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

Elnemo is running on a new server.
Should you encounter any unexpected behaviour,
please let us know.


***  5chk  ***

elNémo ID: 19072622212952509

Job options:

ID        	=	 19072622212952509
JOBID     	=	 5chk
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 5chk

HEADER    GLYCOPROTEIN                            10-JUL-15   5CHK              
TITLE     CRYSTAL STRUCTURE OF AVIDIN - HABA COMPLEX (HEXAGONAL CRYSTAL FORM)   
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: AVIDIN;                                                    
COMPND   3 CHAIN: A;                                                            
COMPND   4 FRAGMENT: UNP RESIDUES 25-152                                        
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: GALLUS GALLUS;                                  
SOURCE   3 ORGANISM_COMMON: CHICKEN;                                            
SOURCE   4 ORGANISM_TAXID: 9031                                                 
KEYWDS    GLYCOPROTEIN, COMPLEX                                                 
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    P.STRZELCZYK,A.BUJACZ,G.BUJACZ                                        
REVDAT   1   23-MAR-16 5CHK    0                                                
JRNL        AUTH   P.STRZELCZYK,G.BUJACZ                                        
JRNL        TITL   CRYSTAL STRUCTURE AND LIGAND AFFINITY OF AVIDIN IN THE       
JRNL        TITL 2 COMPLEX WITH 4-HYDROXYAZOBENZENE-2-CARBOXYLIC ACID           
JRNL        REF    J.MOL.STRUCT.                 V.1109   232 2016              
JRNL        REFN                   ISSN 0022-2860                               
JRNL        DOI    10.1016/J.MOLSTRUC.2016.01.013                               
REMARK   2                                                                      
REMARK   2 RESOLUTION.    2.20 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0103                                      
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) : 2.20                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 40.18                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : NULL                           
REMARK   3   COMPLETENESS FOR RANGE        (%) : 100.0                          
REMARK   3   NUMBER OF REFLECTIONS             : 6957                           
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) : 0.164                           
REMARK   3   R VALUE            (WORKING SET) : 0.161                           
REMARK   3   FREE R VALUE                     : 0.227                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 5.000                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 368                             
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) : 2.20                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 2.26                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 491                          
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 100.0                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3130                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 27                           
REMARK   3   BIN FREE R VALUE                    : 0.2870                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 946                                     
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 32                                      
REMARK   3   SOLVENT ATOMS            : 51                                      
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 72.69                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : -2.03000                                             
REMARK   3    B22 (A**2) : -2.03000                                             
REMARK   3    B33 (A**2) : 6.59000                                              
REMARK   3    B12 (A**2) : -1.02000                                             
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): 0.216         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.196         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.188         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 15.725        
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.976                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.951                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):   999 ; 0.020 ; 0.019       
REMARK   3   BOND LENGTHS OTHERS               (A):   920 ; 0.003 ; 0.020       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1354 ; 2.003 ; 1.933       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2112 ; 1.134 ; 2.991       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   120 ; 8.359 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    42 ;37.054 ;24.048       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   166 ;16.188 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     6 ;25.006 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   155 ; 0.115 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1120 ; 0.009 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   243 ; 0.002 ; 0.020       
REMARK   3   NON-BONDED CONTACTS REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED CONTACTS OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   NON-BONDED TORSION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) REFINED ATOMS      (A):  NULL ;  NULL ;  NULL       
REMARK   3   H-BOND (X...Y) OTHERS             (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION REFINED ATOMS (A):  NULL ;  NULL ;  NULL       
REMARK   3   POTENTIAL METAL-ION OTHERS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW REFINED ATOMS        (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY VDW OTHERS               (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND REFINED ATOMS     (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY H-BOND OTHERS            (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION REFINED ATOMS  (A):  NULL ;  NULL ;  NULL       
REMARK   3   SYMMETRY METAL-ION OTHERS         (A):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  ISOTROPIC THERMAL FACTOR RESTRAINTS.     COUNT   RMS    WEIGHT      
REMARK   3   MAIN-CHAIN BOND REFINED ATOMS  (A**2):   483 ; 3.819 ; 4.898       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):   482 ; 3.802 ; 4.887       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):   602 ; 6.491 ; 7.328       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):   603 ; 6.491 ; 7.340       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):   516 ; 4.223 ; 5.494       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):   517 ; 4.219 ; 5.493       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):   753 ; 6.858 ; 8.003       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  1097 ;11.323 ;40.176       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  1098 ;11.318 ;40.195       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 3                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A     3        A    46                          
REMARK   3    RESIDUE RANGE :   A    47        A    95                          
REMARK   3    RESIDUE RANGE :   A    96        A   122                          
REMARK   3    ORIGIN FOR THE GROUP (A):  15.6265   0.2207  22.1386              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0374 T22:   0.2404                                     
REMARK   3      T33:   0.1294 T12:   0.0318                                     
REMARK   3      T13:  -0.0117 T23:  -0.0926                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   3.1042 L22:   2.2411                                     
REMARK   3      L33:   2.8976 L12:   0.9012                                     
REMARK   3      L13:   0.0235 L23:  -0.4046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:   0.0832 S12:  -0.0814 S13:   0.1393                       
REMARK   3      S21:   0.1741 S22:   0.1295 S23:  -0.2718                       
REMARK   3      S31:  -0.0750 S32:   0.6746 S33:  -0.2127                       
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 5CHK COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY RCSB ON 10-JUL-15.                  
REMARK 100 THE DEPOSITION ID IS D_1000211639.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 30-MAY-14                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : NULL                               
REMARK 200  NUMBER OF CRYSTALS USED        : NULL                               
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : Y                                  
REMARK 200  RADIATION SOURCE               : BESSY                              
REMARK 200  BEAMLINE                       : 14.1                               
REMARK 200  X-RAY GENERATOR MODEL          : NULL                               
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 0.977609                           
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : PIXEL                              
REMARK 200  DETECTOR MANUFACTURER          : DECTRIS PILATUS 6M                 
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : XDS                                
REMARK 200  DATA SCALING SOFTWARE          : XDS                                
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 7329                               
REMARK 200  RESOLUTION RANGE HIGH      (A) : 2.200                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 50.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 100.0                              
REMARK 200  DATA REDUNDANCY                : 5.100                              
REMARK 200  R MERGE                    (I) : NULL                               
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 31.9200                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : NULL                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : NULL                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : NULL                               
REMARK 200  DATA REDUNDANCY IN SHELL       : NULL                               
REMARK 200  R MERGE FOR SHELL          (I) : NULL                               
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: MOLREP                                                
REMARK 200 STARTING MODEL: 1VYO                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 46.02                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.28                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 0.1M SODIUM CITRATE TRIBASIC DEHYDRATE   
REMARK 280  PH 4.5, 24% W/V POLYETHYLENE GLYCOL 1000, VAPOR DIFFUSION,          
REMARK 280  TEMPERATURE 292.15K                                                 
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 64 2 2                         
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                                                 
REMARK 290       5555   Y,-X+Y,Z+1/3                                            
REMARK 290       6555   X-Y,X,Z+2/3                                             
REMARK 290       7555   Y,X,-Z+1/3                                              
REMARK 290       8555   X-Y,-Y,-Z                                               
REMARK 290       9555   -X,-X+Y,-Z+2/3                                          
REMARK 290      10555   -Y,-X,-Z+1/3                                            
REMARK 290      11555   -X+Y,Y,-Z                                               
REMARK 290      12555   X,X-Y,-Z+2/3                                            
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       40.17667            
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       80.35333            
REMARK 290   SMTRY1   4 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000  1.000000        0.00000            
REMARK 290   SMTRY1   5  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       40.17667            
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       80.35333            
REMARK 290   SMTRY1   7 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   7  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   7  0.000000  0.000000 -1.000000       40.17667            
REMARK 290   SMTRY1   8  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   8  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   8  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   9 -0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   9 -0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   9  0.000000  0.000000 -1.000000       80.35333            
REMARK 290   SMTRY1  10  0.500000 -0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  10 -0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  10  0.000000  0.000000 -1.000000       40.17667            
REMARK 290   SMTRY1  11 -1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2  11  0.000000  1.000000  0.000000        0.00000            
REMARK 290   SMTRY3  11  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1  12  0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2  12  0.866025 -0.500000  0.000000        0.00000            
REMARK 290   SMTRY3  12  0.000000  0.000000 -1.000000       80.35333            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: TETRAMERIC                        
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: TETRAMERIC                 
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 10460 ANGSTROM**2                         
REMARK 350 SURFACE AREA OF THE COMPLEX: 21900 ANGSTROM**2                       
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -39.0 KCAL/MOL                        
REMARK 350 APPLY THE FOLLOWING TO CHAINS: A                                     
REMARK 350   BIOMT1   1  1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   1  0.000000  1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   1  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   2 -1.000000  0.000000  0.000000        0.00000            
REMARK 350   BIOMT2   2  0.000000 -1.000000  0.000000        0.00000            
REMARK 350   BIOMT3   2  0.000000  0.000000  1.000000        0.00000            
REMARK 350   BIOMT1   3 -0.500000  0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   3  0.866025  0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   3  0.000000  0.000000 -1.000000       40.17667            
REMARK 350   BIOMT1   4  0.500000 -0.866025  0.000000        0.00000            
REMARK 350   BIOMT2   4 -0.866025 -0.500000  0.000000        0.00000            
REMARK 350   BIOMT3   4  0.000000  0.000000 -1.000000       40.17667            
REMARK 375                                                                      
REMARK 375 SPECIAL POSITION                                                     
REMARK 375 THE FOLLOWING ATOMS ARE FOUND TO BE WITHIN 0.15 ANGSTROMS            
REMARK 375 OF A SYMMETRY RELATED ATOM AND ARE ASSUMED TO BE ON SPECIAL          
REMARK 375 POSITIONS.                                                           
REMARK 375                                                                      
REMARK 375 ATOM RES CSSEQI                                                      
REMARK 375      HOH A 321  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 336  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 342  LIES ON A SPECIAL POSITION.                          
REMARK 375      HOH A 346  LIES ON A SPECIAL POSITION.                          
REMARK 465                                                                      
REMARK 465 MISSING RESIDUES                                                     
REMARK 465 THE FOLLOWING RESIDUES WERE NOT LOCATED IN THE                       
REMARK 465 EXPERIMENT. (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 465 IDENTIFIER; SSSEQ=SEQUENCE NUMBER; I=INSERTION CODE.)                
REMARK 465                                                                      
REMARK 465   M RES C SSSEQI                                                     
REMARK 465     ALA A     1                                                      
REMARK 465     ARG A     2                                                      
REMARK 465     ARG A   124                                                      
REMARK 465     THR A   125                                                      
REMARK 465     GLN A   126                                                      
REMARK 465     LYS A   127                                                      
REMARK 465     GLU A   128                                                      
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    ASP A 105   CB  -  CG  -  OD1 ANGL. DEV. =   5.9 DEGREES          
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: TORSION ANGLES                                             
REMARK 500                                                                      
REMARK 500 TORSION ANGLES OUTSIDE THE EXPECTED RAMACHANDRAN REGIONS:            
REMARK 500 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 500 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                             
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT:(10X,I3,1X,A3,1X,A1,I4,A1,4X,F7.2,3X,F7.2)                    
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES: GJ KLEYWEGT AND TA JONES (1996). PHI/PSI-           
REMARK 500 CHOLOGY: RAMACHANDRAN REVISITED. STRUCTURE 4, 1395 - 1400            
REMARK 500                                                                      
REMARK 500  M RES CSSEQI        PSI       PHI                                   
REMARK 500    ASN A  57       13.10     82.42                                   
REMARK 500    LYS A  58      -56.28     68.29                                   
REMARK 500    ARG A  59      -55.10     75.01                                   
REMARK 500    THR A  60       -0.76     61.36                                   
REMARK 500    ARG A  87       71.95     59.52                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 800                                                                      
REMARK 800 SITE                                                                 
REMARK 800 SITE_IDENTIFIER: AC1                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for residue 55R A 202                 
REMARK 800                                                                      
REMARK 800 SITE_IDENTIFIER: AC2                                                 
REMARK 800 EVIDENCE_CODE: SOFTWARE                                              
REMARK 800 SITE_DESCRIPTION: binding site for Mono-Saccharide NAG A 201 bound   
REMARK 800  to ASN A 17                                                         
REMARK 900                                                                      
REMARK 900 RELATED ENTRIES                                                      
REMARK 900 RELATED ID: 1VYO   RELATED DB: PDB                                   
REMARK 900 AVIDIN, FREE-LIGAND STRUCTURE                                        
REMARK 900 RELATED ID: 4I60   RELATED DB: PDB                                   
REMARK 900 AVIDIN - BIOTINYLRUTHENOCENE COMPLEX                                 
REMARK 900 RELATED ID: 2AVI   RELATED DB: PDB                                   
REMARK 900 AVIDIN - BIOTIN COMPLEX                                              
DBREF  5CHK A    1   128  UNP    P02701   AVID_CHICK      25    152             
SEQADV 5CHK THR A   34  UNP  P02701    ILE    58 CONFLICT                       
SEQADV 5CHK GLU A   53  UNP  P02701    GLN    77 CONFLICT                       
SEQRES   1 A  128  ALA ARG LYS CYS SER LEU THR GLY LYS TRP THR ASN ASP          
SEQRES   2 A  128  LEU GLY SER ASN MET THR ILE GLY ALA VAL ASN SER ARG          
SEQRES   3 A  128  GLY GLU PHE THR GLY THR TYR THR THR ALA VAL THR ALA          
SEQRES   4 A  128  THR SER ASN GLU ILE LYS GLU SER PRO LEU HIS GLY THR          
SEQRES   5 A  128  GLU ASN THR ILE ASN LYS ARG THR GLN PRO THR PHE GLY          
SEQRES   6 A  128  PHE THR VAL ASN TRP LYS PHE SER GLU SER THR THR VAL          
SEQRES   7 A  128  PHE THR GLY GLN CYS PHE ILE ASP ARG ASN GLY LYS GLU          
SEQRES   8 A  128  VAL LEU LYS THR MET TRP LEU LEU ARG SER SER VAL ASN          
SEQRES   9 A  128  ASP ILE GLY ASP ASP TRP LYS ALA THR ARG VAL GLY ILE          
SEQRES  10 A  128  ASN ILE PHE THR ARG LEU ARG THR GLN LYS GLU                  
HET    NAG  A 201      14                                                       
HET    55R  A 202      18                                                       
HETNAM     NAG N-ACETYL-D-GLUCOSAMINE                                           
HETNAM     55R 2-[2-(4-OXOCYCLOHEXA-2,5-DIEN-1-YLIDENE)                         
HETNAM   2 55R  HYDRAZINYL]BENZOIC ACID                                         
FORMUL   2  NAG    C8 H15 N O6                                                  
FORMUL   3  55R    C13 H10 N2 O3                                                
FORMUL   4  HOH   *51(H2 O)                                                     
HELIX    1 AA1 ASP A  105  LYS A  111  5                                   7    
SHEET    1 AA1 9 GLY A   8  ASN A  12  0                                        
SHEET    2 AA1 9 ASN A  17  ILE A  20 -1  O  ILE A  20   N  GLY A   8           
SHEET    3 AA1 9 GLU A  28  THR A  34 -1  O  THR A  34   N  ASN A  17           
SHEET    4 AA1 9 GLU A  46  GLU A  53 -1  O  GLY A  51   N  PHE A  29           
SHEET    5 AA1 9 THR A  63  ASN A  69 -1  O  THR A  67   N  HIS A  50           
SHEET    6 AA1 9 THR A  76  ASP A  86 -1  O  PHE A  79   N  PHE A  66           
SHEET    7 AA1 9 LYS A  90  ARG A 100 -1  O  ARG A 100   N  THR A  76           
SHEET    8 AA1 9 THR A 113  ARG A 122 -1  O  ARG A 114   N  LEU A  99           
SHEET    9 AA1 9 GLY A   8  ASN A  12 -1  N  THR A  11   O  THR A 121           
SSBOND   1 CYS A    4    CYS A   83                          1555   1555  2.00  
LINK         ND2 ASN A  17                 C1  NAG A 201     1555   1555  1.45  
SITE     1 AC1 10 ASN A  12  SER A  16  TYR A  33  THR A  35                    
SITE     2 AC1 10 VAL A  37  TRP A  70  SER A  73  THR A  77                    
SITE     3 AC1 10 TRP A  97  ASN A 118                                          
SITE     1 AC2  4 GLY A  15  ASN A  17  THR A  34  LEU A 123                    
CRYST1   61.310   61.310  120.530  90.00  90.00 120.00 P 64 2 2     12          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.016311  0.009417  0.000000        0.00000                         
SCALE2      0.000000  0.018834  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.008297        0.00000                         
ATOM      1  N   LYS A   3      25.027   6.716   5.189  1.00 93.43           N  
ANISOU    1  N   LYS A   3     9276  15355  10868  -1846   1444   -451       N  
