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***  HYDROLASE/HYDROLASE INHIBITOR 08-MAR-07 2P3B  ***

elNémo ID: 21040914423043491

Job options:

ID        	=	 21040914423043491
JOBID     	=	 HYDROLASE/HYDROLASE INHIBITOR 08-MAR-07 2P3B
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    HYDROLASE/HYDROLASE INHIBITOR           08-MAR-07   2P3B              
TITLE     CRYSTAL STRUCTURE OF THE SUBTYPE B WILD TYPE HIV PROTEASE COMPLEXED   
TITLE    2 WITH TL-3 INHIBITOR                                                  
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: PROTEASE;                                                  
COMPND   3 CHAIN: A;                                                            
COMPND   4 EC: 3.4.23.16;                                                       
COMPND   5 ENGINEERED: YES;                                                     
COMPND   6 OTHER_DETAILS: CYS AT POSITION 67;                                   
COMPND   7 MOL_ID: 2;                                                           
COMPND   8 MOLECULE: PROTEASE;                                                  
COMPND   9 CHAIN: B;                                                            
COMPND  10 EC: 3.4.23.16;                                                       
COMPND  11 ENGINEERED: YES;                                                     
COMPND  12 OTHER_DETAILS: CME AT POSITION 67                                    
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE   3 ORGANISM_TAXID: 11676;                                               
SOURCE   4 GENE: GAG-POL;                                                       
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PET11A;                                   
SOURCE  10 MOL_ID: 2;                                                           
SOURCE  11 ORGANISM_SCIENTIFIC: HUMAN IMMUNODEFICIENCY VIRUS 1;                 
SOURCE  12 ORGANISM_TAXID: 11676;                                               
SOURCE  13 GENE: GAG-POL;                                                       
SOURCE  14 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21(DE3);                       
SOURCE  15 EXPRESSION_SYSTEM_TAXID: 469008;                                     
SOURCE  16 EXPRESSION_SYSTEM_STRAIN: BL21(DE3);                                 
SOURCE  17 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE  18 EXPRESSION_SYSTEM_PLASMID: PET11A                                    
KEYWDS    WILD TYPE SUBTYPE B HIV PROTEASE, TL-3 INHIBITOR, HYDROLASE-HYDROLASE 
KEYWDS   2 INHIBITOR COMPLEX                                                    
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    M.SANCHES,S.KRAUCHENCO,N.H.MARTINS,A.GUSTCHINA,A.WLODAWER,            
AUTHOR   2 I.POLIKARPOV                                                         
REVDAT   5   18-OCT-17 2P3B    1       REMARK                                   
REVDAT   4   13-JUL-11 2P3B    1       VERSN                                    
REVDAT   3   24-FEB-09 2P3B    1       VERSN                                    
REVDAT   2   29-MAY-07 2P3B    1       JRNL                                     
REVDAT   1   24-APR-07 2P3B    0                                                
JRNL        AUTH   M.SANCHES,S.KRAUCHENCO,N.H.MARTINS,A.GUSTCHINA,A.WLODAWER,   
JRNL        AUTH 2 I.POLIKARPOV                                                 
JRNL        TITL   STRUCTURAL CHARACTERIZATION OF B AND NON-B SUBTYPES OF       
JRNL        TITL 2 HIV-PROTEASE: INSIGHTS INTO THE NATURAL SUSCEPTIBILITY TO    
JRNL        TITL 3 DRUG RESISTANCE DEVELOPMENT.                                 
JRNL        REF    J.MOL.BIOL.                   V. 369  1029 2007              
JRNL        REFN                   ISSN 0022-2836                               
JRNL        PMID   17467738                                                     
JRNL        DOI    10.1016/J.JMB.2007.03.049                                    
REMARK   1                                                                      
REMARK   1 REFERENCE 1                                                          
REMARK   1  AUTH   M.SANCHES,N.H.MARTINS,A.CALAZANS,R.M.BRINDEIRO,A.TANURI,     
REMARK   1  AUTH 2 O.A.C.ANTUNES,I.POLIKARPOV                                   
REMARK   1  TITL   CRYSTALLIZATION OF A NON-B AND A B MUTANT HIV PROTEASE       
REMARK   1  REF    ACTA CRYSTALLOGR.,SECT.D      V. D60  1625 2004              
REMARK   1  REFN                   ISSN 0907-4449                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.10 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.2.0003                                      
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) : 2.10                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 16.58                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 99.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 11011                          
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) : 0.165                           
REMARK   3   R VALUE            (WORKING SET) : 0.159                           
REMARK   3   FREE R VALUE                     : 0.219                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 9.800                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 1084                            
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 2.10                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.15                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 708                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.1910                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 74                           
REMARK   3   BIN FREE R VALUE                    : 0.2730                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1520                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 66                                      
REMARK   3   SOLVENT ATOMS            : 98                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 31.32                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.04000                                              
REMARK   3    B22 (A**2) : 0.04000                                              
REMARK   3    B33 (A**2) : -0.06000                                             
REMARK   3    B12 (A**2) : 0.02000                                              
REMARK   3    B13 (A**2) : 0.00000                                              
REMARK   3    B23 (A**2) : 0.00000                                              
REMARK   3                                                                      
REMARK   3  ESTIMATED OVERALL COORDINATE ERROR.                                 
REMARK   3   ESU BASED ON R VALUE                            (A): NULL          
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.202         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.142         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 10.370        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.968                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.947                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1737 ; 0.015 ; 0.022       
REMARK   3   BOND LENGTHS OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  2366 ; 1.575 ; 2.055       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  NULL ;  NULL ;  NULL       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   212 ; 6.534 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    52 ;40.853 ;25.000       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   282 ;17.262 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;18.410 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   277 ; 0.085 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1268 ; 0.005 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):   690 ; 0.222 ; 0.200       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  1184 ; 0.320 ; 0.200       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):    91 ; 0.230 ; 0.200       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):    26 ; 0.172 ; 0.200       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):     2 ; 0.111 ; 0.200       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):  1066 ; 1.638 ; 1.500       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  1684 ; 2.840 ; 2.000       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   758 ; 2.785 ; 3.000       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):   682 ; 3.911 ; 4.500       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  1678 ; 1.947 ; 3.000       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  1563 ;13.270 ; 3.000       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : 1                                 
REMARK   3                                                                      
REMARK   3  NCS GROUP NUMBER               : 1                                  
REMARK   3     CHAIN NAMES                    : A B                             
REMARK   3     NUMBER OF COMPONENTS NCS GROUP : 3                               
REMARK   3       COMPONENT C  SSSEQI  TO  C   SSSEQI   CODE                     
REMARK   3           1     A      1       A      34      1                      
REMARK   3           1     B      1       B      34      1                      
REMARK   3           2     A     35       A      64      2                      
REMARK   3           2     B     35       B      64      2                      
REMARK   3           3     A     65       A      99      1                      
REMARK   3           3     B     65       B      99      1                      
REMARK   3                   GROUP CHAIN        COUNT   RMS     WEIGHT          
REMARK   3   TIGHT POSITIONAL   1    A    (A):    649 ; 0.030 ; 0.050           
REMARK   3   MEDIUM POSITIONAL  1    A    (A):    109 ; 0.200 ; 0.500           
REMARK   3   TIGHT THERMAL      1    A (A**2):    649 ; 0.090 ; 0.500           
REMARK   3   MEDIUM THERMAL     1    A (A**2):    109 ; 0.630 ; 2.000           
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : NULL                                       
REMARK   3                                                                      
REMARK   3  BULK SOLVENT MODELLING.                                             
REMARK   3   METHOD USED : MASK                                                 
REMARK   3   PARAMETERS FOR MASK CALCULATION                                    
REMARK   3   VDW PROBE RADIUS   : 1.20                                          
REMARK   3   ION PROBE RADIUS   : 0.80                                          
REMARK   3   SHRINKAGE RADIUS   : 0.80                                          
REMARK   3                                                                      
REMARK   3  OTHER REFINEMENT REMARKS: HYDROGENS HAVE BEEN ADDED IN THE RIDING   
REMARK   3  POSITIONS                                                           
REMARK   4                                                                      
REMARK   4 2P3B COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 29-MAR-07.                  
REMARK 100 THE DEPOSITION ID IS D_1000041912.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 01-FEB-98                          
REMARK 200  TEMPERATURE           (KELVIN) : 298                                
REMARK 200  PH                             : 6.2                                
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          : RIGAKU RU200                       
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.5418                             
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : MIRRORS                            
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : MAR SCANNER 345 MM PLATE           
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : DENZO, MOSFLM                      
REMARK 200  DATA SCALING SOFTWARE          : SCALEPACK                          
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 11047                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.100                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 54.720                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 99.7                               
REMARK 200  DATA REDUNDANCY                : 3.700                              
REMARK 200  R MERGE                    (I) : 0.07500                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 13.6000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 2.10                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 2.21                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY IN SHELL       : 3.70                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.41400                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : 2.700                              
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: CRYSTAL STRUCTURE OF THE MULTI-DRUG RESISTANT        
REMARK 200  MUTANT SUBTYPE B HIV PROTEASE COMPLEXED WITH TL-3 INHIBITOR         
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 44.44                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.21                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 15% SATURATED AMMONIUM SULFATE           
REMARK 280  SOLUTION, 6% (V/V) MPD, 85MM SODIUM CITRATE/170MM SODIUM            
REMARK 280  PHOSPHATE, 0.02% SODIUM AZIDE, PH 6.2, VAPOR DIFFUSION, HANGING     
REMARK 280  DROP, TEMPERATURE 277K                                              
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 61                             
REMARK 290                                                                      
REMARK 290      SYMOP   SYMMETRY                                                
REMARK 290     NNNMMM   OPERATOR                                                
REMARK 290       1555   X,Y,Z                                                   
REMARK 290       2555   -Y,X-Y,Z+1/3                                            
REMARK 290       3555   -X+Y,-X,Z+2/3                                           
REMARK 290       4555   -X,-Y,Z+1/2                                             
REMARK 290       5555   Y,-X+Y,Z+5/6                                            
REMARK 290       6555   X-Y,X,Z+1/6                                             
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 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   2  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   2  0.000000  0.000000  1.000000       27.80467            
REMARK 290   SMTRY1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   3 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   3  0.000000  0.000000  1.000000       55.60933            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000       41.70700            
REMARK 290   SMTRY1   5  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   5 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000  1.000000       69.51167            
REMARK 290   SMTRY1   6  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   6  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   6  0.000000  0.000000  1.000000       13.90233            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: DIMERIC                           
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: DIMERIC                    
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 5180 ANGSTROM**2                          
REMARK 350 SURFACE AREA OF THE COMPLEX: 9560 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -26.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A, B                                  
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 480                                                                      
REMARK 480 ZERO OCCUPANCY ATOM                                                  
REMARK 480 THE FOLLOWING RESIDUES HAVE ATOMS MODELED WITH ZERO                  
REMARK 480 OCCUPANCY. THE LOCATION AND PROPERTIES OF THESE ATOMS                
REMARK 480 MAY NOT BE RELIABLE. (M=MODEL NUMBER; RES=RESIDUE NAME;              
REMARK 480 C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):         
REMARK 480   M RES C SSEQI ATOMS                                                
REMARK 480     ARG A   41   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS A   43   CD   CE   NZ                                        
REMARK 480     LYS A   55   CG   CD   CE   NZ                                   
REMARK 480     SER B   37   OG                                                  
REMARK 480     ARG B   41   CG   CD   NE   CZ   NH1  NH2                        
REMARK 480     LYS B   43   CD   CE   NZ                                        
REMARK 480     LYS B   55   CG   CD   CE   NZ                                   
REMARK 480     CME B   67   SD   CE   CZ   OH                                   
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: CLOSE CONTACTS IN SAME ASYMMETRIC UNIT                     
REMARK 500                                                                      
REMARK 500 THE FOLLOWING ATOMS ARE IN CLOSE CONTACT.                            
REMARK 500                                                                      
REMARK 500  ATM1  RES C  SSEQI   ATM2  RES C  SSEQI           DISTANCE          
REMARK 500   OE1  GLU A    34     O    HOH A   146              2.19            
REMARK 500   O    HOH B   108     O    HOH B   144              2.19            
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    ARG A  41   CB    ARG A  41   CG     -0.540                       
REMARK 500    LYS A  43   CG    LYS A  43   CD     -0.252                       
REMARK 500    SER B  37   CB    SER B  37   OG     -0.342                       
REMARK 500    ARG B  41   CB    ARG B  41   CG     -0.791                       
REMARK 500    LYS B  43   CG    LYS B  43   CD     -0.305                       
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND ANGLES                                       
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,A3,1X,A1,I4,A1,3(1X,A4,2X),12X,F5.1)              
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   ATM2   ATM3                                     
REMARK 500    ARG B  41   CA  -  CB  -  CG  ANGL. DEV. =  33.3 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 600                                                                      
REMARK 600 HETEROGEN                                                            
REMARK 600                                                                      
REMARK 600 THE INHIBITOR IS A C2 SYMMETRIC HIV PROTEASE                         
REMARK 630                                                                      
REMARK 630 MOLECULE TYPE: PEPTIDE-LIKE INHIBITOR                                
REMARK 630 MOLECULE NAME: BENZYL [(1S,4S,7S,8R,9R,10S,13S,16S)-7,10-DIBENZYL-   
REMARK 630 8,9-DIHYDROXY-1,16-DIMETHYL-4,13-BIS(1-METHYLETHYL)-2,5,12,15,18-    
REMARK 630 PENTAOXO-20-PHENYL-19-OXA-3,6,11,14,17-PENTAAZAICOS-1-YL]CARBAMATE   
REMARK 630 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 630  SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                           
REMARK 630                                                                      
REMARK 630   M RES C SSSEQI                                                     
REMARK 630     3TL A   101                                                      
REMARK 630 SOURCE: NULL                                                         
REMARK 630 TAXONOMY: NULL                                                       
REMARK 630 SUBCOMP:    PHQ ALA VAL PHL PHL VAL ALA PHQ                          
REMARK 630 DETAILS: NULL                                                        
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: BINDING SITE FOR RESIDUE 3TL A 101                 
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 3TLH   RELATED DB: PDB                                   
REMARK 900 SAME DATASET PREVIOUSLY PUBLISHED IN P6(1)22 SPACE GROUP.            
REMARK 900 RELATED ID: 2P3A   RELATED DB: PDB                                   
REMARK 900 CRYSTAL STRUCTURE OF THE MULTI-DRUG RESISTANT MUTANT SUBTYPE B HIV   
REMARK 900 PROTEASE COMPLEXED WITH TL-3 INHIBITOR                               
DBREF  2P3B A    1    99  UNP    P03367   POL_HV1BR      501    599             
DBREF  2P3B B    1    99  UNP    P03367   POL_HV1BR      501    599             
SEQADV 2P3B LYS A    7  UNP  P03367    GLN   507 ENGINEERED                     
SEQADV 2P3B LYS B    7  UNP  P03367    GLN   507 ENGINEERED                     
SEQRES   1 A   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 A   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 A   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO          
SEQRES   4 A   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 A   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
SEQRES   6 A   99  ILE CYS GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 A   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 A   99  GLN ILE GLY CYS THR LEU ASN PHE                              
SEQRES   1 B   99  PRO GLN ILE THR LEU TRP LYS ARG PRO LEU VAL THR ILE          
SEQRES   2 B   99  LYS ILE GLY GLY GLN LEU LYS GLU ALA LEU LEU ASP THR          
SEQRES   3 B   99  GLY ALA ASP ASP THR VAL LEU GLU GLU MET SER LEU PRO          
SEQRES   4 B   99  GLY ARG TRP LYS PRO LYS MET ILE GLY GLY ILE GLY GLY          
SEQRES   5 B   99  PHE ILE LYS VAL ARG GLN TYR ASP GLN ILE LEU ILE GLU          
SEQRES   6 B   99  ILE CME GLY HIS LYS ALA ILE GLY THR VAL LEU VAL GLY          
SEQRES   7 B   99  PRO THR PRO VAL ASN ILE ILE GLY ARG ASN LEU LEU THR          
SEQRES   8 B   99  GLN ILE GLY CYS THR LEU ASN PHE                              
MODRES 2P3B CME B   67  CYS  S,S-(2-HYDROXYETHYL)THIOCYSTEINE                   
HET    CME  B  67      20                                                       
HET    3TL  A 101     132                                                       
HETNAM     CME S,S-(2-HYDROXYETHYL)THIOCYSTEINE                                 
HETNAM     3TL BENZYL [(1S,4S,7S,8R,9R,10S,13S,16S)-7,10-DIBENZYL-8,9-          
HETNAM   2 3TL  DIHYDROXY-1,16-DIMETHYL-4,13-BIS(1-METHYLETHYL)-2,5,            
HETNAM   3 3TL  12,15,18-PENTAOXO-20-PHENYL-19-OXA-3,6,11,14,17-                
HETNAM   4 3TL  PENTAAZAICOS-1-YL]CARBAMATE                                     
HETSYN     3TL TL-3, C2 SYMMETRIC INHIBITOR                                     
FORMUL   2  CME    C5 H11 N O3 S2                                               
FORMUL   3  3TL    C50 H64 N6 O10                                               
FORMUL   4  HOH   *98(H2 O)                                                     
HELIX    1   1 GLY A   86  THR A   91  1                                   6    
HELIX    2   2 GLY B   86  THR B   91  1                                   6    
SHEET    1   A 4 GLN A   2  ILE A   3  0                                        
SHEET    2   A 4 THR B  96  ASN B  98 -1  O  LEU B  97   N  ILE A   3           
SHEET    3   A 4 THR A  96  ASN A  98 -1  N  THR A  96   O  ASN B  98           
SHEET    4   A 4 GLN B   2  ILE B   3 -1  O  ILE B   3   N  LEU A  97           
SHEET    1   B 8 LYS A  43  GLY A  49  0                                        
SHEET    2   B 8 GLY A  52  ILE A  66 -1  O  VAL A  56   N  LYS A  45           
SHEET    3   B 8 HIS A  69  VAL A  77 -1  O  VAL A  77   N  ARG A  57           
SHEET    4   B 8 VAL A  32  LEU A  33  1  N  LEU A  33   O  LEU A  76           
SHEET    5   B 8 ILE A  84  ILE A  85 -1  O  ILE A  84   N  VAL A  32           
SHEET    6   B 8 GLN A  18  LEU A  24  1  N  LEU A  23   O  ILE A  85           
SHEET    7   B 8 LEU A  10  ILE A  15 -1  N  ILE A  13   O  LYS A  20           
SHEET    8   B 8 GLY A  52  ILE A  66 -1  O  GLU A  65   N  LYS A  14           
SHEET    1   C 8 LYS B  43  GLY B  49  0                                        
SHEET    2   C 8 GLY B  52  ILE B  66 -1  O  VAL B  56   N  LYS B  45           
SHEET    3   C 8 HIS B  69  VAL B  77 -1  O  VAL B  77   N  ARG B  57           
SHEET    4   C 8 VAL B  32  LEU B  33  1  N  LEU B  33   O  LEU B  76           
SHEET    5   C 8 ILE B  84  ILE B  85 -1  O  ILE B  84   N  VAL B  32           
SHEET    6   C 8 GLN B  18  LEU B  24  1  N  LEU B  23   O  ILE B  85           
SHEET    7   C 8 LEU B  10  ILE B  15 -1  N  ILE B  13   O  LYS B  20           
SHEET    8   C 8 GLY B  52  ILE B  66 -1  O  GLU B  65   N  LYS B  14           
LINK         C   ILE B  66                 N  ACME B  67     1555   1555  1.33  
LINK         C   ILE B  66                 N  BCME B  67     1555   1555  1.33  
LINK         C  ACME B  67                 N   GLY B  68     1555   1555  1.33  
LINK         C  BCME B  67                 N   GLY B  68     1555   1555  1.33  
SITE     1 AC1 31 ARG A   8  ASP A  25  GLY A  27  ALA A  28                    
SITE     2 AC1 31 ASP A  29  MET A  46  ILE A  47  GLY A  48                    
SITE     3 AC1 31 GLY A  49  ILE A  50  PHE A  53  PRO A  81                    
SITE     4 AC1 31 VAL A  82  ILE A  84  HOH A 102  HOH A 107                    
SITE     5 AC1 31 ARG B   8  ASP B  25  GLY B  27  ALA B  28                    
SITE     6 AC1 31 ASP B  29  MET B  46  ILE B  47  GLY B  48                    
SITE     7 AC1 31 GLY B  49  ILE B  50  PHE B  53  PRO B  81                    
SITE     8 AC1 31 VAL B  82  ILE B  84  HOH B 105                               
CRYST1   63.164   63.164   83.414  90.00  90.00 120.00 P 61          6          
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      0.015832  0.009140  0.000000        0.00000                         
SCALE2      0.000000  0.018281  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.011988        0.00000                         
ATOM      1  N   PRO A   1      39.964  -8.579   4.008  1.00 39.48           N  
ANISOU    1  N   PRO A   1     3893   5389   5719    599    555   1109       N  
ATOM      2  CA  PRO A   1      39.750  -8.712   2.571  1.00 39.22           C  
ANISOU    2  CA  PRO A   1     3870   5353   5678    631    640   1128       C  
ATOM      3  C   PRO A   1      39.528  -7.370   1.876  1.00 39.29           C  
ANISOU    3  C   PRO A   1     3912   5313   5703    692    728   1112       C  
ATOM      4  O   PRO A   1      39.085  -6.405   2.490  1.00 39.99           O  
ANISOU    4  O   PRO A   1     4079   5306   5806    621    585   1094       O  
ATOM      5  CB  PRO A   1      38.464  -9.563   2.484  1.00 39.10           C  
ANISOU    5  CB  PRO A   1     3835   5381   5637    621    584   1112       C  
ATOM      6  CG  PRO A   1      37.952  -9.709   3.932  1.00 38.99           C  
ANISOU    6  CG  PRO A   1     3805   5393   5614    577    539   1017       C  
ATOM      7  CD  PRO A   1      39.184  -9.573   4.780  1.00 39.22           C  
ANISOU    7  CD  PRO A   1     3821   5413   5665    524    550   1076       C  
ATOM      8  N   GLN A   2      39.856  -7.334   0.599  1.00 39.67           N  
ANISOU    8  N   GLN A   2     4099   5273   5700    752    814   1055       N  
ATOM      9  CA  GLN A   2      39.467  -6.280  -0.285  1.00 40.51           C  
ANISOU    9  CA  GLN A   2     4374   5282   5733    733    953   1002       C  
ATOM     10  C   GLN A   2      38.344  -6.893  -1.127  1.00 38.70           C  
ANISOU   10  C   GLN A   2     4409   4937   5358    807    955    830       C  
ATOM     11  O   GLN A   2      38.507  -7.956  -1.687  1.00 39.75           O  
ANISOU   11  O   GLN A   2     4613   5008   5481    798    890    749       O  
ATOM     12  CB  GLN A   2      40.650  -5.851  -1.157  1.00 40.89           C  
ANISOU   12  CB  GLN A   2     4393   5366   5777    717   1007    968       C  
ATOM     13  CG  GLN A   2      40.282  -4.704  -2.117  1.00 43.53           C  
ANISOU   13  CG  GLN A   2     4689   5739   6109    645    959   1107       C  
ATOM     14  CD  GLN A   2      41.495  -3.994  -2.745  1.00 46.06           C  
ANISOU   14  CD  GLN A   2     4928   6051   6519    559   1119   1124       C  
ATOM     15  OE1 GLN A   2      42.286  -4.614  -3.465  1.00 51.39           O  
ANISOU   15  OE1 GLN A   2     5654   6723   7147    632   1314    928       O  
ATOM     16  NE2 GLN A   2      41.629  -2.691  -2.478  1.00 48.68           N  
ANISOU   16  NE2 GLN A   2     5285   6314   6895    488    969   1134       N  
ATOM     17  N   ILE A   3      37.192  -6.242  -1.176  1.00 36.16           N  
ANISOU   17  N   ILE A   3     4424   4487   4825    815    840    705       N  
ATOM     18  CA  ILE A   3      36.011  -6.778  -1.839  1.00 33.30           C  
ANISOU   18  CA  ILE A   3     4436   3998   4216    769    826    558       C  
ATOM     19  C   ILE A   3      35.646  -5.826  -3.008  1.00 33.82           C  
ANISOU   19  C   ILE A   3     4762   3972   4113    839    839    489       C  
ATOM     20  O   ILE A   3      35.329  -4.643  -2.772  1.00 32.94           O  
ANISOU   20  O   ILE A   3     4715   3815   3985    780    743    442       O  
ATOM     21  CB  ILE A   3      34.875  -6.940  -0.784  1.00 32.47           C  
ANISOU   21  CB  ILE A   3     4287   3881   4169    724    739    532       C  
ATOM     22  CG1 ILE A   3      35.297  -8.002   0.254  1.00 31.47           C  
ANISOU   22  CG1 ILE A   3     4114   3923   3917    541    640    431       C  
ATOM     23  CG2 ILE A   3      33.538  -7.332  -1.403  1.00 30.76           C  
ANISOU   23  CG2 ILE A   3     4219   3671   3797    767    609    427       C  
ATOM     24  CD1 ILE A   3      34.326  -8.216   1.366  1.00 30.65           C  
ANISOU   24  CD1 ILE A   3     3796   3886   3964    466    532    353       C  
ATOM     25  N   THR A   4      35.744  -6.331  -4.252  1.00 34.00           N  
ANISOU   25  N   THR A   4     5067   3868   3981    886    967    451       N  
ATOM     26  CA  THR A   4      35.208  -5.619  -5.443  1.00 34.77           C  
ANISOU   26  CA  THR A   4     5462   3888   3861    879   1020    327       C  
ATOM     27  C   THR A   4      33.678  -5.753  -5.511  1.00 33.48           C  
ANISOU   27  C   THR A   4     5523   3618   3578    819    904    245       C  
ATOM     28  O   THR A   4      33.073  -6.529  -4.760  1.00 33.23           O  
ANISOU   28  O   THR A   4     5480   3540   3602    717    878    249       O  
ATOM     29  CB  THR A   4      35.818  -6.138  -6.750  1.00 35.46           C  
ANISOU   29  CB  THR A   4     5534   3976   3963    887   1025    351       C  
ATOM     30  OG1 THR A   4      35.595  -7.552  -6.829  1.00 36.50           O  
ANISOU   30  OG1 THR A   4     5813   3917   4137    982    922    315       O  
ATOM     31  CG2 THR A   4      37.343  -5.939  -6.758  1.00 37.47           C  
ANISOU   31  CG2 THR A   4     5674   4285   4275    899   1131    338       C  
ATOM     32  N   LEU A   5      33.053  -4.998  -6.404  1.00 31.96           N  
ANISOU   32  N   LEU A   5     5640   3313   3190    796    782    128       N  
ATOM     33  CA  LEU A   5      31.607  -4.883  -6.362  1.00 30.90           C  
ANISOU   33  CA  LEU A   5     5719   3101   2918    707    743     87       C  
ATOM     34  C   LEU A   5      30.917  -5.386  -7.639  1.00 32.29           C  
ANISOU   34  C   LEU A   5     6156   3130   2982    724    689     50       C  
ATOM     35  O   LEU A   5      29.762  -5.045  -7.891  1.00 31.02           O  
ANISOU   35  O   LEU A   5     6033   2978   2775    773    695    -31       O  
ATOM     36  CB  LEU A   5      31.199  -3.441  -5.976  1.00 29.46           C  
ANISOU   36  CB  LEU A   5     5379   3036   2775    618    709    113       C  
ATOM     37  CG  LEU A   5      31.661  -3.012  -4.574  1.00 27.08           C  
ANISOU   37  CG  LEU A   5     4773   2742   2773    471    576     88       C  
ATOM     38  CD1 LEU A   5      31.665  -1.497  -4.387  1.00 24.63           C  
ANISOU   38  CD1 LEU A   5     4248   2502   2605    265    485    212       C  
ATOM     39  CD2 LEU A   5      30.801  -3.694  -3.485  1.00 22.44           C  
ANISOU   39  CD2 LEU A   5     4097   2325   2104    337    376     15       C  
ATOM     40  N   TRP A   6      31.621  -6.231  -8.412  1.00 33.90           N  
ANISOU   40  N   TRP A   6     6678   3165   3036    816    701    -33       N  
ATOM     41  CA  TRP A   6      31.036  -6.894  -9.591  1.00 36.21           C  
ANISOU   41  CA  TRP A   6     7256   3330   3171    851    675    -59       C  
ATOM     42  C   TRP A   6      29.845  -7.767  -9.202  1.00 35.43           C  
ANISOU   42  C   TRP A   6     7199   3172   3090    820    483   -126       C  
ATOM     43  O   TRP A   6      28.861  -7.870  -9.944  1.00 36.00           O  
ANISOU   43  O   TRP A   6     7341   3268   3069    803    459    -88       O  
ATOM     44  CB  TRP A   6      32.104  -7.653 -10.390  1.00 39.52           C  
ANISOU   44  CB  TRP A   6     7775   3693   3545    968    849   -115       C  
ATOM     45  CG  TRP A   6      33.187  -6.719 -10.785  1.00 41.69           C  
ANISOU   45  CG  TRP A   6     8098   3962   3780   1024   1142    -88       C  
ATOM     46  CD1 TRP A   6      34.356  -6.501 -10.130  1.00 43.48           C  
ANISOU   46  CD1 TRP A   6     8254   4257   4007   1017   1214    -37       C  
ATOM     47  CD2 TRP A   6      33.173  -5.821 -11.893  1.00 43.36           C  
ANISOU   47  CD2 TRP A   6     8452   4121   3901   1103   1305    -97       C  
ATOM     48  NE1 TRP A   6      35.087  -5.533 -10.773  1.00 44.51           N  
ANISOU   48  NE1 TRP A   6     8314   4427   4168   1086   1299      7       N  
ATOM     49  CE2 TRP A   6      34.380  -5.091 -11.856  1.00 43.89           C  
ANISOU   49  CE2 TRP A   6     8388   4373   3914   1094   1399    -54       C  
ATOM     50  CE3 TRP A   6      32.262  -5.559 -12.923  1.00 44.84           C  
ANISOU   50  CE3 TRP A   6     8700   4377   3960   1031   1187      0       C  
ATOM     51  CZ2 TRP A   6      34.700  -4.117 -12.796  1.00 44.86           C  
ANISOU   51  CZ2 TRP A   6     8505   4319   4219   1025   1316     82       C  
ATOM     52  CZ3 TRP A   6      32.585  -4.599 -13.868  1.00 45.12           C  
ANISOU   52  CZ3 TRP A   6     8715   4376   4052    977   1183     43       C  
ATOM     53  CH2 TRP A   6      33.800  -3.896 -13.803  1.00 45.00           C  
ANISOU   53  CH2 TRP A   6     8656   4342   4097    989   1246     79       C  
ATOM     54  N  ALYS A   7      29.921  -8.399  -8.038  0.50 34.24           N  
ANISOU   54  N  ALYS A   7     6946   3020   3043    743    346   -104       N  
ATOM     55  N  BLYS A   7      29.931  -8.335  -8.001  0.50 34.40           N  
ANISOU   55  N  BLYS A   7     6968   3036   3064    760    369    -97       N  
ATOM     56  CA ALYS A   7      28.737  -9.018  -7.468  0.50 33.05           C  
ANISOU   56  CA ALYS A   7     6641   2926   2988    685    168   -148       C  
ATOM     57  CA BLYS A   7      28.892  -9.164  -7.413  0.50 33.50           C  
ANISOU   57  CA BLYS A   7     6693   2981   3051    699    209   -143       C  
ATOM     58  C  ALYS A   7      28.395  -8.407  -6.134  0.50 31.39           C  
ANISOU   58  C  ALYS A   7     6237   2780   2909    648    113   -115       C  
ATOM     59  C  BLYS A   7      28.458  -8.516  -6.090  0.50 31.56           C  
ANISOU   59  C  BLYS A   7     6251   2804   2936    664    142   -112       C  
ATOM     60  O  ALYS A   7      29.145  -7.587  -5.590  0.50 30.92           O  
ANISOU   60  O  ALYS A   7     6086   2756   2905    643     86    -91       O  
ATOM     61  O  BLYS A   7      29.215  -7.719  -5.522  0.50 31.06           O  
ANISOU   61  O  BLYS A   7     6106   2764   2930    659    117    -90       O  
ATOM     62  CB ALYS A   7      28.900 -10.534  -7.310  0.50 33.93           C  
ANISOU   62  CB ALYS A   7     6753   2962   3177    576    130   -155       C  
ATOM     63  CB BLYS A   7      29.475 -10.573  -7.186  0.50 34.10           C  
ANISOU   63  CB BLYS A   7     6740   3001   3213    642    216   -115       C  
ATOM     64  CG ALYS A   7      27.684 -11.236  -6.644  0.50 34.78           C  
ANISOU   64  CG ALYS A   7     6754   3246   3215    525     80   -204       C  
ATOM     65  CG BLYS A   7      28.617 -11.745  -7.702  0.50 37.26           C  
ANISOU   65  CG BLYS A   7     7110   3424   3621    554     79   -178       C  
ATOM     66  CD ALYS A   7      26.317 -10.865  -7.274  0.50 35.43           C  
ANISOU   66  CD ALYS A   7     6838   3258   3364    412   -157   -224       C  
ATOM     67  CD BLYS A   7      27.332 -11.288  -8.403  0.50 38.35           C  
ANISOU   67  CD BLYS A   7     7364   3596   3610    437   -160   -119       C  
ATOM     68  CE ALYS A   7      25.133 -11.448  -6.494  0.50 35.21           C  
ANISOU   68  CE ALYS A   7     6792   3194   3391    366   -159   -223       C  
ATOM     69  CE BLYS A   7      26.094 -11.911  -7.713  0.50 38.37           C  
ANISOU   69  CE BLYS A   7     7331   3610   3637    353   -238   -168       C  
ATOM     70  NZ ALYS A   7      25.162 -12.936  -6.415  0.50 37.14           N  
ANISOU   70  NZ ALYS A   7     6969   3248   3894    212   -310   -207       N  
ATOM     71  NZ BLYS A   7      25.021 -10.895  -7.441  0.50 36.76           N  
ANISOU   71  NZ BLYS A   7     6980   3501   3484    304   -285   -223       N  
ATOM     72  N   ARG A   8      27.247  -8.829  -5.617  1.00 30.22           N  
ANISOU   72  N   ARG A   8     5999   2654   2826    631     26   -103       N  
ATOM     73  CA  ARG A   8      26.764  -8.392  -4.307  1.00 27.91           C  
ANISOU   73  CA  ARG A   8     5310   2584   2708    483   -125   -125       C  
ATOM     74  C   ARG A   8      27.803  -8.800  -3.274  1.00 25.19           C  
ANISOU   74  C   ARG A   8     4777   2289   2503    477    -31    -98       C  
ATOM     75  O   ARG A   8      28.287  -9.944  -3.303  1.00 24.03           O  
ANISOU   75  O   ARG A   8     4616   2158   2353    394     28   -116       O  
ATOM     76  CB  ARG A   8      25.418  -9.027  -3.965  1.00 27.54           C  
ANISOU   76  CB  ARG A   8     5230   2551   2681    500   -128   -136       C  
ATOM     77  CG  ARG A   8      24.242  -8.313  -4.581  1.00 29.08           C  
ANISOU   77  CG  ARG A   8     5182   2833   3033    319   -392   -153       C  
ATOM     78  CD  ARG A   8      22.885  -8.959  -4.342  1.00 30.02           C  
ANISOU   78  CD  ARG A   8     5304   3001   3099    218   -397    -76       C  
ATOM     79  NE  ARG A   8      21.879  -8.368  -5.265  1.00 34.26           N  
ANISOU   79  NE  ARG A   8     5726   3363   3926    -79   -868    -10       N  
ATOM     80  CZ  ARG A   8      20.609  -8.803  -5.417  1.00 36.40           C  
ANISOU   80  CZ  ARG A   8     5822   3764   4244    -24   -918    165       C  
ATOM     81  NH1 ARG A   8      20.158  -9.836  -4.703  1.00 39.24           N  
ANISOU   81  NH1 ARG A   8     6101   4007   4802   -109   -802    148       N  
ATOM     82  NH2 ARG A   8      19.785  -8.229  -6.283  1.00 35.31           N  
ANISOU   82  NH2 ARG A   8     5924   3510   3981    -39  -1098    203       N  
