645   6492    -98     74    177       C
ATOM    336  CG  LEU B  45      39.044 -34.625  13.713  1.00 50.79           C
ANISOU  336  CG  LEU B  45     6280   6562   6457    -58     32    -17       C
ATOM    337  CD1 LEU B  45      39.876 -33.396  13.371  1.00 49.09           C
ANISOU  337  CD1 LEU B  45     5929   6572   6152     32      5    -94       C
ATOM    338  CD2 LEU B  45      39.757 -35.895  13.281  1.00 52.42           C
ANISOU  338  CD2 LEU B  45     6590   6565   6763     62    -39    -60       C
ATOM    339  N   LEU B  46      36.715 -31.993  14.647  1.00 48.16           N
ANISOU  339  N   LEU B  46     5739   6622   5939   -338    208     45       N
ATOM    340  CA  LEU B  46      35.438 -31.499  14.145  1.00 47.67           C
ANISOU  340  CA  LEU B  46     5575   6632   5905   -471    268    -16       C
ATOM    341  C   LEU B  46      35.521 -31.171  12.665  1.00 46.68           C
ANISOU  341  C   LEU B  46     5360   6548   5831   -457    217   -182       C
ATOM    342  O   LEU B  46      36.357 -30.366  12.250  1.00 45.53           O
ANISOU  342  O   LEU B  46     5165   6508   5626   -361    174   -238       O
ATOM    343  CB  LEU B  46      35.010 -30.257  14.939  1.00 46.86           C
ANISOU  343  CB  LEU B  46     5414   6714   5677   -475    314     21       C
ATOM    344  CG  LEU B  46      33.925 -29.321  14.385  1.00 46.05           C
ANISOU  344  CG  LEU B  46     5180   6741   5574   -550    351    -66       C
ATOM    345  CD1 LEU B  46      32.656 -30.080  14.030  1.00 47.20           C
ANISOU  345  CD1 LEU B  46     5278   6821   5832   -700    410    -70       C
ATOM    346  CD2 LEU B  46      33.629 -28.222  15.393  1.00 45.72           C
ANISOU  346  CD2 LEU B  46     5118   6853   5401   -516    390    -24       C
ATOM    347  N   LYS B  47      34.653 -31.799  11.875  1.00 47.40           N
ANISOU  347  N   LYS B  47     5426   6556   6026   -558    221   -255       N
ATOM    348  CA  LYS B  47      34.444 -31.394  10.494  1.00 46.69           C
ANISOU  348  CA  LYS B  47     5248   6539   5953   -552    178   -413       C
ATOM    349  C   LYS B  47      33.344 -30.323  10.464  1.00 45.95           C
ANISOU  349  C   LYS B  47     5036   6604   5819   -629    216   -430       C
ATOM    350  O   LYS B  47      32.161 -30.607  10.687  1.00 46.85           O
ANISOU  350  O   LYS B  47     5103   6701   5995   -756    259   -415       O
ATOM    351  CB  LYS B  47      34.078 -32.590   9.624  1.00 48.12           C
ANISOU  351  CB  LYS B  47     5466   6557   6261   -603    132   -515       C
ATOM    352  CG  LYS B  47      34.182 -32.301   8.137  1.00 47.67           C
ANISOU  352  CG  LYS B  47     5352   6579   6183   -542     69   -689       C
ATOM    353  CD  LYS B  47      34.216 -33.578   7.320  1.00 49.31           C
ANISOU  353  CD  LYS B  47     5634   6609   6494   -534     -1   -814       C
ATOM    354  CE  LYS B  47      32.903 -34.325   7.399  1.00 50.88           C
ANISOU  354  CE  LYS B  47     5823   6673   6837   -720    -12   -833       C
ATOM    355  NZ  LYS B  47      32.915 -35.509   6.500  1.00 52.69           N
ANISOU  355  NZ  LYS B  47     6131   6713   7177   -713   -110   -991       N
ATOM    356  N   SER B  48      33.757 -29.089  10.201  1.00 44.53           N
ANISOU  356  N   SER B  48     4803   6574   5543   -550    200   -457       N
ATOM    357  CA  SER B  48      32.903 -27.924  10.366  1.00 43.88           C
ANISOU  357  CA  SER B  48     4632   6634   5407   -579    226   -460       C
ATOM    358  C   SER B  48      32.031 -27.654   9.168  1.00 43.90           C
ANISOU  358  C   SER B  48     4544   6699   5438   -612    191   -576       C
ATOM    359  O   SER B  48      31.039 -26.940   9.277  1.00 43.86           O
ANISOU  359  O   SER B  48     4453   6793   5417   -646    210   -588       O
ATOM    360  CB  SER B  48      33.762 -26.688  10.571  1.00 42.67           C
ANISOU  360  CB  SER B  48     4477   6578   5156   -481    203   -438       C
ATOM    361  OG  SER B  48      34.408 -26.343   9.359  1.00 42.10           O
ANISOU  361  OG  SER B  48     4383   6542   5072   -422    153   -509       O
ATOM    362  N   GLY B  49      32.416 -28.192   8.016  1.00 44.14           N
ANISOU  362  N   GLY B  49     4592   6685   5493   -581    134   -671       N
ATOM    363  CA  GLY B  49      31.845 -27.754   6.757  1.00 44.14           C
ANISOU  363  CA  GLY B  49     4523   6775   5472   -568     79   -786       C
ATOM    364  C   GLY B  49      32.455 -26.429   6.338  1.00 42.96           C
ANISOU  364  C   GLY B  49     4359   6752   5210   -468     67   -767       C
ATOM    365  O   GLY B  49      33.161 -25.773   7.111  1.00 42.17           O
ANISOU  365  O   GLY B  49     4284   6670   5070   -432     96   -677       O
ATOM    366  N   ILE B  50      32.145 -26.029   5.111  1.00 43.08           N
ANISOU  366  N   ILE B  50     4338   6852   5177   -429     16   -851       N
ATOM    367  CA  ILE B  50      32.752 -24.867   4.483  1.00 42.38           C
ANISOU  367  CA  ILE B  50     4250   6868   4985   -341      5   -820       C
ATOM    368  C   ILE B  50      31.959 -23.589   4.783  1.00 41.96           C
ANISOU  368  C   ILE B  50     4147   6892   4904   -342     -4   -782       C
ATOM    369  O   ILE B  50      30.729 -23.615   4.838  1.00 42.47           O
ANISOU  369  O   ILE B  50     4147   6985   5003   -383    -24   -833       O
ATOM    370  CB  ILE B  50      32.860 -25.109   2.961  1.00 43.09           C
ANISOU  370  CB  ILE B  50     4348   7020   5007   -275    -42   -917       C
ATOM    371  CG1 ILE B  50      33.762 -26.320   2.706  1.00 43.70           C
ANISOU  371  CG1 ILE B  50     4482   7018   5104   -240    -32   -969       C
ATOM    372  CG2 ILE B  50      33.387 -23.876   2.239  1.00 42.75           C
ANISOU  372  CG2 ILE B  50     4306   7090   4847   -196    -40   -855       C
ATOM    373  CD1 ILE B  50      34.000 -26.633   1.243  1.00 44.68           C
ANISOU  373  CD1 ILE B  50     4628   7216   5134   -146    -71  -1080       C
ATOM    374  N   GLY B  51      32.666 -22.478   4.986  1.00 41.27           N
ANISOU  374  N   GLY B  51     4083   6831   4766   -296      5   -699       N
ATOM    375  CA  GLY B  51      32.038 -21.153   5.118  1.00 41.09           C
ANISOU  375  CA  GLY B  51     4039   6860   4715   -268    -22   -671       C
ATOM    376  C   GLY B  51      31.943 -20.638   6.538  1.00 40.71           C
ANISOU  376  C   GLY B  51     3997   6777   4693   -283      3   -624       C
ATOM    377  O   GLY B  51      32.118 -21.389   7.497  1.00 40.67           O
ANISOU  377  O   GLY B  51     4005   6724   4724   -326     47   -607       O
ATOM    378  N   LYS B  52      31.654 -19.347   6.664  1.00 40.68           N
ANISOU  378  N   LYS B  52     3998   6795   4663   -234    -31   -603       N
ATOM    379  CA  LYS B  52      31.636 -18.662   7.964  1.00 40.55           C
ANISOU  379  CA  LYS B  52     4006   6751   4651   -219    -24   -579       C
ATOM    380  C   LYS B  52      30.572 -19.182   8.910  1.00 40.98           C
ANISOU  380  C   LYS B  52     4008   6844   4719   -238     28   -618       C
ATOM    381  O   LYS B  52      30.843 -19.427  10.080  1.00 40.98           O
ANISOU  381  O   LYS B  52     4039   6822   4710   -252     70   -589       O
ATOM    382  CB  LYS B  52      31.400 -17.163   7.789  1.00 40.79           C
ANISOU  382  CB  LYS B  52     4061   6776   4660   -146    -88   -572       C
ATOM    383  CG  LYS B  52      32.524 -16.384   7.141  1.00 40.70           C
ANISOU  383  CG  LYS B  52     4109   6708   4645   -145   -129   -497       C
ATOM    384  CD  LYS B  52      32.179 -14.906   7.191  1.00 41.25           C
ANISOU  384  CD  LYS B  52     4226   6731   4715    -79   -201   -485       C
ATOM    385  CE  LYS B  52      33.127 -14.052   6.368  1.00 41.59           C
ANISOU  385  CE  LYS B  52     4325   6710   4767    -96   -239   -385       C
ATOM    386  NZ  LYS B  52      32.820 -12.605   6.541  1.00 42.39           N
ANISOU  386  NZ  LYS B  52     4496   6718   4893    -36   -323   -370       N
ATOM    387  N   VAL B  53      29.353 -19.314   8.406  1.00 41.59           N
ANISOU  387  N   VAL B  53     3998   6993   4812   -237     24   -677       N
ATOM    388  CA  VAL B  53      28.234 -19.748   9.232  1.00 42.38           C
ANISOU  388  CA  VAL B  53     4010   7156   4935   -267     89   -705       C
ATOM    389  C   VAL B  53      28.437 -21.190   9.705  1.00 42.57           C
ANISOU  389  C   VAL B  53     4038   7131   5005   -378    163   -670       C
ATOM    390  O   VAL B  53      28.224 -21.488  10.879  1.00 43.03           O
ANISOU  390  O   VAL B  53     4095   7201   5052   -403    242   -626       O
ATOM    391  CB  VAL B  53      26.887 -19.580   8.490  1.00 43.27           C
ANISOU  391  CB  VAL B  53     3997   7371   5075   -246     55   -784       C
ATOM    392  CG1 VAL B  53      25.746 -20.238   9.254  1.00 44.41           C
ANISOU  392  CG1 VAL B  53     4012   7596   5268   -312    141   -803       C
ATOM    393  CG2 VAL B  53      26.592 -18.102   8.276  1.00 43.40           C
ANISOU  393  CG2 VAL B  53     4024   7422   5043   -110    -16   -806       C
ATOM    394  N   ASN B  54      28.855 -22.077   8.801  1.00 42.47           N
ANISOU  394  N   ASN B  54     4041   7060   5035   -431    135   -687       N
ATOM    395  CA  ASN B  54      29.168 -23.458   9.168  1.00 42.85           C
ANISOU  395  CA  ASN B  54     4120   7019   5140   -523    185   -654       C
ATOM    396  C   ASN B  54      30.228 -23.521  10.245  1.00 42.36           C
ANISOU  396  C   ASN B  54     4162   6896   5038   -500    222   -563       C
ATOM    397  O   ASN B  54      30.047 -24.179  11.261  1.00 43.02           O
ANISOU  397  O   ASN B  54     4264   6952   5131   -550    292   -500       O
ATOM    398  CB  ASN B  54      29.634 -24.260   7.956  1.00 42.90           C
ANISOU  398  CB  ASN B  54     4153   6962   5184   -541    129   -711       C
ATOM    399  CG  ASN B  54      28.482 -24.812   7.147  1.00 43.99           C
ANISOU  399  CG  ASN B  54     4193   7131   5392   -606     91   -810       C
ATOM    400  OD1 ASN B  54      27.381 -25.015   7.666  1.00 44.94           O
ANISOU  400  OD1 ASN B  54     4213   7289   5572   -683    130   -813       O
ATOM    401  ND2 ASN B  54      28.727 -25.075   5.877  1.00 44.14           N
ANISOU  401  ND2 ASN B  54     4228   7144   5398   -576     13   -895       N
ATOM    402  N   ALA B  55      31.326 -22.812  10.034  1.00 41.47           N
ANISOU  402  N   ALA B  55     4111   6768   4877   -427    172   -549       N
ATOM    403  CA  ALA B  55      32.399 -22.778  11.013  1.00 41.19           C
ANISOU  403  CA  ALA B  55     4157   6688   4804   -397    178   -480       C
ATOM    404  C   ALA B  55      31.948 -22.168  12.346  1.00 41.52           C
ANISOU  404  C   ALA B  55     4212   6781   4783   -368    213   -451       C
ATOM    405  O   ALA B  55      32.277 -22.687  13.406  1.00 41.95           O
ANISOU  405  O   ALA B  55     4324   6811   4803   -369    250   -389       O
ATOM    406  CB  ALA B  55      33.585 -22.014  10.456  1.00 40.47           C
ANISOU  406  CB  ALA B  55     4094   6588   4695   -342    113   -476       C
ATOM    407  N   ALA B  56      31.197 -21.074  12.289  1.00 41.56           N
ANISOU  407  N   ALA B  56     4172   6860   4761   -322    197   -500       N
ATOM    408  CA  ALA B  56      30.747 -20.403  13.503  1.00 42.13           C
ANISOU  408  CA  ALA B  56     4258   6993   4755   -263    226   -501       C
ATOM    409  C   ALA B  56      29.810 -21.298  14.317  1.00 43.23           C
ANISOU  409  C   ALA B  56     4354   7191   4880   -315    344   -459       C
ATOM    410  O   ALA B  56      29.985 -21.440  15.527  1.00 43.86           O
ANISOU  410  O   ALA B  56     4494   7294   4876   -288    394   -405       O
ATOM    411  CB  ALA B  56      30.067 -19.087  13.169  1.00 42.21           C
ANISOU  411  CB  ALA B  56     4228   7058   4750   -184    179   -575       C
ATOM    412  N   MET B  57      28.836 -21.901  13.640  1.00 43.72           N
ANISOU  412  N   MET B  57     4309   7280   5021   -394    386   -479       N
ATOM    413  CA  MET B  57      27.889 -22.812  14.269  1.00 45.11           C
ANISOU  413  CA  MET B  57     4416   7505   5219   -483    506   -425       C
ATOM    414  C   MET B  57      28.617 -23.988  14.899  1.00 45.46           C
ANISOU  414  C   MET B  57     4564   7443   5266   -549    550   -313       C
ATOM    415  O   MET B  57      28.446 -24.283  16.086  1.00 46.52           O
ANISOU  415  O   MET B  57     4733   7617   5325   -551    645   -222       O
ATOM    416  CB  MET B  57      26.876 -23.333  13.228  1.00 45.69           C
ANISOU  416  CB  MET B  57     4348   7596   5415   -581    504   -481       C
ATOM    417  CG  MET B  57      25.816 -24.270  13.801  1.00 47.49           C
ANISOU  417  CG  MET B  57     4471   7870   5704   -709    630   -420       C
ATOM    418  SD  MET B  57      24.845 -25.158  12.564  1.00 48.49           S
ANISOU  418  SD  MET B  57     4441   7970   6012   -863    592   -496       S
ATOM    419  CE  MET B  57      26.033 -26.375  12.008  1.00 47.93           C
ANISOU  419  CE  MET B  57     4530   7668   6012   -932    525   -471       C
ATOM    420  N   SER B  58      29.418 -24.662  14.078  1.00 44.78           N
ANISOU  420  N   SER B  58     4531   7228   5257   -586    482   -320       N
ATOM    421  CA  SER B  58      30.147 -25.852  14.493  1.00 45.27           C
ANISOU  421  CA  SER B  58     4696   7160   5343   -630    501   -226       C
ATOM    422  C   SER B  58      31.134 -25.557  15.639  1.00 45.13           C
ANISOU  422  C   SER B  58     4799   7146   5201   -532    492   -152       C
ATOM    423  O   SER B  58      31.224 -26.327  16.588  1.00 46.23           O
ANISOU  423  O   SER B  58     5014   7249   5303   -552    555    -37       O
ATOM    424  CB  SER B  58      30.827 -26.507  13.278  1.00 44.71           C
ANISOU  424  CB  SER B  58     4650   6966   5370   -650    417   -283       C
ATOM    425  OG  SER B  58      32.244 -26.473  13.380  1.00 43.96           O
ANISOU  425  OG  SER B  58     4656   6814   5234   -560    356   -261       O
ATOM    426  N   THR B  59      31.842 -24.434  15.563  1.00 44.03           N
ANISOU  426  N   THR B  59     4680   7050   5002   -430    408   -213       N
ATOM    427  CA  THR B  59      32.743 -24.019  16.642  1.00 44.09           C
ANISOU  427  CA  THR B  59     4785   7074   4895   -336    370   -174       C
ATOM    428  C   THR B  59      31.967 -23.756  17.929  1.00 45.31           C
ANISOU  428  C   THR B  59     4957   7339   4920   -302    458   -130       C
ATOM    429  O   THR B  59      32.445 -24.063  19.017  1.00 46.15           O
ANISOU  429  O   THR B  59     5163   7452   4919   -252    469    -51       O
ATOM    430  CB  THR B  59      33.552 -22.742  16.286  1.00 43.03           C
ANISOU  430  CB  THR B  59     4649   6954   4745   -259    253   -260       C
ATOM    431  OG1 THR B  59      34.249 -22.921  15.049  1.00 42.14           O
ANISOU  431  OG1 THR B  59     4507   6773   4733   -285    195   -289       O
ATOM    432  CG2 THR B  59      34.569 -22.410  17.375  1.00 43.35           C
ANISOU  432  CG2 THR B  59     4783   7001   4688   -173    183   -237       C
ATOM    433  N   THR B  60      30.780 -23.174  17.808  1.00 45.61           N
ANISOU  433  N   THR B  60     4896   7481   4954   -311    520   -185       N
ATOM    434  CA  THR B  60      29.949 -22.879  18.974  1.00 47.03           C
ANISOU  434  CA  THR B  60     5068   7802   5000   -261    625   -156       C
ATOM    435  C   THR B  60      29.476 -24.160  19.650  1.00 48.63           C
ANISOU  435  C   THR B  60     5283   8005   5187   -354    768     -2       C
ATOM    436  O   THR B  60      29.476 -24.263  20.879  1.00 49.97           O
ANISOU  436  O   THR B  60     5531   8253   5201   -297    840     84       O
ATOM    437  CB  THR B  60      28.726 -22.014  18.596  1.00 47.24           C
ANISOU  437  CB  THR B  60     4956   7950   5044   -237    662   -256       C
ATOM    438  OG1 THR B  60      29.170 -20.785  18.014  1.00 46.04           O
ANISOU  438  OG1 THR B  60     4818   7772   4904   -147    526   -378       O
ATOM    439  CG2 THR B  60      27.880 -21.698  19.822  1.00 48.99           C
ANISOU  439  CG2 THR B  60     5157   8345   5111   -161    787   -236       C
ATOM    440  N   ILE B  61      29.058 -25.127  18.842  1.00 48.76           N
ANISOU  440  N   ILE B  61     5231   7931   5363   -499    803     34       N
ATOM    441  CA  ILE B  61      28.625 -26.420  19.368  1.00 50.54           C
ANISOU  441  CA  ILE B  61     5474   8109   5619   -621    929    193       C
ATOM    442  C   ILE B  61      29.774 -27.079  20.126  1.00 50.87           C
ANISOU  442  C   ILE B  61     5704   8045   5581   -570    896    313       C
ATOM    443  O   ILE B  61      29.580 -27.596  21.228  1.00 52.65           O
ANISOU  443  O   ILE B  61     6002   8307   5697   -574   1005    466       O
ATOM    444  CB  ILE B  61      28.134 -27.361  18.252  1.00 50.70           C
ANISOU  444  CB  ILE B  61     5407   8003   5855   -789    927    181       C
ATOM    445  CG1 ILE B  61      26.838 -26.827  17.639  1.00 50.95           C
ANISOU  445  CG1 ILE B  61     5234   8166   5958   -844    966     80       C
ATOM    446  CG2 ILE B  61      27.889 -28.755  18.809  1.00 52.74           C
ANISOU  446  CG2 ILE B  61     5719   8150   6170   -926   1033    361       C
ATOM    447  CD1 ILE B  61      26.392 -27.549  16.384  1.00 51.03           C
ANISOU  447  CD1 ILE B  61     5148   8067   6173   -987    914     14       C
ATOM    448  N   LEU B  62      30.962 -27.053  19.523  1.00 49.40           N
ANISOU  448  N   LEU B  62     5587   7740   5443   -513    748    250       N
ATOM    449  CA  LEU B  62      32.175 -27.570  20.151  1.00 49.67           C
ANISOU  449  CA  LEU B  62     5779   7685   5409   -433    682    337       C
ATOM    450  C   LEU B  62      32.385 -26.965  21.534  1.00 50.54           C
ANISOU  450  C   LEU B  62     5975   7932   5294   -305    697    384       C
ATOM    451  O   LEU B  62      32.492 -27.677  22.526  1.00 52.21           O
ANISOU  451  O   LEU B  62     6301   8136   5400   -286    757    539       O
ATOM    452  CB  LEU B  62      33.389 -27.263  19.270  1.00 47.96           C
ANISOU  452  CB  LEU B  62     5570   7388   5264   -367    522    225       C
ATOM    453  CG  LEU B  62      34.780 -27.537  19.857  1.00 48.16           C
ANISOU  453  CG  LEU B  62     5719   7356   5222   -252    419    275       C
ATOM    454  CD1 LEU B  62      35.040 -29.029  19.940  1.00 49.41           C
ANISOU  454  CD1 LEU B  62     5975   7350   5449   -287    442    405       C
ATOM    455  CD2 LEU B  62      35.848 -26.847  19.029  1.00 46.57           C
ANISOU  455  CD2 LEU B  62     5468   7146   5080   -191    281    148       C
ATOM    456  N   LEU B  63      32.420 -25.640  21.584  1.00 49.64           N
ANISOU  456  N   LEU B  63     5819   7939   5105   -212    636    247       N
ATOM    457  CA  LEU B  63      32.685 -24.922  22.822  1.00 50.51           C
ANISOU  457  CA  LEU B  63     6016   8178   4997    -69    613    241       C
ATOM    458  C   LEU B  63      31.590 -25.101  23.876  1.00 52.59           C
ANISOU  458  C   LEU B  63     6288   8593   5101    -64    794    344       C
ATOM    459  O   LEU B  63      31.874 -25.076  25.078  1.00 54.04           O
ANISOU  459  O   LEU B  63     6593   8866   5075     48    805    411       O
ATOM    460  CB  LEU B  63      32.912 -23.430  22.532  1.00 49.28           C
ANISOU  460  CB  LEU B  63     5814   8081   4829     18    494     52       C
ATOM    461  CG  LEU B  63      34.123 -23.069  21.658  1.00 47.63           C
ANISOU  461  CG  LEU B  63     5596   7754   4746     22    320    -35       C
ATOM    462  CD1 LEU B  63      34.474 -21.603  21.828  1.00 47.25           C
ANISOU  462  CD1 LEU B  63     5551   7755   4648    116    195   -184       C
ATOM    463  CD2 LEU B  63      35.338 -23.930  21.966  1.00 47.94           C
ANISOU  463  CD2 LEU B  63     5729   7705   4781     50    242     51       C
ATOM    464  N   GLU B  64      30.348 -25.276  23.440  1.00 52.97           N
ANISOU  464  N   GLU B  64     6199   8689   5239   -178    935    359       N
ATOM    465  CA  GLU B  64      29.244 -25.498  24.374  1.00 55.25           C
ANISOU  465  CA  GLU B  64     6456   9143   5394   -193   1137    473       C
ATOM    466  C   GLU B  64      29.301 -26.905  24.953  1.00 57.10           C
ANISOU  466  C   GLU B  64     6789   9294   5612   -287   1245    713       C
ATOM    467  O   GLU B  64      29.290 -27.080  26.170  1.00 59.06           O
ANISOU  467  O   GLU B  64     7146   9653   5642   -209   1334    844       O
ATOM    468  CB  GLU B  64      27.894 -25.269  23.689  1.00 55.38           C
ANISOU  468  CB  GLU B  64     6260   9245   5537   -296   1248    412       C
ATOM    469  CG  GLU B  64      27.537 -23.801  23.513  1.00 54.56           C
ANISOU  469  CG  GLU B  64     6073   9278   5380   -161   1190    208       C
ATOM    470  CD  GLU B  64      27.086 -23.135  24.802  1.00 56.44           C
ANISOU  470  CD  GLU B  64     6342   9742   5361      1   1290    200       C
ATOM    471  OE1 GLU B  64      26.282 -23.734  25.544  1.00 58.71           O
ANISOU  471  OE1 GLU B  64     6588  10166   5555    -44   1493    347       O
ATOM    472  OE2 GLU B  64      27.527 -22.003  25.078  1.00 55.91           O
ANISOU  472  OE2 GLU B  64     6343   9718   5182    173   1168     45       O
ATOM    473  N   ARG B  65      29.389 -27.898  24.073  1.00 56.63           N
ANISOU  473  N   ARG B  65     6708   9033   5777   -444   1226    769       N
ATOM    474  CA  ARG B  65      29.322 -29.308  24.470  1.00 58.62           C
ANISOU  474  CA  ARG B  65     7052   9154   6069   -563   1325   1002       C
ATOM    475  C   ARG B  65      30.638 -29.903  24.983  1.00 58.87           C
ANISOU  475  C   ARG B  65     7300   9046   6020   -458   1209   1101       C
ATOM    476  O   ARG B  65      30.625 -30.688  25.921  1.00 61.15           O
ANISOU  476  O   ARG B  65     7720   9318   6198   -462   1303   1319       O
ATOM    477  CB  ARG B  65      28.832 -30.161  23.302  1.00 58.42           C
ANISOU  477  CB  ARG B  65     6921   8944   6333   -770   1333    998       C
ATOM    478  CG  ARG B  65      27.372 -29.961  22.963  1.00 59.22           C
ANISOU  478  CG  ARG B  65     6800   9173   6527   -912   1474    966       C
ATOM    479  CD  ARG B  65      26.995 -30.788  21.751  1.00 59.07           C
ANISOU  479  CD  ARG B  65     6687   8960   6797  -1108   1435    927       C
ATOM    480  NE  ARG B  65      25.643 -30.478  21.292  1.00 59.70           N
ANISOU  480  NE  ARG B  65     6524   9178   6981  -1230   1529    856       N
ATOM    481  CZ  ARG B  65      24.579 -31.271  21.422  1.00 62.17           C
ANISOU  481  CZ  ARG B  65     6716   9487   7418  -1440   1680    985       C
ATOM    482  NH1 ARG B  65      24.677 -32.465  21.995  1.00 64.37           N
ANISOU  482  NH1 ARG B  65     7116   9603   7739  -1566   1764   1212       N
ATOM    483  NH2 ARG B  65      23.398 -30.867  20.960  1.00 62.71           N
ANISOU  483  NH2 ARG B  65     6533   9710   7582  -1528   1741    890       N
ATOM    484  N   TYR B  66      31.760 -29.551  24.361  1.00 56.79           N
ANISOU  484  N   TYR B  66     7070   8691   5816   -365   1011    955       N
ATOM    485  CA  TYR B  66      33.031 -30.215  24.655  1.00 57.07           C
ANISOU  485  CA  TYR B  66     7276   8584   5825   -269    885   1033       C
ATOM    486  C   TYR B  66      34.004 -29.416  25.519  1.00 56.92           C
ANISOU  486  C   TYR B  66     7353   8690   5585    -60    758    979       C
ATOM    487  O   TYR B  66      34.846 -30.002  26.200  1.00 58.12           O
ANISOU  487  O   TYR B  66     7659   8783   5639     41    687   1094       O
ATOM    488  CB  TYR B  66      33.692 -30.656  23.352  1.00 55.45           C
ANISOU  488  CB  TYR B  66     7034   8176   5858   -314    757    932       C
ATOM    489  CG  TYR B  66      32.897 -31.743  22.674  1.00 56.31           C
ANISOU  489  CG  TYR B  66     7106   8116   6175   -506    851   1006       C
ATOM    490  CD1 TYR B  66      33.097 -33.076  23.007  1.00 58.29           C
ANISOU  490  CD1 TYR B  66     7502   8166   6479   -549    874   1194       C
ATOM    491  CD2 TYR B  66      31.915 -31.438  21.737  1.00 55.47           C
ANISOU  491  CD2 TYR B  66     6823   8041   6212   -643    904    890       C
ATOM    492  CE1 TYR B  66      32.360 -34.089  22.415  1.00 59.46           C
ANISOU  492  CE1 TYR B  66     7624   8129   6838   -741    944   1256       C
ATOM    493  CE2 TYR B  66      31.169 -32.440  21.132  1.00 56.57           C
ANISOU  493  CE2 TYR B  66     6920   8023   6551   -830    969    941       C
ATOM    494  CZ  TYR B  66      31.394 -33.767  21.476  1.00 58.58           C
ANISOU  494  CZ  TYR B  66     7324   8060   6875   -888    988   1120       C
ATOM    495  OH  TYR B  66      30.668 -34.772  20.874  1.00 59.97           O
ANISOU  495  OH  TYR B  66     7466   8048   7273  -1088   1033   1160       O
ATOM    496  N   LYS B  67      33.884 -28.094  25.501  1.00 55.74           N
ANISOU  496  N   LYS B  67     7117   8699   5361      8    714    801       N
ATOM    497  CA  LYS B  67      34.692 -27.241  26.367  1.00 55.94           C
ANISOU  497  CA  LYS B  67     7226   8846   5181    193    583    723       C
ATOM    498  C   LYS B  67      36.208 -27.498  26.241  1.00 55.41           C
ANISOU  498  C   LYS B  67     7230   8663   5158    284    377    698       C
ATOM    499  O   LYS B  67      36.885 -27.735  27.244  1.00 56.92           O
ANISOU  499  O   LYS B  67     7561   8893   5174    417    303    777       O
ATOM    500  CB  LYS B  67      34.257 -27.434  27.826  1.00 58.59           C
ANISOU  500  CB  LYS B  67     7691   9335   5235    282    698    875       C
ATOM    501  CG  LYS B  67      32.753 -27.403  28.044  1.00 59.74           C
ANISOU  501  CG  LYS B  67     7752   9613   5333    189    936    942       C
ATOM    502  CD  LYS B  67      32.458 -27.051  29.488  1.00 62.14           C
ANISOU  502  CD  LYS B  67     8164  10145   5302    339   1021   1008       C
ATOM    503  CE  LYS B  67      30.982 -26.924  29.758  1.00 63.59           C
ANISOU  503  CE  LYS B  67     8235  10506   5419    270   1272   1064       C
ATOM    504  NZ  LYS B  67      30.529 -25.511  29.669  1.00 62.72           N
ANISOU  504  NZ  LYS B  67     8016  10563   5253    369   1244    820       N
ATOM    505  N   PRO B  68      36.745 -27.446  25.010  1.00 53.46           N
ANISOU  505  N   PRO B  68     6882   8296   5136    225    285    588       N
ATOM    506  CA  PRO B  68      38.181 -27.616  24.842  1.00 53.12           C
ANISOU  506  CA  PRO B  68     6864   8175   5144    317    101    552       C
ATOM    507  C   PRO B  68      38.953 -26.400  25.325  1.00 52.88           C
ANISOU  507  C   PRO B  68     6819   8265   5007    434    -64    406       C
ATOM    508  O   PRO B  68      38.450 -25.279  25.245  1.00 52.15           O
ANISOU  508  O   PRO B  68     6660   8263   4890    416    -57    278       O
ATOM    509  CB  PRO B  68      38.335 -27.778  23.331  1.00 51.30           C
ANISOU  509  CB  PRO B  68     6506   7821   5164    214     88    466       C
ATOM    510  CG  PRO B  68      37.219 -26.980  22.768  1.00 50.20           C
ANISOU  510  CG  PRO B  68     6255   7749   5069    109    186    375       C
ATOM    511  CD  PRO B  68      36.075 -27.156  23.728  1.00 51.74           C
ANISOU  511  CD  PRO B  68     6511   8035   5115     89    341    486       C
ATOM    512  N   GLU B  69      40.160 -26.630  25.828  1.00 53.73           N
ANISOU  512  N   GLU B  69     6988   8365   5062    557   -224    419       N
ATOM    513  CA  GLU B  69      40.989 -25.567  26.387  1.00 53.99           C
ANISOU  513  CA  GLU B  69     7009   8503   5002    663   -411    279       C
ATOM    514  C   GLU B  69      41.625 -24.726  25.300  1.00 52.20           C
ANISOU  514  C   GLU B  69     6614   8239   4981    595   -515    116       C
ATOM    515  O   GLU B  69      41.876 -23.541  25.502  1.00 52.10           O
ANISOU  515  O   GLU B  69     6560   8293   4943    614   -628    -28       O
ATOM    516  CB  GLU B  69      42.097 -26.152  27.248  1.00 55.76           C
