CNRS Nantes University UFIP UFIP
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***  ENDOCYTOSIS 29-OCT-19 6L6O  ***

elNémo ID: 22032415353494955

Job options:

ID        	=	 22032415353494955
JOBID     	=	 ENDOCYTOSIS 29-OCT-19 6L6O
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    ENDOCYTOSIS                             29-OCT-19   6L6O              
TITLE     CRYSTAL STRUCTURE OF STABILIZED RAB5A GTPASE DOMAIN FROM LEISHMANIA   
TITLE    2 DONOVANI                                                             
COMPND    MOL_ID: 1;                                                            
COMPND   2 MOLECULE: RAB5A;                                                     
COMPND   3 CHAIN: A;                                                            
COMPND   4 ENGINEERED: YES;                                                     
COMPND   5 MUTATION: YES;                                                       
COMPND   6 OTHER_DETAILS: RESIDUE 60-79 DELETION                                
SOURCE    MOL_ID: 1;                                                            
SOURCE   2 ORGANISM_SCIENTIFIC: LEISHMANIA DONOVANI;                            
SOURCE   3 ORGANISM_TAXID: 5661;                                                
SOURCE   4 GENE: RAB5A;                                                         
SOURCE   5 EXPRESSION_SYSTEM: ESCHERICHIA COLI BL21;                            
SOURCE   6 EXPRESSION_SYSTEM_TAXID: 511693;                                     
SOURCE   7 EXPRESSION_SYSTEM_STRAIN: BL21;                                      
SOURCE   8 EXPRESSION_SYSTEM_VECTOR_TYPE: PLASMID;                              
SOURCE   9 EXPRESSION_SYSTEM_PLASMID: PGEX4T1                                   
KEYWDS    INTRACELLULAR TRAFFICKING, GTPASE, ENDOCYTOSIS                        
EXPDTA    X-RAY DIFFRACTION                                                     
AUTHOR    A.ARORA,M.ZOHIB,B.K.BISWAL,D.MAHESHWARI,R.K.PAL                       
REVDAT   1   11-NOV-20 6L6O    0                                                
JRNL        AUTH   M.ZOHIB,D.MAHESHWARI,R.K.PAL,S.FREITAG-POHL,B.K.BISWAL,      
JRNL        AUTH 2 E.POHL,A.ARORA                                               
JRNL        TITL   CRYSTAL STRUCTURE OF THE GDP-BOUND GTPASE DOMAIN OF RAB5A    
JRNL        TITL 2 FROM LEISHMANIA DONOVANI.                                    
JRNL        REF    ACTA CRYSTALLOGR.,SECT.F      V.  76   544 2020              
JRNL        REFN                   ESSN 2053-230X                               
JRNL        PMID   33135673                                                     
JRNL        DOI    10.1107/S2053230X20013722                                    
REMARK   2                                                                      
REMARK   2 RESOLUTION.    1.80 ANGSTROMS.                                       
REMARK   3                                                                      
REMARK   3 REFINEMENT.                                                          
REMARK   3   PROGRAM     : REFMAC 5.8.0257                                      
REMARK   3   AUTHORS     : MURSHUDOV,SKUBAK,LEBEDEV,PANNU,STEINER,              
REMARK   3               : NICHOLLS,WINN,LONG,VAGIN                             
REMARK   3                                                                      
REMARK   3    REFINEMENT TARGET : MAXIMUM LIKELIHOOD                            
REMARK   3                                                                      
REMARK   3  DATA USED IN REFINEMENT.                                            
REMARK   3   RESOLUTION RANGE HIGH (ANGSTROMS) : 1.80                           
REMARK   3   RESOLUTION RANGE LOW  (ANGSTROMS) : 24.42                          
REMARK   3   DATA CUTOFF            (SIGMA(F)) : 0.000                          
REMARK   3   COMPLETENESS FOR RANGE        (%) : 98.8                           
REMARK   3   NUMBER OF REFLECTIONS             : 18075                          
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) : 0.167                           
REMARK   3   R VALUE            (WORKING SET) : 0.165                           
REMARK   3   FREE R VALUE                     : 0.203                           
REMARK   3   FREE R VALUE TEST SET SIZE   (%) : 4.900                           
REMARK   3   FREE R VALUE TEST SET COUNT      : 938                             
REMARK   3                                                                      
REMARK   3  FIT IN THE HIGHEST RESOLUTION BIN.                                  