ATOM      2  CA  LYS A   3      25.249   5.543   6.109  1.00 96.70           C  
ANISOU    2  CA  LYS A   3     9613  15763  11364  -1538   1379   -685       C  
ATOM      3  C   LYS A   3      24.845   5.805   7.621  1.00 94.86           C  
ANISOU    3  C   LYS A   3     9463  15235  11343  -1451   1205   -695       C  
ATOM      4  O   LYS A   3      25.602   6.444   8.376  1.00 99.19           O  
ANISOU    4  O   LYS A   3     9879  15805  12002  -1561   1177   -715       O  
ATOM      5  CB  LYS A   3      26.694   5.108   5.987  1.00104.24           C  
ANISOU    5  CB  LYS A   3    10256  17063  12285  -1512   1500   -853       C  
ATOM      6  CG  LYS A   3      27.712   6.264   5.933  1.00113.08           C  
ANISOU    6  CG  LYS A   3    11180  18349  13435  -1814   1572   -766       C  
ATOM      7  CD  LYS A   3      29.138   5.771   5.708  1.00117.84           C  
ANISOU    7  CD  LYS A   3    11436  19340  13996  -1781   1709   -929       C  
ATOM      8  CE  LYS A   3      29.332   5.120   4.338  1.00118.80           C  
ANISOU    8  CE  LYS A   3    11503  19737  13896  -1750   1905   -990       C  
ATOM      9  NZ  LYS A   3      30.788   4.898   4.053  1.00122.83           N  
ANISOU    9  NZ  LYS A   3    11642  20650  14375  -1769   2072  -1123       N  
ATOM     10  N   CYS A   4      23.632   5.354   8.021  1.00 92.38           N  
ANISOU   10  N   CYS A   4     9371  14660  11070  -1281   1094   -677       N  
ATOM     11  CA  CYS A   4      23.055   5.526   9.430  1.00 87.87           C  
ANISOU   11  CA  CYS A   4     8911  13805  10669  -1186    943   -687       C  
ATOM     12  C   CYS A   4      23.344   4.271  10.194  1.00 82.46           C  
ANISOU   12  C   CYS A   4     8151  13167  10010   -914    881   -874       C  
ATOM     13  O   CYS A   4      22.939   3.157   9.803  1.00 79.38           O  
ANISOU   13  O   CYS A   4     7818  12790   9550   -722    887   -942       O  
ATOM     14  CB  CYS A   4      21.523   5.801   9.500  1.00 85.00           C  
ANISOU   14  CB  CYS A   4     8815  13133  10348  -1160    864   -543       C  
ATOM     15  SG  CYS A   4      20.857   6.660  10.980  1.00 84.18           S  
ANISOU   15  SG  CYS A   4     8849  12691  10443  -1171    742   -503       S  
ATOM     16  N   SER A   5      24.079   4.473  11.278  1.00 77.24           N  
ANISOU   16  N   SER A   5     7364  12532   9451   -912    815   -952       N  
ATOM     17  CA  SER A   5      24.675   3.405  11.986  1.00 72.46           C  
ANISOU   17  CA  SER A   5     6626  12029   8876   -684    756  -1108       C  
ATOM     18  C   SER A   5      24.218   3.422  13.385  1.00 64.64           C  
ANISOU   18  C   SER A   5     5740  10834   7984   -604    604  -1120       C  
ATOM     19  O   SER A   5      24.277   4.448  14.014  1.00 61.86           O  
ANISOU   19  O   SER A   5     5409  10399   7693   -778    563  -1078       O  
ATOM     20  CB  SER A   5      26.179   3.586  11.991  1.00 75.91           C  
ANISOU   20  CB  SER A   5     6755  12763   9322   -765    810  -1189       C  
ATOM     21  OG  SER A   5      26.716   2.457  12.652  1.00 80.51           O  
ANISOU   21  OG  SER A   5     7203  13438   9947   -505    740  -1324       O  
ATOM     22  N   LEU A   6      23.795   2.257  13.859  1.00 64.27           N  
ANISOU   22  N   LEU A   6     5761  10712   7945   -348    527  -1184       N  
ATOM     23  CA  LEU A   6      23.328   2.064  15.240  1.00 63.67           C  
ANISOU   23  CA  LEU A   6     5789  10465   7936   -247    381  -1196       C  
ATOM     24  C   LEU A   6      24.434   2.003  16.306  1.00 63.27           C  
ANISOU   24  C   LEU A   6     5541  10566   7930   -223    286  -1281       C  
ATOM     25  O   LEU A   6      24.181   2.301  17.483  1.00 63.02           O  
ANISOU   25  O   LEU A   6     5588  10423   7930   -245    174  -1280       O  
ATOM     26  CB  LEU A   6      22.497   0.778  15.350  1.00 65.02           C  
ANISOU   26  CB  LEU A   6     6102  10505   8095      4    328  -1213       C  
ATOM     27  CG  LEU A   6      21.137   0.629  14.644  1.00 67.99           C  
ANISOU   27  CG  LEU A   6     6706  10693   8432     13    363  -1125       C  
ATOM     28  CD1 LEU A   6      20.547  -0.695  15.078  1.00 70.85           C  
ANISOU   28  CD1 LEU A   6     7174  10941   8803    250    281  -1162       C  
ATOM     29  CD2 LEU A   6      20.186   1.732  14.979  1.00 65.01           C  
ANISOU   29  CD2 LEU A   6     6491  10116   8094   -139    346  -1007       C  
ATOM     30  N   THR A   7      25.616   1.544  15.905  1.00 64.38           N  
ANISOU   30  N   THR A   7     5424  10970   8065   -166    329  -1359       N  
ATOM     31  CA  THR A   7      26.732   1.408  16.794  1.00 66.44           C  
ANISOU   31  CA  THR A   7     5456  11417   8372   -132    231  -1426       C  
ATOM     32  C   THR A   7      27.051   2.805  17.400  1.00 66.36           C  
ANISOU   32  C   THR A   7     5419  11414   8378   -430    193  -1400       C  
ATOM     33  O   THR A   7      27.201   3.794  16.674  1.00 68.91           O  
ANISOU   33  O   THR A   7     5722  11766   8692   -669    301  -1356       O  
ATOM     34  CB  THR A   7      27.959   0.834  16.026  1.00 68.73           C  
ANISOU   34  CB  THR A   7     5438  12011   8664    -42    324  -1506       C  
ATOM     35  OG1 THR A   7      27.672  -0.486  15.516  1.00 68.45           O  
ANISOU   35  OG1 THR A   7     5447  11938   8623    243    362  -1559       O  
ATOM     36  CG2 THR A   7      29.102   0.720  16.915  1.00 68.92           C  
ANISOU   36  CG2 THR A   7     5195  12243   8745     -7    212  -1555       C  
ATOM     37  N   GLY A   8      27.148   2.878  18.718  1.00 64.22           N  
ANISOU   37  N   GLY A   8     5161  11113   8127   -428     38  -1425       N  
ATOM     38  CA  GLY A   8      27.412   4.143  19.377  1.00 64.37           C  
ANISOU   38  CA  GLY A   8     5184  11117   8156   -710     -7  -1431       C  
ATOM     39  C   GLY A   8      26.594   4.349  20.638  1.00 65.98           C  
ANISOU   39  C   GLY A   8     5618  11106   8345   -710   -127  -1438       C  
ATOM     40  O   GLY A   8      26.055   3.384  21.215  1.00 67.57           O  
ANISOU   40  O   GLY A   8     5918  11232   8523   -480   -210  -1434       O  
ATOM     41  N   LYS A   9      26.512   5.621  21.038  1.00 70.41           N  
ANISOU   41  N   LYS A   9     6268  11563   8920   -977   -125  -1453       N  
ATOM     42  CA  LYS A   9      25.932   6.082  22.292  1.00 75.51           C  
ANISOU   42  CA  LYS A   9     7109  12038   9541  -1041   -219  -1497       C  
ATOM     43  C   LYS A   9      24.723   6.950  21.976  1.00 74.10           C  
ANISOU   43  C   LYS A   9     7205  11539   9408  -1133   -109  -1448       C  
ATOM     44  O   LYS A   9      24.797   7.832  21.082  1.00 74.39           O  
ANISOU   44  O   LYS A   9     7240  11518   9504  -1315      1  -1398       O  
ATOM     45  CB  LYS A   9      26.929   6.924  23.006  1.00 85.03           C  
ANISOU   45  CB  LYS A   9     8182  13386  10736  -1295   -302  -1583       C  
ATOM     46  CG  LYS A   9      27.813   6.140  23.918  1.00 95.39           C  
ANISOU   46  CG  LYS A   9     9294  14961  11986  -1195   -476  -1633       C  
ATOM     47  CD  LYS A   9      27.127   6.016  25.276  1.00106.71           C  
ANISOU   47  CD  LYS A   9    10939  16270  13335  -1148   -597  -1677       C  
ATOM     48  CE  LYS A   9      28.045   5.351  26.308  1.00112.62           C  
ANISOU   48  CE  LYS A   9    11495  17293  14002  -1087   -802  -1707       C  
ATOM     49  NZ  LYS A   9      29.436   5.871  26.332  1.00119.26           N  
ANISOU   49  NZ  LYS A   9    12039  18417  14856  -1301   -872  -1757       N  
ATOM     50  N   TRP A  10      23.609   6.682  22.657  1.00 65.59           N  
ANISOU   50  N   TRP A  10     6350  10259   8309  -1004   -136  -1445       N  
ATOM     51  CA  TRP A  10      22.350   7.335  22.303  1.00 61.24           C  
ANISOU   51  CA  TRP A  10     6039   9409   7821  -1030    -28  -1382       C  
ATOM     52  C   TRP A  10      21.702   7.711  23.570  1.00 60.01           C  
ANISOU   52  C   TRP A  10     6067   9092   7641  -1049    -72  -1459       C  
ATOM     53  O   TRP A  10      21.962   7.070  24.587  1.00 57.92           O  
ANISOU   53  O   TRP A  10     5774   8948   7282   -969   -188  -1525       O  
ATOM     54  CB  TRP A  10      21.410   6.372  21.628  1.00 57.24           C  
ANISOU   54  CB  TRP A  10     5610   8826   7310   -797     14  -1281       C  
ATOM     55  CG  TRP A  10      21.909   5.864  20.409  1.00 58.44           C  
ANISOU   55  CG  TRP A  10     5613   9130   7459   -751     67  -1226       C  
ATOM     56  CD1 TRP A  10      22.574   4.686  20.218  1.00 59.40           C  
ANISOU   56  CD1 TRP A  10     5570   9464   7534   -582     21  -1251       C  
ATOM     57  CD2 TRP A  10      21.764   6.457  19.132  1.00 58.33           C  
ANISOU   57  CD2 TRP A  10     5604   9074   7485   -862    185  -1132       C  
ATOM     58  NE1 TRP A  10      22.839   4.501  18.873  1.00 59.68           N  
ANISOU   58  NE1 TRP A  10     5510   9595   7568   -580    122  -1204       N  
ATOM     59  CE2 TRP A  10      22.372   5.590  18.190  1.00 59.08           C  
ANISOU   59  CE2 TRP A  10     5534   9383   7530   -765    219  -1123       C  
ATOM     60  CE3 TRP A  10      21.179   7.632  18.681  1.00 60.83           C  
ANISOU   60  CE3 TRP A  10     6050   9189   7873  -1029    267  -1048       C  
ATOM     61  CZ2 TRP A  10      22.435   5.883  16.831  1.00 58.48           C  
ANISOU   61  CZ2 TRP A  10     5420   9356   7442   -856    334  -1039       C  
ATOM     62  CZ3 TRP A  10      21.224   7.917  17.284  1.00 63.85           C  
ANISOU   62  CZ3 TRP A  10     6393   9608   8258  -1115    366   -931       C  
ATOM     63  CH2 TRP A  10      21.859   7.046  16.399  1.00 59.63           C  
ANISOU   63  CH2 TRP A  10     5695   9319   7641  -1038    399   -932       C  
ATOM     64  N   THR A  11      20.841   8.715  23.516  1.00 58.57           N  
ANISOU   64  N   THR A  11     6072   8640   7539  -1143     21  -1446       N  
ATOM     65  CA  THR A  11      20.036   9.045  24.678  1.00 60.24           C  
ANISOU   65  CA  THR A  11     6479   8678   7729  -1131     15  -1531       C  
ATOM     66  C   THR A  11      18.623   9.389  24.200  1.00 56.71           C  
ANISOU   66  C   THR A  11     6215   7944   7387  -1044    137  -1434       C  
ATOM     67  O   THR A  11      18.444   9.781  23.040  1.00 53.91           O  
ANISOU   67  O   THR A  11     5847   7504   7130  -1080    215  -1315       O  
ATOM     68  CB  THR A  11      20.731  10.109  25.540  1.00 66.37           C  
ANISOU   68  CB  THR A  11     7274   9448   8493  -1382    -18  -1689       C  
ATOM     69  OG1 THR A  11      20.047  10.261  26.801  1.00 68.23           O  
ANISOU   69  OG1 THR A  11     7692   9570   8662  -1358    -28  -1805       O  
ATOM     70  CG2 THR A  11      20.770  11.417  24.806  1.00 68.44           C  
ANISOU   70  CG2 THR A  11     7585   9516   8902  -1589     86  -1665       C  
ATOM     71  N   ASN A  12      17.637   9.055  25.024  1.00 55.65           N  
ANISOU   71  N   ASN A  12     6223   7706   7216   -910    144  -1461       N  
ATOM     72  CA  ASN A  12      16.215   9.142  24.616  1.00 57.55           C  
ANISOU   72  CA  ASN A  12     6598   7714   7550   -783    247  -1352       C  
ATOM     73  C   ASN A  12      15.594  10.353  25.213  1.00 63.09           C  
ANISOU   73  C   ASN A  12     7463   8162   8345   -870    340  -1437       C  
ATOM     74  O   ASN A  12      16.195  10.994  26.090  1.00 61.34           O  
ANISOU   74  O   ASN A  12     7277   7944   8082  -1022    320  -1604       O  
ATOM     75  CB  ASN A  12      15.359   7.836  24.797  1.00 51.76           C  
ANISOU   75  CB  ASN A  12     5891   7029   6745   -553    217  -1276       C  
ATOM     76  CG  ASN A  12      15.024   7.481  26.199  1.00 51.73           C  
ANISOU   76  CG  ASN A  12     5976   7050   6628   -497    183  -1377       C  
ATOM     77  OD1 ASN A  12      15.114   8.300  27.112  1.00 54.24           O  
ANISOU   77  OD1 ASN A  12     6377   7305   6924   -612    208  -1518       O  
ATOM     78  ND2 ASN A  12      14.663   6.209  26.403  1.00 52.15           N  
ANISOU   78  ND2 ASN A  12     6017   7202   6594   -332    122  -1309       N  
ATOM     79  N   ASP A  13      14.390  10.661  24.722  1.00 66.96           N  
ANISOU   79  N   ASP A  13     8046   8430   8963   -773    441  -1326       N  
ATOM     80  CA  ASP A  13      13.669  11.831  25.192  1.00 68.93           C  
ANISOU   80  CA  ASP A  13     8449   8396   9342   -814    553  -1397       C  
ATOM     81  C   ASP A  13      13.385  11.753  26.697  1.00 67.27           C  
ANISOU   81  C   ASP A  13     8344   8192   9021   -786    567  -1587       C  
ATOM     82  O   ASP A  13      13.168  12.786  27.275  1.00 72.02           O  
ANISOU   82  O   ASP A  13     9070   8596   9697   -867    653  -1722       O  
ATOM     83  CB  ASP A  13      12.420  12.109  24.349  1.00 71.96           C  
ANISOU   83  CB  ASP A  13     8880   8563   9897   -688    647  -1215       C  
ATOM     84  CG  ASP A  13      11.533  10.899  24.231  1.00 76.00           C  
ANISOU   84  CG  ASP A  13     9358   9175  10343   -483    625  -1101       C  
ATOM     85  OD1 ASP A  13      11.914   9.982  23.481  1.00 68.67           O  
ANISOU   85  OD1 ASP A  13     8322   8431   9335   -450    544   -999       O  
ATOM     86  OD2 ASP A  13      10.490  10.840  24.933  1.00 84.90           O  
ANISOU   86  OD2 ASP A  13    10565  10203  11489   -363    693  -1129       O  
ATOM     87  N   LEU A  14      13.409  10.569  27.327  1.00 63.91           N  
ANISOU   87  N   LEU A  14     7880   7986   8416   -683    485  -1602       N  
ATOM     88  CA  LEU A  14      13.258  10.425  28.797  1.00 64.65           C  
ANISOU   88  CA  LEU A  14     8069   8140   8354   -683    482  -1772       C  
ATOM     89  C   LEU A  14      14.549  10.556  29.602  1.00 67.06           C  
ANISOU   89  C   LEU A  14     8344   8631   8505   -864    368  -1941       C  
ATOM     90  O   LEU A  14      14.521  10.473  30.814  1.00 67.56           O  
ANISOU   90  O   LEU A  14     8489   8771   8409   -893    350  -2083       O  
ATOM     91  CB  LEU A  14      12.659   9.060  29.139  1.00 69.18           C  
ANISOU   91  CB  LEU A  14     8623   8862   8800   -500    436  -1678       C  
ATOM     92  CG  LEU A  14      11.362   8.652  28.400  1.00 71.57           C  
ANISOU   92  CG  LEU A  14     8930   9041   9221   -322    517  -1496       C  
ATOM     93  CD1 LEU A  14      10.992   7.251  28.843  1.00 71.82           C  
ANISOU   93  CD1 LEU A  14     8942   9239   9106   -189    447  -1419       C  
ATOM     94  CD2 LEU A  14      10.210   9.651  28.632  1.00 70.32           C  
ANISOU   94  CD2 LEU A  14     8887   8622   9207   -286    691  -1537       C  
ATOM     95  N   GLY A  15      15.698  10.737  28.954  1.00 64.93           N  
ANISOU   95  N   GLY A  15     7943   8463   8263   -995    285  -1922       N  
ATOM     96  CA  GLY A  15      16.982  10.692  29.677  1.00 66.17           C  
ANISOU   96  CA  GLY A  15     8021   8853   8266  -1160    146  -2054       C  
ATOM     97  C   GLY A  15      17.665   9.312  29.831  1.00 67.33           C  
ANISOU   97  C   GLY A  15     8006   9317   8258  -1057    -18  -1976       C  
ATOM     98  O   GLY A  15      18.729   9.254  30.431  1.00 69.65           O  
ANISOU   98  O   GLY A  15     8210   9822   8432  -1182   -148  -2065       O  
ATOM     99  N   SER A  16      17.090   8.210  29.314  1.00 62.61           N  
ANISOU   99  N   SER A  16     7369   8750   7668   -837    -22  -1811       N  
ATOM    100  CA  SER A  16      17.771   6.906  29.362  1.00 62.39           C  
ANISOU  100  CA  SER A  16     7192   8980   7532   -724   -173  -1732       C  
ATOM    101  C   SER A  16      18.938   6.918  28.385  1.00 61.53           C  
ANISOU  101  C   SER A  16     6877   9006   7493   -789   -224  -1694       C  
ATOM    102  O   SER A  16      18.909   7.632  27.399  1.00 62.95           O  
ANISOU  102  O   SER A  16     7043   9065   7810   -864   -128  -1661       O  
ATOM    103  CB  SER A  16      16.816   5.773  29.021  1.00 59.56           C  
ANISOU  103  CB  SER A  16     6868   8579   7182   -491   -154  -1580       C  
ATOM    104  OG  SER A  16      15.762   5.796  29.967  1.00 58.28           O  
ANISOU  104  OG  SER A  16     6877   8318   6948   -450    -95  -1613       O  
ATOM    105  N   ASN A  17      19.986   6.186  28.708  1.00 61.42           N  
ANISOU  105  N   ASN A  17     6699   9252   7385   -769   -375  -1697       N  
ATOM    106  CA  ASN A  17      21.158   6.065  27.815  1.00 66.46           C  
ANISOU  106  CA  ASN A  17     7102  10065   8084   -807   -418  -1665       C  
ATOM    107  C   ASN A  17      21.262   4.617  27.380  1.00 62.51           C  
ANISOU  107  C   ASN A  17     6492   9684   7574   -560   -480  -1548       C  
ATOM    108  O   ASN A  17      21.080   3.688  28.184  1.00 63.46           O  
ANISOU  108  O   ASN A  17     6645   9868   7598   -419   -582  -1518       O  
ATOM    109  CB  ASN A  17      22.477   6.479  28.498  1.00 68.94           C  
ANISOU  109  CB  ASN A  17     7263  10606   8322   -997   -547  -1775       C  
ATOM    110  CG  ASN A  17      22.494   7.943  28.927  1.00 74.65           C  
ANISOU  110  CG  ASN A  17     8102  11202   9058  -1274   -492  -1917       C  
ATOM    111  OD1 ASN A  17      21.844   8.775  28.308  1.00 69.80           O  
ANISOU  111  OD1 ASN A  17     7611  10341   8566  -1338   -344  -1911       O  
ATOM    112  ND2 ASN A  17      23.258   8.266  29.980  1.00 89.40           N  
ANISOU  112  ND2 ASN A  17     9930  13232  10803  -1446   -621  -2043       N  
ATOM    113  N   MET A  18      21.525   4.413  26.107  1.00 60.37           N  
ANISOU  113  N   MET A  18     6104   9433   7401   -510   -413  -1483       N  
ATOM    114  CA  MET A  18      21.979   3.095  25.691  1.00 62.98           C  
ANISOU  114  CA  MET A  18     6288   9911   7728   -298   -479  -1416       C  
ATOM    115  C   MET A  18      23.235   3.145  24.857  1.00 62.78           C  
ANISOU  115  C   MET A  18     6004  10093   7754   -345   -473  -1433       C  
ATOM    116  O   MET A  18      23.481   4.108  24.084  1.00 62.11           O  
ANISOU  116  O   MET A  18     5877   9992   7730   -525   -369  -1449       O  
ATOM    117  CB  MET A  18      20.888   2.310  24.926  1.00 60.91           C  
ANISOU  117  CB  MET A  18     6149   9482   7509   -110   -399  -1318       C  
ATOM    118  CG  MET A  18      20.569   2.825  23.538  1.00 58.92           C  
ANISOU  118  CG  MET A  18     5905   9136   7345   -169   -252  -1277       C  
ATOM    119  SD  MET A  18      19.350   1.747  22.790  1.00 57.48           S  
ANISOU  119  SD  MET A  18     5856   8801   7183     40   -203  -1171       S  
ATOM    120  CE  MET A  18      19.241   2.589  21.218  1.00 55.79           C  
ANISOU  120  CE  MET A  18     5619   8542   7036    -89    -54  -1125       C  
ATOM    121  N   THR A  19      23.936   2.024  24.925  1.00 63.09           N  
ANISOU  121  N   THR A  19     5876  10311   7781   -162   -571  -1413       N  
ATOM    122  CA  THR A  19      25.131   1.838  24.127  1.00 69.14           C  
ANISOU  122  CA  THR A  19     6365  11300   8601   -150   -555  -1431       C  
ATOM    123  C   THR A  19      25.017   0.584  23.374  1.00 65.93           C  
ANISOU  123  C   THR A  19     5921  10891   8237    113   -524  -1385       C  
ATOM    124  O   THR A  19      24.771  -0.449  23.949  1.00 70.30           O  
ANISOU  124  O   THR A  19     6525  11411   8773    315   -624  -1347       O  
ATOM    125  CB  THR A  19      26.323   1.772  25.048  1.00 72.49           C  
ANISOU  125  CB  THR A  19     6572  11981   8987   -189   -720  -1473       C  
ATOM    126  OG1 THR A  19      26.307   2.957  25.851  1.00 78.10           O  
ANISOU  126  OG1 THR A  19     7367  12667   9640   -458   -755  -1538       O  
ATOM    127  CG2 THR A  19      27.635   1.697  24.267  1.00 74.33           C  
ANISOU  127  CG2 THR A  19     6474  12478   9287   -196   -694  -1496       C  
ATOM    128  N   ILE A  20      25.192   0.701  22.078  1.00 66.26           N  
ANISOU  128  N   ILE A  20     5886  10963   8327     95   -381  -1391       N  
ATOM    129  CA  ILE A  20      25.081  -0.422  21.134  1.00 63.72           C  
ANISOU  129  CA  ILE A  20     5540  10633   8038    323   -315  -1380       C  
ATOM    130  C   ILE A  20      26.465  -0.643  20.497  1.00 63.35           C  
ANISOU  130  C   ILE A  20     5172  10865   8032    361   -276  -1439       C  
ATOM    131  O   ILE A  20      27.108   0.316  20.026  1.00 59.68           O  
ANISOU  131  O   ILE A  20     4564  10542   7567    146   -196  -1464       O  
ATOM    132  CB  ILE A  20      24.087  -0.137  20.004  1.00 62.21           C  
ANISOU  132  CB  ILE A  20     5525  10269   7842    268   -162  -1343       C  
ATOM    133  CG1 ILE A  20      22.675   0.026  20.593  1.00 63.30           C  
ANISOU  133  CG1 ILE A  20     5950  10140   7958    254   -191  -1278       C  
ATOM    134  CG2 ILE A  20      24.169  -1.228  18.895  1.00 62.39           C  
ANISOU  134  CG2 ILE A  20     5498  10328   7877    464    -80  -1368       C  
ATOM    135  CD1 ILE A  20      21.611   0.457  19.581  1.00 62.15           C  
ANISOU  135  CD1 ILE A  20     5973   9824   7814    179    -64  -1217       C  
ATOM    136  N   GLY A  21      26.847  -1.919  20.428  1.00 61.49           N  
ANISOU  136  N   GLY A  21     4834  10689   7839    636   -316  -1458       N  
ATOM    137  CA  GLY A  21      28.159  -2.328  20.043  1.00 61.38           C  
ANISOU  137  CA  GLY A  21     4495  10941   7882    739   -297  -1519       C  
ATOM    138  C   GLY A  21      28.125  -2.560  18.572  1.00 62.91           C  
ANISOU  138  C   GLY A  21     4668  11155   8079    780    -97  -1572       C  
ATOM    139  O   GLY A  21      27.274  -2.031  17.848  1.00 60.66           O  
ANISOU  139  O   GLY A  21     4578  10733   7737    638     15  -1549       O  
ATOM    140  N   ALA A  22      29.065  -3.353  18.116  1.00 65.85           N  
ANISOU  140  N   ALA A  22     4796  11710   8514    977    -52  -1645       N  
ATOM    141  CA  ALA A  22      29.193  -3.665  16.692  1.00 69.12           C  
ANISOU  141  CA  ALA A  22     5159  12189   8911   1029    154  -1729       C  
ATOM    142  C   ALA A  22      28.030  -4.475  16.169  1.00 67.56           C  
ANISOU  142  C   ALA A  22     5259  11724   8685   1169    199  -1738       C  
ATOM    143  O   ALA A  22      27.448  -5.318  16.884  1.00 69.54           O  
ANISOU  143  O   ALA A  22     5670  11771   8979   1353     69  -1704       O  
ATOM    144  CB  ALA A  22      30.489  -4.433  16.471  1.00 74.24           C  
ANISOU  144  CB  ALA A  22     5465  13090   9652   1253    191  -1823       C  