ANISOU  516  CB  GLU B  69     7333   8740   5114    818   -564    348       C
ATOM    517  CG  GLU B  69      41.631 -26.947  28.430  1.00 57.97           C
ANISOU  517  CG  GLU B  69     7805   9065   5157    909   -482    532       C
ATOM    518  CD  GLU B  69      42.807 -27.529  29.171  1.00 59.79           C
ANISOU  518  CD  GLU B  69     8132   9298   5286   1080   -661    599       C
ATOM    519  OE1 GLU B  69      43.910 -26.938  29.110  1.00 59.63           O
ANISOU  519  OE1 GLU B  69     8024   9316   5318   1148   -873    453       O
ATOM    520  OE2 GLU B  69      42.624 -28.571  29.807  1.00 61.59           O
ANISOU  520  OE2 GLU B  69     8519   9490   5392   1143   -592    802       O
ATOM    521  N   LYS B  70      41.938 -25.360  24.174  1.00 51.13           N
ANISOU  521  N   LYS B  70     6391   7993   5044    523   -483    142       N
ATOM    522  CA  LYS B  70      42.549 -24.686  23.028  1.00 49.66           C
ANISOU  522  CA  LYS B  70     6040   7781   5048    453   -549     21       C
ATOM    523  C   LYS B  70      41.947 -25.216  21.735  1.00 48.32           C
ANISOU  523  C   LYS B  70     5804   7520   5035    339   -408     45       C
ATOM    524  O   LYS B  70      41.374 -26.305  21.704  1.00 48.70           O
ANISOU  524  O   LYS B  70     5925   7496   5084    321   -298    152       O
ATOM    525  CB  LYS B  70      44.072 -24.890  23.024  1.00 50.33           C
ANISOU  525  CB  LYS B  70     6060   7867   5198    535   -717      0       C
ATOM    526  CG  LYS B  70      44.807 -24.146  24.137  1.00 51.70           C
ANISOU  526  CG  LYS B  70     6257   8138   5250    634   -906    -72       C
ATOM    527  CD  LYS B  70      46.214 -24.684  24.362  1.00 52.96           C
ANISOU  527  CD  LYS B  70     6366   8312   5444    745  -1069    -59       C
ATOM    528  CE  LYS B  70      46.879 -24.179  25.671  1.00 54.86           C
ANISOU  528  CE  LYS B  70     6662   8658   5526    870  -1277   -119       C
ATOM    529  NZ  LYS B  70      46.599 -22.777  26.141  1.00 54.97           N
ANISOU  529  NZ  LYS B  70     6678   8734   5474    830  -1362   -265       N
ATOM    530  N   VAL B  71      42.073 -24.430  20.675  1.00 46.99           N
ANISOU  530  N   VAL B  71     5505   7352   4998    260   -418    -52       N
ATOM    531  CA  VAL B  71      41.462 -24.748  19.394  1.00 45.80           C
ANISOU  531  CA  VAL B  71     5291   7141   4972    163   -301    -56       C
ATOM    532  C   VAL B  71      42.453 -24.491  18.268  1.00 45.16           C
ANISOU  532  C   VAL B  71     5074   7055   5031    145   -356   -115       C
ATOM    533  O   VAL B  71      43.077 -23.438  18.208  1.00 45.04           O
ANISOU  533  O   VAL B  71     4978   7091   5044    132   -446   -180       O
ATOM    534  CB  VAL B  71      40.215 -23.872  19.151  1.00 44.99           C
ANISOU  534  CB  VAL B  71     5170   7074   4851     82   -220   -107       C
ATOM    535  CG1 VAL B  71      39.668 -24.087  17.740  1.00 43.90           C
ANISOU  535  CG1 VAL B  71     4954   6890   4838     -9   -133   -129       C
ATOM    536  CG2 VAL B  71      39.148 -24.147  20.208  1.00 45.88           C
ANISOU  536  CG2 VAL B  71     5388   7222   4822     97   -132    -44       C
ATOM    537  N   ILE B  72      42.588 -25.460  17.375  1.00 45.01           N
ANISOU  537  N   ILE B  72     5029   6973   5098    143   -298    -94       N
ATOM    538  CA  ILE B  72      43.422 -25.292  16.202  1.00 44.58           C
ANISOU  538  CA  ILE B  72     4843   6942   5156    136   -314   -145       C
ATOM    539  C   ILE B  72      42.565 -25.472  14.964  1.00 43.69           C
ANISOU  539  C   ILE B  72     4708   6796   5097     61   -204   -173       C
ATOM    540  O   ILE B  72      41.767 -26.400  14.884  1.00 43.83           O
ANISOU  540  O   ILE B  72     4804   6735   5115     46   -135   -149       O
ATOM    541  CB  ILE B  72      44.552 -26.324  16.148  1.00 45.61           C
ANISOU  541  CB  ILE B  72     4952   7049   5330    249   -362   -122       C
ATOM    542  CG1 ILE B  72      45.480 -26.162  17.354  1.00 46.77           C
ANISOU  542  CG1 ILE B  72     5106   7244   5421    341   -497   -101       C
ATOM    543  CG2 ILE B  72      45.337 -26.162  14.854  1.00 45.41           C
ANISOU  543  CG2 ILE B  72     4772   7078   5405    248   -345   -177       C
ATOM    544  CD1 ILE B  72      46.358 -27.367  17.616  1.00 48.14           C
ANISOU  544  CD1 ILE B  72     5305   7378   5609    486   -552    -57       C
ATOM    545  N   ASN B  73      42.744 -24.583  13.999  1.00 43.02           N
ANISOU  545  N   ASN B  73     4517   6770   5059      9   -196   -221       N
ATOM    546  CA  ASN B  73      42.027 -24.667  12.748  1.00 42.37           C
ANISOU  546  CA  ASN B  73     4410   6680   5007    -43   -112   -256       C
ATOM    547  C   ASN B  73      42.994 -25.080  11.641  1.00 42.74           C
ANISOU  547  C   ASN B  73     4367   6764   5108      7    -97   -280       C
ATOM    548  O   ASN B  73      44.029 -24.450  11.448  1.00 43.03           O
ANISOU  548  O   ASN B  73     4297   6879   5174     17   -131   -274       O
ATOM    549  CB  ASN B  73      41.373 -23.318  12.426  1.00 41.60           C
ANISOU  549  CB  ASN B  73     4281   6628   4897   -122   -106   -278       C
ATOM    550  CG  ASN B  73      40.437 -23.380  11.225  1.00 41.08           C
ANISOU  550  CG  ASN B  73     4204   6565   4839   -165    -34   -313       C
ATOM    551  OD1 ASN B  73      40.349 -22.436  10.437  1.00 40.75           O
ANISOU  551  OD1 ASN B  73     4111   6569   4801   -199    -30   -323       O
ATOM    552  ND2 ASN B  73      39.751 -24.496  11.075  1.00 41.26           N
ANISOU  552  ND2 ASN B  73     4278   6531   4867   -163     12   -329       N
ATOM    553  N   THR B  74      42.622 -26.126  10.908  1.00 42.94           N
ANISOU  553  N   THR B  74     4429   6736   5149     36    -44   -315       N
ATOM    554  CA  THR B  74      43.477 -26.713   9.889  1.00 43.62           C
ANISOU  554  CA  THR B  74     4450   6859   5264    120    -23   -359       C
ATOM    555  C   THR B  74      42.797 -26.728   8.514  1.00 43.35           C
ANISOU  555  C   THR B  74     4406   6852   5211     93     42   -425       C
ATOM    556  O   THR B  74      41.668 -26.271   8.366  1.00 42.62           O
ANISOU  556  O   THR B  74     4350   6748   5098      6     58   -433       O
ATOM    557  CB  THR B  74      43.917 -28.134  10.302  1.00 44.72           C
ANISOU  557  CB  THR B  74     4661   6896   5434    232    -50   -364       C
ATOM    558  OG1 THR B  74      44.764 -28.696   9.295  1.00 45.59           O
ANISOU  558  OG1 THR B  74     4703   7054   5565    343    -28   -428       O
ATOM    559  CG2 THR B  74      42.714 -29.060  10.540  1.00 44.82           C
ANISOU  559  CG2 THR B  74     4817   6754   5458    188    -30   -367       C
ATOM    560  N   GLY B  75      43.508 -27.219   7.506  1.00 44.14           N
ANISOU  560  N   GLY B  75     4453   7009   5309    184     73   -478       N
ATOM    561  CA  GLY B  75      42.954 -27.344   6.160  1.00 44.27           C
ANISOU  561  CA  GLY B  75     4474   7067   5281    190    122   -557       C
ATOM    562  C   GLY B  75      43.744 -26.599   5.103  1.00 44.65           C
ANISOU  562  C   GLY B  75     4401   7291   5275    223    180   -545       C
ATOM    563  O   GLY B  75      44.878 -26.176   5.329  1.00 45.11           O
ANISOU  563  O   GLY B  75     4349   7435   5355    247    189   -485       O
ATOM    564  N   SER B  76      43.121 -26.447   3.941  1.00 44.75           N
ANISOU  564  N   SER B  76     4429   7362   5212    220    219   -596       N
ATOM    565  CA  SER B  76      43.721 -25.754   2.812  1.00 45.41           C
ANISOU  565  CA  SER B  76     4418   7623   5213    251    293   -566       C
ATOM    566  C   SER B  76      43.488 -24.242   2.904  1.00 44.66           C
ANISOU  566  C   SER B  76     4285   7573   5111    124    298   -447       C
ATOM    567  O   SER B  76      42.672 -23.774   3.699  1.00 43.59           O
ANISOU  567  O   SER B  76     4207   7338   5018     33    240   -424       O
ATOM    568  CB  SER B  76      43.163 -26.321   1.494  1.00 46.20           C
ANISOU  568  CB  SER B  76     4574   7773   5207    331    319   -682       C
ATOM    569  OG  SER B  76      41.743 -26.436   1.521  1.00 45.47           O
ANISOU  569  OG  SER B  76     4583   7576   5117    260    258   -741       O
ATOM    570  N   ALA B  77      44.222 -23.489   2.090  1.00 45.49           N
ANISOU  570  N   ALA B  77     4294   7826   5165    125    372   -369       N
ATOM    571  CA  ALA B  77      44.046 -22.042   1.978  1.00 45.24           C
ANISOU  571  CA  ALA B  77     4239   7818   5130      8    378   -245       C
ATOM    572  C   ALA B  77      44.673 -21.536   0.692  1.00 46.66           C
ANISOU  572  C   ALA B  77     4341   8174   5212     32    488   -164       C
ATOM    573  O   ALA B  77      45.523 -22.200   0.109  1.00 47.90           O
ANISOU  573  O   ALA B  77     4420   8459   5321    135    567   -193       O
ATOM    574  CB  ALA B  77      44.654 -21.336   3.169  1.00 44.92           C
ANISOU  574  CB  ALA B  77     4138   7713   5214    -87    324   -166       C
ATOM    575  N   GLY B  78      44.242 -20.361   0.249  1.00 46.72           N
ANISOU  575  N   GLY B  78     4376   8192   5183    -51    496    -56       N
ATOM    576  CA  GLY B  78      44.737 -19.769  -0.987  1.00 48.32           C
ANISOU  576  CA  GLY B  78     4526   8559   5276    -41    610     61       C
ATOM    577  C   GLY B  78      45.879 -18.820  -0.720  1.00 49.32           C
ANISOU  577  C   GLY B  78     4513   8720   5506   -160    659    227       C
ATOM    578  O   GLY B  78      45.745 -17.878   0.056  1.00 48.75           O
ANISOU  578  O   GLY B  78     4456   8513   5555   -290    580    298       O
ATOM    579  N   GLY B  79      47.003 -19.056  -1.378  1.00 51.05           N
ANISOU  579  N   GLY B  79     4590   9124   5683   -116    788    283       N
ATOM    580  CA  GLY B  79      48.175 -18.221  -1.188  1.00 52.43           C
ANISOU  580  CA  GLY B  79     4593   9354   5975   -245    846    445       C
ATOM    581  C   GLY B  79      47.954 -16.798  -1.663  1.00 53.26           C
ANISOU  581  C   GLY B  79     4734   9422   6079   -391    871    641       C
ATOM    582  O   GLY B  79      47.423 -16.569  -2.753  1.00 53.94           O
ANISOU  582  O   GLY B  79     4910   9588   5998   -342    942    703       O
ATOM    583  N   PHE B  80      48.372 -15.844  -0.835  1.00 53.44           N
ANISOU  583  N   PHE B  80     4697   9316   6291   -565    799    736       N
ATOM    584  CA  PHE B  80      48.217 -14.429  -1.136  1.00 54.45           C
ANISOU  584  CA  PHE B  80     4871   9351   6464   -721    798    927       C
ATOM    585  C   PHE B  80      49.545 -13.671  -1.250  1.00 56.89           C
ANISOU  585  C   PHE B  80     4976   9729   6911   -892    886   1118       C
ATOM    586  O   PHE B  80      49.676 -12.809  -2.104  1.00 58.72           O
ANISOU  586  O   PHE B  80     5210   9994   7106   -984    984   1323       O
ATOM    587  CB  PHE B  80      47.342 -13.774  -0.073  1.00 52.83           C
ANISOU  587  CB  PHE B  80     4812   8884   6377   -790    610    865       C
ATOM    588  CG  PHE B  80      46.492 -12.663  -0.605  1.00 53.24           C
ANISOU  588  CG  PHE B  80     5022   8820   6388   -839    584    987       C
ATOM    589  CD1 PHE B  80      45.249 -12.933  -1.166  1.00 52.25           C
ANISOU  589  CD1 PHE B  80     5060   8700   6092   -704    566    920       C
ATOM    590  CD2 PHE B  80      46.937 -11.354  -0.560  1.00 54.90           C
ANISOU  590  CD2 PHE B  80     5216   8907   6738  -1019    564   1169       C
ATOM    591  CE1 PHE B  80      44.453 -11.912  -1.658  1.00 52.81           C
ANISOU  591  CE1 PHE B  80     5276   8668   6120   -722    527   1031       C
ATOM    592  CE2 PHE B  80      46.151 -10.327  -1.051  1.00 55.53           C
ANISOU  592  CE2 PHE B  80     5460   8856   6783  -1045    529   1289       C
ATOM    593  CZ  PHE B  80      44.907 -10.604  -1.605  1.00 54.45           C
ANISOU  593  CZ  PHE B  80     5487   8740   6461   -885    510   1221       C
ATOM    594  N   HIS B  81      50.509 -13.986  -0.383  1.00 57.11           N
ANISOU  594  N   HIS B  81     4825   9775   7099   -939    844   1057       N
ATOM    595  CA  HIS B  81      51.827 -13.349  -0.400  1.00 59.65           C
ANISOU  595  CA  HIS B  81     4906  10175   7584  -1114    912   1218       C
ATOM    596  C   HIS B  81      52.703 -13.979  -1.481  1.00 61.65           C
ANISOU  596  C   HIS B  81     4969  10744   7712  -1026   1141   1292       C
ATOM    597  O   HIS B  81      52.727 -15.200  -1.635  1.00 60.94           O
ANISOU  597  O   HIS B  81     4862  10797   7496   -819   1184   1136       O
ATOM    598  CB  HIS B  81      52.501 -13.475   0.973  1.00 59.30           C
ANISOU  598  CB  HIS B  81     4733  10047   7753  -1178    755   1102       C
ATOM    599  CG  HIS B  81      53.666 -12.553   1.162  1.00 61.92           C
ANISOU  599  CG  HIS B  81     4837  10384   8308  -1411    758   1254       C
ATOM    600  ND1 HIS B  81      54.970 -12.953   0.970  1.00 64.03           N
ANISOU  600  ND1 HIS B  81     4802  10886   8643  -1426    868   1296       N
ATOM    601  CD2 HIS B  81      53.721 -11.247   1.514  1.00 63.05           C
ANISOU  601  CD2 HIS B  81     5000  10320   8635  -1641    658   1368       C
ATOM    602  CE1 HIS B  81      55.780 -11.935   1.198  1.00 66.36           C
ANISOU  602  CE1 HIS B  81     4923  11128   9163  -1676    839   1437       C
ATOM    603  NE2 HIS B  81      55.047 -10.886   1.525  1.00 65.82           N
ANISOU  603  NE2 HIS B  81     5058  10778   9173  -1815    706   1483       N
ATOM    604  N   HIS B  82      53.446 -13.138  -2.200  1.00 64.47           N
ANISOU  604  N   HIS B  82     5181  11204   8110  -1185   1287   1532       N
ATOM    605  CA  HIS B  82      54.139 -13.548  -3.429  1.00 66.83           C
ANISOU  605  CA  HIS B  82     5323  11829   8242  -1099   1543   1643       C
ATOM    606  C   HIS B  82      55.336 -14.486  -3.231  1.00 67.98           C
ANISOU  606  C   HIS B  82     5179  12215   8437  -1004   1622   1548       C
ATOM    607  O   HIS B  82      55.826 -15.080  -4.191  1.00 69.70           O
ANISOU  607  O   HIS B  82     5279  12723   8482   -861   1827   1575       O
ATOM    608  CB  HIS B  82      54.587 -12.310  -4.224  1.00 69.88           C
ANISOU  608  CB  HIS B  82     5634  12255   8663  -1318   1693   1965       C
ATOM    609  CG  HIS B  82      53.453 -11.432  -4.680  1.00 69.35           C
ANISOU  609  CG  HIS B  82     5857  11991   8501  -1365   1647   2086       C
ATOM    610  ND1 HIS B  82      52.237 -11.934  -5.105  1.00 67.32           N
ANISOU  610  ND1 HIS B  82     5858  11713   8006  -1155   1605   1960       N
ATOM    611  CD2 HIS B  82      53.365 -10.083  -4.804  1.00 70.90           C
ANISOU  611  CD2 HIS B  82     6122  12002   8817  -1592   1628   2324       C
ATOM    612  CE1 HIS B  82      51.448 -10.932  -5.456  1.00 67.56           C
ANISOU  612  CE1 HIS B  82     6094  11570   8005  -1234   1560   2111       C
ATOM    613  NE2 HIS B  82      52.109  -9.799  -5.287  1.00 69.73           N
ANISOU  613  NE2 HIS B  82     6272  11731   8491  -1493   1575   2337       N
ATOM    614  N   SER B  83      55.811 -14.609  -1.998  1.00 67.27           N
ANISOU  614  N   SER B  83     4974  12015   8571  -1065   1454   1433       N
ATOM    615  CA  SER B  83      56.907 -15.525  -1.675  1.00 68.30           C
ANISOU  615  CA  SER B  83     4836  12352   8765   -951   1487   1323       C
ATOM    616  C   SER B  83      56.447 -16.978  -1.552  1.00 66.29           C
ANISOU  616  C   SER B  83     4707  12130   8349   -646   1443   1072       C
ATOM    617  O   SER B  83      57.256 -17.892  -1.684  1.00 67.51           O
ANISOU  617  O   SER B  83     4675  12500   8477   -477   1522    984       O
ATOM    618  CB  SER B  83      57.570 -15.101  -0.362  1.00 68.52           C
ANISOU  618  CB  SER B  83     4705  12244   9085  -1121   1293   1289       C
ATOM    619  OG  SER B  83      56.662 -15.234   0.731  1.00 65.51           O
ANISOU  619  OG  SER B  83     4568  11583   8737  -1086   1051   1118       O
ATOM    620  N   LEU B  84      55.154 -17.188  -1.300  1.00 63.47           N
ANISOU  620  N   LEU B  84     4660  11557   7899   -577   1316    956       N
ATOM    621  CA  LEU B  84      54.651 -18.511  -0.924  1.00 61.52           C
ANISOU  621  CA  LEU B  84     4547  11265   7561   -339   1229    719       C
ATOM    622  C   LEU B  84      54.248 -19.356  -2.118  1.00 61.82           C
ANISOU  622  C   LEU B  84     4684  11463   7343   -118   1372    649       C
ATOM    623  O   LEU B  84      53.817 -18.839  -3.147  1.00 62.53           O
ANISOU  623  O   LEU B  84     4854  11623   7280   -145   1490    764       O
ATOM    624  CB  LEU B  84      53.467 -18.381   0.026  1.00 58.62           C
ANISOU  624  CB  LEU B  84     4440  10597   7237   -382   1021    623       C
ATOM    625  CG  LEU B  84      53.698 -17.499   1.255  1.00 58.28           C
ANISOU  625  CG  LEU B  84     4352  10373   7417   -581    852    662       C
ATOM    626  CD1 LEU B  84      52.406 -17.344   2.037  1.00 55.64           C
ANISOU  626  CD1 LEU B  84     4289   9776   7076   -596    683    570       C
ATOM    627  CD2 LEU B  84      54.797 -18.059   2.146  1.00 59.11           C
ANISOU  627  CD2 LEU B  84     4247  10547   7665   -537    775    581       C
ATOM    628  N   ASN B  85      54.417 -20.666  -1.966  1.00 61.56           N
ANISOU  628  N   ASN B  85     4649  11479   7262    110   1350    455       N
ATOM    629  CA  ASN B  85      54.070 -21.632  -2.996  1.00 62.03           C
ANISOU  629  CA  ASN B  85     4811  11667   7092    347   1450    333       C
ATOM    630  C   ASN B  85      53.060 -22.626  -2.488  1.00 59.71           C
ANISOU  630  C   ASN B  85     4761  11155   6772    475   1289    121       C
ATOM    631  O   ASN B  85      52.843 -22.742  -1.284  1.00 58.05           O
ANISOU  631  O   ASN B  85     4603  10737   6715    415   1123     69       O
ATOM    632  CB  ASN B  85      55.307 -22.402  -3.425  1.00 64.60           C
ANISOU  632  CB  ASN B  85     4897  12266   7383    535   1589    281       C
ATOM    633  CG  ASN B  85      56.434 -21.493  -3.853  1.00 67.33           C
ANISOU  633  CG  ASN B  85     4946  12855   7782    398   1766    499       C
ATOM    634  OD1 ASN B  85      57.586 -21.817  -3.626  1.00 69.19           O
ANISOU  634  OD1 ASN B  85     4914  13260   8115    460   1818    487       O
ATOM    635  ND2 ASN B  85      56.111 -20.347  -4.450  1.00 67.81           N
ANISOU  635  ND2 ASN B  85     5044  12928   7791    206   1854    707       N
ATOM    636  N   VAL B  86      52.462 -23.354  -3.420  1.00 59.93           N
ANISOU  636  N   VAL B  86     4933  11238   6600    650   1338      0       N
ATOM    637  CA  VAL B  86      51.586 -24.460  -3.084  1.00 58.37           C
ANISOU  637  CA  VAL B  86     4946  10848   6384    780   1200   -211       C
ATOM    638  C   VAL B  86      52.397 -25.461  -2.257  1.00 58.79           C
ANISOU  638  C   VAL B  86     4905  10866   6565    913   1137   -327       C
ATOM    639  O   VAL B  86      53.558 -25.742  -2.577  1.00 60.96           O
ANISOU  639  O   VAL B  86     4974  11355   6832   1036   1246   -326       O
ATOM    640  CB  VAL B  86      51.008 -25.131  -4.352  1.00 59.30           C
ANISOU  640  CB  VAL B  86     5201  11064   6266    964   1264   -344       C
ATOM    641  CG1 VAL B  86      50.169 -26.350  -3.992  1.00 58.11           C
ANISOU  641  CG1 VAL B  86     5252  10694   6133   1081   1111   -571       C
ATOM    642  CG2 VAL B  86      50.185 -24.129  -5.159  1.00 59.07           C
ANISOU  642  CG2 VAL B  86     5272  11074   6096    850   1308   -222       C
ATOM    643  N   GLY B  87      51.794 -25.959  -1.180  1.00 56.91           N
ANISOU  643  N   GLY B  87     4811  10370   6442    892    965   -411       N
ATOM    644  CA  GLY B  87      52.464 -26.875  -0.260  1.00 57.23           C
ANISOU  644  CA  GLY B  87     4801  10339   6607   1014    876   -498       C
ATOM    645  C   GLY B  87      52.894 -26.221   1.044  1.00 56.43           C
ANISOU  645  C   GLY B  87     4601  10156   6685    858    774   -389       C
ATOM    646  O   GLY B  87      52.998 -26.898   2.078  1.00 55.98           O
ANISOU  646  O   GLY B  87     4592   9954   6724    921    644   -451       O
ATOM    647  N   ASP B  88      53.130 -24.909   1.010  1.00 56.46           N
ANISOU  647  N   ASP B  88     4482  10241   6731    657    820   -227       N
ATOM    648  CA  ASP B  88      53.618 -24.177   2.183  1.00 56.13           C
ANISOU  648  CA  ASP B  88     4331  10135   6860    501    711   -138       C
ATOM    649  C   ASP B  88      52.578 -24.078   3.293  1.00 53.77           C
ANISOU  649  C   ASP B  88     4249   9571   6611    407    545   -165       C
ATOM    650  O   ASP B  88      51.382 -23.961   3.033  1.00 52.29           O
ANISOU  650  O   ASP B  88     4257   9265   6344    359    539   -182       O
ATOM    651  CB  ASP B  88      54.082 -22.769   1.793  1.00 57.07           C
ANISOU  651  CB  ASP B  88     4281  10377   7027    293    797     39       C
ATOM    652  CG  ASP B  88      55.330 -22.779   0.916  1.00 59.90           C
ANISOU  652  CG  ASP B  88     4360  11030   7367    359    971     99       C
ATOM    653  OD1 ASP B  88      55.969 -23.851   0.747  1.00 61.16           O
ANISOU  653  OD1 ASP B  88     4432  11312   7496    584   1008    -13       O
ATOM    654  OD2 ASP B  88      55.661 -21.693   0.381  1.00 61.05           O
ANISOU  654  OD2 ASP B  88     4376  11288   7534    186   1077    266       O
ATOM    655  N   VAL B  89      53.062 -24.124   4.532  1.00 53.72           N
ANISOU  655  N   VAL B  89     4193   9492   6726    393    410   -170       N
ATOM    656  CA  VAL B  89      52.228 -24.034   5.720  1.00 51.91           C
ANISOU  656  CA  VAL B  89     4149   9045   6531    322    258   -188       C
ATOM    657  C   VAL B  89      52.290 -22.620   6.288  1.00 51.64           C
ANISOU  657  C   VAL B  89     4056   8979   6585    109    192    -92       C
ATOM    658  O   VAL B  89      53.355 -22.004   6.316  1.00 53.19           O
ANISOU  658  O   VAL B  89     4033   9296   6880     37    193    -28       O
ATOM    659  CB  VAL B  89      52.682 -25.060   6.780  1.00 52.29           C
ANISOU  659  CB  VAL B  89     4216   9026   6626    471    137   -260       C
ATOM    660  CG1 VAL B  89      52.044 -24.788   8.135  1.00 50.96           C
ANISOU  660  CG1 VAL B  89     4199   8680   6484    389    -14   -250       C
ATOM    661  CG2 VAL B  89      52.339 -26.471   6.315  1.00 52.44           C
ANISOU  661  CG2 VAL B  89     4365   8991   6569    670    175   -364       C
ATOM    662  N   VAL B  90      51.147 -22.124   6.753  1.00 49.94           N
ANISOU  662  N   VAL B  90     4032   8599   6344     10    128    -90       N
ATOM    663  CA  VAL B  90      51.051 -20.797   7.351  1.00 49.70           C
ANISOU  663  CA  VAL B  90     3994   8498   6393   -172     43    -26       C
ATOM    664  C   VAL B  90      50.454 -20.891   8.752  1.00 48.59           C
ANISOU  664  C   VAL B  90     4009   8201   6254   -165   -111    -86       C
ATOM    665  O   VAL B  90      49.357 -21.414   8.924  1.00 47.23           O
ANISOU  665  O   VAL B  90     4024   7927   5995   -114   -107   -131       O
ATOM    666  CB  VAL B  90      50.165 -19.864   6.495  1.00 49.04           C
ANISOU  666  CB  VAL B  90     3996   8376   6259   -289    120     41       C
ATOM    667  CG1 VAL B  90      50.147 -18.449   7.068  1.00 49.20           C
ANISOU  667  CG1 VAL B  90     4013   8301   6380   -468     23    103       C
ATOM    668  CG2 VAL B  90      50.649 -19.856   5.048  1.00 50.31           C
ANISOU  668  CG2 VAL B  90     4035   8709   6370   -274    289    112       C
ATOM    669  N   ILE B  91      51.174 -20.379   9.747  1.00 49.41           N
ANISOU  669  N   ILE B  91     4027   8297   6450   -217   -245    -87       N
ATOM    670  CA  ILE B  91      50.624 -20.194  11.089  1.00 48.68           C
ANISOU  670  CA  ILE B  91     4084   8076   6337   -222   -393   -137       C
ATOM    671  C   ILE B  91      50.021 -18.799  11.171  1.00 48.29           C
ANISOU  671  C   ILE B  91     4098   7932   6319   -382   -433   -114       C
ATOM    672  O   ILE B  91      50.645 -17.820  10.754  1.00 49.40           O
ANISOU  672  O   ILE B  91     4104   8100   6567   -514   -437    -57       O
ATOM    673  CB  ILE B  91      51.694 -20.335  12.196  1.00 50.07           C
ANISOU  673  CB  ILE B  91     4153   8292   6578   -175   -551   -172       C
ATOM    674  CG1 ILE B  91      52.371 -21.708  12.135  1.00 50.80           C
ANISOU  674  CG1 ILE B  91     4180   8471   6650     10   -527   -193       C
ATOM    675  CG2 ILE B  91      51.093 -20.103  13.582  1.00 49.55           C
ANISOU  675  CG2 ILE B  91     4262   8113   6452   -164   -701   -226       C
ATOM    676  CD1 ILE B  91      53.823 -21.655  11.703  1.00 52.83           C
ANISOU  676  CD1 ILE B  91     4151   8899   7024     18   -522   -174       C
ATOM    677  N   SER B  92      48.812 -18.711  11.718  1.00 46.96           N
ANISOU  677  N   SER B  92     4130   7649   6063   -367   -462   -155       N
ATOM    678  CA  SER B  92      48.170 -17.425  11.930  1.00 46.72           C
ANISOU  678  CA  SER B  92     4182   7514   6054   -479   -519   -157       C
ATOM    679  C   SER B  92      48.884 -16.651  13.023  1.00 47.98           C
ANISOU  679  C   SER B  92     4296   7635   6297   -536   -700   -202       C
ATOM    680  O   SER B  92      49.008 -17.138  14.149  1.00 48.16           O
ANISOU  680  O   SER B  92     4371   7661   6267   -445   -804   -269       O
ATOM    681  CB  SER B  92      46.719 -17.608  12.355  1.00 45.27           C
ANISOU  681  CB  SER B  92     4202   7248   5751   -421   -504   -205       C
ATOM    682  OG  SER B  92      46.638 -18.173  13.654  1.00 45.29           O
ANISOU  682  OG  SER B  92     4287   7235   5685   -330   -592   -265       O
ATOM    683  N   THR B  93      49.360 -15.456  12.687  1.00 49.10           N
ANISOU  683  N   THR B  93     4350   7737   6570   -687   -744   -163       N
ATOM    684  CA  THR B  93      49.680 -14.460  13.695  1.00 50.32           C
ANISOU  684  CA  THR B  93     4515   7797   6807   -762   -938   -233       C
ATOM    685  C   THR B  93      48.373 -13.831  14.136  1.00 49.35           C
ANISOU  685  C   THR B  93     4615   7538   6599   -739   -974   -295       C
ATOM    686  O   THR B  93      48.084 -13.723  15.326  1.00 49.51           O
ANISOU  686  O   THR B  93     4746   7513   6551   -670  -1104   -403       O
ATOM    687  CB  THR B  93      50.585 -13.346  13.139  1.00 52.17           C
ANISOU  687  CB  THR B  93     4584   8000   7239   -958   -975   -162       C
ATOM    688  OG1 THR B  93      50.088 -12.915  11.870  1.00 51.75           O
ANISOU  688  OG1 THR B  93     4552   7919   7193  -1032   -818    -44       O
ATOM    689  CG2 THR B  93      51.994 -13.839  12.977  1.00 53.68           C
ANISOU  689  CG2 THR B  93     4518   8345   7534   -983   -974   -125       C
ATOM    690  N   GLU B  94      47.582 -13.426  13.147  1.00 48.58           N
ANISOU  690  N   GLU B  94     4577   7391   6490   -779   -855   -227       N
ATOM    691  CA  GLU B  94      46.331 -12.723  13.367  1.00 47.91           C
ANISOU  691  CA  GLU B  94     4677   7184   6343   -753   -879   -277       C
ATOM    692  C   GLU B  94      45.340 -13.186  12.309  1.00 46.46           C
ANISOU  692  C   GLU B  94     4546   7040   6068   -704   -706   -213       C
ATOM    693  O   GLU B  94      45.745 -13.666  11.249  1.00 46.36           O
ANISOU  693  O   GLU B  94     4431   7117   6068   -730   -585   -119       O
ATOM    694  CB  GLU B  94      46.584 -11.219  13.248  1.00 49.44           C
ANISOU  694  CB  GLU B  94     4876   7223   6687   -893   -988   -263       C
ATOM    695  CG  GLU B  94      45.344 -10.339  13.301  1.00 49.13           C
ANISOU  695  CG  GLU B  94     5021   7041   6606   -856  -1017   -309       C
ATOM    696  CD  GLU B  94      45.670  -8.861  13.183  1.00 51.01           C
ANISOU  696  CD  GLU B  94     5281   7087   7015   -994  -1142   -292       C
ATOM    697  OE1 GLU B  94      46.752  -8.529  12.654  1.00 52.40           O