REMARK   3   TOTAL NUMBER OF BINS USED           : 20                           
REMARK   3   BIN RESOLUTION RANGE HIGH       (A) : 1.80                         
REMARK   3   BIN RESOLUTION RANGE LOW        (A) : 1.85                         
REMARK   3   REFLECTION IN BIN     (WORKING SET) : 1134                         
REMARK   3   BIN COMPLETENESS (WORKING+TEST) (%) : 85.66                        
REMARK   3   BIN R VALUE           (WORKING SET) : 0.3740                       
REMARK   3   BIN FREE R VALUE SET COUNT          : 55                           
REMARK   3   BIN FREE R VALUE                    : 0.3690                       
REMARK   3                                                                      
REMARK   3  NUMBER OF NON-HYDROGEN ATOMS USED IN REFINEMENT.                    
REMARK   3   PROTEIN ATOMS            : 1266                                    
REMARK   3   NUCLEIC ACID ATOMS       : 0                                       
REMARK   3   HETEROGEN ATOMS          : 39                                      
REMARK   3   SOLVENT ATOMS            : 124                                     
REMARK   3                                                                      
REMARK   3  B VALUES.                                                           
REMARK   3   FROM WILSON PLOT           (A**2) : NULL                           
REMARK   3   MEAN B VALUE      (OVERALL, A**2) : 35.10                          
REMARK   3   OVERALL ANISOTROPIC B VALUE.                                       
REMARK   3    B11 (A**2) : 0.71000                                              
REMARK   3    B22 (A**2) : 0.71000                                              
REMARK   3    B33 (A**2) : -2.29000                                             
REMARK   3    B12 (A**2) : 0.35000                                              
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): 0.104         
REMARK   3   ESU BASED ON FREE R VALUE                       (A): 0.106         
REMARK   3   ESU BASED ON MAXIMUM LIKELIHOOD                 (A): 0.079         
REMARK   3   ESU FOR B VALUES BASED ON MAXIMUM LIKELIHOOD (A**2): 5.151         
REMARK   3                                                                      
REMARK   3 CORRELATION COEFFICIENTS.                                            
REMARK   3   CORRELATION COEFFICIENT FO-FC      : 0.973                         
REMARK   3   CORRELATION COEFFICIENT FO-FC FREE : 0.960                         
REMARK   3                                                                      
REMARK   3  RMS DEVIATIONS FROM IDEAL VALUES        COUNT    RMS    WEIGHT      
REMARK   3   BOND LENGTHS REFINED ATOMS        (A):  1344 ; 0.017 ; 0.013       
REMARK   3   BOND LENGTHS OTHERS               (A):  1271 ; 0.001 ; 0.017       
REMARK   3   BOND ANGLES REFINED ATOMS   (DEGREES):  1827 ; 2.146 ; 1.665       
REMARK   3   BOND ANGLES OTHERS          (DEGREES):  2940 ; 1.537 ; 1.587       
REMARK   3   TORSION ANGLES, PERIOD 1    (DEGREES):   173 ; 7.658 ; 5.000       
REMARK   3   TORSION ANGLES, PERIOD 2    (DEGREES):    65 ;33.024 ;22.308       
REMARK   3   TORSION ANGLES, PERIOD 3    (DEGREES):   233 ;13.271 ;15.000       
REMARK   3   TORSION ANGLES, PERIOD 4    (DEGREES):     9 ;21.764 ;15.000       
REMARK   3   CHIRAL-CENTER RESTRAINTS       (A**3):   181 ; 0.094 ; 0.200       
REMARK   3   GENERAL PLANES REFINED ATOMS      (A):  1506 ; 0.012 ; 0.020       
REMARK   3   GENERAL PLANES OTHERS             (A):   285 ; 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):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   MAIN-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND REFINED ATOMS  (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN BOND OTHER ATOMS    (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE REFINED ATOMS (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SIDE-CHAIN ANGLE OTHER ATOMS   (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B REFINED ATOMS     (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   LONG RANGE B OTHER ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3 ANISOTROPIC THERMAL FACTOR RESTRAINTS.    COUNT   RMS   WEIGHT       
REMARK   3   RIGID-BOND RESTRAINTS          (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; FREE ATOMS         (A**2):  NULL ;  NULL ;  NULL       
REMARK   3   SPHERICITY; BONDED ATOMS       (A**2):  NULL ;  NULL ;  NULL       
REMARK   3                                                                      
REMARK   3  NCS RESTRAINTS STATISTICS                                           