ATOM    145  N   VAL A  23      27.678  -4.167  14.935  1.00 67.06           N  
ANISOU  145  N   VAL A  23     5272  11670   8536   1051    375  -1770       N  
ATOM    146  CA  VAL A  23      26.681  -4.903  14.193  1.00 67.46           C  
ANISOU  146  CA  VAL A  23     5571  11520   8538   1149    438  -1800       C  
ATOM    147  C   VAL A  23      27.403  -5.812  13.237  1.00 69.90           C  
ANISOU  147  C   VAL A  23     5728  11971   8858   1344    583  -1957       C  
ATOM    148  O   VAL A  23      28.200  -5.340  12.455  1.00 72.04           O  
ANISOU  148  O   VAL A  23     5793  12497   9080   1243    736  -2016       O  
ATOM    149  CB  VAL A  23      25.743  -3.964  13.388  1.00 69.23           C  
ANISOU  149  CB  VAL A  23     5993  11670   8639    882    530  -1724       C  
ATOM    150  CG1 VAL A  23      24.724  -4.770  12.563  1.00 68.70           C  
ANISOU  150  CG1 VAL A  23     6168  11427   8507    968    583  -1758       C  
ATOM    151  CG2 VAL A  23      24.963  -3.023  14.333  1.00 66.16           C  
ANISOU  151  CG2 VAL A  23     5763  11114   8260    706    405  -1582       C  
ATOM    152  N   ASN A  24      27.105  -7.110  13.271  1.00 69.81           N  
ANISOU  152  N   ASN A  24     5827  11789   8909   1615    549  -2030       N  
ATOM    153  CA  ASN A  24      27.887  -8.080  12.516  1.00 70.14           C  
ANISOU  153  CA  ASN A  24     5713  11941   8994   1851    683  -2208       C  
ATOM    154  C   ASN A  24      27.339  -8.240  11.101  1.00 73.12           C  
ANISOU  154  C   ASN A  24     6250  12304   9226   1777    869  -2313       C  
ATOM    155  O   ASN A  24      26.434  -7.482  10.708  1.00 74.01           O  
ANISOU  155  O   ASN A  24     6558  12355   9207   1525    882  -2218       O  
ATOM    156  CB  ASN A  24      27.905  -9.367  13.284  1.00 69.50           C  
ANISOU  156  CB  ASN A  24     5673  11664   9070   2178    548  -2232       C  
ATOM    157  CG  ASN A  24      26.568 -10.069  13.320  1.00 72.80           C  
ANISOU  157  CG  ASN A  24     6457  11735   9467   2220    476  -2202       C  
ATOM    158  OD1 ASN A  24      25.640  -9.801  12.551  1.00 71.45           O  
ANISOU  158  OD1 ASN A  24     6502  11480   9164   2047    551  -2204       O  
ATOM    159  ND2 ASN A  24      26.468 -11.011  14.215  1.00 75.44           N  
ANISOU  159  ND2 ASN A  24     6855  11870   9936   2448    321  -2162       N  
ATOM    160  N   SER A  25      27.827  -9.219  10.355  1.00 75.75           N  
ANISOU  160  N   SER A  25     6516  12686   9580   1994   1006  -2505       N  
ATOM    161  CA  SER A  25      27.360  -9.504   8.983  1.00 80.56           C  
ANISOU  161  CA  SER A  25     7283  13299  10027   1934   1187  -2641       C  
ATOM    162  C   SER A  25      25.877  -9.879   8.924  1.00 80.84           C  
ANISOU  162  C   SER A  25     7701  13014   9999   1876   1088  -2585       C  
ATOM    163  O   SER A  25      25.211  -9.596   7.925  1.00 80.81           O  
ANISOU  163  O   SER A  25     7859  13030   9814   1686   1181  -2600       O  
ATOM    164  CB  SER A  25      28.196 -10.623   8.338  1.00 82.95           C  
ANISOU  164  CB  SER A  25     7447  13681  10387   2223   1350  -2893       C  
ATOM    165  OG  SER A  25      28.637 -11.501   9.361  1.00 88.89           O  
ANISOU  165  OG  SER A  25     8110  14289  11373   2537   1212  -2901       O  
ATOM    166  N   ARG A  26      25.344 -10.493   9.986  1.00 80.83           N  
ANISOU  166  N   ARG A  26     7839  12735  10138   2022    894  -2505       N  
ATOM    167  CA  ARG A  26      23.960 -10.954   9.980  1.00 78.63           C  
ANISOU  167  CA  ARG A  26     7900  12157   9819   1976    800  -2453       C  
ATOM    168  C   ARG A  26      22.984  -9.939  10.583  1.00 76.57           C  
ANISOU  168  C   ARG A  26     7770  11813   9506   1730    670  -2222       C  
ATOM    169  O   ARG A  26      21.821 -10.271  10.808  1.00 76.71           O  
ANISOU  169  O   ARG A  26     8038  11589   9517   1696    568  -2146       O  
ATOM    170  CB  ARG A  26      23.871 -12.311  10.668  1.00 87.94           C  
ANISOU  170  CB  ARG A  26     9176  13065  11171   2270    685  -2504       C  
ATOM    171  CG  ARG A  26      24.745 -13.367   9.968  1.00102.42           C  
ANISOU  171  CG  ARG A  26    10906  14935  13071   2535    832  -2756       C  
ATOM    172  CD  ARG A  26      24.583 -14.790  10.502  1.00116.80           C  
ANISOU  172  CD  ARG A  26    12866  16434  15078   2829    728  -2813       C  
ATOM    173  NE  ARG A  26      25.570 -15.115  11.551  1.00134.33           N  
ANISOU  173  NE  ARG A  26    14852  18674  17510   3087    626  -2758       N  
ATOM    174  CZ  ARG A  26      25.298 -15.447  12.826  1.00143.37           C  
ANISOU  174  CZ  ARG A  26    16063  19622  18788   3181    406  -2577       C  
ATOM    175  NH1 ARG A  26      24.026 -15.536  13.293  1.00139.79           N  
ANISOU  175  NH1 ARG A  26    15905  18915  18292   3046    268  -2433       N  
ATOM    176  NH2 ARG A  26      26.327 -15.713  13.653  1.00148.10           N  
ANISOU  176  NH2 ARG A  26    16415  20294  19560   3414    320  -2531       N  
ATOM    177  N   GLY A  27      23.465  -8.715  10.849  1.00 71.66           N  
ANISOU  177  N   GLY A  27     6977  11389   8862   1560    680  -2119       N  
ATOM    178  CA  GLY A  27      22.705  -7.659  11.470  1.00 67.44           C  
ANISOU  178  CA  GLY A  27     6538  10783   8304   1345    577  -1922       C  
ATOM    179  C   GLY A  27      22.567  -7.670  12.973  1.00 64.14           C  
ANISOU  179  C   GLY A  27     6133  10228   8008   1418    395  -1809       C  
ATOM    180  O   GLY A  27      21.876  -6.817  13.498  1.00 62.57           O  
ANISOU  180  O   GLY A  27     6029   9955   7788   1248    325  -1667       O  
ATOM    181  N   GLU A  28      23.200  -8.592  13.690  1.00 65.12           N  
ANISOU  181  N   GLU A  28     6167  10318   8257   1665    316  -1861       N  
ATOM    182  CA  GLU A  28      22.958  -8.680  15.160  1.00 63.16           C  
ANISOU  182  CA  GLU A  28     5965   9938   8095   1723    126  -1734       C  
ATOM    183  C   GLU A  28      23.764  -7.663  15.938  1.00 61.42           C  
ANISOU  183  C   GLU A  28     5535   9912   7887   1615     76  -1673       C  
ATOM    184  O   GLU A  28      24.900  -7.306  15.533  1.00 61.88           O  
ANISOU  184  O   GLU A  28     5336  10220   7954   1604    162  -1750       O  
ATOM    185  CB  GLU A  28      23.272 -10.089  15.677  1.00 67.42           C  
ANISOU  185  CB  GLU A  28     6507  10346   8763   2026     34  -1778       C  
ATOM    186  CG  GLU A  28      22.416 -11.137  14.983  1.00 75.35           C  
ANISOU  186  CG  GLU A  28     7749  11116   9763   2114     70  -1847       C  
ATOM    187  CD  GLU A  28      23.115 -12.471  14.759  1.00 86.87           C  
ANISOU  187  CD  GLU A  28     9150  12508  11347   2418     90  -1988       C  
ATOM    188  OE1 GLU A  28      24.053 -12.523  13.917  1.00 95.46           O  
ANISOU  188  OE1 GLU A  28    10047  13784  12437   2496    240  -2149       O  
ATOM    189  OE2 GLU A  28      22.701 -13.466  15.408  1.00 89.31           O  
ANISOU  189  OE2 GLU A  28     9608  12567  11756   2577    -35  -1937       O  
ATOM    190  N   PHE A  29      23.208  -7.209  17.058  1.00 57.74           N  
ANISOU  190  N   PHE A  29     5171   9346   7420   1528    -57  -1546       N  
ATOM    191  CA  PHE A  29      23.995  -6.389  17.957  1.00 56.62           C  
ANISOU  191  CA  PHE A  29     4848   9372   7290   1438   -134  -1505       C  
ATOM    192  C   PHE A  29      23.546  -6.631  19.367  1.00 57.06           C  
ANISOU  192  C   PHE A  29     5020   9299   7362   1484   -314  -1401       C  
ATOM    193  O   PHE A  29      22.444  -7.158  19.620  1.00 58.66           O  
ANISOU  193  O   PHE A  29     5461   9273   7553   1526   -359  -1336       O  
ATOM    194  CB  PHE A  29      23.878  -4.929  17.567  1.00 56.94           C  
ANISOU  194  CB  PHE A  29     4877   9501   7256   1144    -44  -1480       C  
ATOM    195  CG  PHE A  29      22.446  -4.410  17.534  1.00 54.69           C  
ANISOU  195  CG  PHE A  29     4865   8999   6914    997    -34  -1388       C  
ATOM    196  CD1 PHE A  29      21.790  -4.000  18.712  1.00 56.20           C  
ANISOU  196  CD1 PHE A  29     5186   9065   7102    930   -144  -1301       C  
ATOM    197  CD2 PHE A  29      21.734  -4.388  16.353  1.00 53.56           C  
ANISOU  197  CD2 PHE A  29     4843   8788   6719    935     81  -1390       C  
ATOM    198  CE1 PHE A  29      20.457  -3.526  18.663  1.00 55.26           C  
ANISOU  198  CE1 PHE A  29     5292   8754   6950    815   -120  -1218       C  
ATOM    199  CE2 PHE A  29      20.432  -3.952  16.317  1.00 51.09           C  
ANISOU  199  CE2 PHE A  29     4748   8290   6371    819     78  -1292       C  
ATOM    200  CZ  PHE A  29      19.798  -3.498  17.433  1.00 49.15           C  
ANISOU  200  CZ  PHE A  29     4609   7920   6146    764    -12  -1207       C  
ATOM    201  N   THR A  30      24.391  -6.171  20.260  1.00 57.44           N  
ANISOU  201  N   THR A  30     4893   9514   7419   1446   -412  -1381       N  
ATOM    202  CA  THR A  30      24.257  -6.278  21.682  1.00 60.31           C  
ANISOU  202  CA  THR A  30     5311   9836   7766   1465   -592  -1289       C  
ATOM    203  C   THR A  30      24.557  -4.939  22.263  1.00 60.68           C  
ANISOU  203  C   THR A  30     5287  10021   7746   1214   -615  -1285       C  
ATOM    204  O   THR A  30      25.164  -4.098  21.608  1.00 58.44           O  
ANISOU  204  O   THR A  30     4850   9890   7461   1066   -514  -1348       O  
ATOM    205  CB  THR A  30      25.262  -7.270  22.181  1.00 66.64           C  
ANISOU  205  CB  THR A  30     5924  10742   8653   1710   -717  -1283       C  
ATOM    206  OG1 THR A  30      24.803  -8.526  21.725  1.00 73.09           O  
ANISOU  206  OG1 THR A  30     6868  11361   9541   1937   -698  -1286       O  
ATOM    207  CG2 THR A  30      25.316  -7.358  23.697  1.00 70.70           C  
ANISOU  207  CG2 THR A  30     6460  11274   9127   1717   -925  -1171       C  
ATOM    208  N   GLY A  31      24.070  -4.722  23.486  1.00 64.61           N  
ANISOU  208  N   GLY A  31     5916  10453   8179   1149   -739  -1214       N  
ATOM    209  CA  GLY A  31      24.336  -3.473  24.190  1.00 63.09           C  
ANISOU  209  CA  GLY A  31     5683  10370   7915    905   -773  -1232       C  
ATOM    210  C   GLY A  31      23.923  -3.456  25.629  1.00 62.04           C  
ANISOU  210  C   GLY A  31     5683  10197   7690    869   -920  -1171       C  
ATOM    211  O   GLY A  31      23.523  -4.486  26.187  1.00 60.85           O  
ANISOU  211  O   GLY A  31     5634   9956   7530   1043  -1018  -1087       O  
ATOM    212  N   THR A  32      24.013  -2.263  26.214  1.00 62.48           N  
ANISOU  212  N   THR A  32     5750  10317   7672    628   -929  -1216       N  
ATOM    213  CA  THR A  32      23.472  -2.002  27.543  1.00 65.25           C  
ANISOU  213  CA  THR A  32     6265  10625   7899    540  -1027  -1190       C  
ATOM    214  C   THR A  32      22.516  -0.790  27.516  1.00 61.96           C  
ANISOU  214  C   THR A  32     6046  10044   7449    325   -893  -1243       C  
ATOM    215  O   THR A  32      22.637   0.099  26.663  1.00 63.08           O  
ANISOU  215  O   THR A  32     6145  10166   7654    188   -767  -1300       O  
ATOM    216  CB  THR A  32      24.572  -1.704  28.503  1.00 69.65           C  
ANISOU  216  CB  THR A  32     6649  11431   8383    448  -1191  -1218       C  
ATOM    217  OG1 THR A  32      25.245  -0.558  27.989  1.00 74.03           O  
ANISOU  217  OG1 THR A  32     7063  12092   8972    233  -1114  -1321       O  
ATOM    218  CG2 THR A  32      25.526  -2.915  28.660  1.00 72.88           C  
ANISOU  218  CG2 THR A  32     6843  12005   8840    686  -1348  -1142       C  
ATOM    219  N   TYR A  33      21.567  -0.807  28.439  1.00 59.04           N  
ANISOU  219  N   TYR A  33     5889   9557   6986    310   -915  -1212       N  
ATOM    220  CA  TYR A  33      20.526   0.210  28.548  1.00 57.88           C  
ANISOU  220  CA  TYR A  33     5940   9232   6819    155   -785  -1258       C  
ATOM    221  C   TYR A  33      20.559   0.706  29.982  1.00 61.23           C  
ANISOU  221  C   TYR A  33     6445   9729   7090     21   -870  -1318       C  
ATOM    222  O   TYR A  33      20.455  -0.108  30.922  1.00 61.88           O  
ANISOU  222  O   TYR A  33     6576   9875   7060    113   -992  -1251       O  
ATOM    223  CB  TYR A  33      19.169  -0.403  28.244  1.00 57.62           C  
ANISOU  223  CB  TYR A  33     6091   8985   6815    284   -701  -1166       C  
ATOM    224  CG  TYR A  33      18.132   0.589  27.761  1.00 52.82           C  
ANISOU  224  CG  TYR A  33     5623   8181   6264    174   -532  -1191       C  
ATOM    225  CD1 TYR A  33      17.819   0.699  26.437  1.00 51.45           C  
ANISOU  225  CD1 TYR A  33     5433   7909   6206    196   -422  -1156       C  
ATOM    226  CD2 TYR A  33      17.519   1.404  28.619  1.00 50.88           C  
ANISOU  226  CD2 TYR A  33     5516   7859   5955     56   -486  -1248       C  
ATOM    227  CE1 TYR A  33      16.879   1.626  25.997  1.00 50.12           C  
ANISOU  227  CE1 TYR A  33     5378   7562   6101    104   -285  -1150       C  
ATOM    228  CE2 TYR A  33      16.585   2.329  28.192  1.00 52.35           C  
ANISOU  228  CE2 TYR A  33     5816   7852   6222    -18   -331  -1264       C  
ATOM    229  CZ  TYR A  33      16.250   2.440  26.885  1.00 48.76           C  
ANISOU  229  CZ  TYR A  33     5337   7294   5895      9   -239  -1201       C  
ATOM    230  OH  TYR A  33      15.309   3.411  26.514  1.00 47.27           O  
ANISOU  230  OH  TYR A  33     5253   6910   5796    -59   -101  -1194       O  
ATOM    231  N   THR A  34      20.748   2.013  30.168  1.00 61.02           N  
ANISOU  231  N   THR A  34     6437   9696   7049   -203   -813  -1443       N  
ATOM    232  CA  THR A  34      20.746   2.605  31.492  1.00 64.60           C  
ANISOU  232  CA  THR A  34     6991  10210   7344   -359   -874  -1539       C  
ATOM    233  C   THR A  34      19.556   3.528  31.544  1.00 63.99           C  
ANISOU  233  C   THR A  34     7134   9888   7289   -448   -695  -1609       C  
ATOM    234  O   THR A  34      19.530   4.587  30.916  1.00 62.23           O  
ANISOU  234  O   THR A  34     6923   9542   7179   -577   -577  -1683       O  
ATOM    235  CB  THR A  34      22.028   3.384  31.736  1.00 71.73           C  
ANISOU  235  CB  THR A  34     7731  11306   8217   -566   -965  -1653       C  
ATOM    236  OG1 THR A  34      23.138   2.497  31.568  1.00 77.20           O  
ANISOU  236  OG1 THR A  34     8176  12232   8921   -453  -1121  -1574       O  
ATOM    237  CG2 THR A  34      22.068   3.956  33.161  1.00 74.50           C  
ANISOU  237  CG2 THR A  34     8196  11738   8370   -747  -1045  -1773       C  
ATOM    238  N   THR A  35      18.569   3.110  32.304  1.00 64.06           N  
ANISOU  238  N   THR A  35     7313   9828   7198   -372   -674  -1574       N  
ATOM    239  CA  THR A  35      17.261   3.740  32.241  1.00 64.16           C  
ANISOU  239  CA  THR A  35     7513   9600   7262   -385   -487  -1606       C  
ATOM    240  C   THR A  35      17.204   4.940  33.152  1.00 64.45           C  
ANISOU  240  C   THR A  35     7671   9605   7210   -585   -430  -1795       C  
ATOM    241  O   THR A  35      17.847   4.950  34.214  1.00 71.85           O  
ANISOU  241  O   THR A  35     8607  10729   7963   -692   -553  -1879       O  
ATOM    242  CB  THR A  35      16.106   2.758  32.617  1.00 62.83           C  
ANISOU  242  CB  THR A  35     7466   9370   7035   -218   -460  -1483       C  
ATOM    243  OG1 THR A  35      14.875   3.481  32.759  1.00 63.63           O  
ANISOU  243  OG1 THR A  35     7728   9274   7172   -246   -277  -1534       O  
ATOM    244  CG2 THR A  35      16.358   2.028  33.923  1.00 62.27           C  
ANISOU  244  CG2 THR A  35     7429   9489   6740   -211   -607  -1459       C  
ATOM    245  N   ALA A  36      16.420   5.945  32.755  1.00 65.53           N  
ANISOU  245  N   ALA A  36     7918   9502   7477   -636   -247  -1863       N  
ATOM    246  CA  ALA A  36      16.177   7.172  33.596  1.00 68.23           C  
ANISOU  246  CA  ALA A  36     8414   9744   7764   -811   -150  -2071       C  
ATOM    247  C   ALA A  36      14.877   7.147  34.397  1.00 71.79           C  
ANISOU  247  C   ALA A  36     9049  10092   8135   -738    -19  -2105       C  
ATOM    248  O   ALA A  36      14.491   8.132  35.025  1.00 79.85           O  
ANISOU  248  O   ALA A  36    10212  10995   9130   -846    101  -2287       O  
ATOM    249  CB  ALA A  36      16.205   8.419  32.733  1.00 66.34           C  
ANISOU  249  CB  ALA A  36     8185   9282   7737   -920    -27  -2138       C  
ATOM    250  N   VAL A  37      14.233   5.991  34.423  1.00 75.94           N  
ANISOU  250  N   VAL A  37     9570  10670   8613   -561    -40  -1939       N  
ATOM    251  CA  VAL A  37      12.803   5.860  34.656  1.00 74.03           C  
ANISOU  251  CA  VAL A  37     9450  10294   8385   -449    118  -1898       C  
ATOM    252  C   VAL A  37      12.468   5.353  36.094  1.00 79.91           C  
ANISOU  252  C   VAL A  37    10303  11200   8857   -464     97  -1937       C  
ATOM    253  O   VAL A  37      11.303   5.421  36.518  1.00 83.47           O  
ANISOU  253  O   VAL A  37    10863  11566   9286   -409    256  -1948       O  
ATOM    254  CB  VAL A  37      12.288   4.984  33.496  1.00 73.17           C  
ANISOU  254  CB  VAL A  37     9252  10112   8435   -270    117  -1673       C  
ATOM    255  CG1 VAL A  37      11.401   3.781  33.926  1.00 66.80           C  
ANISOU  255  CG1 VAL A  37     8488   9362   7530   -135    109  -1523       C  
ATOM    256  CG2 VAL A  37      11.771   5.902  32.359  1.00 76.96           C  
ANISOU  256  CG2 VAL A  37     9723  10348   9168   -258    261  -1665       C  
ATOM    257  N   THR A  38      13.486   4.925  36.857  1.00 82.03           N  
ANISOU  257  N   THR A  38    10539  11712   8916   -551    -91  -1959       N  
ATOM    258  CA  THR A  38      13.323   4.312  38.190  1.00 87.90           C  
ANISOU  258  CA  THR A  38    11374  12654   9368   -577   -154  -1953       C  
ATOM    259  C   THR A  38      13.677   5.189  39.399  1.00 92.91           C  
ANISOU  259  C   THR A  38    12127  13401   9773   -787   -144  -2199       C  
ATOM    260  O   THR A  38      14.355   6.205  39.226  1.00 95.56           O  
ANISOU  260  O   THR A  38    12449  13685  10173   -932   -144  -2376       O  
ATOM    261  CB  THR A  38      14.203   3.062  38.315  1.00 89.09           C  
ANISOU  261  CB  THR A  38    11408  13028   9414   -518   -406  -1770       C  
ATOM    262  OG1 THR A  38      15.591   3.451  38.471  1.00 96.48           O  
ANISOU  262  OG1 THR A  38    12239  14126  10291   -657   -575  -1867       O  
ATOM    263  CG2 THR A  38      13.963   2.159  37.124  1.00 81.64           C  
ANISOU  263  CG2 THR A  38    10359  11974   8687   -322   -423  -1558       C  
ATOM    264  N   ALA A  39      13.231   4.760  40.603  1.00101.90           N  
ANISOU  264  N   ALA A  39    13384  14697  10633   -815   -141  -2204       N  
ATOM    265  CA  ALA A  39      13.541   5.448  41.897  1.00113.66           C  
ANISOU  265  CA  ALA A  39    15008  16344  11832  -1028   -144  -2441       C  
ATOM    266  C   ALA A  39      15.000   5.278  42.115  1.00120.76           C  
ANISOU  266  C   ALA A  39    15793  17475  12615  -1153   -419  -2436       C  
ATOM    267  O   ALA A  39      15.540   4.193  41.875  1.00130.24           O  
ANISOU  267  O   ALA A  39    16855  18813  13815  -1048   -619  -2203       O  
ATOM    268  CB  ALA A  39      12.790   4.852  43.100  1.00114.80           C  
ANISOU  268  CB  ALA A  39    15290  16657  11670  -1031    -98  -2404       C  
ATOM    269  N   THR A  40      15.639   6.337  42.576  1.00129.02           N  
ANISOU  269  N   THR A  40    16890  18560  13569  -1376   -432  -2692       N  
ATOM    270  CA  THR A  40      17.079   6.359  42.576  1.00133.70           C  
ANISOU  270  CA  THR A  40    17333  19353  14114  -1511   -685  -2698       C  
ATOM    271  C   THR A  40      17.636   5.196  43.415  1.00141.99           C  
ANISOU  271  C   THR A  40    18320  20743  14884  -1498   -945  -2512       C  
ATOM    272  O   THR A  40      17.342   5.096  44.616  1.00141.30           O  
ANISOU  272  O   THR A  40    18382  20828  14476  -1597   -958  -2570       O  
ATOM    273  CB  THR A  40      17.627   7.726  42.999  1.00130.62           C  
ANISOU  273  CB  THR A  40    17026  18944  13658  -1791   -657  -3019       C  
ATOM    274  OG1 THR A  40      19.013   7.775  42.664  1.00128.37           O  
ANISOU  274  OG1 THR A  40    16539  18816  13417  -1907   -887  -2994       O  
ATOM    275  CG2 THR A  40      17.427   7.993  44.479  1.00134.04           C  
ANISOU  275  CG2 THR A  40    17657  19557  13711  -1971   -649  -3214       C  
ATOM    276  N   SER A  41      18.320   4.268  42.721  1.00148.33           N  
ANISOU  276  N   SER A  41    18910  21621  15827  -1349  -1130  -2271       N  
ATOM    277  CA  SER A  41      19.146   3.208  43.334  1.00152.41           C  
ANISOU  277  CA  SER A  41    19309  22447  16150  -1322  -1424  -2072       C  
ATOM    278  C   SER A  41      20.592   3.706  43.316  1.00158.51           C  
ANISOU  278  C   SER A  41    19897  23411  16915  -1494  -1630  -2165       C  
ATOM    279  O   SER A  41      21.080   4.158  42.272  1.00157.68           O  
ANISOU  279  O   SER A  41    19646  23185  17079  -1486  -1594  -2207       O  
ATOM    280  CB  SER A  41      19.083   1.852  42.577  1.00147.00           C  
ANISOU  280  CB  SER A  41    18489  21715  15648  -1035  -1505  -1759       C  
ATOM    281  OG  SER A  41      18.039   0.988  43.024  1.00141.45           O  
ANISOU  281  OG  SER A  41    17929  20977  14837   -910  -1444  -1595       O  
ATOM    282  N   ASN A  42      21.260   3.625  44.473  1.00161.78           N  
ANISOU  282  N   ASN A  42    20315  24142  17013  -1664  -1846  -2187       N  
ATOM    283  CA  ASN A  42      22.736   3.655  44.557  1.00165.72           C  
ANISOU  283  CA  ASN A  42    20573  24911  17478  -1784  -2127  -2171       C  
ATOM    284  C   ASN A  42      23.393   2.570  43.699  1.00171.87           C  
ANISOU  284  C   ASN A  42    21077  25733  18492  -1526  -2281  -1891       C  
ATOM    285  O   ASN A  42      24.560   2.707  43.317  1.00177.88           O  
ANISOU  285  O   ASN A  42    21587  26641  19357  -1577  -2439  -1888       O  
ATOM    286  CB  ASN A  42      23.229   3.488  46.015  1.00163.94           C  
ANISOU  286  CB  ASN A  42    20396  25053  16839  -1976  -2368  -2173       C  
ATOM    287  CG  ASN A  42      23.382   4.814  46.752  1.00163.75           C  
ANISOU  287  CG  ASN A  42    20524  25093  16599  -2330  -2321  -2521       C  