ANISOU  697  OE1 GLU B  94     5310   7252   7346  -1154  -1147   -188       O
ATOM    698  OE2 GLU B  94      44.833  -8.036  13.616  1.00 51.30           O
ANISOU  698  OE2 GLU B  94     5479   6980   7035   -940  -1232   -380       O
ATOM    699  N   VAL B  95      44.049 -13.048  12.598  1.00 45.56           N
ANISOU  699  N   VAL B  95     4581   6875   5856   -625   -699   -273       N
ATOM    700  CA  VAL B  95      43.002 -13.392  11.639  1.00 44.41           C
ANISOU  700  CA  VAL B  95     4481   6763   5630   -580   -565   -232       C
ATOM    701  C   VAL B  95      42.030 -12.227  11.445  1.00 44.62           C
ANISOU  701  C   VAL B  95     4617   6675   5663   -579   -604   -245       C
ATOM    702  O   VAL B  95      41.652 -11.559  12.407  1.00 45.09           O
ANISOU  702  O   VAL B  95     4766   6647   5718   -543   -713   -339       O
ATOM    703  CB  VAL B  95      42.224 -14.644  12.088  1.00 43.21           C
ANISOU  703  CB  VAL B  95     4378   6690   5350   -467   -496   -287       C
ATOM    704  CG1 VAL B  95      41.215 -15.063  11.029  1.00 42.30           C
ANISOU  704  CG1 VAL B  95     4283   6616   5174   -436   -376   -258       C
ATOM    705  CG2 VAL B  95      43.189 -15.787  12.385  1.00 43.27           C
ANISOU  705  CG2 VAL B  95     4304   6781   5355   -444   -480   -276       C
ATOM    706  N   ARG B  96      41.629 -12.006  10.197  1.00 44.48           N
ANISOU  706  N   ARG B  96     4596   6664   5640   -598   -521   -157       N
ATOM    707  CA  ARG B  96      40.680 -10.962   9.847  1.00 44.83           C
ANISOU  707  CA  ARG B  96     4744   6604   5685   -575   -555   -153       C
ATOM    708  C   ARG B  96      39.657 -11.458   8.826  1.00 43.96           C
ANISOU  708  C   ARG B  96     4648   6580   5473   -503   -447   -124       C
ATOM    709  O   ARG B  96      39.861 -12.477   8.170  1.00 43.33           O
ANISOU  709  O   ARG B  96     4497   6624   5341   -500   -345    -90       O
ATOM    710  CB  ARG B  96      41.416  -9.742   9.286  1.00 46.43           C
ANISOU  710  CB  ARG B  96     4942   6679   6021   -698   -611    -44       C
ATOM    711  CG  ARG B  96      42.197  -8.961  10.323  1.00 47.73           C
ANISOU  711  CG  ARG B  96     5113   6710   6311   -775   -765   -102       C
ATOM    712  CD  ARG B  96      42.864  -7.716   9.740  1.00 49.67           C
ANISOU  712  CD  ARG B  96     5356   6796   6720   -925   -824     19       C
ATOM    713  NE  ARG B  96      43.819  -7.115  10.692  1.00 51.19           N
ANISOU  713  NE  ARG B  96     5518   6872   7060  -1030   -982    -45       N
ATOM    714  CZ  ARG B  96      43.790  -5.865  11.162  1.00 52.85           C
ANISOU  714  CZ  ARG B  96     5833   6856   7393  -1079  -1145    -95       C
ATOM    715  NH1 ARG B  96      42.873  -4.988  10.775  1.00 53.35           N
ANISOU  715  NH1 ARG B  96     6047   6765   7457  -1027  -1174    -76       N
ATOM    716  NH2 ARG B  96      44.720  -5.474  12.025  1.00 54.32           N
ANISOU  716  NH2 ARG B  96     5972   6958   7710  -1178  -1300   -173       N
ATOM    717  N   HIS B  97      38.540 -10.743   8.722  1.00 44.12           N
ANISOU  717  N   HIS B  97     4761   6537   5466   -432   -485   -156       N
ATOM    718  CA  HIS B  97      37.587 -10.939   7.633  1.00 43.78           C
ANISOU  718  CA  HIS B  97     4728   6563   5342   -368   -419   -123       C
ATOM    719  C   HIS B  97      38.052 -10.062   6.483  1.00 44.96           C
ANISOU  719  C   HIS B  97     4897   6652   5532   -430   -418     28       C
ATOM    720  O   HIS B  97      38.315  -8.887   6.700  1.00 46.16           O
ANISOU  720  O   HIS B  97     5115   6645   5780   -474   -508     69       O
ATOM    721  CB  HIS B  97      36.184 -10.486   8.047  1.00 43.78           C
ANISOU  721  CB  HIS B  97     4801   6533   5300   -247   -470   -222       C
ATOM    722  CG  HIS B  97      35.594 -11.259   9.187  1.00 43.00           C
ANISOU  722  CG  HIS B  97     4683   6507   5147   -185   -450   -350       C
ATOM    723  ND1 HIS B  97      34.864 -12.414   9.001  1.00 42.13           N
ANISOU  723  ND1 HIS B  97     4513   6531   4964   -152   -361   -387       N
ATOM    724  CD2 HIS B  97      35.593 -11.023  10.523  1.00 43.25           C
ANISOU  724  CD2 HIS B  97     4755   6497   5181   -151   -506   -444       C
ATOM    725  CE1 HIS B  97      34.457 -12.869  10.174  1.00 41.89           C
ANISOU  725  CE1 HIS B  97     4481   6538   4899   -113   -347   -473       C
ATOM    726  NE2 HIS B  97      34.884 -12.041  11.115  1.00 42.54           N
ANISOU  726  NE2 HIS B  97     4627   6528   5009    -99   -431   -511       N
ATOM    727  N   HIS B  98      38.153 -10.601   5.272  1.00 44.89           N
ANISOU  727  N   HIS B  98     4844   6762   5450   -433   -321    115       N
ATOM    728  CA  HIS B  98      38.470  -9.750   4.118  1.00 46.29           C
ANISOU  728  CA  HIS B  98     5055   6902   5631   -476   -304    283       C
ATOM    729  C   HIS B  98      37.245  -9.222   3.382  1.00 46.73           C
ANISOU  729  C   HIS B  98     5207   6944   5605   -363   -340    299       C
ATOM    730  O   HIS B  98      37.355  -8.301   2.577  1.00 48.19           O
ANISOU  730  O   HIS B  98     5461   7056   5794   -381   -353    447       O
ATOM    731  CB  HIS B  98      39.446 -10.416   3.135  1.00 46.63           C
ANISOU  731  CB  HIS B  98     5001   7093   5624   -535   -177    393       C
ATOM    732  CG  HIS B  98      38.898 -11.597   2.398  1.00 45.78           C
ANISOU  732  CG  HIS B  98     4863   7163   5367   -436    -97    331       C
ATOM    733  ND1 HIS B  98      37.915 -11.495   1.438  1.00 46.09           N
ANISOU  733  ND1 HIS B  98     4968   7258   5287   -339    -99    343       N
ATOM    734  CD2 HIS B  98      39.240 -12.906   2.449  1.00 44.92           C
ANISOU  734  CD2 HIS B  98     4670   7181   5216   -416    -27    250       C
ATOM    735  CE1 HIS B  98      37.656 -12.697   0.951  1.00 45.43           C
ANISOU  735  CE1 HIS B  98     4837   7326   5097   -275    -41    257       C
ATOM    736  NE2 HIS B  98      38.446 -13.570   1.548  1.00 44.72           N
ANISOU  736  NE2 HIS B  98     4664   7269   5057   -320      7    201       N
ATOM    737  N   ASP B  99      36.082  -9.794   3.664  1.00 45.71           N
ANISOU  737  N   ASP B  99     5077   6884   5405   -248   -357    156       N
ATOM    738  CA  ASP B  99      34.846  -9.419   2.969  1.00 46.20           C
ANISOU  738  CA  ASP B  99     5199   6967   5387   -121   -402    147       C
ATOM    739  C   ASP B  99      33.873  -8.666   3.874  1.00 46.41           C
ANISOU  739  C   ASP B  99     5286   6882   5464    -26   -509     40       C
ATOM    740  O   ASP B  99      32.712  -8.495   3.510  1.00 46.74           O
ANISOU  740  O   ASP B  99     5347   6967   5448    102   -553     -8       O
ATOM    741  CB  ASP B  99      34.172 -10.667   2.368  1.00 45.35           C
ANISOU  741  CB  ASP B  99     5019   7054   5161    -57   -343     63       C
ATOM    742  CG  ASP B  99      33.647 -11.622   3.430  1.00 44.04           C
ANISOU  742  CG  ASP B  99     4780   6937   5017    -46   -331   -104       C
ATOM    743  OD1 ASP B  99      34.074 -11.509   4.607  1.00 43.61           O
ANISOU  743  OD1 ASP B  99     4725   6802   5043    -93   -342   -142       O
ATOM    744  OD2 ASP B  99      32.819 -12.494   3.098  1.00 43.64           O
ANISOU  744  OD2 ASP B  99     4674   7006   4903      4   -313   -192       O
ATOM    745  N   VAL B 100      34.323  -8.230   5.049  1.00 46.40           N
ANISOU  745  N   VAL B 100     5310   6756   5565    -71   -557    -12       N
ATOM    746  CA  VAL B 100      33.482  -7.420   5.924  1.00 46.98           C
ANISOU  746  CA  VAL B 100     5453   6720   5675     40   -660   -124       C
ATOM    747  C   VAL B 100      33.702  -5.934   5.635  1.00 48.82           C
ANISOU  747  C   VAL B 100     5823   6731   5997     43   -768    -26       C
ATOM    748  O   VAL B 100      34.831  -5.454   5.626  1.00 49.57           O
ANISOU  748  O   VAL B 100     5948   6697   6188    -96   -785     79       O
ATOM    749  CB  VAL B 100      33.739  -7.721   7.412  1.00 46.33           C
ANISOU  749  CB  VAL B 100     5348   6626   5631     20   -670   -258       C
ATOM    750  CG1 VAL B 100      33.217  -6.598   8.305  1.00 47.50           C
ANISOU  750  CG1 VAL B 100     5598   6624   5826    128   -791   -363       C
ATOM    751  CG2 VAL B 100      33.103  -9.047   7.800  1.00 44.95           C
ANISOU  751  CG2 VAL B 100     5066   6645   5367     57   -576   -359       C
ATOM    752  N   ASP B 101      32.610  -5.213   5.397  1.00 49.80           N
ANISOU  752  N   ASP B 101     6022   6803   6098    202   -848    -57       N
ATOM    753  CA  ASP B 101      32.677  -3.781   5.132  1.00 51.85           C
ANISOU  753  CA  ASP B 101     6436   6818   6445    232   -967     34       C
ATOM    754  C   ASP B 101      31.527  -3.028   5.793  1.00 52.79           C
ANISOU  754  C   ASP B 101     6631   6851   6577    438  -1084   -120       C
ATOM    755  O   ASP B 101      30.415  -2.958   5.263  1.00 53.21           O
ANISOU  755  O   ASP B 101     6679   6985   6553    606  -1106   -144       O
ATOM    756  CB  ASP B 101      32.682  -3.508   3.627  1.00 52.86           C
ANISOU  756  CB  ASP B 101     6614   6956   6517    230   -946    240       C
ATOM    757  CG  ASP B 101      32.791  -2.026   3.298  1.00 55.31           C
ANISOU  757  CG  ASP B 101     7104   6986   6926    248  -1067    373       C
ATOM    758  OD1 ASP B 101      32.993  -1.201   4.213  1.00 56.26           O
ANISOU  758  OD1 ASP B 101     7312   6882   7183    240  -1175    300       O
ATOM    759  OD2 ASP B 101      32.670  -1.684   2.110  1.00 56.53           O
ANISOU  759  OD2 ASP B 101     7326   7136   7017    277  -1062    553       O
ATOM    760  N   VAL B 102      31.826  -2.464   6.959  1.00 53.36           N
ANISOU  760  N   VAL B 102     6767   6767   6742    436  -1165   -236       N
ATOM    761  CA  VAL B 102      30.927  -1.545   7.637  1.00 54.82           C
ANISOU  761  CA  VAL B 102     7051   6825   6952    640  -1291   -387       C
ATOM    762  C   VAL B 102      31.685  -0.236   7.828  1.00 56.92           C
ANISOU  762  C   VAL B 102     7497   6750   7382    577  -1438   -335       C
ATOM    763  O   VAL B 102      31.634   0.377   8.885  1.00 57.94           O
ANISOU  763  O   VAL B 102     7709   6736   7571    652  -1547   -500       O
ATOM    764  CB  VAL B 102      30.449  -2.114   8.985  1.00 53.92           C
ANISOU  764  CB  VAL B 102     6856   6857   6775    731  -1257   -614       C
ATOM    765  CG1 VAL B 102      29.200  -1.388   9.458  1.00 55.40           C
ANISOU  765  CG1 VAL B 102     7096   7017   6936    998  -1343   -778       C
ATOM    766  CG2 VAL B 102      30.174  -3.608   8.870  1.00 51.78           C
ANISOU  766  CG2 VAL B 102     6398   6889   6385    683  -1092   -622       C
ATOM    767  N   THR B 103      32.381   0.192   6.775  1.00 57.84           N
ANISOU  767  N   THR B 103     7675   6735   7567    437  -1441   -102       N
ATOM    768  CA  THR B 103      33.168   1.423   6.809  1.00 60.18           C
ANISOU  768  CA  THR B 103     8136   6684   8048    328  -1574     -9       C
ATOM    769  C   THR B 103      32.290   2.670   6.741  1.00 62.61           C
ANISOU  769  C   THR B 103     8634   6744   8409    540  -1738    -45       C
ATOM    770  O   THR B 103      32.762   3.775   7.003  1.00 64.89           O
ANISOU  770  O   THR B 103     9086   6699   8869    488  -1884    -25       O
ATOM    771  CB  THR B 103      34.181   1.480   5.649  1.00 60.78           C
ANISOU  771  CB  THR B 103     8205   6713   8175    101  -1499    287       C
ATOM    772  OG1 THR B 103      33.487   1.332   4.409  1.00 60.83           O
ANISOU  772  OG1 THR B 103     8221   6842   8048    207  -1435    434       O
ATOM    773  CG2 THR B 103      35.230   0.380   5.776  1.00 58.90           C
ANISOU  773  CG2 THR B 103     7783   6679   7915   -106  -1356    317       C
ATOM    774  N   ALA B 104      31.023   2.498   6.377  1.00 62.33           N
ANISOU  774  N   ALA B 104     8577   6863   8242    779  -1725   -102       N
ATOM    775  CA  ALA B 104      30.053   3.589   6.426  1.00 64.62           C
ANISOU  775  CA  ALA B 104     9028   6959   8568   1037  -1884   -178       C
ATOM    776  C   ALA B 104      29.845   4.102   7.857  1.00 65.50           C
ANISOU  776  C   ALA B 104     9205   6938   8745   1163  -2002   -455       C
ATOM    777  O   ALA B 104      29.378   5.223   8.047  1.00 67.99           O
ANISOU  777  O   ALA B 104     9697   6993   9143   1345  -2167   -528       O
ATOM    778  CB  ALA B 104      28.724   3.146   5.828  1.00 64.09           C
ANISOU  778  CB  ALA B 104     8868   7146   8338   1273  -1841   -212       C
ATOM    779  N   PHE B 105      30.169   3.279   8.853  1.00 63.68           N
ANISOU  779  N   PHE B 105     8843   6890   8463   1089  -1920   -613       N
ATOM    780  CA  PHE B 105      30.123   3.694  10.251  1.00 64.61           C
ANISOU  780  CA  PHE B 105     9026   6910   8611   1194  -2023   -875       C
ATOM    781  C   PHE B 105      31.519   3.662  10.878  1.00 64.47           C
ANISOU  781  C   PHE B 105     9024   6766   8705    934  -2057   -873       C
ATOM    782  O   PHE B 105      31.682   3.358  12.062  1.00 64.07           O
ANISOU  782  O   PHE B 105     8940   6796   8608    958  -2068  -1076       O
ATOM    783  CB  PHE B 105      29.144   2.813  11.022  1.00 63.13           C
ANISOU  783  CB  PHE B 105     8678   7067   8240   1381  -1910  -1082       C
ATOM    784  CG  PHE B 105      27.756   2.843  10.463  1.00 63.53           C
ANISOU  784  CG  PHE B 105     8677   7263   8200   1635  -1887  -1103       C
ATOM    785  CD1 PHE B 105      26.908   3.903  10.735  1.00 66.05           C
ANISOU  785  CD1 PHE B 105     9124   7424   8548   1920  -2032  -1246       C
ATOM    786  CD2 PHE B 105      27.298   1.816   9.649  1.00 61.64           C
ANISOU  786  CD2 PHE B 105     8254   7315   7851   1598  -1736   -993       C
ATOM    787  CE1 PHE B 105      25.627   3.933  10.214  1.00 66.65           C
ANISOU  787  CE1 PHE B 105     9127   7651   8545   2168  -2021  -1271       C
ATOM    788  CE2 PHE B 105      26.018   1.839   9.125  1.00 62.25           C
ANISOU  788  CE2 PHE B 105     8260   7538   7854   1827  -1735  -1024       C
ATOM    789  CZ  PHE B 105      25.180   2.899   9.410  1.00 64.75           C
ANISOU  789  CZ  PHE B 105     8686   7716   8200   2114  -1875  -1159       C
ATOM    790  N   ASN B 106      32.515   3.994  10.059  1.00 65.11           N
ANISOU  790  N   ASN B 106     9151   6661   8928    690  -2075   -636       N
ATOM    791  CA  ASN B 106      33.893   4.186  10.491  1.00 65.72           C
ANISOU  791  CA  ASN B 106     9240   6569   9161    425  -2138   -607       C
ATOM    792  C   ASN B 106      34.555   3.044  11.252  1.00 63.49           C
ANISOU  792  C   ASN B 106     8779   6546   8797    301  -2034   -694       C
ATOM    793  O   ASN B 106      35.451   3.275  12.061  1.00 64.34           O
ANISOU  793  O   ASN B 106     8906   6530   9009    174  -2138   -786       O
ATOM    794  CB  ASN B 106      33.974   5.459  11.329  1.00 68.69           C
ANISOU  794  CB  ASN B 106     9825   6579   9695    498  -2379   -784       C
ATOM    795  CG  ASN B 106      33.151   6.577  10.743  1.00 71.11           C
ANISOU  795  CG  ASN B 106    10328   6621  10068    687  -2499   -740       C
ATOM    796  OD1 ASN B 106      33.105   6.749   9.529  1.00 71.45           O
ANISOU  796  OD1 ASN B 106    10396   6615  10137    629  -2447   -479       O
ATOM    797  ND2 ASN B 106      32.483   7.336  11.599  1.00 72.99           N
ANISOU  797  ND2 ASN B 106    10716   6698  10319    937  -2663   -998       N
ATOM    798  N   TYR B 107      34.111   1.820  11.002  1.00 60.89           N
ANISOU  798  N   TYR B 107     8283   6564   8288    343  -1845   -669       N
ATOM    799  CA  TYR B 107      34.885   0.660  11.389  1.00 58.85           C
ANISOU  799  CA  TYR B 107     7857   6533   7970    189  -1729   -669       C
ATOM    800  C   TYR B 107      35.869   0.492  10.260  1.00 58.66           C
ANISOU  800  C   TYR B 107     7764   6489   8035    -55  -1650   -402       C
ATOM    801  O   TYR B 107      35.516   0.724   9.103  1.00 59.00           O
ANISOU  801  O   TYR B 107     7837   6510   8070    -43  -1601   -225       O
ATOM    802  CB  TYR B 107      34.011  -0.583  11.520  1.00 56.50           C
ANISOU  802  CB  TYR B 107     7419   6582   7464    320  -1562   -736       C
ATOM    803  CG  TYR B 107      33.057  -0.514  12.679  1.00 56.83           C
ANISOU  803  CG  TYR B 107     7499   6697   7399    555  -1601   -985       C
ATOM    804  CD1 TYR B 107      33.476  -0.862  13.963  1.00 56.68           C
ANISOU  804  CD1 TYR B 107     7465   6744   7327    553  -1625  -1147       C
ATOM    805  CD2 TYR B 107      31.743  -0.093  12.506  1.00 57.58           C
ANISOU  805  CD2 TYR B 107     7636   6811   7430    793  -1612  -1059       C
ATOM    806  CE1 TYR B 107      32.615  -0.797  15.041  1.00 57.27           C
ANISOU  806  CE1 TYR B 107     7576   6912   7274    779  -1642  -1367       C
ATOM    807  CE2 TYR B 107      30.873  -0.025  13.582  1.00 58.18           C
ANISOU  807  CE2 TYR B 107     7726   6983   7398   1019  -1628  -1288       C
ATOM    808  CZ  TYR B 107      31.317  -0.382  14.848  1.00 58.04           C
ANISOU  808  CZ  TYR B 107     7701   7039   7314   1009  -1633  -1437       C
ATOM    809  OH  TYR B 107      30.466  -0.320  15.932  1.00 58.91           O
ANISOU  809  OH  TYR B 107     7826   7270   7286   1244  -1630  -1657       O
ATOM    810  N   GLU B 108      37.104   0.115  10.573  1.00 58.39           N
ANISOU  810  N   GLU B 108     7634   6475   8077   -264  -1639   -368       N
ATOM    811  CA  GLU B 108      38.084  -0.080   9.513  1.00 58.46           C
ANISOU  811  CA  GLU B 108     7548   6500   8162   -491  -1542   -114       C
ATOM    812  C   GLU B 108      37.736  -1.330   8.722  1.00 56.09           C
ANISOU  812  C   GLU B 108     7112   6516   7684   -452  -1336    -24       C
ATOM    813  O   GLU B 108      36.986  -2.178   9.191  1.00 54.32           O
ANISOU  813  O   GLU B 108     6837   6494   7310   -307  -1275   -165       O
ATOM    814  CB  GLU B 108      39.514  -0.099  10.045  1.00 59.18           C
ANISOU  814  CB  GLU B 108     7548   6535   8402   -719  -1595   -108       C
ATOM    815  CG  GLU B 108      39.874  -1.245  10.961  1.00 57.32           C
ANISOU  815  CG  GLU B 108     7175   6538   8065   -707  -1547   -252       C
ATOM    816  CD  GLU B 108      41.268  -1.064  11.543  1.00 58.61           C
ANISOU  816  CD  GLU B 108     7256   6616   8396   -913  -1649   -266       C
ATOM    817  OE1 GLU B 108      41.497  -0.058  12.250  1.00 60.74           O
ANISOU  817  OE1 GLU B 108     7635   6635   8807   -945  -1850   -382       O
ATOM    818  OE2 GLU B 108      42.137  -1.924  11.290  1.00 57.72           O
ANISOU  818  OE2 GLU B 108     6965   6687   8278  -1037  -1540   -173       O
ATOM    819  N   TYR B 109      38.238  -1.407   7.498  1.00 56.38           N
ANISOU  819  N   TYR B 109     7099   6588   7736   -578  -1232    211       N
ATOM    820  CA  TYR B 109      37.833  -2.458   6.582  1.00 54.63           C
ANISOU  820  CA  TYR B 109     6779   6636   7340   -522  -1060    290       C
ATOM    821  C   TYR B 109      38.086  -3.827   7.194  1.00 52.43           C
ANISOU  821  C   TYR B 109     6349   6603   6972   -524   -966    171       C
ATOM    822  O   TYR B 109      39.134  -4.062   7.790  1.00 52.47           O
ANISOU  822  O   TYR B 109     6271   6607   7058   -655   -979    151       O
ATOM    823  CB  TYR B 109      38.566  -2.324   5.243  1.00 55.68           C
ANISOU  823  CB  TYR B 109     6879   6784   7492   -668   -958    561       C
ATOM    824  CG  TYR B 109      38.017  -3.252   4.190  1.00 54.36           C
ANISOU  824  CG  TYR B 109     6651   6874   7128   -574   -810    627       C
ATOM    825  CD1 TYR B 109      37.012  -2.840   3.324  1.00 55.01           C
ANISOU  825  CD1 TYR B 109     6842   6944   7114   -431   -825    696       C
ATOM    826  CD2 TYR B 109      38.489  -4.555   4.076  1.00 52.67           C
ANISOU  826  CD2 TYR B 109     6277   6910   6824   -613   -674    603       C
ATOM    827  CE1 TYR B 109      36.509  -3.701   2.366  1.00 54.03           C
ANISOU  827  CE1 TYR B 109     6663   7062   6807   -342   -714    731       C
ATOM    828  CE2 TYR B 109      37.992  -5.421   3.125  1.00 51.70           C
ANISOU  828  CE2 TYR B 109     6110   7007   6528   -524   -559    634       C
ATOM    829  CZ  TYR B 109      37.000  -4.992   2.272  1.00 52.39           C
ANISOU  829  CZ  TYR B 109     6300   7088   6517   -393   -583    693       C
ATOM    830  OH  TYR B 109      36.496  -5.854   1.320  1.00 51.66           O
ANISOU  830  OH  TYR B 109     6164   7219   6247   -302   -492    702       O
ATOM    831  N   GLY B 110      37.117  -4.724   7.050  1.00 50.76           N
ANISOU  831  N   GLY B 110     6098   6590   6600   -380   -884     93       N
ATOM    832  CA  GLY B 110      37.228  -6.070   7.600  1.00 48.87           C
ANISOU  832  CA  GLY B 110     5734   6559   6274   -373   -794     -8       C
ATOM    833  C   GLY B 110      36.760  -6.209   9.038  1.00 48.39           C
ANISOU  833  C   GLY B 110     5698   6499   6191   -278   -861   -212       C
ATOM    834  O   GLY B 110      36.555  -7.321   9.508  1.00 46.97           O
ANISOU  834  O   GLY B 110     5440   6487   5919   -241   -783   -289       O
ATOM    835  N   GLN B 111      36.580  -5.089   9.734  1.00 49.80           N
ANISOU  835  N   GLN B 111     5993   6484   6444   -230  -1003   -297       N
ATOM    836  CA  GLN B 111      36.186  -5.114  11.130  1.00 49.77           C
ANISOU  836  CA  GLN B 111     6025   6487   6396   -121  -1070   -496       C
ATOM    837  C   GLN B 111      34.680  -5.283  11.298  1.00 49.33           C
ANISOU  837  C   GLN B 111     5987   6541   6217     81  -1030   -604       C
ATOM    838  O   GLN B 111      33.897  -4.448  10.842  1.00 50.34           O
ANISOU  838  O   GLN B 111     6194   6574   6360    188  -1085   -604       O
ATOM    839  CB  GLN B 111      36.618  -3.837  11.825  1.00 51.79           C
ANISOU  839  CB  GLN B 111     6406   6492   6780   -136  -1253   -574       C
ATOM    840  CG  GLN B 111      36.281  -3.807  13.305  1.00 52.11           C
ANISOU  840  CG  GLN B 111     6499   6551   6749     -5  -1332   -797       C
ATOM    841  CD  GLN B 111      36.769  -2.560  13.988  1.00 54.38           C
ANISOU  841  CD  GLN B 111     6920   6577   7166    -19  -1538   -902       C
ATOM    842  OE1 GLN B 111      36.995  -1.532  13.354  1.00 55.93           O
ANISOU  842  OE1 GLN B 111     7199   6539   7513    -87  -1631   -819       O
ATOM    843  NE2 GLN B 111      36.938  -2.641  15.294  1.00 54.85           N
ANISOU  843  NE2 GLN B 111     7010   6666   7163     47  -1619  -1086       N
ATOM    844  N   VAL B 112      34.297  -6.369  11.969  1.00 48.06           N
ANISOU  844  N   VAL B 112     5745   6578   5939    131   -935   -687       N
ATOM    845  CA  VAL B 112      32.922  -6.613  12.385  1.00 47.94           C
ANISOU  845  CA  VAL B 112     5711   6694   5810    305   -884   -802       C
ATOM    846  C   VAL B 112      32.607  -5.696  13.573  1.00 49.46           C
ANISOU  846  C   VAL B 112     6012   6791   5989    445   -998   -972       C
ATOM    847  O   VAL B 112      33.412  -5.593  14.495  1.00 49.90           O
ANISOU  847  O   VAL B 112     6115   6791   6056    403  -1067  -1037       O
ATOM    848  CB  VAL B 112      32.735  -8.087  12.805  1.00 46.48           C
ANISOU  848  CB  VAL B 112     5410   6732   5520    282   -741   -813       C
ATOM    849  CG1 VAL B 112      31.381  -8.313  13.475  1.00 46.78           C
ANISOU  849  CG1 VAL B 112     5411   6914   5448    442   -679   -932       C
ATOM    850  CG2 VAL B 112      32.908  -8.998  11.600  1.00 45.24           C
ANISOU  850  CG2 VAL B 112     5157   6663   5370    175   -641   -681       C
ATOM    851  N   PRO B 113      31.443  -5.021  13.553  1.00 50.50           N
ANISOU  851  N   PRO B 113     6184   6911   6091    629  -1030  -1058       N
ATOM    852  CA  PRO B 113      31.115  -4.092  14.640  1.00 52.28           C
ANISOU  852  CA  PRO B 113     6525   7043   6295    795  -1143  -1242       C
ATOM    853  C   PRO B 113      31.073  -4.739  16.028  1.00 52.19           C
ANISOU  853  C   PRO B 113     6488   7199   6145    854  -1085  -1371       C
ATOM    854  O   PRO B 113      30.510  -5.821  16.187  1.00 51.12           O
ANISOU  854  O   PRO B 113     6229   7296   5898    863   -926  -1349       O
ATOM    855  CB  PRO B 113      29.732  -3.589  14.254  1.00 53.20           C
ANISOU  855  CB  PRO B 113     6635   7198   6381   1001  -1139  -1298       C
ATOM    856  CG  PRO B 113      29.700  -3.686  12.770  1.00 52.48           C
ANISOU  856  CG  PRO B 113     6500   7082   6357    912  -1114  -1120       C
ATOM    857  CD  PRO B 113      30.497  -4.900  12.427  1.00 50.50           C
ANISOU  857  CD  PRO B 113     6144   6952   6094    702   -997   -992       C
ATOM    858  N   GLY B 114      31.681  -4.083  17.013  1.00 53.55           N
ANISOU  858  N   GLY B 114     6781   7245   6321    889  -1220  -1498       N
ATOM    859  CA  GLY B 114      31.795  -4.633  18.353  1.00 53.78           C
ANISOU  859  CA  GLY B 114     6813   7426   6195    949  -1186  -1612       C
ATOM    860  C   GLY B 114      32.959  -5.592  18.520  1.00 52.47           C
ANISOU  860  C   GLY B 114     6591   7313   6031    757  -1154  -1509       C
ATOM    861  O   GLY B 114      33.189  -6.096  19.618  1.00 52.75           O
ANISOU  861  O   GLY B 114     6641   7468   5932    798  -1138  -1580       O
ATOM    862  N   MET B 115      33.683  -5.857  17.431  1.00 51.23           N
ANISOU  862  N   MET B 115     6372   7082   6012    565  -1141  -1340       N
ATOM    863  CA  MET B 115      34.861  -6.724  17.448  1.00 50.18           C
ANISOU  863  CA  MET B 115     6171   6990   5903    392  -1118  -1239       C
ATOM    864  C   MET B 115      36.100  -5.893  17.214  1.00 51.12           C
ANISOU  864  C   MET B 115     6336   6888   6198    252  -1286  -1217       C
ATOM    865  O   MET B 115      36.029  -4.843  16.572  1.00 52.09           O
ANISOU  865  O   MET B 115     6523   6819   6449    235  -1374  -1201       O
ATOM    866  CB  MET B 115      34.779  -7.781  16.341  1.00 48.27           C
ANISOU  866  CB  MET B 115     5798   6863   5679    283   -956  -1066       C
ATOM    867  CG  MET B 115      33.655  -8.778  16.520  1.00 47.44           C
ANISOU  867  CG  MET B 115     5620   6972   5435    370   -788  -1069       C
ATOM    868  SD  MET B 115      33.910  -9.756  18.010  1.00 47.55           S
ANISOU  868  SD  MET B 115     5640   7142   5285    408   -735  -1119       S
ATOM    869  CE  MET B 115      32.240  -9.796  18.641  1.00 48.35           C
ANISOU  869  CE  MET B 115     5727   7416   5230    598   -615  -1214       C
ATOM    870  N   PRO B 116      37.252  -6.369  17.714  1.00 51.05           N
ANISOU  870  N   PRO B 116     6288   6903   6205    145  -1333  -1205       N
ATOM    871  CA  PRO B 116      38.500  -5.712  17.343  1.00 52.00           C
ANISOU  871  CA  PRO B 116     6397   6840   6520    -30  -1471  -1154       C
ATOM    872  C   PRO B 116      38.727  -5.895  15.844  1.00 50.97           C
ANISOU  872  C   PRO B 116     6172   6693   6503   -173  -1362   -946       C
ATOM    873  O   PRO B 116      38.179  -6.828  15.267  1.00 49.34           O
ANISOU  873  O   PRO B 116     5891   6648   6207   -147  -1194   -861       O
ATOM    874  CB  PRO B 116      39.556  -6.459  18.163  1.00 51.98           C
ANISOU  874  CB  PRO B 116     6331   6938   6480    -87  -1513  -1178       C
ATOM    875  CG  PRO B 116      38.949  -7.782  18.454  1.00 50.38           C
ANISOU  875  CG  PRO B 116     6082   6971   6087      7  -1338  -1148       C
ATOM    876  CD  PRO B 116      37.476  -7.542  18.579  1.00 50.34           C
ANISOU  876  CD  PRO B 116     6151   7010   5966    175  -1262  -1219       C
ATOM    877  N   PRO B 117      39.524  -5.016  15.214  1.00 52.21           N
ANISOU  877  N   PRO B 117     6330   6658   6851   -325  -1457   -864       N
ATOM    878  CA  PRO B 117      39.778  -5.111  13.769  1.00 51.66           C