ATOM     83  N   PRO A   9      28.209  -7.846  -2.426  1.00 23.15           N  
ANISOU   83  N   PRO A   9     4265   2106   2421    470    -32    -93       N  
ATOM     84  CA  PRO A   9      29.175  -8.136  -1.368  1.00 21.95           C  
ANISOU   84  CA  PRO A   9     3978   1980   2382    474    -27    -46       C  
ATOM     85  C   PRO A   9      28.523  -8.931  -0.198  1.00 21.70           C  
ANISOU   85  C   PRO A   9     3798   2041   2403    442    -13    -35       C  
ATOM     86  O   PRO A   9      28.184  -8.362   0.834  1.00 20.85           O  
ANISOU   86  O   PRO A   9     3735   1804   2381    428     37     78       O  
ATOM     87  CB  PRO A   9      29.664  -6.736  -0.955  1.00 21.70           C  
ANISOU   87  CB  PRO A   9     3794   2037   2412    382     -4    -56       C  
ATOM     88  CG  PRO A   9      28.458  -5.846  -1.178  1.00 20.41           C  
ANISOU   88  CG  PRO A   9     3764   1715   2274    434    -81     28       C  
ATOM     89  CD  PRO A   9      27.809  -6.415  -2.440  1.00 22.42           C  
ANISOU   89  CD  PRO A   9     4155   1948   2414    453    -60    -80       C  
ATOM     90  N   LEU A  10      28.347 -10.241  -0.397  1.00 21.92           N  
ANISOU   90  N   LEU A  10     3796   2027   2505    498    -13     52       N  
ATOM     91  CA  LEU A  10      27.829 -11.152   0.633  1.00 22.68           C  
ANISOU   91  CA  LEU A  10     3767   2218   2629    454     19    -23       C  
ATOM     92  C   LEU A  10      28.953 -11.781   1.412  1.00 22.31           C  
ANISOU   92  C   LEU A  10     3634   2194   2648    511     64     42       C  
ATOM     93  O   LEU A  10      29.941 -12.249   0.833  1.00 22.52           O  
ANISOU   93  O   LEU A  10     3758   2077   2721    635    124     35       O  
ATOM     94  CB  LEU A  10      27.026 -12.302   0.014  1.00 23.24           C  
ANISOU   94  CB  LEU A  10     3903   2249   2678    393    -56    -76       C  
ATOM     95  CG  LEU A  10      25.749 -11.849  -0.680  1.00 25.66           C  
ANISOU   95  CG  LEU A  10     4097   2678   2974    331   -174   -211       C  
ATOM     96  CD1 LEU A  10      25.290 -12.978  -1.547  1.00 28.00           C  
ANISOU   96  CD1 LEU A  10     4493   2771   3373    136   -258   -246       C  
ATOM     97  CD2 LEU A  10      24.646 -11.388   0.292  1.00 25.23           C  
ANISOU   97  CD2 LEU A  10     3933   2655   2998    241   -146   -137       C  
ATOM     98  N   VAL A  11      28.814 -11.803   2.728  1.00 21.75           N  
ANISOU   98  N   VAL A  11     3435   2192   2637    498     92     52       N  
ATOM     99  CA  VAL A  11      29.773 -12.505   3.550  1.00 21.42           C  
ANISOU   99  CA  VAL A  11     3214   2182   2741    496     13    136       C  
ATOM    100  C   VAL A  11      29.070 -13.436   4.538  1.00 21.17           C  
ANISOU  100  C   VAL A  11     3146   2172   2724    491     37    155       C  
ATOM    101  O   VAL A  11      27.863 -13.322   4.739  1.00 19.75           O  
ANISOU  101  O   VAL A  11     2980   1901   2620    578    -98    188       O  
ATOM    102  CB  VAL A  11      30.732 -11.552   4.289  1.00 21.70           C  
ANISOU  102  CB  VAL A  11     3276   2225   2743    446     95    112       C  
ATOM    103  CG1 VAL A  11      31.656 -10.825   3.275  1.00 24.17           C  
ANISOU  103  CG1 VAL A  11     3392   2527   3264    233     45    190       C  
ATOM    104  CG2 VAL A  11      29.969 -10.598   5.123  1.00 21.73           C  
ANISOU  104  CG2 VAL A  11     3125   2314   2815    477    -90    167       C  
ATOM    105  N   THR A  12      29.836 -14.368   5.127  1.00 21.05           N  
ANISOU  105  N   THR A  12     3102   2097   2797    549    -11    210       N  
ATOM    106  CA  THR A  12      29.329 -15.263   6.165  1.00 21.62           C  
ANISOU  106  CA  THR A  12     3122   2168   2925    533      7    200       C  
ATOM    107  C   THR A  12      29.307 -14.537   7.493  1.00 21.16           C  
ANISOU  107  C   THR A  12     2964   2162   2911    466    -31    209       C  
ATOM    108  O   THR A  12      30.295 -13.871   7.867  1.00 22.09           O  
ANISOU  108  O   THR A  12     2946   2271   3177    563    -42    117       O  
ATOM    109  CB  THR A  12      30.244 -16.515   6.272  1.00 22.82           C  
ANISOU  109  CB  THR A  12     3401   2267   3002    483     47    206       C  
ATOM    110  OG1 THR A  12      30.249 -17.185   4.996  1.00 23.69           O  
ANISOU  110  OG1 THR A  12     3494   2250   3255    655    254    127       O  
ATOM    111  CG2 THR A  12      29.624 -17.551   7.201  1.00 24.04           C  
ANISOU  111  CG2 THR A  12     3581   2438   3112    484     -7    222       C  
ATOM    112  N   ILE A  13      28.189 -14.658   8.214  1.00 20.49           N  
ANISOU  112  N   ILE A  13     2820   2092   2871    363   -139    251       N  
ATOM    113  CA  ILE A  13      28.053 -14.155   9.587  1.00 19.27           C  
ANISOU  113  CA  ILE A  13     2707   1991   2623    222   -153    208       C  
ATOM    114  C   ILE A  13      27.617 -15.335  10.469  1.00 20.56           C  
ANISOU  114  C   ILE A  13     2885   2209   2717    186   -159    183       C  
ATOM    115  O   ILE A  13      26.967 -16.306  10.005  1.00 21.37           O  
ANISOU  115  O   ILE A  13     3099   2241   2779    152   -120    161       O  
ATOM    116  CB  ILE A  13      27.052 -12.930   9.675  1.00 19.44           C  
ANISOU  116  CB  ILE A  13     2712   2061   2613    145   -162    193       C  
ATOM    117  CG1 ILE A  13      25.589 -13.409   9.581  1.00 18.62           C  
ANISOU  117  CG1 ILE A  13     2564   1919   2589    156    -48    135       C  
ATOM    118  CG2 ILE A  13      27.395 -11.864   8.589  1.00 18.52           C  
ANISOU  118  CG2 ILE A  13     2584   1821   2631    173   -274    221       C  
ATOM    119  CD1 ILE A  13      24.499 -12.354   9.450  1.00 19.16           C  
ANISOU  119  CD1 ILE A  13     2639   1950   2690    150    -75    224       C  
ATOM    120  N   LYS A  14      27.997 -15.282  11.734  1.00 20.75           N  
ANISOU  120  N   LYS A  14     2997   2221   2666    149   -160    211       N  
ATOM    121  CA  LYS A  14      27.538 -16.251  12.703  1.00 21.21           C  
ANISOU  121  CA  LYS A  14     3098   2239   2720     86   -103    256       C  
ATOM    122  C   LYS A  14      26.886 -15.425  13.789  1.00 21.71           C  
ANISOU  122  C   LYS A  14     3186   2305   2756     29   -112    285       C  
ATOM    123  O   LYS A  14      27.475 -14.440  14.295  1.00 21.18           O  
ANISOU  123  O   LYS A  14     3100   2321   2626    -75    -21    280       O  
ATOM    124  CB  LYS A  14      28.701 -17.050  13.260  1.00 21.65           C  
ANISOU  124  CB  LYS A  14     3186   2352   2686    113   -176    263       C  
ATOM    125  CG  LYS A  14      28.277 -18.025  14.380  1.00 24.98           C  
ANISOU  125  CG  LYS A  14     3585   2614   3288    134   -126    213       C  
ATOM    126  CD  LYS A  14      28.997 -19.341  14.304  1.00 29.94           C  
ANISOU  126  CD  LYS A  14     4053   3273   4047    304   -304    346       C  
ATOM    127  CE  LYS A  14      30.239 -19.323  15.149  1.00 33.05           C  
ANISOU  127  CE  LYS A  14     4370   3868   4318     87   -275    382       C  
ATOM    128  NZ  LYS A  14      31.138 -18.177  14.799  1.00 34.76           N  
ANISOU  128  NZ  LYS A  14     4692   3790   4723    120   -153    590       N  
ATOM    129  N   ILE A  15      25.652 -15.803  14.111  1.00 21.99           N  
ANISOU  129  N   ILE A  15     3222   2296   2837    -59    -60    266       N  
ATOM    130  CA  ILE A  15      24.848 -15.088  15.078  1.00 23.42           C  
ANISOU  130  CA  ILE A  15     3431   2461   3006    -95     26    268       C  
ATOM    131  C   ILE A  15      23.881 -16.089  15.733  1.00 25.35           C  
ANISOU  131  C   ILE A  15     3737   2758   3137   -182     42    238       C  
ATOM    132  O   ILE A  15      23.203 -16.885  15.051  1.00 26.11           O  
ANISOU  132  O   ILE A  15     3778   2875   3267   -244     97    180       O  
ATOM    133  CB  ILE A  15      24.100 -13.872  14.433  1.00 23.46           C  
ANISOU  133  CB  ILE A  15     3394   2560   2959    -76     16    143       C  
ATOM    134  CG1 ILE A  15      23.187 -13.225  15.505  1.00 25.37           C  
ANISOU  134  CG1 ILE A  15     3567   2700   3369     31     49    155       C  
ATOM    135  CG2 ILE A  15      23.345 -14.284  13.131  1.00 22.10           C  
ANISOU  135  CG2 ILE A  15     3158   2365   2872    -78     -4    222       C  
ATOM    136  CD1 ILE A  15      22.774 -11.784  15.264  1.00 23.97           C  
ANISOU  136  CD1 ILE A  15     3463   2456   3188   -103     82    265       C  
ATOM    137  N   GLY A  16      23.862 -16.085  17.062  1.00 26.63           N  
ANISOU  137  N   GLY A  16     3987   2895   3236   -204    116    303       N  
ATOM    138  CA  GLY A  16      23.001 -16.990  17.830  1.00 27.03           C  
ANISOU  138  CA  GLY A  16     4109   2785   3375   -209    150    344       C  
ATOM    139  C   GLY A  16      23.251 -18.464  17.585  1.00 27.33           C  
ANISOU  139  C   GLY A  16     4200   2787   3397   -211    112    311       C  
ATOM    140  O   GLY A  16      22.315 -19.257  17.571  1.00 28.03           O  
ANISOU  140  O   GLY A  16     4271   2970   3408   -298    124    306       O  
ATOM    141  N   GLY A  17      24.505 -18.845  17.397  1.00 27.11           N  
ANISOU  141  N   GLY A  17     4153   2717   3428   -150     50    328       N  
ATOM    142  CA  GLY A  17      24.834 -20.219  17.007  1.00 26.78           C  
ANISOU  142  CA  GLY A  17     4131   2613   3431   -108     15    357       C  
ATOM    143  C   GLY A  17      24.526 -20.592  15.555  1.00 25.94           C  
ANISOU  143  C   GLY A  17     3980   2471   3405    -95    -51    351       C  
ATOM    144  O   GLY A  17      24.757 -21.727  15.157  1.00 26.63           O  
ANISOU  144  O   GLY A  17     4105   2589   3421    -50    -54    350       O  
ATOM    145  N   GLN A  18      24.030 -19.651  14.756  1.00 24.72           N  
ANISOU  145  N   GLN A  18     3834   2273   3286   -125    -21    374       N  
ATOM    146  CA  GLN A  18      23.619 -19.940  13.370  1.00 24.09           C  
ANISOU  146  CA  GLN A  18     3719   2143   3288    -92    -44    313       C  
ATOM    147  C   GLN A  18      24.446 -19.213  12.316  1.00 22.99           C  
ANISOU  147  C   GLN A  18     3565   2084   3085      9    -60    279       C  
ATOM    148  O   GLN A  18      24.867 -18.066  12.514  1.00 21.40           O  
ANISOU  148  O   GLN A  18     3280   2060   2788    -60     41    324       O  
ATOM    149  CB  GLN A  18      22.155 -19.574  13.149  1.00 24.31           C  
ANISOU  149  CB  GLN A  18     3744   2222   3269   -136    -24    288       C  
ATOM    150  CG  GLN A  18      21.192 -20.217  14.124  1.00 27.20           C  
ANISOU  150  CG  GLN A  18     3848   2679   3805   -210      0    257       C  
ATOM    151  CD  GLN A  18      19.851 -19.565  14.022  1.00 29.20           C  
ANISOU  151  CD  GLN A  18     3993   2990   4109   -298     -8    285       C  
ATOM    152  OE1 GLN A  18      19.225 -19.657  12.984  1.00 30.55           O  
ANISOU  152  OE1 GLN A  18     4066   3218   4323   -485   -136    380       O  
ATOM    153  NE2 GLN A  18      19.409 -18.882  15.085  1.00 30.57           N  
ANISOU  153  NE2 GLN A  18     4246   2904   4463   -267     85    278       N  
ATOM    154  N   LEU A  19      24.597 -19.870  11.179  1.00 22.15           N  
ANISOU  154  N   LEU A  19     3464   1874   3077     73   -118    166       N  
ATOM    155  CA  LEU A  19      25.408 -19.390  10.065  1.00 22.81           C  
ANISOU  155  CA  LEU A  19     3628   1943   3096    142   -193    166       C  
ATOM    156  C   LEU A  19      24.500 -18.802   9.028  1.00 22.10           C  
ANISOU  156  C   LEU A  19     3472   1888   3037    135   -171    135       C  
ATOM    157  O   LEU A  19      23.572 -19.472   8.571  1.00 21.02           O  
ANISOU  157  O   LEU A  19     3461   1538   2985     59   -227    236       O  
ATOM    158  CB  LEU A  19      26.246 -20.542   9.435  1.00 23.53           C  
ANISOU  158  CB  LEU A  19     3683   2115   3141    222   -157    132       C  
ATOM    159  CG  LEU A  19      27.352 -21.172  10.312  1.00 25.82           C  
ANISOU  159  CG  LEU A  19     3988   2290   3531    324   -113    242       C  
ATOM    160  CD1 LEU A  19      28.055 -22.262   9.550  1.00 26.32           C  
ANISOU  160  CD1 LEU A  19     4228   2271   3500    462   -105    262       C  
ATOM    161  CD2 LEU A  19      28.373 -20.107  10.836  1.00 26.89           C  
ANISOU  161  CD2 LEU A  19     3819   2762   3635    494   -265    145       C  
ATOM    162  N   LYS A  20      24.775 -17.559   8.647  1.00 20.92           N  
ANISOU  162  N   LYS A  20     3282   1699   2967     57   -163     78       N  
ATOM    163  CA  LYS A  20      24.006 -16.894   7.615  1.00 21.60           C  
ANISOU  163  CA  LYS A  20     3273   1962   2970     26   -221     65       C  
ATOM    164  C   LYS A  20      24.884 -16.155   6.613  1.00 20.90           C  
ANISOU  164  C   LYS A  20     3259   1929   2751     87   -263     50       C  
ATOM    165  O   LYS A  20      26.089 -15.959   6.827  1.00 20.41           O  
ANISOU  165  O   LYS A  20     3259   1969   2527     87   -194    101       O  
ATOM    166  CB  LYS A  20      22.994 -15.921   8.253  1.00 21.95           C  
ANISOU  166  CB  LYS A  20     3292   1991   3056      4   -217     75       C  
ATOM    167  CG  LYS A  20      21.839 -16.667   8.896  1.00 24.05           C  
ANISOU  167  CG  LYS A  20     3461   2348   3328    -30    -73    -18       C  
ATOM    168  CD  LYS A  20      20.869 -15.825   9.695  1.00 23.80           C  
ANISOU  168  CD  LYS A  20     3350   2313   3378    -10   -142    161       C  
ATOM    169  CE  LYS A  20      19.814 -16.743  10.393  1.00 26.43           C  
ANISOU  169  CE  LYS A  20     3553   2638   3851   -314   -167    137       C  
ATOM    170  NZ  LYS A  20      19.401 -17.875   9.493  1.00 31.00           N  
ANISOU  170  NZ  LYS A  20     4068   3235   4472   -288   -222    127       N  
ATOM    171  N   GLU A  21      24.276 -15.738   5.512  1.00 20.58           N  
ANISOU  171  N   GLU A  21     3223   1866   2728    119   -301    -11       N  
ATOM    172  CA  GLU A  21      24.952 -14.850   4.570  1.00 20.32           C  
ANISOU  172  CA  GLU A  21     3271   1777   2671    208   -330    -27       C  
ATOM    173  C   GLU A  21      24.296 -13.500   4.665  1.00 19.25           C  
ANISOU  173  C   GLU A  21     3086   1666   2563    171   -312    -47       C  
ATOM    174  O   GLU A  21      23.067 -13.416   4.764  1.00 19.38           O  
ANISOU  174  O   GLU A  21     3170   1489   2703    248   -276    -19       O  
ATOM    175  CB  GLU A  21      24.858 -15.362   3.143  1.00 21.27           C  
ANISOU  175  CB  GLU A  21     3448   1858   2776    204   -296    -82       C  
ATOM    176  CG  GLU A  21      25.589 -16.672   2.907  1.00 26.07           C  
ANISOU  176  CG  GLU A  21     4233   2590   3079    355   -239    -40       C  
ATOM    177  CD  GLU A  21      26.118 -16.731   1.488  1.00 32.73           C  
ANISOU  177  CD  GLU A  21     5103   3756   3576    563   -152    -58       C  
ATOM    178  OE1 GLU A  21      25.367 -16.322   0.556  1.00 35.63           O  
ANISOU  178  OE1 GLU A  21     5588   3961   3988    436   -390      8       O  
ATOM    179  OE2 GLU A  21      27.302 -17.125   1.308  1.00 36.16           O  
ANISOU  179  OE2 GLU A  21     5308   4108   4323    755   -113   -119       O  
ATOM    180  N   ALA A  22      25.117 -12.457   4.628  1.00 17.82           N  
ANISOU  180  N   ALA A  22     2759   1583   2426    204   -332    -40       N  
ATOM    181  CA  ALA A  22      24.643 -11.088   4.791  1.00 16.79           C  
ANISOU  181  CA  ALA A  22     2620   1521   2236    151   -301     -9       C  
ATOM    182  C   ALA A  22      25.374 -10.133   3.843  1.00 16.81           C  
ANISOU  182  C   ALA A  22     2568   1578   2238    134   -263    -71       C  
ATOM    183  O   ALA A  22      26.529 -10.334   3.505  1.00 16.91           O  
ANISOU  183  O   ALA A  22     2668   1613   2142    123   -221    -63       O  
ATOM    184  CB  ALA A  22      24.753 -10.637   6.218  1.00 14.87           C  
ANISOU  184  CB  ALA A  22     2268   1248   2131    166   -295     36       C  
ATOM    185  N   LEU A  23      24.668  -9.105   3.420  1.00 16.54           N  
ANISOU  185  N   LEU A  23     2565   1619   2099    129   -315     22       N  
ATOM    186  CA  LEU A  23      25.202  -8.096   2.535  1.00 17.65           C  
ANISOU  186  CA  LEU A  23     2695   1750   2258    164   -292     12       C  
ATOM    187  C   LEU A  23      25.911  -6.987   3.337  1.00 16.89           C  
ANISOU  187  C   LEU A  23     2586   1666   2163    172   -207     43       C  
ATOM    188  O   LEU A  23      25.367  -6.467   4.340  1.00 18.00           O  
ANISOU  188  O   LEU A  23     2831   1705   2303     26   -170    133       O  
ATOM    189  CB  LEU A  23      24.014  -7.543   1.745  1.00 17.86           C  
ANISOU  189  CB  LEU A  23     2715   1797   2273    148   -288     34       C  
ATOM    190  CG  LEU A  23      24.091  -6.491   0.633  1.00 19.75           C  
ANISOU  190  CG  LEU A  23     2938   2163   2403    264   -356     15       C  
ATOM    191  CD1 LEU A  23      24.709  -7.096  -0.570  1.00 20.03           C  
ANISOU  191  CD1 LEU A  23     3181   2287   2143    259   -152   -111       C  
ATOM    192  CD2 LEU A  23      22.647  -6.126   0.330  1.00 20.44           C  
ANISOU  192  CD2 LEU A  23     2917   2062   2785    223   -352     94       C  
ATOM    193  N   LEU A  24      27.133  -6.642   2.934  1.00 16.25           N  
ANISOU  193  N   LEU A  24     2452   1640   2081    252   -188     47       N  
ATOM    194  CA  LEU A  24      27.832  -5.508   3.539  1.00 16.12           C  
ANISOU  194  CA  LEU A  24     2361   1693   2070    229   -162     27       C  
ATOM    195  C   LEU A  24      27.287  -4.225   2.887  1.00 16.35           C  
ANISOU  195  C   LEU A  24     2490   1678   2043    159   -105      1       C  
ATOM    196  O   LEU A  24      27.454  -3.994   1.689  1.00 17.41           O  
ANISOU  196  O   LEU A  24     2807   1664   2144    221   -131     26       O  
ATOM    197  CB  LEU A  24      29.343  -5.638   3.335  1.00 16.76           C  
ANISOU  197  CB  LEU A  24     2456   1813   2096    224   -129     36       C  
ATOM    198  CG  LEU A  24      29.993  -6.886   3.977  1.00 17.28           C  
ANISOU  198  CG  LEU A  24     2357   1894   2314    335    -57    140       C  
ATOM    199  CD1 LEU A  24      31.422  -6.824   3.756  1.00 19.21           C  
ANISOU  199  CD1 LEU A  24     2265   2171   2861    256    -39    194       C  
ATOM    200  CD2 LEU A  24      29.742  -6.972   5.456  1.00 17.19           C  
ANISOU  200  CD2 LEU A  24     2348   1888   2293    475   -109     95       C  
ATOM    201  N   ASP A  25      26.604  -3.408   3.653  1.00 15.67           N  
ANISOU  201  N   ASP A  25     2372   1565   2016    150    -96    -21       N  
ATOM    202  CA  ASP A  25      25.769  -2.411   3.010  1.00 16.41           C  
ANISOU  202  CA  ASP A  25     2554   1648   2032     97    -57     56       C  
ATOM    203  C   ASP A  25      26.085  -1.002   3.533  1.00 16.23           C  
ANISOU  203  C   ASP A  25     2647   1572   1948    119    -36     43       C  
ATOM    204  O   ASP A  25      25.657  -0.627   4.627  1.00 15.08           O  
ANISOU  204  O   ASP A  25     2518   1213   1997     90     -3    193       O  
ATOM    205  CB  ASP A  25      24.308  -2.816   3.225  1.00 16.53           C  
ANISOU  205  CB  ASP A  25     2509   1731   2040    179   -121     12       C  
ATOM    206  CG  ASP A  25      23.333  -1.896   2.570  1.00 19.38           C  
ANISOU  206  CG  ASP A  25     2774   2110   2478    102    -74     82       C  
ATOM    207  OD1 ASP A  25      23.719  -0.931   1.882  1.00 19.10           O  
ANISOU  207  OD1 ASP A  25     3026   1689   2539    -40    -14     -6       O  
ATOM    208  OD2 ASP A  25      22.106  -2.076   2.687  1.00 22.59           O  
ANISOU  208  OD2 ASP A  25     2960   2575   3047    157     19     48       O  
ATOM    209  N   THR A  26      26.848  -0.225   2.744  1.00 17.19           N  
ANISOU  209  N   THR A  26     2800   1692   2038     68    -70      6       N  
ATOM    210  CA  THR A  26      27.212   1.134   3.138  1.00 17.68           C  
ANISOU  210  CA  THR A  26     2958   1635   2121     99     31     36       C  
ATOM    211  C   THR A  26      26.031   2.111   3.135  1.00 18.55           C  
ANISOU  211  C   THR A  26     3045   1809   2193    121     89      1       C  
ATOM    212  O   THR A  26      26.145   3.199   3.725  1.00 19.43           O  
ANISOU  212  O   THR A  26     3193   1775   2411    218    103    -41       O  
ATOM    213  CB  THR A  26      28.363   1.737   2.263  1.00 17.40           C  
ANISOU  213  CB  THR A  26     2948   1629   2032    112     74     37       C  
ATOM    214  OG1 THR A  26      27.998   1.641   0.881  1.00 16.91           O  
ANISOU  214  OG1 THR A  26     2993   1389   2040    127     49     29       O  
ATOM    215  CG2 THR A  26      29.675   0.985   2.385  1.00 17.00           C  
ANISOU  215  CG2 THR A  26     2753   1718   1986    -44     -7     30       C  
ATOM    216  N   GLY A  27      24.941   1.756   2.451  1.00 18.76           N  
ANISOU  216  N   GLY A  27     3151   1782   2192    118    127     -3       N  
ATOM    217  CA  GLY A  27      23.701   2.566   2.423  1.00 19.40           C  
ANISOU  217  CA  GLY A  27     3218   1832   2321    224    105     85       C  
ATOM    218  C   GLY A  27      22.734   2.301   3.571  1.00 20.09           C  
ANISOU  218  C   GLY A  27     3275   1930   2426    317    124    -44       C  
ATOM    219  O   GLY A  27      21.647   2.892   3.614  1.00 20.83           O  
ANISOU  219  O   GLY A  27     3390   1972   2552    308     49     -7       O  
ATOM    220  N   ALA A  28      23.095   1.402   4.485  1.00 19.21           N  
ANISOU  220  N   ALA A  28     3270   1749   2279    281    147    -41       N  
ATOM    221  CA  ALA A  28      22.255   1.111   5.625  1.00 19.90           C  
ANISOU  221  CA  ALA A  28     3328   1815   2417    256    200    -83       C  
ATOM    222  C   ALA A  28      22.809   1.744   6.910  1.00 20.70           C  
ANISOU  222  C   ALA A  28     3487   1858   2519    266    246    -88       C  
ATOM    223  O   ALA A  28      23.941   1.465   7.292  1.00 19.33           O  
ANISOU  223  O   ALA A  28     3273   1611   2461    281    245   -193       O  
ATOM    224  CB  ALA A  28      22.085  -0.449   5.809  1.00 18.90           C  
ANISOU  224  CB  ALA A  28     3117   1836   2225    263    142    -81       C  
ATOM    225  N   ASP A  29      22.005   2.572   7.588  1.00 22.15           N  
ANISOU  225  N   ASP A  29     3785   1944   2686    319    378    -50       N  
ATOM    226  CA  ASP A  29      22.374   3.103   8.909  1.00 23.31           C  
ANISOU  226  CA  ASP A  29     4052   2059   2745    302    415     -1       C  
ATOM    227  C   ASP A  29      22.503   1.945   9.902  1.00 23.86           C  
ANISOU  227  C   ASP A  29     4031   2175   2859    334    407    -15       C  
ATOM    228  O   ASP A  29      23.437   1.931  10.690  1.00 25.22           O  
ANISOU  228  O   ASP A  29     4265   2412   2903    274    380     -2       O  
ATOM    229  CB  ASP A  29      21.306   4.073   9.469  1.00 23.45           C  
ANISOU  229  CB  ASP A  29     4150   2029   2730    288    418    -16       C  
ATOM    230  CG  ASP A  29      21.065   5.269   8.574  1.00 25.73           C  
ANISOU  230  CG  ASP A  29     4477   2163   3132    339    462    -61       C  
ATOM    231  OD1 ASP A  29      21.942   5.635   7.752  1.00 26.20           O  
ANISOU  231  OD1 ASP A  29     4877   2001   3074    282    409    175       O  
ATOM    232  OD2 ASP A  29      20.002   5.897   8.612  1.00 26.78           O  
ANISOU  232  OD2 ASP A  29     4980   1828   3366    528    503    -86       O  
ATOM    233  N   ASP A  30      21.574   0.989   9.838  1.00 23.10           N  
ANISOU  233  N   ASP A  30     3841   2070   2865    309    464    -14       N  
ATOM    234  CA  ASP A  30      21.433  -0.079  10.815  1.00 23.08           C  
ANISOU  234  CA  ASP A  30     3770   2100   2897    292    480     11       C  
ATOM    235  C   ASP A  30      21.635  -1.461  10.213  1.00 21.80           C  
ANISOU  235  C   ASP A  30     3499   2035   2748    256    456     36       C  
ATOM    236  O   ASP A  30      21.672  -1.647   8.982  1.00 20.99           O  
ANISOU  236  O   ASP A  30     3549   1810   2616    206    368    175       O  
ATOM    237  CB  ASP A  30      20.027  -0.036  11.431  1.00 24.05           C  
ANISOU  237  CB  ASP A  30     3916   2187   3031    292    564     -3       C  
ATOM    238  CG  ASP A  30      19.715   1.300  12.116  1.00 28.01           C  
ANISOU  238  CG  ASP A  30     4452   2653   3535    356    579    -48       C  
ATOM    239  OD1 ASP A  30      20.510   1.762  12.955  1.00 30.59           O  
ANISOU  239  OD1 ASP A  30     5059   3004   3556    363    714   -270       O  
ATOM    240  OD2 ASP A  30      18.685   1.956  11.874  1.00 32.31           O  
ANISOU  240  OD2 ASP A  30     4899   3035   4342    527    668   -106       O  
ATOM    241  N   THR A  31      21.754  -2.444  11.106  1.00 20.78           N  
ANISOU  241  N   THR A  31     3220   2023   2651    201    445     29       N  
ATOM    242  CA  THR A  31      21.860  -3.834  10.734  1.00 20.16           C  
ANISOU  242  CA  THR A  31     3022   1940   2694    246    330     61       C  
ATOM    243  C   THR A  31      20.528  -4.530  10.846  1.00 20.78           C  
ANISOU  243  C   THR A  31     2960   2053   2880    241    293    131       C  
ATOM    244  O   THR A  31      19.877  -4.452  11.882  1.00 21.28           O  
ANISOU  244  O   THR A  31     3182   2049   2855    207    281    172       O  
ATOM    245  CB  THR A  31      22.891  -4.465  11.632  1.00 20.35           C  
ANISOU  245  CB  THR A  31     3022   2063   2646    181    283    -53       C  
ATOM    246  OG1 THR A  31      24.175  -4.010  11.165  1.00 18.15           O  
ANISOU  246  OG1 THR A  31     2920   1544   2429     75    233   -122       O  
ATOM    247  CG2 THR A  31      22.885  -6.039  11.497  1.00 18.62           C  
ANISOU  247  CG2 THR A  31     2847   1785   2440    133     64    159       C  
ATOM    248  N   VAL A  32      20.082  -5.141   9.759  1.00 20.81           N  
ANISOU  248  N   VAL A  32     2853   2000   3050    278    227    148       N  
ATOM    249  CA  VAL A  32      18.731  -5.708   9.695  1.00 22.33           C  
ANISOU  249  CA  VAL A  32     2707   2327   3449    225    148    210       C  
ATOM    250  C   VAL A  32      18.802  -7.143   9.175  1.00 22.38           C  
ANISOU  250  C   VAL A  32     2615   2370   3514    167     85    204       C  
ATOM    251  O   VAL A  32      19.296  -7.404   8.063  1.00 22.96           O  
ANISOU  251  O   VAL A  32     2653   2374   3697    127    -17    158       O  
ATOM    252  CB  VAL A  32      17.723  -4.920   8.771  1.00 22.95           C  
ANISOU  252  CB  VAL A  32     2772   2376   3571    236    146    152       C  
ATOM    253  CG1 VAL A  32      16.284  -5.312   9.126  1.00 23.23           C  
ANISOU  253  CG1 VAL A  32     2604   2608   3611    266    165    170       C  
ATOM    254  CG2 VAL A  32      17.887  -3.404   8.844  1.00 23.56           C  
ANISOU  254  CG2 VAL A  32     2731   2582   3636    166    161    237       C  
ATOM    255  N   LEU A  33      18.309  -8.052   9.999  1.00 22.55           N  
ANISOU  255  N   LEU A  33     2477   2465   3624     78    -14    285       N  
ATOM    256  CA  LEU A  33      18.351  -9.480   9.750  1.00 23.48           C  
ANISOU  256  CA  LEU A  33     2563   2569   3785     52    -33    301       C  
ATOM    257  C   LEU A  33      16.953 -10.037   9.558  1.00 25.39           C  
ANISOU  257  C   LEU A  33     2756   2759   4129    -27    -59    434       C  
ATOM    258  O   LEU A  33      15.984  -9.533  10.148  1.00 24.18           O  
ANISOU  258  O   LEU A  33     2534   2726   3925     41     -4    447       O  
ATOM    259  CB  LEU A  33      19.046 -10.214  10.916  1.00 22.92           C  
ANISOU  259  CB  LEU A  33     2595   2437   3674    -18     66    304       C  
ATOM    260  CG  LEU A  33      20.518  -9.890  11.184  1.00 23.16           C  
ANISOU  260  CG  LEU A  33     2717   2729   3353    124    -22    312       C  
ATOM    261  CD1 LEU A  33      21.091 -10.910  12.156  1.00 24.68           C  
ANISOU  261  CD1 LEU A  33     3244   2613   3520    115     34    316       C  
ATOM    262  CD2 LEU A  33      21.363  -9.888   9.901  1.00 21.88           C  
ANISOU  262  CD2 LEU A  33     2643   2499   3171     47     55    232       C  
ATOM    263  N   GLU A  34      16.856 -11.067   8.718  1.00 27.60           N  
ANISOU  263  N   GLU A  34     3032   2896   4555   -142   -216    438       N  
ATOM    264  CA  GLU A  34      15.602 -11.754   8.527  1.00 31.95           C  
ANISOU  264  CA  GLU A  34     3464   3388   5288   -248   -413    419       C  
ATOM    265  C   GLU A  34      15.118 -12.300   9.873  1.00 35.29           C  
ANISOU  265  C   GLU A  34     3850   3715   5841   -317   -422    472       C  
ATOM    266  O   GLU A  34      15.894 -12.355  10.849  1.00 34.11           O  
ANISOU  266  O   GLU A  34     3583   3581   5796   -290   -319    436       O  
ATOM    267  CB  GLU A  34      15.774 -12.909   7.549  1.00 31.15           C  
ANISOU  267  CB  GLU A  34     3405   3329   5098   -254   -346    392       C  
ATOM    268  CG  GLU A  34      15.977 -12.527   6.091  1.00 32.05           C  
ANISOU  268  CG  GLU A  34     3613   3456   5105   -225   -543    305       C  
ATOM    269  CD  GLU A  34      16.191 -13.756   5.190  1.00 33.80           C  
ANISOU  269  CD  GLU A  34     3926   3667   5248   -146   -629    309       C  
ATOM    270  OE1 GLU A  34      16.912 -14.691   5.605  1.00 37.07           O  
ANISOU  270  OE1 GLU A  34     4412   3974   5698     45   -509    174       O  
ATOM    271  OE2 GLU A  34      15.635 -13.821   4.069  1.00 38.18           O  
ANISOU  271  OE2 GLU A  34     4862   4207   5437   -278   -884     76       O  
ATOM    272  N   GLU A  35      13.838 -12.682   9.931  1.00 40.27           N  
ANISOU  272  N   GLU A  35     4327   4179   6795   -475   -599    519       N  
ATOM    273  CA  GLU A  35      13.274 -13.313  11.132  1.00 45.61           C  
ANISOU  273  CA  GLU A  35     5057   4759   7514   -551   -653    597       C  
ATOM    274  C   GLU A  35      14.145 -14.458  11.660  1.00 47.31           C  
ANISOU  274  C   GLU A  35     5215   4779   7982   -660   -768    720       C  
ATOM    275  O   GLU A  35      14.528 -15.373  10.932  1.00 47.90           O  
ANISOU  275  O   GLU A  35     5289   4728   8182   -670   -836    714       O  
ATOM    276  CB  GLU A  35      11.843 -13.829  10.895  1.00 45.73           C  
ANISOU  276  CB  GLU A  35     5106   4938   7329   -442   -541    458       C  
ATOM    277  CG  GLU A  35      10.896 -13.483  12.033  1.00 50.82           C  
ANISOU  277  CG  GLU A  35     5979   5978   7351   -296   -326    277       C  
ATOM    278  CD  GLU A  35      10.684 -11.976  12.161  1.00 54.25           C  
ANISOU  278  CD  GLU A  35     6793   6470   7350    -99   -192     82       C  
ATOM    279  OE1 GLU A  35      10.134 -11.361  11.200  1.00 57.18           O  
ANISOU  279  OE1 GLU A  35     7094   6992   7639   -222   -100    113       O  
ATOM    280  OE2 GLU A  35      11.072 -11.405  13.224  1.00 58.27           O  
ANISOU  280  OE2 GLU A  35     7152   7249   7738   -136    -60     57       O  
ATOM    281  N   MET A  36      14.461 -14.360  12.937  1.00 48.94           N  
ANISOU  281  N   MET A  36     5407   4976   8211   -744   -765    846       N  
ATOM    282  CA  MET A  36      15.137 -15.416  13.658  1.00 50.31           C  
ANISOU  282  CA  MET A  36     5624   5256   8236   -750   -592    932       C  
ATOM    283  C   MET A  36      14.841 -15.177  15.120  1.00 51.92           C  
ANISOU  283  C   MET A  36     5793   5417   8515   -817   -521   1183       C  
ATOM    284  O   MET A  36      14.395 -14.081  15.500  1.00 52.37           O  
ANISOU  284  O   MET A  36     5844   5406   8646   -862   -478   1206       O  
ATOM    285  CB  MET A  36      16.645 -15.387  13.406  1.00 50.05           C  
ANISOU  285  CB  MET A  36     5657   5369   7987   -618   -506    773       C  
ATOM    286  CG  MET A  36      17.354 -14.179  14.005  1.00 49.30           C  
ANISOU  286  CG  MET A  36     5705   5589   7437   -428   -351    494       C  
ATOM    287  SD  MET A  36      19.098 -14.235  13.604  1.00 47.99           S  
ANISOU  287  SD  MET A  36     5512   5358   7365   -690   -362    614       S  
ATOM    288  CE  MET A  36      18.972 -13.916  11.871  1.00 51.43           C  
ANISOU  288  CE  MET A  36     6130   6171   7239   -305   -100    176       C  
ATOM    289  N   SER A  37      15.066 -16.208  15.932  1.00 53.40           N  
ANISOU  289  N   SER A  37     5977   5671   8639   -826   -394   1409       N  
ATOM    290  CA  SER A  37      14.901 -16.080  17.370  1.00 54.56           C  
ANISOU  290  CA  SER A  37     6197   5959   8574   -757   -219   1532       C  
ATOM    291  C   SER A  37      16.204 -15.620  18.012  1.00 54.04           C  
ANISOU  291  C   SER A  37     6176   6002   8353   -703    -81   1670       C  
ATOM    292  O   SER A  37      17.269 -16.241  17.856  1.00 54.04           O  
ANISOU  292  O   SER A  37     6206   5954   8372   -716    -66   1743       O  
ATOM    293  CB  SER A  37      14.425 -17.397  17.997  1.00 54.77           C  
ANISOU  293  CB  SER A  37     6347   6100   8363   -674   -149   1291       C  
ATOM    294  OG  SER A  37      14.313 -17.251  19.409  1.00 57.16           O  
ANISOU  294  OG  SER A  37     6784   6621   8313   -488   -133    844       O  
ATOM    295  N   LEU A  38      16.118 -14.495  18.703  1.00 53.61           N  
ANISOU  295  N   LEU A  38     6236   6210   7921   -531    111   1687       N  
ATOM    296  CA  LEU A  38      17.219 -14.048  19.507  1.00 53.19           C  
ANISOU  296  CA  LEU A  38     6251   6517   7440   -334    302   1642       C  
ATOM    297  C   LEU A  38      16.764 -14.024  20.956  1.00 55.05           C  
ANISOU  297  C   LEU A  38     6530   6954   7431   -211    504   1808       C  
ATOM    298  O   LEU A  38      15.669 -13.522  21.265  1.00 55.61           O  
ANISOU  298  O   LEU A  38     6581   7044   7503   -262    551   1851       O  
ATOM    299  CB  LEU A  38      17.729 -12.672  19.073  1.00 51.62           C  
ANISOU  299  CB  LEU A  38     6179   6325   7110   -239    244   1329       C  
ATOM    300  CG  LEU A  38      18.604 -12.595  17.822  1.00 49.12           C  
ANISOU  300  CG  LEU A  38     5918   6055   6690   -119    109    760       C  
ATOM    301  CD1 LEU A  38      19.038 -11.175  17.598  1.00 45.16           C  
ANISOU  301  CD1 LEU A  38     5526   5756   5873    -10     24    367       C  
ATOM    302  CD2 LEU A  38      19.823 -13.510  17.932  1.00 47.33           C  
ANISOU  302  CD2 LEU A  38     5915   6019   6047   -132     58    377       C  
ATOM    303  N   PRO A  39      17.588 -14.578  21.841  1.00 56.56           N  
ANISOU  303  N   PRO A  39     6845   7387   7254    -29    629   1851       N  
ATOM    304  CA  PRO A  39      17.357 -14.428  23.276  1.00 58.43           C  
ANISOU  304  CA  PRO A  39     7134   7837   7229    130    781   1919       C  
ATOM    305  C   PRO A  39      17.394 -12.945  23.672  1.00 59.82           C  
ANISOU  305  C   PRO A  39     7420   8183   7124    328    986   2052       C  
ATOM    306  O   PRO A  39      18.177 -12.174  23.106  1.00 59.66           O  
ANISOU  306  O   PRO A  39     7441   8173   7052    294    961   2077       O  
ATOM    307  CB  PRO A  39      18.525 -15.211  23.912  1.00 58.12           C  
ANISOU  307  CB  PRO A  39     7130   7735   7215    122    615   1596       C  
ATOM    308  CG  PRO A  39      19.545 -15.386  22.819  1.00 57.07           C  
ANISOU  308  CG  PRO A  39     6976   7480   7226     78    499   1345       C  
ATOM    309  CD  PRO A  39      18.784 -15.395  21.543  1.00 56.55           C  
ANISOU  309  CD  PRO A  39     6908   7348   7229    -11    543   1519       C  
ATOM    310  N   GLY A  40      16.527 -12.558  24.606  1.00 62.79           N  
ANISOU  310  N   GLY A  40     7779   8910   7167    593   1167   2172       N  
ATOM    311  CA  GLY A  40      16.579 -11.226  25.216  1.00 65.43           C  
ANISOU  311  CA  GLY A  40     8214   9524   7123    914   1366   2141       C  
ATOM    312  C   GLY A  40      15.320 -10.392  25.062  1.00 67.10           C  
ANISOU  312  C   GLY A  40     8431   9998   7066   1134   1487   2138       C  
ATOM    313  O   GLY A  40      14.395 -10.769  24.332  1.00 67.93           O  
ANISOU  313  O   GLY A  40     8509  10129   7169   1103   1480   2137       O  
ATOM    314  N   ARG A  41      15.296  -9.260  25.771  1.00 67.63           N  
ANISOU  314  N   ARG A  41     8559  10210   6925   1270   1526   2008       N  
ATOM    315  CA  ARG A  41      14.246  -8.256  25.641  1.00 67.38           C  
ANISOU  315  CA  ARG A  41     8596  10252   6751   1388   1544   1800       C  
ATOM    316  C   ARG A  41      14.456  -7.472  24.336  1.00 66.75           C  
ANISOU  316  C   ARG A  41     8507  10205   6650   1442   1555   1692       C  
ATOM    317  O   ARG A  41      15.547  -7.508  23.753  1.00 66.77           O  
ANISOU  317  O   ARG A  41     8575  10201   6592   1431   1525   1606       O  
ATOM    318  CB  ARG A  41      14.278  -7.312  26.846  1.00 67.64           C  
ANISOU  318  CB  ARG A  41     8585  10053   7062   1124   1274   1519       C  
ATOM    319  CG  ARG A  41      15.088  -6.960  27.274  0.00 69.42           C  
ANISOU  319  CG  ARG A  41     9822  13337   3215   5591   3589   3467       C  
ATOM    320  CD  ARG A  41      15.216  -7.200  28.781  0.00 78.09           C  
ANISOU  320  CD  ARG A  41    11153  15268   3251   6693   3916   3842       C  
ATOM    321  NE  ARG A  41      14.065  -6.707  29.544  0.00 87.64           N  
ANISOU  321  NE  ARG A  41    12139  17568   3589   7882   4553   4375       N  
ATOM    322  CZ  ARG A  41      13.755  -7.094  30.784  0.00 97.51           C  
ANISOU  322  CZ  ARG A  41    13277  19859   3912   8928   5131   5163       C  
ATOM    323  NH1 ARG A  41      14.506  -7.989  31.411  0.00 98.76           N  
ANISOU  323  NH1 ARG A  41    13542  20041   3941   8869   5123   5500       N  
ATOM    324  NH2 ARG A  41      12.690  -6.593  31.406  0.00106.87           N  
ANISOU  324  NH2 ARG A  41    14220  22135   4248  10118   5748   5669       N  
ATOM    325  N   TRP A  42      13.416  -6.783  23.868  1.00 65.58           N  
ANISOU  325  N   TRP A  42     8332  10012   6572   1434   1515   1480       N  
ATOM    326  CA  TRP A  42      13.505  -5.990  22.647  1.00 64.14           C  
ANISOU  326  CA  TRP A  42     8136   9704   6529   1386   1380   1267       C  