ATOM    288  OD1 ASN A  42      23.701   5.840  46.156  1.00163.18           O  
ANISOU  288  OD1 ASN A  42    20414  24873  16711  -2469  -2223  -2732       O  
ATOM    289  ND2 ASN A  42      23.177   4.789  48.064  1.00166.32           N  
ANISOU  289  ND2 ASN A  42    21028  25642  16522  -2492  -2396  -2582       N  
ATOM    290  N   GLU A  43      22.656   1.482  43.452  1.00174.70           N  
ANISOU  290  N   GLU A  43    21481  25972  18922  -1258  -2236  -1663       N  
ATOM    291  CA  GLU A  43      23.018   0.463  42.459  1.00171.44           C  
ANISOU  291  CA  GLU A  43    20859  25498  18781   -977  -2307  -1432       C  
ATOM    292  C   GLU A  43      22.551   0.895  41.008  1.00165.12           C  
ANISOU  292  C   GLU A  43    20038  24375  18322   -878  -2050  -1510       C  
ATOM    293  O   GLU A  43      21.331   1.032  40.730  1.00155.93           O  
ANISOU  293  O   GLU A  43    19070  22957  17219   -821  -1818  -1541       O  
ATOM    294  CB  GLU A  43      22.466  -0.910  42.929  1.00170.08           C  
ANISOU  294  CB  GLU A  43    20767  25339  18516   -766  -2395  -1154       C  
ATOM    295  CG  GLU A  43      23.409  -2.094  42.731  1.00170.52           C  
ANISOU  295  CG  GLU A  43    20582  25534  18674   -551  -2653   -895       C  
ATOM    296  CD  GLU A  43      23.389  -2.603  41.294  1.00172.58           C  
ANISOU  296  CD  GLU A  43    20709  25559  19302   -297  -2544   -823       C  
ATOM    297  OE1 GLU A  43      22.270  -2.859  40.782  1.00172.11           O  
ANISOU  297  OE1 GLU A  43    20814  25229  19350   -186  -2341   -796       O  
ATOM    298  OE2 GLU A  43      24.479  -2.736  40.670  1.00172.79           O  
ANISOU  298  OE2 GLU A  43    20463  25684  19505   -218  -2656   -800       O  
ATOM    299  N   ILE A  44      23.542   1.144  40.121  1.00154.05           N  
ANISOU  299  N   ILE A  44    18391  23012  17128   -875  -2098  -1538       N  
ATOM    300  CA  ILE A  44      23.311   1.601  38.723  1.00140.22           C  
ANISOU  300  CA  ILE A  44    16591  21010  15674   -815  -1886  -1601       C  
ATOM    301  C   ILE A  44      22.444   0.611  37.965  1.00124.14           C  
ANISOU  301  C   ILE A  44    14609  18757  13799   -533  -1777  -1428       C  
ATOM    302  O   ILE A  44      22.819  -0.550  37.746  1.00114.74           O  
ANISOU  302  O   ILE A  44    13289  17632  12675   -318  -1908  -1239       O  
ATOM    303  CB  ILE A  44      24.631   1.900  37.897  1.00142.72           C  
ANISOU  303  CB  ILE A  44    16603  21456  16168   -858  -1966  -1630       C  
ATOM    304  CG1 ILE A  44      24.317   2.509  36.500  1.00129.50           C  
ANISOU  304  CG1 ILE A  44    14914  19529  14757   -842  -1731  -1700       C  
ATOM    305  CG2 ILE A  44      25.535   0.664  37.712  1.00146.05           C  
ANISOU  305  CG2 ILE A  44    16761  22071  16657   -632  -2174  -1423       C  
ATOM    306  CD1 ILE A  44      23.551   3.826  36.512  1.00121.27           C  
ANISOU  306  CD1 ILE A  44    14094  18268  13714  -1050  -1525  -1898       C  
ATOM    307  N   LYS A  45      21.283   1.088  37.560  1.00114.34           N  
ANISOU  307  N   LYS A  45    13558  17253  12631   -536  -1540  -1498       N  
ATOM    308  CA  LYS A  45      20.379   0.245  36.792  1.00114.26           C  
ANISOU  308  CA  LYS A  45    13607  17033  12774   -305  -1430  -1351       C  
ATOM    309  C   LYS A  45      20.783   0.053  35.306  1.00100.22           C  
ANISOU  309  C   LYS A  45    11653  15161  11265   -175  -1375  -1312       C  
ATOM    310  O   LYS A  45      20.315   0.808  34.445  1.00102.90           O  
ANISOU  310  O   LYS A  45    12033  15315  11746   -224  -1190  -1396       O  
ATOM    311  CB  LYS A  45      18.951   0.783  36.946  1.00118.53           C  
ANISOU  311  CB  LYS A  45    14393  17354  13288   -350  -1207  -1422       C  
ATOM    312  CG  LYS A  45      18.318   0.233  38.213  1.00129.81           C  
ANISOU  312  CG  LYS A  45    15986  18865  14469   -351  -1255  -1352       C  
ATOM    313  CD  LYS A  45      17.592   1.277  39.040  1.00136.81           C  
ANISOU  313  CD  LYS A  45    17072  19715  15195   -538  -1104  -1542       C  
ATOM    314  CE  LYS A  45      17.038   0.656  40.320  1.00135.98           C  
ANISOU  314  CE  LYS A  45    17117  19740  14809   -549  -1154  -1460       C  
ATOM    315  NZ  LYS A  45      16.343   1.642  41.194  1.00133.07           N  
ANISOU  315  NZ  LYS A  45    16942  19359  14257   -725   -989  -1670       N  
ATOM    316  N   GLU A  46      21.642  -0.951  35.028  1.00 89.78           N  
ANISOU  316  N   GLU A  46    10137  13966  10007     -9  -1534  -1182       N  
ATOM    317  CA  GLU A  46      21.979  -1.395  33.629  1.00 80.81           C  
ANISOU  317  CA  GLU A  46     8843  12754   9108    154  -1475  -1137       C  
ATOM    318  C   GLU A  46      21.350  -2.693  33.249  1.00 70.85           C  
ANISOU  318  C   GLU A  46     7645  11348   7924    403  -1471   -977       C  
ATOM    319  O   GLU A  46      21.413  -3.626  34.014  1.00 67.89           O  
ANISOU  319  O   GLU A  46     7292  11038   7462    512  -1623   -845       O  
ATOM    320  CB  GLU A  46      23.452  -1.628  33.399  1.00 83.47           C  
ANISOU  320  CB  GLU A  46     8884  13323   9506    193  -1625  -1128       C  
ATOM    321  CG  GLU A  46      24.197  -0.364  33.102  1.00 95.38           C  
ANISOU  321  CG  GLU A  46    10263  14935  11041    -39  -1580  -1287       C  
ATOM    322  CD  GLU A  46      25.638  -0.623  32.704  1.00105.13           C  
ANISOU  322  CD  GLU A  46    11166  16412  12365      8  -1702  -1271       C  
ATOM    323  OE1 GLU A  46      26.032  -1.796  32.437  1.00112.41           O  
ANISOU  323  OE1 GLU A  46    11953  17386  13372    262  -1789  -1147       O  
ATOM    324  OE2 GLU A  46      26.380   0.371  32.657  1.00113.58           O  
ANISOU  324  OE2 GLU A  46    12107  17615  13432   -213  -1704  -1388       O  
ATOM    325  N   SER A  47      20.845  -2.783  32.022  1.00 60.61           N  
ANISOU  325  N   SER A  47     6366   9866   6797    487  -1314   -981       N  
ATOM    326  CA  SER A  47      20.267  -4.008  31.562  1.00 57.90           C  
ANISOU  326  CA  SER A  47     6088   9373   6538    703  -1308   -850       C  
ATOM    327  C   SER A  47      20.804  -4.264  30.194  1.00 57.63           C  
ANISOU  327  C   SER A  47     5896   9314   6685    815  -1244   -880       C  
ATOM    328  O   SER A  47      21.000  -3.357  29.412  1.00 57.37           O  
ANISOU  328  O   SER A  47     5794   9287   6715    701  -1125   -985       O  
ATOM    329  CB  SER A  47      18.712  -3.904  31.571  1.00 56.53           C  
ANISOU  329  CB  SER A  47     6160   8978   6340    668  -1162   -822       C  
ATOM    330  OG  SER A  47      18.231  -3.758  32.896  1.00 59.20           O  
ANISOU  330  OG  SER A  47     6639   9363   6490    575  -1209   -797       O  
ATOM    331  N   PRO A  48      21.046  -5.522  29.870  1.00 61.45           N  
ANISOU  331  N   PRO A  48     6327   9762   7256   1041  -1317   -787       N  
ATOM    332  CA  PRO A  48      21.449  -5.775  28.512  1.00 60.44           C  
ANISOU  332  CA  PRO A  48     6073   9602   7286   1147  -1223   -841       C  
ATOM    333  C   PRO A  48      20.341  -5.550  27.502  1.00 58.55           C  
ANISOU  333  C   PRO A  48     5988   9156   7101   1106  -1039   -868       C  
ATOM    334  O   PRO A  48      19.138  -5.547  27.848  1.00 59.24           O  
ANISOU  334  O   PRO A  48     6285   9087   7136   1059   -997   -812       O  
ATOM    335  CB  PRO A  48      21.839  -7.239  28.518  1.00 64.23           C  
ANISOU  335  CB  PRO A  48     6502  10051   7848   1411  -1341   -743       C  
ATOM    336  CG  PRO A  48      21.411  -7.837  29.806  1.00 64.35           C  
ANISOU  336  CG  PRO A  48     6658  10035   7755   1443  -1492   -600       C  
ATOM    337  CD  PRO A  48      20.841  -6.748  30.661  1.00 65.28           C  
ANISOU  337  CD  PRO A  48     6897  10203   7703   1201  -1464   -631       C  
ATOM    338  N   LEU A  49      20.750  -5.369  26.256  1.00 56.53           N  
ANISOU  338  N   LEU A  49     5615   8918   6942   1120   -930   -947       N  
ATOM    339  CA  LEU A  49      19.816  -5.430  25.107  1.00 54.32           C  
ANISOU  339  CA  LEU A  49     5458   8461   6718   1120   -781   -955       C  
ATOM    340  C   LEU A  49      20.385  -6.269  23.940  1.00 53.71           C  
ANISOU  340  C   LEU A  49     5269   8394   6742   1286   -737  -1002       C  
ATOM    341  O   LEU A  49      21.591  -6.328  23.712  1.00 52.25           O  
ANISOU  341  O   LEU A  49     4866   8386   6601   1349   -758  -1063       O  
ATOM    342  CB  LEU A  49      19.504  -4.010  24.607  1.00 54.05           C  
ANISOU  342  CB  LEU A  49     5438   8427   6669    900   -645  -1015       C  
ATOM    343  CG  LEU A  49      20.620  -3.224  23.861  1.00 53.02           C  
ANISOU  343  CG  LEU A  49     5096   8473   6574    804   -582  -1108       C  
ATOM    344  CD1 LEU A  49      20.600  -3.492  22.375  1.00 51.91           C  
ANISOU  344  CD1 LEU A  49     4919   8308   6494    853   -459  -1135       C  
ATOM    345  CD2 LEU A  49      20.365  -1.731  24.026  1.00 52.69           C  
ANISOU  345  CD2 LEU A  49     5100   8416   6501    561   -511  -1141       C  
ATOM    346  N   HIS A  50      19.492  -6.860  23.175  1.00 54.16           N  
ANISOU  346  N   HIS A  50     5472   8273   6831   1342   -666   -985       N  
ATOM    347  CA  HIS A  50      19.881  -7.626  21.987  1.00 53.55           C  
ANISOU  347  CA  HIS A  50     5330   8186   6829   1480   -599  -1058       C  
ATOM    348  C   HIS A  50      18.921  -7.378  20.887  1.00 48.12           C  
ANISOU  348  C   HIS A  50     4773   7385   6124   1381   -469  -1074       C  
ATOM    349  O   HIS A  50      17.685  -7.412  21.094  1.00 46.50           O  
ANISOU  349  O   HIS A  50     4761   7015   5892   1319   -472   -992       O  
ATOM    350  CB  HIS A  50      19.847  -9.128  22.301  1.00 56.19           C  
ANISOU  350  CB  HIS A  50     5733   8385   7230   1711   -702  -1014       C  
ATOM    351  CG  HIS A  50      20.819  -9.517  23.335  1.00 61.24           C  
ANISOU  351  CG  HIS A  50     6234   9135   7896   1839   -853   -970       C  
ATOM    352  ND1 HIS A  50      20.506  -9.495  24.675  1.00 63.02           N  
ANISOU  352  ND1 HIS A  50     6543   9347   8052   1802   -987   -848       N  
ATOM    353  CD2 HIS A  50      22.155  -9.793  23.248  1.00 63.01           C  
ANISOU  353  CD2 HIS A  50     6215   9529   8194   1984   -891  -1028       C  
ATOM    354  CE1 HIS A  50      21.601  -9.783  25.370  1.00 67.42           C  
ANISOU  354  CE1 HIS A  50     6925  10055   8634   1916  -1122   -821       C  
ATOM    355  NE2 HIS A  50      22.604 -10.000  24.526  1.00 64.17           N  
ANISOU  355  NE2 HIS A  50     6307   9750   8325   2040  -1070   -924       N  
ATOM    356  N   GLY A  51      19.464  -7.254  19.692  1.00 47.13           N  
ANISOU  356  N   GLY A  51     4539   7355   6010   1377   -357  -1172       N  
ATOM    357  CA  GLY A  51      18.659  -6.872  18.542  1.00 47.74           C  
ANISOU  357  CA  GLY A  51     4719   7374   6047   1253   -237  -1180       C  
ATOM    358  C   GLY A  51      19.290  -7.190  17.228  1.00 49.92           C  
ANISOU  358  C   GLY A  51     4896   7752   6317   1300   -125  -1299       C  
ATOM    359  O   GLY A  51      20.411  -7.719  17.152  1.00 52.96           O  
ANISOU  359  O   GLY A  51     5114   8256   6750   1448   -121  -1392       O  
ATOM    360  N   THR A  52      18.538  -6.869  16.187  1.00 49.36           N  
ANISOU  360  N   THR A  52     4927   7643   6182   1175    -33  -1292       N  
ATOM    361  CA  THR A  52      18.963  -7.032  14.830  1.00 54.81           C  
ANISOU  361  CA  THR A  52     5557   8446   6821   1169     91  -1401       C  
ATOM    362  C   THR A  52      18.468  -5.882  14.042  1.00 51.81           C  
ANISOU  362  C   THR A  52     5206   8123   6355    938    177  -1334       C  
ATOM    363  O   THR A  52      17.363  -5.373  14.291  1.00 51.23           O  
ANISOU  363  O   THR A  52     5273   7918   6273    826    137  -1209       O  
ATOM    364  CB  THR A  52      18.433  -8.355  14.154  1.00 60.53           C  
ANISOU  364  CB  THR A  52     6431   9027   7538   1296     99  -1479       C  
ATOM    365  OG1 THR A  52      17.016  -8.379  14.160  1.00 70.10           O  
ANISOU  365  OG1 THR A  52     7855  10059   8720   1196     48  -1370       O  
ATOM    366  CG2 THR A  52      18.821  -9.519  14.950  1.00 64.75           C  
ANISOU  366  CG2 THR A  52     6965   9454   8181   1530      4  -1518       C  
ATOM    367  N   GLU A  53      19.232  -5.551  13.026  1.00 51.20           N  
ANISOU  367  N   GLU A  53     5001   8239   6214    876    299  -1411       N  
ATOM    368  CA  GLU A  53      18.795  -4.605  12.029  1.00 53.31           C  
ANISOU  368  CA  GLU A  53     5304   8570   6380    660    387  -1339       C  
ATOM    369  C   GLU A  53      18.663  -5.266  10.700  1.00 55.59           C  
ANISOU  369  C   GLU A  53     5649   8918   6555    666    477  -1430       C  
ATOM    370  O   GLU A  53      19.303  -6.298  10.482  1.00 54.77           O  
ANISOU  370  O   GLU A  53     5493   8857   6459    839    515  -1591       O  
ATOM    371  CB  GLU A  53      19.750  -3.450  11.971  1.00 54.47           C  
ANISOU  371  CB  GLU A  53     5265   8908   6521    517    457  -1321       C  
ATOM    372  CG  GLU A  53      20.874  -3.669  11.127  1.00 59.63           C  
ANISOU  372  CG  GLU A  53     5741   9796   7117    539    581  -1447       C  
ATOM    373  CD  GLU A  53      21.796  -2.481  11.115  1.00 65.29           C  
ANISOU  373  CD  GLU A  53     6268  10705   7835    365    645  -1411       C  
ATOM    374  OE1 GLU A  53      21.905  -1.676  12.089  1.00 65.73           O  
ANISOU  374  OE1 GLU A  53     6287  10714   7971    284    568  -1335       O  
ATOM    375  OE2 GLU A  53      22.441  -2.401  10.072  1.00 67.17           O  
ANISOU  375  OE2 GLU A  53     6391  11150   7979    301    782  -1471       O  
ATOM    376  N   ASN A  54      17.797  -4.711   9.844  1.00 57.56           N  
ANISOU  376  N   ASN A  54     6012   9158   6699    487    505  -1328       N  
ATOM    377  CA  ASN A  54      17.530  -5.278   8.516  1.00 60.88           C  
ANISOU  377  CA  ASN A  54     6513   9648   6968    450    581  -1406       C  
ATOM    378  C   ASN A  54      18.610  -4.939   7.543  1.00 65.66           C  
ANISOU  378  C   ASN A  54     6962  10526   7458    378    739  -1498       C  
ATOM    379  O   ASN A  54      18.774  -3.755   7.227  1.00 67.40           O  
ANISOU  379  O   ASN A  54     7113  10863   7630    186    787  -1373       O  
ATOM    380  CB  ASN A  54      16.168  -4.870   7.911  1.00 57.75           C  
ANISOU  380  CB  ASN A  54     6289   9168   6483    278    531  -1246       C  
ATOM    381  CG  ASN A  54      15.780  -5.731   6.780  1.00 58.13           C  
ANISOU  381  CG  ASN A  54     6453   9255   6379    262    565  -1348       C  
ATOM    382  OD1 ASN A  54      16.436  -5.694   5.747  1.00 63.59           O  
ANISOU  382  OD1 ASN A  54     7082  10154   6922    198    690  -1444       O  
ATOM    383  ND2 ASN A  54      14.670  -6.486   6.915  1.00 58.02           N  
ANISOU  383  ND2 ASN A  54     6612   9051   6381    293    457  -1327       N  
ATOM    384  N   THR A  55      19.218  -6.018   7.027  1.00 68.54           N  
ANISOU  384  N   THR A  55     7295  10969   7778    527    822  -1711       N  
ATOM    385  CA  THR A  55      20.224  -5.970   5.998  1.00 80.83           C  
ANISOU  385  CA  THR A  55     8706  12801   9204    490   1002  -1845       C  
ATOM    386  C   THR A  55      19.686  -5.883   4.576  1.00 85.12           C  
ANISOU  386  C   THR A  55     9372  13459   9509    308   1086  -1846       C  
ATOM    387  O   THR A  55      20.423  -5.463   3.687  1.00 83.51           O  
ANISOU  387  O   THR A  55     9048  13520   9161    197   1242  -1891       O  
ATOM    388  CB  THR A  55      21.217  -7.184   6.098  1.00 81.79           C  
ANISOU  388  CB  THR A  55     8714  12962   9399    764   1077  -2098       C  
ATOM    389  OG1 THR A  55      20.552  -8.442   5.910  1.00 85.61           O  
ANISOU  389  OG1 THR A  55     9398  13249   9880    904   1034  -2224       O  
ATOM    390  CG2 THR A  55      21.862  -7.209   7.439  1.00 82.76           C  
ANISOU  390  CG2 THR A  55     8686  13022   9734    928    986  -2075       C  
ATOM    391  N   ILE A  56      18.448  -6.300   4.326  1.00 91.59           N  
ANISOU  391  N   ILE A  56    10418  14109  10272    266    987  -1797       N  
ATOM    392  CA  ILE A  56      17.983  -6.349   2.943  1.00100.72           C  
ANISOU  392  CA  ILE A  56    11690  15400  11176     95   1053  -1817       C  
ATOM    393  C   ILE A  56      18.233  -4.957   2.364  1.00108.31           C  
ANISOU  393  C   ILE A  56    12557  16578  12018   -152   1121  -1628       C  
ATOM    394  O   ILE A  56      17.754  -3.944   2.903  1.00111.13           O  
ANISOU  394  O   ILE A  56    12920  16838  12465   -263   1021  -1387       O  
ATOM    395  CB  ILE A  56      16.534  -6.891   2.770  1.00104.94           C  
ANISOU  395  CB  ILE A  56    12470  15737  11666     45    909  -1758       C  
ATOM    396  CG1 ILE A  56      16.502  -8.443   2.746  1.00110.13           C  
ANISOU  396  CG1 ILE A  56    13243  16255  12343    236    910  -2018       C  
ATOM    397  CG2 ILE A  56      15.916  -6.463   1.442  1.00104.16           C  
ANISOU  397  CG2 ILE A  56    12471  15806  11300   -208    931  -1669       C  
ATOM    398  CD1 ILE A  56      17.276  -9.170   3.832  1.00111.63           C  
ANISOU  398  CD1 ILE A  56    13341  16305  12767    519    907  -2152       C  
ATOM    399  N   ASN A  57      19.097  -4.978   1.339  1.00117.20           N  
ANISOU  399  N   ASN A  57    13582  17988  12959   -215   1305  -1760       N  
ATOM    400  CA  ASN A  57      19.454  -3.885   0.426  1.00126.79           C  
ANISOU  400  CA  ASN A  57    14717  19470  13986   -471   1415  -1622       C  
ATOM    401  C   ASN A  57      20.515  -2.864   0.894  1.00134.63           C  
ANISOU  401  C   ASN A  57    15468  20600  15083   -523   1498  -1547       C  
ATOM    402  O   ASN A  57      20.697  -1.857   0.211  1.00148.04           O  
ANISOU  402  O   ASN A  57    17106  22507  16633   -755   1587  -1411       O  
ATOM    403  CB  ASN A  57      18.210  -3.135  -0.102  1.00132.36           C  
ANISOU  403  CB  ASN A  57    15593  20123  14574   -706   1293  -1348       C  
ATOM    404  CG  ASN A  57      17.340  -3.984  -1.032  1.00139.92           C  
ANISOU  404  CG  ASN A  57    16754  21094  15315   -751   1259  -1432       C  
ATOM    405  OD1 ASN A  57      16.210  -4.340  -0.674  1.00142.70           O  
ANISOU  405  OD1 ASN A  57    17260  21218  15740   -718   1090  -1361       O  
ATOM    406  ND2 ASN A  57      17.841  -4.271  -2.252  1.00137.61           N  
ANISOU  406  ND2 ASN A  57    16459  21084  14740   -850   1421  -1580       N  
ATOM    407  N   LYS A  58      21.260  -3.144   1.977  1.00135.06           N  
ANISOU  407  N   LYS A  58    15381  20562  15373   -324   1472  -1635       N  
ATOM    408  CA  LYS A  58      22.142  -2.168   2.710  1.00129.77           C  
ANISOU  408  CA  LYS A  58    14493  19969  14846   -382   1494  -1544       C  
ATOM    409  C   LYS A  58      21.371  -1.084   3.439  1.00126.10           C  
ANISOU  409  C   LYS A  58    14137  19264  14507   -498   1325  -1287       C  
ATOM    410  O   LYS A  58      21.474  -0.922   4.661  1.00121.98           O  
ANISOU  410  O   LYS A  58    13605  18549  14193   -375   1207  -1274       O  
ATOM    411  CB  LYS A  58      23.139  -1.403   1.801  1.00133.39           C  
ANISOU  411  CB  LYS A  58    14766  20768  15147   -591   1684  -1520       C  
ATOM    412  CG  LYS A  58      24.053  -2.272   0.939  1.00141.68           C  
ANISOU  412  CG  LYS A  58    15686  22101  16044   -494   1894  -1783       C  
ATOM    413  CD  LYS A  58      24.336  -1.651  -0.440  1.00146.01           C  
ANISOU  413  CD  LYS A  58    16204  22968  16306   -768   2071  -1718       C  
ATOM    414  CE  LYS A  58      25.540  -2.261  -1.165  1.00152.30           C  
ANISOU  414  CE  LYS A  58    16790  24105  16971   -693   2325  -1978       C  
ATOM    415  NZ  LYS A  58      26.845  -1.734  -0.642  1.00157.20           N  
ANISOU  415  NZ  LYS A  58    17082  24910  17736   -696   2415  -1984       N  
ATOM    416  N   ARG A  59      20.558  -0.382   2.663  1.00121.41           N  
ANISOU  416  N   ARG A  59    13659  18690  13781   -729   1317  -1083       N  
ATOM    417  CA  ARG A  59      19.618   0.617   3.114  1.00112.31           C  
ANISOU  417  CA  ARG A  59    12621  17316  12733   -849   1180   -825       C  
ATOM    418  C   ARG A  59      20.298   1.945   3.515  1.00 99.85           C  
ANISOU  418  C   ARG A  59    10897  15788  11250  -1015   1221   -696       C  
ATOM    419  O   ARG A  59      19.959   3.006   2.994  1.00104.08           O  
ANISOU  419  O   ARG A  59    11460  16377  11708  -1249   1249   -491       O  
ATOM    420  CB  ARG A  59      18.662   0.095   4.218  1.00108.56           C  
ANISOU  420  CB  ARG A  59    12276  16532  12438   -663   1012   -829       C  
ATOM    421  CG  ARG A  59      17.643  -0.938   3.757  1.00110.15           C  
ANISOU  421  CG  ARG A  59    12657  16652  12541   -580    948   -881       C  
ATOM    422  CD  ARG A  59      16.475  -0.277   3.028  1.00118.22           C  
ANISOU  422  CD  ARG A  59    13823  17627  13464   -767    875   -638       C  
ATOM    423  NE  ARG A  59      15.802   0.833   3.756  1.00122.60           N  
ANISOU  423  NE  ARG A  59    14410  17974  14198   -830    772   -401       N  
ATOM    424  CZ  ARG A  59      15.161   1.862   3.169  1.00127.58           C  
ANISOU  424  CZ  ARG A  59    15096  18587  14789  -1017    737   -141       C  
ATOM    425  NH1 ARG A  59      14.604   2.815   3.915  1.00122.37           N  
ANISOU  425  NH1 ARG A  59    14461  17708  14324  -1036    658     40       N  
ATOM    426  NH2 ARG A  59      15.063   1.961   1.832  1.00131.34           N  
ANISOU  426  NH2 ARG A  59    15609  19264  15030  -1184    779    -57       N  
ATOM    427  N   THR A  60      21.252   1.905   4.413  1.00 81.57           N  
ANISOU  427  N   THR A  60     8432  13458   9100   -913   1216   -806       N  
ATOM    428  CA  THR A  60      21.708   3.130   5.013  1.00 83.91           C  
ANISOU  428  CA  THR A  60     8632  13732   9516  -1079   1212   -682       C  
ATOM    429  C   THR A  60      20.657   3.926   5.806  1.00 74.48           C  
ANISOU  429  C   THR A  60     7593  12209   8497  -1096   1062   -522       C  
ATOM    430  O   THR A  60      20.981   4.958   6.349  1.00 73.07           O  
ANISOU  430  O   THR A  60     7350  11953   8458  -1173   1036   -486       O  
ATOM    431  CB  THR A  60      22.165   4.140   3.937  1.00 88.44           C  