ANISOU  878  CA  PRO B 117     6178   6584   6864   -453  -1345   -653       C
ATOM    879  C   PRO B 117      40.311  -6.469  13.301  1.00 49.96           C
ANISOU  879  C   PRO B 117     5805   6588   6592   -520  -1186   -542       C
ATOM    880  O   PRO B 117      40.108  -6.852  12.149  1.00 49.11           O
ANISOU  880  O   PRO B 117     5642   6552   6465   -548  -1053   -404       O
ATOM    881  CB  PRO B 117      40.830  -4.024  13.527  1.00 53.76           C
ANISOU  881  CB  PRO B 117     6455   6621   7350   -634  -1484   -589       C
ATOM    882  CG  PRO B 117      40.644  -3.051  14.635  1.00 55.54           C
ANISOU  882  CG  PRO B 117     6826   6661   7616   -556  -1690   -789       C
ATOM    883  CD  PRO B 117      40.211  -3.859  15.819  1.00 54.53           C
ANISOU  883  CD  PRO B 117     6706   6721   7291   -390  -1676   -963       C
ATOM    884  N   GLY B 118      41.005  -7.172  14.192  1.00 49.73           N
ANISOU  884  N   GLY B 118     5713   6656   6528   -531  -1213   -609       N
ATOM    885  CA  GLY B 118      41.483  -8.526  13.922  1.00 48.34           C
ANISOU  885  CA  GLY B 118     5403   6673   6290   -557  -1080   -531       C
ATOM    886  C   GLY B 118      41.612  -9.335  15.199  1.00 48.02           C
ANISOU  886  C   GLY B 118     5367   6743   6135   -469  -1113   -645       C
ATOM    887  O   GLY B 118      41.565  -8.788  16.298  1.00 49.09           O
ANISOU  887  O   GLY B 118     5591   6817   6245   -408  -1251   -783       O
ATOM    888  N   PHE B 119      41.780 -10.643  15.040  1.00 46.77           N
ANISOU  888  N   PHE B 119     5125   6745   5902   -453   -990   -586       N
ATOM    889  CA  PHE B 119      41.829 -11.568  16.165  1.00 46.52           C
ANISOU  889  CA  PHE B 119     5109   6822   5743   -359   -997   -655       C
ATOM    890  C   PHE B 119      43.224 -12.181  16.280  1.00 46.92           C
ANISOU  890  C   PHE B 119     5039   6931   5857   -425  -1037   -612       C
ATOM    891  O   PHE B 119      43.636 -12.976  15.428  1.00 46.19           O
ANISOU  891  O   PHE B 119     4841   6914   5796   -467   -926   -508       O
ATOM    892  CB  PHE B 119      40.773 -12.660  15.990  1.00 45.06           C
ANISOU  892  CB  PHE B 119     4943   6755   5424   -272   -829   -624       C
ATOM    893  CG  PHE B 119      39.380 -12.129  15.808  1.00 44.81           C
ANISOU  893  CG  PHE B 119     4990   6699   5338   -201   -782   -666       C
ATOM    894  CD1 PHE B 119      38.614 -11.769  16.902  1.00 45.47           C
ANISOU  894  CD1 PHE B 119     5173   6793   5312    -82   -824   -783       C
ATOM    895  CD2 PHE B 119      38.837 -11.986  14.540  1.00 44.16           C
ANISOU  895  CD2 PHE B 119     4876   6602   5302   -235   -699   -593       C
ATOM    896  CE1 PHE B 119      37.332 -11.284  16.741  1.00 45.48           C
ANISOU  896  CE1 PHE B 119     5221   6792   5267      2   -778   -829       C
ATOM    897  CE2 PHE B 119      37.552 -11.496  14.370  1.00 44.14           C
ANISOU  897  CE2 PHE B 119     4929   6589   5254   -153   -671   -637       C
ATOM    898  CZ  PHE B 119      36.798 -11.145  15.473  1.00 44.80           C
ANISOU  898  CZ  PHE B 119     5092   6684   5245    -34   -708   -757       C
ATOM    899  N   LYS B 120      43.945 -11.798  17.332  1.00 48.30           N
ANISOU  899  N   LYS B 120     5226   7079   6048   -420  -1207   -705       N
ATOM    900  CA  LYS B 120      45.298 -12.293  17.564  1.00 49.07           C
ANISOU  900  CA  LYS B 120     5193   7240   6212   -468  -1280   -683       C
ATOM    901  C   LYS B 120      45.254 -13.751  18.016  1.00 48.23           C
ANISOU  901  C   LYS B 120     5091   7276   5960   -349  -1197   -656       C
ATOM    902  O   LYS B 120      44.455 -14.128  18.884  1.00 47.98           O
ANISOU  902  O   LYS B 120     5189   7281   5761   -226  -1182   -708       O
ATOM    903  CB  LYS B 120      46.066 -11.428  18.575  1.00 51.11           C
ANISOU  903  CB  LYS B 120     5460   7427   6532   -495  -1517   -809       C
ATOM    904  CG  LYS B 120      47.024 -10.438  17.938  1.00 52.55           C
ANISOU  904  CG  LYS B 120     5515   7498   6954   -686  -1611   -774       C
ATOM    905  CD  LYS B 120      47.691  -9.525  18.969  1.00 54.86           C
ANISOU  905  CD  LYS B 120     5826   7693   7326   -724  -1874   -926       C
ATOM    906  CE  LYS B 120      48.823 -10.267  19.664  1.00 55.79           C
ANISOU  906  CE  LYS B 120     5814   7948   7436   -698  -1981   -958       C
ATOM    907  NZ  LYS B 120      49.386  -9.521  20.823  1.00 58.15           N
ANISOU  907  NZ  LYS B 120     6146   8179   7768   -700  -2262  -1139       N
ATOM    908  N   ALA B 121      46.098 -14.571  17.401  1.00 48.03           N
ANISOU  908  N   ALA B 121     4924   7326   5998   -381  -1136   -567       N
ATOM    909  CA  ALA B 121      46.213 -15.968  17.785  1.00 47.59           C
ANISOU  909  CA  ALA B 121     4874   7373   5834   -268  -1078   -534       C
ATOM    910  C   ALA B 121      46.953 -16.055  19.114  1.00 49.07           C
ANISOU  910  C   ALA B 121     5079   7600   5966   -192  -1258   -610       C
ATOM    911  O   ALA B 121      47.589 -15.093  19.543  1.00 50.48           O
ANISOU  911  O   ALA B 121     5217   7737   6226   -250  -1430   -690       O
ATOM    912  CB  ALA B 121      46.931 -16.763  16.704  1.00 47.24           C
ANISOU  912  CB  ALA B 121     4679   7393   5878   -299   -972   -438       C
ATOM    913  N   ASP B 122      46.861 -17.207  19.765  1.00 49.00           N
ANISOU  913  N   ASP B 122     5137   7661   5819    -62  -1230   -582       N
ATOM    914  CA  ASP B 122      47.474 -17.407  21.076  1.00 50.54           C
ANISOU  914  CA  ASP B 122     5375   7911   5915     45  -1399   -642       C
ATOM    915  C   ASP B 122      49.004 -17.346  21.017  1.00 51.98           C
ANISOU  915  C   ASP B 122     5367   8140   6242     10  -1549   -658       C
ATOM    916  O   ASP B 122      49.638 -18.067  20.245  1.00 51.73           O
ANISOU  916  O   ASP B 122     5197   8156   6304      1  -1473   -578       O
ATOM    917  CB  ASP B 122      47.045 -18.752  21.641  1.00 50.30           C
ANISOU  917  CB  ASP B 122     5463   7935   5714    187  -1313   -566       C
ATOM    918  CG  ASP B 122      47.577 -18.988  23.023  1.00 52.06           C
ANISOU  918  CG  ASP B 122     5762   8225   5793    322  -1483   -608       C
ATOM    919  OD1 ASP B 122      47.161 -18.252  23.940  1.00 52.89           O
ANISOU  919  OD1 ASP B 122     5984   8337   5775    364  -1576   -704       O
ATOM    920  OD2 ASP B 122      48.420 -19.904  23.194  1.00 52.82           O
ANISOU  920  OD2 ASP B 122     5807   8373   5891    405  -1531   -553       O
ATOM    921  N   GLU B 123      49.587 -16.496  21.857  1.00 53.69           N
ANISOU  921  N   GLU B 123     5571   8352   6478     -2  -1768   -774       N
ATOM    922  CA  GLU B 123      51.030 -16.290  21.874  1.00 55.46           C
ANISOU  922  CA  GLU B 123     5585   8626   6860    -56  -1937   -807       C
ATOM    923  C   GLU B 123      51.799 -17.573  22.166  1.00 56.07           C
ANISOU  923  C   GLU B 123     5595   8825   6885     88  -1958   -750       C
ATOM    924  O   GLU B 123      52.824 -17.847  21.531  1.00 56.73           O
ANISOU  924  O   GLU B 123     5456   8973   7125     48  -1961   -710       O
ATOM    925  CB  GLU B 123      51.408 -15.248  22.921  1.00 57.50           C
ANISOU  925  CB  GLU B 123     5875   8853   7120    -72  -2201   -968       C
ATOM    926  CG  GLU B 123      50.910 -13.845  22.624  1.00 57.56           C
ANISOU  926  CG  GLU B 123     5927   8710   7233   -221  -2232  -1042       C
ATOM    927  CD  GLU B 123      51.781 -12.777  23.264  1.00 60.13           C
ANISOU  927  CD  GLU B 123     6179   8983   7686   -307  -2519  -1196       C
ATOM    928  OE1 GLU B 123      52.354 -13.029  24.348  1.00 61.83           O
ANISOU  928  OE1 GLU B 123     6406   9285   7802   -192  -2719  -1296       O
ATOM    929  OE2 GLU B 123      51.897 -11.681  22.672  1.00 60.71           O
ANISOU  929  OE2 GLU B 123     6185   8919   7963   -493  -2554  -1215       O
ATOM    930  N   ALA B 124      51.303 -18.352  23.124  1.00 56.12           N
ANISOU  930  N   ALA B 124     5791   8863   6667    263  -1967   -740       N
ATOM    931  CA  ALA B 124      51.945 -19.610  23.508  1.00 56.94           C
ANISOU  931  CA  ALA B 124     5877   9056   6701    428  -1999   -675       C
ATOM    932  C   ALA B 124      51.936 -20.609  22.357  1.00 55.61           C
ANISOU  932  C   ALA B 124     5632   8881   6616    429  -1791   -551       C
ATOM    933  O   ALA B 124      52.964 -21.226  22.061  1.00 56.56           O
ANISOU  933  O   ALA B 124     5588   9073   6830    490  -1829   -525       O
ATOM    934  CB  ALA B 124      51.265 -20.209  24.734  1.00 57.38           C
ANISOU  934  CB  ALA B 124     6187   9131   6485    603  -2023   -655       C
ATOM    935  N   LEU B 125      50.779 -20.761  21.709  1.00 53.66           N
ANISOU  935  N   LEU B 125     5497   8555   6335    375  -1581   -492       N
ATOM    936  CA  LEU B 125      50.655 -21.659  20.563  1.00 52.48           C
ANISOU  936  CA  LEU B 125     5297   8387   6256    374  -1391   -401       C
ATOM    937  C   LEU B 125      51.525 -21.213  19.399  1.00 52.61           C
ANISOU  937  C   LEU B 125     5062   8449   6477    262  -1362   -408       C
ATOM    938  O   LEU B 125      52.193 -22.035  18.774  1.00 52.97           O
ANISOU  938  O   LEU B 125     4987   8549   6589    329  -1307   -368       O
ATOM    939  CB  LEU B 125      49.205 -21.771  20.100  1.00 50.60           C
ANISOU  939  CB  LEU B 125     5213   8063   5950    320  -1198   -357       C
ATOM    940  CG  LEU B 125      48.206 -22.416  21.065  1.00 50.51           C
ANISOU  940  CG  LEU B 125     5433   8017   5743    416  -1157   -312       C
ATOM    941  CD1 LEU B 125      46.840 -22.528  20.408  1.00 48.84           C
ANISOU  941  CD1 LEU B 125     5309   7736   5513    339   -961   -274       C
ATOM    942  CD2 LEU B 125      48.694 -23.778  21.527  1.00 51.59           C
ANISOU  942  CD2 LEU B 125     5624   8158   5818    573  -1182   -232       C
ATOM    943  N   VAL B 126      51.524 -19.920  19.105  1.00 52.57           N
ANISOU  943  N   VAL B 126     4982   8423   6570    100  -1395   -455       N
ATOM    944  CA  VAL B 126      52.361 -19.400  18.030  1.00 53.08           C
ANISOU  944  CA  VAL B 126     4804   8537   6826    -29  -1358   -435       C
ATOM    945  C   VAL B 126      53.840 -19.654  18.348  1.00 55.24           C
ANISOU  945  C   VAL B 126     4856   8933   7198     25  -1503   -459       C
ATOM    946  O   VAL B 126      54.585 -20.149  17.492  1.00 55.73           O
ANISOU  946  O   VAL B 126     4727   9091   7357     43  -1415   -412       O
ATOM    947  CB  VAL B 126      52.099 -17.900  17.762  1.00 53.07           C
ANISOU  947  CB  VAL B 126     4784   8457   6923   -223  -1388   -464       C
ATOM    948  CG1 VAL B 126      53.097 -17.338  16.756  1.00 54.18           C
ANISOU  948  CG1 VAL B 126     4662   8658   7268   -373  -1355   -416       C
ATOM    949  CG2 VAL B 126      50.681 -17.696  17.240  1.00 51.10           C
ANISOU  949  CG2 VAL B 126     4716   8108   6590   -258  -1231   -434       C
ATOM    950  N   ALA B 127      54.254 -19.339  19.577  1.00 56.70           N
ANISOU  950  N   ALA B 127     5063   9132   7348     69  -1729   -541       N
ATOM    951  CA  ALA B 127      55.642 -19.550  20.011  1.00 59.04           C
ANISOU  951  CA  ALA B 127     5142   9557   7735    133  -1907   -581       C
ATOM    952  C   ALA B 127      56.039 -21.008  19.865  1.00 59.24           C
ANISOU  952  C   ALA B 127     5141   9662   7705    341  -1843   -523       C
ATOM    953  O   ALA B 127      57.127 -21.334  19.399  1.00 60.65           O
ANISOU  953  O   ALA B 127     5067   9965   8012    376  -1853   -514       O
ATOM    954  CB  ALA B 127      55.821 -19.106  21.453  1.00 60.57           C
ANISOU  954  CB  ALA B 127     5423   9747   7843    186  -2173   -692       C
ATOM    955  N   LEU B 128      55.137 -21.886  20.268  1.00 58.04           N
ANISOU  955  N   LEU B 128     5250   9435   7370    480  -1774   -481       N
ATOM    956  CA  LEU B 128      55.357 -23.316  20.152  1.00 58.29           C
ANISOU  956  CA  LEU B 128     5313   9487   7347    681  -1715   -419       C
ATOM    957  C   LEU B 128      55.490 -23.707  18.682  1.00 57.52           C
ANISOU  957  C   LEU B 128     5076   9415   7366    648  -1507   -376       C
ATOM    958  O   LEU B 128      56.446 -24.372  18.300  1.00 58.87           O
ANISOU  958  O   LEU B 128     5069   9685   7613    767  -1510   -374       O
ATOM    959  CB  LEU B 128      54.198 -24.070  20.810  1.00 57.21           C
ANISOU  959  CB  LEU B 128     5500   9231   7008    784  -1658   -362       C
ATOM    960  CG  LEU B 128      54.478 -25.531  21.156  1.00 58.21           C
ANISOU  960  CG  LEU B 128     5717   9343   7058   1015  -1675   -296       C
ATOM    961  CD1 LEU B 128      53.477 -26.034  22.190  1.00 57.97           C
ANISOU  961  CD1 LEU B 128     5998   9211   6816   1094  -1675   -228       C
ATOM    962  CD2 LEU B 128      54.455 -26.405  19.909  1.00 57.50           C
ANISOU  962  CD2 LEU B 128     5574   9215   7057   1050  -1489   -256       C
ATOM    963  N   ALA B 129      54.529 -23.296  17.859  1.00 55.61           N
ANISOU  963  N   ALA B 129     4913   9094   7122    507  -1331   -349       N
ATOM    964  CA  ALA B 129      54.565 -23.605  16.431  1.00 54.98           C
ANISOU  964  CA  ALA B 129     4725   9048   7118    480  -1134   -316       C
ATOM    965  C   ALA B 129      55.868 -23.135  15.799  1.00 56.69           C
ANISOU  965  C   ALA B 129     4610   9428   7500    426  -1146   -325       C
ATOM    966  O   ALA B 129      56.476 -23.858  15.005  1.00 57.45           O
ANISOU  966  O   ALA B 129     4566   9623   7640    531  -1049   -314       O
ATOM    967  CB  ALA B 129      53.383 -22.970  15.717  1.00 52.98           C
ANISOU  967  CB  ALA B 129     4590   8703   6838    321   -984   -292       C
ATOM    968  N   GLU B 130      56.283 -21.924  16.165  1.00 57.52           N
ANISOU  968  N   GLU B 130     4592   9564   7700    263  -1265   -350       N
ATOM    969  CA  GLU B 130      57.536 -21.338  15.683  1.00 59.56           C
ANISOU  969  CA  GLU B 130     4511   9978   8142    166  -1290   -347       C
ATOM    970  C   GLU B 130      58.699 -22.298  15.829  1.00 61.56           C
ANISOU  970  C   GLU B 130     4567  10388   8437    366  -1354   -371       C
ATOM    971  O   GLU B 130      59.460 -22.516  14.877  1.00 62.70           O
ANISOU  971  O   GLU B 130     4465  10684   8676    384  -1231   -343       O
ATOM    972  CB  GLU B 130      57.873 -20.045  16.431  1.00 60.70           C
ANISOU  972  CB  GLU B 130     4578  10097   8390    -16  -1485   -395       C
ATOM    973  CG  GLU B 130      57.409 -18.779  15.731  1.00 60.07           C
ANISOU  973  CG  GLU B 130     4492   9933   8397   -271  -1395   -350       C
ATOM    974  CD  GLU B 130      57.845 -17.516  16.452  1.00 61.70           C
ANISOU  974  CD  GLU B 130     4615  10089   8739   -453  -1610   -411       C
ATOM    975  OE1 GLU B 130      58.989 -17.463  16.945  1.00 64.07           O
ANISOU  975  OE1 GLU B 130     4682  10502   9158   -452  -1778   -462       O
ATOM    976  OE2 GLU B 130      57.036 -16.571  16.527  1.00 60.80           O
ANISOU  976  OE2 GLU B 130     4666   9816   8618   -590  -1624   -420       O
ATOM    977  N   LYS B 131      58.834 -22.877  17.017  1.00 62.22           N
ANISOU  977  N   LYS B 131     4758  10446   8435    534  -1542   -418       N
ATOM    978  CA  LYS B 131      59.922 -23.800  17.269  1.00 64.35           C
ANISOU  978  CA  LYS B 131     4859  10854   8738    757  -1636   -444       C
ATOM    979  C   LYS B 131      59.930 -24.987  16.317  1.00 64.10           C
ANISOU  979  C   LYS B 131     4830  10849   8676    937  -1446   -412       C
ATOM    980  O   LYS B 131      60.993 -25.453  15.909  1.00 66.09           O
ANISOU  980  O   LYS B 131     4822  11270   9018   1066  -1438   -431       O
ATOM    981  CB  LYS B 131      59.872 -24.300  18.706  1.00 65.01           C
ANISOU  981  CB  LYS B 131     5131  10879   8691    930  -1863   -479       C
ATOM    982  CG  LYS B 131      60.241 -23.250  19.738  1.00 66.30           C
ANISOU  982  CG  LYS B 131     5230  11070   8889    816  -2110   -552       C
ATOM    983  CD  LYS B 131      60.249 -23.851  21.133  1.00 67.30           C
ANISOU  983  CD  LYS B 131     5548  11173   8849   1029  -2331   -581       C
ATOM    984  CE  LYS B 131      61.629 -24.404  21.477  1.00 70.26           C
ANISOU  984  CE  LYS B 131     5667  11726   9302   1222  -2515   -622       C
ATOM    985  NZ  LYS B 131      61.811 -24.688  22.932  1.00 71.87           N
ANISOU  985  NZ  LYS B 131     6019  11938   9352   1405  -2789   -662       N
ATOM    986  N   CYS B 132      58.756 -25.476  15.955  1.00 61.88           N
ANISOU  986  N   CYS B 132     4831  10409   8274    953  -1299   -378       N
ATOM    987  CA  CYS B 132      58.676 -26.632  15.076  1.00 61.77           C
ANISOU  987  CA  CYS B 132     4856  10386   8226   1127  -1141   -372       C
ATOM    988  C   CYS B 132      58.770 -26.287  13.581  1.00 61.52           C
ANISOU  988  C   CYS B 132     4653  10464   8260   1026   -918   -360       C
ATOM    989  O   CYS B 132      58.731 -27.186  12.739  1.00 61.65           O
ANISOU  989  O   CYS B 132     4691  10493   8242   1174   -782   -378       O
ATOM    990  CB  CYS B 132      57.428 -27.460  15.405  1.00 60.02           C
ANISOU  990  CB  CYS B 132     5007   9940   7859   1202  -1106   -347       C
ATOM    991  SG  CYS B 132      57.700 -28.533  16.842  1.00 61.51           S
ANISOU  991  SG  CYS B 132     5366  10045   7960   1458  -1319   -335       S
ATOM    992  N   MET B 133      58.941 -25.007  13.245  1.00 61.54           N
ANISOU  992  N   MET B 133     4485  10545   8350    785   -885   -329       N
ATOM    993  CA  MET B 133      59.112 -24.597  11.841  1.00 61.73           C
ANISOU  993  CA  MET B 133     4335  10696   8422    682   -668   -288       C
ATOM    994  C   MET B 133      60.300 -25.292  11.157  1.00 64.15           C
ANISOU  994  C   MET B 133     4357  11230   8788    866   -588   -313       C
ATOM    995  O   MET B 133      60.360 -25.324   9.927  1.00 64.44           O
ANISOU  995  O   MET B 133     4298  11381   8807    863   -380   -290       O
ATOM    996  CB  MET B 133      59.298 -23.078  11.724  1.00 62.04           C
ANISOU  996  CB  MET B 133     4218  10779   8577    390   -674   -229       C
ATOM    997  CG  MET B 133      58.078 -22.246  12.081  1.00 59.81           C
ANISOU  997  CG  MET B 133     4199  10289   8238    208   -707   -207       C
ATOM    998  SD  MET B 133      58.435 -20.476  12.089  1.00 60.80           S
ANISOU  998  SD  MET B 133     4149  10421   8531   -116   -764   -150       S
ATOM    999  CE  MET B 133      57.952 -19.985  10.438  1.00 60.13           C
ANISOU  999  CE  MET B 133     4052  10371   8424   -250   -484    -34       C
ATOM   1000  N   GLN B 134      61.246 -25.820  11.938  1.00 66.10           N
ANISOU 1000  N   GLN B 134     4463  11560   9093   1038   -752   -363       N
ATOM   1001  CA  GLN B 134      62.365 -26.589  11.394  1.00 68.63           C
ANISOU 1001  CA  GLN B 134     4513  12097   9464   1262   -693   -404       C
ATOM   1002  C   GLN B 134      62.300 -28.029  11.876  1.00 68.91           C
ANISOU 1002  C   GLN B 134     4742  12025   9415   1586   -783   -474       C
ATOM   1003  O   GLN B 134      61.664 -28.864  11.241  1.00 67.98           O
ANISOU 1003  O   GLN B 134     4828  11802   9198   1715   -660   -500       O
ATOM   1004  CB  GLN B 134      63.706 -25.976  11.784  1.00 71.43           C
ANISOU 1004  CB  GLN B 134     4469  12678   9993   1205   -810   -405       C
ATOM   1005  CG  GLN B 134      63.775 -24.469  11.606  1.00 71.47           C
ANISOU 1005  CG  GLN B 134     4310  12728  10116    849   -783   -328       C
ATOM   1006  CD  GLN B 134      63.089 -23.668  12.711  1.00 69.88           C
ANISOU 1006  CD  GLN B 134     4329  12313   9911    663   -984   -329       C
ATOM   1007  OE1 GLN B 134      62.294 -24.197  13.505  1.00 68.18           O
ANISOU 1007  OE1 GLN B 134     4438  11904   9564    774  -1094   -366       O
ATOM   1008  NE2 GLN B 134      63.410 -22.376  12.771  1.00 70.74           N
ANISOU 1008  NE2 GLN B 134     4257  12456  10167    377  -1030   -287       N
ATOM   1009  N   GLN B 140      58.293 -25.790   3.627  1.00 63.30           N
ANISOU 1009  N   GLN B 140     4376  11554   8123    943    630   -236       N
ATOM   1010  CA  GLN B 140      58.447 -24.428   4.127  1.00 63.06           C
ANISOU 1010  CA  GLN B 140     4233  11512   8217    656    578    -99       C
ATOM   1011  C   GLN B 140      57.248 -23.973   4.983  1.00 60.27           C
ANISOU 1011  C   GLN B 140     4166  10868   7866    501    426    -92       C
ATOM   1012  O   GLN B 140      56.107 -23.971   4.516  1.00 58.52           O
ANISOU 1012  O   GLN B 140     4182  10526   7529    473    474   -100       O
ATOM   1013  CB  GLN B 140      58.646 -23.452   2.963  1.00 64.25           C
ANISOU 1013  CB  GLN B 140     4232  11847   8334    495    783     42       C
ATOM   1014  CG  GLN B 140      58.371 -21.997   3.337  1.00 63.55           C
ANISOU 1014  CG  GLN B 140     4143  11648   8354    176    725    185       C
ATOM   1015  CD  GLN B 140      58.743 -20.984   2.268  1.00 65.34           C
ANISOU 1015  CD  GLN B 140     4195  12050   8579     -1    921    363       C
ATOM   1016  OE1 GLN B 140      59.840 -20.430   2.293  1.00 67.74           O
ANISOU 1016  OE1 GLN B 140     4190  12519   9030   -118    960    458       O
ATOM   1017  NE2 GLN B 140      57.804 -20.672   1.373  1.00 64.33           N
ANISOU 1017  NE2 GLN B 140     4267  11878   8297    -40   1034    422       N
ATOM   1018  N   VAL B 141      57.533 -23.561   6.222  1.00 60.11           N
ANISOU 1018  N   VAL B 141     4108  10759   7973    409    242    -84       N
ATOM   1019  CA  VAL B 141      56.527 -23.070   7.168  1.00 57.92           C
ANISOU 1019  CA  VAL B 141     4073  10237   7697    278     94    -84       C
ATOM   1020  C   VAL B 141      56.767 -21.587   7.458  1.00 58.35           C
ANISOU 1020  C   VAL B 141     4011  10283   7877     12     40     14       C
ATOM   1021  O   VAL B 141      57.895 -21.177   7.665  1.00 60.41           O
ANISOU 1021  O   VAL B 141     4002  10677   8275    -51      1     48       O
ATOM   1022  CB  VAL B 141      56.575 -23.858   8.493  1.00 57.58           C
ANISOU 1022  CB  VAL B 141     4131  10077   7669    416    -99   -170       C
ATOM   1023  CG1 VAL B 141      55.558 -23.316   9.485  1.00 55.64           C
ANISOU 1023  CG1 VAL B 141     4122   9616   7403    291   -232   -168       C
ATOM   1024  CG2 VAL B 141      56.322 -25.335   8.247  1.00 57.42           C
ANISOU 1024  CG2 VAL B 141     4250  10017   7551    669    -61   -258       C
ATOM   1025  N   VAL B 142      55.698 -20.794   7.467  1.00 56.62           N
ANISOU 1025  N   VAL B 142     3993   9900   7621   -140     29     54       N
ATOM   1026  CA  VAL B 142      55.777 -19.356   7.738  1.00 57.07           C
ANISOU 1026  CA  VAL B 142     3994   9893   7799   -389    -38    137       C
ATOM   1027  C   VAL B 142      54.686 -18.917   8.718  1.00 55.11           C
ANISOU 1027  C   VAL B 142     4009   9408   7521   -448   -191     86       C
ATOM   1028  O   VAL B 142      53.748 -19.658   9.014  1.00 53.32           O
ANISOU 1028  O   VAL B 142     4006   9083   7171   -323   -205     16       O
ATOM   1029  CB  VAL B 142      55.653 -18.506   6.454  1.00 57.68           C
ANISOU 1029  CB  VAL B 142     4019  10031   7866   -537    143    276       C
ATOM   1030  CG1 VAL B 142      56.794 -18.806   5.499  1.00 60.08           C
ANISOU 1030  CG1 VAL B 142     4035  10602   8191   -492    314    342       C
ATOM   1031  CG2 VAL B 142      54.297 -18.724   5.776  1.00 55.63           C
ANISOU 1031  CG2 VAL B 142     4028   9677   7430   -478    234    268       C
ATOM   1032  N   LYS B 143      54.822 -17.689   9.198  1.00 55.74           N
ANISOU 1032  N   LYS B 143     4054   9401   7723   -642   -301    122       N
ATOM   1033  CA  LYS B 143      53.962 -17.133  10.226  1.00 54.46           C
ANISOU 1033  CA  LYS B 143     4110   9039   7545   -690   -462     58       C
ATOM   1034  C   LYS B 143      53.454 -15.790   9.711  1.00 54.51           C
ANISOU 1034  C   LYS B 143     4175   8929   7606   -888   -434    144       C
ATOM   1035  O   LYS B 143      54.248 -14.932   9.329  1.00 56.44           O
ANISOU 1035  O   LYS B 143     4237   9207   8001  -1059   -424    236       O
ATOM   1036  CB  LYS B 143      54.789 -16.993  11.509  1.00 55.78           C
ANISOU 1036  CB  LYS B 143     4177   9202   7816   -699   -681    -22       C
ATOM   1037  CG  LYS B 143      54.393 -15.881  12.464  1.00 55.83           C
ANISOU 1037  CG  LYS B 143     4304   9032   7876   -824   -868    -75       C
ATOM   1038  CD  LYS B 143      55.378 -15.777  13.622  1.00 57.63           C
ANISOU 1038  CD  LYS B 143     4400   9294   8204   -826  -1095   -165       C
ATOM   1039  CE  LYS B 143      55.434 -14.363  14.178  1.00 58.85           C
ANISOU 1039  CE  LYS B 143     4566   9299   8493  -1022  -1271   -202       C
ATOM   1040  NZ  LYS B 143      56.494 -14.231  15.205  1.00 61.05           N
ANISOU 1040  NZ  LYS B 143     4683   9629   8884  -1036  -1508   -300       N
ATOM   1041  N   GLY B 144      52.138 -15.616   9.663  1.00 52.66           N
ANISOU 1041  N   GLY B 144     4188   8560   7260   -864   -416    126       N
ATOM   1042  CA  GLY B 144      51.564 -14.404   9.081  1.00 52.75           C
ANISOU 1042  CA  GLY B 144     4281   8454   7308  -1014   -386    213       C
ATOM   1043  C   GLY B 144      50.050 -14.325   9.149  1.00 50.75           C
ANISOU 1043  C   GLY B 144     4291   8069   6922   -947   -386    166       C
ATOM   1044  O   GLY B 144      49.391 -15.213   9.682  1.00 49.24           O
ANISOU 1044  O   GLY B 144     4220   7875   6614   -803   -400     69       O
ATOM   1045  N   MET B 145      49.505 -13.243   8.611  1.00 50.97           N
ANISOU 1045  N   MET B 145     4402   7986   6978  -1053   -370    243       N
ATOM   1046  CA  MET B 145      48.081 -12.973   8.725  1.00 49.45           C
ANISOU 1046  CA  MET B 145     4436   7667   6684   -993   -391    193       C
ATOM   1047  C   MET B 145      47.260 -13.771   7.718  1.00 48.15           C
ANISOU 1047  C   MET B 145     4339   7594   6361   -880   -235    215       C
ATOM   1048  O   MET B 145      47.634 -13.886   6.545  1.00 48.83           O
ANISOU 1048  O   MET B 145     4339   7792   6423   -898    -99    321       O
ATOM   1049  CB  MET B 145      47.787 -11.483   8.537  1.00 50.46           C
ANISOU 1049  CB  MET B 145     4642   7623   6908  -1127   -455    261       C
ATOM   1050  CG  MET B 145      46.350 -11.121   8.884  1.00 49.19           C
ANISOU 1050  CG  MET B 145     4702   7331   6657  -1041   -511    180       C
ATOM   1051  SD  MET B 145      45.799  -9.515   8.286  1.00 50.38           S
ANISOU 1051  SD  MET B 145     4975   7281   6887  -1143   -553    281       S
ATOM   1052  CE  MET B 145      46.753  -8.348   9.256  1.00 52.58           C
ANISOU 1052  CE  MET B 145     5213   7375   7392  -1311   -754    250       C
ATOM   1053  N   ILE B 146      46.133 -14.297   8.198  1.00 46.51           N
ANISOU 1053  N   ILE B 146     4282   7345   6045   -766   -258    111       N
ATOM   1054  CA  ILE B 146      45.183 -15.030   7.385  1.00 45.36           C
ANISOU 1054  CA  ILE B 146     4213   7259   5765   -667   -148    101       C
ATOM   1055  C   ILE B 146      43.841 -14.307   7.444  1.00 44.67           C
ANISOU 1055  C   ILE B 146     4282   7058   5634   -655   -191     75       C
ATOM   1056  O   ILE B 146      43.392 -13.907   8.516  1.00 44.38           O
ANISOU 1056  O   ILE B 146     4325   6921   5617   -646   -297     -3       O
ATOM   1057  CB  ILE B 146      45.028 -16.467   7.904  1.00 44.38           C
ANISOU 1057  CB  ILE B 146     4103   7191   5570   -547   -133      1       C
ATOM   1058  CG1 ILE B 146      46.335 -17.237   7.682  1.00 45.27           C
ANISOU 1058  CG1 ILE B 146     4058   7425   5717   -521    -85     23       C
ATOM   1059  CG2 ILE B 146      43.861 -17.172   7.215  1.00 43.33           C