ATOM    327  C   TRP A  42      12.570  -4.799  22.646  1.00 63.51           C  
ANISOU  327  C   TRP A  42     8085   9706   6338   1501   1487   1230       C  
ATOM    328  O   TRP A  42      11.612  -4.760  23.402  1.00 63.91           O  
ANISOU  328  O   TRP A  42     8186   9806   6291   1541   1559   1232       O  
ATOM    329  CB  TRP A  42      13.253  -6.840  21.401  1.00 65.13           C  
ANISOU  329  CB  TRP A  42     8250   9394   7101    903    997    924       C  
ATOM    330  CG  TRP A  42      11.982  -7.655  21.386  1.00 65.37           C  
ANISOU  330  CG  TRP A  42     8261   9030   7544    574    607    564       C  
ATOM    331  CD1 TRP A  42      11.835  -8.950  21.806  1.00 67.58           C  
ANISOU  331  CD1 TRP A  42     8673   9041   7962    131    491    191       C  
ATOM    332  CD2 TRP A  42      10.701  -7.254  20.879  1.00 65.23           C  
ANISOU  332  CD2 TRP A  42     8127   8767   7887    305    273    315       C  
ATOM    333  NE1 TRP A  42      10.543  -9.373  21.606  1.00 66.77           N  
ANISOU  333  NE1 TRP A  42     8251   9032   8085     73    339    178       N  
ATOM    334  CE2 TRP A  42       9.820  -8.355  21.043  1.00 66.05           C  
ANISOU  334  CE2 TRP A  42     8287   8785   8024    315    227    310       C  
ATOM    335  CE3 TRP A  42      10.200  -6.073  20.313  1.00 66.54           C  
ANISOU  335  CE3 TRP A  42     8519   8789   7974    118    340    167       C  
ATOM    336  CZ2 TRP A  42       8.471  -8.309  20.658  1.00 66.73           C  
ANISOU  336  CZ2 TRP A  42     8358   9015   7981    279    368    307       C  
ATOM    337  CZ3 TRP A  42       8.858  -6.025  19.929  1.00 64.46           C  
ANISOU  337  CZ3 TRP A  42     7961   8696   7833    451    220    425       C  
ATOM    338  CH2 TRP A  42       8.010  -7.139  20.104  1.00 65.37           C  
ANISOU  338  CH2 TRP A  42     8071   8874   7892    421    279    408       C  
ATOM    339  N   LYS A  43      12.862  -3.835  21.778  1.00 61.72           N  
ANISOU  339  N   LYS A  43     7912   9441   6094   1572   1450   1105       N  
ATOM    340  CA  LYS A  43      12.057  -2.637  21.614  1.00 59.96           C  
ANISOU  340  CA  LYS A  43     7704   9061   6014   1474   1304    890       C  
ATOM    341  C   LYS A  43      11.549  -2.585  20.162  1.00 58.54           C  
ANISOU  341  C   LYS A  43     7476   8858   5906   1526   1320    835       C  
ATOM    342  O   LYS A  43      12.294  -2.908  19.225  1.00 57.93           O  
ANISOU  342  O   LYS A  43     7445   8745   5818   1529   1255    838       O  
ATOM    343  CB  LYS A  43      12.896  -1.390  21.925  1.00 60.29           C  
ANISOU  343  CB  LYS A  43     7739   8950   6218   1278   1098    744       C  
ATOM    344  CG  LYS A  43      13.469  -1.311  23.339  1.00 60.33           C  
ANISOU  344  CG  LYS A  43     7745   8559   6617    865    706    513       C  
ATOM    345  CD  LYS A  43      14.394  -0.493  23.628  0.00 56.84           C  
ANISOU  345  CD  LYS A  43     9527   9627   2442   5792   1546   -303       C  
ATOM    346  CE  LYS A  43      15.707  -1.286  23.614  0.00 52.32           C  
ANISOU  346  CE  LYS A  43     9093   8578   2207   5120   1238   -377       C  
ATOM    347  NZ  LYS A  43      16.785  -0.571  22.854  0.00 47.64           N  
ANISOU  347  NZ  LYS A  43     8799   7070   2231   4580    485  -1019       N  
ATOM    348  N   PRO A  44      10.282  -2.215  19.968  1.00 57.33           N  
ANISOU  348  N   PRO A  44     7307   8576   5897   1447   1229    716       N  
ATOM    349  CA  PRO A  44       9.772  -1.945  18.618  1.00 55.30           C  
ANISOU  349  CA  PRO A  44     7044   8227   5738   1381   1206    642       C  
ATOM    350  C   PRO A  44      10.481  -0.746  17.999  1.00 52.80           C  
ANISOU  350  C   PRO A  44     6709   7825   5526   1381   1146    562       C  
ATOM    351  O   PRO A  44      10.868   0.189  18.710  1.00 52.95           O  
ANISOU  351  O   PRO A  44     6744   7888   5484   1402   1151    571       O  
ATOM    352  CB  PRO A  44       8.275  -1.662  18.835  1.00 55.57           C  
ANISOU  352  CB  PRO A  44     7027   8155   5929   1167    966    544       C  
ATOM    353  CG  PRO A  44       8.148  -1.287  20.271  1.00 56.75           C  
ANISOU  353  CG  PRO A  44     7172   8235   6154   1058    919    490       C  
ATOM    354  CD  PRO A  44       9.237  -2.055  21.002  1.00 57.46           C  
ANISOU  354  CD  PRO A  44     7295   8472   6063   1195   1074    603       C  
ATOM    355  N   LYS A  45      10.672  -0.799  16.686  1.00 48.75           N  
ANISOU  355  N   LYS A  45     6202   7046   5274   1196   1025    461       N  
ATOM    356  CA  LYS A  45      11.327   0.262  15.937  1.00 45.43           C  
ANISOU  356  CA  LYS A  45     5753   6381   5125    960    789    297       C  
ATOM    357  C   LYS A  45      10.804   0.233  14.506  1.00 43.10           C  
ANISOU  357  C   LYS A  45     5452   5995   4926    915    807    291       C  
ATOM    358  O   LYS A  45      10.364  -0.803  14.035  1.00 42.64           O  
ANISOU  358  O   LYS A  45     5378   5962   4858    873    786    323       O  
ATOM    359  CB  LYS A  45      12.850   0.085  15.967  1.00 45.16           C  
ANISOU  359  CB  LYS A  45     5727   6203   5228    784    641    281       C  
ATOM    360  CG  LYS A  45      13.620   1.201  15.264  1.00 45.41           C  
ANISOU  360  CG  LYS A  45     5679   6131   5443    581    427    166       C  
ATOM    361  CD  LYS A  45      15.122   0.965  15.251  1.00 46.02           C  
ANISOU  361  CD  LYS A  45     5817   6172   5493    552    425    163       C  
ATOM    362  CE  LYS A  45      15.890   1.955  14.352  1.00 45.40           C  
ANISOU  362  CE  LYS A  45     5808   5857   5584    312    269     95       C  
ATOM    363  NZ  LYS A  45      15.666   3.384  14.700  1.00 46.68           N  
ANISOU  363  NZ  LYS A  45     6059   5821   5856    108    165    -96       N  
ATOM    364  N   MET A  46      10.832   1.373  13.825  1.00 41.26           N  
ANISOU  364  N   MET A  46     5174   5665   4836    819    692    181       N  
ATOM    365  CA  MET A  46      10.449   1.452  12.408  1.00 39.39           C  
ANISOU  365  CA  MET A  46     4888   5303   4774    679    585    158       C  
ATOM    366  C   MET A  46      11.673   1.858  11.588  1.00 36.79           C  
ANISOU  366  C   MET A  46     4575   4887   4514    677    492    149       C  
ATOM    367  O   MET A  46      12.460   2.692  12.023  1.00 36.81           O  
ANISOU  367  O   MET A  46     4586   4908   4490    647    497    173       O  
ATOM    368  CB  MET A  46       9.312   2.459  12.216  1.00 41.42           C  
ANISOU  368  CB  MET A  46     5148   5519   5070    576    438    112       C  
ATOM    369  CG  MET A  46       8.017   2.126  13.000  1.00 44.90           C  
ANISOU  369  CG  MET A  46     5489   5919   5652    357    409    115       C  
ATOM    370  SD  MET A  46       6.723   1.371  11.964  1.00 53.77           S  
ANISOU  370  SD  MET A  46     6295   7269   6864     62    329   -172       S  
ATOM    371  CE  MET A  46       5.281   1.450  13.063  1.00 48.69           C  
ANISOU  371  CE  MET A  46     5782   6446   6271    142    176     70       C  
ATOM    372  N   ILE A  47      11.864   1.246  10.425  1.00 33.68           N  
ANISOU  372  N   ILE A  47     4088   4422   4285    637    427    130       N  
ATOM    373  CA  ILE A  47      12.915   1.686   9.521  1.00 31.79           C  
ANISOU  373  CA  ILE A  47     3834   4102   4139    495    362     95       C  
ATOM    374  C   ILE A  47      12.364   1.927   8.146  1.00 30.74           C  
ANISOU  374  C   ILE A  47     3570   4027   4081    547    392    158       C  
ATOM    375  O   ILE A  47      11.438   1.271   7.711  1.00 30.22           O  
ANISOU  375  O   ILE A  47     3521   3973   3987    517    432    181       O  
ATOM    376  CB  ILE A  47      14.095   0.688   9.434  1.00 32.01           C  
ANISOU  376  CB  ILE A  47     3865   4145   4153    389    258     90       C  
ATOM    377  CG1 ILE A  47      13.595  -0.735   9.205  1.00 32.93           C  
ANISOU  377  CG1 ILE A  47     4069   4111   4330    308    310     76       C  
ATOM    378  CG2 ILE A  47      14.965   0.777  10.668  1.00 33.40           C  
ANISOU  378  CG2 ILE A  47     4160   4245   4284    304    205     36       C  
ATOM    379  CD1 ILE A  47      14.545  -1.584   8.378  1.00 35.97           C  
ANISOU  379  CD1 ILE A  47     4327   4602   4737    262    231     33       C  
ATOM    380  N   GLY A  48      12.969   2.850   7.428  1.00 30.86           N  
ANISOU  380  N   GLY A  48     3547   4088   4089    611    352    198       N  
ATOM    381  CA  GLY A  48      12.481   3.161   6.092  1.00 31.29           C  
ANISOU  381  CA  GLY A  48     3477   4293   4116    603    283    312       C  
ATOM    382  C   GLY A  48      13.459   2.842   4.998  1.00 31.52           C  
ANISOU  382  C   GLY A  48     3454   4444   4077    681    264    342       C  
ATOM    383  O   GLY A  48      14.684   2.738   5.221  1.00 31.19           O  
ANISOU  383  O   GLY A  48     3465   4427   3957    577    232    337       O  
ATOM    384  N   GLY A  49      12.908   2.682   3.807  1.00 32.37           N  
ANISOU  384  N   GLY A  49     3397   4729   4173    767    177    396       N  
ATOM    385  CA  GLY A  49      13.707   2.469   2.614  1.00 34.63           C  
ANISOU  385  CA  GLY A  49     3587   5241   4328    846    169    431       C  
ATOM    386  C   GLY A  49      12.949   2.836   1.354  1.00 36.18           C  
ANISOU  386  C   GLY A  49     3753   5531   4461    931    105    464       C  
ATOM    387  O   GLY A  49      11.953   3.567   1.401  1.00 36.31           O  
ANISOU  387  O   GLY A  49     3831   5476   4487    930    107    453       O  
ATOM    388  N   ILE A  50      13.414   2.313   0.229  1.00 37.75           N  
ANISOU  388  N   ILE A  50     3923   5829   4591    989     77    389       N  
ATOM    389  CA  ILE A  50      12.715   2.462  -1.034  1.00 40.00           C  
ANISOU  389  CA  ILE A  50     4311   6100   4784    968     -3    357       C  
ATOM    390  C   ILE A  50      11.327   1.768  -0.936  1.00 40.68           C  
ANISOU  390  C   ILE A  50     4300   6312   4842   1096    -30    324       C  
ATOM    391  O   ILE A  50      11.200   0.640  -0.454  1.00 41.68           O  
ANISOU  391  O   ILE A  50     4513   6423   4899   1043     -8    344       O  
ATOM    392  CB  ILE A  50      13.602   1.917  -2.187  1.00 39.68           C  
ANISOU  392  CB  ILE A  50     4360   5929   4784    815     -2    280       C  
ATOM    393  CG1 ILE A  50      13.915   3.025  -3.187  1.00 42.10           C  
ANISOU  393  CG1 ILE A  50     4783   5994   5216    474     34    194       C  
ATOM    394  CG2 ILE A  50      12.955   0.748  -2.907  1.00 41.07           C  
ANISOU  394  CG2 ILE A  50     4617   5865   5123    602     46    175       C  
ATOM    395  CD1 ILE A  50      15.312   3.554  -3.120  1.00 43.01           C  
ANISOU  395  CD1 ILE A  50     5055   5855   5429    285    -95      7       C  
ATOM    396  N   GLY A  51      10.274   2.442  -1.346  1.00 40.59           N  
ANISOU  396  N   GLY A  51     4196   6321   4905   1158    -75    246       N  
ATOM    397  CA  GLY A  51       8.949   1.823  -1.236  1.00 41.03           C  
ANISOU  397  CA  GLY A  51     4244   6281   5061   1035    -54    208       C  
ATOM    398  C   GLY A  51       8.236   1.846   0.115  1.00 40.49           C  
ANISOU  398  C   GLY A  51     4073   6159   5153    967    -62    198       C  
ATOM    399  O   GLY A  51       7.092   1.399   0.217  1.00 41.54           O  
ANISOU  399  O   GLY A  51     4184   6244   5353    936    -57    213       O  
ATOM    400  N   GLY A  52       8.891   2.355   1.149  1.00 39.22           N  
ANISOU  400  N   GLY A  52     3896   5936   5069    925    -20    224       N  
ATOM    401  CA  GLY A  52       8.226   2.562   2.418  1.00 37.73           C  
ANISOU  401  CA  GLY A  52     3697   5571   5068    787    113    249       C  
ATOM    402  C   GLY A  52       8.938   2.174   3.696  1.00 36.83           C  
ANISOU  402  C   GLY A  52     3628   5379   4984    652    162    220       C  
ATOM    403  O   GLY A  52      10.172   2.104   3.741  1.00 36.03           O  
ANISOU  403  O   GLY A  52     3518   5246   4924    730    216    227       O  
ATOM    404  N  APHE A  53       8.132   1.884   4.708  0.50 36.97           N  
ANISOU  404  N  APHE A  53     3691   5299   5056    570    190    218       N  
ATOM    405  N  BPHE A  53       8.149   1.959   4.761  0.50 36.39           N  
ANISOU  405  N  BPHE A  53     3614   5226   4984    572    200    216       N  
ATOM    406  CA APHE A  53       8.631   1.571   6.025  0.50 37.20           C  
ANISOU  406  CA APHE A  53     3814   5218   5101    457    217    238       C  
ATOM    407  CA BPHE A  53       8.637   1.758   6.147  0.50 36.06           C  
ANISOU  407  CA BPHE A  53     3668   5079   4952    469    245    224       C  
ATOM    408  C  APHE A  53       8.309   0.141   6.391  0.50 36.98           C  
ANISOU  408  C  APHE A  53     3697   5228   5124    422    269    249       C  
ATOM    409  C  BPHE A  53       8.160   0.399   6.720  0.50 36.41           C  
ANISOU  409  C  BPHE A  53     3632   5149   5053    428    297    255       C  
ATOM    410  O  APHE A  53       7.423  -0.477   5.803  0.50 37.07           O  
ANISOU  410  O  APHE A  53     3678   5266   5141    422    260    229       O  
ATOM    411  O  BPHE A  53       6.982   0.080   6.583  0.50 36.76           O  
ANISOU  411  O  BPHE A  53     3645   5239   5082    447    252    247       O  
ATOM    412  CB APHE A  53       8.004   2.507   7.049  0.50 37.79           C  
ANISOU  412  CB APHE A  53     4097   5188   5073    377    155    169       C  
ATOM    413  CB BPHE A  53       8.110   2.884   7.068  0.50 35.07           C  
ANISOU  413  CB BPHE A  53     3703   4819   4800    310    184    162       C  
ATOM    414  CG APHE A  53       6.557   2.214   7.335  0.50 38.66           C  
ANISOU  414  CG APHE A  53     4393   5136   5156    174    109    102       C  
ATOM    415  CG BPHE A  53       8.921   4.178   7.049  0.50 34.44           C  
ANISOU  415  CG BPHE A  53     3849   4680   4554    272    148     68       C  
ATOM    416  CD1APHE A  53       6.193   1.500   8.478  0.50 40.41           C  
ANISOU  416  CD1APHE A  53     4871   5203   5279     95     43     83       C  
ATOM    417  CD1BPHE A  53       8.705   5.148   6.077  0.50 33.30           C  
ANISOU  417  CD1BPHE A  53     3901   4417   4335    175    120    -57       C  
ATOM    418  CD2APHE A  53       5.558   2.668   6.479  0.50 38.88           C  
ANISOU  418  CD2APHE A  53     4612   5107   5054     98    -26      7       C  
ATOM    419  CD2BPHE A  53       9.856   4.449   8.054  0.50 34.28           C  
ANISOU  419  CD2BPHE A  53     4127   4473   4423    145    101    -17       C  
ATOM    420  CE1APHE A  53       4.857   1.233   8.756  0.50 40.09           C  
ANISOU  420  CE1APHE A  53     4698   5274   5257     56     33     55       C  
ATOM    421  CE1BPHE A  53       9.445   6.346   6.076  0.50 32.51           C  
ANISOU  421  CE1BPHE A  53     3885   4288   4179    146     74    -30       C  
ATOM    422  CE2APHE A  53       4.221   2.407   6.751  0.50 39.24           C  
ANISOU  422  CE2APHE A  53     4732   5098   5077     50     37     73       C  
ATOM    423  CE2BPHE A  53      10.604   5.636   8.055  0.50 31.76           C  
ANISOU  423  CE2BPHE A  53     3926   4130   4010    135     94   -103       C  
ATOM    424  CZ APHE A  53       3.867   1.695   7.886  0.50 39.70           C  
ANISOU  424  CZ APHE A  53     4653   5203   5227     72     75     28       C  
ATOM    425  CZ BPHE A  53      10.391   6.585   7.073  0.50 33.36           C  
ANISOU  425  CZ BPHE A  53     3969   4438   4265    248    206   -104       C  
ATOM    426  N   ILE A  54       9.053  -0.380   7.363  1.00 36.51           N  
ANISOU  426  N   ILE A  54     3598   5195   5080    409    325    312       N  
ATOM    427  CA  ILE A  54       8.690  -1.642   8.042  1.00 36.39           C  
ANISOU  427  CA  ILE A  54     3666   5081   5078    301    344    315       C  
ATOM    428  C   ILE A  54       8.888  -1.532   9.555  1.00 37.12           C  
ANISOU  428  C   ILE A  54     3720   5190   5192    311    444    432       C  
ATOM    429  O   ILE A  54       9.676  -0.716  10.040  1.00 36.77           O  
ANISOU  429  O   ILE A  54     3761   5070   5138    333    453    433       O  
ATOM    430  CB  ILE A  54       9.440  -2.923   7.528  1.00 36.13           C  
ANISOU  430  CB  ILE A  54     3752   5049   4925    241    269    267       C  
ATOM    431  CG1 ILE A  54      10.966  -2.799   7.652  1.00 35.31           C  
ANISOU  431  CG1 ILE A  54     3766   4912   4738    224    243    175       C  
ATOM    432  CG2 ILE A  54       8.976  -3.364   6.127  1.00 37.16           C  
ANISOU  432  CG2 ILE A  54     4025   5009   5083     74    216    170       C  
ATOM    433  CD1 ILE A  54      11.696  -4.189   7.625  1.00 34.96           C  
ANISOU  433  CD1 ILE A  54     3779   4766   4735    108    219    195       C  
ATOM    434  N   LYS A  55       8.152  -2.365  10.293  1.00 38.49           N  
ANISOU  434  N   LYS A  55     3893   5356   5374    285    538    512       N  
ATOM    435  CA  LYS A  55       8.358  -2.512  11.733  1.00 39.30           C  
ANISOU  435  CA  LYS A  55     4027   5478   5427    232    607    618       C  
ATOM    436  C   LYS A  55       9.348  -3.658  11.995  1.00 39.22           C  
ANISOU  436  C   LYS A  55     4059   5456   5386    206    688    668       C  
ATOM    437  O   LYS A  55       9.286  -4.705  11.355  1.00 39.39           O  
ANISOU  437  O   LYS A  55     4038   5428   5498    174    652    698       O  
ATOM    438  CB  LYS A  55       7.020  -2.707  12.470  1.00 39.57           C  
ANISOU  438  CB  LYS A  55     4122   5446   5463    157    521    530       C  
ATOM    439  CG  LYS A  55       6.598  -1.704  13.370  0.00 40.76           C  
ANISOU  439  CG  LYS A  55     2705   7170   5612   1460   2194   2230       C  
ATOM    440  CD  LYS A  55       5.808  -2.271  14.552  0.00 47.25           C  
ANISOU  440  CD  LYS A  55     3010   8554   6385   1712   2680   3001       C  
ATOM    441  CE  LYS A  55       4.609  -1.407  14.912  0.00 52.60           C  
ANISOU  441  CE  LYS A  55     3359   9836   6786   2357   3095   3298       C  
ATOM    442  NZ  LYS A  55       3.470  -1.517  13.930  0.00 54.49           N  
ANISOU  442  NZ  LYS A  55     2944  10076   7684   2061   2953   3605       N  
ATOM    443  N   VAL A  56      10.294  -3.418  12.895  1.00 38.71           N  
ANISOU  443  N   VAL A  56     4086   5420   5201    193    730    676       N  
ATOM    444  CA  VAL A  56      11.308  -4.413  13.239  1.00 39.04           C  
ANISOU  444  CA  VAL A  56     4357   5392   5083    212    676    614       C  
ATOM    445  C   VAL A  56      11.429  -4.510  14.750  1.00 39.85           C  
ANISOU  445  C   VAL A  56     4491   5528   5122    231    767    697       C  
ATOM    446  O   VAL A  56      10.917  -3.656  15.479  1.00 39.82           O  
ANISOU  446  O   VAL A  56     4530   5544   5055    220    792    703       O  
ATOM    447  CB  VAL A  56      12.724  -4.083  12.643  1.00 38.38           C  
ANISOU  447  CB  VAL A  56     4313   5269   4998    158    532    494       C  
ATOM    448  CG1 VAL A  56      12.715  -4.109  11.116  1.00 38.22           C  
ANISOU  448  CG1 VAL A  56     4462   5071   4989    185    423    303       C  
ATOM    449  CG2 VAL A  56      13.238  -2.748  13.138  1.00 37.98           C  
ANISOU  449  CG2 VAL A  56     4427   5159   4846    192    302    439       C  
ATOM    450  N   ARG A  57      12.116  -5.545  15.210  1.00 40.39           N  
ANISOU  450  N   ARG A  57     4694   5594   5059    270    782    723       N  
ATOM    451  CA  ARG A  57      12.443  -5.687  16.625  1.00 41.73           C  
ANISOU  451  CA  ARG A  57     5061   5693   5101    276    680    667       C  
ATOM    452  C   ARG A  57      13.904  -5.343  16.840  1.00 39.76           C  
ANISOU  452  C   ARG A  57     4979   5449   4676    374    727    728       C  
ATOM    453  O   ARG A  57      14.767  -5.807  16.114  1.00 39.04           O  
ANISOU  453  O   ARG A  57     4842   5341   4648    293    677    794       O  
ATOM    454  CB  ARG A  57      12.099  -7.099  17.117  1.00 41.45           C  
ANISOU  454  CB  ARG A  57     5080   5600   5067    210    604    611       C  
ATOM    455  CG  ARG A  57      10.593  -7.389  16.963  1.00 43.79           C  
ANISOU  455  CG  ARG A  57     5384   5772   5483    112    346    396       C  
ATOM    456  CD  ARG A  57      10.147  -8.785  17.353  1.00 45.29           C  
ANISOU  456  CD  ARG A  57     5625   5919   5664     84    368    500       C  
ATOM    457  NE  ARG A  57      10.990  -9.786  16.703  1.00 52.31           N  
ANISOU  457  NE  ARG A  57     6626   6619   6630    168    298     89       N  
ATOM    458  CZ  ARG A  57      11.310 -10.968  17.235  1.00 55.22           C  
ANISOU  458  CZ  ARG A  57     7097   6855   7026     81    196    181       C  
ATOM    459  NH1 ARG A  57      10.842 -11.311  18.445  1.00 57.24           N  
ANISOU  459  NH1 ARG A  57     7342   7145   7261      4     91     74       N  
ATOM    460  NH2 ARG A  57      12.102 -11.811  16.553  1.00 57.01           N  
ANISOU  460  NH2 ARG A  57     7173   7107   7378    -24    159    166       N  
ATOM    461  N   GLN A  58      14.166  -4.490  17.814  1.00 39.51           N  
ANISOU  461  N   GLN A  58     5169   5403   4438    488    718    705       N  
ATOM    462  CA  GLN A  58      15.513  -4.102  18.107  1.00 39.61           C  
ANISOU  462  CA  GLN A  58     5386   5377   4287    492    664    508       C  
ATOM    463  C   GLN A  58      16.117  -4.867  19.291  1.00 40.00           C  
ANISOU  463  C   GLN A  58     5573   5441   4182    517    655    424       C  
ATOM    464  O   GLN A  58      15.557  -4.856  20.386  1.00 40.60           O  
ANISOU  464  O   GLN A  58     5634   5549   4241    559    674    422       O  
ATOM    465  CB  GLN A  58      15.565  -2.623  18.400  1.00 40.05           C  
ANISOU  465  CB  GLN A  58     5364   5447   4404    415    514    441       C  
ATOM    466  CG  GLN A  58      16.898  -2.220  18.973  1.00 40.82           C  
ANISOU  466  CG  GLN A  58     5396   5377   4737    220    340    287       C  
ATOM    467  CD  GLN A  58      17.059  -0.757  19.044  1.00 42.34           C  
ANISOU  467  CD  GLN A  58     5521   5429   5136    193     42     86       C  
ATOM    468  OE1 GLN A  58      17.862  -0.251  19.833  1.00 44.51           O  
ANISOU  468  OE1 GLN A  58     5954   5441   5515    258    131     84       O  
ATOM    469  NE2 GLN A  58      16.322  -0.049  18.208  1.00 44.79           N  
ANISOU  469  NE2 GLN A  58     5736   5735   5547    157     94    100       N  
ATOM    470  N   TYR A  59      17.270  -5.495  19.066  1.00 39.20           N  
ANISOU  470  N   TYR A  59     5634   5214   4045    563    576    326       N  
ATOM    471  CA  TYR A  59      18.057  -6.112  20.122  1.00 39.26           C  
ANISOU  471  CA  TYR A  59     5795   5105   4016    542    476    283       C  
ATOM    472  C   TYR A  59      19.415  -5.428  20.305  1.00 39.23           C  
ANISOU  472  C   TYR A  59     5981   5042   3883    630    379    221       C  
ATOM    473  O   TYR A  59      20.158  -5.249  19.329  1.00 38.44           O  
ANISOU  473  O   TYR A  59     5922   4914   3769    617    374    216       O  
ATOM    474  CB  TYR A  59      18.324  -7.561  19.771  1.00 39.30           C  
ANISOU  474  CB  TYR A  59     5628   5071   4232    334    371    277       C  
ATOM    475  CG  TYR A  59      17.108  -8.429  19.695  1.00 39.63           C  
ANISOU  475  CG  TYR A  59     5409   5016   4631    240    219    169       C  
ATOM    476  CD1 TYR A  59      16.379  -8.522  18.528  1.00 39.27           C  
ANISOU  476  CD1 TYR A  59     5262   4943   4714    119    215    159       C  
ATOM    477  CD2 TYR A  59      16.708  -9.200  20.798  1.00 40.18           C  
ANISOU  477  CD2 TYR A  59     5262   5132   4872    106    260    121       C  
ATOM    478  CE1 TYR A  59      15.271  -9.344  18.444  1.00 41.32           C  
ANISOU  478  CE1 TYR A  59     5357   5263   5080     72    162     89       C  
ATOM    479  CE2 TYR A  59      15.605 -10.037  20.720  1.00 40.76           C  
ANISOU  479  CE2 TYR A  59     5336   5231   4917     48    202    215       C  
ATOM    480  CZ  TYR A  59      14.896 -10.103  19.550  1.00 41.08           C  
ANISOU  480  CZ  TYR A  59     5415   5290   4903      0    139    177       C  
ATOM    481  OH  TYR A  59      13.801 -10.916  19.461  1.00 42.71           O  
ANISOU  481  OH  TYR A  59     5710   5423   5094     31    230    339       O  
ATOM    482  N   ASP A  60      19.751  -5.086  21.551  1.00 39.76           N  
ANISOU  482  N   ASP A  60     6263   5041   3802    704    299    130       N  
ATOM    483  CA  ASP A  60      21.060  -4.498  21.885  1.00 40.77           C  
ANISOU  483  CA  ASP A  60     6513   5110   3868    694    128     28       C  
ATOM    484  C   ASP A  60      22.096  -5.517  22.363  1.00 40.22           C  
ANISOU  484  C   ASP A  60     6607   4999   3675    701     43    -27       C  
ATOM    485  O   ASP A  60      21.764  -6.613  22.807  1.00 39.74           O  
ANISOU  485  O   ASP A  60     6632   4994   3470    782     20    -12       O  
ATOM    486  CB  ASP A  60      20.923  -3.383  22.925  1.00 41.40           C  
ANISOU  486  CB  ASP A  60     6398   5190   4140    563    121     -7       C  
ATOM    487  CG  ASP A  60      19.982  -2.288  22.479  1.00 44.20           C  
ANISOU  487  CG  ASP A  60     6455   5546   4794    471     43      0       C  
ATOM    488  OD1 ASP A  60      19.451  -1.572  23.350  1.00 47.58           O  
ANISOU  488  OD1 ASP A  60     6510   6166   5402    377    132   -121       O  
ATOM    489  OD2 ASP A  60      19.696  -2.064  21.283  1.00 46.01           O  
ANISOU  489  OD2 ASP A  60     6525   5772   5184    362     38    -19       O  
ATOM    490  N   GLN A  61      23.356  -5.125  22.233  1.00 39.82           N  
ANISOU  490  N   GLN A  61     6605   4863   3658    638    -73    -44       N  
ATOM    491  CA  GLN A  61      24.489  -5.878  22.724  1.00 39.20           C  
ANISOU  491  CA  GLN A  61     6440   4676   3776    509   -108    -70       C  
ATOM    492  C   GLN A  61      24.419  -7.317  22.246  1.00 36.95           C  
ANISOU  492  C   GLN A  61     6122   4419   3497    434   -151     -9       C  
ATOM    493  O   GLN A  61      24.517  -8.255  23.023  1.00 36.15           O  
ANISOU  493  O   GLN A  61     6069   4270   3396    458   -141    -31       O  
ATOM    494  CB  GLN A  61      24.595  -5.752  24.252  1.00 40.56           C  
ANISOU  494  CB  GLN A  61     6358   5004   4047    416    -60    -24       C  
ATOM    495  CG  GLN A  61      24.762  -4.283  24.699  1.00 45.79           C  
ANISOU  495  CG  GLN A  61     6715   5480   5201    222   -115   -103       C  
ATOM    496  CD  GLN A  61      24.184  -4.007  26.074  1.00 52.42           C  
ANISOU  496  CD  GLN A  61     7208   6617   6091    137     65    -92       C  
ATOM    497  OE1 GLN A  61      23.073  -3.449  26.201  1.00 56.50           O  
ANISOU  497  OE1 GLN A  61     7395   7167   6906    145    -83    -52       O  
ATOM    498  NE2 GLN A  61      24.924  -4.397  27.116  1.00 54.73           N  
ANISOU  498  NE2 GLN A  61     7195   6974   6623    160   -116     -3       N  
ATOM    499  N   ILE A  62      24.231  -7.471  20.940  1.00 33.78           N  
ANISOU  499  N   ILE A  62     5598   3951   3284    286   -190     -2       N  
ATOM    500  CA  ILE A  62      24.237  -8.788  20.330  1.00 30.91           C  
ANISOU  500  CA  ILE A  62     5034   3533   3176    141   -184     72       C  
ATOM    501  C   ILE A  62      25.623  -8.999  19.707  1.00 29.15           C  
ANISOU  501  C   ILE A  62     4810   3213   3052     55   -251    100       C  
ATOM    502  O   ILE A  62      26.174  -8.096  19.046  1.00 27.37           O  
ANISOU  502  O   ILE A  62     4517   3005   2877     40   -303     53       O  
ATOM    503  CB  ILE A  62      23.093  -8.944  19.258  1.00 30.48           C  
ANISOU  503  CB  ILE A  62     4778   3503   3298     92   -175     55       C  
ATOM    504  CG1 ILE A  62      21.696  -8.853  19.892  1.00 31.40           C  
ANISOU  504  CG1 ILE A  62     4751   3739   3438      4   -166    106       C  
ATOM    505  CG2 ILE A  62      23.257 -10.244  18.454  1.00 30.32           C  
ANISOU  505  CG2 ILE A  62     4564   3657   3298     80   -238    -36       C  
ATOM    506  CD1 ILE A  62      21.395  -9.853  21.040  1.00 31.85           C  
ANISOU  506  CD1 ILE A  62     4199   3845   4054   -113   -142    257       C  
ATOM    507  N   LEU A  63      26.165 -10.192  19.952  1.00 27.17           N  
ANISOU  507  N   LEU A  63     4496   2906   2920    -15   -261    129       N  
ATOM    508  CA  LEU A  63      27.423 -10.641  19.400  1.00 26.06           C  
ANISOU  508  CA  LEU A  63     4163   2760   2977    -82   -258    164       C  
ATOM    509  C   LEU A  63      27.207 -11.206  18.022  1.00 25.34           C  
ANISOU  509  C   LEU A  63     3963   2638   3026    -36   -248    170       C  
ATOM    510  O   LEU A  63      26.369 -12.093  17.831  1.00 24.89           O  
ANISOU  510  O   LEU A  63     3925   2569   2963    -66   -234    216       O  
ATOM    511  CB  LEU A  63      28.044 -11.729  20.275  1.00 25.77           C  
ANISOU  511  CB  LEU A  63     4066   2798   2925    -39   -210    122       C  
ATOM    512  CG  LEU A  63      29.348 -12.342  19.781  1.00 25.96           C  
ANISOU  512  CG  LEU A  63     3941   2870   3051   -104   -214     72       C  
ATOM    513  CD1 LEU A  63      30.396 -11.317  19.711  1.00 26.66           C  
ANISOU  513  CD1 LEU A  63     3786   3067   3276    -55   -105    112       C  
ATOM    514  CD2 LEU A  63      29.777 -13.413  20.729  1.00 26.92           C  
ANISOU  514  CD2 LEU A  63     3962   3014   3249     20   -365    -77       C  
ATOM    515  N  AILE A  64      27.937 -10.665  17.052  0.50 24.86           N  
ANISOU  515  N  AILE A  64     3698   2661   3083    -39   -196    164       N  
ATOM    516  N  BILE A  64      27.998 -10.717  17.076  0.50 24.58           N  
ANISOU  516  N  BILE A  64     3671   2623   3045    -36   -204    156       N  
ATOM    517  CA AILE A  64      27.933 -11.177  15.688  0.50 24.92           C  
ANISOU  517  CA AILE A  64     3561   2714   3193    -22   -162    144       C  
ATOM    518  CA BILE A  64      27.915 -11.137  15.691  0.50 24.26           C  
ANISOU  518  CA BILE A  64     3480   2633   3104    -11   -177    137       C  
ATOM    519  C  AILE A  64      29.367 -11.375  15.223  0.50 25.36           C  
ANISOU  519  C  AILE A  64     3537   2766   3330      0   -193    193       C  
ATOM    520  C  BILE A  64      29.329 -11.309  15.112  0.50 25.06           C  
ANISOU  520  C  BILE A  64     3502   2733   3285      0   -189    183       C  
ATOM    521  O  AILE A  64      30.244 -10.568  15.504  0.50 24.47           O  
ANISOU  521  O  AILE A  64     3403   2678   3215    -31   -216    149       O  
ATOM    522  O  BILE A  64      30.175 -10.431  15.249  0.50 24.19           O  
ANISOU  522  O  BILE A  64     3360   2658   3171    -33   -217    124       O  
ATOM    523  CB AILE A  64      27.218 -10.210  14.709  0.50 24.88           C  
ANISOU  523  CB AILE A  64     3517   2777   3159    -39   -146    117       C  
ATOM    524  CB BILE A  64      27.045 -10.119  14.879  0.50 24.06           C  
ANISOU  524  CB BILE A  64     3432   2671   3037    -31   -161     98       C  
ATOM    525  CG1AILE A  64      25.759  -9.989  15.101  0.50 24.81           C  
ANISOU  525  CG1AILE A  64     3406   2914   3106     -1    -86    132       C  
ATOM    526  CG1BILE A  64      26.938 -10.542  13.405  0.50 23.24           C  
ANISOU  526  CG1BILE A  64     3255   2583   2989    -15    -49    111       C  
ATOM    527  CG2AILE A  64      27.280 -10.741  13.264  0.50 25.26           C  
ANISOU  527  CG2AILE A  64     3588   2807   3201    -23     -2    132       C  
ATOM    528  CG2BILE A  64      27.541  -8.647  15.081  0.50 22.76           C  
ANISOU  528  CG2BILE A  64     3191   2603   2852     78    -85    108       C  
ATOM    529  CD1AILE A  64      24.885  -9.564  13.929  0.50 26.02           C  
ANISOU  529  CD1AILE A  64     3350   3256   3278    -91      8     35       C  
ATOM    530  CD1BILE A  64      25.681 -10.114  12.723  0.50 20.42           C  
ANISOU  530  CD1BILE A  64     2861   2281   2615    -21    -39   -131       C  
ATOM    531  N   GLU A  65      29.596 -12.455  14.498  1.00 25.59           N  
ANISOU  531  N   GLU A  65     3542   2712   3468     72   -232    261       N  
ATOM    532  CA  GLU A  65      30.856 -12.647  13.838  1.00 28.04           C  
ANISOU  532  CA  GLU A  65     3614   3024   4013    124   -199    353       C  
ATOM    533  C   GLU A  65      30.652 -12.406  12.325  1.00 28.62           C  
ANISOU  533  C   GLU A  65     3657   3064   4151    132   -156    330       C  
ATOM    534  O   GLU A  65      29.865 -13.112  11.691  1.00 28.53           O  
ANISOU  534  O   GLU A  65     3738   3021   4078     96   -118    248       O  
ATOM    535  CB  GLU A  65      31.365 -14.044  14.108  1.00 28.58           C  
ANISOU  535  CB  GLU A  65     3612   3003   4241    209   -204    387       C  
ATOM    536  CG  GLU A  65      32.838 -14.226  13.804  1.00 33.61           C  
ANISOU  536  CG  GLU A  65     4022   3781   4967    281   -156    478       C  
ATOM    537  CD  GLU A  65      33.470 -15.281  14.707  1.00 39.42           C  
ANISOU  537  CD  GLU A  65     4688   4399   5890    474   -127    712       C  
ATOM    538  OE1 GLU A  65      34.693 -15.582  14.535  1.00 43.14           O  
ANISOU  538  OE1 GLU A  65     4871   5077   6440    485    -50    665       O  
ATOM    539  OE2 GLU A  65      32.742 -15.804  15.609  1.00 41.35           O  
ANISOU  539  OE2 GLU A  65     4731   4722   6255    360    -36    631       O  
ATOM    540  N   ILE A  66      31.325 -11.386  11.782  1.00 28.67           N  
ANISOU  540  N   ILE A  66     3586   3066   4241    123    -91    342       N  
ATOM    541  CA  ILE A  66      31.249 -11.028  10.354  1.00 28.51           C  
ANISOU  541  CA  ILE A  66     3499   3068   4263    188    -84    257       C  
ATOM    542  C   ILE A  66      32.566 -11.372   9.727  1.00 30.35           C  
ANISOU  542  C   ILE A  66     3641   3380   4508    182     14    259       C  
ATOM    543  O   ILE A  66      33.549 -10.683   9.946  1.00 30.40           O  
ANISOU  543  O   ILE A  66     3720   3307   4522    224     58    251       O  
ATOM    544  CB  ILE A  66      31.009  -9.514  10.170  1.00 27.43           C  
ANISOU  544  CB  ILE A  66     3333   2981   4108    138    -73    252       C  
ATOM    545  CG1 ILE A  66      29.803  -9.055  10.991  1.00 26.24           C  
ANISOU  545  CG1 ILE A  66     3329   2813   3825    180   -201    107       C  
ATOM    546  CG2 ILE A  66      30.866  -9.158   8.645  1.00 26.47           C  
ANISOU  546  CG2 ILE A  66     3230   2833   3993     79    -82    210       C  
ATOM    547  CD1 ILE A  66      29.832  -7.582  11.334  1.00 25.18           C  
ANISOU  547  CD1 ILE A  66     3161   2706   3700     95   -151      8       C  
ATOM    548  N   CYS A  67      32.610 -12.467   8.980  1.00 32.59           N  
ANISOU  548  N   CYS A  67     3928   3733   4719    127     52    251       N  
ATOM    549  CA  CYS A  67      33.828 -12.863   8.341  1.00 35.68           C  
ANISOU  549  CA  CYS A  67     4251   4255   5051    206     72    239       C  
ATOM    550  C   CYS A  67      34.958 -13.122   9.326  1.00 36.17           C  
ANISOU  550  C   CYS A  67     4237   4326   5178    256     53    277       C  
ATOM    551  O   CYS A  67      36.090 -12.688   9.090  1.00 37.04           O  
ANISOU  551  O   CYS A  67     4277   4494   5300    271    142    197       O  
ATOM    552  CB  CYS A  67      34.277 -11.735   7.423  1.00 36.87           C  
ANISOU  552  CB  CYS A  67     4489   4424   5094    161     43    211       C  
ATOM    553  SG  CYS A  67      34.263 -12.256   5.747  1.00 44.56           S  
ANISOU  553  SG  CYS A  67     5680   5786   5464     66     54     67       S  
ATOM    554  N   GLY A  68      34.674 -13.786  10.440  1.00 36.08           N  
ANISOU  554  N   GLY A  68     4110   4302   5296    366     32    374       N  
ATOM    555  CA  GLY A  68      35.725 -14.017  11.431  1.00 37.04           C  
ANISOU  555  CA  GLY A  68     4098   4479   5495    436    -59    495       C  
ATOM    556  C   GLY A  68      36.063 -12.846  12.348  1.00 36.83           C  
ANISOU  556  C   GLY A  68     3974   4476   5542    400   -164    605       C  
ATOM    557  O   GLY A  68      36.851 -13.023  13.271  1.00 38.71           O  
ANISOU  557  O   GLY A  68     4158   4759   5789    457   -159    556       O  
ATOM    558  N   HIS A  69      35.474 -11.677  12.123  1.00 35.30           N  
ANISOU  558  N   HIS A  69     3757   4343   5312    342   -209    677       N  
ATOM    559  CA  HIS A  69      35.666 -10.508  12.988  1.00 34.74           C  
ANISOU  559  CA  HIS A  69     3666   4349   5184    231   -268    697       C  
ATOM    560  C   HIS A  69      34.469 -10.351  13.911  1.00 33.74           C  
ANISOU  560  C   HIS A  69     3692   4160   4968    134   -337    697       C  
ATOM    561  O   HIS A  69      33.349 -10.149  13.448  1.00 33.34           O  
ANISOU  561  O   HIS A  69     3626   4060   4979    120   -229    655       O  
ATOM    562  CB  HIS A  69      35.773  -9.214  12.168  1.00 34.54           C  
ANISOU  562  CB  HIS A  69     3618   4341   5161    190   -223    672       C  
ATOM    563  CG  HIS A  69      36.975  -9.142  11.279  1.00 37.25           C  
ANISOU  563  CG  HIS A  69     3827   4826   5500    150   -127    594       C  
ATOM    564  ND1 HIS A  69      37.163  -9.988  10.201  1.00 38.05           N  
ANISOU  564  ND1 HIS A  69     3822   4954   5679     50    -45    542       N  
ATOM    565  CD2 HIS A  69      38.030  -8.287  11.277  1.00 38.16           C  
ANISOU  565  CD2 HIS A  69     3717   5169   5610    134   -188    534       C  
ATOM    566  CE1 HIS A  69      38.294  -9.676   9.592  1.00 40.29           C  
ANISOU  566  CE1 HIS A  69     4013   5407   5885    195    -62    574       C  
ATOM    567  NE2 HIS A  69      38.836  -8.643  10.221  1.00 40.11           N  
ANISOU  567  NE2 HIS A  69     3842   5463   5932     88   -152    555       N  
ATOM    568  N   LYS A  70      34.713 -10.403  15.208  1.00 33.51           N  
ANISOU  568  N   LYS A  70     3769   4117   4846     36   -411    676       N  
ATOM    569  CA  LYS A  70      33.661 -10.226  16.225  1.00 33.12           C  
ANISOU  569  CA  LYS A  70     3819   4077   4685    -42   -503    643       C  
ATOM    570  C   LYS A  70      33.302  -8.755  16.436  1.00 31.63           C  