ANISOU  431  CB  THR A  60     9143  14505   9953  -1370   1334   -527       C  
ATOM    432  OG1 THR A  60      21.021   4.788   3.370  1.00 83.24           O  
ANISOU  432  OG1 THR A  60     8685  13697   9242  -1508   1269   -286       O  
ATOM    433  CG2 THR A  60      23.047   3.491   2.861  1.00 92.67           C  
ANISOU  433  CG2 THR A  60     9538  15398  10274  -1383   1514   -674       C  
ATOM    434  N   GLN A  61      19.420   3.469   5.883  1.00 66.16           N  
ANISOU  434  N   GLN A  61     6734  10967   7436  -1030    970   -436       N  
ATOM    435  CA  GLN A  61      18.507   3.970   6.871  1.00 62.03           C  
ANISOU  435  CA  GLN A  61     6330  10144   7091   -970    842   -348       C  
ATOM    436  C   GLN A  61      17.688   2.747   7.149  1.00 58.33           C  
ANISOU  436  C   GLN A  61     5970   9571   6619   -754    761   -441       C  
ATOM    437  O   GLN A  61      16.525   2.696   6.755  1.00 58.17           O  
ANISOU  437  O   GLN A  61     6096   9429   6576   -762    696   -315       O  
ATOM    438  CB  GLN A  61      17.627   5.115   6.384  1.00 64.83           C  
ANISOU  438  CB  GLN A  61     6806  10359   7467  -1146    812    -84       C  
ATOM    439  CG  GLN A  61      18.312   6.480   6.187  1.00 69.33           C  
ANISOU  439  CG  GLN A  61     7304  10957   8079  -1384    876     48       C  
ATOM    440  CD  GLN A  61      17.297   7.647   5.968  1.00 73.28           C  
ANISOU  440  CD  GLN A  61     7946  11223   8671  -1512    818    327       C  
ATOM    441  OE1 GLN A  61      17.548   8.787   6.353  1.00 77.21           O  
ANISOU  441  OE1 GLN A  61     8441  11587   9308  -1645    826    422       O  
ATOM    442  NE2 GLN A  61      16.144   7.349   5.386  1.00 78.18           N  
ANISOU  442  NE2 GLN A  61     8690  11784   9229  -1464    753    454       N  
ATOM    443  N   PRO A  62      18.283   1.751   7.832  1.00 57.34           N  
ANISOU  443  N   PRO A  62     5769   9490   6527   -565    755   -648       N  
ATOM    444  CA  PRO A  62      17.568   0.481   7.954  1.00 54.80           C  
ANISOU  444  CA  PRO A  62     5558   9072   6189   -376    687   -737       C  
ATOM    445  C   PRO A  62      16.598   0.443   9.063  1.00 52.05           C  
ANISOU  445  C   PRO A  62     5326   8468   5982   -282    563   -675       C  
ATOM    446  O   PRO A  62      16.730   1.192   9.998  1.00 51.46           O  
ANISOU  446  O   PRO A  62     5221   8299   6031   -307    533   -634       O  
ATOM    447  CB  PRO A  62      18.682  -0.534   8.274  1.00 58.90           C  
ANISOU  447  CB  PRO A  62     5941   9722   6715   -199    729   -964       C  
ATOM    448  CG  PRO A  62      19.719   0.275   8.981  1.00 59.96           C  
ANISOU  448  CG  PRO A  62     5902   9933   6944   -259    751   -972       C  
ATOM    449  CD  PRO A  62      19.710   1.621   8.270  1.00 59.77           C  
ANISOU  449  CD  PRO A  62     5871   9966   6871   -522    815   -803       C  
ATOM    450  N   THR A  63      15.655  -0.489   8.989  1.00 52.57           N  
ANISOU  450  N   THR A  63     5521   8429   6024   -178    497   -687       N  
ATOM    451  CA  THR A  63      14.817  -0.775  10.166  1.00 51.32           C  
ANISOU  451  CA  THR A  63     5454   8049   5994    -63    389   -657       C  
ATOM    452  C   THR A  63      15.542  -1.733  11.082  1.00 54.12           C  
ANISOU  452  C   THR A  63     5752   8405   6405    122    361   -826       C  
ATOM    453  O   THR A  63      16.565  -2.348  10.670  1.00 54.30           O  
ANISOU  453  O   THR A  63     5671   8585   6372    190    422   -974       O  
ATOM    454  CB  THR A  63      13.427  -1.351   9.826  1.00 52.79           C  
ANISOU  454  CB  THR A  63     5794   8113   6151    -46    316   -575       C  
ATOM    455  OG1 THR A  63      13.519  -2.696   9.304  1.00 49.87           O  
ANISOU  455  OG1 THR A  63     5467   7792   5686     47    315   -720       O  
ATOM    456  CG2 THR A  63      12.687  -0.387   8.843  1.00 53.97           C  
ANISOU  456  CG2 THR A  63     5984   8280   6242   -228    325   -377       C  
ATOM    457  N   PHE A  64      15.035  -1.822  12.316  1.00 49.22           N  
ANISOU  457  N   PHE A  64     5188   7619   5893    205    275   -796       N  
ATOM    458  CA  PHE A  64      15.667  -2.597  13.369  1.00 48.25           C  
ANISOU  458  CA  PHE A  64     5017   7485   5830    370    222   -910       C  
ATOM    459  C   PHE A  64      14.737  -2.888  14.527  1.00 45.18           C  
ANISOU  459  C   PHE A  64     4744   6907   5515    443    125   -847       C  
ATOM    460  O   PHE A  64      13.679  -2.260  14.666  1.00 43.62           O  
ANISOU  460  O   PHE A  64     4636   6591   5345    362    113   -723       O  
ATOM    461  CB  PHE A  64      16.931  -1.891  13.879  1.00 50.85           C  
ANISOU  461  CB  PHE A  64     5176   7949   6195    334    250   -966       C  
ATOM    462  CG  PHE A  64      16.657  -0.593  14.547  1.00 50.37           C  
ANISOU  462  CG  PHE A  64     5131   7811   6195    197    241   -870       C  
ATOM    463  CD1 PHE A  64      16.328  -0.555  15.881  1.00 50.56           C  
ANISOU  463  CD1 PHE A  64     5209   7717   6285    252    162   -862       C  
ATOM    464  CD2 PHE A  64      16.715   0.597  13.829  1.00 52.57           C  
ANISOU  464  CD2 PHE A  64     5383   8127   6461      9    316   -788       C  
ATOM    465  CE1 PHE A  64      15.996   0.612  16.484  1.00 49.91           C  
ANISOU  465  CE1 PHE A  64     5163   7541   6257    134    168   -801       C  
ATOM    466  CE2 PHE A  64      16.432   1.790  14.455  1.00 51.15           C  
ANISOU  466  CE2 PHE A  64     5238   7834   6362   -106    311   -712       C  
ATOM    467  CZ  PHE A  64      16.085   1.788  15.792  1.00 51.47           C  
ANISOU  467  CZ  PHE A  64     5336   7749   6469    -38    242   -735       C  
ATOM    468  N   GLY A  65      15.118  -3.865  15.332  1.00 43.93           N  
ANISOU  468  N   GLY A  65     4579   6724   5388    602     59   -925       N  
ATOM    469  CA  GLY A  65      14.415  -4.159  16.539  1.00 42.99           C  
ANISOU  469  CA  GLY A  65     4555   6459   5320    664    -27   -866       C  
ATOM    470  C   GLY A  65      15.348  -4.620  17.587  1.00 43.60           C  
ANISOU  470  C   GLY A  65     4554   6585   5427    785    -93   -934       C  
ATOM    471  O   GLY A  65      16.464  -5.100  17.308  1.00 46.65           O  
ANISOU  471  O   GLY A  65     4816   7093   5814    876    -86  -1036       O  
ATOM    472  N   PHE A  66      14.935  -4.424  18.822  1.00 43.83           N  
ANISOU  472  N   PHE A  66     4639   6539   5476    786   -157   -876       N  
ATOM    473  CA  PHE A  66      15.659  -5.006  19.938  1.00 45.34           C  
ANISOU  473  CA  PHE A  66     4780   6769   5676    904   -253   -909       C  
ATOM    474  C   PHE A  66      14.833  -5.169  21.186  1.00 46.19           C  
ANISOU  474  C   PHE A  66     5011   6765   5773    914   -324   -824       C  
ATOM    475  O   PHE A  66      13.807  -4.490  21.357  1.00 46.02           O  
ANISOU  475  O   PHE A  66     5082   6657   5746    811   -279   -757       O  
ATOM    476  CB  PHE A  66      16.964  -4.232  20.242  1.00 48.48           C  
ANISOU  476  CB  PHE A  66     4998   7350   6072    855   -251   -981       C  
ATOM    477  CG  PHE A  66      16.788  -2.817  20.768  1.00 45.22           C  
ANISOU  477  CG  PHE A  66     4591   6943   5647    677   -218   -961       C  
ATOM    478  CD1 PHE A  66      16.647  -2.570  22.129  1.00 46.42           C  
ANISOU  478  CD1 PHE A  66     4790   7073   5772    658   -288   -946       C  
ATOM    479  CD2 PHE A  66      16.862  -1.749  19.947  1.00 44.77           C  
ANISOU  479  CD2 PHE A  66     4492   6916   5600    527   -119   -965       C  
ATOM    480  CE1 PHE A  66      16.503  -1.296  22.610  1.00 45.72           C  
ANISOU  480  CE1 PHE A  66     4722   6971   5676    499   -247   -959       C  
ATOM    481  CE2 PHE A  66      16.668  -0.429  20.425  1.00 43.56           C  
ANISOU  481  CE2 PHE A  66     4365   6723   5461    366    -84   -951       C  
ATOM    482  CZ  PHE A  66      16.509  -0.201  21.757  1.00 42.80           C  
ANISOU  482  CZ  PHE A  66     4324   6590   5347    356   -144   -965       C  
ATOM    483  N   THR A  67      15.349  -6.045  22.055  1.00 45.08           N  
ANISOU  483  N   THR A  67     4858   6641   5630   1043   -431   -823       N  
ATOM    484  CA  THR A  67      14.713  -6.450  23.284  1.00 44.42           C  
ANISOU  484  CA  THR A  67     4888   6477   5512   1067   -512   -734       C  
ATOM    485  C   THR A  67      15.564  -6.056  24.451  1.00 45.04           C  
ANISOU  485  C   THR A  67     4884   6690   5538   1057   -591   -752       C  
ATOM    486  O   THR A  67      16.792  -6.304  24.478  1.00 44.71           O  
ANISOU  486  O   THR A  67     4693   6780   5512   1137   -654   -807       O  
ATOM    487  CB  THR A  67      14.598  -7.989  23.326  1.00 44.94           C  
ANISOU  487  CB  THR A  67     5028   6434   5611   1229   -599   -686       C  
ATOM    488  OG1 THR A  67      13.715  -8.408  22.285  1.00 43.39           O  
ANISOU  488  OG1 THR A  67     4928   6107   5448   1214   -538   -676       O  
ATOM    489  CG2 THR A  67      13.959  -8.414  24.634  1.00 45.08           C  
ANISOU  489  CG2 THR A  67     5165   6384   5578   1235   -684   -567       C  
ATOM    490  N   VAL A  68      14.920  -5.469  25.433  1.00 46.12           N  
ANISOU  490  N   VAL A  68     5108   6807   5607    959   -588   -711       N  
ATOM    491  CA  VAL A  68      15.546  -5.228  26.753  1.00 49.79           C  
ANISOU  491  CA  VAL A  68     5538   7398   5980    933   -683   -719       C  
ATOM    492  C   VAL A  68      14.920  -6.059  27.865  1.00 52.04           C  
ANISOU  492  C   VAL A  68     5955   7629   6187    985   -770   -604       C  
ATOM    493  O   VAL A  68      13.727  -6.040  28.137  1.00 54.56           O  
ANISOU  493  O   VAL A  68     6413   7839   6477    935   -709   -540       O  
ATOM    494  CB  VAL A  68      15.453  -3.748  27.162  1.00 48.16           C  
ANISOU  494  CB  VAL A  68     5333   7240   5725    752   -605   -795       C  
ATOM    495  CG1 VAL A  68      16.290  -3.449  28.369  1.00 48.50           C  
ANISOU  495  CG1 VAL A  68     5322   7444   5659    699   -711   -837       C  
ATOM    496  CG2 VAL A  68      15.946  -2.857  26.043  1.00 50.02           C  
ANISOU  496  CG2 VAL A  68     5459   7504   6040    671   -511   -879       C  
ATOM    497  N   ASN A  69      15.754  -6.706  28.598  1.00 59.06           N  
ANISOU  497  N   ASN A  69     6789   8617   7033   1072   -915   -567       N  
ATOM    498  CA  ASN A  69      15.311  -7.653  29.561  1.00 65.17           C  
ANISOU  498  CA  ASN A  69     7680   9344   7735   1134  -1018   -429       C  
ATOM    499  C   ASN A  69      15.624  -6.997  30.915  1.00 63.94           C  
ANISOU  499  C   ASN A  69     7525   9357   7412   1022  -1083   -438       C  
ATOM    500  O   ASN A  69      16.753  -7.053  31.351  1.00 65.87           O  
ANISOU  500  O   ASN A  69     7644   9762   7619   1055  -1212   -451       O  
ATOM    501  CB  ASN A  69      16.186  -8.889  29.280  1.00 74.76           C  
ANISOU  501  CB  ASN A  69     8815  10547   9043   1336  -1148   -377       C  
ATOM    502  CG  ASN A  69      15.739 -10.082  30.002  1.00 82.33           C  
ANISOU  502  CG  ASN A  69     9904  11400   9976   1426  -1260   -209       C  
ATOM    503  OD1 ASN A  69      14.555 -10.239  30.220  1.00 93.62           O  
ANISOU  503  OD1 ASN A  69    11495  12710  11364   1355  -1202   -132       O  
ATOM    504  ND2 ASN A  69      16.681 -10.952  30.381  1.00 90.83           N  
ANISOU  504  ND2 ASN A  69    10904  12520  11086   1586  -1423   -135       N  
ATOM    505  N   TRP A  70      14.647  -6.383  31.574  1.00 63.27           N  
ANISOU  505  N   TRP A  70     7571   9249   7219    889   -994   -438       N  
ATOM    506  CA  TRP A  70      14.960  -5.414  32.631  1.00 63.72           C  
ANISOU  506  CA  TRP A  70     7627   9467   7115    743  -1007   -520       C  
ATOM    507  C   TRP A  70      15.486  -6.084  33.917  1.00 68.45           C  
ANISOU  507  C   TRP A  70     8242  10219   7547    765  -1193   -416       C  
ATOM    508  O   TRP A  70      14.951  -7.104  34.356  1.00 70.37           O  
ANISOU  508  O   TRP A  70     8588  10400   7748    838  -1253   -254       O  
ATOM    509  CB  TRP A  70      13.787  -4.505  32.944  1.00 58.90           C  
ANISOU  509  CB  TRP A  70     7147   8785   6447    609   -834   -578       C  
ATOM    510  CG  TRP A  70      13.355  -3.665  31.812  1.00 57.07           C  
ANISOU  510  CG  TRP A  70     6889   8425   6367    572   -672   -668       C  
ATOM    511  CD1 TRP A  70      12.225  -3.837  31.088  1.00 57.98           C  
ANISOU  511  CD1 TRP A  70     7068   8374   6586    605   -557   -608       C  
ATOM    512  CD2 TRP A  70      13.978  -2.499  31.286  1.00 54.79           C  
ANISOU  512  CD2 TRP A  70     6508   8166   6142    481   -612   -814       C  
ATOM    513  NE1 TRP A  70      12.108  -2.894  30.142  1.00 56.35           N  
ANISOU  513  NE1 TRP A  70     6815   8096   6499    555   -440   -692       N  
ATOM    514  CE2 TRP A  70      13.177  -2.049  30.230  1.00 53.35           C  
ANISOU  514  CE2 TRP A  70     6345   7822   6101    476   -465   -817       C  
ATOM    515  CE3 TRP A  70      15.152  -1.810  31.579  1.00 55.75           C  
ANISOU  515  CE3 TRP A  70     6525   8438   6218    390   -678   -929       C  
ATOM    516  CZ2 TRP A  70      13.480  -0.941  29.475  1.00 52.52           C  
ANISOU  516  CZ2 TRP A  70     6176   7686   6092    390   -378   -916       C  
ATOM    517  CZ3 TRP A  70      15.466  -0.694  30.817  1.00 54.59           C  
ANISOU  517  CZ3 TRP A  70     6311   8256   6173    290   -583  -1043       C  
ATOM    518  CH2 TRP A  70      14.644  -0.299  29.748  1.00 55.38           C  
ANISOU  518  CH2 TRP A  70     6446   8180   6416    298   -435  -1027       C  
ATOM    519  N   LYS A  71      16.568  -5.533  34.479  1.00 72.50           N  
ANISOU  519  N   LYS A  71     8645  10936   7966    692  -1298   -496       N  
ATOM    520  CA  LYS A  71      17.094  -6.033  35.753  1.00 81.18           C  
ANISOU  520  CA  LYS A  71     9751  12217   8876    686  -1492   -394       C  
ATOM    521  C   LYS A  71      16.240  -5.541  36.888  1.00 76.06           C  
ANISOU  521  C   LYS A  71     9280  11618   7999    524  -1426   -411       C  
ATOM    522  O   LYS A  71      15.638  -4.462  36.843  1.00 78.01           O  
ANISOU  522  O   LYS A  71     9596  11819   8225    389  -1248   -566       O  
ATOM    523  CB  LYS A  71      18.535  -5.596  36.003  1.00 91.64           C  
ANISOU  523  CB  LYS A  71    10882  13774  10162    642  -1641   -471       C  
ATOM    524  CG  LYS A  71      19.537  -6.407  35.194  1.00102.83           C  
ANISOU  524  CG  LYS A  71    12099  15201  11771    844  -1754   -407       C  
ATOM    525  CD  LYS A  71      20.951  -6.188  35.736  1.00114.24           C  
ANISOU  525  CD  LYS A  71    13335  16924  13148    810  -1949   -428       C  
ATOM    526  CE  LYS A  71      22.016  -7.019  34.996  1.00119.16           C  
ANISOU  526  CE  LYS A  71    13723  17580  13971   1037  -2058   -365       C  
ATOM    527  NZ  LYS A  71      22.727  -6.292  33.902  1.00115.47           N  
ANISOU  527  NZ  LYS A  71    13056  17159  13657   1006  -1953   -531       N  
ATOM    528  N   PHE A  72      16.166  -6.341  37.918  1.00 74.91           N  
ANISOU  528  N   PHE A  72     9214  11563   7682    540  -1561   -246       N  
ATOM    529  CA  PHE A  72      15.338  -5.986  39.061  1.00 78.80           C  
ANISOU  529  CA  PHE A  72     9883  12132   7926    385  -1491   -252       C  
ATOM    530  C   PHE A  72      13.863  -5.741  38.712  1.00 69.34           C  
ANISOU  530  C   PHE A  72     8820  10737   6785    358  -1244   -280       C  
ATOM    531  O   PHE A  72      13.186  -4.991  39.358  1.00 68.49           O  
ANISOU  531  O   PHE A  72     8820  10673   6529    221  -1106   -383       O  
ATOM    532  CB  PHE A  72      15.944  -4.771  39.792  1.00 90.59           C  
ANISOU  532  CB  PHE A  72    11353  13833   9232    189  -1502   -454       C  
ATOM    533  CG  PHE A  72      17.305  -5.032  40.433  1.00 99.26           C  
ANISOU  533  CG  PHE A  72    12321  15185  10207    176  -1771   -400       C  
ATOM    534  CD1 PHE A  72      17.590  -6.252  41.072  1.00106.72           C  
ANISOU  534  CD1 PHE A  72    13270  16221  11056    280  -1986   -147       C  
ATOM    535  CD2 PHE A  72      18.279  -4.018  40.439  1.00107.40           C  
ANISOU  535  CD2 PHE A  72    13225  16365  11214     44  -1816   -595       C  
ATOM    536  CE1 PHE A  72      18.816  -6.447  41.698  1.00117.85           C  
ANISOU  536  CE1 PHE A  72    14544  17881  12351    270  -2247    -82       C  
ATOM    537  CE2 PHE A  72      19.495  -4.204  41.070  1.00119.24           C  
ANISOU  537  CE2 PHE A  72    14586  18127  12590     12  -2071   -544       C  
ATOM    538  CZ  PHE A  72      19.769  -5.421  41.701  1.00121.73           C  
ANISOU  538  CZ  PHE A  72    14891  18547  12812    133  -2292   -283       C  
ATOM    539  N   SER A  73      13.377  -6.433  37.696  1.00 64.46           N  
ANISOU  539  N   SER A  73     8192   9912   6386    495  -1197   -185       N  
ATOM    540  CA  SER A  73      12.012  -6.309  37.236  1.00 58.88           C  
ANISOU  540  CA  SER A  73     7578   9028   5763    482   -990   -184       C  
ATOM    541  C   SER A  73      11.688  -7.589  36.484  1.00 54.49           C  
ANISOU  541  C   SER A  73     7031   8297   5376    630  -1045     -3       C  
ATOM    542  O   SER A  73      12.583  -8.230  35.953  1.00 52.12           O  
ANISOU  542  O   SER A  73     6638   7972   5191    756  -1186     41       O  
ATOM    543  CB  SER A  73      11.901  -5.087  36.365  1.00 57.07           C  
ANISOU  543  CB  SER A  73     7288   8718   5678    436   -824   -387       C  
ATOM    544  OG  SER A  73      10.576  -4.788  36.142  1.00 58.28           O  
ANISOU  544  OG  SER A  73     7484   8689   5968    465   -666   -353       O  
ATOM    545  N   GLU A  74      10.421  -7.982  36.493  1.00 52.91           N  
ANISOU  545  N   GLU A  74     6939   7980   5184    608   -934     96       N  
ATOM    546  CA  GLU A  74       9.939  -9.113  35.712  1.00 52.19           C  
ANISOU  546  CA  GLU A  74     6875   7695   5259    712   -962    245       C  
ATOM    547  C   GLU A  74       9.591  -8.770  34.259  1.00 52.31           C  
ANISOU  547  C   GLU A  74     6825   7549   5500    753   -845    145       C  
ATOM    548  O   GLU A  74       9.240  -9.684  33.469  1.00 52.92           O  
ANISOU  548  O   GLU A  74     6925   7461   5720    829   -870    237       O  
ATOM    549  CB  GLU A  74       8.779  -9.781  36.431  1.00 55.93           C  
ANISOU  549  CB  GLU A  74     7486   8136   5627    645   -919    422       C  
ATOM    550  CG  GLU A  74       9.220 -10.436  37.770  1.00 59.42           C  
ANISOU  550  CG  GLU A  74     8005   8726   5846    620  -1080    583       C  
ATOM    551  CD  GLU A  74       8.049 -11.015  38.521  1.00 62.46           C  
ANISOU  551  CD  GLU A  74     8525   9103   6102    523  -1016    764       C  
ATOM    552  OE1 GLU A  74       6.914 -10.741  38.152  1.00 72.11           O  
ANISOU  552  OE1 GLU A  74     9763  10245   7387    464   -833    737       O  
ATOM    553  OE2 GLU A  74       8.208 -11.783  39.464  1.00 69.45           O  
ANISOU  553  OE2 GLU A  74     9494  10064   6827    501  -1147    954       O  
ATOM    554  N   SER A  75       9.746  -7.492  33.880  1.00 49.88           N  
ANISOU  554  N   SER A  75     6442   7284   5223    697   -730    -38       N  
ATOM    555  CA  SER A  75       9.266  -6.975  32.598  1.00 47.63           C  
ANISOU  555  CA  SER A  75     6106   6870   5121    705   -603   -116       C  
ATOM    556  C   SER A  75      10.222  -7.061  31.426  1.00 45.41           C  
ANISOU  556  C   SER A  75     5714   6550   4986    793   -664   -185       C  
ATOM    557  O   SER A  75      11.437  -7.184  31.584  1.00 49.34           O  
ANISOU  557  O   SER A  75     6135   7149   5463    845   -784   -223       O  
ATOM    558  CB  SER A  75       8.884  -5.473  32.765  1.00 49.16           C  
ANISOU  558  CB  SER A  75     6285   7103   5289    597   -436   -266       C  
ATOM    559  OG  SER A  75       8.044  -5.345  33.881  1.00 52.75           O  
ANISOU  559  OG  SER A  75     6833   7613   5594    521   -356   -232       O  
ATOM    560  N   THR A  76       9.674  -6.913  30.232  1.00 43.78           N  
ANISOU  560  N   THR A  76     5486   6223   4925    801   -574   -205       N  
ATOM    561  CA  THR A  76      10.495  -6.847  28.995  1.00 45.43           C  
ANISOU  561  CA  THR A  76     5589   6412   5257    863   -592   -289       C  
ATOM    562  C   THR A  76       9.902  -5.681  28.164  1.00 44.68           C  
ANISOU  562  C   THR A  76     5462   6273   5239    778   -439   -362       C  
ATOM    563  O   THR A  76       8.629  -5.518  28.086  1.00 44.12           O  
ANISOU  563  O   THR A  76     5452   6116   5194    730   -344   -299       O  
ATOM    564  CB  THR A  76      10.439  -8.173  28.217  1.00 46.78           C  
ANISOU  564  CB  THR A  76     5789   6462   5520    972   -664   -212       C  
ATOM    565  OG1 THR A  76      10.898  -9.259  29.040  1.00 48.73           O  
ANISOU  565  OG1 THR A  76     6080   6716   5718   1060   -808   -117       O  
ATOM    566  CG2 THR A  76      11.269  -8.130  26.919  1.00 48.15           C  
ANISOU  566  CG2 THR A  76     5857   6637   5801   1035   -659   -317       C  
ATOM    567  N   THR A  77      10.783  -4.846  27.626  1.00 43.78           N  
ANISOU  567  N   THR A  77     5246   6222   5163    753   -418   -477       N  
ATOM    568  CA  THR A  77      10.455  -3.898  26.549  1.00 45.06           C  
ANISOU  568  CA  THR A  77     5367   6328   5423    691   -303   -522       C  
ATOM    569  C   THR A  77      11.041  -4.336  25.218  1.00 41.72           C  
ANISOU  569  C   THR A  77     4871   5904   5077    745   -328   -541       C  
ATOM    570  O   THR A  77      12.176  -4.757  25.171  1.00 46.67           O  
ANISOU  570  O   THR A  77     5420   6618   5693    808   -405   -593       O  
ATOM    571  CB  THR A  77      10.899  -2.480  26.914  1.00 44.97           C  
ANISOU  571  CB  THR A  77     5314   6374   5398    587   -236   -633       C  
ATOM    572  OG1 THR A  77      10.293  -2.177  28.149  1.00 44.64           O  
ANISOU  572  OG1 THR A  77     5358   6335   5268    544   -200   -635       O  
ATOM    573  CG2 THR A  77      10.441  -1.460  25.868  1.00 45.67           C  
ANISOU  573  CG2 THR A  77     5378   6376   5599    521   -119   -643       C  
ATOM    574  N   VAL A  78      10.256  -4.218  24.140  1.00 42.82           N  