ANISOU 1059  CG2 ILE B 146     4063   7081   5319   -464    -54    -37       C
ATOM   1060  CD1 ILE B 146      46.394 -18.578   8.386  1.00 44.73           C
ANISOU 1060  CD1 ILE B 146     4011   7375   5609   -402   -103    -64       C
ATOM   1061  N   ALA B 147      43.211 -14.123   6.290  1.00 44.65           N
ANISOU 1061  N   ALA B 147     4320   7086   5561   -638   -114    134       N
ATOM   1062  CA  ALA B 147      41.935 -13.412   6.217  1.00 44.25           C
ANISOU 1062  CA  ALA B 147     4400   6943   5469   -607   -158    114       C
ATOM   1063  C   ALA B 147      40.878 -14.295   5.583  1.00 43.29           C
ANISOU 1063  C   ALA B 147     4321   6907   5220   -503    -92     57       C
ATOM   1064  O   ALA B 147      41.170 -15.041   4.652  1.00 43.42           O
ANISOU 1064  O   ALA B 147     4286   7040   5171   -474      0     82       O
ATOM   1065  CB  ALA B 147      42.080 -12.116   5.436  1.00 45.62           C
ANISOU 1065  CB  ALA B 147     4599   7043   5690   -685   -166    249       C
ATOM   1066  N   THR B 148      39.645 -14.179   6.070  1.00 42.60           N
ANISOU 1066  N   THR B 148     4320   6766   5100   -444   -143    -28       N
ATOM   1067  CA  THR B 148      38.573 -15.061   5.652  1.00 41.84           C
ANISOU 1067  CA  THR B 148     4243   6743   4911   -364   -101   -101       C
ATOM   1068  C   THR B 148      37.437 -14.321   4.974  1.00 42.13           C
ANISOU 1068  C   THR B 148     4342   6767   4899   -316   -129    -94       C
ATOM   1069  O   THR B 148      37.071 -13.236   5.400  1.00 42.52           O
ANISOU 1069  O   THR B 148     4449   6717   4989   -313   -203    -85       O
ATOM   1070  CB  THR B 148      37.941 -15.744   6.898  1.00 41.02           C
ANISOU 1070  CB  THR B 148     4158   6618   4809   -332   -124   -212       C
ATOM   1071  OG1 THR B 148      38.900 -16.581   7.564  1.00 40.86           O
ANISOU 1071  OG1 THR B 148     4096   6611   4819   -351   -108   -221       O
ATOM   1072  CG2 THR B 148      36.754 -16.552   6.485  1.00 40.59           C
ANISOU 1072  CG2 THR B 148     4108   6623   4692   -280    -89   -282       C
ATOM   1073  N   GLY B 149      36.852 -14.940   3.952  1.00 42.11           N
ANISOU 1073  N   GLY B 149     4331   6862   4806   -263    -87   -115       N
ATOM   1074  CA  GLY B 149      35.609 -14.459   3.362  1.00 42.42           C
ANISOU 1074  CA  GLY B 149     4416   6915   4788   -192   -131   -136       C
ATOM   1075  C   GLY B 149      34.746 -15.627   2.950  1.00 42.08           C
ANISOU 1075  C   GLY B 149     4336   6970   4681   -143   -112   -246       C
ATOM   1076  O   GLY B 149      35.223 -16.756   2.881  1.00 41.76           O
ANISOU 1076  O   GLY B 149     4258   6976   4633   -162    -59   -287       O
ATOM   1077  N   ASP B 150      33.470 -15.365   2.670  1.00 42.36           N
ANISOU 1077  N   ASP B 150     4379   7032   4682    -78   -167   -302       N
ATOM   1078  CA  ASP B 150      32.540 -16.431   2.269  1.00 42.34           C
ANISOU 1078  CA  ASP B 150     4326   7120   4643    -49   -171   -421       C
ATOM   1079  C   ASP B 150      32.586 -16.697   0.768  1.00 43.18           C
ANISOU 1079  C   ASP B 150     4445   7327   4633      3   -175   -414       C
ATOM   1080  O   ASP B 150      31.568 -16.988   0.148  1.00 43.75           O
ANISOU 1080  O   ASP B 150     4494   7474   4656     57   -232   -501       O
ATOM   1081  CB  ASP B 150      31.108 -16.117   2.730  1.00 42.52           C
ANISOU 1081  CB  ASP B 150     4313   7152   4692     -3   -230   -501       C
ATOM   1082  CG  ASP B 150      30.622 -17.059   3.819  1.00 41.99           C
ANISOU 1082  CG  ASP B 150     4179   7080   4696    -58   -192   -590       C
ATOM   1083  OD1 ASP B 150      31.316 -18.060   4.103  1.00 41.51           O
ANISOU 1083  OD1 ASP B 150     4115   6997   4660   -124   -135   -595       O
ATOM   1084  OD2 ASP B 150      29.534 -16.817   4.385  1.00 42.27           O
ANISOU 1084  OD2 ASP B 150     4163   7140   4760    -29   -213   -647       O
ATOM   1085  N   SER B 151      33.780 -16.634   0.190  1.00 43.49           N
ANISOU 1085  N   SER B 151     4513   7389   4625    -10   -116   -319       N
ATOM   1086  CA  SER B 151      33.959 -16.877  -1.221  1.00 44.55           C
ANISOU 1086  CA  SER B 151     4669   7643   4616     55   -100   -304       C
ATOM   1087  C   SER B 151      35.274 -17.599  -1.479  1.00 44.66           C
ANISOU 1087  C   SER B 151     4660   7702   4605     33     -1   -279       C
ATOM   1088  O   SER B 151      36.251 -17.417  -0.746  1.00 44.19           O
ANISOU 1088  O   SER B 151     4575   7580   4634    -37     52   -205       O
ATOM   1089  CB  SER B 151      33.918 -15.547  -1.970  1.00 45.65           C
ANISOU 1089  CB  SER B 151     4876   7794   4674    102   -126   -158       C
ATOM   1090  OG  SER B 151      32.636 -14.955  -1.871  1.00 45.85           O
ANISOU 1090  OG  SER B 151     4918   7794   4707    162   -231   -201       O
ATOM   1091  N   PHE B 152      35.281 -18.426  -2.522  1.00 45.49           N
ANISOU 1091  N   PHE B 152     4771   7925   4589    106     14   -356       N
ATOM   1092  CA  PHE B 152      36.513 -19.018  -3.040  1.00 46.12           C
ANISOU 1092  CA  PHE B 152     4831   8087   4604    130    115   -334       C
ATOM   1093  C   PHE B 152      37.152 -18.004  -3.981  1.00 47.44           C
ANISOU 1093  C   PHE B 152     5025   8354   4646    157    182   -153       C
ATOM   1094  O   PHE B 152      36.571 -17.660  -5.019  1.00 48.58           O
ANISOU 1094  O   PHE B 152     5229   8594   4636    241    148   -135       O
ATOM   1095  CB  PHE B 152      36.224 -20.325  -3.776  1.00 46.80           C
ANISOU 1095  CB  PHE B 152     4927   8252   4602    217     94   -514       C
ATOM   1096  CG  PHE B 152      37.457 -21.115  -4.106  1.00 47.45           C
ANISOU 1096  CG  PHE B 152     4983   8406   4641    266    194   -532       C
ATOM   1097  CD1 PHE B 152      38.125 -21.815  -3.115  1.00 46.62           C
ANISOU 1097  CD1 PHE B 152     4832   8204   4679    219    225   -565       C
ATOM   1098  CD2 PHE B 152      37.948 -21.163  -5.403  1.00 49.13           C
ANISOU 1098  CD2 PHE B 152     5216   8795   4656    378    257   -518       C
ATOM   1099  CE1 PHE B 152      39.257 -22.547  -3.411  1.00 47.43           C
ANISOU 1099  CE1 PHE B 152     4899   8377   4746    289    309   -591       C
ATOM   1100  CE2 PHE B 152      39.081 -21.895  -5.708  1.00 49.99           C
ANISOU 1100  CE2 PHE B 152     5286   8991   4719    448    358   -547       C
ATOM   1101  CZ  PHE B 152      39.739 -22.587  -4.709  1.00 49.11           C
ANISOU 1101  CZ  PHE B 152     5117   8774   4770    406    380   -588       C
ATOM   1102  N   MET B 153      38.323 -17.500  -3.602  1.00 47.52           N
ANISOU 1102  N   MET B 153     4987   8342   4726     82    269     -9       N
ATOM   1103  CA  MET B 153      38.992 -16.436  -4.365  1.00 49.02           C
ANISOU 1103  CA  MET B 153     5190   8602   4835     65    348    203       C
ATOM   1104  C   MET B 153      39.694 -16.954  -5.627  1.00 50.75           C
ANISOU 1104  C   MET B 153     5390   9035   4857    162    467    227       C
ATOM   1105  O   MET B 153      40.914 -17.079  -5.660  1.00 51.45           O
ANISOU 1105  O   MET B 153     5388   9199   4962    131    589    306       O
ATOM   1106  CB  MET B 153      39.995 -15.688  -3.485  1.00 48.83           C
ANISOU 1106  CB  MET B 153     5099   8473   4981    -75    390    344       C
ATOM   1107  CG  MET B 153      39.437 -15.159  -2.175  1.00 47.40           C
ANISOU 1107  CG  MET B 153     4942   8092   4977   -154    276    308       C
ATOM   1108  SD  MET B 153      38.109 -13.971  -2.372  1.00 47.66           S
ANISOU 1108  SD  MET B 153     5100   8026   4984   -121    160    357       S
ATOM   1109  CE  MET B 153      38.902 -12.371  -2.307  1.00 49.03           C
ANISOU 1109  CE  MET B 153     5303   8074   5253   -241    175    602       C
ATOM   1110  N   SER B 154      38.914 -17.257  -6.659  1.00 51.64           N
ANISOU 1110  N   SER B 154     5581   9262   4778    290    427    149       N
ATOM   1111  CA  SER B 154      39.453 -17.655  -7.959  1.00 53.65           C
ANISOU 1111  CA  SER B 154     5845   9743   4797    414    532    164       C
ATOM   1112  C   SER B 154      39.488 -16.479  -8.944  1.00 55.59           C
ANISOU 1112  C   SER B 154     6163  10087   4872    435    586    400       C
ATOM   1113  O   SER B 154      40.268 -16.485  -9.897  1.00 57.60           O
ANISOU 1113  O   SER B 154     6404  10538   4942    500    728    506       O
ATOM   1114  CB  SER B 154      38.639 -18.813  -8.541  1.00 53.87           C
ANISOU 1114  CB  SER B 154     5926   9847   4697    557    441    -90       C
ATOM   1115  OG  SER B 154      37.250 -18.569  -8.439  1.00 53.23           O
ANISOU 1115  OG  SER B 154     5912   9679   4635    563    277   -169       O
ATOM   1116  N   ASP B 155      38.649 -15.474  -8.705  1.00 55.22           N
ANISOU 1116  N   ASP B 155     6194   9904   4882    390    478    490       N
ATOM   1117  CA  ASP B 155      38.587 -14.284  -9.549  1.00 57.18           C
ANISOU 1117  CA  ASP B 155     6537  10196   4991    409    506    734       C
ATOM   1118  C   ASP B 155      39.754 -13.332  -9.243  1.00 57.96           C
ANISOU 1118  C   ASP B 155     6581  10228   5213    246    639   1001       C
ATOM   1119  O   ASP B 155      39.894 -12.871  -8.108  1.00 56.60           O
ANISOU 1119  O   ASP B 155     6366   9849   5289    105    590   1020       O
ATOM   1120  CB  ASP B 155      37.255 -13.568  -9.318  1.00 56.62           C
ANISOU 1120  CB  ASP B 155     6568   9980   4965    435    324    716       C
ATOM   1121  CG  ASP B 155      37.096 -12.323 -10.168  1.00 58.81           C
ANISOU 1121  CG  ASP B 155     6971  10270   5103    474    326    973       C
ATOM   1122  OD1 ASP B 155      37.860 -12.135 -11.144  1.00 60.98           O
ANISOU 1122  OD1 ASP B 155     7271  10710   5189    502    469   1156       O
ATOM   1123  OD2 ASP B 155      36.194 -11.523  -9.845  1.00 58.55           O
ANISOU 1123  OD2 ASP B 155     7016  10082   5147    485    186   1000       O
ATOM   1124  N   PRO B 156      40.600 -13.043 -10.248  1.00 60.41           N
ANISOU 1124  N   PRO B 156     6885  10719   5348    262    806   1206       N
ATOM   1125  CA  PRO B 156      41.720 -12.114 -10.051  1.00 61.67           C
ANISOU 1125  CA  PRO B 156     6973  10825   5636     83    939   1481       C
ATOM   1126  C   PRO B 156      41.300 -10.732  -9.554  1.00 61.74           C
ANISOU 1126  C   PRO B 156     7079  10568   5813    -40    833   1656       C
ATOM   1127  O   PRO B 156      42.027 -10.117  -8.777  1.00 61.70           O
ANISOU 1127  O   PRO B 156     6996  10403   6042   -226    857   1768       O
ATOM   1128  CB  PRO B 156      42.334 -11.996 -11.453  1.00 64.79           C
ANISOU 1128  CB  PRO B 156     7382  11489   5747    161   1128   1682       C
ATOM   1129  CG  PRO B 156      41.976 -13.263 -12.138  1.00 64.73           C
ANISOU 1129  CG  PRO B 156     7390  11707   5497    378   1125   1436       C
ATOM   1130  CD  PRO B 156      40.640 -13.675 -11.582  1.00 62.34           C
ANISOU 1130  CD  PRO B 156     7170  11249   5269    445    891   1174       C
ATOM   1131  N   ASN B 157      40.144 -10.252 -10.004  1.00 62.09           N
ANISOU 1131  N   ASN B 157     7289  10560   5742     73    704   1666       N
ATOM   1132  CA  ASN B 157      39.654  -8.935  -9.606  1.00 62.46           C
ANISOU 1132  CA  ASN B 157     7453  10346   5934     -2    587   1818       C
ATOM   1133  C   ASN B 157      39.329  -8.881  -8.126  1.00 59.95           C
ANISOU 1133  C   ASN B 157     7089   9784   5903    -91    448   1642       C
ATOM   1134  O   ASN B 157      39.677  -7.907  -7.449  1.00 60.27           O
ANISOU 1134  O   ASN B 157     7146   9600   6155   -239    415   1768       O
ATOM   1135  CB  ASN B 157      38.414  -8.561 -10.406  1.00 63.43           C
ANISOU 1135  CB  ASN B 157     7752  10490   5856    182    460   1832       C
ATOM   1136  CG  ASN B 157      38.697  -8.430 -11.889  1.00 66.39           C
ANISOU 1136  CG  ASN B 157     8209  11099   5917    282    586   2042       C
ATOM   1137  OD1 ASN B 157      39.837  -8.591 -12.338  1.00 67.83           O
ANISOU 1137  OD1 ASN B 157     8308  11436   6030    209    790   2190       O
ATOM   1138  ND2 ASN B 157      37.659  -8.133 -12.662  1.00 67.55           N
ANISOU 1138  ND2 ASN B 157     8513  11291   5860    463    466   2059       N
ATOM   1139  N   ARG B 158      38.669  -9.934  -7.639  1.00 57.70           N
ANISOU 1139  N   ARG B 158     6756   9548   5621     -1    368   1352       N
ATOM   1140  CA  ARG B 158      38.356 -10.090  -6.216  1.00 55.37           C
ANISOU 1140  CA  ARG B 158     6407   9071   5559    -66    260   1169       C
ATOM   1141  C   ARG B 158      39.647 -10.087  -5.394  1.00 55.02           C
ANISOU 1141  C   ARG B 158     6237   8961   5708   -244    346   1218       C
ATOM   1142  O   ARG B 158      39.720  -9.457  -4.333  1.00 54.38           O
ANISOU 1142  O   ARG B 158     6156   8669   5838   -350    264   1213       O
ATOM   1143  CB  ARG B 158      37.557 -11.394  -5.972  1.00 53.48           C
ANISOU 1143  CB  ARG B 158     6120   8930   5269     45    198    879       C
ATOM   1144  CG  ARG B 158      36.043 -11.313  -6.177  1.00 53.25           C
ANISOU 1144  CG  ARG B 158     6177   8891   5167    186     45    761       C
ATOM   1145  CD  ARG B 158      35.369 -10.323  -5.224  1.00 52.70           C
ANISOU 1145  CD  ARG B 158     6159   8594   5272    159    -82    764       C
ATOM   1146  NE  ARG B 158      35.405 -10.695  -3.793  1.00 50.70           N
ANISOU 1146  NE  ARG B 158     5822   8226   5218     75   -109    610       N
ATOM   1147  CZ  ARG B 158      34.608 -11.605  -3.233  1.00 49.21           C
ANISOU 1147  CZ  ARG B 158     5570   8074   5052    121   -161    391       C
ATOM   1148  NH1 ARG B 158      33.708 -12.264  -3.962  1.00 49.41           N
ANISOU 1148  NH1 ARG B 158     5592   8239   4942    237   -206    276       N
ATOM   1149  NH2 ARG B 158      34.709 -11.859  -1.937  1.00 47.74           N
ANISOU 1149  NH2 ARG B 158     5325   7789   5024     46   -171    290       N
ATOM   1150  N   VAL B 159      40.677 -10.757  -5.909  1.00 55.75           N
ANISOU 1150  N   VAL B 159     6218   9242   5721   -265    503   1260       N
ATOM   1151  CA  VAL B 159      41.968 -10.827  -5.235  1.00 55.78           C
ANISOU 1151  CA  VAL B 159     6070   9226   5898   -419    587   1305       C
ATOM   1152  C   VAL B 159      42.637  -9.451  -5.194  1.00 57.70           C
ANISOU 1152  C   VAL B 159     6323   9320   6281   -596    610   1568       C
ATOM   1153  O   VAL B 159      43.108  -9.017  -4.138  1.00 57.28           O
ANISOU 1153  O   VAL B 159     6212   9091   6461   -739    546   1558       O
ATOM   1154  CB  VAL B 159      42.899 -11.862  -5.905  1.00 56.51           C
ANISOU 1154  CB  VAL B 159     6029   9583   5859   -369    758   1289       C
ATOM   1155  CG1 VAL B 159      44.286 -11.834  -5.279  1.00 56.99           C
ANISOU 1155  CG1 VAL B 159     5907   9644   6103   -524    844   1357       C
ATOM   1156  CG2 VAL B 159      42.310 -13.259  -5.784  1.00 54.73           C
ANISOU 1156  CG2 VAL B 159     5799   9447   5547   -217    712   1010       C
ATOM   1157  N   ALA B 160      42.674  -8.767  -6.335  1.00 60.07           N
ANISOU 1157  N   ALA B 160     6704   9682   6439   -587    692   1803       N
ATOM   1158  CA  ALA B 160      43.255  -7.421  -6.419  1.00 62.40           C
ANISOU 1158  CA  ALA B 160     7029   9811   6868   -768    717   2087       C
ATOM   1159  C   ALA B 160      42.584  -6.435  -5.459  1.00 61.74           C
ANISOU 1159  C   ALA B 160     7072   9392   6996   -826    514   2052       C
ATOM   1160  O   ALA B 160      43.257  -5.627  -4.805  1.00 62.67           O
ANISOU 1160  O   ALA B 160     7152   9309   7350  -1017    479   2150       O
ATOM   1161  CB  ALA B 160      43.165  -6.904  -7.842  1.00 65.11           C
ANISOU 1161  CB  ALA B 160     7483  10275   6983   -711    827   2348       C
ATOM   1162  N   ALA B 161      41.260  -6.524  -5.361  1.00 60.33           N
ANISOU 1162  N   ALA B 161     7029   9159   6734   -654    373   1895       N
ATOM   1163  CA  ALA B 161      40.482  -5.669  -4.457  1.00 59.73           C
ANISOU 1163  CA  ALA B 161     7074   8794   6828   -655    179   1823       C
ATOM   1164  C   ALA B 161      40.898  -5.825  -2.987  1.00 58.10           C
ANISOU 1164  C   ALA B 161     6767   8453   6855   -765    103   1646       C
ATOM   1165  O   ALA B 161      40.841  -4.867  -2.208  1.00 58.58           O
ANISOU 1165  O   ALA B 161     6900   8252   7108   -844    -24   1653       O
ATOM   1166  CB  ALA B 161      38.996  -5.963  -4.615  1.00 58.48           C
ANISOU 1166  CB  ALA B 161     7025   8671   6524   -432     63   1654       C
ATOM   1167  N   ILE B 162      41.314  -7.037  -2.628  1.00 56.39           N
ANISOU 1167  N   ILE B 162     6397   8415   6612   -754    172   1485       N
ATOM   1168  CA  ILE B 162      41.729  -7.371  -1.260  1.00 54.89           C
ANISOU 1168  CA  ILE B 162     6109   8143   6602   -830    104   1313       C
ATOM   1169  C   ILE B 162      43.155  -6.912  -0.956  1.00 56.41           C
ANISOU 1169  C   ILE B 162     6175   8280   6979  -1043    152   1447       C
ATOM   1170  O   ILE B 162      43.450  -6.534   0.182  1.00 56.15           O
ANISOU 1170  O   ILE B 162     6120   8076   7138  -1137     36   1362       O
ATOM   1171  CB  ILE B 162      41.626  -8.896  -1.029  1.00 52.75           C
ANISOU 1171  CB  ILE B 162     5736   8076   6231   -726    155   1105       C
ATOM   1172  CG1 ILE B 162      40.160  -9.341  -1.174  1.00 51.38           C
ANISOU 1172  CG1 ILE B 162     5665   7937   5919   -544     85    952       C
ATOM   1173  CG2 ILE B 162      42.199  -9.311   0.326  1.00 51.54           C
ANISOU 1173  CG2 ILE B 162     5480   7864   6237   -797    100    960       C
ATOM   1174  CD1 ILE B 162      39.126  -8.662  -0.279  1.00 50.70           C
ANISOU 1174  CD1 ILE B 162     5687   7653   5923   -499    -76    847       C
ATOM   1175  N   ARG B 163      44.032  -6.981  -1.961  1.00 58.20           N
ANISOU 1175  N   ARG B 163     6306   8669   7139  -1114    321   1645       N
ATOM   1176  CA  ARG B 163      45.461  -6.642  -1.798  1.00 60.02           C
ANISOU 1176  CA  ARG B 163     6364   8898   7545  -1328    394   1786       C
ATOM   1177  C   ARG B 163      45.679  -5.302  -1.128  1.00 61.54           C
ANISOU 1177  C   ARG B 163     6617   8777   7989  -1511    255   1873       C
ATOM   1178  O   ARG B 163      46.542  -5.146  -0.259  1.00 61.97           O
ANISOU 1178  O   ARG B 163     6541   8751   8252  -1664    196   1830       O
ATOM   1179  CB  ARG B 163      46.170  -6.594  -3.154  1.00 62.46           C
ANISOU 1179  CB  ARG B 163     6595   9410   7726  -1374    610   2045       C
ATOM   1180  CG  ARG B 163      46.266  -7.935  -3.851  1.00 61.61           C
ANISOU 1180  CG  ARG B 163     6395   9631   7383  -1206    762   1956       C
ATOM   1181  CD  ARG B 163      47.470  -8.036  -4.772  1.00 64.20           C
ANISOU 1181  CD  ARG B 163     6545  10198   7650  -1287    991   2167       C
ATOM   1182  NE  ARG B 163      47.579  -9.401  -5.288  1.00 63.35           N
ANISOU 1182  NE  ARG B 163     6352  10391   7329  -1098   1111   2025       N
ATOM   1183  CZ  ARG B 163      48.038 -10.447  -4.598  1.00 61.85           C
ANISOU 1183  CZ  ARG B 163     6014  10289   7195  -1046   1100   1815       C
ATOM   1184  NH1 ARG B 163      48.468 -10.319  -3.341  1.00 60.98           N
ANISOU 1184  NH1 ARG B 163     5813  10021   7333  -1167    978   1724       N
ATOM   1185  NH2 ARG B 163      48.071 -11.640  -5.173  1.00 61.43           N
ANISOU 1185  NH2 ARG B 163     5918  10481   6943   -860   1201   1690       N
ATOM   1186  N   ASP B 164      44.870  -4.340  -1.545  1.00 62.54           N
ANISOU 1186  N   ASP B 164     6949   8719   8093  -1481    186   1986       N
ATOM   1187  CA  ASP B 164      45.029  -2.963  -1.125  1.00 64.58           C
ANISOU 1187  CA  ASP B 164     7305   8648   8585  -1646     54   2099       C
ATOM   1188  C   ASP B 164      44.379  -2.651   0.232  1.00 63.09           C
ANISOU 1188  C   ASP B 164     7219   8219   8532  -1592   -178   1844       C
ATOM   1189  O   ASP B 164      44.484  -1.524   0.717  1.00 64.81           O
ANISOU 1189  O   ASP B 164     7531   8137   8957  -1712   -320   1886       O
ATOM   1190  CB  ASP B 164      44.453  -2.055  -2.214  1.00 66.67           C
ANISOU 1190  CB  ASP B 164     7765   8808   8758  -1615     79   2347       C
ATOM   1191  CG  ASP B 164      45.036  -2.357  -3.596  1.00 68.41           C
ANISOU 1191  CG  ASP B 164     7903   9295   8795  -1642    321   2607       C
ATOM   1192  OD1 ASP B 164      46.073  -3.050  -3.679  1.00 68.57           O
ANISOU 1192  OD1 ASP B 164     7695   9538   8819  -1733    471   2624       O
ATOM   1193  OD2 ASP B 164      44.457  -1.906  -4.603  1.00 69.82           O
ANISOU 1193  OD2 ASP B 164     8245   9472   8811  -1555    361   2792       O
ATOM   1194  N   LYS B 165      43.711  -3.632   0.838  1.00 60.21           N
ANISOU 1194  N   LYS B 165     6842   7984   8053  -1413   -214   1584       N
ATOM   1195  CA  LYS B 165      43.012  -3.415   2.111  1.00 58.90           C
ANISOU 1195  CA  LYS B 165     6772   7638   7968  -1332   -407   1342       C
ATOM   1196  C   LYS B 165      43.848  -3.798   3.335  1.00 58.26           C
ANISOU 1196  C   LYS B 165     6550   7557   8029  -1427   -474   1180       C
ATOM   1197  O   LYS B 165      43.652  -3.223   4.403  1.00 58.40           O
ANISOU 1197  O   LYS B 165     6647   7371   8171  -1431   -650   1035       O
ATOM   1198  CB  LYS B 165      41.677  -4.178   2.135  1.00 56.49           C
ANISOU 1198  CB  LYS B 165     6543   7461   7461  -1084   -414   1163       C
ATOM   1199  CG  LYS B 165      40.456  -3.442   1.622  1.00 57.08           C
ANISOU 1199  CG  LYS B 165     6813   7417   7460   -940   -486   1202       C
ATOM   1200  CD  LYS B 165      40.704  -2.634   0.371  1.00 59.58           C
ANISOU 1200  CD  LYS B 165     7207   7673   7758  -1008   -422   1494       C
ATOM   1201  CE  LYS B 165      39.435  -1.968  -0.127  1.00 60.22           C
ANISOU 1201  CE  LYS B 165     7487   7648   7748   -827   -512   1522       C
ATOM   1202  NZ  LYS B 165      38.687  -2.853  -1.060  1.00 59.11           N
ANISOU 1202  NZ  LYS B 165     7330   7779   7348   -652   -419   1506       N
ATOM   1203  N   PHE B 166      44.758  -4.765   3.194  1.00 57.75           N
ANISOU 1203  N   PHE B 166     6283   7725   7933  -1481   -346   1193       N
ATOM   1204  CA  PHE B 166      45.554  -5.243   4.342  1.00 57.20           C
ANISOU 1204  CA  PHE B 166     6072   7686   7977  -1543   -417   1037       C
ATOM   1205  C   PHE B 166      47.058  -5.107   4.136  1.00 59.28           C
ANISOU 1205  C   PHE B 166     6121   8004   8398  -1760   -354   1182       C
ATOM   1206  O   PHE B 166      47.536  -4.935   3.007  1.00 60.87           O
ANISOU 1206  O   PHE B 166     6251   8295   8581  -1850   -198   1410       O
ATOM   1207  CB  PHE B 166      45.209  -6.695   4.674  1.00 54.56           C
ANISOU 1207  CB  PHE B 166     5681   7577   7472  -1370   -358    862       C
ATOM   1208  CG  PHE B 166      43.768  -6.902   5.045  1.00 52.69           C
ANISOU 1208  CG  PHE B 166     5612   7303   7104  -1178   -421    704       C
ATOM   1209  CD1 PHE B 166      43.255  -6.372   6.227  1.00 52.45           C
ANISOU 1209  CD1 PHE B 166     5691   7097   7142  -1137   -592    543       C
ATOM   1210  CD2 PHE B 166      42.921  -7.617   4.208  1.00 51.44           C
ANISOU 1210  CD2 PHE B 166     5492   7298   6755  -1034   -312    708       C
ATOM   1211  CE1 PHE B 166      41.922  -6.557   6.567  1.00 51.03           C
ANISOU 1211  CE1 PHE B 166     5637   6910   6841   -958   -630    405       C
ATOM   1212  CE2 PHE B 166      41.591  -7.808   4.545  1.00 50.00           C
ANISOU 1212  CE2 PHE B 166     5430   7096   6472   -873   -368    566       C
ATOM   1213  CZ  PHE B 166      41.088  -7.275   5.724  1.00 49.80           C
ANISOU 1213  CZ  PHE B 166     5494   6911   6517   -836   -516    423       C
ATOM   1214  N   GLU B 167      47.794  -5.187   5.241  1.00 59.48           N
ANISOU 1214  N   GLU B 167     6036   7994   8571  -1838   -476   1049       N
ATOM   1215  CA  GLU B 167      49.198  -4.783   5.272  1.00 62.00           C
ANISOU 1215  CA  GLU B 167     6145   8308   9105  -2075   -478   1162       C
ATOM   1216  C   GLU B 167      50.157  -5.736   4.551  1.00 62.30           C
ANISOU 1216  C   GLU B 167     5930   8659   9082  -2094   -270   1267       C
ATOM   1217  O   GLU B 167      50.913  -5.310   3.662  1.00 64.68           O
ANISOU 1217  O   GLU B 167     6100   9015   9460  -2259   -137   1498       O
ATOM   1218  CB  GLU B 167      49.651  -4.564   6.710  1.00 62.36           C
ANISOU 1218  CB  GLU B 167     6152   8224   9317  -2133   -704    962       C
ATOM   1219  CG  GLU B 167      51.073  -3.981   6.781  1.00 65.44           C
ANISOU 1219  CG  GLU B 167     6315   8576   9973  -2407   -746   1069       C
ATOM   1220  CD  GLU B 167      51.129  -2.551   7.290  1.00 67.87           C
ANISOU 1220  CD  GLU B 167     6734   8528  10524  -2589   -961   1066       C
ATOM   1221  OE1 GLU B 167      50.072  -1.895   7.417  1.00 67.39           O
ANISOU 1221  OE1 GLU B 167     6940   8242  10424  -2499  -1056   1015       O
ATOM   1222  OE2 GLU B 167      52.251  -2.074   7.561  1.00 70.49           O
ANISOU 1222  OE2 GLU B 167     6879   8802  11103  -2823  -1043   1108       O
ATOM   1223  N   ASN B 168      50.153  -7.001   4.948  1.00 60.21           N
ANISOU 1223  N   ASN B 168     5594   8595   8686  -1926   -240   1104       N
ATOM   1224  CA  ASN B 168      50.766  -8.036   4.120  1.00 60.17           C
ANISOU 1224  CA  ASN B 168     5405   8892   8565  -1865    -31   1176       C
ATOM   1225  C   ASN B 168      50.121  -9.371   4.438  1.00 57.35           C
ANISOU 1225  C   ASN B 168     5111   8669   8012  -1620    -17    984       C
ATOM   1226  O   ASN B 168      50.631 -10.171   5.223  1.00 56.73           O
ANISOU 1226  O   ASN B 168     4922   8677   7954  -1559    -71    847       O
ATOM   1227  CB  ASN B 168      52.296  -8.066   4.248  1.00 62.46           C
ANISOU 1227  CB  ASN B 168     5390   9307   9035  -2027     -2   1242       C
ATOM   1228  CG  ASN B 168      52.763  -8.301   5.665  1.00 62.12           C
ANISOU 1228  CG  ASN B 168     5270   9213   9119  -2029   -207   1039       C
ATOM   1229  OD1 ASN B 168      52.099  -7.905   6.626  1.00 61.12           O
ANISOU 1229  OD1 ASN B 168     5324   8879   9020  -1999   -401    892       O
ATOM   1230  ND2 ASN B 168      53.895  -8.977   5.805  1.00 63.08           N
ANISOU 1230  ND2 ASN B 168     5124   9542   9301  -2038   -167   1021       N
ATOM   1231  N   LEU B 169      48.958  -9.562   3.823  1.00 55.88           N
ANISOU 1231  N   LEU B 169     5110   8480   7642  -1484     43    981       N
ATOM   1232  CA  LEU B 169      48.187 -10.785   3.916  1.00 53.50           C
ANISOU 1232  CA  LEU B 169     4885   8285   7157  -1272     71    823       C
ATOM   1233  C   LEU B 169      48.981 -11.961   3.344  1.00 53.70           C
ANISOU 1233  C   LEU B 169     4734   8569   7100  -1192    224    827       C
ATOM   1234  O   LEU B 169      49.625 -11.832   2.300  1.00 55.42           O
ANISOU 1234  O   LEU B 169     4835   8929   7293  -1243    378    984       O
ATOM   1235  CB  LEU B 169      46.876 -10.595   3.141  1.00 52.60           C
ANISOU 1235  CB  LEU B 169     4969   8131   6885  -1174    109    850       C
ATOM   1236  CG  LEU B 169      45.809 -11.687   3.151  1.00 50.38           C
ANISOU 1236  CG  LEU B 169     4791   7921   6429   -979    120    693       C
ATOM   1237  CD1 LEU B 169      45.343 -12.031   4.556  1.00 48.78           C
ANISOU 1237  CD1 LEU B 169     4650   7617   6269   -925    -20    507       C
ATOM   1238  CD2 LEU B 169      44.632 -11.223   2.306  1.00 50.19           C
ANISOU 1238  CD2 LEU B 169     4930   7856   6283   -915    137    744       C
ATOM   1239  N   TYR B 170      48.930 -13.101   4.034  1.00 52.20           N
ANISOU 1239  N   TYR B 170     4532   8437   6862  -1058    185    657       N