ANISOU  570  C   LYS A  70     3737   3903   4375   -114   -515    573       C  
ATOM    571  O   LYS A  70      34.173  -7.891  16.519  1.00 31.39           O  
ANISOU  571  O   LYS A  70     3643   3859   4422   -122   -471    464       O  
ATOM    572  CB  LYS A  70      34.105 -10.847  17.559  1.00 33.60           C  
ANISOU  572  CB  LYS A  70     3930   4184   4652     -9   -489    733       C  
ATOM    573  CG  LYS A  70      34.214 -12.363  17.539  1.00 35.89           C  
ANISOU  573  CG  LYS A  70     4143   4409   5085    128   -505    698       C  
ATOM    574  CD  LYS A  70      34.812 -12.825  18.851  1.00 40.01           C  
ANISOU  574  CD  LYS A  70     4742   4907   5551    213   -489    926       C  
ATOM    575  CE  LYS A  70      35.763 -14.007  18.651  1.00 43.62           C  
ANISOU  575  CE  LYS A  70     5057   5370   6145    287   -462    946       C  
ATOM    576  NZ  LYS A  70      35.066 -15.223  18.127  1.00 43.38           N  
ANISOU  576  NZ  LYS A  70     4984   5176   6319    312   -446    873       N  
ATOM    577  N   ALA A  71      32.009  -8.493  16.530  1.00 29.68           N  
ANISOU  577  N   ALA A  71     3645   3672   3960   -267   -607    447       N  
ATOM    578  CA  ALA A  71      31.466  -7.178  16.844  1.00 28.75           C  
ANISOU  578  CA  ALA A  71     3776   3469   3676   -305   -596    465       C  
ATOM    579  C   ALA A  71      30.279  -7.354  17.807  1.00 28.76           C  
ANISOU  579  C   ALA A  71     3920   3434   3573   -321   -587    410       C  
ATOM    580  O   ALA A  71      29.649  -8.438  17.849  1.00 28.64           O  
ANISOU  580  O   ALA A  71     3913   3389   3578   -352   -545    350       O  
ATOM    581  CB  ALA A  71      31.048  -6.475  15.584  1.00 28.79           C  
ANISOU  581  CB  ALA A  71     3818   3465   3653   -241   -538    379       C  
ATOM    582  N   ILE A  72      30.014  -6.341  18.631  1.00 28.52           N  
ANISOU  582  N   ILE A  72     4113   3322   3399   -401   -571    361       N  
ATOM    583  CA  ILE A  72      28.854  -6.352  19.529  1.00 29.00           C  
ANISOU  583  CA  ILE A  72     4334   3385   3298   -434   -498    368       C  
ATOM    584  C   ILE A  72      28.049  -5.119  19.180  1.00 27.59           C  
ANISOU  584  C   ILE A  72     4248   3164   3069   -437   -415    313       C  
ATOM    585  O   ILE A  72      28.601  -4.030  19.064  1.00 27.23           O  
ANISOU  585  O   ILE A  72     4124   3093   3127   -459   -507    246       O  
ATOM    586  CB  ILE A  72      29.233  -6.432  21.068  1.00 29.57           C  
ANISOU  586  CB  ILE A  72     4409   3457   3368   -390   -477    387       C  
ATOM    587  CG1 ILE A  72      29.587  -7.871  21.462  1.00 31.59           C  
ANISOU  587  CG1 ILE A  72     4672   3755   3572   -384   -543    378       C  
ATOM    588  CG2 ILE A  72      28.044  -6.045  21.982  1.00 30.07           C  
ANISOU  588  CG2 ILE A  72     4520   3609   3293   -361   -455    412       C  
ATOM    589  CD1 ILE A  72      30.002  -8.096  22.934  1.00 30.79           C  
ANISOU  589  CD1 ILE A  72     4634   3629   3433   -449   -464    480       C  
ATOM    590  N   GLY A  73      26.744  -5.289  18.984  1.00 26.28           N  
ANISOU  590  N   GLY A  73     4221   2930   2832   -407   -329    238       N  
ATOM    591  CA  GLY A  73      25.925  -4.178  18.572  1.00 25.14           C  
ANISOU  591  CA  GLY A  73     4107   2734   2710   -328   -173    188       C  
ATOM    592  C   GLY A  73      24.453  -4.413  18.564  1.00 25.00           C  
ANISOU  592  C   GLY A  73     4174   2633   2689   -222    -89    179       C  
ATOM    593  O   GLY A  73      23.955  -5.467  18.962  1.00 24.93           O  
ANISOU  593  O   GLY A  73     4053   2573   2845   -262   -150    175       O  
ATOM    594  N   THR A  74      23.754  -3.374  18.147  1.00 24.95           N  
ANISOU  594  N   THR A  74     4161   2658   2660   -126     31    131       N  
ATOM    595  CA  THR A  74      22.332  -3.407  17.930  1.00 24.46           C  
ANISOU  595  CA  THR A  74     4037   2560   2694    -57    126     83       C  
ATOM    596  C   THR A  74      22.072  -4.057  16.589  1.00 23.64           C  
ANISOU  596  C   THR A  74     3799   2444   2737    -61    122    135       C  
ATOM    597  O   THR A  74      22.661  -3.693  15.550  1.00 23.01           O  
ANISOU  597  O   THR A  74     3679   2420   2642    -50    122    126       O  
ATOM    598  CB  THR A  74      21.792  -1.950  17.940  1.00 25.25           C  
ANISOU  598  CB  THR A  74     4167   2644   2780    -23    132     29       C  
ATOM    599  OG1 THR A  74      21.913  -1.448  19.262  1.00 26.39           O  
ANISOU  599  OG1 THR A  74     4366   2772   2888     71    217    -59       O  
ATOM    600  CG2 THR A  74      20.286  -1.897  17.687  1.00 24.75           C  
ANISOU  600  CG2 THR A  74     3989   2689   2723     21    281     36       C  
ATOM    601  N   VAL A  75      21.171  -5.020  16.632  1.00 22.76           N  
ANISOU  601  N   VAL A  75     3534   2331   2781    -16    141    209       N  
ATOM    602  CA  VAL A  75      20.761  -5.768  15.495  1.00 22.47           C  
ANISOU  602  CA  VAL A  75     3374   2382   2779     -9    178    141       C  
ATOM    603  C   VAL A  75      19.239  -5.633  15.448  1.00 22.78           C  
ANISOU  603  C   VAL A  75     3372   2457   2824     -2    244    188       C  
ATOM    604  O   VAL A  75      18.579  -5.788  16.463  1.00 23.76           O  
ANISOU  604  O   VAL A  75     3372   2684   2972    -11    257    214       O  
ATOM    605  CB  VAL A  75      21.211  -7.242  15.704  1.00 22.57           C  
ANISOU  605  CB  VAL A  75     3342   2402   2829    -27    101    117       C  
ATOM    606  CG1 VAL A  75      20.457  -8.191  14.835  1.00 24.31           C  
ANISOU  606  CG1 VAL A  75     3456   2500   3278    -40      2     88       C  
ATOM    607  CG2 VAL A  75      22.729  -7.364  15.428  1.00 22.67           C  
ANISOU  607  CG2 VAL A  75     3346   2523   2746     33     77    150       C  
ATOM    608  N   LEU A  76      18.695  -5.306  14.281  1.00 22.41           N  
ANISOU  608  N   LEU A  76     3243   2389   2883     28    285    240       N  
ATOM    609  CA  LEU A  76      17.260  -5.272  14.067  1.00 22.70           C  
ANISOU  609  CA  LEU A  76     3157   2493   2974     12    335    284       C  
ATOM    610  C   LEU A  76      16.790  -6.539  13.373  1.00 23.04           C  
ANISOU  610  C   LEU A  76     3080   2520   3155    -52    292    336       C  
ATOM    611  O   LEU A  76      17.491  -7.089  12.487  1.00 22.50           O  
ANISOU  611  O   LEU A  76     2898   2460   3190   -121    228    300       O  
ATOM    612  CB  LEU A  76      16.839  -4.034  13.234  1.00 22.46           C  
ANISOU  612  CB  LEU A  76     3203   2444   2883     56    378    267       C  
ATOM    613  CG  LEU A  76      17.411  -2.691  13.643  1.00 22.80           C  
ANISOU  613  CG  LEU A  76     3365   2459   2839    171    409    235       C  
ATOM    614  CD1 LEU A  76      16.882  -1.616  12.703  1.00 22.71           C  
ANISOU  614  CD1 LEU A  76     3158   2514   2957    198    331    211       C  
ATOM    615  CD2 LEU A  76      17.017  -2.370  15.089  1.00 24.57           C  
ANISOU  615  CD2 LEU A  76     3603   2790   2943    210    342    258       C  
ATOM    616  N   VAL A  77      15.610  -7.016  13.755  1.00 23.97           N  
ANISOU  616  N   VAL A  77     3028   2724   3354   -103    259    471       N  
ATOM    617  CA  VAL A  77      15.104  -8.242  13.151  1.00 25.39           C  
ANISOU  617  CA  VAL A  77     3114   2915   3615   -181    245    492       C  
ATOM    618  C   VAL A  77      13.698  -8.004  12.639  1.00 26.65           C  
ANISOU  618  C   VAL A  77     3143   3150   3830   -231    244    509       C  
ATOM    619  O   VAL A  77      12.866  -7.429  13.327  1.00 27.30           O  
ANISOU  619  O   VAL A  77     3128   3320   3924   -286    328    478       O  
ATOM    620  CB  VAL A  77      15.166  -9.410  14.168  1.00 26.51           C  
ANISOU  620  CB  VAL A  77     3287   3024   3761   -173    155    466       C  
ATOM    621  CG1 VAL A  77      14.626 -10.691  13.578  1.00 26.71           C  
ANISOU  621  CG1 VAL A  77     3348   2955   3845   -207    138    385       C  
ATOM    622  CG2 VAL A  77      16.625  -9.630  14.634  1.00 25.99           C  
ANISOU  622  CG2 VAL A  77     3173   2944   3757   -152    206    574       C  
ATOM    623  N   GLY A  78      13.442  -8.406  11.408  1.00 27.81           N  
ANISOU  623  N   GLY A  78     3131   3404   4029   -265    202    547       N  
ATOM    624  CA  GLY A  78      12.158  -8.131  10.779  1.00 29.59           C  
ANISOU  624  CA  GLY A  78     3192   3706   4342   -357     73    600       C  
ATOM    625  C   GLY A  78      12.086  -8.653   9.356  1.00 30.71           C  
ANISOU  625  C   GLY A  78     3196   3935   4534   -426    -21    599       C  
ATOM    626  O   GLY A  78      12.974  -9.403   8.903  1.00 30.22           O  
ANISOU  626  O   GLY A  78     3139   3786   4557   -461    -17    565       O  
ATOM    627  N   PRO A  79      11.025  -8.263   8.647  1.00 31.90           N  
ANISOU  627  N   PRO A  79     3251   4143   4724   -467   -109    640       N  
ATOM    628  CA  PRO A  79      10.714  -8.862   7.360  1.00 31.98           C  
ANISOU  628  CA  PRO A  79     3265   4228   4658   -478   -144    619       C  
ATOM    629  C   PRO A  79      11.534  -8.284   6.232  1.00 31.66           C  
ANISOU  629  C   PRO A  79     3271   4127   4631   -521   -225    556       C  
ATOM    630  O   PRO A  79      11.006  -7.571   5.392  1.00 32.18           O  
ANISOU  630  O   PRO A  79     3366   4217   4642   -423   -277    574       O  
ATOM    631  CB  PRO A  79       9.229  -8.547   7.165  1.00 32.85           C  
ANISOU  631  CB  PRO A  79     3264   4403   4813   -457   -180    605       C  
ATOM    632  CG  PRO A  79       8.807  -7.710   8.366  1.00 32.99           C  
ANISOU  632  CG  PRO A  79     3296   4384   4851   -432   -116    635       C  
ATOM    633  CD  PRO A  79      10.032  -7.249   9.048  1.00 32.22           C  
ANISOU  633  CD  PRO A  79     3287   4169   4783   -438   -118    584       C  
ATOM    634  N   THR A  80      12.833  -8.590   6.213  1.00 30.89           N  
ANISOU  634  N   THR A  80     3369   3898   4468   -551   -208    439       N  
ATOM    635  CA  THR A  80      13.699  -8.090   5.141  1.00 28.66           C  
ANISOU  635  CA  THR A  80     3244   3577   4069   -560   -257    293       C  
ATOM    636  C   THR A  80      13.977  -9.295   4.261  1.00 28.92           C  
ANISOU  636  C   THR A  80     3381   3604   4001   -632   -366    227       C  
ATOM    637  O   THR A  80      13.988 -10.400   4.736  1.00 29.08           O  
ANISOU  637  O   THR A  80     3432   3612   4004   -644   -366    263       O  
ATOM    638  CB  THR A  80      14.974  -7.404   5.734  1.00 27.69           C  
ANISOU  638  CB  THR A  80     3166   3410   3945   -555   -217    285       C  
ATOM    639  OG1 THR A  80      15.891  -7.087   4.682  1.00 25.50           O  
ANISOU  639  OG1 THR A  80     2957   2858   3873   -350   -115    238       O  
ATOM    640  CG2 THR A  80      15.755  -8.354   6.617  1.00 25.06           C  
ANISOU  640  CG2 THR A  80     2946   3071   3505   -481   -177    156       C  
ATOM    641  N   PRO A  81      14.080  -9.119   2.957  1.00 29.49           N  
ANISOU  641  N   PRO A  81     3538   3657   4007   -695   -377    161       N  
ATOM    642  CA  PRO A  81      14.369 -10.265   2.070  1.00 28.90           C  
ANISOU  642  CA  PRO A  81     3621   3450   3910   -764   -449     47       C  
ATOM    643  C   PRO A  81      15.842 -10.710   2.059  1.00 28.44           C  
ANISOU  643  C   PRO A  81     3756   3241   3806   -716   -431    -15       C  
ATOM    644  O   PRO A  81      16.177 -11.745   1.470  1.00 29.29           O  
ANISOU  644  O   PRO A  81     3946   3275   3907   -775   -412    -87       O  
ATOM    645  CB  PRO A  81      13.973  -9.745   0.673  1.00 29.72           C  
ANISOU  645  CB  PRO A  81     3675   3626   3989   -746   -477     56       C  
ATOM    646  CG  PRO A  81      13.873  -8.272   0.766  1.00 29.04           C  
ANISOU  646  CG  PRO A  81     3519   3567   3947   -711   -487    103       C  
ATOM    647  CD  PRO A  81      13.851  -7.860   2.224  1.00 29.33           C  
ANISOU  647  CD  PRO A  81     3536   3567   4039   -685   -365    155       C  
ATOM    648  N   VAL A  82      16.717  -9.922   2.683  1.00 26.62           N  
ANISOU  648  N   VAL A  82     3589   2942   3581   -620   -340    -25       N  
ATOM    649  CA  VAL A  82      18.134 -10.172   2.658  1.00 25.22           C  
ANISOU  649  CA  VAL A  82     3482   2721   3378   -572   -260   -124       C  
ATOM    650  C   VAL A  82      18.673  -9.644   3.978  1.00 23.42           C  
ANISOU  650  C   VAL A  82     3232   2382   3284   -511   -241   -149       C  
ATOM    651  O   VAL A  82      18.155  -8.677   4.522  1.00 22.38           O  
ANISOU  651  O   VAL A  82     3022   2279   3202   -506   -251   -110       O  
ATOM    652  CB  VAL A  82      18.797  -9.540   1.379  1.00 26.19           C  
ANISOU  652  CB  VAL A  82     3577   2783   3587   -550   -224   -112       C  
ATOM    653  CG1 VAL A  82      18.715  -8.040   1.407  1.00 26.73           C  
ANISOU  653  CG1 VAL A  82     3796   2821   3539   -407   -175   -192       C  
ATOM    654  CG2 VAL A  82      20.260 -10.022   1.162  1.00 26.13           C  
ANISOU  654  CG2 VAL A  82     3678   2829   3419   -484   -159   -169       C  
ATOM    655  N   ASN A  83      19.632 -10.366   4.540  1.00 21.83           N  
ANISOU  655  N   ASN A  83     3025   2138   3130   -432   -183   -192       N  
ATOM    656  CA  ASN A  83      20.309  -9.963   5.760  1.00 20.12           C  
ANISOU  656  CA  ASN A  83     2852   1884   2905   -333   -170   -169       C  
ATOM    657  C   ASN A  83      21.241  -8.772   5.414  1.00 18.45           C  
ANISOU  657  C   ASN A  83     2659   1674   2677   -236   -165   -146       C  
ATOM    658  O   ASN A  83      21.995  -8.828   4.467  1.00 18.12           O  
ANISOU  658  O   ASN A  83     2617   1610   2657   -293   -227    -43       O  
ATOM    659  CB  ASN A  83      21.100 -11.147   6.308  1.00 20.39           C  
ANISOU  659  CB  ASN A  83     3026   1773   2948   -351   -113   -166       C  
ATOM    660  CG  ASN A  83      20.204 -12.298   6.744  1.00 22.48           C  
ANISOU  660  CG  ASN A  83     3094   2111   3336   -347    -92   -200       C  
ATOM    661  OD1 ASN A  83      19.233 -12.083   7.455  1.00 23.08           O  
ANISOU  661  OD1 ASN A  83     3537   2005   3225   -400      3    -35       O  
ATOM    662  ND2 ASN A  83      20.536 -13.526   6.333  1.00 21.99           N  
ANISOU  662  ND2 ASN A  83     3060   1670   3622   -345   -260   -207       N  
ATOM    663  N  AILE A  84      21.147  -7.714   6.206  0.50 18.22           N  
ANISOU  663  N  AILE A  84     2634   1672   2614   -223   -169   -114       N  
ATOM    664  N  BILE A  84      21.170  -7.702   6.188  0.50 18.22           N  
ANISOU  664  N  BILE A  84     2628   1685   2610   -229   -174   -108       N  
ATOM    665  CA AILE A  84      21.901  -6.479   5.978  0.50 17.45           C  
ANISOU  665  CA AILE A  84     2516   1612   2499   -180    -73   -128       C  
ATOM    666  CA BILE A  84      21.921  -6.478   5.875  0.50 17.43           C  
ANISOU  666  CA BILE A  84     2508   1643   2470   -196    -78   -109       C  
ATOM    667  C  AILE A  84      22.856  -6.221   7.130  0.50 16.95           C  
ANISOU  667  C  AILE A  84     2427   1545   2467   -162    -73   -113       C  
ATOM    668  C  BILE A  84      22.827  -6.079   7.040  0.50 16.94           C  
ANISOU  668  C  BILE A  84     2430   1561   2445   -187    -79    -98       C  
ATOM    669  O  AILE A  84      22.437  -6.122   8.295  0.50 16.91           O  
ANISOU  669  O  AILE A  84     2332   1583   2506   -159    -78   -168       O  
ATOM    670  O  BILE A  84      22.342  -5.745   8.131  0.50 16.90           O  
ANISOU  670  O  BILE A  84     2367   1579   2472   -235    -94   -161       O  
ATOM    671  CB AILE A  84      20.925  -5.250   5.840  0.50 17.45           C  
ANISOU  671  CB AILE A  84     2484   1678   2467   -177    -61   -129       C  
ATOM    672  CB BILE A  84      20.929  -5.302   5.529  0.50 17.48           C  
ANISOU  672  CB BILE A  84     2473   1695   2472   -196    -95   -101       C  
ATOM    673  CG1AILE A  84      19.981  -5.408   4.648  0.50 17.99           C  
ANISOU  673  CG1AILE A  84     2540   1833   2461   -166    -30   -102       C  
ATOM    674  CG1BILE A  84      20.152  -5.589   4.237  0.50 17.81           C  
ANISOU  674  CG1BILE A  84     2558   1800   2407   -178    -54    -78       C  
ATOM    675  CG2AILE A  84      21.713  -3.933   5.731  0.50 16.68           C  
ANISOU  675  CG2AILE A  84     2497   1502   2339    -63    -18   -159       C  
ATOM    676  CG2BILE A  84      21.683  -3.971   5.408  0.50 16.78           C  
ANISOU  676  CG2BILE A  84     2481   1539   2353    -65    -69   -125       C  
ATOM    677  CD1AILE A  84      20.693  -5.555   3.337  0.50 18.68           C  
ANISOU  677  CD1AILE A  84     2629   2022   2442   -169    -85   -192       C  
ATOM    678  CD1BILE A  84      18.855  -4.793   4.088  0.50 17.09           C  
ANISOU  678  CD1BILE A  84     2433   1714   2345   -196    -57    -32       C  
ATOM    679  N   ILE A  85      24.136  -6.103   6.812  1.00 16.80           N  
ANISOU  679  N   ILE A  85     2461   1460   2463   -135    -52    -89       N  
ATOM    680  CA  ILE A  85      25.094  -5.509   7.783  1.00 16.70           C  
ANISOU  680  CA  ILE A  85     2481   1524   2340   -135    -96   -203       C  
ATOM    681  C   ILE A  85      25.226  -4.011   7.481  1.00 16.12           C  
ANISOU  681  C   ILE A  85     2443   1489   2191   -208    -95   -201       C  
ATOM    682  O   ILE A  85      25.724  -3.649   6.431  1.00 15.91           O  
ANISOU  682  O   ILE A  85     2501   1358   2186   -323   -111   -261       O  
ATOM    683  CB  ILE A  85      26.469  -6.179   7.744  1.00 17.44           C  
ANISOU  683  CB  ILE A  85     2512   1666   2447   -123   -124   -209       C  
ATOM    684  CG1 ILE A  85      26.333  -7.727   7.760  1.00 17.88           C  
ANISOU  684  CG1 ILE A  85     2618   1670   2503    -82   -113    -83       C  
ATOM    685  CG2 ILE A  85      27.361  -5.652   8.922  1.00 18.16           C  
ANISOU  685  CG2 ILE A  85     2604   1833   2461     12   -191   -249       C  
ATOM    686  CD1 ILE A  85      25.552  -8.251   9.004  1.00 18.17           C  
ANISOU  686  CD1 ILE A  85     2516   1582   2804     80     88    -65       C  
ATOM    687  N   GLY A  86      24.807  -3.156   8.420  1.00 16.07           N  
ANISOU  687  N   GLY A  86     2396   1478   2230   -173    -88   -173       N  
ATOM    688  CA  GLY A  86      24.782  -1.708   8.186  1.00 16.02           C  
ANISOU  688  CA  GLY A  86     2588   1456   2043   -257    -46   -134       C  
ATOM    689  C   GLY A  86      25.981  -1.061   8.855  1.00 17.08           C  
ANISOU  689  C   GLY A  86     2785   1579   2125   -235     15    -98       C  
ATOM    690  O   GLY A  86      26.853  -1.730   9.436  1.00 16.82           O  
ANISOU  690  O   GLY A  86     2793   1469   2126   -228     19    -13       O  
ATOM    691  N   ARG A  87      26.029   0.257   8.788  1.00 17.74           N  
ANISOU  691  N   ARG A  87     3016   1561   2162   -251    -23    -71       N  
ATOM    692  CA  ARG A  87      27.198   1.027   9.200  1.00 18.80           C  
ANISOU  692  CA  ARG A  87     3243   1709   2191   -303    -77    -69       C  
ATOM    693  C   ARG A  87      27.505   0.920  10.690  1.00 19.21           C  
ANISOU  693  C   ARG A  87     3322   1701   2273   -289   -120    -90       C  
ATOM    694  O   ARG A  87      28.653   1.028  11.057  1.00 19.73           O  
ANISOU  694  O   ARG A  87     3443   1759   2291   -415   -213    -69       O  
ATOM    695  CB  ARG A  87      27.001   2.495   8.796  1.00 18.60           C  
ANISOU  695  CB  ARG A  87     3192   1668   2204   -388      0    -62       C  
ATOM    696  CG  ARG A  87      27.130   2.744   7.286  1.00 17.70           C  
ANISOU  696  CG  ARG A  87     3006   1748   1970   -232   -239    -68       C  
ATOM    697  CD  ARG A  87      27.158   4.252   6.920  1.00 19.33           C  
ANISOU  697  CD  ARG A  87     3390   1772   2180   -279      4      0       C  
ATOM    698  NE  ARG A  87      25.954   4.953   7.387  1.00 20.91           N  
ANISOU  698  NE  ARG A  87     3905   1829   2209   -166    151    -61       N  
ATOM    699  CZ  ARG A  87      25.900   5.697   8.514  1.00 23.43           C  
ANISOU  699  CZ  ARG A  87     4113   2128   2660   -218    125    -29       C  
ATOM    700  NH1 ARG A  87      26.972   5.861   9.319  1.00 22.32           N  
ANISOU  700  NH1 ARG A  87     4146   1986   2347   -461     21    -40       N  
ATOM    701  NH2 ARG A  87      24.769   6.276   8.848  1.00 23.25           N  
ANISOU  701  NH2 ARG A  87     4184   2054   2594    -29    282    -16       N  
ATOM    702  N   ASN A  88      26.507   0.686  11.540  1.00 19.42           N  
ANISOU  702  N   ASN A  88     3410   1719   2247   -249    -79    -47       N  
ATOM    703  CA  ASN A  88      26.781   0.562  12.975  1.00 20.83           C  
ANISOU  703  CA  ASN A  88     3516   2032   2367   -258    -99   -111       C  
ATOM    704  C   ASN A  88      27.806  -0.554  13.294  1.00 21.76           C  
ANISOU  704  C   ASN A  88     3548   2262   2456   -313   -185    -64       C  
ATOM    705  O   ASN A  88      28.575  -0.447  14.249  1.00 22.68           O  
ANISOU  705  O   ASN A  88     3600   2485   2530   -321   -198   -108       O  
ATOM    706  CB  ASN A  88      25.500   0.329  13.788  1.00 20.68           C  
ANISOU  706  CB  ASN A  88     3445   2038   2372   -324    -62    -83       C  
ATOM    707  CG  ASN A  88      24.857  -1.016  13.514  1.00 20.95           C  
ANISOU  707  CG  ASN A  88     3600   2095   2265   -221    -26   -114       C  
ATOM    708  OD1 ASN A  88      24.543  -1.338  12.384  1.00 20.02           O  
ANISOU  708  OD1 ASN A  88     3269   2170   2167    -37    188   -236       O  
ATOM    709  ND2 ASN A  88      24.602  -1.788  14.577  1.00 21.75           N  
ANISOU  709  ND2 ASN A  88     3617   2056   2588   -253     34    -21       N  
ATOM    710  N   LEU A  89      27.816  -1.593  12.461  1.00 20.80           N  
ANISOU  710  N   LEU A  89     3390   2075   2437   -357   -146    -53       N  
ATOM    711  CA  LEU A  89      28.710  -2.702  12.624  1.00 20.58           C  
ANISOU  711  CA  LEU A  89     3111   2234   2474   -352   -204     33       C  
ATOM    712  C   LEU A  89      29.914  -2.645  11.702  1.00 20.60           C  
ANISOU  712  C   LEU A  89     2997   2259   2570   -395   -251     25       C  
ATOM    713  O   LEU A  89      30.972  -3.133  12.076  1.00 21.33           O  
ANISOU  713  O   LEU A  89     3004   2498   2603   -405   -299      3       O  
ATOM    714  CB  LEU A  89      27.963  -4.042  12.432  1.00 20.27           C  
ANISOU  714  CB  LEU A  89     3028   2229   2442   -340   -189    -27       C  
ATOM    715  CG  LEU A  89      26.861  -4.349  13.454  1.00 21.02           C  
ANISOU  715  CG  LEU A  89     3061   2297   2628   -357   -177     56       C  
ATOM    716  CD1 LEU A  89      26.256  -5.711  13.211  1.00 20.83           C  
ANISOU  716  CD1 LEU A  89     3148   1888   2876   -139    -43    164       C  
ATOM    717  CD2 LEU A  89      27.366  -4.251  14.861  1.00 21.91           C  
ANISOU  717  CD2 LEU A  89     3310   2503   2509   -330    -82    108       C  
ATOM    718  N   LEU A  90      29.740  -2.126  10.491  1.00 20.09           N  
ANISOU  718  N   LEU A  90     2902   2243   2486   -430   -278     95       N  
ATOM    719  CA  LEU A  90      30.858  -1.923   9.571  1.00 21.20           C  
ANISOU  719  CA  LEU A  90     2935   2484   2636   -383   -292     24       C  
ATOM    720  C   LEU A  90      31.975  -1.039  10.206  1.00 22.29           C  
ANISOU  720  C   LEU A  90     3117   2620   2729   -521   -330     82       C  
ATOM    721  O   LEU A  90      33.161  -1.308   9.990  1.00 21.53           O  
ANISOU  721  O   LEU A  90     2990   2569   2621   -521   -288     77       O  
ATOM    722  CB  LEU A  90      30.413  -1.317   8.216  1.00 20.09           C  
ANISOU  722  CB  LEU A  90     2837   2409   2387   -312   -185    -60       C  
ATOM    723  CG  LEU A  90      29.409  -2.168   7.382  1.00 18.95           C  
ANISOU  723  CG  LEU A  90     2542   2163   2495   -282   -140    -89       C  
ATOM    724  CD1 LEU A  90      28.891  -1.433   6.156  1.00 17.09           C  
ANISOU  724  CD1 LEU A  90     2285   1917   2291   -282    -38   -138       C  
ATOM    725  CD2 LEU A  90      29.990  -3.498   6.957  1.00 17.34           C  
ANISOU  725  CD2 LEU A  90     2292   1874   2420   -374     57    -90       C  
ATOM    726  N   THR A  91      31.615  -0.002  10.977  1.00 23.60           N  
ANISOU  726  N   THR A  91     3395   2816   2756   -622   -369    117       N  
ATOM    727  CA  THR A  91      32.663   0.778  11.659  1.00 25.96           C  
ANISOU  727  CA  THR A  91     3716   3094   3050   -690   -415    150       C  
ATOM    728  C   THR A  91      33.418  -0.063  12.672  1.00 27.56           C  
ANISOU  728  C   THR A  91     3810   3436   3224   -770   -508    217       C  
ATOM    729  O   THR A  91      34.616   0.130  12.827  1.00 28.71           O  
ANISOU  729  O   THR A  91     3881   3629   3396   -824   -502    274       O  
ATOM    730  CB  THR A  91      32.124   2.016  12.357  1.00 26.35           C  
ANISOU  730  CB  THR A  91     3786   3165   3061   -665   -393     88       C  
ATOM    731  OG1 THR A  91      31.082   1.610  13.260  1.00 25.85           O  
ANISOU  731  OG1 THR A  91     3981   2941   2899   -699   -266    235       O  
ATOM    732  CG2 THR A  91      31.423   2.948  11.333  1.00 25.50           C  
ANISOU  732  CG2 THR A  91     3952   2924   2810   -610   -308     68       C  
ATOM    733  N   GLN A  92      32.742  -1.020  13.333  1.00 28.51           N  
ANISOU  733  N   GLN A  92     3908   3565   3358   -743   -516    266       N  
ATOM    734  CA  GLN A  92      33.418  -1.840  14.340  1.00 29.31           C  
ANISOU  734  CA  GLN A  92     3881   3717   3536   -665   -509    307       C  
ATOM    735  C   GLN A  92      34.426  -2.817  13.767  1.00 29.52           C  
ANISOU  735  C   GLN A  92     3699   3859   3658   -619   -549    345       C  
ATOM    736  O   GLN A  92      35.382  -3.188  14.438  1.00 30.24           O  
ANISOU  736  O   GLN A  92     3828   3970   3691   -564   -558    397       O  
ATOM    737  CB  GLN A  92      32.409  -2.602  15.181  1.00 29.31           C  
ANISOU  737  CB  GLN A  92     3953   3642   3538   -726   -501    250       C  
ATOM    738  CG  GLN A  92      31.796  -1.756  16.251  1.00 31.72           C  
ANISOU  738  CG  GLN A  92     4248   4018   3785   -607   -370    290       C  
ATOM    739  CD  GLN A  92      30.874  -2.548  17.117  1.00 33.68           C  
ANISOU  739  CD  GLN A  92     4549   4224   4023   -498   -390    336       C  
ATOM    740  OE1 GLN A  92      29.647  -2.356  17.040  1.00 34.96           O  
ANISOU  740  OE1 GLN A  92     4553   4355   4374   -420   -492     24       O  
ATOM    741  NE2 GLN A  92      31.435  -3.467  17.940  1.00 34.23           N  
ANISOU  741  NE2 GLN A  92     4736   4243   4028   -400   -433    312       N  
ATOM    742  N   ILE A  93      34.219  -3.252  12.537  1.00 29.17           N  
ANISOU  742  N   ILE A  93     3458   3887   3738   -574   -514    377       N  
ATOM    743  CA  ILE A  93      35.168  -4.155  11.928  1.00 29.18           C  
ANISOU  743  CA  ILE A  93     3352   3892   3843   -465   -456    386       C  
ATOM    744  C   ILE A  93      36.193  -3.402  11.061  1.00 30.44           C  
ANISOU  744  C   ILE A  93     3367   4139   4058   -524   -419    372       C  
ATOM    745  O   ILE A  93      37.018  -4.038  10.394  1.00 31.87           O  
ANISOU  745  O   ILE A  93     3372   4398   4339   -480   -381    357       O  
ATOM    746  CB  ILE A  93      34.451  -5.296  11.167  1.00 28.76           C  
ANISOU  746  CB  ILE A  93     3304   3815   3806   -438   -418    387       C  
ATOM    747  CG1 ILE A  93      33.719  -4.732   9.930  1.00 28.53           C  
ANISOU  747  CG1 ILE A  93     3253   3713   3872   -326   -439    251       C  
ATOM    748  CG2 ILE A  93      33.512  -6.044  12.104  1.00 27.08           C  
ANISOU  748  CG2 ILE A  93     3252   3330   3707   -307   -374    248       C  
ATOM    749  CD1 ILE A  93      33.120  -5.768   9.038  1.00 27.87           C  
ANISOU  749  CD1 ILE A  93     3366   3540   3680   -177   -257    105       C  
ATOM    750  N   GLY A  94      36.159  -2.064  11.084  1.00 30.04           N  
ANISOU  750  N   GLY A  94     3304   4110   3997   -508   -422    499       N  
ATOM    751  CA  GLY A  94      37.180  -1.275  10.404  1.00 30.19           C  
ANISOU  751  CA  GLY A  94     3302   4170   3997   -548   -389    427       C  
ATOM    752  C   GLY A  94      36.990  -1.232   8.882  1.00 30.35           C  
ANISOU  752  C   GLY A  94     3310   4185   4037   -526   -317    402       C  
ATOM    753  O   GLY A  94      37.947  -1.108   8.100  1.00 30.49           O  
ANISOU  753  O   GLY A  94     3330   4237   4017   -561   -308    523       O  
ATOM    754  N   CYS A  95      35.748  -1.343   8.449  1.00 29.18           N  
ANISOU  754  N   CYS A  95     3236   3969   3881   -555   -251    283       N  
ATOM    755  CA  CYS A  95      35.479  -1.405   7.039  1.00 28.79           C  
ANISOU  755  CA  CYS A  95     3232   3875   3831   -572   -186    283       C  
ATOM    756  C   CYS A  95      35.454   0.005   6.386  1.00 28.05           C  
ANISOU  756  C   CYS A  95     3161   3771   3723   -610   -167    266       C  
ATOM    757  O   CYS A  95      34.780   0.905   6.892  1.00 27.30           O  
ANISOU  757  O   CYS A  95     3104   3649   3617   -612   -172    281       O  
ATOM    758  CB  CYS A  95      34.176  -2.181   6.851  1.00 28.07           C  
ANISOU  758  CB  CYS A  95     3141   3821   3703   -565   -189    189       C  
ATOM    759  SG  CYS A  95      33.656  -2.233   5.162  1.00 31.24           S  
ANISOU  759  SG  CYS A  95     3529   4205   4135   -462   -118    150       S  
ATOM    760  N   THR A  96      36.209   0.190   5.295  1.00 27.89           N  
ANISOU  760  N   THR A  96     3168   3773   3654   -644   -134    265       N  
ATOM    761  CA  THR A  96      36.225   1.467   4.547  1.00 28.70           C  
ANISOU  761  CA  THR A  96     3217   3962   3724   -692    -70    279       C  
ATOM    762  C   THR A  96      35.904   1.278   3.066  1.00 28.02           C  
ANISOU  762  C   THR A  96     3093   3904   3646   -718    -33    242       C  
ATOM    763  O   THR A  96      36.096   0.189   2.524  1.00 27.76           O  
ANISOU  763  O   THR A  96     2984   3964   3597   -638     39    292       O  
ATOM    764  CB  THR A  96      37.607   2.212   4.660  1.00 28.63           C  
ANISOU  764  CB  THR A  96     3206   3961   3708   -661   -103    292       C  
ATOM    765  OG1 THR A  96      38.638   1.442   4.034  1.00 28.81           O  
ANISOU  765  OG1 THR A  96     3091   4183   3672   -605   -142    590       O  
ATOM    766  CG2 THR A  96      38.060   2.344   6.104  1.00 30.42           C  
ANISOU  766  CG2 THR A  96     3373   4222   3962   -720   -180    317       C  
ATOM    767  N   LEU A  97      35.406   2.326   2.426  1.00 28.06           N  
ANISOU  767  N   LEU A  97     3211   3765   3682   -743     45    212       N  
ATOM    768  CA  LEU A  97      35.309   2.370   0.957  1.00 29.05           C  
ANISOU  768  CA  LEU A  97     3358   3934   3742   -663    120    187       C  
ATOM    769  C   LEU A  97      36.528   3.047   0.337  1.00 30.86           C  
ANISOU  769  C   LEU A  97     3534   4244   3946   -650    175    231       C  
ATOM    770  O   LEU A  97      37.026   4.033   0.854  1.00 30.91           O  
ANISOU  770  O   LEU A  97     3578   4163   4003   -725    161    165       O  
ATOM    771  CB  LEU A  97      34.103   3.172   0.531  1.00 28.79           C  
ANISOU  771  CB  LEU A  97     3387   3830   3722   -639    109    116       C  
ATOM    772  CG  LEU A  97      32.741   2.551   0.645  1.00 26.37           C  
ANISOU  772  CG  LEU A  97     3224   3407   3386   -521    192     12       C  
ATOM    773  CD1 LEU A  97      31.746   3.661   0.426  1.00 26.79           C  
ANISOU  773  CD1 LEU A  97     3557   3271   3347   -389    110     11       C  
ATOM    774  CD2 LEU A  97      32.617   1.524  -0.430  1.00 26.39           C  
ANISOU  774  CD2 LEU A  97     3307   3446   3272   -317    241    -86       C  
ATOM    775  N   ASN A  98      37.006   2.518  -0.781  1.00 32.55           N  
ANISOU  775  N   ASN A  98     3676   4632   4056   -641    265    292       N  
ATOM    776  CA  ASN A  98      38.244   3.002  -1.355  1.00 34.65           C  
ANISOU  776  CA  ASN A  98     3840   4996   4328   -664    381    394       C  
ATOM    777  C   ASN A  98      38.109   3.116  -2.858  1.00 35.31           C  
ANISOU  777  C   ASN A  98     3961   5135   4318   -657    444    409       C  
ATOM    778  O   ASN A  98      37.627   2.211  -3.509  1.00 35.05           O  
ANISOU  778  O   ASN A  98     3955   5090   4272   -658    474    471       O  
ATOM    779  CB  ASN A  98      39.413   2.070  -0.998  1.00 35.01           C  
ANISOU  779  CB  ASN A  98     3833   5086   4381   -623    355    377       C  
ATOM    780  CG  ASN A  98      39.648   1.979   0.496  1.00 37.34           C  
ANISOU  780  CG  ASN A  98     3942   5403   4841   -611    232    460       C  
ATOM    781  OD1 ASN A  98      38.925   1.284   1.226  1.00 38.54           O  
ANISOU  781  OD1 ASN A  98     3917   5636   5089   -473    228    468       O  
ATOM    782  ND2 ASN A  98      40.651   2.691   0.967  1.00 40.05           N  
ANISOU  782  ND2 ASN A  98     4106   5708   5402   -644    107    440       N  
ATOM    783  N   PHE A  99      38.509   4.258  -3.397  1.00 36.75           N  
ANISOU  783  N   PHE A  99     4135   5376   4451   -708    542    427       N  
ATOM    784  CA  PHE A  99      38.601   4.417  -4.846  1.00 38.11           C  
ANISOU  784  CA  PHE A  99     4397   5535   4545   -755    609    454       C  
ATOM    785  C   PHE A  99      39.613   5.491  -5.186  1.00 39.64           C  
ANISOU  785  C   PHE A  99     4536   5777   4748   -782    620    476       C  
ATOM    786  O   PHE A  99      40.117   6.178  -4.294  1.00 40.42           O  
ANISOU  786  O   PHE A  99     4579   5941   4835   -805    588    482       O  
ATOM    787  CB  PHE A  99      37.226   4.634  -5.517  1.00 37.20           C  
ANISOU  787  CB  PHE A  99     4415   5311   4406   -718    608    426       C  
ATOM    788  CG  PHE A  99      36.539   5.920  -5.143  1.00 37.21           C  
ANISOU  788  CG  PHE A  99     4529   5268   4340   -699    532    400       C  
ATOM    789  CD1 PHE A  99      36.657   7.045  -5.954  1.00 36.97           C  
ANISOU  789  CD1 PHE A  99     4699   5021   4325   -661    397    326       C  
ATOM    790  CD2 PHE A  99      35.741   6.002  -3.996  1.00 35.75           C  
ANISOU  790  CD2 PHE A  99     4567   4853   4163   -677    389    221       C  
ATOM    791  CE1 PHE A  99      36.007   8.236  -5.610  1.00 36.65           C  
ANISOU  791  CE1 PHE A  99     4769   4977   4178   -706    338    271       C  
ATOM    792  CE2 PHE A  99      35.082   7.180  -3.658  1.00 34.90           C  
ANISOU  792  CE2 PHE A  99     4510   4661   4086   -656    378    292       C  
ATOM    793  CZ  PHE A  99      35.218   8.296  -4.457  1.00 35.47           C  
ANISOU  793  CZ  PHE A  99     4567   4835   4074   -767    367    357       C  
ATOM    794  OXT PHE A  99      39.959   5.701  -6.345  1.00 40.92           O  
ANISOU  794  OXT PHE A  99     4700   5941   4903   -784    684    446       O  
TER     795      PHE A  99                                                      
ATOM    796  N   PRO B   1      39.913   8.589  -2.684  1.00 39.34           N  
ANISOU  796  N   PRO B   1     3878   5363   5705   -599   -564   1109       N  
ATOM    797  CA  PRO B   1      39.697   8.722  -1.247  1.00 39.17           C  
ANISOU  797  CA  PRO B   1     3872   5338   5672   -627   -635   1127       C  
ATOM    798  C   PRO B   1      39.481   7.384  -0.548  1.00 39.32           C  
ANISOU  798  C   PRO B   1     3925   5314   5699   -697   -726   1108       C  
ATOM    799  O   PRO B   1      39.003   6.433  -1.159  1.00 39.99           O  
ANISOU  799  O   PRO B   1     4075   5315   5804   -633   -589   1095       O  
ATOM    800  CB  PRO B   1      38.403   9.565  -1.160  1.00 39.09           C  
ANISOU  800  CB  PRO B   1     3820   5392   5638   -634   -585   1115       C  
ATOM    801  CG  PRO B   1      37.927   9.763  -2.600  1.00 38.98           C  
ANISOU  801  CG  PRO B   1     3801   5398   5610   -588   -547   1027       C  
ATOM    802  CD  PRO B   1      39.164   9.610  -3.448  1.00 39.24           C  
ANISOU  802  CD  PRO B   1     3813   5428   5667   -536   -550   1067       C  
ATOM    803  N   GLN B   2      39.861   7.328   0.719  1.00 39.76           N  
ANISOU  803  N   GLN B   2     4124   5283   5698   -755   -815   1052       N  
ATOM    804  CA  GLN B   2      39.452   6.284   1.620  1.00 40.10           C  
ANISOU  804  CA  GLN B   2     4346   5213   5677   -735   -942    996       C  
ATOM    805  C   GLN B   2      38.358   6.891   2.501  1.00 38.65           C  
ANISOU  805  C   GLN B   2     4406   4926   5352   -805   -955    830       C  
ATOM    806  O   GLN B   2      38.587   7.904   3.135  1.00 39.77           O  
ANISOU  806  O   GLN B   2     4610   5019   5479   -787   -908    742       O  
ATOM    807  CB  GLN B   2      40.631   5.856   2.484  1.00 40.92           C  
ANISOU  807  CB  GLN B   2     4397   5370   5780   -713  -1013    966       C  
ATOM    808  CG  GLN B   2      40.265   4.738   3.463  1.00 43.46           C  
ANISOU  808  CG  GLN B   2     4672   5736   6103   -644   -964   1107       C  
ATOM    809  CD  GLN B   2      41.478   4.033   4.054  1.00 46.73           C  
ANISOU  809  CD  GLN B   2     4994   6172   6589   -563  -1106   1116       C  
ATOM    810  OE1 GLN B   2      42.278   4.655   4.755  1.00 51.49           O  
ANISOU  810  OE1 GLN B   2     5639   6777   7147   -637  -1346    933       O  
ATOM    811  NE2 GLN B   2      41.622   2.733   3.767  1.00 48.46           N  
ANISOU  811  NE2 GLN B   2     5283   6289   6841   -485   -982   1129       N  
ATOM    812  N   ILE B   3      37.180   6.276   2.527  1.00 36.13           N  
ANISOU  812  N   ILE B   3     4418   4481   4827   -809   -842    700       N  
ATOM    813  CA  ILE B   3      35.994   6.813   3.193  1.00 33.19           C  
ANISOU  813  CA  ILE B   3     4419   3987   4204   -765   -814    551       C  
ATOM    814  C   ILE B   3      35.609   5.865   4.353  1.00 33.82           C  
ANISOU  814  C   ILE B   3     4765   3971   4111   -832   -844    481       C  