ANISOU  574  N   VAL A  78     5026   5956   5287    718   -259   -499       N  
ATOM    575  CA  VAL A  78      10.768  -4.364  22.764  1.00 40.98           C  
ANISOU  575  CA  VAL A  78     4727   5743   5101    732   -251   -536       C  
ATOM    576  C   VAL A  78      10.677  -3.015  22.018  1.00 39.91           C  
ANISOU  576  C   VAL A  78     4539   5614   5008    620   -151   -552       C  
ATOM    577  O   VAL A  78       9.668  -2.286  22.157  1.00 40.39           O  
ANISOU  577  O   VAL A  78     4645   5595   5106    559    -84   -490       O  
ATOM    578  CB  VAL A  78      10.065  -5.482  21.983  1.00 42.28           C  
ANISOU  578  CB  VAL A  78     4959   5817   5287    779   -279   -474       C  
ATOM    579  CG1 VAL A  78      10.409  -6.861  22.524  1.00 43.72           C  
ANISOU  579  CG1 VAL A  78     5189   5968   5452    898   -385   -466       C  
ATOM    580  CG2 VAL A  78       8.558  -5.290  21.949  1.00 42.38           C  
ANISOU  580  CG2 VAL A  78     5045   5731   5325    712   -234   -363       C  
ATOM    581  N   PHE A  79      11.749  -2.634  21.330  1.00 38.74           N  
ANISOU  581  N   PHE A  79     4290   5564   4864    594   -137   -628       N  
ATOM    582  CA  PHE A  79      11.756  -1.419  20.520  1.00 40.04           C  
ANISOU  582  CA  PHE A  79     4411   5732   5069    477    -50   -621       C  
ATOM    583  C   PHE A  79      11.939  -1.741  19.048  1.00 40.27           C  
ANISOU  583  C   PHE A  79     4401   5808   5090    468    -29   -611       C  
ATOM    584  O   PHE A  79      12.672  -2.671  18.669  1.00 45.13           O  
ANISOU  584  O   PHE A  79     4974   6504   5670    548    -65   -679       O  
ATOM    585  CB  PHE A  79      12.925  -0.512  20.861  1.00 42.56           C  
ANISOU  585  CB  PHE A  79     4635   6149   5385    402    -35   -713       C  
ATOM    586  CG  PHE A  79      12.973  -0.060  22.288  1.00 43.64           C  
ANISOU  586  CG  PHE A  79     4805   6274   5502    380    -56   -759       C  
ATOM    587  CD1 PHE A  79      13.354  -0.942  23.304  1.00 45.32           C  
ANISOU  587  CD1 PHE A  79     5022   6550   5645    469   -152   -790       C  
ATOM    588  CD2 PHE A  79      12.726   1.261  22.598  1.00 45.72           C  
ANISOU  588  CD2 PHE A  79     5096   6465   5808    264     17   -777       C  
ATOM    589  CE1 PHE A  79      13.419  -0.515  24.619  1.00 48.01           C  
ANISOU  589  CE1 PHE A  79     5400   6908   5930    428   -175   -836       C  
ATOM    590  CE2 PHE A  79      12.791   1.689  23.920  1.00 46.79           C  
ANISOU  590  CE2 PHE A  79     5277   6597   5903    230      7   -850       C  
ATOM    591  CZ  PHE A  79      13.131   0.811  24.923  1.00 46.59           C  
ANISOU  591  CZ  PHE A  79     5258   6663   5778    303    -88   -880       C  
ATOM    592  N   THR A  80      11.275  -0.987  18.220  1.00 39.91           N  
ANISOU  592  N   THR A  80     4372   5715   5074    375     28   -528       N  
ATOM    593  CA  THR A  80      11.493  -1.089  16.749  1.00 41.36           C  
ANISOU  593  CA  THR A  80     4520   5976   5218    327     57   -513       C  
ATOM    594  C   THR A  80      11.376   0.234  16.062  1.00 43.41           C  
ANISOU  594  C   THR A  80     4753   6231   5510    189    124   -430       C  
ATOM    595  O   THR A  80      10.620   1.110  16.483  1.00 48.24           O  
ANISOU  595  O   THR A  80     5404   6721   6202    149    147   -346       O  
ATOM    596  CB  THR A  80      10.587  -2.120  16.082  1.00 39.67           C  
ANISOU  596  CB  THR A  80     4385   5718   4968    368     18   -462       C  
ATOM    597  OG1 THR A  80      11.036  -2.332  14.767  1.00 41.09           O  
ANISOU  597  OG1 THR A  80     4532   6006   5073    325     46   -494       O  
ATOM    598  CG2 THR A  80       9.098  -1.751  16.060  1.00 39.25           C  
ANISOU  598  CG2 THR A  80     4400   5545   4967    323     14   -311       C  
ATOM    599  N   GLY A  81      12.165   0.408  15.024  1.00 46.77           N  
ANISOU  599  N   GLY A  81     5107   6784   5877    119    164   -454       N  
ATOM    600  CA  GLY A  81      12.234   1.705  14.391  1.00 46.97           C  
ANISOU  600  CA  GLY A  81     5103   6810   5931    -28    225   -361       C  
ATOM    601  C   GLY A  81      13.132   1.783  13.200  1.00 45.96           C  
ANISOU  601  C   GLY A  81     4894   6859   5709   -119    277   -381       C  
ATOM    602  O   GLY A  81      13.520   0.759  12.631  1.00 43.14           O  
ANISOU  602  O   GLY A  81     4512   6623   5254    -58    276   -468       O  
ATOM    603  N   GLN A  82      13.515   3.014  12.872  1.00 46.26           N  
ANISOU  603  N   GLN A  82     4890   6906   5780   -268    333   -311       N  
ATOM    604  CA  GLN A  82      14.422   3.254  11.770  1.00 47.38           C  
ANISOU  604  CA  GLN A  82     4942   7234   5825   -388    400   -312       C  
ATOM    605  C   GLN A  82      15.402   4.344  12.065  1.00 49.51           C  
ANISOU  605  C   GLN A  82     5122   7536   6151   -522    451   -327       C  
ATOM    606  O   GLN A  82      15.052   5.338  12.648  1.00 50.02           O  
ANISOU  606  O   GLN A  82     5238   7433   6334   -585    446   -259       O  
ATOM    607  CB  GLN A  82      13.585   3.628  10.563  1.00 52.62           C  
ANISOU  607  CB  GLN A  82     5671   7886   6433   -488    408   -128       C  
ATOM    608  CG  GLN A  82      14.282   3.598   9.227  1.00 53.10           C  
ANISOU  608  CG  GLN A  82     5669   8170   6336   -608    477   -118       C  
ATOM    609  CD  GLN A  82      13.316   3.748   8.093  1.00 51.71           C  
ANISOU  609  CD  GLN A  82     5575   7996   6073   -694    453     66       C  
ATOM    610  OE1 GLN A  82      12.084   3.604   8.224  1.00 52.64           O  
ANISOU  610  OE1 GLN A  82     5785   7970   6243   -636    374    170       O  
ATOM    611  NE2 GLN A  82      13.850   4.000   6.978  1.00 57.02           N  
ANISOU  611  NE2 GLN A  82     6207   8853   6604   -835    517    113       N  
ATOM    612  N   CYS A  83      16.647   4.140  11.649  1.00 56.72           N  
ANISOU  612  N   CYS A  83     5897   8670   6984   -569    506   -427       N  
ATOM    613  CA  CYS A  83      17.744   5.110  11.762  1.00 62.26           C  
ANISOU  613  CA  CYS A  83     6479   9455   7719   -733    559   -444       C  
ATOM    614  C   CYS A  83      17.605   6.125  10.591  1.00 62.17           C  
ANISOU  614  C   CYS A  83     6491   9454   7675   -942    627   -259       C  
ATOM    615  O   CYS A  83      17.673   5.719   9.437  1.00 66.31           O  
ANISOU  615  O   CYS A  83     6993  10142   8059   -974    677   -222       O  
ATOM    616  CB  CYS A  83      19.094   4.328  11.757  1.00 70.25           C  
ANISOU  616  CB  CYS A  83     7303  10728   8659   -675    592   -619       C  
ATOM    617  SG  CYS A  83      20.655   5.167  12.300  1.00 81.57           S  
ANISOU  617  SG  CYS A  83     8528  12320  10145   -837    624   -700       S  
ATOM    618  N   PHE A  84      17.319   7.394  10.899  1.00 61.44           N  
ANISOU  618  N   PHE A  84     6463   9172   7709  -1076    625   -141       N  
ATOM    619  CA  PHE A  84      17.330   8.492   9.946  1.00 65.76           C  
ANISOU  619  CA  PHE A  84     7028   9701   8255  -1291    679     52       C  
ATOM    620  C   PHE A  84      18.603   9.333  10.125  1.00 77.67           C  
ANISOU  620  C   PHE A  84     8414  11295   9799  -1490    737      8       C  
ATOM    621  O   PHE A  84      19.269   9.262  11.171  1.00 71.31           O  
ANISOU  621  O   PHE A  84     7535  10503   9054  -1462    713   -158       O  
ATOM    622  CB  PHE A  84      16.087   9.368  10.040  1.00 63.29           C  
ANISOU  622  CB  PHE A  84     6875   9086   8083  -1303    638    242       C  
ATOM    623  CG  PHE A  84      14.825   8.650   9.629  1.00 63.26           C  
ANISOU  623  CG  PHE A  84     6964   9037   8034  -1155    581    330       C  
ATOM    624  CD1 PHE A  84      14.014   8.057  10.587  1.00 59.91           C  
ANISOU  624  CD1 PHE A  84     6603   8473   7685   -961    520    249       C  
ATOM    625  CD2 PHE A  84      14.454   8.545   8.289  1.00 60.57           C  
ANISOU  625  CD2 PHE A  84     6641   8811   7559  -1227    585    497       C  
ATOM    626  CE1 PHE A  84      12.867   7.405  10.219  1.00 53.38           C  
ANISOU  626  CE1 PHE A  84     5845   7614   6823   -850    464    334       C  
ATOM    627  CE2 PHE A  84      13.324   7.868   7.934  1.00 57.20           C  
ANISOU  627  CE2 PHE A  84     6289   8360   7085  -1114    518    570       C  
ATOM    628  CZ  PHE A  84      12.542   7.311   8.888  1.00 55.29           C  
ANISOU  628  CZ  PHE A  84     6098   7972   6939   -930    458    490       C  
ATOM    629  N   ILE A  85      18.932  10.059   9.037  1.00 90.83           N  
ANISOU  629  N   ILE A  85    10055  13047  11408  -1704    807    170       N  
ATOM    630  CA  ILE A  85      20.120  10.950   8.894  1.00 95.85           C  
ANISOU  630  CA  ILE A  85    10569  13787  12060  -1955    877    183       C  
ATOM    631  C   ILE A  85      19.800  12.248   8.164  1.00103.35           C  
ANISOU  631  C   ILE A  85    11618  14580  13068  -2185    905    447       C  
ATOM    632  O   ILE A  85      19.540  12.225   6.968  1.00106.61           O  
ANISOU  632  O   ILE A  85    12051  15104  13348  -2256    941    619       O  
ATOM    633  CB  ILE A  85      21.240  10.332   8.049  1.00 91.93           C  
ANISOU  633  CB  ILE A  85     9875  13678  11374  -2018    974    110       C  
ATOM    634  CG1 ILE A  85      21.688   9.000   8.636  1.00 91.59           C  
ANISOU  634  CG1 ILE A  85     9713  13804  11280  -1782    955   -139       C  
ATOM    635  CG2 ILE A  85      22.398  11.332   7.984  1.00 98.72           C  
ANISOU  635  CG2 ILE A  85    10601  14636  12271  -2301   1043    141       C  
ATOM    636  CD1 ILE A  85      23.202   8.750   8.640  1.00 95.90           C  
ANISOU  636  CD1 ILE A  85     9998  14667  11771  -1847   1031   -288       C  
ATOM    637  N   ASP A  86      19.900  13.381   8.855  1.00114.92           N  
ANISOU  637  N   ASP A  86    13142  15799  14721  -2318    889    478       N  
ATOM    638  CA  ASP A  86      19.497  14.676   8.279  1.00123.18           C  
ANISOU  638  CA  ASP A  86    14311  16616  15873  -2516    902    743       C  
ATOM    639  C   ASP A  86      20.097  15.894   9.032  1.00130.87           C  
ANISOU  639  C   ASP A  86    15323  17348  17052  -2710    905    718       C  
ATOM    640  O   ASP A  86      20.698  15.763  10.104  1.00135.00           O  
ANISOU  640  O   ASP A  86    15817  17825  17652  -2663    876    490       O  
ATOM    641  CB  ASP A  86      17.964  14.704   8.106  1.00119.99           C  
ANISOU  641  CB  ASP A  86    14085  15960  15544  -2345    835    910       C  
ATOM    642  CG  ASP A  86      17.221  14.247   9.356  1.00116.02           C  
ANISOU  642  CG  ASP A  86    13654  15265  15161  -2091    770    734       C  
ATOM    643  OD1 ASP A  86      17.484  13.119   9.857  1.00107.02           O  
ANISOU  643  OD1 ASP A  86    12432  14311  13921  -1933    755    519       O  
ATOM    644  OD2 ASP A  86      16.385  15.050   9.834  1.00114.89           O  
ANISOU  644  OD2 ASP A  86    13650  14781  15219  -2054    743    818       O  
ATOM    645  N   ARG A  87      19.917  17.072   8.445  1.00137.48           N  
ANISOU  645  N   ARG A  87    16235  18029  17969  -2940    934    960       N  
ATOM    646  CA  ARG A  87      20.479  18.337   8.943  1.00143.85           C  
ANISOU  646  CA  ARG A  87    17096  18588  18970  -3177    946    967       C  
ATOM    647  C   ARG A  87      22.001  18.385   9.046  1.00148.44           C  
ANISOU  647  C   ARG A  87    17478  19451  19471  -3417    999    831       C  
ATOM    648  O   ARG A  87      22.556  18.393  10.145  1.00145.19           O  
ANISOU  648  O   ARG A  87    17014  19024  19127  -3429    970    594       O  
ATOM    649  CB  ARG A  87      19.775  18.715  10.262  1.00145.18           C  
ANISOU  649  CB  ARG A  87    17420  18379  19361  -3029    890    820       C  
ATOM    650  CG  ARG A  87      18.265  18.782  10.097  1.00148.64           C  
ANISOU  650  CG  ARG A  87    18029  18541  19904  -2806    851    983       C  
ATOM    651  CD  ARG A  87      17.894  19.892   9.107  1.00157.02           C  
ANISOU  651  CD  ARG A  87    19200  19383  21075  -2975    863   1328       C  
ATOM    652  NE  ARG A  87      16.656  19.651   8.343  1.00161.04           N  
ANISOU  652  NE  ARG A  87    19782  19832  21571  -2796    819   1570       N  
ATOM    653  CZ  ARG A  87      16.270  20.348   7.260  1.00165.05           C  
ANISOU  653  CZ  ARG A  87    20358  20243  22108  -2912    807   1917       C  
ATOM    654  NH1 ARG A  87      17.016  21.351   6.771  1.00165.56           N  
ANISOU  654  NH1 ARG A  87    20440  20241  22221  -3217    847   2080       N  
ATOM    655  NH2 ARG A  87      15.120  20.036   6.645  1.00163.61           N  
ANISOU  655  NH2 ARG A  87    20222  20038  21902  -2736    744   2123       N  
ATOM    656  N   ASN A  88      22.641  18.449   7.865  1.00152.71           N  
ANISOU  656  N   ASN A  88    17902  20261  19857  -3619   1076    998       N  
ATOM    657  CA  ASN A  88      24.107  18.317   7.666  1.00154.73           C  
ANISOU  657  CA  ASN A  88    17910  20890  19991  -3838   1153    901       C  
ATOM    658  C   ASN A  88      24.729  16.995   8.263  1.00153.91           C  
ANISOU  658  C   ASN A  88    17594  21123  19761  -3626   1146    596       C  
ATOM    659  O   ASN A  88      25.938  16.940   8.528  1.00160.59           O  
ANISOU  659  O   ASN A  88    18222  22221  20574  -3769   1179    461       O  
ATOM    660  CB  ASN A  88      24.852  19.618   8.127  1.00155.74           C  
ANISOU  660  CB  ASN A  88    18048  20830  20295  -4178   1158    920       C  
ATOM    661  CG  ASN A  88      25.295  20.541   6.960  1.00157.39           C  
ANISOU  661  CG  ASN A  88    18248  21081  20471  -4532   1242   1219       C  
ATOM    662  OD1 ASN A  88      26.014  20.125   6.038  1.00160.27           O  
ANISOU  662  OD1 ASN A  88    18422  21849  20624  -4645   1338   1280       O  
ATOM    663  ND2 ASN A  88      24.912  21.820   7.039  1.00154.64           N  
ANISOU  663  ND2 ASN A  88    18105  20311  20337  -4715   1214   1399       N  
ATOM    664  N   GLY A  89      23.914  15.935   8.433  1.00148.95           N  
ANISOU  664  N   GLY A  89    17021  20502  19071  -3292   1099    507       N  
ATOM    665  CA  GLY A  89      24.372  14.622   8.975  1.00140.51           C  
ANISOU  665  CA  GLY A  89    15782  19704  17901  -3057   1081    246       C  
ATOM    666  C   GLY A  89      23.961  14.128  10.379  1.00131.23           C  
ANISOU  666  C   GLY A  89    14670  18365  16826  -2817    969     35       C  
ATOM    667  O   GLY A  89      24.533  13.121  10.842  1.00125.31           O  
ANISOU  667  O   GLY A  89    13757  17852  16001  -2660    948   -159       O  
ATOM    668  N   LYS A  90      22.996  14.788  11.056  1.00124.36           N  
ANISOU  668  N   LYS A  90    14025  17106  16119  -2779    904     72       N  
ATOM    669  CA  LYS A  90      22.542  14.358  12.424  1.00119.42           C  
ANISOU  669  CA  LYS A  90    13474  16330  15567  -2565    810   -123       C  
ATOM    670  C   LYS A  90      21.680  13.100  12.398  1.00103.71           C  
ANISOU  670  C   LYS A  90    11527  14386  13490  -2241    776   -158       C  
ATOM    671  O   LYS A  90      20.593  13.083  11.823  1.00 96.31           O  
ANISOU  671  O   LYS A  90    10732  13300  12561  -2147    780     -5       O  
ATOM    672  CB  LYS A  90      21.786  15.459  13.225  1.00124.57           C  
ANISOU  672  CB  LYS A  90    14351  16558  16421  -2617    775   -106       C  
ATOM    673  CG  LYS A  90      22.685  16.471  13.941  1.00133.67           C  
ANISOU  673  CG  LYS A  90    15478  17632  17677  -2889    765   -209       C  
ATOM    674  CD  LYS A  90      23.694  15.839  14.913  1.00136.72           C  
ANISOU  674  CD  LYS A  90    15681  18280  17984  -2877    702   -458       C  
ATOM    675  CE  LYS A  90      24.726  16.844  15.441  1.00142.46           C  
ANISOU  675  CE  LYS A  90    16346  18993  18787  -3204    687   -544       C  
ATOM    676  NZ  LYS A  90      24.090  17.867  16.326  1.00144.90           N  
ANISOU  676  NZ  LYS A  90    16904  18885  19263  -3275    660   -607       N  
ATOM    677  N   GLU A  91      22.168  12.074  13.076  1.00 93.85           N  
ANISOU  677  N   GLU A  91    10154  13333  12170  -2081    730   -353       N  
ATOM    678  CA  GLU A  91      21.473  10.807  13.157  1.00 86.65           C  
ANISOU  678  CA  GLU A  91     9276  12463  11182  -1787    691   -406       C  
ATOM    679  C   GLU A  91      20.364  10.758  14.228  1.00 79.81           C  
ANISOU  679  C   GLU A  91     8597  11316  10411  -1621    616   -450       C  
ATOM    680  O   GLU A  91      20.560  11.130  15.378  1.00 78.72           O  
ANISOU  680  O   GLU A  91     8485  11080  10344  -1650    567   -571       O  
ATOM    681  CB  GLU A  91      22.462   9.691  13.440  1.00 85.79           C  
ANISOU  681  CB  GLU A  91     8959  12663  10975  -1668    670   -579       C  
ATOM    682  CG  GLU A  91      23.590   9.586  12.445  1.00 88.54           C  
ANISOU  682  CG  GLU A  91     9088  13329  11223  -1795    764   -569       C  
ATOM    683  CD  GLU A  91      24.460   8.393  12.738  1.00 87.24           C  
ANISOU  683  CD  GLU A  91     8712  13444  10989  -1619    745   -741       C  
ATOM    684  OE1 GLU A  91      25.472   8.616  13.420  1.00100.02           O  
ANISOU  684  OE1 GLU A  91    10159  15195  12645  -1708    709   -839       O  
ATOM    685  OE2 GLU A  91      24.156   7.257  12.321  1.00 77.10           O  
ANISOU  685  OE2 GLU A  91     7429  12241   9623  -1398    757   -779       O  
ATOM    686  N   VAL A  92      19.221  10.214  13.857  1.00 73.30           N  
ANISOU  686  N   VAL A  92     7889  10393   9567  -1447    607   -362       N  
ATOM    687  CA  VAL A  92      18.120  10.040  14.813  1.00 72.47           C  
ANISOU  687  CA  VAL A  92     7937  10058   9538  -1276    552   -397       C  
ATOM    688  C   VAL A  92      17.544   8.644  14.683  1.00 69.44           C  
ANISOU  688  C   VAL A  92     7557   9768   9057  -1041    513   -418       C  
ATOM    689  O   VAL A  92      17.248   8.226  13.558  1.00 68.37           O  
ANISOU  689  O   VAL A  92     7415   9717   8843  -1019    540   -312       O  
ATOM    690  CB  VAL A  92      17.030  11.069  14.497  1.00 70.88           C  
ANISOU  690  CB  VAL A  92     7899   9560   9469  -1327    581   -220       C  
ATOM    691  CG1 VAL A  92      15.780  10.775  15.227  1.00 74.06           C  
ANISOU  691  CG1 VAL A  92     8433   9768   9939  -1132    548   -230       C  
ATOM    692  CG2 VAL A  92      17.518  12.439  14.910  1.00 79.46           C  
ANISOU  692  CG2 VAL A  92     9022  10482  10687  -1541    611   -233       C  
ATOM    693  N   LEU A  93      17.344   7.948  15.812  1.00 64.45           N  
ANISOU  693  N   LEU A  93     6951   9113   8423   -882    449   -547       N  
ATOM    694  CA  LEU A  93      16.478   6.756  15.834  1.00 59.55           C  
ANISOU  694  CA  LEU A  93     6387   8486   7749   -668    407   -540       C  
ATOM    695  C   LEU A  93      15.011   7.094  16.302  1.00 56.56           C  
ANISOU  695  C   LEU A  93     6177   7845   7469   -594    400   -455       C  
ATOM    696  O   LEU A  93      14.796   7.495  17.456  1.00 52.34           O  
ANISOU  696  O   LEU A  93     5705   7180   6999   -579    389   -533       O  
ATOM    697  CB  LEU A  93      17.056   5.672  16.741  1.00 58.33           C  
ANISOU  697  CB  LEU A  93     6162   8466   7531   -527    337   -697       C  
ATOM    698  CG  LEU A  93      18.557   5.329  16.771  1.00 60.43           C  
ANISOU  698  CG  LEU A  93     6235   8986   7737   -559    324   -815       C  
ATOM    699  CD1 LEU A  93      18.884   4.404  17.942  1.00 58.12           C  
ANISOU  699  CD1 LEU A  93     5906   8760   7416   -404    226   -935       C  
ATOM    700  CD2 LEU A  93      19.016   4.730  15.461  1.00 59.10           C  
ANISOU  700  CD2 LEU A  93     5962   9005   7488   -543    381   -792       C  
ATOM    701  N   LYS A  94      14.036   6.902  15.400  1.00 51.00           N  
ANISOU  701  N   LYS A  94     5530   7085   6762   -549    409   -304       N  
ATOM    702  CA  LYS A  94      12.613   7.023  15.696  1.00 50.57           C  
ANISOU  702  CA  LYS A  94     5591   6827   6797   -455    400   -208       C  
ATOM    703  C   LYS A  94      12.115   5.630  15.997  1.00 49.62           C  
ANISOU  703  C   LYS A  94     5484   6772   6596   -287    343   -256       C  
ATOM    704  O   LYS A  94      12.185   4.740  15.124  1.00 43.06           O  
ANISOU  704  O   LYS A  94     4620   6076   5662   -255    319   -234       O  
ATOM    705  CB  LYS A  94      11.822   7.544  14.489  1.00 54.63           C  
ANISOU  705  CB  LYS A  94     6137   7268   7349   -511    418      8       C  
ATOM    706  CG  LYS A  94      12.300   8.844  13.873  1.00 61.09           C  
ANISOU  706  CG  LYS A  94     6947   8027   8236   -694    468    111       C  
ATOM    707  CD  LYS A  94      11.724  10.050  14.573  1.00 64.94           C  
ANISOU  707  CD  LYS A  94     7522   8231   8920   -709    503    151       C  
ATOM    708  CE  LYS A  94      10.298  10.274  14.133  1.00 66.34           C  
ANISOU  708  CE  LYS A  94     7759   8249   9198   -622    490    353       C  
ATOM    709  NZ  LYS A  94       9.948  11.675  14.425  1.00 73.78           N  
ANISOU  709  NZ  LYS A  94     8773   8909  10351   -668    542    428       N  
ATOM    710  N   THR A  95      11.650   5.414  17.237  1.00 45.94           N  
ANISOU  710  N   THR A  95     5073   6213   6167   -190    325   -331       N  
ATOM    711  CA  THR A  95      11.210   4.082  17.634  1.00 43.64           C  
ANISOU  711  CA  THR A  95     4804   5972   5805    -46    266   -365       C  
ATOM    712  C   THR A  95       9.824   4.109  18.232  1.00 41.92           C  
ANISOU  712  C   THR A  95     4670   5595   5660     32    276   -294       C  
ATOM    713  O   THR A  95       9.371   5.106  18.721  1.00 45.52           O  
ANISOU  713  O   THR A  95     5166   5908   6221      6    331   -276       O  
ATOM    714  CB  THR A  95      12.162   3.422  18.657  1.00 44.85           C  
ANISOU  714  CB  THR A  95     4919   6234   5887      6    218   -527       C  
ATOM    715  OG1 THR A  95      12.123   4.099  19.908  1.00 46.95           O  
ANISOU  715  OG1 THR A  95     5229   6413   6194    -15    234   -600       O  
ATOM    716  CG2 THR A  95      13.591   3.467  18.219  1.00 47.54           C  
ANISOU  716  CG2 THR A  95     5140   6746   6175    -64    216   -608       C  
ATOM    717  N   MET A  96       9.165   2.981  18.196  1.00 40.20           N  
ANISOU  717  N   MET A  96     4476   5404   5392    128    226   -260       N  