ATOM   1240  CA  TYR B 170      49.663 -14.297   3.613  1.00 52.47           C
ANISOU 1240  CA  TYR B 170     4418   8691   6829   -948    303    628       C
ATOM   1241  C   TYR B 170      48.773 -15.294   2.882  1.00 51.14           C
ANISOU 1241  C   TYR B 170     4370   8603   6458   -769    391    553       C
ATOM   1242  O   TYR B 170      49.118 -15.748   1.793  1.00 52.09           O
ANISOU 1242  O   TYR B 170     4419   8902   6471   -701    542    604       O
ATOM   1243  CB  TYR B 170      50.334 -14.969   4.818  1.00 52.20           C
ANISOU 1243  CB  TYR B 170     4286   8662   6886   -908    193    500       C
ATOM   1244  CG  TYR B 170      51.747 -14.485   5.093  1.00 54.40           C
ANISOU 1244  CG  TYR B 170     4320   9004   7344  -1044    170    573       C
ATOM   1245  CD1 TYR B 170      52.093 -13.148   4.943  1.00 56.09           C
ANISOU 1245  CD1 TYR B 170     4480   9129   7701  -1257    147    710       C
ATOM   1246  CD2 TYR B 170      52.730 -15.368   5.522  1.00 55.04           C
ANISOU 1246  CD2 TYR B 170     4221   9224   7467   -962    159    503       C
ATOM   1247  CE1 TYR B 170      53.380 -12.705   5.193  1.00 58.39           C
ANISOU 1247  CE1 TYR B 170     4526   9477   8182  -1408    118    775       C
ATOM   1248  CE2 TYR B 170      54.018 -14.934   5.776  1.00 57.30           C
ANISOU 1248  CE2 TYR B 170     4253   9588   7929  -1088    127    560       C
ATOM   1249  CZ  TYR B 170      54.338 -13.603   5.611  1.00 58.97           C
ANISOU 1249  CZ  TYR B 170     4397   9717   8292  -1322    108    695       C
ATOM   1250  OH  TYR B 170      55.615 -13.164   5.871  1.00 61.50           O
ANISOU 1250  OH  TYR B 170     4443  10111   8814  -1473     67    750       O
ATOM   1251  N   ALA B 171      47.634 -15.631   3.482  1.00 49.20           N
ANISOU 1251  N   ALA B 171     4299   8234   6160   -692    296    426       N
ATOM   1252  CA  ALA B 171      46.711 -16.607   2.899  1.00 48.06           C
ANISOU 1252  CA  ALA B 171     4266   8140   5854   -542    348    334       C
ATOM   1253  C   ALA B 171      45.263 -16.200   3.082  1.00 46.73           C
ANISOU 1253  C   ALA B 171     4283   7833   5638   -535    270    289       C
ATOM   1254  O   ALA B 171      44.939 -15.405   3.961  1.00 46.32           O
ANISOU 1254  O   ALA B 171     4289   7635   5675   -608    161    285       O
ATOM   1255  CB  ALA B 171      46.951 -17.984   3.508  1.00 47.36           C
ANISOU 1255  CB  ALA B 171     4152   8084   5759   -422    328    195       C
ATOM   1256  N   VAL B 172      44.393 -16.782   2.263  1.00 46.22           N
ANISOU 1256  N   VAL B 172     4303   7824   5435   -434    319    237       N
ATOM   1257  CA  VAL B 172      42.936 -16.529   2.349  1.00 45.13           C
ANISOU 1257  CA  VAL B 172     4313   7586   5247   -408    248    179       C
ATOM   1258  C   VAL B 172      42.159 -17.840   2.362  1.00 44.13           C
ANISOU 1258  C   VAL B 172     4238   7482   5047   -300    245     28       C
ATOM   1259  O   VAL B 172      42.530 -18.803   1.687  1.00 44.58           O
ANISOU 1259  O   VAL B 172     4258   7646   5034   -220    314    -18       O
ATOM   1260  CB  VAL B 172      42.358 -15.617   1.220  1.00 45.93           C
ANISOU 1260  CB  VAL B 172     4483   7710   5259   -412    276    284       C
ATOM   1261  CG1 VAL B 172      43.020 -14.250   1.261  1.00 47.18           C
ANISOU 1261  CG1 VAL B 172     4614   7796   5515   -541    267    450       C
ATOM   1262  CG2 VAL B 172      42.461 -16.257  -0.161  1.00 46.82           C
ANISOU 1262  CG2 VAL B 172     4580   8000   5209   -319    385    294       C
ATOM   1263  N   GLU B 173      41.088 -17.880   3.140  1.00 43.01           N
ANISOU 1263  N   GLU B 173     4179   7236   4928   -298    164    -53       N
ATOM   1264  CA  GLU B 173      40.208 -19.028   3.117  1.00 42.37           C
ANISOU 1264  CA  GLU B 173     4144   7157   4799   -228    158   -180       C
ATOM   1265  C   GLU B 173      38.794 -18.651   3.575  1.00 41.65           C
ANISOU 1265  C   GLU B 173     4125   6990   4711   -237     91   -230       C
ATOM   1266  O   GLU B 173      38.363 -17.520   3.328  1.00 41.87           O
ANISOU 1266  O   GLU B 173     4184   6998   4728   -254     59   -172       O
ATOM   1267  CB  GLU B 173      40.837 -20.216   3.866  1.00 42.16           C
ANISOU 1267  CB  GLU B 173     4086   7109   4822   -200    165   -243       C
ATOM   1268  CG  GLU B 173      41.505 -19.895   5.189  1.00 41.92           C
ANISOU 1268  CG  GLU B 173     4030   7011   4889   -249    116   -209       C
ATOM   1269  CD  GLU B 173      40.568 -19.215   6.156  1.00 41.20           C
ANISOU 1269  CD  GLU B 173     4009   6823   4823   -291     45   -223       C
ATOM   1270  OE1 GLU B 173      40.488 -17.977   6.111  1.00 41.40           O
ANISOU 1270  OE1 GLU B 173     4043   6821   4867   -339     12   -167       O
ATOM   1271  OE2 GLU B 173      39.913 -19.912   6.966  1.00 40.67           O
ANISOU 1271  OE2 GLU B 173     3990   6707   4756   -273     27   -286       O
ATOM   1272  N   MET B 174      38.062 -19.577   4.202  1.00 41.06           N
ANISOU 1272  N   MET B 174     4072   6874   4654   -224     73   -328       N
ATOM   1273  CA  MET B 174      36.635 -19.370   4.449  1.00 40.72           C
ANISOU 1273  CA  MET B 174     4063   6803   4605   -224     30   -384       C
ATOM   1274  C   MET B 174      36.138 -19.775   5.836  1.00 40.19           C
ANISOU 1274  C   MET B 174     4008   6667   4594   -250     16   -425       C
ATOM   1275  O   MET B 174      34.931 -19.862   6.031  1.00 40.16           O
ANISOU 1275  O   MET B 174     4005   6665   4589   -251      4   -479       O
ATOM   1276  CB  MET B 174      35.813 -20.103   3.377  1.00 41.12           C
ANISOU 1276  CB  MET B 174     4114   6916   4594   -184     31   -468       C
ATOM   1277  CG  MET B 174      36.104 -19.668   1.943  1.00 41.92           C
ANISOU 1277  CG  MET B 174     4220   7113   4594   -133     43   -430       C
ATOM   1278  SD  MET B 174      35.174 -20.542   0.658  1.00 42.74           S
ANISOU 1278  SD  MET B 174     4334   7304   4601    -65     13   -560       S
ATOM   1279  CE  MET B 174      33.478 -20.098   1.005  1.00 42.58           C
ANISOU 1279  CE  MET B 174     4300   7263   4615    -79    -72   -619       C
ATOM   1280  N   GLU B 175      37.020 -19.990   6.811  1.00 40.03           N
ANISOU 1280  N   GLU B 175     3992   6604   4615   -266     19   -394       N
ATOM   1281  CA  GLU B 175      36.565 -20.342   8.177  1.00 39.81           C
ANISOU 1281  CA  GLU B 175     3993   6527   4608   -279     13   -415       C
ATOM   1282  C   GLU B 175      37.287 -19.656   9.334  1.00 39.81           C
ANISOU 1282  C   GLU B 175     4013   6492   4623   -281    -30   -377       C
ATOM   1283  O   GLU B 175      36.671 -19.376  10.357  1.00 39.83           O
ANISOU 1283  O   GLU B 175     4050   6477   4606   -273    -45   -396       O
ATOM   1284  CB  GLU B 175      36.627 -21.856   8.402  1.00 39.97           C
ANISOU 1284  CB  GLU B 175     4025   6517   4647   -280     50   -440       C
ATOM   1285  CG  GLU B 175      35.678 -22.673   7.537  1.00 40.27           C
ANISOU 1285  CG  GLU B 175     4051   6562   4688   -292     70   -508       C
ATOM   1286  CD  GLU B 175      36.253 -23.034   6.178  1.00 40.60           C
ANISOU 1286  CD  GLU B 175     4078   6642   4706   -252     73   -541       C
ATOM   1287  OE1 GLU B 175      37.471 -23.266   6.080  1.00 40.76           O
ANISOU 1287  OE1 GLU B 175     4093   6667   4727   -215     86   -512       O
ATOM   1288  OE2 GLU B 175      35.470 -23.089   5.206  1.00 40.91           O
ANISOU 1288  OE2 GLU B 175     4104   6723   4716   -247     61   -603       O
ATOM   1289  N   ALA B 176      38.587 -19.408   9.185  1.00 40.04           N
ANISOU 1289  N   ALA B 176     4011   6521   4682   -289    -52   -332       N
ATOM   1290  CA  ALA B 176      39.443 -18.971  10.282  1.00 40.33           C
ANISOU 1290  CA  ALA B 176     4052   6526   4744   -294   -115   -314       C
ATOM   1291  C   ALA B 176      38.870 -17.858  11.143  1.00 40.43           C
ANISOU 1291  C   ALA B 176     4119   6498   4744   -294   -179   -341       C
ATOM   1292  O   ALA B 176      38.937 -17.927  12.363  1.00 40.66           O
ANISOU 1292  O   ALA B 176     4190   6513   4745   -267   -219   -365       O
ATOM   1293  CB  ALA B 176      40.811 -18.565   9.744  1.00 40.86           C
ANISOU 1293  CB  ALA B 176     4041   6616   4868   -325   -134   -260       C
ATOM   1294  N   ALA B 177      38.288 -16.846  10.515  1.00 40.47           N
ANISOU 1294  N   ALA B 177     4135   6486   4757   -304   -193   -341       N
ATOM   1295  CA  ALA B 177      37.849 -15.659  11.241  1.00 40.89           C
ANISOU 1295  CA  ALA B 177     4246   6480   4810   -285   -270   -379       C
ATOM   1296  C   ALA B 177      36.587 -15.970  12.026  1.00 40.75           C
ANISOU 1296  C   ALA B 177     4268   6497   4719   -221   -238   -446       C
ATOM   1297  O   ALA B 177      36.395 -15.444  13.120  1.00 41.24           O
ANISOU 1297  O   ALA B 177     4383   6540   4746   -175   -288   -498       O
ATOM   1298  CB  ALA B 177      37.621 -14.497  10.291  1.00 41.26           C
ANISOU 1298  CB  ALA B 177     4304   6479   4895   -301   -301   -346       C
ATOM   1299  N   ALA B 178      35.727 -16.821  11.469  1.00 40.35           N
ANISOU 1299  N   ALA B 178     4183   6504   4642   -218   -155   -449       N
ATOM   1300  CA  ALA B 178      34.555 -17.306  12.194  1.00 40.48           C
ANISOU 1300  CA  ALA B 178     4203   6572   4604   -183    -99   -492       C
ATOM   1301  C   ALA B 178      34.996 -18.079  13.440  1.00 40.72           C
ANISOU 1301  C   ALA B 178     4271   6610   4591   -178    -78   -475       C
ATOM   1302  O   ALA B 178      34.460 -17.873  14.527  1.00 41.28           O
ANISOU 1302  O   ALA B 178     4379   6715   4592   -128    -68   -505       O
ATOM   1303  CB  ALA B 178      33.695 -18.187  11.301  1.00 40.27           C
ANISOU 1303  CB  ALA B 178     4117   6595   4591   -211    -29   -497       C
ATOM   1304  N   VAL B 179      35.981 -18.954  13.276  1.00 40.51           N
ANISOU 1304  N   VAL B 179     4238   6560   4593   -211    -73   -428       N
ATOM   1305  CA  VAL B 179      36.504 -19.723  14.396  1.00 40.93           C
ANISOU 1305  CA  VAL B 179     4338   6610   4602   -191    -70   -396       C
ATOM   1306  C   VAL B 179      37.056 -18.759  15.449  1.00 41.48           C
ANISOU 1306  C   VAL B 179     4459   6676   4624   -142   -166   -428       C
ATOM   1307  O   VAL B 179      36.705 -18.851  16.626  1.00 42.14           O
ANISOU 1307  O   VAL B 179     4603   6796   4610    -88   -158   -437       O
ATOM   1308  CB  VAL B 179      37.600 -20.720  13.949  1.00 40.81           C
ANISOU 1308  CB  VAL B 179     4304   6564   4638   -207    -72   -350       C
ATOM   1309  CG1 VAL B 179      38.247 -21.395  15.155  1.00 41.48           C
ANISOU 1309  CG1 VAL B 179     4449   6639   4672   -162    -98   -310       C
ATOM   1310  CG2 VAL B 179      37.019 -21.767  13.007  1.00 40.58           C
ANISOU 1310  CG2 VAL B 179     4248   6522   4649   -243      7   -345       C
ATOM   1311  N   ALA B 180      37.905 -17.833  15.009  1.00 41.45           N
ANISOU 1311  N   ALA B 180     4431   6629   4688   -163   -258   -444       N
ATOM   1312  CA  ALA B 180      38.573 -16.898  15.903  1.00 42.23           C
ANISOU 1312  CA  ALA B 180     4570   6699   4774   -135   -381   -491       C
ATOM   1313  C   ALA B 180      37.584 -15.998  16.619  1.00 42.78           C
ANISOU 1313  C   ALA B 180     4710   6774   4769    -68   -403   -573       C
ATOM   1314  O   ALA B 180      37.674 -15.802  17.825  1.00 43.65           O
ANISOU 1314  O   ALA B 180     4891   6907   4788      2   -461   -625       O
ATOM   1315  CB  ALA B 180      39.583 -16.061  15.132  1.00 42.36           C
ANISOU 1315  CB  ALA B 180     4528   6654   4912   -206   -464   -478       C
ATOM   1316  N   GLN B 181      36.630 -15.464  15.870  1.00 42.46           N
ANISOU 1316  N   GLN B 181     4653   6725   4755    -68   -362   -591       N
ATOM   1317  CA  GLN B 181      35.617 -14.580  16.433  1.00 43.15           C
ANISOU 1317  CA  GLN B 181     4792   6823   4778     22   -378   -679       C
ATOM   1318  C   GLN B 181      34.787 -15.284  17.501  1.00 43.65           C
ANISOU 1318  C   GLN B 181     4880   7002   4703     95   -284   -694       C
ATOM   1319  O   GLN B 181      34.467 -14.689  18.526  1.00 44.71           O
ANISOU 1319  O   GLN B 181     5081   7169   4737    196   -319   -776       O
ATOM   1320  CB  GLN B 181      34.726 -14.039  15.324  1.00 42.83           C
ANISOU 1320  CB  GLN B 181     4714   6766   4795     21   -349   -682       C
ATOM   1321  CG  GLN B 181      33.739 -12.971  15.751  1.00 43.76           C
ANISOU 1321  CG  GLN B 181     4878   6880   4870    136   -386   -783       C
ATOM   1322  CD  GLN B 181      32.935 -12.418  14.577  1.00 43.61           C
ANISOU 1322  CD  GLN B 181     4821   6838   4912    151   -380   -776       C
ATOM   1323  OE1 GLN B 181      33.437 -12.302  13.456  1.00 43.12           O
ANISOU 1323  OE1 GLN B 181     4738   6712   4933     73   -403   -702       O
ATOM   1324  NE2 GLN B 181      31.685 -12.069  14.834  1.00 44.29           N
ANISOU 1324  NE2 GLN B 181     4892   6993   4943    264   -348   -850       N
ATOM   1325  N   VAL B 182      34.448 -16.547  17.277  1.00 43.16           N
ANISOU 1325  N   VAL B 182     4768   6999   4631     46   -162   -613       N
ATOM   1326  CA  VAL B 182      33.715 -17.313  18.298  1.00 43.93           C
ANISOU 1326  CA  VAL B 182     4886   7202   4605     88    -53   -588       C
ATOM   1327  C   VAL B 182      34.612 -17.492  19.528  1.00 44.73           C
ANISOU 1327  C   VAL B 182     5082   7314   4600    142   -114   -579       C
ATOM   1328  O   VAL B 182      34.221 -17.157  20.650  1.00 45.95           O
ANISOU 1328  O   VAL B 182     5301   7548   4608    244   -107   -626       O
ATOM   1329  CB  VAL B 182      33.223 -18.683  17.765  1.00 43.52           C
ANISOU 1329  CB  VAL B 182     4767   7172   4597     -3     77   -493       C
ATOM   1330  CG1 VAL B 182      32.700 -19.561  18.893  1.00 44.65           C
ANISOU 1330  CG1 VAL B 182     4943   7400   4624     13    192   -424       C
ATOM   1331  CG2 VAL B 182      32.147 -18.487  16.715  1.00 43.16           C
ANISOU 1331  CG2 VAL B 182     4622   7150   4628    -36    126   -525       C
ATOM   1332  N   CYS B 183      35.811 -18.020  19.295  1.00 44.28           N
ANISOU 1332  N   CYS B 183     5028   7190   4605     91   -178   -525       N
ATOM   1333  CA  CYS B 183      36.805 -18.215  20.349  1.00 45.12           C
ANISOU 1333  CA  CYS B 183     5212   7307   4626    147   -268   -517       C
ATOM   1334  C   CYS B 183      37.110 -16.924  21.096  1.00 46.09           C
ANISOU 1334  C   CYS B 183     5397   7425   4689    228   -412   -645       C
ATOM   1335  O   CYS B 183      37.265 -16.927  22.313  1.00 47.36           O
ANISOU 1335  O   CYS B 183     5648   7651   4695    326   -457   -675       O
ATOM   1336  CB  CYS B 183      38.087 -18.782  19.758  1.00 44.56           C
ANISOU 1336  CB  CYS B 183     5097   7166   4668     86   -333   -462       C
ATOM   1337  SG  CYS B 183      37.967 -20.522  19.300  1.00 44.15           S
ANISOU 1337  SG  CYS B 183     5025   7100   4649     37   -200   -329       S
ATOM   1338  N   HIS B 184      37.181 -15.823  20.362  1.00 45.70           N
ANISOU 1338  N   HIS B 184     5314   7293   4758    194   -491   -719       N
ATOM   1339  CA  HIS B 184      37.336 -14.510  20.962  1.00 46.82           C
ANISOU 1339  CA  HIS B 184     5524   7391   4874    263   -639   -857       C
ATOM   1340  C   HIS B 184      36.283 -14.280  22.029  1.00 48.02           C
ANISOU 1340  C   HIS B 184     5759   7650   4835    407   -585   -935       C
ATOM   1341  O   HIS B 184      36.608 -13.908  23.152  1.00 49.46           O
ANISOU 1341  O   HIS B 184     6036   7867   4888    509   -687  -1026       O
ATOM   1342  CB  HIS B 184      37.229 -13.414  19.901  1.00 46.39           C
ANISOU 1342  CB  HIS B 184     5432   7215   4980    204   -694   -896       C
ATOM   1343  CG  HIS B 184      37.400 -12.030  20.444  1.00 47.79           C
ANISOU 1343  CG  HIS B 184     5693   7298   5165    265   -863  -1042       C
ATOM   1344  ND1 HIS B 184      36.336 -11.247  20.835  1.00 48.65           N
ANISOU 1344  ND1 HIS B 184     5872   7417   5195    391   -859  -1155       N
ATOM   1345  CD2 HIS B 184      38.513 -11.293  20.668  1.00 48.73           C
ANISOU 1345  CD2 HIS B 184     5836   7305   5374    219  -1051  -1105       C
ATOM   1346  CE1 HIS B 184      36.783 -10.084  21.272  1.00 50.06           C
ANISOU 1346  CE1 HIS B 184     6136   7474   5412    429  -1044  -1288       C
ATOM   1347  NE2 HIS B 184      38.101 -10.086  21.180  1.00 50.15           N
ANISOU 1347  NE2 HIS B 184     6118   7404   5533    312  -1167  -1259       N
ATOM   1348  N   GLN B 185      35.021 -14.518  21.690  1.00 47.66           N
ANISOU 1348  N   GLN B 185     5668   7677   4764    423   -425   -905       N
ATOM   1349  CA  GLN B 185      33.932 -14.237  22.618  1.00 49.02           C
ANISOU 1349  CA  GLN B 185     5887   7979   4760    566   -348   -980       C
ATOM   1350  C   GLN B 185      33.785 -15.262  23.732  1.00 50.02           C
ANISOU 1350  C   GLN B 185     6060   8256   4689    619   -237   -899       C
ATOM   1351  O   GLN B 185      33.326 -14.928  24.831  1.00 51.70           O
ANISOU 1351  O   GLN B 185     6349   8590   4706    766   -217   -975       O
ATOM   1352  CB  GLN B 185      32.627 -14.091  21.862  1.00 48.63           C
ANISOU 1352  CB  GLN B 185     5741   7971   4764    566   -221   -979       C
ATOM   1353  CG  GLN B 185      32.660 -12.927  20.893  1.00 48.15           C
ANISOU 1353  CG  GLN B 185     5668   7767   4861    555   -340  -1058       C
ATOM   1354  CD  GLN B 185      31.334 -12.219  20.828  1.00 48.97           C
ANISOU 1354  CD  GLN B 185     5741   7935   4932    678   -286  -1149       C
ATOM   1355  OE1 GLN B 185      30.885 -11.628  21.822  1.00 50.59           O
ANISOU 1355  OE1 GLN B 185     6012   8214   4996    840   -299  -1271       O
ATOM   1356  NE2 GLN B 185      30.683 -12.271  19.660  1.00 48.08           N
ANISOU 1356  NE2 GLN B 185     5523   7808   4937    621   -231  -1102       N
ATOM   1357  N   TYR B 186      34.180 -16.499  23.458  1.00 49.22           N
ANISOU 1357  N   TYR B 186     5924   8146   4631    512   -165   -744       N
ATOM   1358  CA  TYR B 186      34.280 -17.511  24.504  1.00 50.35           C
ANISOU 1358  CA  TYR B 186     6138   8391   4599    553    -87   -637       C
ATOM   1359  C   TYR B 186      35.587 -17.405  25.307  1.00 51.14           C
ANISOU 1359  C   TYR B 186     6346   8466   4617    620   -267   -672       C
ATOM   1360  O   TYR B 186      35.741 -18.080  26.323  1.00 52.46           O
ANISOU 1360  O   TYR B 186     6604   8728   4602    693   -236   -596       O
ATOM   1361  CB  TYR B 186      34.145 -18.912  23.904  1.00 49.51           C
ANISOU 1361  CB  TYR B 186     5970   8257   4585    420     50   -459       C
ATOM   1362  CG  TYR B 186      32.714 -19.361  23.703  1.00 49.80           C
ANISOU 1362  CG  TYR B 186     5920   8383   4619    374    256   -395       C
ATOM   1363  CD1 TYR B 186      31.979 -18.936  22.609  1.00 48.77           C
ANISOU 1363  CD1 TYR B 186     5668   8225   4639    312    287   -452       C
ATOM   1364  CD2 TYR B 186      32.108 -20.226  24.604  1.00 51.38           C
ANISOU 1364  CD2 TYR B 186     6153   8701   4668    388    418   -267       C
ATOM   1365  CE1 TYR B 186      30.672 -19.355  22.423  1.00 49.30           C
ANISOU 1365  CE1 TYR B 186     5628   8387   4718    265    459   -405       C
ATOM   1366  CE2 TYR B 186      30.801 -20.646  24.434  1.00 51.99           C
ANISOU 1366  CE2 TYR B 186     6122   8869   4763    323    612   -202       C
ATOM   1367  CZ  TYR B 186      30.086 -20.209  23.342  1.00 50.92           C
ANISOU 1367  CZ  TYR B 186     5845   8711   4792    260    625   -282       C
ATOM   1368  OH  TYR B 186      28.789 -20.634  23.157  1.00 51.74           O
ANISOU 1368  OH  TYR B 186     5813   8916   4931    189    800   -228       O
ATOM   1369  N   GLU B 187      36.513 -16.564  24.846  1.00 50.56           N
ANISOU 1369  N   GLU B 187     6258   8272   4681    591   -458   -778       N
ATOM   1370  CA  GLU B 187      37.845 -16.413  25.449  1.00 51.37           C
ANISOU 1370  CA  GLU B 187     6420   8342   4757    628   -659   -827       C
ATOM   1371  C   GLU B 187      38.620 -17.733  25.483  1.00 51.15           C
ANISOU 1371  C   GLU B 187     6383   8316   4734    589   -639   -669       C
ATOM   1372  O   GLU B 187      39.184 -18.114  26.506  1.00 52.55           O
ANISOU 1372  O   GLU B 187     6653   8561   4754    686   -715   -651       O
ATOM   1373  CB  GLU B 187      37.758 -15.786  26.843  1.00 53.55           C
ANISOU 1373  CB  GLU B 187     6831   8720   4795    802   -752   -957       C
ATOM   1374  CG  GLU B 187      37.048 -14.442  26.859  1.00 54.11           C
ANISOU 1374  CG  GLU B 187     6927   8771   4863    872   -796  -1139       C
ATOM   1375  CD  GLU B 187      37.041 -13.786  28.228  1.00 56.53           C
ANISOU 1375  CD  GLU B 187     7379   9174   4926   1066   -911  -1304       C
ATOM   1376  OE1 GLU B 187      36.706 -14.465  29.223  1.00 57.86           O
ANISOU 1376  OE1 GLU B 187     7629   9517   4839   1182   -811  -1240       O
ATOM   1377  OE2 GLU B 187      37.362 -12.582  28.310  1.00 57.35           O
ANISOU 1377  OE2 GLU B 187     7526   9175   5088   1106  -1105  -1497       O
ATOM   1378  N   VAL B 188      38.637 -18.418  24.343  1.00 49.55           N
ANISOU 1378  N   VAL B 188     6081   8039   4708    463   -546   -564       N
ATOM   1379  CA  VAL B 188      39.397 -19.644  24.172  1.00 49.33           C
ANISOU 1379  CA  VAL B 188     6038   7980   4726    431   -536   -432       C
ATOM   1380  C   VAL B 188      40.563 -19.330  23.244  1.00 48.44           C
ANISOU 1380  C   VAL B 188     5813   7774   4819    352   -665   -472       C
ATOM   1381  O   VAL B 188      40.354 -18.761  22.170  1.00 47.25           O
ANISOU 1381  O   VAL B 188     5573   7560   4819    258   -639   -508       O
ATOM   1382  CB  VAL B 188      38.538 -20.755  23.538  1.00 48.53           C
ANISOU 1382  CB  VAL B 188     5905   7859   4673    352   -332   -294       C
ATOM   1383  CG1 VAL B 188      39.374 -21.998  23.273  1.00 48.45           C
ANISOU 1383  CG1 VAL B 188     5893   7783   4734    333   -340   -177       C
ATOM   1384  CG2 VAL B 188      37.356 -21.087  24.433  1.00 49.72           C
ANISOU 1384  CG2 VAL B 188     6136   8117   4638    404   -179   -231       C
ATOM   1385  N   PRO B 189      41.796 -19.679  23.654  1.00 49.25           N
ANISOU 1385  N   PRO B 189     5912   7879   4922    396   -802   -460       N
ATOM   1386  CA  PRO B 189      42.947 -19.541  22.764  1.00 48.70           C
ANISOU 1386  CA  PRO B 189     5705   7750   5051    319   -898   -475       C
ATOM   1387  C   PRO B 189      42.790 -20.326  21.471  1.00 47.27           C
ANISOU 1387  C   PRO B 189     5436   7514   5008    234   -753   -384       C
ATOM   1388  O   PRO B 189      42.260 -21.433  21.480  1.00 47.11           O
ANISOU 1388  O   PRO B 189     5471   7490   4939    254   -630   -285       O
ATOM   1389  CB  PRO B 189      44.100 -20.124  23.588  1.00 50.14           C
ANISOU 1389  CB  PRO B 189     5903   7977   5173    417  -1041   -454       C
ATOM   1390  CG  PRO B 189      43.699 -19.926  25.001  1.00 51.65           C
ANISOU 1390  CG  PRO B 189     6251   8247   5128    542  -1096   -492       C
ATOM   1391  CD  PRO B 189      42.205 -20.045  25.023  1.00 51.06           C
ANISOU 1391  CD  PRO B 189     6258   8189   4953    533   -895   -446       C
ATOM   1392  N   PHE B 190      43.243 -19.745  20.369  1.00 46.48           N
ANISOU 1392  N   PHE B 190     5209   7372   5079    138   -772   -416       N
ATOM   1393  CA  PHE B 190      43.157 -20.389  19.067  1.00 45.34           C
ANISOU 1393  CA  PHE B 190     4982   7195   5048     72   -648   -353       C
ATOM   1394  C   PHE B 190      44.436 -20.172  18.257  1.00 45.46           C
ANISOU 1394  C   PHE B 190     4845   7213   5216     24   -715   -358       C
ATOM   1395  O   PHE B 190      45.235 -19.277  18.544  1.00 46.28           O
ANISOU 1395  O   PHE B 190     4886   7325   5373     -3   -852   -413       O
ATOM   1396  CB  PHE B 190      41.968 -19.833  18.280  1.00 44.24           C
ANISOU 1396  CB  PHE B 190     4845   7029   4934     -1   -539   -371       C
ATOM   1397  CG  PHE B 190      42.275 -18.563  17.544  1.00 44.02           C
ANISOU 1397  CG  PHE B 190     4738   6969   5018    -80   -599   -423       C
ATOM   1398  CD1 PHE B 190      42.734 -18.600  16.233  1.00 43.47           C
ANISOU 1398  CD1 PHE B 190     4557   6889   5070   -152   -552   -383       C
ATOM   1399  CD2 PHE B 190      42.138 -17.338  18.168  1.00 44.66           C
ANISOU 1399  CD2 PHE B 190     4864   7026   5079    -77   -704   -506       C
ATOM   1400  CE1 PHE B 190      43.047 -17.433  15.557  1.00 43.58           C
ANISOU 1400  CE1 PHE B 190     4505   6867   5184   -236   -596   -397       C
ATOM   1401  CE2 PHE B 190      42.438 -16.168  17.498  1.00 44.77           C
ANISOU 1401  CE2 PHE B 190     4820   6975   5214   -162   -766   -536       C
ATOM   1402  CZ  PHE B 190      42.895 -16.214  16.190  1.00 44.23           C
ANISOU 1402  CZ  PHE B 190     4641   6897   5269   -250   -706   -467       C
ATOM   1403  N   VAL B 191      44.604 -20.992  17.231  1.00 44.89           N
ANISOU 1403  N   VAL B 191     4706   7136   5214     11   -617   -305       N
ATOM   1404  CA  VAL B 191      45.592 -20.733  16.204  1.00 45.01           C
ANISOU 1404  CA  VAL B 191     4560   7178   5362    -42   -624   -301       C
ATOM   1405  C   VAL B 191      45.145 -21.430  14.926  1.00 44.11           C
ANISOU 1405  C   VAL B 191     4424   7057   5278    -56   -475   -267       C
ATOM   1406  O   VAL B 191      44.575 -22.520  14.972  1.00 43.85           O
ANISOU 1406  O   VAL B 191     4476   6990   5194     -2   -406   -246       O
ATOM   1407  CB  VAL B 191      47.008 -21.183  16.628  1.00 46.31           C
ANISOU 1407  CB  VAL B 191     4627   7400   5570     28   -731   -297       C
ATOM   1408  CG1 VAL B 191      47.053 -22.669  16.956  1.00 46.61           C
ANISOU 1408  CG1 VAL B 191     4737   7428   5545    157   -699   -253       C
ATOM   1409  CG2 VAL B 191      48.025 -20.841  15.553  1.00 46.73           C
ANISOU 1409  CG2 VAL B 191     4480   7511   5763    -35   -717   -286       C
ATOM   1410  N   ILE B 192      45.409 -20.792  13.790  1.00 43.91           N
ANISOU 1410  N   ILE B 192     4292   7059   5333   -133   -433   -261       N
ATOM   1411  CA  ILE B 192      45.155 -21.398  12.491  1.00 43.40           C
ANISOU 1411  CA  ILE B 192     4196   7013   5280   -130   -308   -244       C
ATOM   1412  C   ILE B 192      46.461 -21.974  11.954  1.00 44.35           C
ANISOU 1412  C   ILE B 192     4178   7212   5461    -75   -298   -229       C
ATOM   1413  O   ILE B 192      47.492 -21.293  11.933  1.00 45.24           O
ANISOU 1413  O   ILE B 192     4153   7388   5649   -117   -351   -213       O
ATOM   1414  CB  ILE B 192      44.624 -20.378  11.461  1.00 42.87           C
ANISOU 1414  CB  ILE B 192     4105   6952   5233   -224   -253   -231       C
ATOM   1415  CG1 ILE B 192      43.634 -19.380  12.091  1.00 42.41           C
ANISOU 1415  CG1 ILE B 192     4144   6827   5143   -271   -300   -255       C
ATOM   1416  CG2 ILE B 192      43.993 -21.097  10.281  1.00 42.36           C
ANISOU 1416  CG2 ILE B 192     4059   6905   5133   -199   -138   -237       C
ATOM   1417  CD1 ILE B 192      42.462 -19.999  12.825  1.00 41.84           C
ANISOU 1417  CD1 ILE B 192     4197   6717   4981   -223   -276   -286       C
ATOM   1418  N   ILE B 193      46.417 -23.230  11.531  1.00 44.41           N
ANISOU 1418  N   ILE B 193     4214   7214   5446     18   -234   -242       N
ATOM   1419  CA  ILE B 193      47.545 -23.839  10.838  1.00 45.45           C
ANISOU 1419  CA  ILE B 193     4214   7433   5624    102   -203   -246       C
ATOM   1420  C   ILE B 193      47.039 -24.517   9.577  1.00 45.20           C
ANISOU 1420  C   ILE B 193     4211   7405   5557    140    -86   -278       C