ATOM    815  O   ILE B   3      35.192   4.720   4.116  1.00 32.92           O  
ANISOU  815  O   ILE B   3     4696   3825   3984   -780   -769    424       O  
ATOM    816  CB  ILE B   3      34.857   6.951   2.136  1.00 32.34           C  
ANISOU  816  CB  ILE B   3     4258   3863   4166   -719   -745    539       C  
ATOM    817  CG1 ILE B   3      35.300   7.930   1.046  1.00 31.55           C  
ANISOU  817  CG1 ILE B   3     4117   3935   3935   -549   -642    416       C  
ATOM    818  CG2 ILE B   3      33.558   7.391   2.746  1.00 30.84           C  
ANISOU  818  CG2 ILE B   3     4238   3692   3785   -774   -621    426       C  
ATOM    819  CD1 ILE B   3      34.271   8.253  -0.009  1.00 30.85           C  
ANISOU  819  CD1 ILE B   3     3815   3931   3977   -490   -560    368       C  
ATOM    820  N   THR B   4      35.778   6.331   5.602  1.00 34.09           N  
ANISOU  820  N   THR B   4     5077   3872   4001   -879   -973    447       N  
ATOM    821  CA  THR B   4      35.226   5.625   6.783  1.00 34.71           C  
ANISOU  821  CA  THR B   4     5458   3877   3853   -877  -1008    334       C  
ATOM    822  C   THR B   4      33.695   5.748   6.842  1.00 33.44           C  
ANISOU  822  C   THR B   4     5522   3613   3568   -814   -904    248       C  
ATOM    823  O   THR B   4      33.079   6.499   6.067  1.00 33.18           O  
ANISOU  823  O   THR B   4     5485   3533   3589   -714   -873    242       O  
ATOM    824  CB  THR B   4      35.839   6.135   8.091  1.00 35.51           C  
ANISOU  824  CB  THR B   4     5541   3982   3969   -883  -1019    347       C  
ATOM    825  OG1 THR B   4      35.637   7.542   8.177  1.00 36.44           O  
ANISOU  825  OG1 THR B   4     5833   3887   4125   -971   -943    311       O  
ATOM    826  CG2 THR B   4      37.351   5.942   8.095  1.00 37.59           C  
ANISOU  826  CG2 THR B   4     5676   4324   4282   -888  -1155    313       C  
ATOM    827  N   LEU B   5      33.072   5.000   7.742  1.00 31.94           N  
ANISOU  827  N   LEU B   5     5642   3315   3176   -788   -786    129       N  
ATOM    828  CA  LEU B   5      31.625   4.906   7.681  1.00 30.94           C  
ANISOU  828  CA  LEU B   5     5727   3117   2909   -713   -743     91       C  
ATOM    829  C   LEU B   5      30.905   5.423   8.930  1.00 32.29           C  
ANISOU  829  C   LEU B   5     6156   3132   2980   -724   -692     45       C  
ATOM    830  O   LEU B   5      29.748   5.043   9.180  1.00 31.13           O  
ANISOU  830  O   LEU B   5     6035   3017   2773   -741   -710    -52       O  
ATOM    831  CB  LEU B   5      31.213   3.472   7.288  1.00 29.53           C  
ANISOU  831  CB  LEU B   5     5400   3034   2783   -610   -706    108       C  
ATOM    832  CG  LEU B   5      31.676   3.034   5.875  1.00 27.06           C  
ANISOU  832  CG  LEU B   5     4770   2745   2764   -463   -577     97       C  
ATOM    833  CD1 LEU B   5      31.681   1.490   5.691  1.00 24.46           C  
ANISOU  833  CD1 LEU B   5     4232   2498   2562   -255   -491    192       C  
ATOM    834  CD2 LEU B   5      30.814   3.700   4.788  1.00 22.57           C  
ANISOU  834  CD2 LEU B   5     4111   2342   2122   -334   -363     26       C  
ATOM    835  N   TRP B   6      31.602   6.275   9.712  1.00 33.91           N  
ANISOU  835  N   TRP B   6     6699   3146   3036   -805   -700    -20       N  
ATOM    836  CA  TRP B   6      31.016   6.926  10.905  1.00 36.17           C  
ANISOU  836  CA  TRP B   6     7258   3322   3162   -839   -677    -52       C  
ATOM    837  C   TRP B   6      29.834   7.801  10.509  1.00 35.43           C  
ANISOU  837  C   TRP B   6     7199   3175   3086   -817   -473   -125       C  
ATOM    838  O   TRP B   6      28.862   7.911  11.239  1.00 36.17           O  
ANISOU  838  O   TRP B   6     7352   3292   3096   -789   -448   -103       O  
ATOM    839  CB  TRP B   6      32.077   7.690  11.722  1.00 39.59           C  
ANISOU  839  CB  TRP B   6     7780   3701   3561   -981   -838   -131       C  
ATOM    840  CG  TRP B   6      33.166   6.753  12.124  1.00 41.69           C  
ANISOU  840  CG  TRP B   6     8098   3959   3781  -1021  -1153    -98       C  
ATOM    841  CD1 TRP B   6      34.335   6.533  11.470  1.00 43.52           C  
ANISOU  841  CD1 TRP B   6     8246   4262   4026  -1016  -1220    -64       C  
ATOM    842  CD2 TRP B   6      33.142   5.844  13.218  1.00 43.25           C  
ANISOU  842  CD2 TRP B   6     8431   4120   3880  -1103  -1283    -77       C  
ATOM    843  NE1 TRP B   6      35.063   5.556  12.106  1.00 44.45           N  
ANISOU  843  NE1 TRP B   6     8323   4426   4138  -1085  -1307      1       N  
ATOM    844  CE2 TRP B   6      34.354   5.114  13.187  1.00 44.04           C  
ANISOU  844  CE2 TRP B   6     8411   4381   3938  -1097  -1383    -77       C  
ATOM    845  CE3 TRP B   6      32.231   5.587  14.251  1.00 45.10           C  
ANISOU  845  CE3 TRP B   6     8763   4389   3984   -985  -1198    -31       C  
ATOM    846  CZ2 TRP B   6      34.673   4.143  14.126  1.00 44.74           C  
ANISOU  846  CZ2 TRP B   6     8521   4287   4189   -990  -1341     83       C  
ATOM    847  CZ3 TRP B   6      32.550   4.612  15.193  1.00 45.14           C  
ANISOU  847  CZ3 TRP B   6     8747   4366   4035   -968  -1184     60       C  
ATOM    848  CH2 TRP B   6      33.766   3.907  15.125  1.00 44.77           C  
ANISOU  848  CH2 TRP B   6     8636   4315   4056   -978  -1242     93       C  
ATOM    849  N  ALYS B   7      29.915   8.430   9.344  0.50 34.28           N  
ANISOU  849  N  ALYS B   7     6954   3019   3051   -734   -354   -112       N  
ATOM    850  N  BLYS B   7      29.922   8.365   9.309  0.50 34.44           N  
ANISOU  850  N  BLYS B   7     6976   3036   3071   -751   -378   -105       N  
ATOM    851  CA ALYS B   7      28.728   9.039   8.773  0.50 33.08           C  
ANISOU  851  CA ALYS B   7     6645   2923   2998   -683   -170   -147       C  
ATOM    852  CA BLYS B   7      28.878   9.189   8.727  0.50 33.50           C  
ANISOU  852  CA BLYS B   7     6692   2975   3060   -699   -209   -141       C  
ATOM    853  C  ALYS B   7      28.363   8.405   7.453  0.50 31.38           C  
ANISOU  853  C  ALYS B   7     6242   2778   2902   -642   -111   -114       C  
ATOM    854  C  BLYS B   7      28.432   8.534   7.405  0.50 31.54           C  
ANISOU  854  C  BLYS B   7     6255   2800   2928   -658   -140   -112       C  
ATOM    855  O  ALYS B   7      29.104   7.577   6.904  0.50 30.95           O  
ANISOU  855  O  ALYS B   7     6096   2762   2900   -637    -98    -92       O  
ATOM    856  O  BLYS B   7      29.190   7.741   6.828  0.50 31.09           O  
ANISOU  856  O  BLYS B   7     6117   2770   2925   -653   -128    -90       O  
ATOM    857  CB ALYS B   7      28.878  10.551   8.588  0.50 33.92           C  
ANISOU  857  CB ALYS B   7     6756   2959   3171   -568   -133   -157       C  
ATOM    858  CB BLYS B   7      29.448  10.607   8.515  0.50 34.12           C  
ANISOU  858  CB BLYS B   7     6746   3007   3208   -630   -217   -116       C  
ATOM    859  CG ALYS B   7      27.635  11.229   7.921  0.50 34.80           C  
ANISOU  859  CG ALYS B   7     6759   3247   3214   -520    -83   -210       C  
ATOM    860  CG BLYS B   7      28.587  11.783   9.069  0.50 37.28           C  
ANISOU  860  CG BLYS B   7     7123   3428   3611   -556    -85   -182       C  
ATOM    861  CD ALYS B   7      26.268  10.842   8.564  0.50 35.37           C  
ANISOU  861  CD ALYS B   7     6839   3244   3354   -376    143   -224       C  
ATOM    862  CD BLYS B   7      27.298  11.332   9.797  0.50 38.45           C  
ANISOU  862  CD BLYS B   7     7404   3587   3616   -411    153   -124       C  
ATOM    863  CE ALYS B   7      25.081  11.452   7.825  0.50 35.27           C  
ANISOU  863  CE ALYS B   7     6791   3218   3389   -372    171   -232       C  
ATOM    864  CE BLYS B   7      26.033  11.911   9.102  0.50 38.35           C  
ANISOU  864  CE BLYS B   7     7324   3600   3646   -342    226   -175       C  
ATOM    865  NZ ALYS B   7      25.136  12.945   7.737  0.50 37.36           N  
ANISOU  865  NZ ALYS B   7     7088   3225   3880   -172    268   -201       N  
ATOM    866  NZ BLYS B   7      25.002  10.848   8.787  0.50 36.89           N  
ANISOU  866  NZ BLYS B   7     7057   3496   3462   -281    276   -226       N  
ATOM    867  N   ARG B   8      27.207   8.824   6.948  1.00 30.23           N  
ANISOU  867  N   ARG B   8     6003   2659   2822   -633    -37   -115       N  
ATOM    868  CA  ARG B   8      26.744   8.401   5.621  1.00 28.01           C  
ANISOU  868  CA  ARG B   8     5325   2595   2720   -477    120   -121       C  
ATOM    869  C   ARG B   8      27.806   8.805   4.607  1.00 25.07           C  
ANISOU  869  C   ARG B   8     4772   2267   2484   -474     31    -93       C  
ATOM    870  O   ARG B   8      28.312   9.930   4.668  1.00 24.06           O  
ANISOU  870  O   ARG B   8     4631   2166   2343   -392    -27   -136       O  
ATOM    871  CB  ARG B   8      25.399   9.023   5.279  1.00 27.49           C  
ANISOU  871  CB  ARG B   8     5214   2539   2690   -498    124   -130       C  
ATOM    872  CG  ARG B   8      24.247   8.334   5.964  1.00 29.24           C  
ANISOU  872  CG  ARG B   8     5207   2851   3051   -304    392   -149       C  
ATOM    873  CD  ARG B   8      22.860   8.892   5.625  1.00 30.08           C  
ANISOU  873  CD  ARG B   8     5298   3020   3112   -206    405    -62       C  
ATOM    874  NE  ARG B   8      21.864   8.349   6.579  1.00 34.43           N  
ANISOU  874  NE  ARG B   8     5757   3376   3945     72    858     -3       N  
ATOM    875  CZ  ARG B   8      20.613   8.811   6.749  1.00 36.20           C  
ANISOU  875  CZ  ARG B   8     5780   3754   4218     27    956    179       C  
ATOM    876  NH1 ARG B   8      20.164   9.845   6.021  1.00 39.35           N  
ANISOU  876  NH1 ARG B   8     6122   4011   4818    113    813    154       N  
ATOM    877  NH2 ARG B   8      19.803   8.259   7.646  1.00 35.61           N  
ANISOU  877  NH2 ARG B   8     5983   3525   4022     77   1074    214       N  
ATOM    878  N   PRO B   9      28.212   7.857   3.750  1.00 23.17           N  
ANISOU  878  N   PRO B   9     4267   2103   2432   -472     24    -81       N  
ATOM    879  CA  PRO B   9      29.171   8.146   2.693  1.00 21.92           C  
ANISOU  879  CA  PRO B   9     3965   1980   2380   -471     27    -49       C  
ATOM    880  C   PRO B   9      28.545   8.958   1.521  1.00 21.70           C  
ANISOU  880  C   PRO B   9     3807   2035   2403   -434      4    -36       C  
ATOM    881  O   PRO B   9      28.264   8.405   0.450  1.00 20.89           O  
ANISOU  881  O   PRO B   9     3763   1803   2368   -414    -40     66       O  
ATOM    882  CB  PRO B   9      29.641   6.753   2.262  1.00 21.65           C  
ANISOU  882  CB  PRO B   9     3795   2018   2412   -396     -1    -53       C  
ATOM    883  CG  PRO B   9      28.397   5.871   2.475  1.00 20.48           C  
ANISOU  883  CG  PRO B   9     3758   1741   2280   -437     83     29       C  
ATOM    884  CD  PRO B   9      27.808   6.421   3.771  1.00 22.45           C  
ANISOU  884  CD  PRO B   9     4165   1945   2418   -443     51    -92       C  
ATOM    885  N   LEU B  10      28.332  10.260   1.741  1.00 21.79           N  
ANISOU  885  N   LEU B  10     3772   2011   2495   -506     16     44       N  
ATOM    886  CA  LEU B  10      27.818  11.164   0.696  1.00 22.55           C  
ANISOU  886  CA  LEU B  10     3748   2195   2625   -456     -5    -25       C  
ATOM    887  C   LEU B  10      28.949  11.810  -0.093  1.00 22.31           C  
ANISOU  887  C   LEU B  10     3639   2182   2654   -502    -72     41       C  
ATOM    888  O   LEU B  10      29.935  12.252   0.486  1.00 22.49           O  
ANISOU  888  O   LEU B  10     3749   2071   2725   -661   -126     34       O  
ATOM    889  CB  LEU B  10      26.975  12.286   1.317  1.00 23.36           C  
ANISOU  889  CB  LEU B  10     3914   2256   2703   -393     61    -74       C  
ATOM    890  CG  LEU B  10      25.673  11.865   2.021  1.00 25.54           C  
ANISOU  890  CG  LEU B  10     4089   2657   2958   -332    180   -225       C  
ATOM    891  CD1 LEU B  10      25.227  12.974   2.971  1.00 28.07           C  
ANISOU  891  CD1 LEU B  10     4499   2781   3386   -144    234   -230       C  
ATOM    892  CD2 LEU B  10      24.570  11.525   1.014  1.00 25.15           C  
ANISOU  892  CD2 LEU B  10     3909   2647   2997   -254    151   -139       C  
ATOM    893  N   VAL B  11      28.829  11.828  -1.414  1.00 21.59           N  
ANISOU  893  N   VAL B  11     3401   2165   2635   -503    -88     55       N  
ATOM    894  CA  VAL B  11      29.776  12.505  -2.243  1.00 21.44           C  
ANISOU  894  CA  VAL B  11     3229   2180   2735   -475    -29    128       C  
ATOM    895  C   VAL B  11      29.043  13.424  -3.227  1.00 21.24           C  
ANISOU  895  C   VAL B  11     3168   2165   2735   -488    -40    143       C  
ATOM    896  O   VAL B  11      27.829  13.301  -3.434  1.00 19.81           O  
ANISOU  896  O   VAL B  11     2963   1918   2644   -549     86    175       O  
ATOM    897  CB  VAL B  11      30.711  11.531  -3.007  1.00 21.72           C  
ANISOU  897  CB  VAL B  11     3274   2242   2735   -440    -88    126       C  
ATOM    898  CG1 VAL B  11      31.651  10.779  -2.016  1.00 24.16           C  
ANISOU  898  CG1 VAL B  11     3382   2531   3266   -241    -53    187       C  
ATOM    899  CG2 VAL B  11      29.922  10.598  -3.849  1.00 21.44           C  
ANISOU  899  CG2 VAL B  11     3084   2269   2790   -469     76    166       C  
ATOM    900  N   THR B  12      29.802  14.332  -3.823  1.00 21.06           N  
ANISOU  900  N   THR B  12     3109   2104   2786   -550     17    208       N  
ATOM    901  CA  THR B  12      29.300  15.236  -4.858  1.00 21.76           C  
ANISOU  901  CA  THR B  12     3160   2173   2935   -521    -13    200       C  
ATOM    902  C   THR B  12      29.281  14.555  -6.215  1.00 21.14           C  
ANISOU  902  C   THR B  12     2979   2149   2902   -465     32    216       C  
ATOM    903  O   THR B  12      30.282  13.919  -6.647  1.00 22.00           O  
ANISOU  903  O   THR B  12     2934   2263   3162   -567     59    134       O  
ATOM    904  CB  THR B  12      30.206  16.490  -4.943  1.00 22.81           C  
ANISOU  904  CB  THR B  12     3398   2272   2994   -501    -46    214       C  
ATOM    905  OG1 THR B  12      30.214  17.140  -3.668  1.00 23.50           O  
ANISOU  905  OG1 THR B  12     3467   2232   3229   -662   -256    138       O  
ATOM    906  CG2 THR B  12      29.555  17.547  -5.871  1.00 24.11           C  
ANISOU  906  CG2 THR B  12     3592   2426   3141   -476      6    219       C  
ATOM    907  N   ILE B  13      28.147  14.673  -6.896  1.00 20.34           N  
ANISOU  907  N   ILE B  13     2808   2069   2849   -373    139    249       N  
ATOM    908  CA  ILE B  13      28.006  14.179  -8.268  1.00 19.40           C  
ANISOU  908  CA  ILE B  13     2730   2001   2640   -226    162    215       C  
ATOM    909  C   ILE B  13      27.599  15.360  -9.142  1.00 20.55           C  
ANISOU  909  C   ILE B  13     2879   2203   2724   -183    151    190       C  
ATOM    910  O   ILE B  13      26.952  16.330  -8.671  1.00 21.21           O  
ANISOU  910  O   ILE B  13     3062   2211   2785   -162    109    156       O  
ATOM    911  CB  ILE B  13      26.997  12.978  -8.363  1.00 19.40           C  
ANISOU  911  CB  ILE B  13     2704   2052   2612   -170    160    186       C  
ATOM    912  CG1 ILE B  13      25.544  13.477  -8.227  1.00 18.50           C  
ANISOU  912  CG1 ILE B  13     2568   1885   2573   -173     45    134       C  
ATOM    913  CG2 ILE B  13      27.406  11.895  -7.327  1.00 18.41           C  
ANISOU  913  CG2 ILE B  13     2566   1799   2630   -196    267    226       C  
ATOM    914  CD1 ILE B  13      24.394  12.411  -8.209  1.00 19.14           C  
ANISOU  914  CD1 ILE B  13     2638   1945   2689   -157     72    217       C  
ATOM    915  N   LYS B  14      28.023  15.306 -10.394  1.00 20.68           N  
ANISOU  915  N   LYS B  14     3004   2199   2652   -155    159    211       N  
ATOM    916  CA  LYS B  14      27.552  16.232 -11.382  1.00 21.27           C  
ANISOU  916  CA  LYS B  14     3112   2245   2725    -80    104    259       C  
ATOM    917  C   LYS B  14      26.894  15.395 -12.450  1.00 21.66           C  
ANISOU  917  C   LYS B  14     3186   2290   2753    -29    113    289       C  
ATOM    918  O   LYS B  14      27.488  14.384 -12.934  1.00 21.20           O  
ANISOU  918  O   LYS B  14     3118   2338   2596     81     20    298       O  
ATOM    919  CB  LYS B  14      28.704  17.062 -11.947  1.00 21.51           C  
ANISOU  919  CB  LYS B  14     3156   2342   2674   -102    180    271       C  
ATOM    920  CG  LYS B  14      28.240  18.036 -13.050  1.00 25.09           C  
ANISOU  920  CG  LYS B  14     3593   2636   3304   -140    137    214       C  
ATOM    921  CD  LYS B  14      28.933  19.399 -13.012  1.00 29.87           C  
ANISOU  921  CD  LYS B  14     4038   3259   4051   -299    311    326       C  
ATOM    922  CE  LYS B  14      30.249  19.380 -13.753  1.00 33.16           C  
ANISOU  922  CE  LYS B  14     4374   3880   4342   -109    272    392       C  
ATOM    923  NZ  LYS B  14      30.979  18.073 -13.507  1.00 34.74           N  
ANISOU  923  NZ  LYS B  14     4652   3790   4757   -118    164    606       N  
ATOM    924  N   ILE B  15      25.662  15.799 -12.791  1.00 21.96           N  
ANISOU  924  N   ILE B  15     3217   2290   2835     53     71    273       N  
ATOM    925  CA  ILE B  15      24.822  15.102 -13.731  1.00 23.44           C  
ANISOU  925  CA  ILE B  15     3439   2471   2994    109    -21    268       C  
ATOM    926  C   ILE B  15      23.846  16.098 -14.386  1.00 25.26           C  
ANISOU  926  C   ILE B  15     3719   2752   3126    180    -35    236       C  
ATOM    927  O   ILE B  15      23.127  16.856 -13.709  1.00 26.05           O  
ANISOU  927  O   ILE B  15     3767   2861   3270    233   -115    188       O  
ATOM    928  CB  ILE B  15      24.066  13.879 -13.074  1.00 23.40           C  
ANISOU  928  CB  ILE B  15     3386   2544   2959     69     -6    151       C  
ATOM    929  CG1 ILE B  15      23.184  13.222 -14.157  1.00 25.35           C  
ANISOU  929  CG1 ILE B  15     3570   2702   3359    -33    -50    162       C  
ATOM    930  CG2 ILE B  15      23.256  14.303 -11.817  1.00 21.92           C  
ANISOU  930  CG2 ILE B  15     3151   2319   2856     70     -5    231       C  
ATOM    931  CD1 ILE B  15      22.804  11.767 -13.945  1.00 23.97           C  
ANISOU  931  CD1 ILE B  15     3473   2447   3187     88    -86    251       C  
ATOM    932  N   GLY B  16      23.870  16.123 -15.715  1.00 26.65           N  
ANISOU  932  N   GLY B  16     3972   2914   3238    201   -125    303       N  
ATOM    933  CA  GLY B  16      22.983  16.969 -16.491  1.00 26.96           C  
ANISOU  933  CA  GLY B  16     4106   2765   3371    213   -147    350       C  
ATOM    934  C   GLY B  16      23.220  18.437 -16.262  1.00 27.38           C  
ANISOU  934  C   GLY B  16     4206   2802   3393    210   -116    306       C  
ATOM    935  O   GLY B  16      22.260  19.207 -16.255  1.00 27.79           O  
ANISOU  935  O   GLY B  16     4249   2922   3384    309   -119    305       O  
ATOM    936  N   GLY B  17      24.486  18.825 -16.076  1.00 27.07           N  
ANISOU  936  N   GLY B  17     4149   2716   3420    154    -38    326       N  
ATOM    937  CA  GLY B  17      24.816  20.186 -15.695  1.00 26.73           C  
ANISOU  937  CA  GLY B  17     4122   2615   3417    103    -15    358       C  
ATOM    938  C   GLY B  17      24.513  20.579 -14.244  1.00 26.03           C  
ANISOU  938  C   GLY B  17     3998   2480   3410     94     66    356       C  
ATOM    939  O   GLY B  17      24.727  21.737 -13.869  1.00 26.64           O  
ANISOU  939  O   GLY B  17     4096   2606   3420     39     51    346       O  
ATOM    940  N   GLN B  18      24.038  19.638 -13.424  1.00 24.83           N  
ANISOU  940  N   GLN B  18     3852   2284   3295    132     26    370       N  
ATOM    941  CA  GLN B  18      23.620  19.943 -12.035  1.00 24.11           C  
ANISOU  941  CA  GLN B  18     3729   2149   3281     94     46    325       C  
ATOM    942  C   GLN B  18      24.449  19.215 -10.972  1.00 23.03           C  
ANISOU  942  C   GLN B  18     3562   2097   3088    -12     61    278       C  
ATOM    943  O   GLN B  18      24.885  18.060 -11.169  1.00 21.31           O  
ANISOU  943  O   GLN B  18     3283   2029   2783     66    -68    332       O  
ATOM    944  CB  GLN B  18      22.147  19.595 -11.819  1.00 24.30           C  
ANISOU  944  CB  GLN B  18     3732   2228   3272    151     21    282       C  
ATOM    945  CG  GLN B  18      21.186  20.261 -12.798  1.00 27.17           C  
ANISOU  945  CG  GLN B  18     3845   2673   3803    213     -1    243       C  
ATOM    946  CD  GLN B  18      19.840  19.603 -12.693  1.00 29.21           C  
ANISOU  946  CD  GLN B  18     3999   2976   4121    293      9    281       C  
ATOM    947  OE1 GLN B  18      19.219  19.669 -11.645  1.00 30.36           O  
ANISOU  947  OE1 GLN B  18     4038   3191   4304    469    143    365       O  
ATOM    948  NE2 GLN B  18      19.402  18.925 -13.769  1.00 30.65           N  
ANISOU  948  NE2 GLN B  18     4244   2932   4467    255    -89    284       N  
ATOM    949  N   LEU B  19      24.593  19.880  -9.836  1.00 22.13           N  
ANISOU  949  N   LEU B  19     3455   1872   3082    -77    112    166       N  
ATOM    950  CA  LEU B  19      25.391  19.394  -8.729  1.00 22.79           C  
ANISOU  950  CA  LEU B  19     3619   1951   3086   -149    192    161       C  
ATOM    951  C   LEU B  19      24.474  18.823  -7.709  1.00 22.07           C  
ANISOU  951  C   LEU B  19     3459   1885   3042   -142    160    125       C  
ATOM    952  O   LEU B  19      23.545  19.500  -7.292  1.00 21.09           O  
ANISOU  952  O   LEU B  19     3476   1559   2975    -62    220    228       O  
ATOM    953  CB  LEU B  19      26.216  20.562  -8.092  1.00 23.56           C  
ANISOU  953  CB  LEU B  19     3680   2110   3161   -220    155    125       C  
ATOM    954  CG  LEU B  19      27.325  21.174  -8.977  1.00 25.76           C  
ANISOU  954  CG  LEU B  19     3983   2284   3519   -321    116    248       C  
ATOM    955  CD1 LEU B  19      28.051  22.247  -8.200  1.00 26.22           C  
ANISOU  955  CD1 LEU B  19     4191   2257   3514   -466     85    265       C  
ATOM    956  CD2 LEU B  19      28.319  20.081  -9.514  1.00 26.79           C  
ANISOU  956  CD2 LEU B  19     3772   2750   3655   -519    254    141       C  
ATOM    957  N   LYS B  20      24.738  17.587  -7.303  1.00 21.00           N  
ANISOU  957  N   LYS B  20     3275   1725   2980    -70    161     79       N  
ATOM    958  CA  LYS B  20      23.959  16.910  -6.277  1.00 21.69           C  
ANISOU  958  CA  LYS B  20     3280   1991   2971    -29    218     67       C  
ATOM    959  C   LYS B  20      24.821  16.159  -5.299  1.00 20.87           C  
ANISOU  959  C   LYS B  20     3252   1914   2761    -85    264     53       C  
ATOM    960  O   LYS B  20      25.988  15.906  -5.552  1.00 20.58           O  
ANISOU  960  O   LYS B  20     3258   2000   2558    -95    203     95       O  
ATOM    961  CB  LYS B  20      22.958  15.926  -6.921  1.00 22.02           C  
ANISOU  961  CB  LYS B  20     3312   2004   3051    -15    224     72       C  
ATOM    962  CG  LYS B  20      21.793  16.687  -7.550  1.00 24.04           C  
ANISOU  962  CG  LYS B  20     3450   2358   3325     27     74    -20       C  
ATOM    963  CD  LYS B  20      20.807  15.833  -8.331  1.00 23.89           C  
ANISOU  963  CD  LYS B  20     3350   2339   3386      1    148    137       C  
ATOM    964  CE  LYS B  20      19.820  16.752  -9.094  1.00 25.96           C  
ANISOU  964  CE  LYS B  20     3516   2547   3801    332    159    134       C  
ATOM    965  NZ  LYS B  20      19.408  17.876  -8.163  1.00 31.15           N  
ANISOU  965  NZ  LYS B  20     4057   3280   4498    248    202    136       N  
ATOM    966  N   GLU B  21      24.239  15.785  -4.172  1.00 20.60           N  
ANISOU  966  N   GLU B  21     3215   1874   2736   -103    301    -14       N  
ATOM    967  CA  GLU B  21      24.904  14.867  -3.238  1.00 20.40           C  
ANISOU  967  CA  GLU B  21     3282   1784   2683   -210    326    -27       C  
ATOM    968  C   GLU B  21      24.273  13.511  -3.360  1.00 19.27           C  
ANISOU  968  C   GLU B  21     3098   1657   2567   -170    315    -44       C  
ATOM    969  O   GLU B  21      23.056  13.408  -3.494  1.00 19.28           O  
ANISOU  969  O   GLU B  21     3136   1494   2693   -231    265    -15       O  
ATOM    970  CB  GLU B  21      24.780  15.347  -1.807  1.00 21.23           C  
ANISOU  970  CB  GLU B  21     3429   1866   2769   -205    294    -75       C  
ATOM    971  CG  GLU B  21      25.509  16.659  -1.566  1.00 26.03           C  
ANISOU  971  CG  GLU B  21     4243   2581   3062   -358    220    -47       C  
ATOM    972  CD  GLU B  21      26.026  16.707  -0.160  1.00 32.91           C  
ANISOU  972  CD  GLU B  21     5141   3769   3594   -559    157    -65       C  
ATOM    973  OE1 GLU B  21      25.262  16.285   0.749  1.00 35.67           O  
ANISOU  973  OE1 GLU B  21     5597   3975   3981   -458    397      3       O  
ATOM    974  OE2 GLU B  21      27.192  17.098   0.042  1.00 36.17           O  
ANISOU  974  OE2 GLU B  21     5290   4130   4321   -766    107   -114       O  
ATOM    975  N   ALA B  22      25.104  12.478  -3.277  1.00 17.78           N  
ANISOU  975  N   ALA B  22     2759   1593   2400   -207    340    -46       N  
ATOM    976  CA  ALA B  22      24.622  11.112  -3.435  1.00 16.91           C  
ANISOU  976  CA  ALA B  22     2643   1537   2245   -139    299    -10       C  
ATOM    977  C   ALA B  22      25.350  10.166  -2.492  1.00 16.98           C  
ANISOU  977  C   ALA B  22     2599   1614   2236   -129    251    -53       C  
ATOM    978  O   ALA B  22      26.530  10.383  -2.156  1.00 16.76           O  
ANISOU  978  O   ALA B  22     2630   1609   2128   -179    230    -58       O  
ATOM    979  CB  ALA B  22      24.742  10.646  -4.888  1.00 15.08           C  
ANISOU  979  CB  ALA B  22     2293   1294   2143   -147    279     20       C  
ATOM    980  N   LEU B  23      24.649   9.110  -2.103  1.00 16.40           N  
ANISOU  980  N   LEU B  23     2522   1626   2083   -163    291     23       N  
ATOM    981  CA  LEU B  23      25.189   8.096  -1.231  1.00 17.61           C  
ANISOU  981  CA  LEU B  23     2683   1745   2263   -171    291     -2       C  
ATOM    982  C   LEU B  23      25.885   6.982  -2.015  1.00 17.03           C  
ANISOU  982  C   LEU B  23     2594   1700   2176   -180    205     31       C  
ATOM    983  O   LEU B  23      25.302   6.448  -2.993  1.00 18.15           O  
ANISOU  983  O   LEU B  23     2847   1741   2307    -24    173    100       O  
ATOM    984  CB  LEU B  23      24.014   7.547  -0.420  1.00 17.97           C  
ANISOU  984  CB  LEU B  23     2739   1801   2288   -166    286     31       C  
ATOM    985  CG  LEU B  23      24.115   6.516   0.698  1.00 19.96           C  
ANISOU  985  CG  LEU B  23     2976   2194   2412   -245    353     17       C  
ATOM    986  CD1 LEU B  23      24.648   7.212   1.905  1.00 20.00           C  
ANISOU  986  CD1 LEU B  23     3173   2276   2148   -272    148   -110       C  
ATOM    987  CD2 LEU B  23      22.687   5.994   0.957  1.00 20.28           C  
ANISOU  987  CD2 LEU B  23     2880   2051   2775   -240    361     92       C  
ATOM    988  N   LEU B  24      27.117   6.623  -1.615  1.00 16.23           N  
ANISOU  988  N   LEU B  24     2456   1640   2070   -246    182     56       N  
ATOM    989  CA  LEU B  24      27.806   5.480  -2.203  1.00 16.07           C  
ANISOU  989  CA  LEU B  24     2364   1693   2046   -223    158     28       C  
ATOM    990  C   LEU B  24      27.295   4.202  -1.532  1.00 16.38           C  
ANISOU  990  C   LEU B  24     2491   1687   2046   -168    101     -9       C  
ATOM    991  O   LEU B  24      27.480   3.978  -0.329  1.00 17.15           O  
ANISOU  991  O   LEU B  24     2766   1634   2116   -201    127     20       O  
ATOM    992  CB  LEU B  24      29.318   5.608  -2.032  1.00 16.76           C  
ANISOU  992  CB  LEU B  24     2461   1809   2096   -237    137     32       C  
ATOM    993  CG  LEU B  24      29.974   6.865  -2.662  1.00 17.56           C  
ANISOU  993  CG  LEU B  24     2389   1951   2331   -322     44    144       C  
ATOM    994  CD1 LEU B  24      31.406   6.836  -2.387  1.00 19.30           C  
ANISOU  994  CD1 LEU B  24     2258   2206   2868   -272     33    187       C  
ATOM    995  CD2 LEU B  24      29.770   6.951  -4.175  1.00 17.39           C  
ANISOU  995  CD2 LEU B  24     2385   1938   2283   -473    116     94       C  
ATOM    996  N   ASP B  25      26.633   3.359  -2.302  1.00 15.92           N  
ANISOU  996  N   ASP B  25     2397   1598   2053   -130     88    -20       N  
ATOM    997  CA  ASP B  25      25.768   2.385  -1.678  1.00 16.23           C  
ANISOU  997  CA  ASP B  25     2530   1625   2012    -96     61     56       C  
ATOM    998  C   ASP B  25      26.077   0.983  -2.197  1.00 16.27           C  
ANISOU  998  C   ASP B  25     2646   1584   1950   -121     34     41       C  
ATOM    999  O   ASP B  25      25.651   0.623  -3.298  1.00 15.14           O  
ANISOU  999  O   ASP B  25     2508   1229   2013    -60    -10    177       O  
ATOM   1000  CB  ASP B  25      24.314   2.799  -1.926  1.00 16.50           C  
ANISOU 1000  CB  ASP B  25     2513   1716   2037   -188    121     17       C  
ATOM   1001  CG  ASP B  25      23.330   1.901  -1.244  1.00 19.55           C  
ANISOU 1001  CG  ASP B  25     2780   2151   2498   -106     67     97       C  
ATOM   1002  OD1 ASP B  25      23.720   0.874  -0.632  1.00 18.98           O  
ANISOU 1002  OD1 ASP B  25     3024   1651   2535     49     33    -11       O  
ATOM   1003  OD2 ASP B  25      22.114   2.152  -1.270  1.00 22.66           O  
ANISOU 1003  OD2 ASP B  25     2968   2573   3067   -141      0     67       O  
ATOM   1004  N   THR B  26      26.847   0.200  -1.412  1.00 17.00           N  
ANISOU 1004  N   THR B  26     2789   1660   2007    -65     78      9       N  
ATOM   1005  CA  THR B  26      27.188  -1.162  -1.794  1.00 17.71           C  
ANISOU 1005  CA  THR B  26     2959   1650   2119    -81    -35     51       C  
ATOM   1006  C   THR B  26      26.006  -2.137  -1.782  1.00 18.52           C  
ANISOU 1006  C   THR B  26     3046   1812   2178   -113   -102      9       C  
ATOM   1007  O   THR B  26      26.112  -3.238  -2.350  1.00 19.26           O  
ANISOU 1007  O   THR B  26     3174   1769   2373   -192   -112    -36       O  
ATOM   1008  CB  THR B  26      28.343  -1.773  -0.896  1.00 17.53           C  
ANISOU 1008  CB  THR B  26     2965   1672   2022    -97    -77     36       C  
ATOM   1009  OG1 THR B  26      27.965  -1.689   0.477  1.00 17.08           O  
ANISOU 1009  OG1 THR B  26     3001   1431   2057    -70    -49     42       O  
ATOM   1010  CG2 THR B  26      29.635  -1.026  -0.985  1.00 16.94           C  
ANISOU 1010  CG2 THR B  26     2743   1714   1977     18      1     26       C  
ATOM   1011  N   GLY B  27      24.919  -1.783  -1.097  1.00 18.55           N  
ANISOU 1011  N   GLY B  27     3129   1756   2162   -110   -130     10       N  
ATOM   1012  CA  GLY B  27      23.701  -2.598  -1.108  1.00 19.42           C  
ANISOU 1012  CA  GLY B  27     3224   1842   2311   -221   -101     80       C  
ATOM   1013  C   GLY B  27      22.724  -2.299  -2.242  1.00 20.08           C  
ANISOU 1013  C   GLY B  27     3286   1928   2413   -314   -124    -29       C  
ATOM   1014  O   GLY B  27      21.643  -2.882  -2.295  1.00 20.65           O  
ANISOU 1014  O   GLY B  27     3368   1948   2528   -328    -43    -11       O  
ATOM   1015  N   ALA B  28      23.077  -1.381  -3.147  1.00 19.42           N  
ANISOU 1015  N   ALA B  28     3300   1784   2293   -292   -153    -51       N  
ATOM   1016  CA  ALA B  28      22.212  -1.098  -4.290  1.00 19.90           C  
ANISOU 1016  CA  ALA B  28     3338   1820   2403   -242   -195    -74       C  
ATOM   1017  C   ALA B  28      22.783  -1.726  -5.584  1.00 20.76           C  
ANISOU 1017  C   ALA B  28     3502   1859   2524   -269   -248    -92       C  
ATOM   1018  O   ALA B  28      23.940  -1.449  -5.967  1.00 19.28           O  
ANISOU 1018  O   ALA B  28     3281   1592   2452   -257   -235   -185       O  
ATOM   1019  CB  ALA B  28      22.033   0.417  -4.454  1.00 19.01           C  
ANISOU 1019  CB  ALA B  28     3129   1860   2230   -263   -138    -89       C  
ATOM   1020  N   ASP B  29      21.982  -2.568  -6.253  1.00 22.26           N  
ANISOU 1020  N   ASP B  29     3789   1970   2695   -306   -372    -55       N  
ATOM   1021  CA  ASP B  29      22.364  -3.098  -7.582  1.00 23.40           C  
ANISOU 1021  CA  ASP B  29     4047   2084   2759   -300   -416      0       C  
ATOM   1022  C   ASP B  29      22.508  -1.940  -8.558  1.00 23.79           C  
ANISOU 1022  C   ASP B  29     4010   2178   2851   -323   -408     -1       C  
ATOM   1023  O   ASP B  29      23.443  -1.927  -9.327  1.00 25.16           O  
ANISOU 1023  O   ASP B  29     4255   2411   2893   -291   -397     12       O  
ATOM   1024  CB  ASP B  29      21.327  -4.061  -8.164  1.00 23.50           C  
ANISOU 1024  CB  ASP B  29     4167   2032   2729   -294   -420     -1       C  
ATOM   1025  CG  ASP B  29      21.055  -5.275  -7.265  1.00 26.04           C  
ANISOU 1025  CG  ASP B  29     4527   2188   3178   -320   -465    -47       C  
ATOM   1026  OD1 ASP B  29      21.892  -5.646  -6.409  1.00 26.06           O  
ANISOU 1026  OD1 ASP B  29     4857   1989   3055   -292   -435    191       O  
ATOM   1027  OD2 ASP B  29      19.991  -5.896  -7.357  1.00 26.72           O  
ANISOU 1027  OD2 ASP B  29     4959   1802   3388   -548   -523    -56       O  
ATOM   1028  N   ASP B  30      21.565  -0.997  -8.516  1.00 23.13           N  
ANISOU 1028  N   ASP B  30     3874   2039   2874   -338   -461    -23       N  
ATOM   1029  CA  ASP B  30      21.434   0.079  -9.492  1.00 23.08           C  
ANISOU 1029  CA  ASP B  30     3774   2099   2895   -288   -486      6       C  
ATOM   1030  C   ASP B  30      21.613   1.464  -8.862  1.00 21.70           C  
ANISOU 1030  C   ASP B  30     3496   2006   2741   -254   -458     38       C  
ATOM   1031  O   ASP B  30      21.640   1.613  -7.655  1.00 20.76           O  
ANISOU 1031  O   ASP B  30     3536   1733   2616   -210   -375    142       O  
ATOM   1032  CB  ASP B  30      20.058   0.037 -10.161  1.00 24.13           C  
ANISOU 1032  CB  ASP B  30     3927   2188   3053   -283   -565    -14       C  
ATOM   1033  CG  ASP B  30      19.731  -1.325 -10.761  1.00 28.11           C  
ANISOU 1033  CG  ASP B  30     4469   2655   3556   -369   -599    -44       C  
ATOM   1034  OD1 ASP B  30      20.498  -1.830 -11.601  1.00 30.42           O  
ANISOU 1034  OD1 ASP B  30     5052   2977   3529   -349   -710   -275       O  
ATOM   1035  OD2 ASP B  30      18.730  -1.970 -10.436  1.00 32.35           O  
ANISOU 1035  OD2 ASP B  30     4875   3041   4373   -537   -684    -92       O  
ATOM   1036  N   THR B  31      21.706   2.468  -9.729  1.00 20.96           N  
ANISOU 1036  N   THR B  31     3262   2028   2672   -214   -448     13       N  
ATOM   1037  CA  THR B  31      21.832   3.851  -9.365  1.00 20.19           C  
ANISOU 1037  CA  THR B  31     3039   1935   2697   -231   -324     65       C  
ATOM   1038  C   THR B  31      20.495   4.556  -9.512  1.00 20.96           C  
ANISOU 1038  C   THR B  31     2974   2091   2898   -250   -293    127       C  
ATOM   1039  O   THR B  31      19.874   4.520 -10.569  1.00 21.38           O  
ANISOU 1039  O   THR B  31     3169   2105   2849   -215   -285    171       O  
ATOM   1040  CB  THR B  31      22.885   4.448 -10.263  1.00 20.42           C  
ANISOU 1040  CB  THR B  31     3036   2064   2657   -170   -271    -58       C  
ATOM   1041  OG1 THR B  31      24.156   3.946  -9.833  1.00 17.90           O  
ANISOU 1041  OG1 THR B  31     2908   1504   2389    -67   -282   -116       O  
ATOM   1042  CG2 THR B  31      22.970   6.026 -10.142  1.00 18.66           C  
ANISOU 1042  CG2 THR B  31     2852   1786   2449   -131    -73    159       C  
ATOM   1043  N   VAL B  32      20.025   5.155  -8.433  1.00 20.81           N  
ANISOU 1043  N   VAL B  32     2842   2009   3054   -283   -210    148       N  
ATOM   1044  CA  VAL B  32      18.678   5.693  -8.391  1.00 22.26           C  
ANISOU 1044  CA  VAL B  32     2710   2311   3436   -216   -149    216       C  
ATOM   1045  C   VAL B  32      18.747   7.114  -7.852  1.00 22.43           C  
ANISOU 1045  C   VAL B  32     2612   2385   3523   -182    -77    203       C  
ATOM   1046  O   VAL B  32      19.200   7.333  -6.712  1.00 23.08           O  
ANISOU 1046  O   VAL B  32     2670   2400   3698   -145      7    163       O  
ATOM   1047  CB  VAL B  32      17.702   4.929  -7.440  1.00 22.78           C  
ANISOU 1047  CB  VAL B  32     2734   2346   3573   -242   -145    145       C  
ATOM   1048  CG1 VAL B  32      16.269   5.328  -7.796  1.00 23.28           C  
ANISOU 1048  CG1 VAL B  32     2625   2587   3632   -273   -174    176       C  
ATOM   1049  CG2 VAL B  32      17.881   3.403  -7.503  1.00 23.63           C  
ANISOU 1049  CG2 VAL B  32     2735   2595   3647   -175   -175    253       C  
ATOM   1050  N   LEU B  33      18.282   8.048  -8.672  1.00 22.34           N  
ANISOU 1050  N   LEU B  33     2443   2441   3605    -71      8    296       N  
ATOM   1051  CA  LEU B  33      18.348   9.461  -8.399  1.00 23.39           C  
ANISOU 1051  CA  LEU B  33     2541   2576   3767    -47     31    300       C  
ATOM   1052  C   LEU B  33      16.942  10.003  -8.225  1.00 25.51           C  
ANISOU 1052  C   LEU B  33     2776   2773   4143     39     52    429       C  
ATOM   1053  O   LEU B  33      15.962   9.471  -8.816  1.00 24.19           O  
ANISOU 1053  O   LEU B  33     2542   2701   3947    -47     -2    442       O  
ATOM   1054  CB  LEU B  33      19.051  10.198  -9.554  1.00 22.88           C  
ANISOU 1054  CB  LEU B  33     2587   2430   3673     11    -71    301       C  
ATOM   1055  CG  LEU B  33      20.518   9.864  -9.880  1.00 23.15           C  
ANISOU 1055  CG  LEU B  33     2734   2717   3344   -123     18    295       C  
ATOM   1056  CD1 LEU B  33      21.066  10.870 -10.903  1.00 24.55           C  
ANISOU 1056  CD1 LEU B  33     3213   2602   3512   -124    -51    318       C  
ATOM   1057  CD2 LEU B  33      21.459   9.821  -8.649  1.00 21.78           C  
ANISOU 1057  CD2 LEU B  33     2643   2476   3153    -44    -64    234       C  
ATOM   1058  N   GLU B  34      16.828  11.034  -7.390  1.00 27.68           N  