ATOM    718  CA  MET A  96       8.048   2.696  19.058  1.00 43.45           C  
ANISOU  718  CA  MET A  96     4946   5719   5842    210    229   -228       C  
ATOM    719  C   MET A  96       8.327   1.457  19.860  1.00 40.64           C  
ANISOU  719  C   MET A  96     4611   5438   5390    293    166   -315       C  
ATOM    720  O   MET A  96       9.115   0.668  19.424  1.00 42.51           O  
ANISOU  720  O   MET A  96     4817   5781   5552    311    112   -365       O  
ATOM    721  CB  MET A  96       6.830   2.513  18.191  1.00 40.55           C  
ANISOU  721  CB  MET A  96     4584   5304   5518    222    218    -62       C  
ATOM    722  CG  MET A  96       6.449   3.868  17.605  1.00 45.87           C  
ANISOU  722  CG  MET A  96     5239   5873   6313    158    276     52       C  
ATOM    723  SD  MET A  96       4.736   3.819  17.089  1.00 52.58           S  
ANISOU  723  SD  MET A  96     6077   6647   7254    202    261    262       S  
ATOM    724  CE  MET A  96       4.020   3.823  18.716  1.00 51.24           C  
ANISOU  724  CE  MET A  96     5936   6379   7151    304    330    187       C  
ATOM    725  N   TRP A  97       7.690   1.311  21.011  1.00 40.83           N  
ANISOU  725  N   TRP A  97     4687   5406   5419    345    180   -327       N  
ATOM    726  CA  TRP A  97       7.985   0.234  21.896  1.00 40.15           C  
ANISOU  726  CA  TRP A  97     4631   5383   5239    412    115   -387       C  
ATOM    727  C   TRP A  97       6.745  -0.371  22.480  1.00 41.71           C  
ANISOU  727  C   TRP A  97     4886   5522   5438    463    120   -304       C  
ATOM    728  O   TRP A  97       5.685   0.280  22.543  1.00 42.17           O  
ANISOU  728  O   TRP A  97     4949   5495   5578    453    197   -232       O  
ATOM    729  CB  TRP A  97       8.896   0.711  23.026  1.00 41.53           C  
ANISOU  729  CB  TRP A  97     4806   5608   5365    389    116   -517       C  
ATOM    730  CG  TRP A  97       8.511   1.963  23.662  1.00 41.98           C  
ANISOU  730  CG  TRP A  97     4895   5575   5479    334    213   -556       C  
ATOM    731  CD1 TRP A  97       9.039   3.192  23.411  1.00 42.84           C  
ANISOU  731  CD1 TRP A  97     4981   5642   5654    243    267   -612       C  
ATOM    732  CD2 TRP A  97       7.585   2.148  24.751  1.00 41.56           C  
ANISOU  732  CD2 TRP A  97     4911   5458   5421    361    279   -563       C  
ATOM    733  NE1 TRP A  97       8.476   4.107  24.232  1.00 41.81           N  
ANISOU  733  NE1 TRP A  97     4912   5399   5574    222    359   -662       N  
ATOM    734  CE2 TRP A  97       7.563   3.492  25.045  1.00 39.31           C  
ANISOU  734  CE2 TRP A  97     4646   5078   5211    300    377   -637       C  
ATOM    735  CE3 TRP A  97       6.784   1.285  25.515  1.00 40.35           C  
ANISOU  735  CE3 TRP A  97     4805   5320   5204    424    271   -515       C  
ATOM    736  CZ2 TRP A  97       6.744   4.020  26.036  1.00 41.04           C  
ANISOU  736  CZ2 TRP A  97     4929   5218   5446    318    482   -684       C  
ATOM    737  CZ3 TRP A  97       5.959   1.825  26.503  1.00 40.64           C  
ANISOU  737  CZ3 TRP A  97     4893   5303   5243    427    378   -545       C  
ATOM    738  CH2 TRP A  97       5.939   3.164  26.743  1.00 39.86           C  
ANISOU  738  CH2 TRP A  97     4810   5113   5221    384    487   -638       C  
ATOM    739  N   LEU A  98       6.883  -1.619  22.913  1.00 39.25           N  
ANISOU  739  N   LEU A  98     4610   5254   5046    519     39   -306       N  
ATOM    740  CA  LEU A  98       5.934  -2.241  23.816  1.00 37.95           C  
ANISOU  740  CA  LEU A  98     4506   5058   4853    549     40   -241       C  
ATOM    741  C   LEU A  98       6.587  -2.668  25.096  1.00 39.92           C  
ANISOU  741  C   LEU A  98     4798   5374   4996    577     -5   -307       C  
ATOM    742  O   LEU A  98       7.622  -3.329  25.087  1.00 42.73           O  
ANISOU  742  O   LEU A  98     5143   5791   5300    618   -100   -354       O  
ATOM    743  CB  LEU A  98       5.364  -3.478  23.183  1.00 39.08           C  
ANISOU  743  CB  LEU A  98     4676   5175   4997    570    -30   -146       C  
ATOM    744  CG  LEU A  98       4.604  -3.270  21.898  1.00 39.69           C  
ANISOU  744  CG  LEU A  98     4716   5211   5149    528    -14    -60       C  
ATOM    745  CD1 LEU A  98       4.285  -4.608  21.295  1.00 41.15           C  
ANISOU  745  CD1 LEU A  98     4946   5378   5309    531   -104     -9       C  
ATOM    746  CD2 LEU A  98       3.316  -2.474  22.179  1.00 41.55           C  
ANISOU  746  CD2 LEU A  98     4923   5396   5468    504     77     35       C  
ATOM    747  N   LEU A  99       5.976  -2.340  26.212  1.00 38.99           N  
ANISOU  747  N   LEU A  99     4722   5253   4837    562     59   -305       N  
ATOM    748  CA  LEU A  99       6.515  -2.700  27.560  1.00 39.13           C  
ANISOU  748  CA  LEU A  99     4792   5358   4716    568     12   -354       C  
ATOM    749  C   LEU A  99       5.566  -3.711  28.077  1.00 39.88           C  
ANISOU  749  C   LEU A  99     4950   5436   4766    586     -2   -229       C  
ATOM    750  O   LEU A  99       4.353  -3.380  28.262  1.00 39.10           O  
ANISOU  750  O   LEU A  99     4856   5297   4704    561    109   -172       O  
ATOM    751  CB  LEU A  99       6.570  -1.499  28.513  1.00 41.64           C  
ANISOU  751  CB  LEU A  99     5128   5703   4988    511    111   -468       C  
ATOM    752  CG  LEU A  99       6.719  -1.767  30.005  1.00 44.52           C  
ANISOU  752  CG  LEU A  99     5565   6171   5179    491     91   -502       C  
ATOM    753  CD1 LEU A  99       7.979  -2.523  30.228  1.00 47.05           C  
ANISOU  753  CD1 LEU A  99     5871   6595   5409    516    -74   -513       C  
ATOM    754  CD2 LEU A  99       6.782  -0.426  30.710  1.00 47.10           C  
ANISOU  754  CD2 LEU A  99     5915   6506   5475    419    207   -656       C  
ATOM    755  N   ARG A 100       6.073  -4.947  28.241  1.00 41.26           N  
ANISOU  755  N   ARG A 100     5162   5633   4880    632   -134   -176       N  
ATOM    756  CA  ARG A 100       5.277  -6.045  28.734  1.00 40.77           C  
ANISOU  756  CA  ARG A 100     5174   5541   4774    633   -169    -39       C  
ATOM    757  C   ARG A 100       5.593  -6.187  30.178  1.00 42.71           C  
ANISOU  757  C   ARG A 100     5479   5887   4859    619   -197    -37       C  
ATOM    758  O   ARG A 100       6.733  -6.496  30.502  1.00 44.37           O  
ANISOU  758  O   ARG A 100     5690   6162   5007    661   -313    -74       O  
ATOM    759  CB  ARG A 100       5.645  -7.333  28.055  1.00 41.36           C  
ANISOU  759  CB  ARG A 100     5275   5546   4891    693   -300     22       C  
ATOM    760  CG  ARG A 100       5.065  -8.589  28.720  1.00 42.82           C  
ANISOU  760  CG  ARG A 100     5558   5684   5024    687   -367    171       C  
ATOM    761  CD  ARG A 100       3.593  -8.713  28.448  1.00 40.39           C  
ANISOU  761  CD  ARG A 100     5261   5315   4770    609   -286    276       C  
ATOM    762  NE  ARG A 100       2.926  -9.662  29.313  1.00 40.90           N  
ANISOU  762  NE  ARG A 100     5412   5362   4765    563   -315    426       N  
ATOM    763  CZ  ARG A 100       1.807 -10.301  29.004  1.00 41.41           C  
ANISOU  763  CZ  ARG A 100     5498   5350   4884    492   -303    550       C  
ATOM    764  NH1 ARG A 100       1.283 -10.183  27.810  1.00 45.06           N  
ANISOU  764  NH1 ARG A 100     5906   5749   5465    467   -285    539       N  
ATOM    765  NH2 ARG A 100       1.257 -11.147  29.818  1.00 42.55           N  
ANISOU  765  NH2 ARG A 100     5722   5484   4962    432   -328    695       N  
ATOM    766  N   SER A 101       4.562  -6.095  31.011  1.00 41.71           N  
ANISOU  766  N   SER A 101     5397   5786   4663    562   -100     24       N  
ATOM    767  CA  SER A 101       4.607  -6.536  32.419  1.00 45.95           C  
ANISOU  767  CA  SER A 101     6016   6429   5012    528   -130     78       C  
ATOM    768  C   SER A 101       4.214  -7.982  32.584  1.00 47.88           C  
ANISOU  768  C   SER A 101     6334   6623   5235    532   -230    268       C  
ATOM    769  O   SER A 101       3.608  -8.583  31.717  1.00 47.41           O  
ANISOU  769  O   SER A 101     6268   6444   5302    539   -242    350       O  
ATOM    770  CB  SER A 101       3.575  -5.774  33.248  1.00 47.97           C  
ANISOU  770  CB  SER A 101     6286   6747   5191    454     52     55       C  
ATOM    771  OG  SER A 101       3.982  -4.417  33.237  1.00 50.69           O  
ANISOU  771  OG  SER A 101     6589   7115   5554    446    143   -131       O  
ATOM    772  N   SER A 102       4.499  -8.500  33.773  1.00 48.98           N  
ANISOU  772  N   SER A 102     6552   6858   5199    508   -300    342       N  
ATOM    773  CA  SER A 102       4.239  -9.859  34.107  1.00 48.14           C  
ANISOU  773  CA  SER A 102     6534   6699   5057    503   -408    540       C  
ATOM    774  C   SER A 102       2.977  -9.944  34.878  1.00 49.54           C  
ANISOU  774  C   SER A 102     6756   6929   5135    392   -282    652       C  
ATOM    775  O   SER A 102       2.882  -9.321  35.885  1.00 50.27           O  
ANISOU  775  O   SER A 102     6867   7175   5059    333   -195    604       O  
ATOM    776  CB  SER A 102       5.409 -10.318  34.958  1.00 54.14           C  
ANISOU  776  CB  SER A 102     7341   7550   5677    546   -576    576       C  
ATOM    777  OG  SER A 102       5.242 -11.602  35.313  1.00 56.79           O  
ANISOU  777  OG  SER A 102     7771   7816   5988    549   -692    780       O  
ATOM    778  N   VAL A 103       2.052 -10.799  34.489  1.00 49.64           N  
ANISOU  778  N   VAL A 103     6794   6830   5234    350   -281    805       N  
ATOM    779  CA  VAL A 103       0.896 -11.091  35.304  1.00 53.29           C  
ANISOU  779  CA  VAL A 103     7294   7360   5592    230   -177    949       C  
ATOM    780  C   VAL A 103       0.914 -12.544  35.793  1.00 58.44           C  
ANISOU  780  C   VAL A 103     8071   7948   6183    189   -326   1178       C  
ATOM    781  O   VAL A 103       1.618 -13.354  35.261  1.00 58.12           O  
ANISOU  781  O   VAL A 103     8078   7762   6240    268   -496   1219       O  
ATOM    782  CB  VAL A 103      -0.377 -10.698  34.583  1.00 53.65           C  
ANISOU  782  CB  VAL A 103     7239   7362   5780    181    -22    948       C  
ATOM    783  CG1 VAL A 103      -0.364  -9.179  34.358  1.00 52.40           C  
ANISOU  783  CG1 VAL A 103     6975   7270   5663    228    130    740       C  
ATOM    784  CG2 VAL A 103      -0.501 -11.377  33.252  1.00 55.16           C  
ANISOU  784  CG2 VAL A 103     7414   7366   6175    205   -123    992       C  
ATOM    785  N   ASN A 104       0.210 -12.846  36.869  1.00 61.45           N  
ANISOU  785  N   ASN A 104     8510   8442   6395     69   -260   1326       N  
ATOM    786  CA  ASN A 104       0.236 -14.157  37.459  1.00 67.23           C  
ANISOU  786  CA  ASN A 104     9373   9119   7051     13   -401   1568       C  
ATOM    787  C   ASN A 104      -1.037 -14.927  37.252  1.00 68.31           C  
ANISOU  787  C   ASN A 104     9525   9164   7263   -119   -346   1750       C  
ATOM    788  O   ASN A 104      -1.286 -15.912  37.958  1.00 74.42           O  
ANISOU  788  O   ASN A 104    10412   9922   7942   -217   -415   1979       O  
ATOM    789  CB  ASN A 104       0.454 -14.017  38.966  1.00 74.15           C  
ANISOU  789  CB  ASN A 104    10323  10221   7630    -57   -384   1636       C  
ATOM    790  CG  ASN A 104       1.799 -13.405  39.290  1.00 77.64           C  
ANISOU  790  CG  ASN A 104    10759  10766   7973     46   -482   1484       C  
ATOM    791  OD1 ASN A 104       2.853 -13.962  38.929  1.00 81.69           O  
ANISOU  791  OD1 ASN A 104    11297  11169   8573    164   -685   1507       O  
ATOM    792  ND2 ASN A 104       1.784 -12.254  39.964  1.00 76.76           N  
ANISOU  792  ND2 ASN A 104    10610  10865   7688      3   -336   1318       N  
ATOM    793  N   ASP A 105      -1.856 -14.474  36.327  1.00 66.07           N  
ANISOU  793  N   ASP A 105     9124   8832   7144   -137   -228   1667       N  
ATOM    794  CA  ASP A 105      -3.166 -15.051  36.075  1.00 69.00           C  
ANISOU  794  CA  ASP A 105     9469   9152   7595   -284   -162   1823       C  
ATOM    795  C   ASP A 105      -3.480 -14.539  34.735  1.00 67.41           C  
ANISOU  795  C   ASP A 105     9142   8860   7608   -233   -126   1685       C  
ATOM    796  O   ASP A 105      -3.441 -13.335  34.512  1.00 68.04           O  
ANISOU  796  O   ASP A 105     9106   9037   7706   -159     -5   1509       O  
ATOM    797  CB  ASP A 105      -4.169 -14.495  37.067  1.00 72.62           C  
ANISOU  797  CB  ASP A 105     9856   9843   7891   -404     56   1872       C  
ATOM    798  CG  ASP A 105      -5.638 -14.915  36.798  1.00 75.74           C  
ANISOU  798  CG  ASP A 105    10164  10233   8378   -565    158   2025       C  
ATOM    799  OD1 ASP A 105      -6.046 -15.431  35.711  1.00 74.72           O  
ANISOU  799  OD1 ASP A 105    10003   9933   8454   -598     78   2065       O  
ATOM    800  OD2 ASP A 105      -6.412 -14.652  37.754  1.00 74.80           O  
ANISOU  800  OD2 ASP A 105     9996  10317   8105   -671    335   2095       O  
ATOM    801  N   ILE A 106      -3.747 -15.457  33.833  1.00 66.67           N  
ANISOU  801  N   ILE A 106     9085   8572   7671   -278   -241   1765       N  
ATOM    802  CA  ILE A 106      -3.975 -15.131  32.429  1.00 67.05           C  
ANISOU  802  CA  ILE A 106     9037   8527   7912   -244   -246   1647       C  
ATOM    803  C   ILE A 106      -5.171 -14.185  32.142  1.00 62.46           C  
ANISOU  803  C   ILE A 106     8262   8081   7387   -305    -62   1623       C  
ATOM    804  O   ILE A 106      -5.227 -13.589  31.084  1.00 67.52           O  
ANISOU  804  O   ILE A 106     8805   8692   8157   -251    -54   1510       O  
ATOM    805  CB  ILE A 106      -4.153 -16.461  31.641  1.00 70.07           C  
ANISOU  805  CB  ILE A 106     9523   8676   8422   -322   -406   1750       C  
ATOM    806  CG1 ILE A 106      -3.840 -16.283  30.150  1.00 69.42           C  
ANISOU  806  CG1 ILE A 106     9401   8477   8498   -248   -471   1588       C  
ATOM    807  CG2 ILE A 106      -5.552 -17.079  31.880  1.00 74.33           C  
ANISOU  807  CG2 ILE A 106    10038   9229   8973   -541   -355   1954       C  
ATOM    808  CD1 ILE A 106      -3.266 -17.537  29.509  1.00 72.25           C  
ANISOU  808  CD1 ILE A 106     9922   8581   8947   -232   -654   1594       C  
ATOM    809  N   GLY A 107      -6.130 -14.111  33.051  1.00 58.58           N  
ANISOU  809  N   GLY A 107     7714   7739   6804   -419     78   1744       N  
ATOM    810  CA  GLY A 107      -7.224 -13.181  33.011  1.00 58.74           C  
ANISOU  810  CA  GLY A 107     7534   7911   6872   -448    275   1726       C  
ATOM    811  C   GLY A 107      -6.815 -11.712  33.195  1.00 61.53           C  
ANISOU  811  C   GLY A 107     7803   8372   7201   -296    415   1521       C  
ATOM    812  O   GLY A 107      -7.602 -10.799  32.907  1.00 62.60           O  
ANISOU  812  O   GLY A 107     7764   8587   7433   -271    566   1474       O  
ATOM    813  N   ASP A 108      -5.606 -11.464  33.686  1.00 58.61           N  
ANISOU  813  N   ASP A 108     7550   8004   6714   -198    365   1403       N  
ATOM    814  CA  ASP A 108      -5.056 -10.121  33.620  1.00 60.58           C  
ANISOU  814  CA  ASP A 108     7740   8303   6973    -66    456   1190       C  
ATOM    815  C   ASP A 108      -4.159  -9.835  32.419  1.00 56.16           C  
ANISOU  815  C   ASP A 108     7181   7606   6549     40    329   1064       C  
ATOM    816  O   ASP A 108      -3.631  -8.723  32.356  1.00 55.15           O  
ANISOU  816  O   ASP A 108     7014   7507   6433    134    396    895       O  
ATOM    817  CB  ASP A 108      -4.289  -9.772  34.871  1.00 62.50           C  
ANISOU  817  CB  ASP A 108     8081   8666   6997    -40    497   1105       C  
ATOM    818  CG  ASP A 108      -5.114  -9.871  36.107  1.00 68.34           C  
ANISOU  818  CG  ASP A 108     8821   9578   7564   -145    655   1199       C  
ATOM    819  OD1 ASP A 108      -6.354  -9.689  36.104  1.00 76.65           O  
ANISOU  819  OD1 ASP A 108     9744  10699   8679   -204    817   1264       O  
ATOM    820  OD2 ASP A 108      -4.473 -10.162  37.109  1.00 70.78           O  
ANISOU  820  OD2 ASP A 108     9259   9972   7661   -173    610   1214       O  
ATOM    821  N   ASP A 109      -4.008 -10.783  31.474  1.00 53.48           N  
ANISOU  821  N   ASP A 109     6888   7122   6309     18    163   1134       N  
ATOM    822  CA  ASP A 109      -3.118 -10.594  30.326  1.00 50.10           C  
ANISOU  822  CA  ASP A 109     6465   6583   5985    112     52   1011       C  
ATOM    823  C   ASP A 109      -3.439  -9.309  29.551  1.00 47.34           C  
ANISOU  823  C   ASP A 109     5969   6263   5755    164    159    908       C  
ATOM    824  O   ASP A 109      -2.536  -8.584  29.091  1.00 46.06           O  
ANISOU  824  O   ASP A 109     5799   6080   5619    255    142    764       O  
ATOM    825  CB  ASP A 109      -3.197 -11.799  29.356  1.00 49.02           C  
ANISOU  825  CB  ASP A 109     6391   6291   5941     59   -107   1093       C  
ATOM    826  CG  ASP A 109      -2.218 -11.678  28.189  1.00 49.48           C  
ANISOU  826  CG  ASP A 109     6464   6256   6079    154   -208    953       C  
ATOM    827  OD1 ASP A 109      -0.997 -11.823  28.384  1.00 48.73           O  
ANISOU  827  OD1 ASP A 109     6445   6135   5935    252   -284    867       O  
ATOM    828  OD2 ASP A 109      -2.649 -11.348  27.086  1.00 50.56           O  
ANISOU  828  OD2 ASP A 109     6518   6371   6320    133   -203    929       O  
ATOM    829  N   TRP A 110      -4.743  -9.068  29.374  1.00 46.45           N  
ANISOU  829  N   TRP A 110     5729   6195   5723     99    261   1002       N  
ATOM    830  CA  TRP A 110      -5.230  -7.966  28.576  1.00 44.74           C  
ANISOU  830  CA  TRP A 110     5361   5990   5647    147    345    957       C  
ATOM    831  C   TRP A 110      -4.626  -6.624  28.918  1.00 45.30           C  
ANISOU  831  C   TRP A 110     5409   6090   5710    259    459    793       C  
ATOM    832  O   TRP A 110      -4.505  -5.767  28.047  1.00 47.37           O  
ANISOU  832  O   TRP A 110     5598   6309   6090    318    469    733       O  
ATOM    833  CB  TRP A 110      -6.752  -7.871  28.701  1.00 46.75           C  
ANISOU  833  CB  TRP A 110     5460   6326   5978     77    463   1095       C  
ATOM    834  CG  TRP A 110      -7.266  -7.456  30.079  1.00 50.45           C  
ANISOU  834  CG  TRP A 110     5891   6921   6353     80    658   1093       C  
ATOM    835  CD1 TRP A 110      -7.531  -8.269  31.131  1.00 50.84           C  
ANISOU  835  CD1 TRP A 110     6011   7046   6259    -12    686   1184       C  
ATOM    836  CD2 TRP A 110      -7.578  -6.116  30.520  1.00 49.67           C  
ANISOU  836  CD2 TRP A 110     5686   6887   6297    180    861    988       C  
ATOM    837  NE1 TRP A 110      -7.961  -7.528  32.207  1.00 50.95           N  
ANISOU  837  NE1 TRP A 110     5967   7193   6195     16    899   1132       N  
ATOM    838  CE2 TRP A 110      -7.990  -6.209  31.857  1.00 50.71           C  
ANISOU  838  CE2 TRP A 110     5832   7147   6285    141   1013    998       C  
ATOM    839  CE3 TRP A 110      -7.498  -4.850  29.914  1.00 48.43           C  
ANISOU  839  CE3 TRP A 110     5438   6678   6284    298    928    884       C  
ATOM    840  CZ2 TRP A 110      -8.375  -5.107  32.578  1.00 52.34           C  
ANISOU  840  CZ2 TRP A 110     5961   7433   6490    220   1240    886       C  
ATOM    841  CZ3 TRP A 110      -7.821  -3.757  30.609  1.00 48.04           C  
ANISOU  841  CZ3 TRP A 110     5322   6672   6256    383   1135    782       C  
ATOM    842  CH2 TRP A 110      -8.307  -3.877  31.935  1.00 53.48           C  
ANISOU  842  CH2 TRP A 110     6019   7494   6806    349   1302    772       C  
ATOM    843  N   LYS A 111      -4.284  -6.447  30.196  1.00 46.28           N  
ANISOU  843  N   LYS A 111     5603   6290   5689    272    542    727       N  
ATOM    844  CA  LYS A 111      -3.749  -5.229  30.719  1.00 48.25           C  
ANISOU  844  CA  LYS A 111     5855   6570   5906    349    657    555       C  
ATOM    845  C   LYS A 111      -2.256  -5.145  30.929  1.00 44.99           C  
ANISOU  845  C   LYS A 111     5560   6144   5391    386    555    419       C  
ATOM    846  O   LYS A 111      -1.802  -4.140  31.273  1.00 47.88           O  
ANISOU  846  O   LYS A 111     5928   6525   5737    426    636    274       O  
ATOM    847  CB  LYS A 111      -4.458  -4.822  31.964  1.00 53.16           C  
ANISOU  847  CB  LYS A 111     6455   7309   6435    334    851    537       C  
ATOM    848  CG  LYS A 111      -4.283  -5.678  33.209  1.00 60.42           C  
ANISOU  848  CG  LYS A 111     7494   8337   7126    256    836    586       C  
ATOM    849  CD  LYS A 111      -4.983  -5.059  34.413  1.00 62.37           C  
ANISOU  849  CD  LYS A 111     7711   8723   7261    241   1067    531       C  
ATOM    850  CE  LYS A 111      -5.297  -6.119  35.423  1.00 72.08           C  
ANISOU  850  CE  LYS A 111     9018  10077   8291    126   1061    673       C  
ATOM    851  NZ  LYS A 111      -5.930  -5.539  36.659  1.00 82.52           N  
ANISOU  851  NZ  LYS A 111    10321  11569   9461    100   1303    603       N  
ATOM    852  N   ALA A 112      -1.512  -6.121  30.504  1.00 42.57           N  
ANISOU  852  N   ALA A 112     5327   5789   5056    377    375    462       N  
ATOM    853  CA  ALA A 112      -0.118  -6.180  30.698  1.00 41.71           C  
ANISOU  853  CA  ALA A 112     5300   5685   4861    418    267    357       C  
ATOM    854  C   ALA A 112       0.761  -5.462  29.714  1.00 42.23           C  
ANISOU  854  C   ALA A 112     5325   5695   5025    475    226    234       C  
ATOM    855  O   ALA A 112       1.976  -5.561  29.833  1.00 44.55           O  
ANISOU  855  O   ALA A 112     5662   6009   5254    506    129    151       O  
ATOM    856  CB  ALA A 112       0.270  -7.652  30.669  1.00 41.76           C  
ANISOU  856  CB  ALA A 112     5397   5650   4818    404     95    470       C  
ATOM    857  N   THR A 113       0.232  -4.773  28.706  1.00 41.00           N  
ANISOU  857  N   THR A 113     5077   5479   5022    485    285    234       N  
ATOM    858  CA  THR A 113       1.104  -4.185  27.701  1.00 38.67           C  
ANISOU  858  CA  THR A 113     4749   5137   4803    519    237    143       C  
ATOM    859  C   THR A 113       0.951  -2.696  27.476  1.00 40.00           C  
ANISOU  859  C   THR A 113     4849   5276   5070    535    363     62       C  
ATOM    860  O   THR A 113      -0.145  -2.239  27.140  1.00 38.91           O  
ANISOU  860  O   THR A 113     4635   5102   5047    539    454    138       O  