ATOM   1421  O   ILE B 193      46.458 -25.600   9.628  1.00 45.07           O
ANISOU 1421  O   ILE B 193     4313   7300   5512    208    -72   -315       O
ATOM   1422  CB  ILE B 193      48.295 -24.854  11.723  1.00 46.48           C
ANISOU 1422  CB  ILE B 193     4351   7545   5762    238   -283   -254       C
ATOM   1423  CG1 ILE B 193      48.971 -24.136  12.892  1.00 47.11           C
ANISOU 1423  CG1 ILE B 193     4377   7654   5867    214   -421   -238       C
ATOM   1424  CG2 ILE B 193      49.334 -25.612  10.903  1.00 47.69           C
ANISOU 1424  CG2 ILE B 193     4373   7790   5957    359   -237   -277       C
ATOM   1425  CD1 ILE B 193      49.647 -25.063  13.878  1.00 48.28           C
ANISOU 1425  CD1 ILE B 193     4551   7790   6002    362   -524   -237       C
ATOM   1426  N   ARG B 194      47.263 -23.864   8.444  1.00 45.37           N
ANISOU 1426  N   ARG B 194     4131   7529   5579     92     -9   -261       N
ATOM   1427  CA  ARG B 194      46.791 -24.357   7.170  1.00 45.35           C
ANISOU 1427  CA  ARG B 194     4156   7558   5516    134     92   -302       C
ATOM   1428  C   ARG B 194      47.929 -24.423   6.165  1.00 46.75           C
ANISOU 1428  C   ARG B 194     4169   7900   5693    203    174   -295       C
ATOM   1429  O   ARG B 194      48.952 -23.755   6.319  1.00 47.61           O
ANISOU 1429  O   ARG B 194     4119   8107   5863    163    168   -232       O
ATOM   1430  CB  ARG B 194      45.674 -23.457   6.656  1.00 44.35           C
ANISOU 1430  CB  ARG B 194     4096   7412   5344     24    121   -282       C
ATOM   1431  CG  ARG B 194      44.361 -23.611   7.412  1.00 43.22           C
ANISOU 1431  CG  ARG B 194     4103   7133   5184    -17     73   -312       C
ATOM   1432  CD  ARG B 194      43.467 -22.404   7.173  1.00 42.47           C
ANISOU 1432  CD  ARG B 194     4039   7033   5065   -119     74   -281       C
ATOM   1433  NE  ARG B 194      42.134 -22.545   7.760  1.00 41.62           N
ANISOU 1433  NE  ARG B 194     4045   6831   4936   -147     48   -317       N
ATOM   1434  CZ  ARG B 194      41.076 -23.069   7.144  1.00 41.37           C
ANISOU 1434  CZ  ARG B 194     4071   6780   4868   -141     80   -372       C
ATOM   1435  NH1 ARG B 194      41.158 -23.526   5.893  1.00 41.85           N
ANISOU 1435  NH1 ARG B 194     4112   6900   4891    -94    127   -413       N
ATOM   1436  NH2 ARG B 194      39.919 -23.132   7.784  1.00 40.87           N
ANISOU 1436  NH2 ARG B 194     4076   6650   4801   -180     63   -392       N
ATOM   1437  N   ALA B 195      47.745 -25.251   5.141  1.00 47.23           N
ANISOU 1437  N   ALA B 195     4262   7998   5684    309    249   -366       N
ATOM   1438  CA  ALA B 195      48.704 -25.370   4.050  1.00 48.80           C
ANISOU 1438  CA  ALA B 195     4315   8382   5843    401    354   -371       C
ATOM   1439  C   ALA B 195      48.073 -24.825   2.776  1.00 48.75           C
ANISOU 1439  C   ALA B 195     4338   8459   5725    359    448   -356       C
ATOM   1440  O   ALA B 195      46.851 -24.708   2.688  1.00 47.57           O
ANISOU 1440  O   ALA B 195     4334   8206   5534    301    416   -382       O
ATOM   1441  CB  ALA B 195      49.117 -26.818   3.860  1.00 49.89           C
ANISOU 1441  CB  ALA B 195     4475   8512   5969    603    357   -487       C
ATOM   1442  N   LEU B 196      48.908 -24.492   1.793  1.00 50.25           N
ANISOU 1442  N   LEU B 196     4383   8850   5859    395    566   -307       N
ATOM   1443  CA  LEU B 196      48.411 -23.901   0.548  1.00 50.58           C
ANISOU 1443  CA  LEU B 196     4453   8995   5768    367    661   -265       C
ATOM   1444  C   LEU B 196      48.088 -24.967  -0.487  1.00 51.39           C
ANISOU 1444  C   LEU B 196     4639   9158   5730    545    710   -409       C
ATOM   1445  O   LEU B 196      48.953 -25.765  -0.869  1.00 52.96           O
ANISOU 1445  O   LEU B 196     4753   9471   5896    707    771   -482       O
ATOM   1446  CB  LEU B 196      49.407 -22.891  -0.037  1.00 52.12           C
ANISOU 1446  CB  LEU B 196     4461   9386   5957    295    781   -107       C
ATOM   1447  CG  LEU B 196      49.418 -21.462   0.498  1.00 51.66           C
ANISOU 1447  CG  LEU B 196     4360   9263   6004     79    743     53       C
ATOM   1448  CD1 LEU B 196      49.103 -21.372   1.986  1.00 50.08           C
ANISOU 1448  CD1 LEU B 196     4222   8859   5945      1    581     18       C
ATOM   1449  CD2 LEU B 196      50.748 -20.817   0.160  1.00 53.74           C
ANISOU 1449  CD2 LEU B 196     4387   9710   6323     15    853    194       C
ATOM   1450  N   SER B 197      46.829 -24.968  -0.923  1.00 50.53           N
ANISOU 1450  N   SER B 197     4690   8971   5539    522    669   -466       N
ATOM   1451  CA  SER B 197      46.355 -25.834  -1.998  1.00 51.45           C
ANISOU 1451  CA  SER B 197     4902   9138   5510    671    689   -617       C
ATOM   1452  C   SER B 197      46.588 -25.177  -3.358  1.00 52.94           C
ANISOU 1452  C   SER B 197     5042   9562   5512    711    818   -547       C
ATOM   1453  O   SER B 197      46.716 -25.861  -4.375  1.00 54.53           O
ANISOU 1453  O   SER B 197     5267   9892   5559    881    874   -664       O
ATOM   1454  CB  SER B 197      44.865 -26.098  -1.813  1.00 50.11           C
ANISOU 1454  CB  SER B 197     4905   8785   5350    612    571   -709       C
ATOM   1455  OG  SER B 197      44.166 -24.879  -1.660  1.00 48.95           O
ANISOU 1455  OG  SER B 197     4775   8617   5207    457    550   -584       O
ATOM   1456  N   ASP B 198      46.639 -23.847  -3.365  1.00 52.68           N
ANISOU 1456  N   ASP B 198     4952   9577   5486    561    861   -354       N
ATOM   1457  CA  ASP B 198      46.749 -23.081  -4.597  1.00 54.17           C
ANISOU 1457  CA  ASP B 198     5117   9968   5496    572    983   -239       C
ATOM   1458  C   ASP B 198      47.118 -21.630  -4.295  1.00 54.12           C
ANISOU 1458  C   ASP B 198     5023   9965   5576    380   1024      2       C
ATOM   1459  O   ASP B 198      47.267 -21.244  -3.140  1.00 52.89           O
ANISOU 1459  O   ASP B 198     4826   9659   5612    249    946     50       O
ATOM   1460  CB  ASP B 198      45.420 -23.122  -5.348  1.00 53.85           C
ANISOU 1460  CB  ASP B 198     5255   9900   5306    613    914   -323       C
ATOM   1461  CG  ASP B 198      44.280 -22.533  -4.542  1.00 51.76           C
ANISOU 1461  CG  ASP B 198     5087   9420   5159    463    775   -298       C
ATOM   1462  OD1 ASP B 198      44.442 -22.306  -3.329  1.00 50.42           O
ANISOU 1462  OD1 ASP B 198     4878   9103   5178    348    720   -254       O
ATOM   1463  OD2 ASP B 198      43.213 -22.280  -5.121  1.00 51.63           O
ANISOU 1463  OD2 ASP B 198     5184   9396   5037    472    718   -327       O
ATOM   1464  N   ILE B 199      47.276 -20.845  -5.354  1.00 55.73           N
ANISOU 1464  N   ILE B 199     5208  10337   5630    368   1144    154       N
ATOM   1465  CA  ILE B 199      47.545 -19.421  -5.250  1.00 56.14           C
ANISOU 1465  CA  ILE B 199     5204  10371   5757    178   1184    398       C
ATOM   1466  C   ILE B 199      46.281 -18.677  -5.639  1.00 55.46           C
ANISOU 1466  C   ILE B 199     5301  10187   5582    138   1106    448       C
ATOM   1467  O   ILE B 199      45.786 -18.824  -6.764  1.00 56.48           O
ANISOU 1467  O   ILE B 199     5525  10448   5489    258   1148    429       O
ATOM   1468  CB  ILE B 199      48.694 -19.000  -6.198  1.00 58.97           C
ANISOU 1468  CB  ILE B 199     5401  10993   6013    182   1396    580       C
ATOM   1469  CG1 ILE B 199      49.953 -19.845  -5.936  1.00 60.03           C
ANISOU 1469  CG1 ILE B 199     5327  11268   6213    268   1481    506       C
ATOM   1470  CG2 ILE B 199      48.984 -17.509  -6.060  1.00 59.72           C
ANISOU 1470  CG2 ILE B 199     5443  11028   6220    -46   1428    850       C
ATOM   1471  CD1 ILE B 199      50.503 -19.754  -4.524  1.00 58.87           C
ANISOU 1471  CD1 ILE B 199     5063  10962   6343    140   1376    500       C
ATOM   1472  N   ALA B 200      45.760 -17.881  -4.712  1.00 53.95           N
ANISOU 1472  N   ALA B 200     5162   9778   5558    -12    984    501       N
ATOM   1473  CA  ALA B 200      44.488 -17.189  -4.921  1.00 53.23           C
ANISOU 1473  CA  ALA B 200     5239   9574   5412    -32    885    527       C
ATOM   1474  C   ALA B 200      44.517 -16.340  -6.186  1.00 55.34           C
ANISOU 1474  C   ALA B 200     5549   9979   5498    -23    989    724       C
ATOM   1475  O   ALA B 200      45.401 -15.506  -6.355  1.00 56.92           O
ANISOU 1475  O   ALA B 200     5658  10224   5744   -137   1095    940       O
ATOM   1476  CB  ALA B 200      44.148 -16.330  -3.712  1.00 51.81           C
ANISOU 1476  CB  ALA B 200     5085   9156   5443   -186    760    570       C
ATOM   1477  N   GLY B 201      43.550 -16.572  -7.071  1.00 55.61           N
ANISOU 1477  N   GLY B 201     5719  10082   5328    111    952    653       N
ATOM   1478  CA  GLY B 201      43.389 -15.778  -8.285  1.00 57.71           C
ANISOU 1478  CA  GLY B 201     6065  10475   5386    148   1026    839       C
ATOM   1479  C   GLY B 201      44.147 -16.287  -9.486  1.00 60.09           C
ANISOU 1479  C   GLY B 201     6315  11072   5446    279   1206    874       C
ATOM   1480  O   GLY B 201      43.990 -15.759 -10.587  1.00 62.11           O
ANISOU 1480  O   GLY B 201     6652  11471   5478    342   1276   1022       O
ATOM   1481  N   LYS B 202      44.975 -17.306  -9.299  1.00 60.15           N
ANISOU 1481  N   LYS B 202     6192  11183   5479    341   1282    741       N
ATOM   1482  CA  LYS B 202      45.768 -17.781 -10.421  1.00 62.72           C
ANISOU 1482  CA  LYS B 202     6452  11811   5567    488   1469    764       C
ATOM   1483  C   LYS B 202      45.029 -18.867 -11.191  1.00 62.97           C
ANISOU 1483  C   LYS B 202     6608  11951   5366    721   1404    506       C
ATOM   1484  O   LYS B 202      44.194 -18.541 -12.048  1.00 63.83           O
ANISOU 1484  O   LYS B 202     6866  12121   5264    801   1358    529       O
ATOM   1485  CB  LYS B 202      47.225 -18.038  -9.997  1.00 63.55           C
ANISOU 1485  CB  LYS B 202     6325  12014   5806    435   1618    816       C
ATOM   1486  CG  LYS B 202      47.954 -16.714  -9.830  1.00 64.76           C
ANISOU 1486  CG  LYS B 202     6369  12147   6089    212   1721   1135       C
ATOM   1487  CD  LYS B 202      48.425 -16.169 -11.167  1.00 68.10           C
ANISOU 1487  CD  LYS B 202     6775  12842   6258    251   1937   1373       C
ATOM   1488  CE  LYS B 202      48.832 -14.728 -11.059  1.00 69.39           C
ANISOU 1488  CE  LYS B 202     6891  12917   6558      4   2002   1712       C
ATOM   1489  NZ  LYS B 202      49.501 -14.389  -9.771  1.00 68.26           N
ANISOU 1489  NZ  LYS B 202     6581  12580   6773   -213   1942   1737       N
ATOM   1490  N   GLU B 203      45.259 -20.133 -10.896  1.00 62.41           N
ANISOU 1490  N   GLU B 203     6492  11884   5335    834   1376    256       N
ATOM   1491  CA  GLU B 203      44.544 -21.177 -11.600  1.00 62.88           C
ANISOU 1491  CA  GLU B 203     6679  12011   5203   1041   1290    -10       C
ATOM   1492  C   GLU B 203      43.909 -21.921 -10.474  1.00 60.27           C
ANISOU 1492  C   GLU B 203     6377  11408   5114    986   1105   -220       C
ATOM   1493  O   GLU B 203      44.023 -23.124 -10.402  1.00 60.35           O
ANISOU 1493  O   GLU B 203     6390  11404   5136   1107   1067   -451       O
ATOM   1494  CB  GLU B 203      45.515 -22.055 -12.408  1.00 65.34           C
ANISOU 1494  CB  GLU B 203     6917  12589   5320   1251   1447   -112       C
ATOM   1495  CG  GLU B 203      46.552 -22.831 -11.589  1.00 64.93           C
ANISOU 1495  CG  GLU B 203     6702  12500   5468   1259   1500   -201       C
ATOM   1496  CD  GLU B 203      47.334 -23.820 -12.431  1.00 67.51           C
ANISOU 1496  CD  GLU B 203     6980  13082   5590   1517   1627   -359       C
ATOM   1497  OE1 GLU B 203      46.698 -24.800 -12.875  1.00 67.88           O
ANISOU 1497  OE1 GLU B 203     7167  13107   5516   1693   1512   -633       O
ATOM   1498  OE2 GLU B 203      48.563 -23.636 -12.642  1.00 69.40           O
ANISOU 1498  OE2 GLU B 203     7034  13539   5795   1545   1834   -223       O
ATOM   1499  N   SER B 204      43.270 -21.166  -9.583  1.00 58.21           N
ANISOU 1499  N   SER B 204     6140  10930   5046    805    997   -127       N
ATOM   1500  CA  SER B 204      43.038 -21.597  -8.213  1.00 55.83           C
ANISOU 1500  CA  SER B 204     5813  10382   5018    700    881   -229       C
ATOM   1501  C   SER B 204      42.335 -22.937  -8.096  1.00 55.26           C
ANISOU 1501  C   SER B 204     5818  10214   4963    800    752   -516       C
ATOM   1502  O   SER B 204      42.831 -23.835  -7.419  1.00 54.78           O
ANISOU 1502  O   SER B 204     5709  10069   5036    819    745   -627       O
ATOM   1503  CB  SER B 204      42.268 -20.516  -7.451  1.00 54.13           C
ANISOU 1503  CB  SER B 204     5638   9980   4949    527    782   -103       C
ATOM   1504  OG  SER B 204      43.079 -19.374  -7.241  1.00 54.57           O
ANISOU 1504  OG  SER B 204     5610  10052   5074    400    882    148       O
ATOM   1505  N   ASN B 205      41.194 -23.086  -8.760  1.00 55.58           N
ANISOU 1505  N   ASN B 205     5978  10261   4877    862    640   -635       N
ATOM   1506  CA  ASN B 205      40.375 -24.289  -8.572  1.00 55.15           C
ANISOU 1506  CA  ASN B 205     5994  10075   4884    910    492   -903       C
ATOM   1507  C   ASN B 205      40.986 -25.547  -9.202  1.00 56.90           C
ANISOU 1507  C   ASN B 205     6232  10389   5001   1097    525  -1106       C
ATOM   1508  O   ASN B 205      40.809 -26.651  -8.688  1.00 56.53           O
ANISOU 1508  O   ASN B 205     6212  10177   5089   1112    437  -1294       O
ATOM   1509  CB  ASN B 205      38.917 -24.057  -9.028  1.00 55.12           C
ANISOU 1509  CB  ASN B 205     6088  10047   4809    905    338   -983       C
ATOM   1510  CG  ASN B 205      38.770 -23.968 -10.534  1.00 57.48           C
ANISOU 1510  CG  ASN B 205     6462  10580   4798   1076    346  -1026       C
ATOM   1511  OD1 ASN B 205      39.734 -23.712 -11.248  1.00 59.06           O
ANISOU 1511  OD1 ASN B 205     6641  10981   4819   1173    500   -920       O
ATOM   1512  ND2 ASN B 205      37.559 -24.186 -11.024  1.00 57.96           N
ANISOU 1512  ND2 ASN B 205     6603  10631   4788   1117    179  -1182       N
ATOM   1513  N   VAL B 206      41.714 -25.372 -10.299  1.00 59.06           N
ANISOU 1513  N   VAL B 206     6492  10919   5030   1245    657  -1062       N
ATOM   1514  CA  VAL B 206      42.429 -26.486 -10.934  1.00 61.10           C
ANISOU 1514  CA  VAL B 206     6756  11297   5164   1457    711  -1254       C
ATOM   1515  C   VAL B 206      43.605 -26.905 -10.063  1.00 60.66           C
ANISOU 1515  C   VAL B 206     6573  11184   5291   1446    806  -1218       C
ATOM   1516  O   VAL B 206      43.860 -28.090  -9.895  1.00 61.22           O
ANISOU 1516  O   VAL B 206     6668  11170   5423   1562    760  -1424       O
ATOM   1517  CB  VAL B 206      42.952 -26.127 -12.345  1.00 63.87           C
ANISOU 1517  CB  VAL B 206     7113  11983   5174   1634    856  -1198       C
ATOM   1518  CG1 VAL B 206      43.816 -27.251 -12.897  1.00 66.14           C
ANISOU 1518  CG1 VAL B 206     7386  12407   5339   1873    932  -1400       C
ATOM   1519  CG2 VAL B 206      41.797 -25.822 -13.291  1.00 64.76           C
ANISOU 1519  CG2 VAL B 206     7366  12170   5070   1688    738  -1259       C
ATOM   1520  N   SER B 207      44.317 -25.928  -9.513  1.00 59.86           N
ANISOU 1520  N   SER B 207     6341  11120   5282   1311    923   -960       N
ATOM   1521  CA  SER B 207      45.397 -26.202  -8.574  1.00 59.37           C
ANISOU 1521  CA  SER B 207     6141  11005   5414   1281    988   -912       C
ATOM   1522  C   SER B 207      44.860 -26.846  -7.292  1.00 57.25           C
ANISOU 1522  C   SER B 207     5923  10425   5402   1184    826  -1015       C
ATOM   1523  O   SER B 207      45.449 -27.789  -6.772  1.00 57.48           O
ANISOU 1523  O   SER B 207     5923  10374   5541   1266    812  -1123       O
ATOM   1524  CB  SER B 207      46.159 -24.914  -8.242  1.00 59.13           C
ANISOU 1524  CB  SER B 207     5959  11063   5446   1124   1117   -617       C
ATOM   1525  OG  SER B 207      47.191 -25.163  -7.300  1.00 58.80           O
ANISOU 1525  OG  SER B 207     5768  10977   5598   1094   1154   -583       O
ATOM   1526  N   PHE B 208      43.733 -26.337  -6.801  1.00 55.40           N
ANISOU 1526  N   PHE B 208     5767  10027   5255   1022    710   -975       N
ATOM   1527  CA  PHE B 208      43.110 -26.828  -5.570  1.00 53.52           C
ANISOU 1527  CA  PHE B 208     5577   9516   5243    911    576  -1040       C
ATOM   1528  C   PHE B 208      42.757 -28.315  -5.635  1.00 54.26           C
ANISOU 1528  C   PHE B 208     5770   9474   5370   1024    475  -1292       C
ATOM   1529  O   PHE B 208      43.103 -29.079  -4.730  1.00 53.85           O
ANISOU 1529  O   PHE B 208     5718   9260   5484   1024    439  -1335       O
ATOM   1530  CB  PHE B 208      41.853 -26.009  -5.258  1.00 51.95           C
ANISOU 1530  CB  PHE B 208     5436   9214   5087    749    483   -972       C
ATOM   1531  CG  PHE B 208      41.036 -26.559  -4.131  1.00 50.42           C
ANISOU 1531  CG  PHE B 208     5295   8774   5090    643    360  -1046       C
ATOM   1532  CD1 PHE B 208      40.076 -27.530  -4.372  1.00 50.87           C
ANISOU 1532  CD1 PHE B 208     5447   8722   5159    671    246  -1243       C
ATOM   1533  CD2 PHE B 208      41.223 -26.104  -2.832  1.00 48.85           C
ANISOU 1533  CD2 PHE B 208     5046   8454   5059    511    358   -917       C
ATOM   1534  CE1 PHE B 208      39.318 -28.041  -3.339  1.00 49.79           C
ANISOU 1534  CE1 PHE B 208     5346   8365   5206    555    154  -1285       C
ATOM   1535  CE2 PHE B 208      40.466 -26.608  -1.793  1.00 47.73           C
ANISOU 1535  CE2 PHE B 208     4954   8110   5071    421    266   -967       C
ATOM   1536  CZ  PHE B 208      39.514 -27.582  -2.050  1.00 48.21           C
ANISOU 1536  CZ  PHE B 208     5101   8069   5150    436    175  -1138       C
ATOM   1537  N   ASP B 209      42.049 -28.713  -6.692  1.00 55.54           N
ANISOU 1537  N   ASP B 209     6031   9693   5380   1120    416  -1457       N
ATOM   1538  CA  ASP B 209      41.733 -30.135  -6.913  1.00 56.77           C
ANISOU 1538  CA  ASP B 209     6294   9714   5564   1234    306  -1721       C
ATOM   1539  C   ASP B 209      42.986 -30.994  -7.001  1.00 58.36           C
ANISOU 1539  C   ASP B 209     6463   9955   5754   1426    380  -1806       C
ATOM   1540  O   ASP B 209      42.971 -32.164  -6.638  1.00 58.95           O
ANISOU 1540  O   ASP B 209     6614   9831   5953   1488    291  -1969       O
ATOM   1541  CB  ASP B 209      40.929 -30.339  -8.206  1.00 58.43           C
ANISOU 1541  CB  ASP B 209     6603  10026   5572   1336    227  -1901       C
ATOM   1542  CG  ASP B 209      39.584 -29.632  -8.179  1.00 57.25           C
ANISOU 1542  CG  ASP B 209     6482   9833   5439   1175    122  -1856       C
ATOM   1543  OD1 ASP B 209      39.006 -29.490  -7.077  1.00 55.38           O
ANISOU 1543  OD1 ASP B 209     6224   9403   5414    991     67  -1780       O
ATOM   1544  OD2 ASP B 209      39.099 -29.234  -9.261  1.00 58.42           O
ANISOU 1544  OD2 ASP B 209     6670  10151   5374   1248     94  -1901       O
ATOM   1545  N   GLN B 210      44.061 -30.403  -7.498  1.00 59.26           N
ANISOU 1545  N   GLN B 210     6460  10329   5727   1522    545  -1688       N
ATOM   1546  CA  GLN B 210      45.308 -31.120  -7.695  1.00 61.12           C
ANISOU 1546  CA  GLN B 210     6630  10665   5928   1733    637  -1766       C
ATOM   1547  C   GLN B 210      46.105 -31.306  -6.396  1.00 60.06           C
ANISOU 1547  C   GLN B 210     6399  10397   6025   1678    647  -1665       C
ATOM   1548  O   GLN B 210      46.715 -32.360  -6.195  1.00 61.31           O
ANISOU 1548  O   GLN B 210     6570  10476   6248   1842    623  -1801       O
ATOM   1549  CB  GLN B 210      46.155 -30.387  -8.743  1.00 62.86           C
ANISOU 1549  CB  GLN B 210     6733  11249   5903   1848    830  -1662       C
ATOM   1550  CG  GLN B 210      46.953 -31.301  -9.653  1.00 65.85           C
ANISOU 1550  CG  GLN B 210     7108  11804   6110   2150    904  -1859       C
ATOM   1551  CD  GLN B 210      47.340 -30.625 -10.962  1.00 67.98           C
ANISOU 1551  CD  GLN B 210     7320  12446   6062   2268   1078  -1788       C
ATOM   1552  OE1 GLN B 210      48.213 -29.754 -10.987  1.00 68.31           O
ANISOU 1552  OE1 GLN B 210     7184  12703   6069   2220   1261  -1554       O
ATOM   1553  NE2 GLN B 210      46.692 -31.026 -12.060  1.00 69.67           N
ANISOU 1553  NE2 GLN B 210     7686  12742   6045   2421   1019  -1986       N
ATOM   1554  N   PHE B 211      46.097 -30.296  -5.521  1.00 58.03           N
ANISOU 1554  N   PHE B 211     6054  10108   5885   1467    669  -1438       N
ATOM   1555  CA  PHE B 211      46.957 -30.293  -4.326  1.00 57.26           C
ANISOU 1555  CA  PHE B 211     5845   9934   5975   1420    680  -1325       C
ATOM   1556  C   PHE B 211      46.205 -30.117  -2.994  1.00 54.89           C
ANISOU 1556  C   PHE B 211     5609   9373   5872   1213    560  -1245       C
ATOM   1557  O   PHE B 211      46.782 -29.635  -2.014  1.00 53.97           O
ANISOU 1557  O   PHE B 211     5394   9237   5876   1124    570  -1100       O
ATOM   1558  CB  PHE B 211      48.021 -29.193  -4.457  1.00 57.68           C
ANISOU 1558  CB  PHE B 211     5690  10242   5985   1382    837  -1121       C
ATOM   1559  CG  PHE B 211      48.850 -29.285  -5.710  1.00 60.29           C
ANISOU 1559  CG  PHE B 211     5925  10872   6110   1580    993  -1162       C
ATOM   1560  CD1 PHE B 211      49.813 -30.283  -5.852  1.00 62.28           C
ANISOU 1560  CD1 PHE B 211     6112  11197   6356   1816   1033  -1298       C
ATOM   1561  CD2 PHE B 211      48.684 -28.365  -6.744  1.00 61.01           C
ANISOU 1561  CD2 PHE B 211     5994  11182   6004   1546   1107  -1056       C
ATOM   1562  CE1 PHE B 211      50.584 -30.368  -6.998  1.00 64.96           C
ANISOU 1562  CE1 PHE B 211     6352  11842   6490   2018   1195  -1342       C
ATOM   1563  CE2 PHE B 211      49.453 -28.446  -7.895  1.00 63.69           C
ANISOU 1563  CE2 PHE B 211     6246  11826   6129   1735   1272  -1079       C
ATOM   1564  CZ  PHE B 211      50.405 -29.448  -8.019  1.00 65.69           C
ANISOU 1564  CZ  PHE B 211     6419  12168   6371   1973   1323  -1227       C
ATOM   1565  N   LEU B 212      44.934 -30.512  -2.946  1.00 54.14           N
ANISOU 1565  N   LEU B 212     5671   9094   5808   1139    445  -1342       N
ATOM   1566  CA  LEU B 212      44.156 -30.449  -1.702  1.00 52.27           C
ANISOU 1566  CA  LEU B 212     5493   8626   5741    957    348  -1273       C
ATOM   1567  C   LEU B 212      44.631 -31.510  -0.707  1.00 52.59           C
ANISOU 1567  C   LEU B 212     5574   8473   5935   1017    289  -1309       C
ATOM   1568  O   LEU B 212      44.789 -31.233   0.484  1.00 51.44           O
ANISOU 1568  O   LEU B 212     5401   8240   5904    919    267  -1180       O
ATOM   1569  CB  LEU B 212      42.663 -30.627  -1.979  1.00 51.81           C
ANISOU 1569  CB  LEU B 212     5559   8446   5679    861    253  -1368       C
ATOM   1570  CG  LEU B 212      41.764 -30.916  -0.765  1.00 50.51           C
ANISOU 1570  CG  LEU B 212     5466   8036   5690    699    161  -1334       C
ATOM   1571  CD1 LEU B 212      41.832 -29.802   0.279  1.00 48.70           C
ANISOU 1571  CD1 LEU B 212     5160   7824   5518    555    193  -1132       C
ATOM   1572  CD2 LEU B 212      40.328 -31.131  -1.203  1.00 50.58           C
ANISOU 1572  CD2 LEU B 212     5558   7962   5699    612     73  -1444       C
ATOM   1573  N   ASP B 213      44.839 -32.725  -1.205  1.00 54.40           N
ANISOU 1573  N   ASP B 213     5884   8629   6156   1192    252  -1489       N
ATOM   1574  CA  ASP B 213      45.316 -33.829  -0.379  1.00 55.19           C
ANISOU 1574  CA  ASP B 213     6047   8527   6396   1284    186  -1529       C
ATOM   1575  C   ASP B 213      46.701 -33.523   0.196  1.00 55.39           C
ANISOU 1575  C   ASP B 213     5918   8680   6447   1372    250  -1412       C
ATOM   1576  O   ASP B 213      46.969 -33.803   1.363  1.00 55.00           O
ANISOU 1576  O   ASP B 213     5886   8489   6524   1349    192  -1329       O
ATOM   1577  CB  ASP B 213      45.332 -35.132  -1.191  1.00 57.51           C
ANISOU 1577  CB  ASP B 213     6461   8721   6668   1483    130  -1767       C
ATOM   1578  CG  ASP B 213      43.928 -35.572  -1.644  1.00 57.65           C
ANISOU 1578  CG  ASP B 213     6631   8571   6701   1378     29  -1903       C
ATOM   1579  OD1 ASP B 213      42.955 -35.352  -0.894  1.00 56.17           O
ANISOU 1579  OD1 ASP B 213     6487   8234   6620   1161    -23  -1810       O
ATOM   1580  OD2 ASP B 213      43.801 -36.156  -2.749  1.00 59.48           O
ANISOU 1580  OD2 ASP B 213     6932   8829   6837   1519     -3  -2113       O
ATOM   1581  N   GLN B 214      47.575 -32.937  -0.623  1.00 56.23           N
ANISOU 1581  N   GLN B 214     5866   9069   6430   1470    367  -1397       N
ATOM   1582  CA  GLN B 214      48.888 -32.494  -0.160  1.00 56.62           C
ANISOU 1582  CA  GLN B 214     5720   9280   6513   1524    433  -1279       C
ATOM   1583  C   GLN B 214      48.767 -31.444   0.943  1.00 54.59           C
ANISOU 1583  C   GLN B 214     5400   8995   6346   1300    410  -1082       C
ATOM   1584  O   GLN B 214      49.500 -31.487   1.928  1.00 54.64           O
ANISOU 1584  O   GLN B 214     5333   8973   6454   1316    368  -1008       O
ATOM   1585  CB  GLN B 214      49.703 -31.914  -1.312  1.00 58.05           C
ANISOU 1585  CB  GLN B 214     5726   9789   6541   1622    589  -1271       C
ATOM   1586  CG  GLN B 214      51.146 -31.608  -0.933  1.00 59.08           C
ANISOU 1586  CG  GLN B 214     5619  10104   6724   1693    660  -1173       C
ATOM   1587  CD  GLN B 214      51.965 -31.024  -2.073  1.00 60.85           C
ANISOU 1587  CD  GLN B 214     5646  10673   6800   1772    841  -1139       C
ATOM   1588  OE1 GLN B 214      51.667 -29.944  -2.587  1.00 60.24           O
ANISOU 1588  OE1 GLN B 214     5523  10727   6638   1616    927  -1016       O
ATOM   1589  NE2 GLN B 214      53.018 -31.727  -2.455  1.00 63.28           N
ANISOU 1589  NE2 GLN B 214     5833  11132   7076   2022    906  -1237       N
ATOM   1590  N   ALA B 215      47.844 -30.503   0.767  1.00 53.04           N
ANISOU 1590  N   ALA B 215     5237   8811   6106   1110    423  -1009       N
ATOM   1591  CA  ALA B 215      47.634 -29.438   1.742  1.00 51.30           C
ANISOU 1591  CA  ALA B 215     4975   8559   5959    909    395   -846       C
ATOM   1592  C   ALA B 215      47.121 -29.988   3.067  1.00 50.36           C
ANISOU 1592  C   ALA B 215     4981   8197   5958    854    278   -834       C
ATOM   1593  O   ALA B 215      47.570 -29.574   4.137  1.00 49.84           O
ANISOU 1593  O   ALA B 215     4859   8113   5965    797    237   -731       O
ATOM   1594  CB  ALA B 215      46.669 -28.403   1.198  1.00 50.15           C
ANISOU 1594  CB  ALA B 215     4860   8459   5736    754    425   -791       C
ATOM   1595  N   ALA B 216      46.176 -30.918   2.991  1.00 50.39           N
ANISOU 1595  N   ALA B 216     5154   8017   5976    866    223   -936       N
ATOM   1596  CA  ALA B 216      45.701 -31.626   4.172  1.00 50.04           C
ANISOU 1596  CA  ALA B 216     5239   7736   6038    824    131   -913       C
ATOM   1597  C   ALA B 216      46.858 -32.328   4.885  1.00 51.25           C
ANISOU 1597  C   ALA B 216     5365   7851   6256    979     90   -896       C
ATOM   1598  O   ALA B 216      47.010 -32.212   6.104  1.00 50.77           O
ANISOU 1598  O   ALA B 216     5319   7720   6253    933     35   -790       O
ATOM   1599  CB  ALA B 216      44.634 -32.634   3.783  1.00 50.55           C
ANISOU 1599  CB  ALA B 216     5470   7612   6126    817     85  -1035       C
ATOM   1600  N   LEU B 217      47.681 -33.034   4.113  1.00 53.03           N
ANISOU 1600  N   LEU B 217     5549   8141   6458   1182    114  -1007       N
ATOM   1601  CA  LEU B 217      48.789 -33.801   4.669  1.00 54.55           C
ANISOU 1601  CA  LEU B 217     5711   8302   6714   1372     66  -1014       C