REMARK   3   NUMBER OF DIFFERENT NCS GROUPS : NULL                              
REMARK   3                                                                      
REMARK   3  TLS DETAILS                                                         
REMARK   3   NUMBER OF TLS GROUPS  : 1                                          
REMARK   3                                                                      
REMARK   3   TLS GROUP : 1                                                      
REMARK   3    NUMBER OF COMPONENTS GROUP : 2                                    
REMARK   3    COMPONENTS        C SSSEQI   TO  C SSSEQI                         
REMARK   3    RESIDUE RANGE :   A    11        A   175                          
REMARK   3    RESIDUE RANGE :   A   201        A   203                          
REMARK   3    ORIGIN FOR THE GROUP (A):  -23.061   20.903  -13.316              
REMARK   3    T TENSOR                                                          
REMARK   3      T11:   0.0227 T22:   0.1200                                     
REMARK   3      T33:   0.0320 T12:   0.0131                                     
REMARK   3      T13:   0.0120 T23:  -0.0061                                     
REMARK   3    L TENSOR                                                          
REMARK   3      L11:   0.4433 L22:   0.4654                                     
REMARK   3      L33:   1.0121 L12:   0.0042                                     
REMARK   3      L13:  -0.5223 L23:   0.2046                                     
REMARK   3    S TENSOR                                                          
REMARK   3      S11:  -0.0259 S12:  -0.1163 S13:   0.0649                       
REMARK   3      S21:  -0.0290 S22:   0.0093 S23:   0.0454                       
REMARK   3      S31:   0.0942 S32:   0.1440 S33:   0.0166                       
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 U VALUES : WITH TLS ADDED                                 
REMARK   4                                                                      
REMARK   4 6L6O COMPLIES WITH FORMAT V. 3.30, 13-JUL-11                         
REMARK 100                                                                      
REMARK 100 THIS ENTRY HAS BEEN PROCESSED BY PDBJ ON 01-NOV-19.                  
REMARK 100 THE DEPOSITION ID IS D_1300013547.                                   
REMARK 200                                                                      
REMARK 200 EXPERIMENTAL DETAILS                                                 
REMARK 200  EXPERIMENT TYPE                : X-RAY DIFFRACTION                  
REMARK 200  DATE OF DATA COLLECTION        : 10-MAY-19                          
REMARK 200  TEMPERATURE           (KELVIN) : 100                                
REMARK 200  PH                             : 8.5                                
REMARK 200  NUMBER OF CRYSTALS USED        : 1                                  
REMARK 200                                                                      
REMARK 200  SYNCHROTRON              (Y/N) : N                                  
REMARK 200  RADIATION SOURCE               : ROTATING ANODE                     
REMARK 200  BEAMLINE                       : NULL                               
REMARK 200  X-RAY GENERATOR MODEL          : RIGAKU FR-E+ SUPERBRIGHT           
REMARK 200  MONOCHROMATIC OR LAUE    (M/L) : M                                  
REMARK 200  WAVELENGTH OR RANGE        (A) : 1.54178                            
REMARK 200  MONOCHROMATOR                  : NULL                               
REMARK 200  OPTICS                         : NULL                               
REMARK 200                                                                      
REMARK 200  DETECTOR TYPE                  : IMAGE PLATE                        
REMARK 200  DETECTOR MANUFACTURER          : RIGAKU RAXIS IV++                  
REMARK 200  INTENSITY-INTEGRATION SOFTWARE : HKL-2000                           
REMARK 200  DATA SCALING SOFTWARE          : HKL-2000                           
REMARK 200                                                                      
REMARK 200  NUMBER OF UNIQUE REFLECTIONS   : 19056                              
REMARK 200  RESOLUTION RANGE HIGH      (A) : 1.800                              
REMARK 200  RESOLUTION RANGE LOW       (A) : 35.000                             
REMARK 200  REJECTION CRITERIA  (SIGMA(I)) : NULL                               
REMARK 200                                                                      
REMARK 200 OVERALL.                                                             
REMARK 200  COMPLETENESS FOR RANGE     (%) : 98.9                               