ANISOU 1058  N   GLU B  34     3051   2894   4572    139    194    421       N  
ATOM   1059  CA  GLU B  34      15.563  11.716  -7.220  1.00 31.92           C  
ANISOU 1059  CA  GLU B  34     3462   3381   5285    249    419    412       C  
ATOM   1060  C   GLU B  34      15.085  12.247  -8.580  1.00 35.21           C  
ANISOU 1060  C   GLU B  34     3824   3709   5844    332    426    473       C  
ATOM   1061  O   GLU B  34      15.864  12.321  -9.556  1.00 34.10           O  
ANISOU 1061  O   GLU B  34     3594   3564   5796    297    312    439       O  
ATOM   1062  CB  GLU B  34      15.718  12.883  -6.243  1.00 31.25           C  
ANISOU 1062  CB  GLU B  34     3433   3332   5108    255    348    399       C  
ATOM   1063  CG  GLU B  34      15.962  12.509  -4.787  1.00 32.06           C  
ANISOU 1063  CG  GLU B  34     3625   3450   5104    215    534    305       C  
ATOM   1064  CD  GLU B  34      16.185  13.727  -3.877  1.00 33.89           C  
ANISOU 1064  CD  GLU B  34     3934   3673   5267    152    615    321       C  
ATOM   1065  OE1 GLU B  34      16.925  14.630  -4.284  1.00 37.17           O  
ANISOU 1065  OE1 GLU B  34     4421   3987   5712    -61    504    191       O  
ATOM   1066  OE2 GLU B  34      15.634  13.803  -2.752  1.00 38.04           O  
ANISOU 1066  OE2 GLU B  34     4830   4196   5424    272    890     84       O  
ATOM   1067  N   GLU B  35      13.805  12.622  -8.636  1.00 40.35           N  
ANISOU 1067  N   GLU B  35     4338   4198   6793    455    595    516       N  
ATOM   1068  CA  GLU B  35      13.223  13.285  -9.803  1.00 45.65           C  
ANISOU 1068  CA  GLU B  35     5061   4763   7520    548    649    597       C  
ATOM   1069  C   GLU B  35      14.082  14.443 -10.340  1.00 47.36           C  
ANISOU 1069  C   GLU B  35     5211   4790   7993    667    766    723       C  
ATOM   1070  O   GLU B  35      14.415  15.395  -9.621  1.00 47.96           O  
ANISOU 1070  O   GLU B  35     5314   4739   8170    656    820    721       O  
ATOM   1071  CB  GLU B  35      11.816  13.805  -9.472  1.00 46.05           C  
ANISOU 1071  CB  GLU B  35     5148   4992   7355    438    545    447       C  
ATOM   1072  CG  GLU B  35      10.766  13.495 -10.530  1.00 50.88           C  
ANISOU 1072  CG  GLU B  35     6056   5937   7339    254    304    266       C  
ATOM   1073  CD  GLU B  35      10.473  12.003 -10.631  1.00 55.69           C  
ANISOU 1073  CD  GLU B  35     6813   6560   7784    107     19    115       C  
ATOM   1074  OE1 GLU B  35       9.896  11.443  -9.653  1.00 56.46           O  
ANISOU 1074  OE1 GLU B  35     7050   6932   7469    132    147    198       O  
ATOM   1075  OE2 GLU B  35      10.822  11.396 -11.687  1.00 57.08           O  
ANISOU 1075  OE2 GLU B  35     7082   7087   7516    146    101      5       O  
ATOM   1076  N   MET B  36      14.436  14.330 -11.611  1.00 48.94           N  
ANISOU 1076  N   MET B  36     5406   4983   8205    751    761    847       N  
ATOM   1077  CA  MET B  36      15.103  15.392 -12.329  1.00 50.40           C  
ANISOU 1077  CA  MET B  36     5647   5265   8237    743    595    928       C  
ATOM   1078  C   MET B  36      14.827  15.144 -13.798  1.00 51.96           C  
ANISOU 1078  C   MET B  36     5795   5423   8522    820    518   1189       C  
ATOM   1079  O   MET B  36      14.390  14.046 -14.179  1.00 52.43           O  
ANISOU 1079  O   MET B  36     5847   5426   8645    853    469   1196       O  
ATOM   1080  CB  MET B  36      16.607  15.377 -12.047  1.00 50.29           C  
ANISOU 1080  CB  MET B  36     5714   5385   8006    602    498    768       C  
ATOM   1081  CG  MET B  36      17.337  14.187 -12.662  1.00 49.56           C  
ANISOU 1081  CG  MET B  36     5766   5591   7471    442    345    503       C  
ATOM   1082  SD  MET B  36      19.098  14.294 -12.415  1.00 48.91           S  
ANISOU 1082  SD  MET B  36     5659   5500   7424    624    403    561       S  
ATOM   1083  CE  MET B  36      19.127  14.144 -10.646  1.00 51.77           C  
ANISOU 1083  CE  MET B  36     6187   6188   7293    256     93    172       C  
ATOM   1084  N   SER B  37      15.070  16.161 -14.617  1.00 53.37           N  
ANISOU 1084  N   SER B  37     5973   5669   8635    824    390   1414       N  
ATOM   1085  CA  SER B  37      14.877  16.049 -16.058  1.00 54.49           C  
ANISOU 1085  CA  SER B  37     6171   5946   8584    761    221   1548       C  
ATOM   1086  C   SER B  37      16.177  15.593 -16.692  1.00 54.07           C  
ANISOU 1086  C   SER B  37     6178   6004   8359    711     81   1675       C  
ATOM   1087  O   SER B  37      17.250  16.195 -16.504  1.00 54.01           O  
ANISOU 1087  O   SER B  37     6194   5960   8364    704     52   1746       O  
ATOM   1088  CB  SER B  37      14.414  17.389 -16.678  1.00 54.28           C  
ANISOU 1088  CB  SER B  37     6248   5992   8384    676    161   1317       C  
ATOM   1089  OG  SER B  37      14.909  18.330 -16.516  0.00 56.41           O  
ANISOU 1089  OG  SER B  37     4806   4442  12185   2363   1262   4810       O  
ATOM   1090  N   LEU B  38      16.085  14.494 -17.417  1.00 53.60           N  
ANISOU 1090  N   LEU B  38     6239   6203   7920    533   -116   1691       N  
ATOM   1091  CA  LEU B  38      17.205  14.073 -18.210  1.00 53.19           C  
ANISOU 1091  CA  LEU B  38     6251   6522   7437    334   -306   1647       C  
ATOM   1092  C   LEU B  38      16.757  14.008 -19.656  1.00 55.12           C  
ANISOU 1092  C   LEU B  38     6540   6967   7436    213   -504   1809       C  
ATOM   1093  O   LEU B  38      15.651  13.515 -19.955  1.00 55.55           O  
ANISOU 1093  O   LEU B  38     6575   7035   7494    256   -558   1849       O  
ATOM   1094  CB  LEU B  38      17.766  12.735 -17.745  1.00 51.72           C  
ANISOU 1094  CB  LEU B  38     6173   6357   7121    261   -257   1312       C  
ATOM   1095  CG  LEU B  38      18.469  12.758 -16.388  1.00 49.58           C  
ANISOU 1095  CG  LEU B  38     5972   6158   6707    140   -117    773       C  
ATOM   1096  CD1 LEU B  38      18.774  11.343 -15.994  1.00 45.60           C  
ANISOU 1096  CD1 LEU B  38     5667   5694   5965     45    -66    395       C  
ATOM   1097  CD2 LEU B  38      19.744  13.623 -16.399  1.00 46.85           C  
ANISOU 1097  CD2 LEU B  38     5865   5939   5996    119    -59    388       C  
ATOM   1098  N   PRO B  39      17.615  14.499 -20.549  1.00 56.57           N  
ANISOU 1098  N   PRO B  39     6846   7396   7251     27   -629   1854       N  
ATOM   1099  CA  PRO B  39      17.355  14.386 -21.974  1.00 58.43           C  
ANISOU 1099  CA  PRO B  39     7135   7838   7226   -133   -779   1917       C  
ATOM   1100  C   PRO B  39      17.382  12.913 -22.368  1.00 59.87           C  
ANISOU 1100  C   PRO B  39     7428   8189   7130   -338   -977   2051       C  
ATOM   1101  O   PRO B  39      18.168  12.144 -21.808  1.00 59.59           O  
ANISOU 1101  O   PRO B  39     7434   8169   7035   -287   -973   2086       O  
ATOM   1102  CB  PRO B  39      18.544  15.129 -22.620  1.00 58.14           C  
ANISOU 1102  CB  PRO B  39     7138   7727   7224   -128   -620   1581       C  
ATOM   1103  CG  PRO B  39      19.238  15.879 -21.508  1.00 57.11           C  
ANISOU 1103  CG  PRO B  39     7019   7465   7213    -73   -467   1356       C  
ATOM   1104  CD  PRO B  39      18.917  15.141 -20.262  1.00 56.72           C  
ANISOU 1104  CD  PRO B  39     6922   7383   7245      2   -547   1521       C  
ATOM   1105  N   GLY B  40      16.519  12.530 -23.307  1.00 62.73           N  
ANISOU 1105  N   GLY B  40     7775   8899   7158   -598  -1172   2166       N  
ATOM   1106  CA  GLY B  40      16.577  11.198 -23.912  1.00 65.44           C  
ANISOU 1106  CA  GLY B  40     8217   9532   7115   -912  -1370   2142       C  
ATOM   1107  C   GLY B  40      15.323  10.362 -23.751  1.00 67.12           C  
ANISOU 1107  C   GLY B  40     8428  10008   7066  -1139  -1486   2140       C  
ATOM   1108  O   GLY B  40      14.402  10.734 -23.014  1.00 67.88           O  
ANISOU 1108  O   GLY B  40     8518  10115   7156  -1107  -1489   2127       O  
ATOM   1109  N   ARG B  41      15.294   9.234 -24.459  1.00 67.61           N  
ANISOU 1109  N   ARG B  41     8564  10206   6918  -1273  -1523   2001       N  
ATOM   1110  CA  ARG B  41      14.239   8.244 -24.318  1.00 67.36           C  
ANISOU 1110  CA  ARG B  41     8600  10247   6746  -1392  -1544   1789       C  
ATOM   1111  C   ARG B  41      14.468   7.459 -23.020  1.00 66.73           C  
ANISOU 1111  C   ARG B  41     8497  10206   6648  -1448  -1555   1688       C  
ATOM   1112  O   ARG B  41      15.561   7.510 -22.456  1.00 66.75           O  
ANISOU 1112  O   ARG B  41     8582  10193   6587  -1428  -1532   1603       O  
ATOM   1113  CB  ARG B  41      14.245   7.309 -25.529  1.00 67.85           C  
ANISOU 1113  CB  ARG B  41     8620  10077   7083  -1128  -1247   1513       C  
ATOM   1114  CG  ARG B  41      14.629   7.033 -26.085  0.00 70.83           C  
ANISOU 1114  CG  ARG B  41    10404  13207   3300  -5353  -4108   3754       C  
ATOM   1115  CD  ARG B  41      14.052   6.563 -27.411  0.00 81.11           C  
ANISOU 1115  CD  ARG B  41    11962  15475   3382  -6750  -4612   4050       C  
ATOM   1116  NE  ARG B  41      14.943   6.858 -28.527  0.00 84.75           N  
ANISOU 1116  NE  ARG B  41    12978  16134   3088  -7279  -4465   3943       N  
ATOM   1117  CZ  ARG B  41      14.543   7.100 -29.767  0.00 94.58           C  
ANISOU 1117  CZ  ARG B  41    14218  18346   3370  -8361  -5036   4616       C  
ATOM   1118  NH1 ARG B  41      13.251   7.094 -30.079  0.00102.23           N  
ANISOU 1118  NH1 ARG B  41    14580  20234   4027  -9057  -5860   5551       N  
ATOM   1119  NH2 ARG B  41      15.441   7.359 -30.705  0.00 97.47           N  
ANISOU 1119  NH2 ARG B  41    15147  18820   3064  -8804  -4799   4426       N  
ATOM   1120  N   TRP B  42      13.442   6.760 -22.537  1.00 65.66           N  
ANISOU 1120  N   TRP B  42     8360  10015   6571  -1440  -1524   1473       N  
ATOM   1121  CA  TRP B  42      13.559   5.933 -21.337  1.00 64.27           C  
ANISOU 1121  CA  TRP B  42     8190   9700   6528  -1391  -1395   1268       C  
ATOM   1122  C   TRP B  42      12.588   4.763 -21.332  1.00 63.61           C  
ANISOU 1122  C   TRP B  42     8115   9711   6340  -1509  -1489   1224       C  
ATOM   1123  O   TRP B  42      11.617   4.756 -22.081  1.00 63.80           O  
ANISOU 1123  O   TRP B  42     8185   9774   6280  -1546  -1555   1232       O  
ATOM   1124  CB  TRP B  42      13.373   6.763 -20.066  1.00 63.66           C  
ANISOU 1124  CB  TRP B  42     7791   9336   7060   -901   -898    920       C  
ATOM   1125  CG  TRP B  42      12.097   7.546 -19.987  1.00 65.60           C  
ANISOU 1125  CG  TRP B  42     8257   9158   7507   -645   -585    530       C  
ATOM   1126  CD1 TRP B  42      11.927   8.856 -20.330  1.00 63.72           C  
ANISOU 1126  CD1 TRP B  42     7650   8734   7826   -449   -168    396       C  
ATOM   1127  CD2 TRP B  42      10.822   7.088 -19.510  1.00 65.96           C  
ANISOU 1127  CD2 TRP B  42     8253   8911   7897   -252   -328    246       C  
ATOM   1128  NE1 TRP B  42      10.629   9.243 -20.101  1.00 65.43           N  
ANISOU 1128  NE1 TRP B  42     8392   8514   7955   -383   -288    373       N  
ATOM   1129  CE2 TRP B  42       9.922   8.179 -19.604  1.00 66.80           C  
ANISOU 1129  CE2 TRP B  42     8384   8945   8051   -184   -278    222       C  
ATOM   1130  CE3 TRP B  42      10.340   5.863 -19.021  1.00 64.37           C  
ANISOU 1130  CE3 TRP B  42     7845   8677   7933   -248   -146    242       C  
ATOM   1131  CZ2 TRP B  42       8.567   8.086 -19.227  1.00 66.53           C  
ANISOU 1131  CZ2 TRP B  42     8421   8900   7956   -393   -352    373       C  
ATOM   1132  CZ3 TRP B  42       8.992   5.768 -18.641  1.00 67.40           C  
ANISOU 1132  CZ3 TRP B  42     8465   9148   7994   -162   -510    187       C  
ATOM   1133  CH2 TRP B  42       8.124   6.879 -18.747  1.00 66.74           C  
ANISOU 1133  CH2 TRP B  42     8389   8990   7975   -276   -501    287       C  
ATOM   1134  N   LYS B  43      12.866   3.782 -20.473  1.00 61.69           N  
ANISOU 1134  N   LYS B  43     7913   9438   6088  -1574  -1454   1099       N  
ATOM   1135  CA  LYS B  43      12.026   2.602 -20.292  1.00 59.96           C  
ANISOU 1135  CA  LYS B  43     7710   9059   6010  -1472  -1302    887       C  
ATOM   1136  C   LYS B  43      11.513   2.574 -18.840  1.00 58.56           C  
ANISOU 1136  C   LYS B  43     7479   8859   5911  -1528  -1320    834       C  
ATOM   1137  O   LYS B  43      12.239   2.938 -17.914  1.00 57.94           O  
ANISOU 1137  O   LYS B  43     7462   8741   5808  -1534  -1259    832       O  
ATOM   1138  CB  LYS B  43      12.816   1.313 -20.590  1.00 60.42           C  
ANISOU 1138  CB  LYS B  43     7755   8980   6220  -1268  -1094    746       C  
ATOM   1139  CG  LYS B  43      13.558   1.256 -21.937  1.00 60.41           C  
ANISOU 1139  CG  LYS B  43     7784   8567   6600   -832   -737    498       C  
ATOM   1140  CD  LYS B  43      14.270   0.334 -22.282  0.00 57.44           C  
ANISOU 1140  CD  LYS B  43    10347   9276   2199  -5546  -1898   -156       C  
ATOM   1141  CE  LYS B  43      15.631   0.767 -21.719  0.00 50.77           C  
ANISOU 1141  CE  LYS B  43     9553   7756   1979  -4621  -1354   -361       C  
ATOM   1142  NZ  LYS B  43      16.763   0.318 -22.595  0.00 53.65           N  
ANISOU 1142  NZ  LYS B  43    10667   7763   1953  -5012   -666   -922       N  
ATOM   1143  N   PRO B  44      10.264   2.159 -18.636  1.00 57.33           N  
ANISOU 1143  N   PRO B  44     7311   8575   5896  -1446  -1229    717       N  
ATOM   1144  CA  PRO B  44       9.761   1.916 -17.283  1.00 55.30           C  
ANISOU 1144  CA  PRO B  44     7047   8226   5735  -1380  -1209    640       C  
ATOM   1145  C   PRO B  44      10.483   0.725 -16.663  1.00 52.83           C  
ANISOU 1145  C   PRO B  44     6714   7831   5527  -1383  -1146    563       C  
ATOM   1146  O   PRO B  44      10.908  -0.199 -17.375  1.00 52.89           O  
ANISOU 1146  O   PRO B  44     6765   7869   5462  -1395  -1167    568       O  
ATOM   1147  CB  PRO B  44       8.270   1.602 -17.497  1.00 55.42           C  
ANISOU 1147  CB  PRO B  44     7015   8141   5899  -1172   -973    549       C  
ATOM   1148  CG  PRO B  44       8.187   1.108 -18.881  1.00 56.76           C  
ANISOU 1148  CG  PRO B  44     7171   8221   6175  -1061   -918    483       C  
ATOM   1149  CD  PRO B  44       9.242   1.877 -19.666  1.00 57.41           C  
ANISOU 1149  CD  PRO B  44     7292   8466   6055  -1197  -1086    593       C  
ATOM   1150  N   LYS B  45      10.646   0.773 -15.344  1.00 48.77           N  
ANISOU 1150  N   LYS B  45     6208   7051   5270  -1196  -1026    459       N  
ATOM   1151  CA  LYS B  45      11.310  -0.285 -14.604  1.00 45.42           C  
ANISOU 1151  CA  LYS B  45     5755   6392   5108   -980   -808    300       C  
ATOM   1152  C   LYS B  45      10.794  -0.263 -13.172  1.00 43.11           C  
ANISOU 1152  C   LYS B  45     5456   5999   4925   -919   -805    289       C  
ATOM   1153  O   LYS B  45      10.359   0.773 -12.689  1.00 42.64           O  
ANISOU 1153  O   LYS B  45     5385   5956   4860   -875   -788    319       O  
ATOM   1154  CB  LYS B  45      12.833  -0.092 -14.650  1.00 45.15           C  
ANISOU 1154  CB  LYS B  45     5717   6201   5237   -809   -674    255       C  
ATOM   1155  CG  LYS B  45      13.638  -1.306 -14.233  1.00 45.45           C  
ANISOU 1155  CG  LYS B  45     5721   6111   5435   -568   -404    164       C  
ATOM   1156  CD  LYS B  45      15.009  -0.909 -13.716  1.00 45.49           C  
ANISOU 1156  CD  LYS B  45     5778   5943   5561   -355   -230    103       C  
ATOM   1157  CE  LYS B  45      15.686  -2.018 -12.891  1.00 45.41           C  
ANISOU 1157  CE  LYS B  45     5784   5876   5592   -198   -105     20       C  
ATOM   1158  NZ  LYS B  45      16.486  -3.001 -13.658  1.00 46.07           N  
ANISOU 1158  NZ  LYS B  45     5890   5789   5825   -162    -31    -75       N  
ATOM   1159  N   MET B  46      10.813  -1.410 -12.505  1.00 41.23           N  
ANISOU 1159  N   MET B  46     5175   5663   4826   -822   -695    183       N  
ATOM   1160  CA  MET B  46      10.441  -1.497 -11.079  1.00 39.41           C  
ANISOU 1160  CA  MET B  46     4884   5305   4785   -684   -589    158       C  
ATOM   1161  C   MET B  46      11.680  -1.880 -10.254  1.00 36.81           C  
ANISOU 1161  C   MET B  46     4582   4889   4511   -675   -495    153       C  
ATOM   1162  O   MET B  46      12.472  -2.724 -10.681  1.00 36.80           O  
ANISOU 1162  O   MET B  46     4590   4914   4478   -639   -506    182       O  
ATOM   1163  CB  MET B  46       9.313  -2.517 -10.875  1.00 41.43           C  
ANISOU 1163  CB  MET B  46     5160   5499   5083   -592   -428    111       C  
ATOM   1164  CG  MET B  46       8.007  -2.194 -11.652  1.00 44.51           C  
ANISOU 1164  CG  MET B  46     5442   5831   5636   -381   -418    110       C  
ATOM   1165  SD  MET B  46       6.710  -1.483 -10.587  1.00 53.18           S  
ANISOU 1165  SD  MET B  46     6169   7124   6912    -80   -388   -122       S  
ATOM   1166  CE  MET B  46       5.460  -0.974 -11.795  1.00 48.98           C  
ANISOU 1166  CE  MET B  46     5892   6471   6247   -103   -217     98       C  
ATOM   1167  N   ILE B  47      11.877  -1.243  -9.105  1.00 33.57           N  
ANISOU 1167  N   ILE B  47     4073   4408   4274   -638   -435    134       N  
ATOM   1168  CA  ILE B  47      12.912  -1.699  -8.186  1.00 31.77           C  
ANISOU 1168  CA  ILE B  47     3835   4102   4132   -504   -365     92       C  
ATOM   1169  C   ILE B  47      12.339  -1.941  -6.811  1.00 30.75           C  
ANISOU 1169  C   ILE B  47     3567   4033   4081   -554   -390    164       C  
ATOM   1170  O   ILE B  47      11.404  -1.290  -6.396  1.00 30.11           O  
ANISOU 1170  O   ILE B  47     3525   3942   3973   -511   -420    169       O  
ATOM   1171  CB  ILE B  47      14.121  -0.720  -8.092  1.00 31.53           C  
ANISOU 1171  CB  ILE B  47     3778   4105   4095   -417   -295     87       C  
ATOM   1172  CG1 ILE B  47      13.635   0.692  -7.757  1.00 32.55           C  
ANISOU 1172  CG1 ILE B  47     4028   4104   4235   -359   -330     70       C  
ATOM   1173  CG2 ILE B  47      14.927  -0.735  -9.355  1.00 32.37           C  
ANISOU 1173  CG2 ILE B  47     3944   4156   4196   -309   -246    -14       C  
ATOM   1174  CD1 ILE B  47      14.729   1.700  -7.708  1.00 35.73           C  
ANISOU 1174  CD1 ILE B  47     4246   4529   4798   -266   -183     15       C  
ATOM   1175  N   GLY B  48      12.929  -2.880  -6.090  1.00 30.89           N  
ANISOU 1175  N   GLY B  48     3547   4098   4089   -627   -352    200       N  
ATOM   1176  CA  GLY B  48      12.468  -3.181  -4.741  1.00 31.25           C  
ANISOU 1176  CA  GLY B  48     3476   4287   4108   -608   -289    313       C  
ATOM   1177  C   GLY B  48      13.468  -2.855  -3.657  1.00 31.54           C  
ANISOU 1177  C   GLY B  48     3459   4442   4080   -678   -269    357       C  
ATOM   1178  O   GLY B  48      14.688  -2.737  -3.899  1.00 31.13           O  
ANISOU 1178  O   GLY B  48     3447   4439   3940   -574   -237    359       O  
ATOM   1179  N   GLY B  49      12.929  -2.690  -2.461  1.00 32.30           N  
ANISOU 1179  N   GLY B  49     3387   4723   4162   -756   -182    394       N  
ATOM   1180  CA  GLY B  49      13.727  -2.503  -1.264  1.00 34.58           C  
ANISOU 1180  CA  GLY B  49     3578   5236   4324   -848   -165    428       C  
ATOM   1181  C   GLY B  49      12.958  -2.872  -0.018  1.00 36.21           C  
ANISOU 1181  C   GLY B  49     3763   5532   4460   -932   -107    464       C  
ATOM   1182  O   GLY B  49      11.974  -3.607  -0.089  1.00 36.25           O  
ANISOU 1182  O   GLY B  49     3811   5477   4483   -932   -109    445       O  
ATOM   1183  N   ILE B  50      13.412  -2.357   1.121  1.00 37.77           N  
ANISOU 1183  N   ILE B  50     3914   5839   4596   -992    -76    389       N  
ATOM   1184  CA  ILE B  50      12.693  -2.450   2.388  1.00 39.92           C  
ANISOU 1184  CA  ILE B  50     4298   6094   4775   -967      3    351       C  
ATOM   1185  C   ILE B  50      11.296  -1.774   2.243  1.00 40.67           C  
ANISOU 1185  C   ILE B  50     4302   6306   4843  -1103     31    323       C  
ATOM   1186  O   ILE B  50      11.171  -0.654   1.735  1.00 41.64           O  
ANISOU 1186  O   ILE B  50     4498   6431   4891  -1036      0    344       O  
ATOM   1187  CB  ILE B  50      13.571  -1.832   3.540  1.00 39.52           C  
ANISOU 1187  CB  ILE B  50     4317   5922   4774   -796     -4    279       C  
ATOM   1188  CG1 ILE B  50      13.992  -2.895   4.546  1.00 41.57           C  
ANISOU 1188  CG1 ILE B  50     4735   5930   5128   -518      2    194       C  
ATOM   1189  CG2 ILE B  50      12.810  -0.821   4.360  1.00 40.45           C  
ANISOU 1189  CG2 ILE B  50     4557   5815   4994   -576    -87    159       C  
ATOM   1190  CD1 ILE B  50      15.248  -3.640   4.241  1.00 43.08           C  
ANISOU 1190  CD1 ILE B  50     5058   5885   5424   -283     58     62       C  
ATOM   1191  N   GLY B  51      10.243  -2.447   2.657  1.00 40.57           N  
ANISOU 1191  N   GLY B  51     4191   6314   4908  -1154     79    246       N  
ATOM   1192  CA  GLY B  51       8.922  -1.834   2.545  1.00 40.96           C  
ANISOU 1192  CA  GLY B  51     4245   6266   5053  -1046     51    211       C  
ATOM   1193  C   GLY B  51       8.224  -1.899   1.192  1.00 40.60           C  
ANISOU 1193  C   GLY B  51     4109   6153   5162   -984     63    199       C  
ATOM   1194  O   GLY B  51       7.053  -1.526   1.077  1.00 41.44           O  
ANISOU 1194  O   GLY B  51     4160   6225   5361   -917     60    207       O  
ATOM   1195  N   GLY B  52       8.914  -2.370   0.163  1.00 39.10           N  
ANISOU 1195  N   GLY B  52     3873   5927   5056   -927     31    229       N  
ATOM   1196  CA  GLY B  52       8.246  -2.628  -1.094  1.00 37.68           C  
ANISOU 1196  CA  GLY B  52     3695   5559   5062   -792   -104    251       C  
ATOM   1197  C   GLY B  52       8.932  -2.214  -2.376  1.00 36.94           C  
ANISOU 1197  C   GLY B  52     3653   5382   4996   -660   -155    214       C  
ATOM   1198  O   GLY B  52      10.163  -2.133  -2.431  1.00 35.99           O  
ANISOU 1198  O   GLY B  52     3518   5250   4905   -731   -214    218       O  
ATOM   1199  N  APHE B  53       8.135  -1.987  -3.432  0.50 36.33           N  
ANISOU 1199  N  APHE B  53     3610   5216   4976   -568   -206    220       N  
ATOM   1200  N  BPHE B  53       8.113  -1.917  -3.378  0.50 36.91           N  
ANISOU 1200  N  BPHE B  53     3681   5295   5048   -568   -197    222       N  
ATOM   1201  CA APHE B  53       8.629  -1.777  -4.813  0.50 36.03           C  
ANISOU 1201  CA APHE B  53     3668   5070   4951   -469   -248    218       C  
ATOM   1202  CA BPHE B  53       8.604  -1.596  -4.694  0.50 37.16           C  
ANISOU 1202  CA BPHE B  53     3805   5214   5098   -458   -222    236       C  
ATOM   1203  C  APHE B  53       8.142  -0.432  -5.397  0.50 36.45           C  
ANISOU 1203  C  APHE B  53     3641   5151   5055   -429   -294    256       C  
ATOM   1204  C  BPHE B  53       8.306  -0.154  -5.047  0.50 37.02           C  
ANISOU 1204  C  BPHE B  53     3700   5235   5128   -429   -272    249       C  
ATOM   1205  O  APHE B  53       6.950  -0.124  -5.284  0.50 36.73           O  
ANISOU 1205  O  APHE B  53     3643   5223   5088   -435   -259    254       O  
ATOM   1206  O  BPHE B  53       7.441   0.486  -4.448  0.50 37.03           O  
ANISOU 1206  O  BPHE B  53     3678   5249   5141   -406   -260    224       O  
ATOM   1207  CB APHE B  53       8.121  -2.906  -5.739  0.50 35.67           C  
ANISOU 1207  CB APHE B  53     3794   4921   4835   -351   -181    150       C  
ATOM   1208  CB BPHE B  53       7.961  -2.515  -5.730  0.50 38.10           C  
ANISOU 1208  CB BPHE B  53     4189   5184   5103   -392   -133    155       C  
ATOM   1209  CG APHE B  53       8.978  -4.170  -5.759  0.50 34.47           C  
ANISOU 1209  CG APHE B  53     3869   4672   4555   -238   -135     87       C  
ATOM   1210  CG BPHE B  53       6.543  -2.153  -6.071  0.50 38.58           C  
ANISOU 1210  CG BPHE B  53     4380   5120   5158   -163   -114    116       C  
ATOM   1211  CD1APHE B  53       8.762  -5.196  -4.848  0.50 33.44           C  
ANISOU 1211  CD1APHE B  53     3898   4418   4390   -146    -96    -57       C  
ATOM   1212  CD1BPHE B  53       6.252  -1.463  -7.249  0.50 40.06           C  
ANISOU 1212  CD1BPHE B  53     4689   5263   5267    -65    -65    110       C  
ATOM   1213  CD2APHE B  53       9.955  -4.356  -6.746  0.50 34.31           C  
ANISOU 1213  CD2APHE B  53     4139   4437   4458    -95   -101    -25       C  
ATOM   1214  CD2BPHE B  53       5.496  -2.510  -5.230  0.50 38.71           C  
ANISOU 1214  CD2BPHE B  53     4631   5034   5042    -91     12     27       C  
ATOM   1215  CE1APHE B  53       9.535  -6.365  -4.885  0.50 33.27           C  
ANISOU 1215  CE1APHE B  53     3993   4316   4330   -212   -227    -24       C  
ATOM   1216  CE1BPHE B  53       4.941  -1.126  -7.576  0.50 40.30           C  
ANISOU 1216  CE1BPHE B  53     4854   5213   5245    -79    -50     36       C  
ATOM   1217  CE2APHE B  53      10.737  -5.522  -6.783  0.50 32.73           C  
ANISOU 1217  CE2APHE B  53     3937   4355   4142   -170   -126   -154       C  
ATOM   1218  CE2BPHE B  53       4.187  -2.181  -5.550  0.50 39.31           C  
ANISOU 1218  CE2BPHE B  53     4729   5074   5132    -89    -12     37       C  
ATOM   1219  CZ APHE B  53      10.519  -6.524  -5.857  0.50 32.11           C  
ANISOU 1219  CZ APHE B  53     3856   4309   4034   -211   -132    -38       C  
ATOM   1220  CZ BPHE B  53       3.904  -1.493  -6.722  0.50 38.96           C  
ANISOU 1220  CZ BPHE B  53     4580   5138   5085    -60    -73     80       C  
ATOM   1221  N   ILE B  54       9.041   0.346  -6.030  1.00 36.43           N  
ANISOU 1221  N   ILE B  54     3580   5183   5078   -423   -330    313       N  
ATOM   1222  CA  ILE B  54       8.687   1.606  -6.692  1.00 36.42           C  
ANISOU 1222  CA  ILE B  54     3654   5088   5095   -312   -347    316       C  
ATOM   1223  C   ILE B  54       8.884   1.503  -8.208  1.00 37.11           C  
ANISOU 1223  C   ILE B  54     3717   5188   5194   -324   -439    428       C  
ATOM   1224  O   ILE B  54       9.671   0.681  -8.693  1.00 36.88           O  
ANISOU 1224  O   ILE B  54     3780   5078   5152   -336   -456    424       O  
ATOM   1225  CB  ILE B  54       9.444   2.861  -6.145  1.00 35.88           C  
ANISOU 1225  CB  ILE B  54     3733   4987   4912   -245   -273    255       C  
ATOM   1226  CG1 ILE B  54      10.961   2.724  -6.264  1.00 34.81           C  
ANISOU 1226  CG1 ILE B  54     3702   4824   4699   -241   -255    138       C  
ATOM   1227  CG2 ILE B  54       9.012   3.230  -4.736  1.00 37.11           C  
ANISOU 1227  CG2 ILE B  54     4087   4941   5069    -98   -213    192       C  
ATOM   1228  CD1 ILE B  54      11.657   4.098  -6.284  1.00 33.51           C  
ANISOU 1228  CD1 ILE B  54     3796   4507   4428     -2   -158    202       C  
ATOM   1229  N   LYS B  55       8.178   2.357  -8.942  1.00 38.36           N  
ANISOU 1229  N   LYS B  55     3853   5352   5367   -288   -548    511       N  
ATOM   1230  CA  LYS B  55       8.359   2.476 -10.389  1.00 39.22           C  
ANISOU 1230  CA  LYS B  55     4008   5473   5419   -234   -611    620       C  
ATOM   1231  C   LYS B  55       9.337   3.616 -10.665  1.00 39.21           C  
ANISOU 1231  C   LYS B  55     4057   5462   5379   -202   -694    669       C  
ATOM   1232  O   LYS B  55       9.279   4.660 -10.025  1.00 39.49           O  
ANISOU 1232  O   LYS B  55     4068   5432   5502   -166   -663    694       O  
ATOM   1233  CB  LYS B  55       7.000   2.672 -11.103  1.00 39.20           C  
ANISOU 1233  CB  LYS B  55     4097   5401   5395   -160   -524    563       C  
ATOM   1234  CG  LYS B  55       5.779   2.152 -10.525  0.00 39.73           C  
ANISOU 1234  CG  LYS B  55     2284   6449   6359   -835  -2153   2410       C  
ATOM   1235  CD  LYS B  55       4.480   2.692 -11.225  0.00 46.74           C  
ANISOU 1235  CD  LYS B  55     2434   7678   7645   -913  -2515   3328       C  
ATOM   1236  CE  LYS B  55       3.206   2.215 -10.525  0.00 49.65           C  
ANISOU 1236  CE  LYS B  55     2280   8155   8427   -932  -2497   3609       C  
ATOM   1237  NZ  LYS B  55       1.982   2.310 -11.411  0.00 57.32           N  
ANISOU 1237  NZ  LYS B  55     2533   9657   9587  -1253  -3057   4589       N  
ATOM   1238  N   VAL B  56      10.273   3.381 -11.575  1.00 38.71           N  
ANISOU 1238  N   VAL B  56     4091   5422   5196   -185   -735    669       N  
ATOM   1239  CA  VAL B  56      11.296   4.360 -11.917  1.00 38.98           C  
ANISOU 1239  CA  VAL B  56     4348   5378   5081   -212   -679    617       C  
ATOM   1240  C   VAL B  56      11.444   4.458 -13.428  1.00 39.86           C  
ANISOU 1240  C   VAL B  56     4486   5531   5128   -231   -768    698       C  
ATOM   1241  O   VAL B  56      10.971   3.593 -14.174  1.00 39.77           O  
ANISOU 1241  O   VAL B  56     4532   5523   5052   -230   -797    703       O  
ATOM   1242  CB  VAL B  56      12.703   4.005 -11.305  1.00 38.39           C  
ANISOU 1242  CB  VAL B  56     4342   5234   5009   -150   -529    499       C  
ATOM   1243  CG1 VAL B  56      12.699   4.101  -9.779  1.00 37.40           C  
ANISOU 1243  CG1 VAL B  56     4367   4923   4917   -191   -443    363       C  
ATOM   1244  CG2 VAL B  56      13.147   2.638 -11.748  1.00 37.96           C  
ANISOU 1244  CG2 VAL B  56     4387   5165   4869   -110   -273    457       C  
ATOM   1245  N   ARG B  57      12.109   5.515 -13.874  1.00 40.40           N  
ANISOU 1245  N   ARG B  57     4697   5596   5054   -279   -789    720       N  
ATOM   1246  CA  ARG B  57      12.433   5.694 -15.279  1.00 41.73           C  
ANISOU 1246  CA  ARG B  57     5066   5689   5100   -278   -679    662       C  
ATOM   1247  C   ARG B  57      13.886   5.346 -15.511  1.00 39.75           C  
ANISOU 1247  C   ARG B  57     4977   5445   4678   -374   -731    726       C  
ATOM   1248  O   ARG B  57      14.757   5.819 -14.805  1.00 39.12           O  
ANISOU 1248  O   ARG B  57     4866   5346   4652   -291   -679    783       O  
ATOM   1249  CB  ARG B  57      12.111   7.129 -15.719  1.00 41.57           C  
ANISOU 1249  CB  ARG B  57     5101   5606   5087   -208   -603    594       C  
ATOM   1250  CG  ARG B  57      10.597   7.438 -15.605  1.00 43.63           C  
ANISOU 1250  CG  ARG B  57     5371   5751   5455   -101   -346    367       C  
ATOM   1251  CD  ARG B  57      10.199   8.857 -15.985  1.00 45.20           C  
ANISOU 1251  CD  ARG B  57     5612   5919   5643    -70   -376    483       C  
ATOM   1252  NE  ARG B  57      11.050   9.826 -15.299  1.00 51.83           N  
ANISOU 1252  NE  ARG B  57     6571   6542   6577   -155   -312    129       N  
ATOM   1253  CZ  ARG B  57      11.268  11.071 -15.713  1.00 56.21           C  
ANISOU 1253  CZ  ARG B  57     7182   6913   7262     -7    -74    133       C  
ATOM   1254  NH1 ARG B  57      10.682  11.522 -16.832  1.00 56.90           N  
ANISOU 1254  NH1 ARG B  57     7330   7131   7157     80   -173    138       N  
ATOM   1255  NH2 ARG B  57      12.074  11.868 -15.009  1.00 55.96           N  
ANISOU 1255  NH2 ARG B  57     7041   6968   7251    -29   -229    109       N  
ATOM   1256  N   GLN B  58      14.140   4.494 -16.489  1.00 39.51           N  
ANISOU 1256  N   GLN B  58     5167   5404   4439   -489   -719    701       N  
ATOM   1257  CA  GLN B  58      15.486   4.094 -16.790  1.00 39.64           C  
ANISOU 1257  CA  GLN B  58     5392   5391   4274   -495   -673    508       C  
ATOM   1258  C   GLN B  58      16.076   4.837 -17.984  1.00 40.04           C  
ANISOU 1258  C   GLN B  58     5576   5446   4191   -522   -646    423       C  
ATOM   1259  O   GLN B  58      15.496   4.814 -19.072  1.00 40.50           O  
ANISOU 1259  O   GLN B  58     5635   5531   4218   -565   -672    429       O  
ATOM   1260  CB  GLN B  58      15.535   2.611 -17.059  1.00 39.82           C  
ANISOU 1260  CB  GLN B  58     5357   5420   4353   -407   -543    405       C  
ATOM   1261  CG  GLN B  58      16.884   2.185 -17.517  1.00 40.15           C  
ANISOU 1261  CG  GLN B  58     5346   5323   4585   -220   -363    240       C  
ATOM   1262  CD  GLN B  58      16.973   0.712 -17.715  1.00 43.75           C  
ANISOU 1262  CD  GLN B  58     5727   5556   5337   -179   -261    114       C  
ATOM   1263  OE1 GLN B  58      17.777   0.241 -18.524  1.00 43.68           O  
ANISOU 1263  OE1 GLN B  58     5818   5374   5405   -116    -86     58       O  
ATOM   1264  NE2 GLN B  58      16.159  -0.038 -16.980  1.00 44.43           N  
ANISOU 1264  NE2 GLN B  58     5677   5749   5455   -170    -24    193       N  
ATOM   1265  N   TYR B  59      17.235   5.458 -17.765  1.00 39.23           N  
ANISOU 1265  N   TYR B  59     5642   5223   4039   -571   -581    327       N  
ATOM   1266  CA  TYR B  59      18.040   6.094 -18.801  1.00 39.28           C  
ANISOU 1266  CA  TYR B  59     5798   5107   4017   -542   -476    283       C  
ATOM   1267  C   TYR B  59      19.413   5.421 -18.985  1.00 39.34           C  
ANISOU 1267  C   TYR B  59     5998   5053   3894   -628   -378    219       C  
ATOM   1268  O   TYR B  59      20.173   5.267 -18.017  1.00 38.45           O  
ANISOU 1268  O   TYR B  59     5921   4925   3761   -610   -379    215       O  
ATOM   1269  CB  TYR B  59      18.298   7.542 -18.416  1.00 38.95           C  
ANISOU 1269  CB  TYR B  59     5530   5018   4248   -298   -361    276       C  
ATOM   1270  CG  TYR B  59      17.083   8.422 -18.353  1.00 40.12           C  
ANISOU 1270  CG  TYR B  59     5508   5071   4663   -335   -226    160       C  
ATOM   1271  CD1 TYR B  59      16.355   8.531 -17.185  1.00 39.31           C  
ANISOU 1271  CD1 TYR B  59     5267   4952   4717   -153   -216    144       C  
ATOM   1272  CD2 TYR B  59      16.688   9.192 -19.462  1.00 40.34           C  
ANISOU 1272  CD2 TYR B  59     5278   5131   4915   -115   -254    145       C  
ATOM   1273  CE1 TYR B  59      15.253   9.358 -17.103  1.00 40.76           C  
ANISOU 1273  CE1 TYR B  59     5329   5180   4976    -24   -224    163       C  
ATOM   1274  CE2 TYR B  59      15.584  10.038 -19.387  1.00 40.26           C  
ANISOU 1274  CE2 TYR B  59     5230   5172   4894     18   -144    213       C  
ATOM   1275  CZ  TYR B  59      14.877  10.112 -18.207  1.00 42.57           C  
ANISOU 1275  CZ  TYR B  59     5653   5421   5098   -127   -187    154       C  
ATOM   1276  OH  TYR B  59      13.771  10.923 -18.087  1.00 42.43           O  
ANISOU 1276  OH  TYR B  59     5657   5274   5190     15   -186    298       O  
ATOM   1277  N   ASP B  60      19.746   5.063 -20.226  1.00 39.76           N  
ANISOU 1277  N   ASP B  60     6275   5036   3797   -687   -296    122       N  
ATOM   1278  CA  ASP B  60      21.047   4.467 -20.542  1.00 40.70           C  
ANISOU 1278  CA  ASP B  60     6504   5108   3851   -691   -137     31       C  
ATOM   1279  C   ASP B  60      22.056   5.474 -21.040  1.00 40.28           C  
ANISOU 1279  C   ASP B  60     6611   5010   3681   -702    -41    -31       C  
ATOM   1280  O   ASP B  60      21.701   6.571 -21.469  1.00 39.79           O  
ANISOU 1280  O   ASP B  60     6639   4994   3486   -764    -35     -1       O  
ATOM   1281  CB  ASP B  60      20.902   3.333 -21.552  1.00 41.32           C  
ANISOU 1281  CB  ASP B  60     6387   5160   4150   -534   -111      1       C  
ATOM   1282  CG  ASP B  60      19.853   2.340 -21.135  1.00 44.44           C  
ANISOU 1282  CG  ASP B  60     6431   5527   4926   -407    -64    -44       C  
ATOM   1283  OD1 ASP B  60      18.913   2.112 -21.909  1.00 48.01           O  
ANISOU 1283  OD1 ASP B  60     6477   6235   5528   -319   -219   -105       O  
ATOM   1284  OD2 ASP B  60      19.857   1.766 -20.032  1.00 45.31           O  
ANISOU 1284  OD2 ASP B  60     6477   5690   5048   -316    -48     37       O  
ATOM   1285  N   GLN B  61      23.323   5.084 -20.936  1.00 39.84           N  
ANISOU 1285  N   GLN B  61     6611   4866   3659   -633     73    -33       N  
ATOM   1286  CA  GLN B  61      24.460   5.850 -21.433  1.00 39.24           C  
ANISOU 1286  CA  GLN B  61     6444   4679   3785   -512    109    -66       C  
ATOM   1287  C   GLN B  61      24.390   7.279 -20.941  1.00 36.94           C  
ANISOU 1287  C   GLN B  61     6120   4415   3498   -433    152    -15       C  
ATOM   1288  O   GLN B  61      24.487   8.227 -21.720  1.00 36.18           O  
ANISOU 1288  O   GLN B  61     6071   4287   3386   -448    146    -19       O  
ATOM   1289  CB  GLN B  61      24.543   5.779 -22.967  1.00 40.28           C  
ANISOU 1289  CB  GLN B  61     6351   4975   3978   -429     91      0       C  
ATOM   1290  CG  GLN B  61      24.377   4.356 -23.535  1.00 45.58           C  
ANISOU 1290  CG  GLN B  61     6721   5477   5119   -278    105   -134       C  
ATOM   1291  CD  GLN B  61      23.716   4.358 -24.916  1.00 52.79           C  
ANISOU 1291  CD  GLN B  61     7221   6729   6108    -76    -52   -113       C  
ATOM   1292  OE1 GLN B  61      24.036   5.213 -25.753  1.00 55.32           O  
ANISOU 1292  OE1 GLN B  61     7534   6931   6551   -123     93     35       O  
ATOM   1293  NE2 GLN B  61      22.791   3.416 -25.154  1.00 54.14           N  
ANISOU 1293  NE2 GLN B  61     7152   6783   6634   -222     24    -72       N  
ATOM   1294  N   ILE B  62      24.206   7.421 -19.630  1.00 33.78           N  
ANISOU 1294  N   ILE B  62     5607   3950   3278   -280    193     21       N  
ATOM   1295  CA  ILE B  62      24.211   8.730 -18.980  1.00 30.86           C  
ANISOU 1295  CA  ILE B  62     5039   3515   3169   -141    173     84       C  
ATOM   1296  C   ILE B  62      25.604   8.965 -18.380  1.00 29.21           C  
ANISOU 1296  C   ILE B  62     4815   3221   3061    -53    245    104       C  
ATOM   1297  O   ILE B  62      26.151   8.070 -17.711  1.00 27.39           O  
ANISOU 1297  O   ILE B  62     4496   3015   2895    -45    309     59       O  
ATOM   1298  CB  ILE B  62      23.085   8.824 -17.889  1.00 30.48           C  
ANISOU 1298  CB  ILE B  62     4798   3511   3269    -77    123     69       C  
ATOM   1299  CG1 ILE B  62      21.669   8.836 -18.512  1.00 32.14           C  
ANISOU 1299  CG1 ILE B  62     4809   3838   3562    -28    142     56       C  
ATOM   1300  CG2 ILE B  62      23.268  10.036 -17.000  1.00 30.26           C  
ANISOU 1300  CG2 ILE B  62     4627   3561   3309    -91    127     21       C  
ATOM   1301  CD1 ILE B  62      21.412   9.932 -19.572  1.00 31.99           C  
ANISOU 1301  CD1 ILE B  62     4264   3863   4028    182     65    319       C  
ATOM   1302  N   LEU B  63      26.154  10.160 -18.641  1.00 27.17           N  