ATOM   1602  C   LEU B 217      49.807 -32.922   5.380  1.00 54.30           C
ANISOU 1602  C   LEU B 217     5488   8442   6702   1354     70   -887       C
ATOM   1603  O   LEU B 217      50.156 -33.192   6.525  1.00 54.48           O
ANISOU 1603  O   LEU B 217     5539   8370   6792   1383    -20   -816       O
ATOM   1604  CB  LEU B 217      49.482 -34.618   3.574  1.00 56.73           C
ANISOU 1604  CB  LEU B 217     5955   8652   6946   1617    104  -1178       C
ATOM   1605  CG  LEU B 217      50.593 -35.579   4.024  1.00 58.78           C
ANISOU 1605  CG  LEU B 217     6195   8864   7275   1864     44  -1218       C
ATOM   1606  CD1 LEU B 217      50.170 -36.428   5.218  1.00 58.83           C
ANISOU 1606  CD1 LEU B 217     6404   8557   7392   1852    -87  -1164       C
ATOM   1607  CD2 LEU B 217      51.028 -36.468   2.865  1.00 61.08           C
ANISOU 1607  CD2 LEU B 217     6498   9198   7513   2119     78  -1418       C
ATOM   1608  N   HIS B 218      50.278 -31.874   4.710  1.00 54.10           N
ANISOU 1608  N   HIS B 218     5272   8664   6619   1301    166   -852       N
ATOM   1609  CA  HIS B 218      51.275 -30.984   5.299  1.00 54.19           C
ANISOU 1609  CA  HIS B 218     5078   8839   6672   1258    163   -741       C
ATOM   1610  C   HIS B 218      50.728 -30.295   6.546  1.00 52.52           C
ANISOU 1610  C   HIS B 218     4933   8515   6507   1071     74   -627       C
ATOM   1611  O   HIS B 218      51.407 -30.227   7.572  1.00 52.93           O
ANISOU 1611  O   HIS B 218     4925   8569   6618   1098    -15   -571       O
ATOM   1612  CB  HIS B 218      51.750 -29.929   4.298  1.00 54.49           C
ANISOU 1612  CB  HIS B 218     4914   9139   6652   1192    294   -701       C
ATOM   1613  CG  HIS B 218      52.514 -30.488   3.135  1.00 56.57           C
ANISOU 1613  CG  HIS B 218     5065   9582   6848   1397    402   -800       C
ATOM   1614  ND1 HIS B 218      52.806 -29.742   2.014  1.00 57.25           N
ANISOU 1614  ND1 HIS B 218     5004   9907   6840   1364    551   -767       N
ATOM   1615  CD2 HIS B 218      53.021 -31.723   2.907  1.00 58.37           C
ANISOU 1615  CD2 HIS B 218     5318   9786   7075   1651    387   -931       C
ATOM   1616  CE1 HIS B 218      53.467 -30.490   1.150  1.00 59.38           C
ANISOU 1616  CE1 HIS B 218     5202  10319   7039   1594    634   -879       C
ATOM   1617  NE2 HIS B 218      53.607 -31.697   1.666  1.00 60.09           N
ANISOU 1617  NE2 HIS B 218     5395  10247   7190   1777    530   -992       N
ATOM   1618  N   SER B 219      49.499 -29.791   6.450  1.00 50.84           N
ANISOU 1618  N   SER B 219     4842   8219   6256    901     92   -605       N
ATOM   1619  CA  SER B 219      48.852 -29.136   7.591  1.00 49.39           C
ANISOU 1619  CA  SER B 219     4734   7937   6095    741     20   -515       C
ATOM   1620  C   SER B 219      48.698 -30.110   8.757  1.00 49.72           C
ANISOU 1620  C   SER B 219     4926   7794   6173    812    -79   -501       C
ATOM   1621  O   SER B 219      49.035 -29.775   9.883  1.00 49.68           O
ANISOU 1621  O   SER B 219     4907   7783   6185    791   -161   -429       O
ATOM   1622  CB  SER B 219      47.488 -28.529   7.216  1.00 47.83           C
ANISOU 1622  CB  SER B 219     4636   7688   5849    578     62   -509       C
ATOM   1623  OG  SER B 219      46.387 -29.230   7.774  1.00 47.28           O
ANISOU 1623  OG  SER B 219     4752   7425   5787    544     22   -523       O
ATOM   1624  N   THR B 220      48.217 -31.319   8.479  1.00 50.35           N
ANISOU 1624  N   THR B 220     5153   7717   6260    899    -80   -568       N
ATOM   1625  CA  THR B 220      48.031 -32.322   9.526  1.00 51.01           C
ANISOU 1625  CA  THR B 220     5402   7598   6381    961   -164   -530       C
ATOM   1626  C   THR B 220      49.347 -32.705  10.213  1.00 52.52           C
ANISOU 1626  C   THR B 220     5521   7831   6605   1139   -248   -502       C
ATOM   1627  O   THR B 220      49.405 -32.805  11.440  1.00 52.73           O
ANISOU 1627  O   THR B 220     5622   7783   6629   1145   -335   -411       O
ATOM   1628  CB  THR B 220      47.355 -33.588   8.972  1.00 51.85           C
ANISOU 1628  CB  THR B 220     5676   7505   6520   1016   -157   -616       C
ATOM   1629  OG1 THR B 220      46.087 -33.247   8.413  1.00 50.64           O
ANISOU 1629  OG1 THR B 220     5576   7320   6344    847   -101   -646       O
ATOM   1630  CG2 THR B 220      47.146 -34.613  10.070  1.00 52.84           C
ANISOU 1630  CG2 THR B 220     5986   7396   6695   1061   -237   -542       C
ATOM   1631  N   ASN B 221      50.397 -32.930   9.428  1.00 53.83           N
ANISOU 1631  N   ASN B 221     5536   8129   6787   1300   -224   -581       N
ATOM   1632  CA  ASN B 221      51.688 -33.352   9.983  1.00 55.61           C
ANISOU 1632  CA  ASN B 221     5663   8414   7053   1497   -310   -572       C
ATOM   1633  C   ASN B 221      52.318 -32.317  10.898  1.00 55.29           C
ANISOU 1633  C   ASN B 221     5473   8519   7016   1422   -379   -483       C
ATOM   1634  O   ASN B 221      52.890 -32.673  11.932  1.00 56.37           O
ANISOU 1634  O   ASN B 221     5628   8622   7168   1532   -502   -436       O
ATOM   1635  CB  ASN B 221      52.663 -33.722   8.871  1.00 57.27           C
ANISOU 1635  CB  ASN B 221     5707   8778   7275   1688   -248   -686       C
ATOM   1636  CG  ASN B 221      52.355 -35.072   8.254  1.00 58.51           C
ANISOU 1636  CG  ASN B 221     6037   8753   7442   1856   -243   -802       C
ATOM   1637  OD1 ASN B 221      51.719 -35.928   8.876  1.00 58.72           O
ANISOU 1637  OD1 ASN B 221     6295   8515   7502   1868   -319   -777       O
ATOM   1638  ND2 ASN B 221      52.809 -35.274   7.023  1.00 59.64           N
ANISOU 1638  ND2 ASN B 221     6071   9033   7555   1987   -154   -928       N
ATOM   1639  N   PHE B 222      52.222 -31.043  10.522  1.00 54.07           N
ANISOU 1639  N   PHE B 222     5180   8517   6848   1242   -315   -463       N
ATOM   1640  CA  PHE B 222      52.753 -29.964  11.357  1.00 53.92           C
ANISOU 1640  CA  PHE B 222     5026   8613   6849   1143   -395   -396       C
ATOM   1641  C   PHE B 222      51.990 -29.893  12.674  1.00 53.06           C
ANISOU 1641  C   PHE B 222     5114   8354   6694   1070   -494   -327       C
ATOM   1642  O   PHE B 222      52.575 -29.690  13.737  1.00 53.82           O
ANISOU 1642  O   PHE B 222     5176   8482   6789   1109   -623   -290       O
ATOM   1643  CB  PHE B 222      52.683 -28.614  10.641  1.00 52.96           C
ANISOU 1643  CB  PHE B 222     4751   8636   6735    949   -307   -381       C
ATOM   1644  CG  PHE B 222      53.402 -27.511  11.369  1.00 53.32           C
ANISOU 1644  CG  PHE B 222     4632   8794   6835    849   -401   -334       C
ATOM   1645  CD1 PHE B 222      52.753 -26.772  12.340  1.00 52.20           C
ANISOU 1645  CD1 PHE B 222     4603   8566   6666    712   -487   -294       C
ATOM   1646  CD2 PHE B 222      54.734 -27.228  11.099  1.00 55.09           C
ANISOU 1646  CD2 PHE B 222     4577   9213   7141    895   -411   -340       C
ATOM   1647  CE1 PHE B 222      53.406 -25.758  13.015  1.00 52.81           C
ANISOU 1647  CE1 PHE B 222     4542   8725   6798    621   -599   -277       C
ATOM   1648  CE2 PHE B 222      55.398 -26.215  11.777  1.00 55.72           C
ANISOU 1648  CE2 PHE B 222     4496   9381   7295    781   -520   -308       C
ATOM   1649  CZ  PHE B 222      54.728 -25.477  12.736  1.00 54.56           C
ANISOU 1649  CZ  PHE B 222     4487   9122   7121    644   -624   -285       C
ATOM   1650  N   ILE B 223      50.680 -30.062  12.586  1.00 51.70           N
ANISOU 1650  N   ILE B 223     5136   8033   6474    970   -431   -314       N
ATOM   1651  CA  ILE B 223      49.814 -30.045  13.759  1.00 51.05           C
ANISOU 1651  CA  ILE B 223     5243   7824   6331    899   -485   -241       C
ATOM   1652  C   ILE B 223      50.168 -31.184  14.707  1.00 52.63           C
ANISOU 1652  C   ILE B 223     5574   7908   6516   1071   -584   -190       C
ATOM   1653  O   ILE B 223      50.188 -31.003  15.923  1.00 52.97           O
ANISOU 1653  O   ILE B 223     5689   7941   6496   1079   -679   -120       O
ATOM   1654  CB  ILE B 223      48.335 -30.135  13.338  1.00 49.68           C
ANISOU 1654  CB  ILE B 223     5220   7528   6127    765   -381   -240       C
ATOM   1655  CG1 ILE B 223      47.970 -28.857  12.565  1.00 48.25           C
ANISOU 1655  CG1 ILE B 223     4924   7464   5944    606   -309   -271       C
ATOM   1656  CG2 ILE B 223      47.420 -30.385  14.528  1.00 49.50           C
ANISOU 1656  CG2 ILE B 223     5392   7376   6040    716   -409   -153       C
ATOM   1657  CD1 ILE B 223      46.559 -28.351  12.719  1.00 46.83           C
ANISOU 1657  CD1 ILE B 223     4856   7219   5717    452   -259   -250       C
ATOM   1658  N   VAL B 224      50.443 -32.354  14.138  1.00 53.79           N
ANISOU 1658  N   VAL B 224     5764   7963   6711   1221   -567   -229       N
ATOM   1659  CA  VAL B 224      50.808 -33.515  14.931  1.00 55.59           C
ANISOU 1659  CA  VAL B 224     6133   8051   6938   1405   -664   -174       C
ATOM   1660  C   VAL B 224      52.074 -33.235  15.728  1.00 56.93           C
ANISOU 1660  C   VAL B 224     6167   8366   7099   1542   -807   -154       C
ATOM   1661  O   VAL B 224      52.157 -33.593  16.893  1.00 57.96           O
ANISOU 1661  O   VAL B 224     6425   8428   7168   1623   -916    -64       O
ATOM   1662  CB  VAL B 224      51.004 -34.770  14.055  1.00 56.92           C
ANISOU 1662  CB  VAL B 224     6357   8090   7179   1567   -636   -249       C
ATOM   1663  CG1 VAL B 224      51.704 -35.881  14.833  1.00 59.26           C
ANISOU 1663  CG1 VAL B 224     6763   8262   7492   1803   -762   -196       C
ATOM   1664  CG2 VAL B 224      49.664 -35.253  13.522  1.00 56.10           C
ANISOU 1664  CG2 VAL B 224     6432   7792   7090   1434   -539   -261       C
ATOM   1665  N   LYS B 225      53.054 -32.591  15.109  1.00 57.18           N
ANISOU 1665  N   LYS B 225     5932   8607   7187   1566   -807   -233       N
ATOM   1666  CA  LYS B 225      54.297 -32.300  15.812  1.00 58.73           C
ANISOU 1666  CA  LYS B 225     5956   8958   7399   1684   -955   -230       C
ATOM   1667  C   LYS B 225      54.164 -31.126  16.785  1.00 57.98           C
ANISOU 1667  C   LYS B 225     5838   8945   7246   1530  -1042   -189       C
ATOM   1668  O   LYS B 225      54.876 -31.070  17.776  1.00 59.40           O
ANISOU 1668  O   LYS B 225     5982   9188   7398   1631  -1206   -168       O
ATOM   1669  CB  LYS B 225      55.476 -32.180  14.847  1.00 59.89           C
ANISOU 1669  CB  LYS B 225     5807   9306   7644   1780   -924   -322       C
ATOM   1670  CG  LYS B 225      55.488 -30.980  13.927  1.00 58.68           C
ANISOU 1670  CG  LYS B 225     5443   9321   7530   1578   -805   -358       C
ATOM   1671  CD  LYS B 225      56.866 -30.821  13.279  1.00 60.52           C
ANISOU 1671  CD  LYS B 225     5345   9794   7855   1682   -793   -417       C
ATOM   1672  CE  LYS B 225      57.181 -31.870  12.225  1.00 61.71           C
ANISOU 1672  CE  LYS B 225     5470   9955   8023   1888   -689   -494       C
ATOM   1673  NZ  LYS B 225      57.574 -33.187  12.788  1.00 63.54           N
ANISOU 1673  NZ  LYS B 225     5822  10063   8257   2169   -807   -512       N
ATOM   1674  N   VAL B 226      53.234 -30.212  16.538  1.00 55.98           N
ANISOU 1674  N   VAL B 226     5618   8685   6967   1305   -948   -186       N
ATOM   1675  CA  VAL B 226      52.893 -29.192  17.533  1.00 55.38           C
ANISOU 1675  CA  VAL B 226     5582   8640   6818   1178  -1031   -159       C
ATOM   1676  C   VAL B 226      52.214 -29.842  18.749  1.00 55.76           C
ANISOU 1676  C   VAL B 226     5902   8552   6731   1247  -1090    -69       C
ATOM   1677  O   VAL B 226      52.542 -29.512  19.890  1.00 56.72           O
ANISOU 1677  O   VAL B 226     6053   8728   6770   1294  -1236    -48       O
ATOM   1678  CB  VAL B 226      51.980 -28.101  16.904  1.00 53.31           C
ANISOU 1678  CB  VAL B 226     5307   8385   6562    944   -910   -181       C
ATOM   1679  CG1 VAL B 226      51.200 -27.284  17.935  1.00 52.56           C
ANISOU 1679  CG1 VAL B 226     5344   8262   6365    835   -965   -158       C
ATOM   1680  CG2 VAL B 226      52.800 -27.184  16.020  1.00 53.41           C
ANISOU 1680  CG2 VAL B 226     5047   8556   6690    858   -888   -236       C
ATOM   1681  N   LEU B 227      51.272 -30.756  18.499  1.00 55.29           N
ANISOU 1681  N   LEU B 227     6039   8320   6648   1248   -976    -14       N
ATOM   1682  CA  LEU B 227      50.627 -31.530  19.567  1.00 56.06           C
ANISOU 1682  CA  LEU B 227     6396   8275   6629   1307  -1001    105       C
ATOM   1683  C   LEU B 227      51.667 -32.329  20.340  1.00 58.44           C
ANISOU 1683  C   LEU B 227     6728   8573   6904   1546  -1162    153       C
ATOM   1684  O   LEU B 227      51.738 -32.271  21.561  1.00 59.51           O
ANISOU 1684  O   LEU B 227     6973   8731   6908   1612  -1274    226       O
ATOM   1685  CB  LEU B 227      49.595 -32.503  18.992  1.00 55.63           C
ANISOU 1685  CB  LEU B 227     6510   8019   6608   1261   -858    151       C
ATOM   1686  CG  LEU B 227      48.307 -31.923  18.420  1.00 53.62           C
ANISOU 1686  CG  LEU B 227     6275   7741   6356   1039   -707    129       C
ATOM   1687  CD1 LEU B 227      47.440 -33.046  17.876  1.00 53.78           C
ANISOU 1687  CD1 LEU B 227     6445   7555   6434   1009   -602    162       C
ATOM   1688  CD2 LEU B 227      47.564 -31.118  19.472  1.00 53.08           C
ANISOU 1688  CD2 LEU B 227     6289   7726   6152    937   -708    188       C
ATOM   1689  N   GLU B 228      52.462 -33.086  19.601  1.00 59.46           N
ANISOU 1689  N   GLU B 228     6765   8681   7145   1694  -1175    105       N
ATOM   1690  CA  GLU B 228      53.531 -33.882  20.149  1.00 61.91           C
ANISOU 1690  CA  GLU B 228     7075   8993   7456   1951  -1331    132       C
ATOM   1691  C   GLU B 228      54.466 -33.060  21.009  1.00 62.89           C
ANISOU 1691  C   GLU B 228     7044   9323   7527   2006  -1513    104       C
ATOM   1692  O   GLU B 228      54.919 -33.528  22.047  1.00 64.84           O
ANISOU 1692  O   GLU B 228     7392   9563   7683   2183  -1670    176       O
ATOM   1693  CB  GLU B 228      54.264 -34.510  18.980  1.00 62.64           C
ANISOU 1693  CB  GLU B 228     7018   9089   7694   2083  -1294     35       C
ATOM   1694  CG  GLU B 228      55.528 -35.304  19.259  1.00 65.36           C
ANISOU 1694  CG  GLU B 228     7292   9465   8075   2382  -1449     23       C
ATOM   1695  CD  GLU B 228      56.163 -35.821  17.978  1.00 66.03           C
ANISOU 1695  CD  GLU B 228     7211   9582   8295   2508  -1378    -98       C
ATOM   1696  OE1 GLU B 228      55.423 -36.096  17.003  1.00 64.84           O
ANISOU 1696  OE1 GLU B 228     7133   9318   8187   2415  -1221   -142       O
ATOM   1697  OE2 GLU B 228      57.406 -35.950  17.949  1.00 67.94           O
ANISOU 1697  OE2 GLU B 228     7243   9978   8595   2712  -1484   -159       O
ATOM   1698  N   GLU B 229      54.727 -31.822  20.609  1.00 61.75           N
ANISOU 1698  N   GLU B 229     6668   9353   7439   1849  -1504      5       N
ATOM   1699  CA  GLU B 229      55.576 -30.932  21.398  1.00 62.80           C
ANISOU 1699  CA  GLU B 229     6641   9671   7548   1862  -1692    -43       C
ATOM   1700  C   GLU B 229      54.933 -30.572  22.752  1.00 62.90           C
ANISOU 1700  C   GLU B 229     6873   9658   7368   1833  -1782     23       C
ATOM   1701  O   GLU B 229      55.351 -29.649  23.430  1.00 63.48           O
ANISOU 1701  O   GLU B 229     6855   9865   7399   1798  -1932    -38       O
ATOM   1702  CB  GLU B 229      56.050 -29.745  20.520  1.00 61.90           C
ANISOU 1702  CB  GLU B 229     6221   9721   7576   1685  -1651   -156       C
ATOM   1703  CG  GLU B 229      57.218 -28.938  21.084  1.00 63.59           C
ANISOU 1703  CG  GLU B 229     6191  10131   7841   1701  -1859   -230       C
ATOM   1704  CD  GLU B 229      58.500 -29.748  21.181  1.00 66.19           C
ANISOU 1704  CD  GLU B 229     6357  10557   8233   1956  -1993   -249       C
ATOM   1705  OE1 GLU B 229      58.922 -30.332  20.146  1.00 66.48           O
ANISOU 1705  OE1 GLU B 229     6258  10618   8384   2036  -1880   -271       O
ATOM   1706  OE2 GLU B 229      59.084 -29.800  22.286  1.00 68.13           O
ANISOU 1706  OE2 GLU B 229     6612  10868   8407   2094  -2218   -250       O
ATOM   1707  N   LEU B 230      53.960 -31.370  23.190  1.00 62.76           N
ANISOU 1707  N   LEU B 230     7148   9470   7228   1862  -1699    149       N
ATOM   1708  CA  LEU B 230      53.587 -31.391  24.592  1.00 63.85           C
ANISOU 1708  CA  LEU B 230     7508   9602   7152   1926  -1797    244       C
ATOM   1709  C   LEU B 230      53.326 -32.851  25.082  1.00 65.49           C
ANISOU 1709  C   LEU B 230     7983   9629   7273   2102  -1783    417       C
ATOM   1710  O   LEU B 230      52.364 -33.470  24.617  1.00 64.56           O
ANISOU 1710  O   LEU B 230     8014   9333   7184   2014  -1601    498       O
ATOM   1711  CB  LEU B 230      52.339 -30.508  24.798  1.00 61.98           C
ANISOU 1711  CB  LEU B 230     7374   9360   6816   1710  -1672    244       C
ATOM   1712  CG  LEU B 230      52.229 -29.144  24.074  1.00 60.03           C
ANISOU 1712  CG  LEU B 230     6921   9210   6679   1498  -1625     99       C
ATOM   1713  CD1 LEU B 230      52.018 -29.303  22.577  1.00 58.34           C
ANISOU 1713  CD1 LEU B 230     6587   8931   6651   1386  -1449     65       C
ATOM   1714  CD2 LEU B 230      51.084 -28.298  24.629  1.00 58.94           C
ANISOU 1714  CD2 LEU B 230     6918   9077   6400   1358  -1558     99       C
ATOM   1715  N   LYS B 231      54.170 -33.480  25.917  1.00 68.13           N
ANISOU 1715  N   LYS B 231     8377   9984   7524   2349  -1972    480       N
ATOM   1716  CA  LYS B 231      55.660 -33.476  25.944  1.00 69.97           C
ANISOU 1716  CA  LYS B 231     8383  10365   7837   2545  -2189    383       C
ATOM   1717  C   LYS B 231      56.445 -32.207  26.277  1.00 70.22           C
ANISOU 1717  C   LYS B 231     8164  10643   7874   2498  -2364    230       C
ATOM   1718  O   LYS B 231      57.671 -32.183  26.209  1.00 71.86           O
ANISOU 1718  O   LYS B 231     8138  10986   8179   2634  -2533    143       O
ATOM   1719  CB  LYS B 231      56.206 -34.207  24.709  1.00 69.99           C
ANISOU 1719  CB  LYS B 231     8236  10299   8059   2622  -2118    328       C
ATOM   1720  CG  LYS B 231      57.674 -34.027  24.345  1.00 71.45           C
ANISOU 1720  CG  LYS B 231     8090  10675   8384   2767  -2271    194       C
ATOM   1721  CD  LYS B 231      57.991 -34.698  23.014  1.00 71.26           C
ANISOU 1721  CD  LYS B 231     7936  10591   8551   2827  -2143    133       C
ATOM   1722  CE  LYS B 231      58.037 -33.715  21.845  1.00 69.23           C
ANISOU 1722  CE  LYS B 231     7395  10470   8437   2603  -2001     -1       C
ATOM   1723  NZ  LYS B 231      59.329 -32.970  21.768  1.00 70.51           N
ANISOU 1723  NZ  LYS B 231     7189  10900   8702   2636  -2138   -117       N
ATOM   1724  N   LEU B 232      55.755 -31.182  26.726  1.00 68.99           N
ANISOU 1724  N   LEU B 232     8059  10542   7610   2319  -2341    196       N
ATOM   1725  CA  LEU B 232      56.416 -29.960  27.136  1.00 69.51           C
ANISOU 1725  CA  LEU B 232     7926  10803   7681   2262  -2527     46       C
ATOM   1726  C   LEU B 232      55.778 -29.537  28.427  1.00 70.16           C
ANISOU 1726  C   LEU B 232     8245  10916   7496   2274  -2605     80       C
ATOM   1727  O   LEU B 232      56.408 -28.882  29.226  1.00 71.77           O
ANISOU 1727  O   LEU B 232     8380  11268   7621   2334  -2837    -18       O
ATOM   1728  CB  LEU B 232      56.333 -28.867  26.065  1.00 67.32           C
ANISOU 1728  CB  LEU B 232     7407  10571   7601   2002  -2414    -85       C
ATOM   1729  CG  LEU B 232      57.018 -27.541  26.483  1.00 68.15           C
ANISOU 1729  CG  LEU B 232     7306  10843   7745   1911  -2619   -243       C
ATOM   1730  CD1 LEU B 232      58.263 -27.157  25.668  1.00 68.93           C
ANISOU 1730  CD1 LEU B 232     7018  11071   8100   1868  -2693   -352       C
ATOM   1731  CD2 LEU B 232      56.017 -26.395  26.522  1.00 66.28           C
ANISOU 1731  CD2 LEU B 232     7152  10571   7459   1683  -2531   -298       C
ATOM   1732  N   GLU B 233      54.524 -29.911  28.647  1.00 69.13           N
ANISOU 1732  N   GLU B 233     8387  10658   7222   2220  -2416    214       N
ATOM   1733  CA  GLU B 233      53.985 -29.866  29.979  1.00 70.51           C
ANISOU 1733  CA  GLU B 233     8821  10872   7098   2307  -2476    295       C
ATOM   1734  C   GLU B 233      54.748 -30.784  30.943  1.00 73.69           C
ANISOU 1734  C   GLU B 233     9351  11304   7343   2600  -2678    404       C
ATOM   1735  O   GLU B 233      54.716 -30.549  32.145  1.00 75.54           O
ANISOU 1735  O   GLU B 233     9740  11645   7315   2715  -2818    423       O
ATOM   1736  CB  GLU B 233      52.510 -30.228  29.970  1.00 69.17           C
ANISOU 1736  CB  GLU B 233     8892  10566   6823   2193  -2207    445       C
ATOM   1737  CG  GLU B 233      51.799 -29.855  31.256  1.00 70.33           C
ANISOU 1737  CG  GLU B 233     9269  10801   6654   2235  -2222    499       C
ATOM   1738  CD  GLU B 233      50.549 -30.656  31.469  1.00 70.24           C
ANISOU 1738  CD  GLU B 233     9513  10662   6514   2195  -1975    719       C
ATOM   1739  OE1 GLU B 233      49.827 -30.875  30.480  1.00 68.15           O
ANISOU 1739  OE1 GLU B 233     9206  10261   6425   2019  -1758    747       O
ATOM   1740  OE2 GLU B 233      50.290 -31.054  32.619  1.00 72.47           O
ANISOU 1740  OE2 GLU B 233    10031  10988   6518   2335  -2000    867       O
ATOM   1741  N   HIS B 234      55.410 -31.826  30.430  1.00 74.52           N
ANISOU 1741  N   HIS B 234     9405  11320   7591   2738  -2697    472       N
ATOM   1742  CA  HIS B 234      56.299 -32.662  31.247  1.00 77.78           C
ANISOU 1742  CA  HIS B 234     9902  11765   7888   3044  -2921    558       C
ATOM   1743  C   HIS B 234      57.788 -32.625  30.798  1.00 79.03           C
ANISOU 1743  C   HIS B 234     9730  12045   8253   3174  -3136    408       C
ATOM   1744  O   HIS B 234      58.669 -32.189  31.538  1.00 81.15           O
ANISOU 1744  O   HIS B 234     9890  12497   8445   3306  -3409    312       O
ATOM   1745  CB  HIS B 234      55.821 -34.125  31.224  1.00 78.64           C
ANISOU 1745  CB  HIS B 234    10280  11639   7961   3161  -2786    800       C
ATOM   1746  CG  HIS B 234      54.334 -34.311  31.131  1.00 76.95           C
ANISOU 1746  CG  HIS B 234    10297  11264   7676   2965  -2500    944       C
ATOM   1747  ND1 HIS B 234      53.582 -34.808  32.173  1.00 78.57           N
ANISOU 1747  ND1 HIS B 234    10828  11414   7612   3027  -2446   1162       N
ATOM   1748  CD2 HIS B 234      53.475 -34.142  30.099  1.00 74.12           C
ANISOU 1748  CD2 HIS B 234     9882  10794   7485   2716  -2253    911       C
ATOM   1749  CE1 HIS B 234      52.319 -34.902  31.800  1.00 76.79           C
ANISOU 1749  CE1 HIS B 234    10713  11057   7407   2810  -2172   1253       C
ATOM   1750  NE2 HIS B 234      52.227 -34.503  30.545  1.00 74.05           N
ANISOU 1750  NE2 HIS B 234    10140  10672   7323   2624  -2063   1095       N
ATOM   1751  N   HIS B 235      58.025 -33.094  29.569  1.00 77.87           N
ANISOU 1751  N   HIS B 235     9421  11803   8363   3137  -3004    384       N
ATOM   1752  CA  HIS B 235      59.353 -33.430  29.001  1.00 79.35           C
ANISOU 1752  CA  HIS B 235     9317  12078   8756   3302  -3143    287       C
ATOM   1753  C   HIS B 235      60.065 -34.634  29.623  1.00 82.64           C
ANISOU 1753  C   HIS B 235     9857  12451   9092   3659  -3325    402       C
ATOM   1754  O   HIS B 235      61.184 -34.952  29.229  1.00 84.24           O
ANISOU 1754  O   HIS B 235     9813  12741   9452   3834  -3452    319       O
ATOM   1755  CB  HIS B 235      60.293 -32.213  28.876  1.00 79.59           C
ANISOU 1755  CB  HIS B 235     8970  12359   8914   3208  -3310     73       C
ATOM   1756  CG  HIS B 235      60.511 -31.788  27.451  1.00 77.64           C
ANISOU 1756  CG  HIS B 235     8415  12138   8947   3018  -3141    -41       C
ATOM   1757  ND1 HIS B 235      61.231 -32.548  26.552  1.00 78.39           N
ANISOU 1757  ND1 HIS B 235     8327  12231   9226   3154  -3095    -57       N
ATOM   1758  CD2 HIS B 235      60.050 -30.719  26.754  1.00 75.17           C
ANISOU 1758  CD2 HIS B 235     7969  11850   8741   2716  -2993   -131       C
ATOM   1759  CE1 HIS B 235      61.219 -31.956  25.369  1.00 76.48           C
ANISOU 1759  CE1 HIS B 235     7847  12032   9178   2941  -2919   -149       C
ATOM   1760  NE2 HIS B 235      60.509 -30.846  25.464  1.00 74.49           N
ANISOU 1760  NE2 HIS B 235     7625  11789   8888   2669  -2857   -185       N
ATOM   1761  N   HIS B 236      59.385 -35.346  30.520  1.00 83.76           N
ANISOU 1761  N   HIS B 236    10377  12449   8998   3768  -3315    606       N
ATOM   1762  CA  HIS B 236      59.966 -36.495  31.201  1.00 87.14           C
ANISOU 1762  CA  HIS B 236    10979  12807   9323   4114  -3492    750       C
ATOM   1763  C   HIS B 236      60.026 -37.704  30.259  1.00 87.29           C
ANISOU 1763  C   HIS B 236    11038  12589   9540   4221  -3364    819       C
ATOM   1764  O   HIS B 236      61.061 -37.944  29.650  1.00 88.34           O
ANISOU 1764  O   HIS B 236    10908  12795   9862   4378  -3462    698       O
ATOM   1765  CB  HIS B 236      59.183 -36.805  32.487  1.00 88.57           C
ANISOU 1765  CB  HIS B 236    11565  12917   9170   4180  -3507    971       C
ATOM   1766  CG  HIS B 236      60.020 -37.360  33.593  1.00 92.55           C
ANISOU 1766  CG  HIS B 236    12187  13499   9480   4535  -3805   1062       C
ATOM   1767  ND1 HIS B 236      61.120 -36.704  34.097  1.00 94.36           N
ANISOU 1767  ND1 HIS B 236    12173  14004   9674   4675  -4112    890       N
ATOM   1768  CD2 HIS B 236      59.898 -38.500  34.311  1.00 95.31           C
ANISOU 1768  CD2 HIS B 236    12878  13682   9654   4778  -3853   1316       C
ATOM   1769  CE1 HIS B 236      61.651 -37.426  35.067  1.00 98.03           C
ANISOU 1769  CE1 HIS B 236    12821  14486   9941   5009  -4345   1023       C
ATOM   1770  NE2 HIS B 236      60.928 -38.521  35.217  1.00 98.68           N
ANISOU 1770  NE2 HIS B 236    13268  14296   9928   5081  -4190   1293       N
ATOM   1771  N   HIS B 237      58.914 -38.416  30.089  1.00 86.36           N
ANISOU 1771  N   HIS B 237    11225  12195   9393   4124  -3141    994       N
ATOM   1772  CA  HIS B 237      58.872 -39.694  29.348  1.00 87.08           C
ANISOU 1772  CA  HIS B 237    11433  12005   9648   4243  -3045   1074       C
ATOM   1773  C   HIS B 237      60.206 -40.456  29.237  1.00 90.09           C
ANISOU 1773  C   HIS B 237    11686  12408  10137   4611  -3265   1023       C
ATOM   1774  O   HIS B 237      60.873 -40.468  28.209  1.00 89.67           O
ANISOU 1774  O   HIS B 237    11347  12415  10309   4654  -3247    847       O
ATOM   1775  CB  HIS B 237      58.192 -39.518  27.974  1.00 83.84           C
ANISOU 1775  CB  HIS B 237    10909  11491   9454   3971  -2774    966       C
ATOM   1776  CG  HIS B 237      58.983 -38.727  26.976  1.00 82.43           C
ANISOU 1776  CG  HIS B 237    10309  11538   9473   3911  -2778    713       C
ATOM   1777  ND1 HIS B 237      59.227 -37.377  27.113  1.00 81.08           N
ANISOU 1777  ND1 HIS B 237     9887  11643   9279   3745  -2829    576       N
ATOM   1778  CD2 HIS B 237      59.545 -39.093  25.799  1.00 82.33           C
ANISOU 1778  CD2 HIS B 237    10088  11511   9684   3984  -2722    580       C
ATOM   1779  CE1 HIS B 237      59.926 -36.952  26.076  1.00 80.29           C
ANISOU 1779  CE1 HIS B 237     9435  11686   9386   3706  -2799    393       C
ATOM   1780  NE2 HIS B 237      60.134 -37.974  25.266  1.00 81.03           N
ANISOU 1780  NE2 HIS B 237     9543  11627   9618   3858  -2727    391       N
CONECT 5732 5733 5734 5735 5736
CONECT 5733 5732 5737
CONECT 5734 5732 5738
CONECT 5735 5732 5739
CONECT 5736 5732
CONECT 5737 5733
CONECT 5738 5734
CONECT 5739 5735
END



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

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