ATOM    861  CB  THR A 113       0.911  -4.915  26.369  1.00 38.69           C  
ANISOU  861  CB  THR A 113     4729   5079   4891    508    134    229       C  
ATOM    862  OG1 THR A 113       1.146  -6.314  26.559  1.00 41.29           O  
ANISOU  862  OG1 THR A 113     5142   5395   5149    500     14    286       O  
ATOM    863  CG2 THR A 113       1.892  -4.468  25.376  1.00 40.13           C  
ANISOU  863  CG2 THR A 113     4888   5243   5116    532     85    140       C  
ATOM    864  N   ARG A 114       2.058  -1.938  27.616  1.00 38.44           N  
ANISOU  864  N   ARG A 114     4671   5087   4845    543    362    -81       N  
ATOM    865  CA  ARG A 114       2.033  -0.527  27.336  1.00 39.32           C  
ANISOU  865  CA  ARG A 114     4737   5134   5065    548    470   -158       C  
ATOM    866  C   ARG A 114       2.710  -0.215  26.030  1.00 39.70           C  
ANISOU  866  C   ARG A 114     4744   5139   5200    540    400   -159       C  
ATOM    867  O   ARG A 114       3.528  -1.017  25.499  1.00 37.11           O  
ANISOU  867  O   ARG A 114     4427   4854   4817    535    275   -158       O  
ATOM    868  CB  ARG A 114       2.728   0.287  28.384  1.00 40.14           C  
ANISOU  868  CB  ARG A 114     4896   5265   5087    529    534   -328       C  
ATOM    869  CG  ARG A 114       2.018   0.226  29.691  1.00 43.31           C  
ANISOU  869  CG  ARG A 114     5344   5722   5388    527    640   -351       C  
ATOM    870  CD  ARG A 114       2.859   0.982  30.660  1.00 48.84           C  
ANISOU  870  CD  ARG A 114     6114   6465   5976    485    678   -541       C  
ATOM    871  NE  ARG A 114       2.122   1.182  31.893  1.00 54.89           N  
ANISOU  871  NE  ARG A 114     6930   7285   6640    476    821   -596       N  
ATOM    872  CZ  ARG A 114       2.236   0.433  32.986  1.00 65.45           C  
ANISOU  872  CZ  ARG A 114     8338   8764   7763    437    787   -592       C  
ATOM    873  NH1 ARG A 114       3.091  -0.600  33.055  1.00 75.53           N  
ANISOU  873  NH1 ARG A 114     9648  10129   8921    416    600   -527       N  
ATOM    874  NH2 ARG A 114       1.492   0.714  34.043  1.00 72.13           N  
ANISOU  874  NH2 ARG A 114     9224   9670   8510    421    946   -650       N  
ATOM    875  N   VAL A 115       2.413   0.979  25.527  1.00 36.58           N  
ANISOU  875  N   VAL A 115     4302   4656   4941    541    488   -162       N  
ATOM    876  CA  VAL A 115       2.940   1.359  24.236  1.00 37.79           C  
ANISOU  876  CA  VAL A 115     4413   4776   5170    515    433   -133       C  
ATOM    877  C   VAL A 115       3.329   2.819  24.244  1.00 39.51           C  
ANISOU  877  C   VAL A 115     4628   4902   5479    492    522   -218       C  
ATOM    878  O   VAL A 115       2.724   3.590  24.900  1.00 39.60           O  
ANISOU  878  O   VAL A 115     4650   4834   5560    519    640   -254       O  
ATOM    879  CB  VAL A 115       1.903   1.013  23.126  1.00 40.89           C  
ANISOU  879  CB  VAL A 115     4740   5144   5652    522    402     44       C  
ATOM    880  CG1 VAL A 115       0.641   1.870  23.182  1.00 43.39           C  
ANISOU  880  CG1 VAL A 115     4991   5373   6121    562    516    135       C  
ATOM    881  CG2 VAL A 115       2.503   1.084  21.743  1.00 39.52           C  
ANISOU  881  CG2 VAL A 115     4538   4981   5494    477    322     83       C  
ATOM    882  N   GLY A 116       4.422   3.164  23.555  1.00 43.07           N  
ANISOU  882  N   GLY A 116     5070   5367   5926    434    468   -263       N  
ATOM    883  CA  GLY A 116       4.683   4.548  23.223  1.00 42.54           C  
ANISOU  883  CA  GLY A 116     4997   5185   5979    390    538   -293       C  
ATOM    884  C   GLY A 116       5.812   4.661  22.229  1.00 41.17           C  
ANISOU  884  C   GLY A 116     4793   5067   5783    309    466   -296       C  
ATOM    885  O   GLY A 116       6.150   3.691  21.549  1.00 38.35           O  
ANISOU  885  O   GLY A 116     4405   4823   5343    310    374   -252       O  
ATOM    886  N   ILE A 117       6.390   5.868  22.182  1.00 41.60           N  
ANISOU  886  N   ILE A 117     4857   5033   5913    234    518   -357       N  
ATOM    887  CA  ILE A 117       7.486   6.218  21.298  1.00 44.53           C  
ANISOU  887  CA  ILE A 117     5191   5454   6274    131    477   -360       C  
ATOM    888  C   ILE A 117       8.751   6.586  22.025  1.00 44.10           C  
ANISOU  888  C   ILE A 117     5146   5454   6153     42    470   -539       C  
ATOM    889  O   ILE A 117       8.727   6.931  23.171  1.00 44.19           O  
ANISOU  889  O   ILE A 117     5216   5420   6151     41    512   -664       O  
ATOM    890  CB  ILE A 117       7.167   7.390  20.380  1.00 48.19           C  
ANISOU  890  CB  ILE A 117     5646   5768   6895     77    528   -236       C  
ATOM    891  CG1 ILE A 117       6.947   8.688  21.143  1.00 50.83           C  
ANISOU  891  CG1 ILE A 117     6046   5896   7369     61    634   -312       C  
ATOM    892  CG2 ILE A 117       5.952   7.055  19.564  1.00 53.02           C  
ANISOU  892  CG2 ILE A 117     6225   6351   7566    152    512    -37       C  
ATOM    893  CD1 ILE A 117       8.006   9.655  20.790  1.00 56.98           C  
ANISOU  893  CD1 ILE A 117     6833   6626   8190    -88    643   -357       C  
ATOM    894  N   ASN A 118       9.876   6.441  21.369  1.00 47.39           N  
ANISOU  894  N   ASN A 118     5496   5996   6511    -37    413   -556       N  
ATOM    895  CA  ASN A 118      11.136   7.047  21.881  1.00 49.29           C  
ANISOU  895  CA  ASN A 118     5718   6290   6719   -160    406   -706       C  
ATOM    896  C   ASN A 118      11.918   7.547  20.705  1.00 48.63           C  
ANISOU  896  C   ASN A 118     5560   6248   6668   -281    406   -645       C  
ATOM    897  O   ASN A 118      11.982   6.879  19.702  1.00 49.47           O  
ANISOU  897  O   ASN A 118     5605   6461   6727   -252    375   -551       O  
ATOM    898  CB  ASN A 118      11.958   6.075  22.698  1.00 50.60           C  
ANISOU  898  CB  ASN A 118     5843   6647   6733   -127    317   -825       C  
ATOM    899  CG  ASN A 118      11.641   6.150  24.175  1.00 53.26           C  
ANISOU  899  CG  ASN A 118     6266   6948   7019   -103    329   -940       C  
ATOM    900  OD1 ASN A 118      11.427   5.161  24.791  1.00 58.63           O  
ANISOU  900  OD1 ASN A 118     6961   7714   7601     -9    275   -944       O  
ATOM    901  ND2 ASN A 118      11.675   7.325  24.742  1.00 56.44           N  
ANISOU  901  ND2 ASN A 118     6734   7229   7481   -202    398  -1040       N  
ATOM    902  N   ILE A 119      12.428   8.760  20.807  1.00 51.78           N  
ANISOU  902  N   ILE A 119     5976   6551   7147   -426    452   -694       N  
ATOM    903  CA  ILE A 119      13.413   9.304  19.876  1.00 56.92           C  
ANISOU  903  CA  ILE A 119     6548   7269   7810   -585    455   -655       C  
ATOM    904  C   ILE A 119      14.757   9.299  20.541  1.00 55.02           C  
ANISOU  904  C   ILE A 119     6229   7189   7486   -692    408   -823       C  
ATOM    905  O   ILE A 119      14.908   9.852  21.625  1.00 52.37           O  
ANISOU  905  O   ILE A 119     5955   6778   7164   -751    412   -959       O  
ATOM    906  CB  ILE A 119      13.103  10.760  19.540  1.00 64.71           C  
ANISOU  906  CB  ILE A 119     7609   8012   8965   -704    532   -579       C  
ATOM    907  CG1 ILE A 119      11.770  10.777  18.787  1.00 73.36           C  
ANISOU  907  CG1 ILE A 119     8751   8967  10151   -591    561   -379       C  
ATOM    908  CG2 ILE A 119      14.198  11.349  18.647  1.00 67.01           C  
ANISOU  908  CG2 ILE A 119     7819   8385   9256   -904    537   -531       C  
ATOM    909  CD1 ILE A 119      10.768  11.808  19.279  1.00 78.76           C  
ANISOU  909  CD1 ILE A 119     9551   9349  11023   -551    638   -354       C  
ATOM    910  N   PHE A 120      15.723   8.711  19.867  1.00 54.30           N  
ANISOU  910  N   PHE A 120     5997   7325   7307   -724    368   -815       N  
ATOM    911  CA  PHE A 120      17.061   8.559  20.381  1.00 54.19           C  
ANISOU  911  CA  PHE A 120     5859   7513   7216   -809    310   -952       C  
ATOM    912  C   PHE A 120      17.979   9.390  19.525  1.00 59.15           C  
ANISOU  912  C   PHE A 120     6389   8201   7881  -1017    352   -915       C  
ATOM    913  O   PHE A 120      18.011   9.207  18.315  1.00 60.43           O  
ANISOU  913  O   PHE A 120     6494   8435   8031  -1023    391   -795       O  
ATOM    914  CB  PHE A 120      17.548   7.112  20.282  1.00 52.05           C  
ANISOU  914  CB  PHE A 120     5467   7483   6826   -656    238   -977       C  
ATOM    915  CG  PHE A 120      16.952   6.176  21.300  1.00 50.08           C  
ANISOU  915  CG  PHE A 120     5289   7218   6517   -478    171  -1022       C  
ATOM    916  CD1 PHE A 120      15.801   5.438  21.016  1.00 46.76           C  
ANISOU  916  CD1 PHE A 120     4959   6707   6099   -319    182   -928       C  
ATOM    917  CD2 PHE A 120      17.553   5.995  22.534  1.00 49.34           C  
ANISOU  917  CD2 PHE A 120     5169   7221   6355   -483     88  -1147       C  
ATOM    918  CE1 PHE A 120      15.296   4.528  21.936  1.00 45.53           C  
ANISOU  918  CE1 PHE A 120     4865   6549   5884   -174    122   -954       C  
ATOM    919  CE2 PHE A 120      17.039   5.092  23.446  1.00 50.17           C  
ANISOU  919  CE2 PHE A 120     5342   7331   6389   -331     24  -1163       C  
ATOM    920  CZ  PHE A 120      15.913   4.361  23.150  1.00 46.84           C  
ANISOU  920  CZ  PHE A 120     5011   6809   5977   -178     47  -1065       C  
ATOM    921  N   THR A 121      18.772  10.239  20.170  1.00 63.79           N  
ANISOU  921  N   THR A 121     6953   8786   8495  -1201    340  -1024       N  
ATOM    922  CA  THR A 121      19.824  11.005  19.493  1.00 69.27           C  
ANISOU  922  CA  THR A 121     7531   9571   9219  -1435    371  -1001       C  
ATOM    923  C   THR A 121      21.209  10.695  20.057  1.00 68.59           C  
ANISOU  923  C   THR A 121     7251   9761   9046  -1520    292  -1141       C  
ATOM    924  O   THR A 121      21.339  10.256  21.187  1.00 63.06           O  
ANISOU  924  O   THR A 121     6552   9121   8286  -1448    205  -1267       O  
ATOM    925  CB  THR A 121      19.575  12.491  19.658  1.00 72.51           C  
ANISOU  925  CB  THR A 121     8080   9699   9768  -1633    427   -992       C  
ATOM    926  OG1 THR A 121      19.286  12.733  21.037  1.00 75.12           O  
ANISOU  926  OG1 THR A 121     8529   9902  10108  -1615    392  -1156       O  
ATOM    927  CG2 THR A 121      18.361  12.894  18.817  1.00 75.17           C  
ANISOU  927  CG2 THR A 121     8558   9789  10213  -1565    504   -804       C  
ATOM    928  N   ARG A 122      22.228  10.918  19.239  1.00 78.00           N  
ANISOU  928  N   ARG A 122     8266  11140  10230  -1676    322  -1102       N  
ATOM    929  CA  ARG A 122      23.637  10.705  19.636  1.00 85.51           C  
ANISOU  929  CA  ARG A 122     8984  12386  11119  -1777    253  -1214       C  
ATOM    930  C   ARG A 122      23.994  11.474  20.909  1.00 95.51           C  
ANISOU  930  C   ARG A 122    10300  13585  12405  -1950    175  -1360       C  
ATOM    931  O   ARG A 122      23.551  12.609  21.090  1.00 95.20           O  
ANISOU  931  O   ARG A 122    10436  13276  12460  -2113    220  -1365       O  
ATOM    932  CB  ARG A 122      24.556  11.181  18.536  1.00 85.62           C  
ANISOU  932  CB  ARG A 122     8822  12563  11145  -1981    330  -1137       C  
ATOM    933  CG  ARG A 122      24.634  10.278  17.324  1.00 86.95           C  
ANISOU  933  CG  ARG A 122     8870  12923  11244  -1836    401  -1044       C  
ATOM    934  CD  ARG A 122      25.475   9.052  17.604  1.00 90.63           C  
ANISOU  934  CD  ARG A 122     9107  13699  11627  -1659    337  -1148       C  
ATOM    935  NE  ARG A 122      25.809   8.371  16.352  1.00 94.38           N  
ANISOU  935  NE  ARG A 122     9437  14380  12039  -1577    434  -1091       N  
ATOM    936  CZ  ARG A 122      25.902   7.043  16.189  1.00101.62           C  
ANISOU  936  CZ  ARG A 122    10264  15450  12897  -1311    421  -1141       C  
ATOM    937  NH1 ARG A 122      25.679   6.200  17.196  1.00105.98           N  
ANISOU  937  NH1 ARG A 122    10850  15970  13446  -1096    302  -1219       N  
ATOM    938  NH2 ARG A 122      26.196   6.534  14.990  1.00106.22           N  
ANISOU  938  NH2 ARG A 122    10734  16209  13416  -1261    533  -1111       N  
ATOM    939  N   LEU A 123      24.781  10.850  21.784  1.00 82.48           N  
ATOM    940  CA  LEU A 123      25.236  11.467  23.033  1.00 92.15           C  
ATOM    941  C   LEU A 123      26.711  11.906  22.926  1.00 98.60           C  
ATOM    942  O   LEU A 123      27.028  13.030  22.499  1.00104.59           O  
ATOM    943  CB  LEU A 123      25.052  10.462  24.169  1.00 97.55           C  
ATOM    944  CG  LEU A 123      25.395  10.911  25.585  1.00106.24           C  
ATOM    945  CD1 LEU A 123      24.579  12.152  25.946  1.00108.64           C  
ATOM    946  CD2 LEU A 123      25.174   9.754  26.563  1.00101.48           C  
TER     947      LEU A 123                                                      
HETATM  948  C1  NAG A 201      23.329   9.635  30.451  1.00 84.51           C  
HETATM  949  C2  NAG A 201      23.091   9.870  31.930  1.00 95.34           C  
HETATM  950  C3  NAG A 201      23.062  11.370  32.243  1.00104.36           C  
HETATM  951  C4  NAG A 201      24.322  12.074  31.755  1.00107.20           C  
HETATM  952  C5  NAG A 201      24.587  11.686  30.286  1.00107.51           C  
HETATM  953  C6  NAG A 201      25.943  12.208  29.808  1.00105.67           C  
HETATM  954  C7  NAG A 201      21.692   8.149  32.982  1.00 82.61           C  
HETATM  955  C8  NAG A 201      20.276   7.781  33.302  1.00 89.33           C  
HETATM  956  N2  NAG A 201      21.818   9.295  32.325  1.00 87.39           N  
HETATM  957  O3  NAG A 201      22.931  11.577  33.654  1.00103.03           O  
HETATM  958  O4  NAG A 201      24.174  13.496  31.968  1.00106.75           O  
HETATM  959  O5  NAG A 201      24.560  10.249  30.094  1.00 95.59           O  
HETATM  960  O6  NAG A 201      26.984  11.315  30.229  1.00109.53           O  
HETATM  961  O7  NAG A 201      22.630   7.436  33.300  1.00 83.28           O  
HETATM  962  O1  55R A 202      13.935   4.484  28.708  1.00 53.45           O  
HETATM  963  O2  55R A 202      13.649   3.240  30.474  1.00 62.48           O  
HETATM  964  C3  55R A 202      13.299   3.602  29.330  1.00 53.90           C  
HETATM  965  C4  55R A 202      12.075   2.980  28.712  1.00 51.56           C  
HETATM  966  C5  55R A 202      11.359   1.938  29.309  1.00 51.87           C  
HETATM  967  C6  55R A 202      10.237   1.404  28.689  1.00 50.53           C  
HETATM  968  C7  55R A 202       9.830   1.907  27.470  1.00 48.94           C  
HETATM  969  C8  55R A 202      10.548   2.925  26.863  1.00 51.71           C  
HETATM  970  C9  55R A 202      11.657   3.472  27.486  1.00 50.14           C  
HETATM  971  O16 55R A 202      12.017  -1.680  36.010  1.00 82.67           O  
HETATM  972  C13 55R A 202      11.803  -1.168  34.882  1.00 74.35           C  
HETATM  973  C12 55R A 202      10.609  -1.560  34.119  1.00 71.23           C  
HETATM  974  C11 55R A 202      10.365  -0.992  32.897  1.00 66.69           C  
HETATM  975  C14 55R A 202      12.722  -0.161  34.323  1.00 69.00           C  
HETATM  976  C15 55R A 202      12.468   0.414  33.102  1.00 66.35           C  
HETATM  977  C10 55R A 202      11.278   0.013  32.327  1.00 63.86           C  
HETATM  978  N9  55R A 202      10.969   0.498  31.146  1.00 51.74           N  
HETATM  979  N8  55R A 202      11.733   1.415  30.550  1.00 52.68           N  
HETATM  980  O   HOH A 301      22.873   0.273   5.943  1.00 90.82           O  
HETATM  981  O   HOH A 302       9.108  -3.464  37.208  1.00 76.07           O  
HETATM  982  O   HOH A 303      13.520 -10.116  28.152  1.00 63.51           O  
HETATM  983  O   HOH A 304      28.675  -1.841  13.833  1.00 74.61           O  
HETATM  984  O   HOH A 305      18.234  -7.775  28.416  1.00 85.82           O  
HETATM  985  O   HOH A 306      -3.386  -6.155  25.854  1.00 47.65           O  
HETATM  986  O   HOH A 307      27.161  -5.513  19.403  1.00 69.59           O  
HETATM  987  O   HOH A 308      17.600  -8.589  25.575  1.00 61.94           O  
HETATM  988  O   HOH A 309      -0.856 -10.261  25.443  1.00 54.84           O  
HETATM  989  O   HOH A 310      -1.187  -7.667  26.766  1.00 41.68           O  
HETATM  990  O   HOH A 311      16.401 -10.697  33.068  1.00 66.86           O  
HETATM  991  O   HOH A 312       3.509  -8.704  38.468  1.00 77.41           O  
HETATM  992  O   HOH A 313      14.292   1.543  43.029  1.00 82.43           O  
HETATM  993  O   HOH A 314       0.582  -2.889  31.913  1.00 55.95           O  
HETATM  994  O   HOH A 315      -5.312 -10.755  26.607  1.00 77.04           O  
HETATM  995  O   HOH A 316       6.434  -7.209  35.298  1.00 61.96           O  
HETATM  996  O   HOH A 317       9.061   7.243  16.966  1.00 66.80           O  
HETATM  997  O   HOH A 318       9.431 -12.462  33.808  1.00 45.04           O  
HETATM  998  O   HOH A 319      18.451  -0.959  33.001  1.00 68.80           O  
HETATM  999  O   HOH A 320      20.319 -10.292  18.319  1.00 68.52           O  
HETATM 1000  O   HOH A 321      15.429  -8.909  20.090  0.50 45.77           O  
HETATM 1001  O   HOH A 322       2.202  -8.689  25.425  1.00 45.41           O  
HETATM 1002  O   HOH A 323       4.175 -11.279  38.746  1.00 79.35           O  
HETATM 1003  O   HOH A 324      -2.381  -3.854  27.984  1.00 46.06           O  
HETATM 1004  O   HOH A 325      -1.797 -10.983  37.723  1.00 69.89           O  
HETATM 1005  O   HOH A 326       3.276  -2.897  30.882  1.00 41.13           O  
HETATM 1006  O   HOH A 327      -6.740 -11.150  29.548  1.00 55.24           O  
HETATM 1007  O   HOH A 328       8.168  -6.558  37.616  1.00 75.20           O  
HETATM 1008  O   HOH A 329      30.344 -11.628  11.720  1.00 70.04           O  
HETATM 1009  O   HOH A 330      -8.430  -7.903  35.069  1.00 75.68           O  
HETATM 1010  O   HOH A 331      24.418   3.105  28.093  1.00 70.25           O  
HETATM 1011  O   HOH A 332       1.481  -6.709  35.845  1.00 68.15           O  
HETATM 1012  O   HOH A 333       6.840  -2.713  34.616  1.00 62.91           O  
HETATM 1013  O   HOH A 334      28.460   7.385  19.580  1.00 65.37           O  
HETATM 1014  O   HOH A 335      30.606  -5.095  20.179  1.00 68.28           O  
HETATM 1015  O   HOH A 336      17.953 -10.366  20.089  1.00119.52           O  
HETATM 1016  O   HOH A 337       4.882   7.653  24.278  1.00 50.63           O  
HETATM 1017  O   HOH A 338      27.246  -8.535  17.306  1.00 76.06           O  
HETATM 1018  O   HOH A 339      18.903  -8.680  33.089  1.00 84.54           O  
HETATM 1019  O   HOH A 340      29.875  13.423  23.978  1.00 90.52           O  
HETATM 1020  O   HOH A 341      -3.314 -18.385  35.266  1.00 85.02           O  
HETATM 1021  O   HOH A 342      17.899  -0.009   0.009  1.00165.18           O  
HETATM 1022  O   HOH A 343       2.737  -2.965  36.018  1.00 90.72           O  
HETATM 1023  O   HOH A 344      27.579  14.131  25.831  1.00 67.15           O  
HETATM 1024  O   HOH A 345      28.140  -8.772  20.181  1.00 83.38           O  
HETATM 1025  O   HOH A 346       0.000   0.000  37.391  1.00119.44           O  
HETATM 1026  O   HOH A 347      -4.363 -10.316  23.809  1.00 75.50           O  
HETATM 1027  O   HOH A 348       4.694   1.303  36.527  1.00 82.28           O  
HETATM 1028  O   HOH A 349      27.866 -11.246  21.878  1.00 86.43           O  
HETATM 1029  O   HOH A 350       8.386   1.411  35.668  1.00 70.70           O  
HETATM 1030  O   HOH A 351      21.096  -8.666  37.727  1.00 76.33           O  
CONECT   15  617                                                                
CONECT  112  948                                                                
CONECT  617   15                                                                
CONECT  948  112  949  959                                                      
CONECT  949  948  950  956                                                      
CONECT  950  949  951  957                                                      
CONECT  951  950  952  958                                                      
CONECT  952  951  953  959                                                      
CONECT  953  952  960                                                           
CONECT  954  955  956  961                                                      
CONECT  955  954                                                                
CONECT  956  949  954                                                           
CONECT  957  950                                                                
CONECT  958  951                                                                
CONECT  959  948  952                                                           
CONECT  960  953                                                                
CONECT  961  954                                                                
CONECT  962  964                                                                
CONECT  963  964                                                                
CONECT  964  962  963  965                                                      
CONECT  965  964  966  970                                                      
CONECT  966  965  967  979                                                      
CONECT  967  966  968                                                           
CONECT  968  967  969                                                           
CONECT  969  968  970                                                           
CONECT  970  965  969                                                           
CONECT  971  972                                                                
CONECT  972  971  973  975                                                      
CONECT  973  972  974                                                           
CONECT  974  973  977                                                           
CONECT  975  972  976                                                           
CONECT  976  975  977                                                           
CONECT  977  974  976  978                                                      
CONECT  978  977  979                                                           
CONECT  979  966  978                                                           
MASTER      384    0    2    1    9    0    4    6 1029    1   35   10          
END                                                                             



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

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