ANISOU 1302  N   LEU B  63     4489   2905   2928     16    252    132       N  
ATOM   1303  CA  LEU B  63      27.404  10.630 -18.067  1.00 26.14           C  
ANISOU 1303  CA  LEU B  63     4166   2768   2997     82    263    170       C  
ATOM   1304  C   LEU B  63      27.197  11.163 -16.656  1.00 25.44           C  
ANISOU 1304  C   LEU B  63     3988   2645   3033     48    247    176       C  
ATOM   1305  O   LEU B  63      26.355  12.029 -16.433  1.00 25.07           O  
ANISOU 1305  O   LEU B  63     3946   2590   2989     60    226    224       O  
ATOM   1306  CB  LEU B  63      28.019  11.736 -18.943  1.00 25.89           C  
ANISOU 1306  CB  LEU B  63     4039   2805   2991     86    151    157       C  
ATOM   1307  CG  LEU B  63      29.313  12.386 -18.458  1.00 26.20           C  
ANISOU 1307  CG  LEU B  63     3945   2833   3174     71    206    155       C  
ATOM   1308  CD1 LEU B  63      30.425  11.362 -18.353  1.00 26.51           C  
ANISOU 1308  CD1 LEU B  63     3657   3117   3298     34    147    120       C  
ATOM   1309  CD2 LEU B  63      29.724  13.484 -19.399  1.00 26.57           C  
ANISOU 1309  CD2 LEU B  63     4001   2937   3154     46    280     58       C  
ATOM   1310  N   ILE B  64      27.963  10.641 -15.703  1.00 25.08           N  
ANISOU 1310  N   ILE B  64     3723   2685   3118     63    221    222       N  
ATOM   1311  CA  ILE B  64      27.961  11.134 -14.327  1.00 25.96           C  
ANISOU 1311  CA  ILE B  64     3706   2888   3267     61    200    208       C  
ATOM   1312  C   ILE B  64      29.387  11.382 -13.838  1.00 26.09           C  
ANISOU 1312  C   ILE B  64     3654   2866   3391     29    248    273       C  
ATOM   1313  O   ILE B  64      30.297  10.574 -14.050  1.00 26.18           O  
ANISOU 1313  O   ILE B  64     3589   2933   3424    174    260    271       O  
ATOM   1314  CB  ILE B  64      27.282  10.132 -13.354  1.00 25.68           C  
ANISOU 1314  CB  ILE B  64     3634   2964   3158     36    189    228       C  
ATOM   1315  CG1 ILE B  64      25.862   9.800 -13.768  1.00 27.18           C  
ANISOU 1315  CG1 ILE B  64     3791   3261   3274   -114    212    202       C  
ATOM   1316  CG2 ILE B  64      27.153  10.732 -11.958  1.00 25.75           C  
ANISOU 1316  CG2 ILE B  64     3789   2807   3185     90    -41    187       C  
ATOM   1317  CD1 ILE B  64      24.929   9.460 -12.504  1.00 28.47           C  
ANISOU 1317  CD1 ILE B  64     3889   3453   3475     32    288    174       C  
ATOM   1318  N   GLU B  65      29.587  12.478 -13.146  1.00 25.87           N  
ANISOU 1318  N   GLU B  65     3563   2744   3520    -75    244    284       N  
ATOM   1319  CA  GLU B  65      30.844  12.673 -12.476  1.00 28.10           C  
ANISOU 1319  CA  GLU B  65     3616   3028   4030   -121    202    371       C  
ATOM   1320  C   GLU B  65      30.640  12.418 -10.976  1.00 28.62           C  
ANISOU 1320  C   GLU B  65     3653   3062   4156   -131    153    331       C  
ATOM   1321  O   GLU B  65      29.797  13.073 -10.349  1.00 28.54           O  
ANISOU 1321  O   GLU B  65     3750   3002   4089    -99    111    252       O  
ATOM   1322  CB  GLU B  65      31.343  14.076 -12.743  1.00 28.71           C  
ANISOU 1322  CB  GLU B  65     3611   3040   4255   -210    197    387       C  
ATOM   1323  CG  GLU B  65      32.826  14.263 -12.478  1.00 33.79           C  
ANISOU 1323  CG  GLU B  65     4022   3819   4997   -270    149    478       C  
ATOM   1324  CD  GLU B  65      33.439  15.301 -13.405  1.00 39.19           C  
ANISOU 1324  CD  GLU B  65     4658   4365   5867   -473    110    737       C  
ATOM   1325  OE1 GLU B  65      34.671  15.568 -13.282  1.00 43.33           O  
ANISOU 1325  OE1 GLU B  65     4895   5058   6509   -477     42    674       O  
ATOM   1326  OE2 GLU B  65      32.700  15.843 -14.287  1.00 41.58           O  
ANISOU 1326  OE2 GLU B  65     4765   4733   6299   -369     47    630       O  
ATOM   1327  N   ILE B  66      31.352  11.418 -10.434  1.00 28.70           N  
ANISOU 1327  N   ILE B  66     3586   3081   4235   -129     90    344       N  
ATOM   1328  CA  ILE B  66      31.259  11.038  -9.010  1.00 28.69           C  
ANISOU 1328  CA  ILE B  66     3511   3100   4290   -187     73    269       C  
ATOM   1329  C   ILE B  66      32.588  11.372  -8.386  1.00 30.51           C  
ANISOU 1329  C   ILE B  66     3662   3400   4531   -192    -13    257       C  
ATOM   1330  O   ILE B  66      33.555  10.681  -8.635  1.00 30.61           O  
ANISOU 1330  O   ILE B  66     3728   3361   4542   -219    -59    249       O  
ATOM   1331  CB  ILE B  66      30.992   9.505  -8.867  1.00 27.49           C  
ANISOU 1331  CB  ILE B  66     3337   2988   4116   -150     69    245       C  
ATOM   1332  CG1 ILE B  66      29.762   9.096  -9.690  1.00 26.29           C  
ANISOU 1332  CG1 ILE B  66     3344   2804   3841   -176    188    104       C  
ATOM   1333  CG2 ILE B  66      30.877   9.084  -7.361  1.00 26.47           C  
ANISOU 1333  CG2 ILE B  66     3219   2837   4000   -100     80    207       C  
ATOM   1334  CD1 ILE B  66      29.703   7.616 -10.027  1.00 25.23           C  
ANISOU 1334  CD1 ILE B  66     3180   2699   3706    -87    148     -7       C  
HETATM 1335  N  ACME B  67      32.623  12.436  -7.594  0.50 32.36           N  
ANISOU 1335  N  ACME B  67     3908   3719   4665   -172    -10    214       N  
HETATM 1336  N  BCME B  67      32.667  12.440  -7.595  0.50 32.24           N  
ANISOU 1336  N  BCME B  67     3891   3710   4646   -178     -9    217       N  
HETATM 1337  CA ACME B  67      33.845  12.883  -6.964  0.50 34.46           C  
ANISOU 1337  CA ACME B  67     4109   4049   4935   -238    -37    197       C  
HETATM 1338  CA BCME B  67      33.917  12.839  -6.926  0.50 34.23           C  
ANISOU 1338  CA BCME B  67     4089   4030   4885   -242    -36    208       C  
HETATM 1339  CB ACME B  67      34.182  11.863  -5.886  0.50 35.05           C  
ANISOU 1339  CB ACME B  67     4241   4144   4931   -189    -10    182       C  
HETATM 1340  CB BCME B  67      34.532  11.645  -6.196  0.50 34.55           C  
ANISOU 1340  CB BCME B  67     4198   4079   4850   -210    -12    173       C  
HETATM 1341  SG ACME B  67      34.590  12.653  -4.377  0.50 37.82           S  
ANISOU 1341  SG ACME B  67     4715   4492   5162   -188    -48     27       S  
HETATM 1342  SG BCME B  67      33.957  11.525  -4.547  0.50 36.75           S  
ANISOU 1342  SG BCME B  67     4688   4449   4826   -235    -12     61       S  
HETATM 1343  SD ACME B  67      33.718  14.449  -4.194  0.50 39.92           S  
ANISOU 1343  SD ACME B  67     4959   4841   5368    103   -102     54       S  
HETATM 1344  SD BCME B  67      33.914  14.113  -4.236  0.00 26.00           S  
ANISOU 1344  SD BCME B  67     3036   1831   5012  -1526  -1088    -63       S  
HETATM 1345  CE ACME B  67      32.860  14.608  -2.656  0.50 38.89           C  
ANISOU 1345  CE ACME B  67     4922   4621   5231   -121    -44    -17       C  
HETATM 1346  CE BCME B  67      33.001  14.521  -2.774  0.00 26.17           C  
ANISOU 1346  CE BCME B  67     3488   1599   4857  -1462  -1293   -491       C  
HETATM 1347  CZ ACME B  67      33.740  14.173  -1.486  0.50 37.72           C  
ANISOU 1347  CZ ACME B  67     4766   4905   4659    -34     29     87       C  
HETATM 1348  CZ BCME B  67      33.810  14.153  -1.529  0.00 27.87           C  
ANISOU 1348  CZ BCME B  67     3635   1961   4990  -1596  -1556   -595       C  
HETATM 1349  OH ACME B  67      32.977  14.159  -0.287  0.50 39.86           O  
ANISOU 1349  OH ACME B  67     5231   4889   5022    -22   -192    -87       O  
HETATM 1350  OH BCME B  67      32.967  14.081  -0.386  0.00 27.41           O  
ANISOU 1350  OH BCME B  67     3914   1818   4679  -1424  -1625   -926       O  
HETATM 1351  C  ACME B  67      34.954  12.980  -8.016  0.50 35.20           C  
ANISOU 1351  C  ACME B  67     4145   4169   5058   -267    -24    246       C  
HETATM 1352  C  BCME B  67      35.028  13.326  -7.869  0.50 35.15           C  
ANISOU 1352  C  BCME B  67     4126   4171   5056   -266    -23    263       C  
HETATM 1353  O  ACME B  67      36.019  12.371  -7.874  0.50 35.51           O  
ANISOU 1353  O  ACME B  67     4223   4210   5057   -243    -50    164       O  
HETATM 1354  O  BCME B  67      36.196  13.350  -7.484  0.50 35.64           O  
ANISOU 1354  O  BCME B  67     4191   4268   5082   -238    -80    234       O  
ATOM   1355  N   GLY B  68      34.682  13.725  -9.087  1.00 35.89           N  
ANISOU 1355  N   GLY B  68     4110   4269   5256   -358    -40    355       N  
ATOM   1356  CA  GLY B  68      35.698  14.029 -10.106  1.00 36.85           C  
ANISOU 1356  CA  GLY B  68     4071   4459   5469   -428     60    488       C  
ATOM   1357  C   GLY B  68      36.012  12.859 -11.034  1.00 36.81           C  
ANISOU 1357  C   GLY B  68     3974   4476   5535   -409    167    605       C  
ATOM   1358  O   GLY B  68      36.771  13.024 -11.981  1.00 38.74           O  
ANISOU 1358  O   GLY B  68     4168   4758   5793   -461    164    548       O  
ATOM   1359  N   HIS B  69      35.443  11.688 -10.776  1.00 35.36           N  
ANISOU 1359  N   HIS B  69     3754   4354   5324   -348    209    670       N  
ATOM   1360  CA  HIS B  69      35.611  10.512 -11.640  1.00 34.76           C  
ANISOU 1360  CA  HIS B  69     3668   4354   5184   -231    275    696       C  
ATOM   1361  C   HIS B  69      34.424  10.343 -12.574  1.00 33.70           C  
ANISOU 1361  C   HIS B  69     3679   4164   4961   -134    336    694       C  
ATOM   1362  O   HIS B  69      33.309  10.101 -12.114  1.00 33.24           O  
ANISOU 1362  O   HIS B  69     3624   4047   4959   -126    224    662       O  
ATOM   1363  CB  HIS B  69      35.731   9.233 -10.811  1.00 34.59           C  
ANISOU 1363  CB  HIS B  69     3615   4356   5169   -191    219    676       C  
ATOM   1364  CG  HIS B  69      36.943   9.188  -9.936  1.00 37.27           C  
ANISOU 1364  CG  HIS B  69     3831   4828   5502   -153    129    596       C  
ATOM   1365  ND1 HIS B  69      37.097  10.001  -8.831  1.00 38.00           N  
ANISOU 1365  ND1 HIS B  69     3834   4937   5666    -44     47    542       N  
ATOM   1366  CD2 HIS B  69      38.048   8.402  -9.986  1.00 38.13           C  
ANISOU 1366  CD2 HIS B  69     3721   5164   5601   -127    180    532       C  
ATOM   1367  CE1 HIS B  69      38.254   9.736  -8.251  1.00 40.08           C  
ANISOU 1367  CE1 HIS B  69     3990   5347   5891   -180     66    549       C  
ATOM   1368  NE2 HIS B  69      38.846   8.764  -8.928  1.00 40.21           N  
ANISOU 1368  NE2 HIS B  69     3842   5475   5960   -106    146    562       N  
ATOM   1369  N   LYS B  70      34.671  10.444 -13.875  1.00 33.48           N  
ANISOU 1369  N   LYS B  70     3757   4110   4854    -30    413    677       N  
ATOM   1370  CA  LYS B  70      33.631  10.253 -14.901  1.00 33.00           C  
ANISOU 1370  CA  LYS B  70     3805   4067   4667     44    502    641       C  
ATOM   1371  C   LYS B  70      33.275   8.789 -15.116  1.00 31.60           C  
ANISOU 1371  C   LYS B  70     3734   3898   4374    120    511    569       C  
ATOM   1372  O   LYS B  70      34.158   7.937 -15.249  1.00 31.48           O  
ANISOU 1372  O   LYS B  70     3643   3873   4444    120    472    466       O  
ATOM   1373  CB  LYS B  70      34.080  10.853 -16.225  1.00 33.62           C  
ANISOU 1373  CB  LYS B  70     3936   4187   4650     13    484    728       C  
ATOM   1374  CG  LYS B  70      34.192  12.361 -16.225  1.00 35.96           C  
ANISOU 1374  CG  LYS B  70     4162   4414   5087   -132    507    706       C  
ATOM   1375  CD  LYS B  70      34.809  12.813 -17.540  1.00 40.18           C  
ANISOU 1375  CD  LYS B  70     4768   4949   5547   -204    493    923       C  
ATOM   1376  CE  LYS B  70      35.711  14.037 -17.357  1.00 43.71           C  
ANISOU 1376  CE  LYS B  70     5065   5357   6184   -297    465    960       C  
ATOM   1377  NZ  LYS B  70      34.959  15.228 -16.836  1.00 43.66           N  
ANISOU 1377  NZ  LYS B  70     5016   5166   6404   -296    463    902       N  
ATOM   1378  N   ALA B  71      31.980   8.513 -15.176  1.00 29.57           N  
ANISOU 1378  N   ALA B  71     3637   3642   3954    272    627    450       N  
ATOM   1379  CA  ALA B  71      31.447   7.191 -15.503  1.00 28.78           C  
ANISOU 1379  CA  ALA B  71     3769   3490   3677    301    609    457       C  
ATOM   1380  C   ALA B  71      30.285   7.351 -16.478  1.00 28.69           C  
ANISOU 1380  C   ALA B  71     3906   3436   3559    319    596    418       C  
ATOM   1381  O   ALA B  71      29.639   8.401 -16.507  1.00 28.57           O  
ANISOU 1381  O   ALA B  71     3908   3378   3570    338    575    348       O  
ATOM   1382  CB  ALA B  71      31.015   6.468 -14.242  1.00 28.70           C  
ANISOU 1382  CB  ALA B  71     3813   3441   3650    234    542    383       C  
ATOM   1383  N   ILE B  72      30.042   6.352 -17.323  1.00 28.54           N  
ANISOU 1383  N   ILE B  72     4112   3338   3394    403    579    355       N  
ATOM   1384  CA  ILE B  72      28.858   6.363 -18.199  1.00 28.98           C  
ANISOU 1384  CA  ILE B  72     4334   3377   3298    430    497    375       C  
ATOM   1385  C   ILE B  72      28.029   5.125 -17.855  1.00 27.66           C  
ANISOU 1385  C   ILE B  72     4256   3178   3074    440    419    317       C  
ATOM   1386  O   ILE B  72      28.566   4.022 -17.756  1.00 27.24           O  
ANISOU 1386  O   ILE B  72     4131   3114   3105    474    528    243       O  
ATOM   1387  CB  ILE B  72      29.213   6.452 -19.742  1.00 29.62           C  
ANISOU 1387  CB  ILE B  72     4409   3481   3361    389    482    392       C  
ATOM   1388  CG1 ILE B  72      29.496   7.897 -20.152  1.00 31.58           C  
ANISOU 1388  CG1 ILE B  72     4685   3756   3557    382    547    380       C  
ATOM   1389  CG2 ILE B  72      28.037   5.989 -20.634  1.00 30.10           C  
ANISOU 1389  CG2 ILE B  72     4523   3637   3277    365    476    398       C  
ATOM   1390  CD1 ILE B  72      29.994   8.074 -21.597  1.00 31.01           C  
ANISOU 1390  CD1 ILE B  72     4661   3690   3430    449    461    484       C  
ATOM   1391  N   GLY B  73      26.730   5.299 -17.629  1.00 26.33           N  
ANISOU 1391  N   GLY B  73     4210   2945   2847    409    334    242       N  
ATOM   1392  CA  GLY B  73      25.935   4.165 -17.209  1.00 25.20           C  
ANISOU 1392  CA  GLY B  73     4110   2741   2722    324    181    193       C  
ATOM   1393  C   GLY B  73      24.454   4.373 -17.208  1.00 25.02           C  
ANISOU 1393  C   GLY B  73     4168   2642   2694    224     79    179       C  
ATOM   1394  O   GLY B  73      23.953   5.417 -17.596  1.00 24.89           O  
ANISOU 1394  O   GLY B  73     4076   2544   2838    263    150    180       O  
ATOM   1395  N   THR B  74      23.751   3.332 -16.787  1.00 24.89           N  
ANISOU 1395  N   THR B  74     4153   2654   2648    124    -34    125       N  
ATOM   1396  CA  THR B  74      22.317   3.383 -16.606  1.00 24.41           C  
ANISOU 1396  CA  THR B  74     4038   2545   2692     58   -120     88       C  
ATOM   1397  C   THR B  74      22.026   4.032 -15.273  1.00 23.56           C  
ANISOU 1397  C   THR B  74     3794   2431   2726     68   -125    123       C  
ATOM   1398  O   THR B  74      22.609   3.682 -14.221  1.00 22.88           O  
ANISOU 1398  O   THR B  74     3679   2367   2648     61   -101    124       O  
ATOM   1399  CB  THR B  74      21.750   1.950 -16.630  1.00 25.31           C  
ANISOU 1399  CB  THR B  74     4169   2668   2777     22   -131     26       C  
ATOM   1400  OG1 THR B  74      21.867   1.434 -17.958  1.00 26.56           O  
ANISOU 1400  OG1 THR B  74     4376   2808   2905    -68   -211    -70       O  
ATOM   1401  CG2 THR B  74      20.236   1.952 -16.353  1.00 24.79           C  
ANISOU 1401  CG2 THR B  74     3993   2713   2710    -19   -295     21       C  
ATOM   1402  N   VAL B  75      21.113   4.987 -15.325  1.00 22.75           N  
ANISOU 1402  N   VAL B  75     3536   2341   2764     20   -155    203       N  
ATOM   1403  CA  VAL B  75      20.724   5.741 -14.176  1.00 22.42           C  
ANISOU 1403  CA  VAL B  75     3357   2372   2786     26   -181    145       C  
ATOM   1404  C   VAL B  75      19.212   5.630 -14.126  1.00 22.88           C  
ANISOU 1404  C   VAL B  75     3379   2474   2840     -9   -244    192       C  
ATOM   1405  O   VAL B  75      18.550   5.785 -15.161  1.00 23.83           O  
ANISOU 1405  O   VAL B  75     3374   2703   2975     15   -264    233       O  
ATOM   1406  CB  VAL B  75      21.186   7.204 -14.357  1.00 22.58           C  
ANISOU 1406  CB  VAL B  75     3343   2405   2832     23    -97    121       C  
ATOM   1407  CG1 VAL B  75      20.409   8.161 -13.445  1.00 24.20           C  
ANISOU 1407  CG1 VAL B  75     3450   2474   3269     39     -1     72       C  
ATOM   1408  CG2 VAL B  75      22.685   7.301 -14.078  1.00 22.60           C  
ANISOU 1408  CG2 VAL B  75     3346   2507   2732    -29    -78    140       C  
ATOM   1409  N   LEU B  76      18.668   5.329 -12.948  1.00 22.46           N  
ANISOU 1409  N   LEU B  76     3247   2417   2866    -25   -289    240       N  
ATOM   1410  CA  LEU B  76      17.224   5.273 -12.739  1.00 22.74           C  
ANISOU 1410  CA  LEU B  76     3171   2497   2969    -11   -325    286       C  
ATOM   1411  C   LEU B  76      16.762   6.538 -12.025  1.00 23.12           C  
ANISOU 1411  C   LEU B  76     3095   2525   3164     62   -293    343       C  
ATOM   1412  O   LEU B  76      17.469   7.082 -11.139  1.00 22.25           O  
ANISOU 1412  O   LEU B  76     2870   2398   3183    116   -244    298       O  
ATOM   1413  CB  LEU B  76      16.814   4.016 -11.924  1.00 22.50           C  
ANISOU 1413  CB  LEU B  76     3212   2446   2888    -56   -373    259       C  
ATOM   1414  CG  LEU B  76      17.418   2.678 -12.354  1.00 22.96           C  
ANISOU 1414  CG  LEU B  76     3386   2487   2848   -176   -404    242       C  
ATOM   1415  CD1 LEU B  76      16.951   1.579 -11.442  1.00 22.80           C  
ANISOU 1415  CD1 LEU B  76     3183   2513   2965   -209   -346    204       C  
ATOM   1416  CD2 LEU B  76      17.030   2.354 -13.822  1.00 24.51           C  
ANISOU 1416  CD2 LEU B  76     3611   2779   2920   -222   -352    237       C  
ATOM   1417  N   VAL B  77      15.577   7.013 -12.393  1.00 24.02           N  
ANISOU 1417  N   VAL B  77     3033   2734   3360     98   -264    472       N  
ATOM   1418  CA  VAL B  77      15.072   8.229 -11.797  1.00 25.36           C  
ANISOU 1418  CA  VAL B  77     3104   2919   3610    183   -246    495       C  
ATOM   1419  C   VAL B  77      13.667   7.978 -11.314  1.00 26.69           C  
ANISOU 1419  C   VAL B  77     3155   3145   3840    230   -251    516       C  
ATOM   1420  O   VAL B  77      12.860   7.386 -12.023  1.00 27.22           O  
ANISOU 1420  O   VAL B  77     3132   3302   3905    288   -338    480       O  
ATOM   1421  CB  VAL B  77      15.121   9.386 -12.820  1.00 26.49           C  
ANISOU 1421  CB  VAL B  77     3268   3033   3763    161   -162    461       C  
ATOM   1422  CG1 VAL B  77      14.546  10.631 -12.253  1.00 26.58           C  
ANISOU 1422  CG1 VAL B  77     3347   2942   3807    210   -163    386       C  
ATOM   1423  CG2 VAL B  77      16.566   9.615 -13.272  1.00 26.08           C  
ANISOU 1423  CG2 VAL B  77     3186   2979   3744    137   -218    554       C  
ATOM   1424  N   GLY B  78      13.386   8.383 -10.082  1.00 27.74           N  
ANISOU 1424  N   GLY B  78     3132   3382   4022    261   -206    554       N  
ATOM   1425  CA  GLY B  78      12.093   8.173  -9.487  1.00 29.47           C  
ANISOU 1425  CA  GLY B  78     3177   3691   4328    356    -75    598       C  
ATOM   1426  C   GLY B  78      12.054   8.643  -8.048  1.00 30.67           C  
ANISOU 1426  C   GLY B  78     3192   3924   4536    431     12    609       C  
ATOM   1427  O   GLY B  78      12.949   9.348  -7.594  1.00 30.07           O  
ANISOU 1427  O   GLY B  78     3128   3748   4546    463      4    582       O  
ATOM   1428  N   PRO B  79      11.012   8.241  -7.323  1.00 31.91           N  
ANISOU 1428  N   PRO B  79     3247   4156   4719    473    115    644       N  
ATOM   1429  CA  PRO B  79      10.706   8.844  -6.036  1.00 32.07           C  
ANISOU 1429  CA  PRO B  79     3276   4233   4674    475    148    618       C  
ATOM   1430  C   PRO B  79      11.522   8.257  -4.902  1.00 31.60           C  
ANISOU 1430  C   PRO B  79     3258   4127   4621    513    220    556       C  
ATOM   1431  O   PRO B  79      10.992   7.555  -4.048  1.00 32.29           O  
ANISOU 1431  O   PRO B  79     3375   4246   4646    418    261    561       O  
ATOM   1432  CB  PRO B  79       9.201   8.536  -5.848  1.00 32.85           C  
ANISOU 1432  CB  PRO B  79     3253   4425   4803    459    176    606       C  
ATOM   1433  CG  PRO B  79       8.793   7.660  -7.011  1.00 32.92           C  
ANISOU 1433  CG  PRO B  79     3289   4380   4836    427     99    644       C  
ATOM   1434  CD  PRO B  79      10.029   7.204  -7.688  1.00 32.16           C  
ANISOU 1434  CD  PRO B  79     3292   4167   4761    431    120    574       C  
ATOM   1435  N   THR B  80      12.820   8.539  -4.887  1.00 30.93           N  
ANISOU 1435  N   THR B  80     3387   3913   4450    546    211    436       N  
ATOM   1436  CA  THR B  80      13.679   8.040  -3.816  1.00 28.69           C  
ANISOU 1436  CA  THR B  80     3244   3577   4078    559    260    297       C  
ATOM   1437  C   THR B  80      13.953   9.255  -2.946  1.00 28.90           C  
ANISOU 1437  C   THR B  80     3391   3597   3994    627    363    220       C  
ATOM   1438  O   THR B  80      13.947  10.367  -3.438  1.00 29.12           O  
ANISOU 1438  O   THR B  80     3446   3631   3986    646    354    250       O  
ATOM   1439  CB  THR B  80      14.943   7.382  -4.398  1.00 27.78           C  
ANISOU 1439  CB  THR B  80     3174   3419   3959    543    214    279       C  
ATOM   1440  OG1 THR B  80      15.863   7.081  -3.331  1.00 25.43           O  
ANISOU 1440  OG1 THR B  80     2967   2846   3848    344    109    262       O  
ATOM   1441  CG2 THR B  80      15.696   8.345  -5.313  1.00 25.07           C  
ANISOU 1441  CG2 THR B  80     2956   3085   3485    484    157    165       C  
ATOM   1442  N   PRO B  81      14.087   9.078  -1.643  1.00 29.43           N  
ANISOU 1442  N   PRO B  81     3546   3628   4005    695    391    168       N  
ATOM   1443  CA  PRO B  81      14.370  10.225  -0.753  1.00 28.93           C  
ANISOU 1443  CA  PRO B  81     3628   3463   3900    752    453     47       C  
ATOM   1444  C   PRO B  81      15.829  10.666  -0.727  1.00 28.39           C  
ANISOU 1444  C   PRO B  81     3746   3245   3794    722    431     -7       C  
ATOM   1445  O   PRO B  81      16.174  11.685  -0.122  1.00 29.25           O  
ANISOU 1445  O   PRO B  81     3931   3282   3899    780    415    -98       O  
ATOM   1446  CB  PRO B  81      13.966   9.700   0.633  1.00 29.82           C  
ANISOU 1446  CB  PRO B  81     3680   3658   3989    739    460     64       C  
ATOM   1447  CG  PRO B  81      13.935   8.227   0.541  1.00 28.93           C  
ANISOU 1447  CG  PRO B  81     3528   3560   3902    720    479     85       C  
ATOM   1448  CD  PRO B  81      13.866   7.822  -0.907  1.00 29.45           C  
ANISOU 1448  CD  PRO B  81     3536   3591   4059    692    359    152       C  
ATOM   1449  N   VAL B  82      16.693   9.889  -1.367  1.00 26.63           N  
ANISOU 1449  N   VAL B  82     3598   2954   3563    627    333    -19       N  
ATOM   1450  CA  VAL B  82      18.117  10.161  -1.355  1.00 25.31           C  
ANISOU 1450  CA  VAL B  82     3486   2726   3402    572    263   -118       C  
ATOM   1451  C   VAL B  82      18.654   9.657  -2.683  1.00 23.35           C  
ANISOU 1451  C   VAL B  82     3219   2389   3262    512    241   -151       C  
ATOM   1452  O   VAL B  82      18.125   8.716  -3.242  1.00 22.18           O  
ANISOU 1452  O   VAL B  82     3002   2248   3177    519    267   -126       O  
ATOM   1453  CB  VAL B  82      18.819   9.526  -0.079  1.00 26.20           C  
ANISOU 1453  CB  VAL B  82     3579   2797   3576    542    217   -111       C  
ATOM   1454  CG1 VAL B  82      18.720   8.030  -0.079  1.00 26.70           C  
ANISOU 1454  CG1 VAL B  82     3793   2826   3525    425    158   -191       C  
ATOM   1455  CG2 VAL B  82      20.285   9.994   0.089  1.00 26.13           C  
ANISOU 1455  CG2 VAL B  82     3661   2876   3390    504    149   -178       C  
ATOM   1456  N   ASN B  83      19.632  10.369  -3.222  1.00 21.74           N  
ANISOU 1456  N   ASN B  83     3028   2119   3111    433    175   -187       N  
ATOM   1457  CA  ASN B  83      20.304   9.961  -4.437  1.00 20.07           C  
ANISOU 1457  CA  ASN B  83     2854   1870   2900    337    168   -174       C  
ATOM   1458  C   ASN B  83      21.226   8.770  -4.097  1.00 18.53           C  
ANISOU 1458  C   ASN B  83     2664   1688   2686    246    157   -130       C  
ATOM   1459  O   ASN B  83      21.950   8.824  -3.139  1.00 18.04           O  
ANISOU 1459  O   ASN B  83     2584   1593   2676    278    218    -69       O  
ATOM   1460  CB  ASN B  83      21.085  11.123  -5.035  1.00 20.32           C  
ANISOU 1460  CB  ASN B  83     3010   1762   2947    355    111   -175       C  
ATOM   1461  CG  ASN B  83      20.174  12.283  -5.484  1.00 22.51           C  
ANISOU 1461  CG  ASN B  83     3100   2114   3338    353     83   -205       C  
ATOM   1462  OD1 ASN B  83      19.188  12.071  -6.168  1.00 22.86           O  
ANISOU 1462  OD1 ASN B  83     3523   1972   3189    438    -33    -53       O  
ATOM   1463  ND2 ASN B  83      20.499  13.499  -5.061  1.00 22.00           N  
ANISOU 1463  ND2 ASN B  83     3060   1655   3641    345    235   -201       N  
ATOM   1464  N  AILE B  84      21.137   7.708  -4.893  0.50 18.14           N  
ANISOU 1464  N  AILE B  84     2632   1661   2598    228    157   -127       N  
ATOM   1465  N  BILE B  84      21.164   7.697  -4.876  0.50 18.16           N  
ANISOU 1465  N  BILE B  84     2628   1676   2593    234    161   -121       N  
ATOM   1466  CA AILE B  84      21.883   6.460  -4.661  0.50 17.45           C  
ANISOU 1466  CA AILE B  84     2510   1614   2505    178     70   -125       C  
ATOM   1467  CA BILE B  84      21.907   6.463  -4.555  0.50 17.41           C  
ANISOU 1467  CA BILE B  84     2497   1633   2482    191     83   -105       C  
ATOM   1468  C  AILE B  84      22.848   6.191  -5.805  0.50 16.98           C  
ANISOU 1468  C  AILE B  84     2425   1549   2475    165     74   -113       C  
ATOM   1469  C  BILE B  84      22.816   6.055  -5.713  0.50 16.97           C  
ANISOU 1469  C  BILE B  84     2430   1565   2453    191     81    -97       C  
ATOM   1470  O  AILE B  84      22.445   6.109  -6.974  0.50 16.82           O  
ANISOU 1470  O  AILE B  84     2314   1574   2501    171     58   -172       O  
ATOM   1471  O  BILE B  84      22.334   5.745  -6.808  0.50 16.82           O  
ANISOU 1471  O  BILE B  84     2352   1568   2469    245     77   -163       O  
ATOM   1472  CB AILE B  84      20.899   5.228  -4.511  0.50 17.50           C  
ANISOU 1472  CB AILE B  84     2488   1685   2474    183     59   -131       C  
ATOM   1473  CB BILE B  84      20.908   5.289  -4.212  0.50 17.55           C  
ANISOU 1473  CB BILE B  84     2478   1713   2474    203     87   -100       C  
ATOM   1474  CG1AILE B  84      19.947   5.400  -3.326  0.50 18.09           C  
ANISOU 1474  CG1AILE B  84     2549   1860   2462    168     42    -97       C  
ATOM   1475  CG1BILE B  84      20.105   5.589  -2.944  0.50 17.83           C  
ANISOU 1475  CG1BILE B  84     2542   1836   2393    179     53    -80       C  
ATOM   1476  CG2AILE B  84      21.665   3.912  -4.380  0.50 16.61           C  
ANISOU 1476  CG2AILE B  84     2489   1516   2304     64     -2   -156       C  
ATOM   1477  CG2BILE B  84      21.634   3.952  -4.077  0.50 16.69           C  
ANISOU 1477  CG2BILE B  84     2473   1550   2317     68     49   -123       C  
ATOM   1478  CD1AILE B  84      20.648   5.579  -2.019  0.50 18.73           C  
ANISOU 1478  CD1AILE B  84     2586   2122   2408    167     56   -194       C  
ATOM   1479  CD1BILE B  84      18.827   4.769  -2.825  0.50 17.14           C  
ANISOU 1479  CD1BILE B  84     2448   1743   2321    205     34    -40       C  
ATOM   1480  N   ILE B  85      24.127   6.062  -5.484  1.00 16.87           N  
ANISOU 1480  N   ILE B  85     2473   1481   2456    154     43    -81       N  
ATOM   1481  CA  ILE B  85      25.079   5.466  -6.456  1.00 16.62           C  
ANISOU 1481  CA  ILE B  85     2459   1530   2324    132    105   -188       C  
ATOM   1482  C   ILE B  85      25.201   3.980  -6.141  1.00 16.20           C  
ANISOU 1482  C   ILE B  85     2439   1513   2199    206     96   -206       C  
ATOM   1483  O   ILE B  85      25.672   3.604  -5.063  1.00 16.04           O  
ANISOU 1483  O   ILE B  85     2508   1381   2204    303    119   -253       O  
ATOM   1484  CB  ILE B  85      26.454   6.122  -6.423  1.00 17.47           C  
ANISOU 1484  CB  ILE B  85     2515   1691   2431    115    105   -220       C  
ATOM   1485  CG1 ILE B  85      26.324   7.661  -6.462  1.00 17.88           C  
ANISOU 1485  CG1 ILE B  85     2616   1673   2504     72    106    -86       C  
ATOM   1486  CG2 ILE B  85      27.353   5.579  -7.609  1.00 17.94           C  
ANISOU 1486  CG2 ILE B  85     2552   1811   2450     -9    182   -245       C  
ATOM   1487  CD1 ILE B  85      25.622   8.226  -7.730  1.00 18.21           C  
ANISOU 1487  CD1 ILE B  85     2527   1595   2797    -83   -109    -56       C  
ATOM   1488  N   GLY B  86      24.782   3.135  -7.083  1.00 16.15           N  
ANISOU 1488  N   GLY B  86     2419   1502   2216    162    103   -166       N  
ATOM   1489  CA  GLY B  86      24.767   1.691  -6.863  1.00 16.17           C  
ANISOU 1489  CA  GLY B  86     2624   1478   2042    267     48   -141       C  
ATOM   1490  C   GLY B  86      25.966   1.050  -7.527  1.00 17.08           C  
ANISOU 1490  C   GLY B  86     2773   1596   2118    242    -29   -101       C  
ATOM   1491  O   GLY B  86      26.828   1.728  -8.124  1.00 16.70           O  
ANISOU 1491  O   GLY B  86     2766   1483   2096    217    -49    -36       O  
ATOM   1492  N   ARG B  87      25.983  -0.274  -7.481  1.00 17.72           N  
ANISOU 1492  N   ARG B  87     3001   1576   2153    263     -1    -64       N  
ATOM   1493  CA  ARG B  87      27.149  -1.060  -7.899  1.00 18.76           C  
ANISOU 1493  CA  ARG B  87     3248   1705   2174    309     78    -71       C  
ATOM   1494  C   ARG B  87      27.465  -0.959  -9.378  1.00 19.18           C  
ANISOU 1494  C   ARG B  87     3321   1688   2277    304    111    -91       C  
ATOM   1495  O   ARG B  87      28.628  -0.986  -9.723  1.00 19.68           O  
ANISOU 1495  O   ARG B  87     3454   1714   2307    410    221    -79       O  
ATOM   1496  CB  ARG B  87      26.994  -2.517  -7.478  1.00 18.62           C  
ANISOU 1496  CB  ARG B  87     3186   1689   2198    376     -4    -76       C  
ATOM   1497  CG  ARG B  87      27.131  -2.740  -5.978  1.00 17.85           C  
ANISOU 1497  CG  ARG B  87     3037   1747   1998    231    217    -47       C  
ATOM   1498  CD  ARG B  87      27.182  -4.231  -5.604  1.00 19.54           C  
ANISOU 1498  CD  ARG B  87     3416   1776   2231    278     -6    -11       C  
ATOM   1499  NE  ARG B  87      25.956  -4.940  -6.041  1.00 21.00           N  
ANISOU 1499  NE  ARG B  87     3902   1856   2219    159   -171    -76       N  
ATOM   1500  CZ  ARG B  87      25.871  -5.701  -7.156  1.00 23.48           C  
ANISOU 1500  CZ  ARG B  87     4093   2145   2684    218   -116    -32       C  
ATOM   1501  NH1 ARG B  87      26.916  -5.871  -7.978  1.00 22.65           N  
ANISOU 1501  NH1 ARG B  87     4180   2034   2389    444    -25    -42       N  
ATOM   1502  NH2 ARG B  87      24.727  -6.291  -7.461  1.00 23.41           N  
ANISOU 1502  NH2 ARG B  87     4204   2063   2626     28   -295     -3       N  
ATOM   1503  N   ASN B  88      26.466  -0.774 -10.240  1.00 19.44           N  
ANISOU 1503  N   ASN B  88     3428   1698   2258    240     83    -57       N  
ATOM   1504  CA  ASN B  88      26.751  -0.598 -11.667  1.00 20.71           C  
ANISOU 1504  CA  ASN B  88     3532   1983   2355    277     93   -112       C  
ATOM   1505  C   ASN B  88      27.769   0.539 -11.959  1.00 21.72           C  
ANISOU 1505  C   ASN B  88     3521   2274   2455    316    181    -74       C  
ATOM   1506  O   ASN B  88      28.539   0.483 -12.912  1.00 22.72           O  
ANISOU 1506  O   ASN B  88     3604   2512   2516    342    190   -123       O  
ATOM   1507  CB  ASN B  88      25.444  -0.369 -12.454  1.00 20.54           C  
ANISOU 1507  CB  ASN B  88     3428   2009   2366    302     65    -94       C  
ATOM   1508  CG  ASN B  88      24.809   1.006 -12.197  1.00 20.76           C  
ANISOU 1508  CG  ASN B  88     3568   2081   2237    232     34   -128       C  
ATOM   1509  OD1 ASN B  88      24.520   1.374 -11.071  1.00 20.04           O  
ANISOU 1509  OD1 ASN B  88     3288   2134   2190     31   -182   -237       O  
ATOM   1510  ND2 ASN B  88      24.546   1.736 -13.267  1.00 21.52           N  
ANISOU 1510  ND2 ASN B  88     3587   2020   2566    236    -44    -39       N  
ATOM   1511  N   LEU B  89      27.754   1.579 -11.129  1.00 20.83           N  
ANISOU 1511  N   LEU B  89     3390   2072   2450    357    154    -60       N  
ATOM   1512  CA  LEU B  89      28.647   2.699 -11.311  1.00 20.58           C  
ANISOU 1512  CA  LEU B  89     3111   2219   2487    352    200     34       C  
ATOM   1513  C   LEU B  89      29.844   2.640 -10.406  1.00 20.51           C  
ANISOU 1513  C   LEU B  89     2981   2238   2573    409    249     24       C  
ATOM   1514  O   LEU B  89      30.884   3.129 -10.795  1.00 21.19           O  
ANISOU 1514  O   LEU B  89     3009   2441   2602    412    297     24       O  
ATOM   1515  CB  LEU B  89      27.899   4.041 -11.088  1.00 20.14           C  
ANISOU 1515  CB  LEU B  89     3015   2199   2437    332    183    -28       C  
ATOM   1516  CG  LEU B  89      26.874   4.383 -12.169  1.00 20.92           C  
ANISOU 1516  CG  LEU B  89     3066   2263   2617    355    182     60       C  
ATOM   1517  CD1 LEU B  89      26.289   5.739 -11.947  1.00 20.88           C  
ANISOU 1517  CD1 LEU B  89     3139   1927   2865    144     42    179       C  
ATOM   1518  CD2 LEU B  89      27.516   4.292 -13.523  1.00 21.90           C  
ANISOU 1518  CD2 LEU B  89     3319   2496   2503    342     71    106       C  
ATOM   1519  N   LEU B  90      29.682   2.109  -9.192  1.00 20.09           N  
ANISOU 1519  N   LEU B  90     2901   2241   2491    431    282     85       N  
ATOM   1520  CA  LEU B  90      30.808   1.911  -8.249  1.00 21.21           C  
ANISOU 1520  CA  LEU B  90     2947   2491   2619    392    305     25       C  
ATOM   1521  C   LEU B  90      31.946   1.061  -8.859  1.00 22.25           C  
ANISOU 1521  C   LEU B  90     3115   2602   2735    533    328     98       C  
ATOM   1522  O   LEU B  90      33.107   1.351  -8.624  1.00 21.38           O  
ANISOU 1522  O   LEU B  90     2977   2529   2615    508    269     90       O  
ATOM   1523  CB  LEU B  90      30.354   1.290  -6.905  1.00 20.17           C  
ANISOU 1523  CB  LEU B  90     2857   2394   2413    311    180    -60       C  
ATOM   1524  CG  LEU B  90      29.375   2.150  -6.062  1.00 19.01           C  
ANISOU 1524  CG  LEU B  90     2543   2186   2493    264    165    -95       C  
ATOM   1525  CD1 LEU B  90      28.938   1.370  -4.825  1.00 17.14           C  
ANISOU 1525  CD1 LEU B  90     2305   1901   2305    304     29   -134       C  
ATOM   1526  CD2 LEU B  90      30.015   3.495  -5.650  1.00 17.41           C  
ANISOU 1526  CD2 LEU B  90     2343   1851   2420    374    -60   -105       C  
ATOM   1527  N   THR B  91      31.615   0.031  -9.641  1.00 23.62           N  
ANISOU 1527  N   THR B  91     3378   2839   2758    624    369    109       N  
ATOM   1528  CA  THR B  91      32.674  -0.763 -10.313  1.00 25.98           C  
ANISOU 1528  CA  THR B  91     3714   3109   3047    699    411    156       C  
ATOM   1529  C   THR B  91      33.428   0.053 -11.345  1.00 27.52           C  
ANISOU 1529  C   THR B  91     3802   3443   3212    767    508    213       C  
ATOM   1530  O   THR B  91      34.620  -0.173 -11.533  1.00 28.66           O  
ANISOU 1530  O   THR B  91     3894   3620   3373    813    501    266       O  
ATOM   1531  CB  THR B  91      32.139  -2.000 -10.991  1.00 26.24           C  
ANISOU 1531  CB  THR B  91     3767   3152   3051    664    392     97       C  
ATOM   1532  OG1 THR B  91      31.096  -1.608 -11.891  1.00 25.92           O  
ANISOU 1532  OG1 THR B  91     3989   2950   2907    687    265    211       O  
ATOM   1533  CG2 THR B  91      31.461  -2.894  -9.971  1.00 25.71           C  
ANISOU 1533  CG2 THR B  91     3969   2966   2833    604    293     66       C  
ATOM   1534  N   GLN B  92      32.751   1.013 -11.996  1.00 28.47           N  
ANISOU 1534  N   GLN B  92     3897   3562   3356    746    523    265       N  
ATOM   1535  CA  GLN B  92      33.415   1.834 -13.012  1.00 29.37           C  
ANISOU 1535  CA  GLN B  92     3891   3729   3537    667    512    305       C  
ATOM   1536  C   GLN B  92      34.443   2.788 -12.445  1.00 29.46           C  
ANISOU 1536  C   GLN B  92     3688   3853   3652    607    549    340       C  
ATOM   1537  O   GLN B  92      35.426   3.087 -13.095  1.00 30.15           O  
ANISOU 1537  O   GLN B  92     3833   3953   3668    575    560    391       O  
ATOM   1538  CB  GLN B  92      32.407   2.591 -13.858  1.00 29.33           C  
ANISOU 1538  CB  GLN B  92     3954   3649   3541    739    500    247       C  
ATOM   1539  CG  GLN B  92      31.752   1.706 -14.899  1.00 31.74           C  
ANISOU 1539  CG  GLN B  92     4248   4018   3793    610    370    288       C  
ATOM   1540  CD  GLN B  92      30.865   2.494 -15.820  1.00 33.73           C  
ANISOU 1540  CD  GLN B  92     4570   4235   4010    502    386    342       C  
ATOM   1541  OE1 GLN B  92      29.622   2.342 -15.761  1.00 34.94           O  
ANISOU 1541  OE1 GLN B  92     4551   4356   4365    404    486     26       O  
ATOM   1542  NE2 GLN B  92      31.474   3.382 -16.661  1.00 34.27           N  
ANISOU 1542  NE2 GLN B  92     4736   4255   4030    410    444    306       N  
ATOM   1543  N   ILE B  93      34.226   3.256 -11.229  1.00 29.13           N  
ANISOU 1543  N   ILE B  93     3436   3889   3742    564    515    360       N  
ATOM   1544  CA  ILE B  93      35.175   4.165 -10.608  1.00 29.22           C  
ANISOU 1544  CA  ILE B  93     3358   3902   3839    458    453    380       C  
ATOM   1545  C   ILE B  93      36.202   3.408  -9.738  1.00 30.40           C  
ANISOU 1545  C   ILE B  93     3361   4141   4047    527    413    374       C  