REMARK 200  DATA REDUNDANCY                : 15.10                              
REMARK 200  R MERGE                    (I) : 0.05700                            
REMARK 200  R SYM                      (I) : NULL                               
REMARK 200   FOR THE DATA SET  : 16.0000                            
REMARK 200                                                                      
REMARK 200 IN THE HIGHEST RESOLUTION SHELL.                                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE HIGH (A) : 1.80                     
REMARK 200  HIGHEST RESOLUTION SHELL, RANGE LOW  (A) : 1.86                     
REMARK 200  COMPLETENESS FOR SHELL     (%) : 89.7                               
REMARK 200  DATA REDUNDANCY IN SHELL       : 8.80                               
REMARK 200  R MERGE FOR SHELL          (I) : 0.74800                            
REMARK 200  R SYM FOR SHELL            (I) : NULL                               
REMARK 200   FOR SHELL         : NULL                               
REMARK 200                                                                      
REMARK 200 DIFFRACTION PROTOCOL: SINGLE WAVELENGTH                              
REMARK 200 METHOD USED TO DETERMINE THE STRUCTURE: MOLECULAR REPLACEMENT        
REMARK 200 SOFTWARE USED: PHASER                                                
REMARK 200 STARTING MODEL: 2HEI                                                 
REMARK 200                                                                      
REMARK 200 REMARK: NULL                                                         
REMARK 280                                                                      
REMARK 280 CRYSTAL                                                              
REMARK 280 SOLVENT CONTENT, VS   (%): 55.80                                     
REMARK 280 MATTHEWS COEFFICIENT, VM (ANGSTROMS**3/DA): 2.78                     
REMARK 280                                                                      
REMARK 280 CRYSTALLIZATION CONDITIONS: 200MM AMMONIUM ACETATE, 100MM TRIS       
REMARK 280  HCL, PH 8.5 15% PEG 3350, VAPOR DIFFUSION, HANGING DROP,            
REMARK 280  TEMPERATURE 277K                                                    
REMARK 290                                                                      
REMARK 290 CRYSTALLOGRAPHIC SYMMETRY                                            
REMARK 290 SYMMETRY OPERATORS FOR SPACE GROUP: P 31 2 1                         
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   Y,X,-Z                                                  
REMARK 290       5555   X-Y,-Y,-Z+2/3                                           
REMARK 290       6555   -X,-X+Y,-Z+1/3                                          
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       34.47267            
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       68.94533            
REMARK 290   SMTRY1   4 -0.500000  0.866025  0.000000        0.00000            
REMARK 290   SMTRY2   4  0.866025  0.500000  0.000000        0.00000            
REMARK 290   SMTRY3   4  0.000000  0.000000 -1.000000        0.00000            
REMARK 290   SMTRY1   5  1.000000  0.000000  0.000000        0.00000            
REMARK 290   SMTRY2   5  0.000000 -1.000000  0.000000        0.00000            
REMARK 290   SMTRY3   5  0.000000  0.000000 -1.000000       68.94533            
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       34.47267            
REMARK 290                                                                      
REMARK 290 REMARK: NULL                                                         
REMARK 300                                                                      
REMARK 300 BIOMOLECULE: 1                                                       
REMARK 300 SEE REMARK 350 FOR THE AUTHOR PROVIDED AND/OR PROGRAM                
REMARK 300 GENERATED ASSEMBLY INFORMATION FOR THE STRUCTURE IN                  
REMARK 300 THIS ENTRY. THE REMARK MAY ALSO PROVIDE INFORMATION ON               
REMARK 300 BURIED SURFACE AREA.                                                 
REMARK 350                                                                      
REMARK 350 COORDINATES FOR A COMPLETE MULTIMER REPRESENTING THE KNOWN           
REMARK 350 BIOLOGICALLY SIGNIFICANT OLIGOMERIZATION STATE OF THE                
REMARK 350 MOLECULE CAN BE GENERATED BY APPLYING BIOMT TRANSFORMATIONS          
REMARK 350 GIVEN BELOW.  BOTH NON-CRYSTALLOGRAPHIC AND                          
REMARK 350 CRYSTALLOGRAPHIC OPERATIONS ARE GIVEN.                               