ATOM   1546  O   ILE B  93      37.005   4.046  -9.050  1.00 31.82           O  
ANISOU 1546  O   ILE B  93     3343   4414   4331    483    387    371       O  
ATOM   1547  CB  ILE B  93      34.457   5.310  -9.838  1.00 28.71           C  
ANISOU 1547  CB  ILE B  93     3304   3808   3796    442    418    391       C  
ATOM   1548  CG1 ILE B  93      33.722   4.748  -8.596  1.00 28.57           C  
ANISOU 1548  CG1 ILE B  93     3262   3713   3879    314    435    249       C  
ATOM   1549  CG2 ILE B  93      33.509   6.047 -10.764  1.00 27.19           C  
ANISOU 1549  CG2 ILE B  93     3263   3338   3728    319    370    242       C  
ATOM   1550  CD1 ILE B  93      33.110   5.788  -7.712  1.00 27.84           C  
ANISOU 1550  CD1 ILE B  93     3342   3547   3686    194    259    103       C  
ATOM   1551  N   GLY B  94      36.167   2.075  -9.771  1.00 29.97           N  
ANISOU 1551  N   GLY B  94     3298   4120   3970    510    430    491       N  
ATOM   1552  CA  GLY B  94      37.167   1.260  -9.085  1.00 30.12           C  
ANISOU 1552  CA  GLY B  94     3294   4167   3982    549    393    434       C  
ATOM   1553  C   GLY B  94      36.948   1.249  -7.570  1.00 30.30           C  
ANISOU 1553  C   GLY B  94     3306   4174   4031    531    310    405       C  
ATOM   1554  O   GLY B  94      37.888   1.172  -6.775  1.00 30.52           O  
ANISOU 1554  O   GLY B  94     3331   4244   4019    564    306    513       O  
ATOM   1555  N   CYS B  95      35.697   1.341  -7.159  1.00 29.08           N  
ANISOU 1555  N   CYS B  95     3228   3959   3860    563    254    296       N  
ATOM   1556  CA  CYS B  95      35.408   1.390  -5.743  1.00 28.87           C  
ANISOU 1556  CA  CYS B  95     3236   3885   3844    581    175    287       C  
ATOM   1557  C   CYS B  95      35.437  -0.025  -5.070  1.00 28.08           C  
ANISOU 1557  C   CYS B  95     3159   3777   3730    600    158    277       C  
ATOM   1558  O   CYS B  95      34.819  -0.953  -5.586  1.00 27.38           O  
ANISOU 1558  O   CYS B  95     3130   3630   3642    607    168    288       O  
ATOM   1559  CB  CYS B  95      34.080   2.123  -5.556  1.00 28.08           C  
ANISOU 1559  CB  CYS B  95     3132   3831   3702    568    193    197       C  
ATOM   1560  SG  CYS B  95      33.695   2.340  -3.848  1.00 31.23           S  
ANISOU 1560  SG  CYS B  95     3535   4206   4124    493    124    130       S  
ATOM   1561  N   THR B  96      36.176  -0.182  -3.962  1.00 27.99           N  
ANISOU 1561  N   THR B  96     3178   3783   3672    633    131    283       N  
ATOM   1562  CA  THR B  96      36.240  -1.469  -3.214  1.00 28.73           C  
ANISOU 1562  CA  THR B  96     3223   3960   3733    683     76    281       C  
ATOM   1563  C   THR B  96      35.912  -1.276  -1.739  1.00 28.01           C  
ANISOU 1563  C   THR B  96     3093   3902   3646    715     28    244       C  
ATOM   1564  O   THR B  96      36.072  -0.180  -1.208  1.00 27.86           O  
ANISOU 1564  O   THR B  96     2993   3977   3615    636    -49    290       O  
ATOM   1565  CB  THR B  96      37.641  -2.193  -3.327  1.00 28.50           C  
ANISOU 1565  CB  THR B  96     3179   3952   3698    659     96    288       C  
ATOM   1566  OG1 THR B  96      38.653  -1.411  -2.685  1.00 28.88           O  
ANISOU 1566  OG1 THR B  96     3097   4182   3694    619    156    583       O  
ATOM   1567  CG2 THR B  96      38.115  -2.306  -4.758  1.00 30.33           C  
ANISOU 1567  CG2 THR B  96     3364   4185   3972    723    164    317       C  
ATOM   1568  N   LEU B  97      35.445  -2.327  -1.088  1.00 28.04           N  
ANISOU 1568  N   LEU B  97     3198   3773   3682    743    -36    211       N  
ATOM   1569  CA  LEU B  97      35.314  -2.342   0.376  1.00 29.01           C  
ANISOU 1569  CA  LEU B  97     3357   3925   3738    662   -125    190       C  
ATOM   1570  C   LEU B  97      36.509  -3.045   0.995  1.00 30.81           C  
ANISOU 1570  C   LEU B  97     3521   4246   3939    657   -175    223       C  
ATOM   1571  O   LEU B  97      36.940  -4.074   0.502  1.00 30.96           O  
ANISOU 1571  O   LEU B  97     3568   4182   4013    717   -175    171       O  
ATOM   1572  CB  LEU B  97      34.081  -3.129   0.790  1.00 28.80           C  
ANISOU 1572  CB  LEU B  97     3388   3829   3723    640    -99    120       C  
ATOM   1573  CG  LEU B  97      32.699  -2.561   0.697  1.00 26.33           C  
ANISOU 1573  CG  LEU B  97     3225   3385   3391    505   -193      6       C  
ATOM   1574  CD1 LEU B  97      31.747  -3.687   0.966  1.00 26.97           C  
ANISOU 1574  CD1 LEU B  97     3557   3281   3409    403   -124     28       C  
ATOM   1575  CD2 LEU B  97      32.528  -1.531   1.778  1.00 26.46           C  
ANISOU 1575  CD2 LEU B  97     3304   3465   3284    321   -249    -77       C  
ATOM   1576  N   ASN B  98      37.022  -2.500   2.092  1.00 32.55           N  
ANISOU 1576  N   ASN B  98     3669   4633   4066    644   -264    288       N  
ATOM   1577  CA  ASN B  98      38.243  -2.985   2.688  1.00 34.60           C  
ANISOU 1577  CA  ASN B  98     3835   4988   4323    664   -378    389       C  
ATOM   1578  C   ASN B  98      38.103  -3.081   4.186  1.00 35.29           C  
ANISOU 1578  C   ASN B  98     3954   5132   4322    655   -441    398       C  
ATOM   1579  O   ASN B  98      37.624  -2.161   4.818  1.00 35.20           O  
ANISOU 1579  O   ASN B  98     3963   5119   4291    644   -479    474       O  
ATOM   1580  CB  ASN B  98      39.417  -2.066   2.331  1.00 34.99           C  
ANISOU 1580  CB  ASN B  98     3829   5086   4378    619   -353    376       C  
ATOM   1581  CG  ASN B  98      39.614  -1.949   0.845  1.00 37.57           C  
ANISOU 1581  CG  ASN B  98     3983   5447   4845    572   -229    447       C  
ATOM   1582  OD1 ASN B  98      38.921  -1.183   0.166  1.00 38.36           O  
ANISOU 1582  OD1 ASN B  98     3882   5611   5083    505   -256    469       O  
ATOM   1583  ND2 ASN B  98      40.540  -2.726   0.315  1.00 39.96           N  
ANISOU 1583  ND2 ASN B  98     4069   5663   5450    669   -104    427       N  
ATOM   1584  N   PHE B  99      38.495  -4.217   4.741  1.00 36.77           N  
ANISOU 1584  N   PHE B  99     4134   5377   4458    703   -543    429       N  
ATOM   1585  CA  PHE B  99      38.578  -4.371   6.180  1.00 38.13           C  
ANISOU 1585  CA  PHE B  99     4403   5542   4541    754   -612    452       C  
ATOM   1586  C   PHE B  99      39.561  -5.461   6.494  1.00 39.56           C  
ANISOU 1586  C   PHE B  99     4532   5769   4730    786   -613    471       C  
ATOM   1587  O   PHE B  99      39.973  -6.199   5.605  1.00 40.51           O  
ANISOU 1587  O   PHE B  99     4587   5946   4858    802   -597    490       O  
ATOM   1588  CB  PHE B  99      37.208  -4.606   6.848  1.00 37.11           C  
ANISOU 1588  CB  PHE B  99     4392   5296   4412    707   -610    422       C  
ATOM   1589  CG  PHE B  99      36.534  -5.915   6.476  1.00 37.25           C  
ANISOU 1589  CG  PHE B  99     4550   5267   4334    711   -525    419       C  
ATOM   1590  CD1 PHE B  99      36.632  -7.030   7.301  1.00 37.10           C  
ANISOU 1590  CD1 PHE B  99     4682   5058   4356    665   -398    310       C  
ATOM   1591  CD2 PHE B  99      35.749  -6.016   5.332  1.00 35.78           C  
ANISOU 1591  CD2 PHE B  99     4563   4869   4160    656   -414    222       C  
ATOM   1592  CE1 PHE B  99      35.983  -8.226   6.960  1.00 36.91           C  
ANISOU 1592  CE1 PHE B  99     4764   4974   4285    700   -321    303       C  
ATOM   1593  CE2 PHE B  99      35.108  -7.226   4.990  1.00 35.28           C  
ANISOU 1593  CE2 PHE B  99     4506   4728   4167    650   -374    277       C  
ATOM   1594  CZ  PHE B  99      35.218  -8.315   5.800  1.00 35.23           C  
ANISOU 1594  CZ  PHE B  99     4537   4826   4019    788   -395    414       C  
ATOM   1595  OXT PHE B  99      39.957  -5.616   7.640  1.00 41.00           O  
ANISOU 1595  OXT PHE B  99     4692   5967   4917    786   -690    461       O  
TER    1596      PHE B  99                                                      
HETATM 1597  C31A3TL A 101      16.667   4.677   8.903  0.50 16.17           C  
HETATM 1598  C31B3TL A 101      15.594   4.525   8.821  0.50 26.42           C  
HETATM 1599  O8 A3TL A 101      15.656   4.102   8.566  0.50 13.59           O  
HETATM 1600  O8 B3TL A 101      14.436   4.568   8.446  0.50 29.15           O  
HETATM 1601  O9 A3TL A 101      16.736   5.173  10.259  0.50 16.84           O  
HETATM 1602  O9 B3TL A 101      15.786   4.690  10.232  0.50 26.67           O  
HETATM 1603  CA A3TL A 101      15.585   5.287  11.119  0.50 17.91           C  
HETATM 1604  CA B3TL A 101      14.627   5.086  10.967  0.50 26.99           C  
HETATM 1605  C  A3TL A 101      14.593   6.385  10.743  0.50 18.01           C  
HETATM 1606  C  B3TL A 101      14.436   6.584  10.903  0.50 27.12           C  
HETATM 1607  C13A3TL A 101      13.366   6.465  11.422  0.50 18.88           C  
HETATM 1608  C13B3TL A 101      13.138   7.110  10.921  0.50 27.27           C  
HETATM 1609  C14A3TL A 101      12.429   7.458  11.128  0.50 17.78           C  
HETATM 1610  C14B3TL A 101      12.939   8.483  10.881  0.50 27.29           C  
HETATM 1611  C15A3TL A 101      12.704   8.380  10.123  0.50 18.37           C  
HETATM 1612  C15B3TL A 101      14.046   9.331  10.826  0.50 27.41           C  
HETATM 1613  C16A3TL A 101      13.918   8.316   9.442  0.50 18.86           C  
HETATM 1614  C16B3TL A 101      15.339   8.805  10.817  0.50 28.33           C  
HETATM 1615  C17A3TL A 101      14.854   7.322   9.754  0.50 17.85           C  
HETATM 1616  C17B3TL A 101      15.540   7.427  10.863  0.50 26.57           C  
HETATM 1617  N4 A3TL A 101      17.713   4.845   8.086  0.50 14.88           N  
HETATM 1618  N4 B3TL A 101      16.669   4.346   8.056  0.50 25.61           N  
HETATM 1619  C18A3TL A 101      17.594   4.473   6.687  0.50 15.36           C  
HETATM 1620  C18B3TL A 101      16.656   4.267   6.617  0.50 24.40           C  
HETATM 1621  C19A3TL A 101      18.400   3.258   6.291  0.50 14.66           C  
HETATM 1622  C19B3TL A 101      17.556   3.167   6.099  0.50 23.90           C  
HETATM 1623  O4 A3TL A 101      19.571   3.126   6.619  0.50 14.30           O  
HETATM 1624  O4 B3TL A 101      18.739   3.122   6.413  0.50 23.24           O  
HETATM 1625  C20A3TL A 101      17.961   5.643   5.794  0.50 16.54           C  
HETATM 1626  C20B3TL A 101      17.097   5.604   6.059  0.50 25.08           C  
HETATM 1627  N2 A3TL A 101      17.747   2.344   5.567  0.50 13.93           N  
HETATM 1628  N2 B3TL A 101      16.984   2.262   5.293  0.50 20.83           N  
HETATM 1629  C10A3TL A 101      18.427   1.258   4.888  0.50 13.44           C  
HETATM 1630  C10B3TL A 101      17.721   1.193   4.617  0.50 19.97           C  
HETATM 1631  C11A3TL A 101      18.106   1.225   3.414  0.50 13.09           C  
HETATM 1632  C11B3TL A 101      17.481   1.161   3.119  0.50 19.64           C  
HETATM 1633  O2 A3TL A 101      16.975   0.945   3.029  0.50 13.61           O  
HETATM 1634  O2 B3TL A 101      16.486   0.627   2.657  0.50 18.41           O  
HETATM 1635  C12A3TL A 101      18.090  -0.061   5.611  0.50 14.14           C  
HETATM 1636  C12B3TL A 101      17.373  -0.146   5.289  0.50 20.65           C  
HETATM 1637  CG2A3TL A 101      18.622  -0.089   7.033  0.50 12.06           C  
HETATM 1638  CG2B3TL A 101      17.688  -0.118   6.777  0.50 20.24           C  
HETATM 1639  CG1A3TL A 101      18.645  -1.282   4.883  0.50 14.59           C  
HETATM 1640  CG1B3TL A 101      18.101  -1.333   4.660  0.50 20.76           C  
HETATM 1641  C2 A3TL A 101      19.917   0.301   0.558  0.50 18.16           C  
HETATM 1642  C2 B3TL A 101      19.658   1.128   0.318  0.50 19.00           C  
HETATM 1643  O1 A3TL A 101      21.246   0.586   0.908  0.50 19.08           O  
HETATM 1644  O1 B3TL A 101      20.761   1.892   0.771  0.50 19.26           O  
HETATM 1645  C1 A3TL A 101      19.001   1.400   1.111  0.50 17.44           C  
HETATM 1646  C1 B3TL A 101      18.401   1.787   0.882  0.50 20.19           C  
HETATM 1647  N1 A3TL A 101      19.105   1.523   2.572  0.50 14.55           N  
HETATM 1648  N1 B3TL A 101      18.408   1.742   2.347  0.50 19.76           N  
HETATM 1649  C3 A3TL A 101      19.304   2.719   0.385  0.50 18.33           C  
HETATM 1650  C3 B3TL A 101      18.427   3.232   0.356  0.50 21.74           C  
HETATM 1651  C4 A3TL A 101      18.500   3.851   0.974  0.50 17.79           C  
HETATM 1652  C4 B3TL A 101      17.293   4.075   0.883  0.50 22.93           C  
HETATM 1653  C5 A3TL A 101      19.074   4.718   1.909  0.50 18.96           C  
HETATM 1654  C5 B3TL A 101      17.364   4.662   2.146  0.50 23.40           C  
HETATM 1655  C9 A3TL A 101      17.169   4.021   0.589  0.50 18.66           C  
HETATM 1656  C9 B3TL A 101      16.176   4.275   0.087  0.50 23.26           C  
HETATM 1657  C6 A3TL A 101      18.327   5.770   2.451  0.50 20.19           C  
HETATM 1658  C6 B3TL A 101      16.318   5.451   2.630  0.50 24.23           C  
HETATM 1659  C8 A3TL A 101      16.422   5.055   1.145  0.50 19.15           C  
HETATM 1660  C8 B3TL A 101      15.132   5.057   0.567  0.50 24.99           C  
HETATM 1661  C7 A3TL A 101      16.993   5.936   2.070  0.50 19.47           C  
HETATM 1662  C7 B3TL A 101      15.197   5.642   1.839  0.50 24.43           C  
HETATM 1663  N51A3TL A 101      18.446  -1.728  -0.984  0.50 18.23           N  
HETATM 1664  N51B3TL A 101      19.056  -1.430  -1.281  0.50 16.81           N  
HETATM 1665  C51A3TL A 101      18.402  -1.795   0.478  0.50 19.18           C  
HETATM 1666  C51B3TL A 101      18.980  -1.376   0.185  0.50 18.39           C  
HETATM 1667  C52A3TL A 101      19.626  -1.112   1.070  0.50 17.81           C  
HETATM 1668  C52B3TL A 101      19.923  -0.315   0.763  0.50 18.97           C  
HETATM 1669  O51A3TL A 101      20.731  -1.910   0.710  0.50 16.89           O  
HETATM 1670  O51B3TL A 101      21.237  -0.629   0.372  0.50 19.76           O  
HETATM 1671  C53A3TL A 101      18.440  -3.243   0.991  0.50 21.51           C  
HETATM 1672  C53B3TL A 101      19.342  -2.709   0.848  0.50 19.06           C  
HETATM 1673  C54A3TL A 101      17.318  -4.104   0.464  0.50 23.32           C  
HETATM 1674  C54B3TL A 101      18.529  -3.871   0.335  0.50 18.24           C  
HETATM 1675  C55A3TL A 101      17.379  -4.674  -0.809  0.50 24.17           C  
HETATM 1676  C55B3TL A 101      19.130  -4.823  -0.490  0.50 19.82           C  
HETATM 1677  C59A3TL A 101      16.226  -4.347   1.286  0.50 23.73           C  
HETATM 1678  C59B3TL A 101      17.183  -3.994   0.677  0.50 19.95           C  
HETATM 1679  C56A3TL A 101      16.344  -5.480  -1.288  0.50 23.81           C  
HETATM 1680  C56B3TL A 101      18.394  -5.909  -0.967  0.50 18.03           C  
HETATM 1681  C58A3TL A 101      15.188  -5.145   0.820  0.50 25.53           C  
HETATM 1682  C58B3TL A 101      16.447  -5.071   0.196  0.50 19.52           C  
HETATM 1683  C57A3TL A 101      15.248  -5.711  -0.460  0.50 25.32           C  
HETATM 1684  C57B3TL A 101      17.044  -6.028  -0.630  0.50 19.27           C  
HETATM 1685  N52A3TL A 101      17.123  -2.313  -3.905  0.50 18.41           N  
HETATM 1686  N52B3TL A 101      17.727  -2.345  -4.256  0.50 16.30           N  
HETATM 1687  C60A3TL A 101      17.818  -1.207  -3.257  0.50 17.59           C  
HETATM 1688  C60B3TL A 101      18.416  -1.254  -3.601  0.50 16.37           C  
HETATM 1689  C61A3TL A 101      17.518  -1.186  -1.776  0.50 17.43           C  
HETATM 1690  C61B3TL A 101      18.059  -1.152  -2.137  0.50 15.63           C  
HETATM 1691  O52A3TL A 101      16.481  -0.711  -1.351  0.50 15.39           O  
HETATM 1692  O52B3TL A 101      16.925  -0.842  -1.794  0.50 14.21           O  
HETATM 1693  C62A3TL A 101      17.431   0.109  -3.936  0.50 19.58           C  
HETATM 1694  C62B3TL A 101      18.140   0.024  -4.386  0.50 17.91           C  
HETATM 1695  CG6A3TL A 101      17.689   0.049  -5.434  0.50 18.63           C  
HETATM 1696  CG6B3TL A 101      18.737  -0.020  -5.782  0.50 16.43           C  
HETATM 1697  CG5A3TL A 101      18.163   1.314  -3.341  0.50 18.69           C  
HETATM 1698  CG5B3TL A 101      18.627   1.268  -3.651  0.50 18.04           C  
HETATM 1699  N54A3TL A 101      16.739  -4.172  -6.766  0.50 20.23           N  
HETATM 1700  N54B3TL A 101      17.681  -4.958  -6.606  0.50 20.70           N  
HETATM 1701  C68A3TL A 101      16.723  -4.226  -5.321  0.50 18.83           C  
HETATM 1702  C68B3TL A 101      17.579  -4.545  -5.219  0.50 19.97           C  
HETATM 1703  C69A3TL A 101      17.676  -3.199  -4.734  0.50 18.83           C  
HETATM 1704  C69B3TL A 101      18.376  -3.296  -4.925  0.50 17.86           C  
HETATM 1705  O54A3TL A 101      18.865  -3.180  -5.027  0.50 17.30           O  
HETATM 1706  O54B3TL A 101      19.530  -3.171  -5.304  0.50 17.17           O  
HETATM 1707  C70A3TL A 101      17.101  -5.625  -4.854  0.50 18.86           C  
HETATM 1708  C70B3TL A 101      17.977  -5.693  -4.307  0.50 18.45           C  
HETATM 1709  C81A3TL A 101      15.722  -4.451  -7.580  0.50 20.21           C  
HETATM 1710  C81B3TL A 101      16.682  -4.682  -7.430  0.50 20.76           C  
HETATM 1711  O58A3TL A 101      14.547  -4.218  -7.356  0.50 23.06           O  
HETATM 1712  O58B3TL A 101      15.635  -4.184  -7.073  0.50 21.95           O  
HETATM 1713  O59A3TL A 101      16.062  -5.078  -8.829  0.50 20.81           O  
HETATM 1714  O59B3TL A 101      16.860  -4.958  -8.826  0.50 21.77           O  
HETATM 1715  CA5A3TL A 101      15.085  -5.424  -9.819  0.50 21.39           C  
HETATM 1716  CA5B3TL A 101      15.754  -4.859  -9.723  0.50 24.07           C  
HETATM 1717  C50A3TL A 101      14.195  -6.571  -9.390  0.50 21.65           C  
HETATM 1718  C50B3TL A 101      14.837  -6.053  -9.583  0.50 24.05           C  
HETATM 1719  C63A3TL A 101      13.046  -6.866 -10.141  0.50 22.01           C  
HETATM 1720  C63B3TL A 101      13.456  -5.858  -9.639  0.50 25.36           C  
HETATM 1721  C64A3TL A 101      12.195  -7.908  -9.767  0.50 20.63           C  
HETATM 1722  C64B3TL A 101      12.594  -6.959  -9.527  0.50 25.92           C  
HETATM 1723  C65A3TL A 101      12.508  -8.663  -8.639  0.50 22.28           C  
HETATM 1724  C65B3TL A 101      13.119  -8.240  -9.357  0.50 24.99           C  
HETATM 1725  C66A3TL A 101      13.648  -8.378  -7.884  0.50 22.78           C  
HETATM 1726  C66B3TL A 101      14.504  -8.429  -9.305  0.50 24.84           C  
HETATM 1727  C67A3TL A 101      14.493  -7.330  -8.262  0.50 21.34           C  
HETATM 1728  C67B3TL A 101      15.364  -7.336  -9.416  0.50 23.09           C  
HETATM 1729  O   HOH A 102      15.332  -0.041   0.640  1.00 18.98           O  
HETATM 1730  O   HOH A 103      24.723   4.969   5.156  1.00 20.82           O  
HETATM 1731  O   HOH A 104      25.203  -0.767  17.406  1.00 24.85           O  
HETATM 1732  O   HOH A 105      21.234  -1.960  13.850  1.00 24.62           O  
HETATM 1733  O   HOH A 106      23.788 -22.708  10.956  1.00 34.35           O  
HETATM 1734  O   HOH A 107      19.260   6.282  11.372  1.00 34.25           O  
HETATM 1735  O   HOH A 108      25.713 -14.341  18.545  1.00 27.48           O  
HETATM 1736  O   HOH A 109      20.843 -12.640   3.080  1.00 34.50           O  
HETATM 1737  O   HOH A 110      39.084  -5.063  10.224  1.00 41.60           O  
HETATM 1738  O   HOH A 111      34.567   2.839   8.747  1.00 26.81           O  
HETATM 1739  O   HOH A 112      21.678   5.272   4.930  1.00 30.27           O  
HETATM 1740  O   HOH A 113      26.948 -17.744  17.639  1.00 38.63           O  
HETATM 1741  O   HOH A 114      24.569 -12.298  21.652  1.00 36.17           O  
HETATM 1742  O   HOH A 115      32.959  -9.178  -7.110  1.00 29.14           O  
HETATM 1743  O   HOH A 116      24.050  -2.509  21.315  1.00 36.56           O  
HETATM 1744  O   HOH A 117      18.231 -14.045   9.220  1.00 47.07           O  
HETATM 1745  O   HOH A 118      28.398 -14.974  16.934  1.00 37.88           O  
HETATM 1746  O   HOH A 119      32.084 -15.733  10.234  1.00 40.98           O  
HETATM 1747  O   HOH A 120      32.808 -14.424   4.048  1.00 37.26           O  
HETATM 1748  O   HOH A 121      18.732  -9.089  23.662  1.00 53.02           O  
HETATM 1749  O   HOH A 122      25.087   3.728  11.932  1.00 34.57           O  
HETATM 1750  O   HOH A 123      28.050 -12.513  -4.153  1.00 43.07           O  
HETATM 1751  O   HOH A 124      39.922  -0.384   5.794  1.00 42.32           O  
HETATM 1752  O   HOH A 125      15.617 -18.543  14.945  1.00 52.48           O  
HETATM 1753  O   HOH A 126      20.717 -20.082   9.201  1.00 48.63           O  
HETATM 1754  O   HOH A 127      30.542 -15.974  17.381  1.00 45.06           O  
HETATM 1755  O   HOH A 128       9.743 -12.154   8.853  1.00 44.65           O  
HETATM 1756  O   HOH A 129      19.238 -19.354   6.738  1.00 47.85           O  
HETATM 1757  O   HOH A 130      25.073 -11.795 -10.159  1.00 48.53           O  
HETATM 1758  O   HOH A 131      24.190  -9.012  -8.770  1.00 53.43           O  
HETATM 1759  O   HOH A 132      19.643 -21.348  11.294  1.00 53.08           O  
HETATM 1760  O   HOH A 133      20.953   4.208  13.849  1.00 45.64           O  
HETATM 1761  O   HOH A 134      21.788 -17.001   4.388  1.00 40.77           O  
HETATM 1762  O   HOH A 135      21.667 -13.325  22.641  1.00 55.12           O  
HETATM 1763  O   HOH A 136      22.821 -12.504  -4.147  1.00 43.18           O  
HETATM 1764  O   HOH A 137      25.653  -7.901 -10.301  1.00 52.35           O  
HETATM 1765  O   HOH A 138      23.692   1.379  16.935  1.00 43.25           O  
HETATM 1766  O   HOH A 139      31.422  -8.202  -4.002  1.00 42.02           O  
HETATM 1767  O   HOH A 140      27.538  -0.085  17.210  1.00 44.09           O  
HETATM 1768  O   HOH A 141      16.458 -19.212   5.629  1.00 50.02           O  
HETATM 1769  O   HOH A 142      38.158  -8.261  -8.923  1.00 50.14           O  
HETATM 1770  O   HOH A 143      28.819 -15.153  -1.641  1.00 50.53           O  
HETATM 1771  O   HOH A 144      12.860 -19.862  19.638  1.00 48.36           O  
HETATM 1772  O   HOH A 145      21.499   0.674  14.866  1.00 48.60           O  
HETATM 1773  O   HOH A 146      18.435 -15.629   6.861  1.00 37.68           O  
HETATM 1774  O   HOH A 147      37.012 -10.513  -6.678  1.00 50.22           O  
HETATM 1775  O   HOH A 148      17.924 -13.315   0.230  1.00 42.52           O  
HETATM 1776  O   HOH A 149      35.440  -9.663  -3.895  1.00 46.91           O  
HETATM 1777  O   HOH A 150      22.919 -21.817   6.551  1.00 44.36           O  
HETATM 1778  O   HOH B 100      24.717  -5.054  -3.837  1.00 21.88           O  
HETATM 1779  O   HOH B 101      21.320   1.907 -12.511  1.00 27.33           O  
HETATM 1780  O   HOH B 102      25.338   0.913 -15.971  1.00 24.07           O  
HETATM 1781  O   HOH B 103      23.686  22.649  -9.655  1.00 36.04           O  
HETATM 1782  O   HOH B 104      25.651  14.275 -17.302  1.00 31.96           O  
HETATM 1783  O   HOH B 105      19.261  -6.054 -10.019  1.00 37.17           O  
HETATM 1784  O   HOH B 106      20.773  12.647  -1.773  1.00 37.92           O  
HETATM 1785  O   HOH B 107      31.280   8.128   5.388  1.00 36.20           O  
HETATM 1786  O   HOH B 108      26.934  17.535 -16.122  1.00 34.54           O  
HETATM 1787  O   HOH B 109      34.643  -2.974  -7.438  1.00 30.72           O  
HETATM 1788  O   HOH B 110      23.956   2.422 -20.093  1.00 37.48           O  
HETATM 1789  O   HOH B 111      33.322   8.949   8.395  1.00 31.77           O  
HETATM 1790  O   HOH B 112      24.470  12.482 -20.076  1.00 35.88           O  
HETATM 1791  O   HOH B 113      21.969  -5.409  -3.780  1.00 33.52           O  
HETATM 1792  O   HOH B 114      21.788  16.983  -3.315  1.00 35.09           O  
HETATM 1793  O   HOH B 115      30.763  15.982 -15.984  1.00 37.13           O  
HETATM 1794  O   HOH B 116      27.977  12.646   5.514  1.00 45.17           O  
HETATM 1795  O   HOH B 117      39.977   0.368  -4.481  1.00 40.88           O  
HETATM 1796  O   HOH B 118       9.793  12.043  -7.045  1.00 49.64           O  
HETATM 1797  O   HOH B 119      31.867  15.738  -8.867  1.00 38.55           O  
HETATM 1798  O   HOH B 120      24.807  -3.779 -10.603  1.00 41.54           O  
HETATM 1799  O   HOH B 121      41.222  -7.626   8.518  1.00 49.72           O  
HETATM 1800  O   HOH B 122      28.490  14.967 -15.665  1.00 33.94           O  
HETATM 1801  O   HOH B 123      15.553  16.499  -7.216  1.00 52.83           O  
HETATM 1802  O   HOH B 124      15.467  18.389 -13.986  1.00 55.51           O  
HETATM 1803  O   HOH B 125      12.346  -4.405 -13.243  1.00 50.36           O  
HETATM 1804  O   HOH B 126      19.154  19.233  -5.696  1.00 49.43           O  
HETATM 1805  O   HOH B 127      37.612  10.428 -14.807  1.00 46.51           O  
HETATM 1806  O   HOH B 128      22.859  21.802  -5.406  1.00 41.63           O  
HETATM 1807  O   HOH B 129      20.829  20.030  -7.989  1.00 52.68           O  
HETATM 1808  O   HOH B 130      29.600  -2.979 -13.257  1.00 48.33           O  
HETATM 1809  O   HOH B 131      36.217  -1.978  -9.510  1.00 43.91           O  
HETATM 1810  O   HOH B 132      36.787   6.850 -13.290  1.00 53.79           O  
HETATM 1811  O   HOH B 133      27.462   0.133 -15.932  1.00 39.83           O  
HETATM 1812  O   HOH B 134      33.425  16.880 -19.528  1.00 48.07           O  
HETATM 1813  O   HOH B 135      26.283   6.945 -27.378  1.00 53.42           O  
HETATM 1814  O   HOH B 136      21.789  -0.904 -13.167  1.00 43.01           O  
HETATM 1815  O   HOH B 137      21.013  -4.068 -12.574  1.00 52.75           O  
HETATM 1816  O   HOH B 138      21.433  11.374   4.040  1.00 48.58           O  
HETATM 1817  O   HOH B 139      22.848  12.816   5.640  1.00 46.92           O  
HETATM 1818  O   HOH B 140      26.268  15.742 -19.828  1.00 43.41           O  
HETATM 1819  O   HOH B 141      35.869  18.609 -12.378  1.00 44.09           O  
HETATM 1820  O   HOH B 142      16.409  19.022 -11.671  1.00 48.06           O  
HETATM 1821  O   HOH B 143      18.474  15.597  -5.620  1.00 41.40           O  
HETATM 1822  O   HOH B 144      27.834  18.014 -18.058  1.00 45.24           O  
HETATM 1823  O   HOH B 145      12.693  17.998 -13.941  1.00 48.99           O  
HETATM 1824  O   HOH B 146      17.831   6.263 -22.589  1.00 37.90           O  
HETATM 1825  O   HOH B 147      20.226  14.073   0.661  1.00 48.49           O  
HETATM 1826  O   HOH B 148      35.272  17.377 -14.748  1.00 48.27           O  
CONECT 1329 1335 1336                                                           
CONECT 1335 1329 1337                                                           
CONECT 1336 1329 1338                                                           
CONECT 1337 1335 1339 1351                                                      
CONECT 1338 1336 1340 1352                                                      
CONECT 1339 1337 1341                                                           
CONECT 1340 1338 1342                                                           
CONECT 1341 1339 1343                                                           
CONECT 1342 1340 1344                                                           
CONECT 1343 1341 1345                                                           
CONECT 1344 1342 1346                                                           
CONECT 1345 1343 1347                                                           
CONECT 1346 1344 1348                                                           
CONECT 1347 1345 1349                                                           
CONECT 1348 1346 1350                                                           
CONECT 1349 1347                                                                
CONECT 1350 1348                                                                
CONECT 1351 1337 1353 1355                                                      
CONECT 1352 1338 1354 1355                                                      
CONECT 1353 1351                                                                
CONECT 1354 1352                                                                
CONECT 1355 1351 1352                                                           
CONECT 1597 1599 1601 1617                                                      
CONECT 1598 1600 1602 1618                                                      
CONECT 1599 1597                                                                
CONECT 1600 1598                                                                
CONECT 1601 1597 1603                                                           
CONECT 1602 1598 1604                                                           
CONECT 1603 1601 1605                                                           
CONECT 1604 1602 1606                                                           
CONECT 1605 1603 1607 1615                                                      
CONECT 1606 1604 1608 1616                                                      
CONECT 1607 1605 1609                                                           
CONECT 1608 1606 1610                                                           
CONECT 1609 1607 1611                                                           
CONECT 1610 1608 1612                                                           
CONECT 1611 1609 1613                                                           
CONECT 1612 1610 1614                                                           
CONECT 1613 1611 1615                                                           
CONECT 1614 1612 1616                                                           
CONECT 1615 1605 1613                                                           
CONECT 1616 1606 1614                                                           
CONECT 1617 1597 1619                                                           
CONECT 1618 1598 1620                                                           
CONECT 1619 1617 1621 1625                                                      
CONECT 1620 1618 1622 1626                                                      
CONECT 1621 1619 1623 1627                                                      
CONECT 1622 1620 1624 1628                                                      
CONECT 1623 1621                                                                
CONECT 1624 1622                                                                
CONECT 1625 1619                                                                
CONECT 1626 1620                                                                
CONECT 1627 1621 1629                                                           
CONECT 1628 1622 1630                                                           
CONECT 1629 1627 1631 1635                                                      
CONECT 1630 1628 1632 1636                                                      
CONECT 1631 1629 1633 1647                                                      
CONECT 1632 1630 1634 1648                                                      
CONECT 1633 1631                                                                
CONECT 1634 1632                                                                
CONECT 1635 1629 1637 1639                                                      
CONECT 1636 1630 1638 1640                                                      
CONECT 1637 1635                                                                
CONECT 1638 1636                                                                
CONECT 1639 1635                                                                
CONECT 1640 1636                                                                
CONECT 1641 1643 1645 1667                                                      
CONECT 1642 1644 1646 1668                                                      
CONECT 1643 1641                                                                
CONECT 1644 1642                                                                
CONECT 1645 1641 1647 1649                                                      
CONECT 1646 1642 1648 1650                                                      
CONECT 1647 1631 1645                                                           
CONECT 1648 1632 1646                                                           
CONECT 1649 1645 1651                                                           
CONECT 1650 1646 1652                                                           
CONECT 1651 1649 1653 1655                                                      
CONECT 1652 1650 1654 1656                                                      
CONECT 1653 1651 1657                                                           
CONECT 1654 1652 1658                                                           
CONECT 1655 1651 1659                                                           
CONECT 1656 1652 1660                                                           
CONECT 1657 1653 1661                                                           
CONECT 1658 1654 1662                                                           
CONECT 1659 1655 1661                                                           
CONECT 1660 1656 1662                                                           
CONECT 1661 1657 1659                                                           
CONECT 1662 1658 1660                                                           
CONECT 1663 1665 1689                                                           
CONECT 1664 1666 1690                                                           
CONECT 1665 1663 1667 1671                                                      
CONECT 1666 1664 1668 1672                                                      
CONECT 1667 1641 1665 1669                                                      
CONECT 1668 1642 1666 1670                                                      
CONECT 1669 1667                                                                
CONECT 1670 1668                                                                
CONECT 1671 1665 1673                                                           
CONECT 1672 1666 1674                                                           
CONECT 1673 1671 1675 1677                                                      
CONECT 1674 1672 1676 1678                                                      
CONECT 1675 1673 1679                                                           
CONECT 1676 1674 1680                                                           
CONECT 1677 1673 1681                                                           
CONECT 1678 1674 1682                                                           
CONECT 1679 1675 1683                                                           
CONECT 1680 1676 1684                                                           
CONECT 1681 1677 1683                                                           
CONECT 1682 1678 1684                                                           
CONECT 1683 1679 1681                                                           
CONECT 1684 1680 1682                                                           
CONECT 1685 1687 1703                                                           
CONECT 1686 1688 1704                                                           
CONECT 1687 1685 1689 1693                                                      
CONECT 1688 1686 1690 1694                                                      
CONECT 1689 1663 1687 1691                                                      
CONECT 1690 1664 1688 1692                                                      
CONECT 1691 1689                                                                
CONECT 1692 1690                                                                
CONECT 1693 1687 1695 1697                                                      
CONECT 1694 1688 1696 1698                                                      
CONECT 1695 1693                                                                
CONECT 1696 1694                                                                
CONECT 1697 1693                                                                
CONECT 1698 1694                                                                
CONECT 1699 1701 1709                                                           
CONECT 1700 1702 1710                                                           
CONECT 1701 1699 1703 1707                                                      
CONECT 1702 1700 1704 1708                                                      
CONECT 1703 1685 1701 1705                                                      
CONECT 1704 1686 1702 1706                                                      
CONECT 1705 1703                                                                
CONECT 1706 1704                                                                
CONECT 1707 1701                                                                
CONECT 1708 1702                                                                
CONECT 1709 1699 1711 1713                                                      
CONECT 1710 1700 1712 1714                                                      
CONECT 1711 1709                                                                
CONECT 1712 1710                                                                
CONECT 1713 1709 1715                                                           
CONECT 1714 1710 1716                                                           
CONECT 1715 1713 1717                                                           
CONECT 1716 1714 1718                                                           
CONECT 1717 1715 1719 1727                                                      
CONECT 1718 1716 1720 1728                                                      
CONECT 1719 1717 1721                                                           
CONECT 1720 1718 1722                                                           
CONECT 1721 1719 1723                                                           
CONECT 1722 1720 1724                                                           
CONECT 1723 1721 1725                                                           
CONECT 1724 1722 1726                                                           
CONECT 1725 1723 1727                                                           
CONECT 1726 1724 1728                                                           
CONECT 1727 1717 1725                                                           
CONECT 1728 1718 1726                                                           
MASTER      370    0    2    2   20    0    8    6 1684    2  154   16          
END                                                                             



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