REMARK 350                                                                      
REMARK 350 BIOMOLECULE: 1                                                       
REMARK 350 AUTHOR DETERMINED BIOLOGICAL UNIT: MONOMERIC                         
REMARK 350 SOFTWARE DETERMINED QUATERNARY STRUCTURE: MONOMERIC                  
REMARK 350 SOFTWARE USED: PISA                                                  
REMARK 350 TOTAL BURIED SURFACE AREA: 900 ANGSTROM**2                           
REMARK 350 SURFACE AREA OF THE COMPLEX: 7880 ANGSTROM**2                        
REMARK 350 CHANGE IN SOLVENT FREE ENERGY: -19.0 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 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     GLY A    -1                                                      
REMARK 465     SER A     0                                                      
REMARK 465     MET A     1                                                      
REMARK 465     ASN A     2                                                      
REMARK 465     THR A     3                                                      
REMARK 465     HIS A     4                                                      
REMARK 465     PRO A     5                                                      
REMARK 465     PRO A     6                                                      
REMARK 465     GLN A     7                                                      
REMARK 465     LEU A     8                                                      
REMARK 465     MET A     9                                                      
REMARK 465     GLU A    10                                                      
REMARK 470                                                                      
REMARK 470 MISSING ATOM                                                         
REMARK 470 THE FOLLOWING RESIDUES HAVE MISSING ATOMS (M=MODEL NUMBER;           
REMARK 470 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE NUMBER;          
REMARK 470 I=INSERTION CODE):                                                   
REMARK 470   M RES CSSEQI  ATOMS                                                
REMARK 470     ASN A  41    OD1  ND2                                            
REMARK 470     ILE A  57    CD1                                                 
REMARK 470     LYS A 174    CD   CE   NZ                                        
REMARK 500                                                                      
REMARK 500 GEOMETRY AND STEREOCHEMISTRY                                         
REMARK 500 SUBTOPIC: COVALENT BOND LENGTHS                                      
REMARK 500                                                                      
REMARK 500 THE STEREOCHEMICAL PARAMETERS OF THE FOLLOWING RESIDUES              
REMARK 500 HAVE VALUES WHICH DEVIATE FROM EXPECTED VALUES BY MORE               
REMARK 500 THAN 6*RMSD (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN               
REMARK 500 IDENTIFIER; SSEQ=SEQUENCE NUMBER; I=INSERTION CODE).                 
REMARK 500                                                                      
REMARK 500 STANDARD TABLE:                                                      
REMARK 500 FORMAT: (10X,I3,1X,2(A3,1X,A1,I4,A1,1X,A4,3X),1X,F6.3)               
REMARK 500                                                                      
REMARK 500 EXPECTED VALUES PROTEIN: ENGH AND HUBER, 1999                        
REMARK 500 EXPECTED VALUES NUCLEIC ACID: CLOWNEY ET AL 1996                     
REMARK 500                                                                      
REMARK 500  M RES CSSEQI ATM1   RES CSSEQI ATM2   DEVIATION                     
REMARK 500    GLU A 110   CD    GLU A 110   OE2     0.084                       
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  41       49.12     38.03                                   
REMARK 500    ILE A  57     -165.32   -100.66                                   
REMARK 500    ALA A 173      -58.09    -26.09                                   
REMARK 500                                                                      
REMARK 500 REMARK: NULL                                                         
REMARK 525                                                                      
REMARK 525 SOLVENT                                                              
REMARK 525                                                                      
REMARK 525 THE SOLVENT MOLECULES HAVE CHAIN IDENTIFIERS THAT                    
REMARK 525 INDICATE THE POLYMER CHAIN WITH WHICH THEY ARE MOST                  
REMARK 525 CLOSELY ASSOCIATED. THE REMARK LISTS ALL THE SOLVENT                 
REMARK 525 MOLECULES WHICH ARE MORE THAN 5A AWAY FROM THE                       
REMARK 525 NEAREST POLYMER CHAIN (M = MODEL NUMBER;                             
REMARK 525 RES=RESIDUE NAME; C=CHAIN IDENTIFIER; SSEQ=SEQUENCE                  
REMARK 525 NUMBER; I=INSERTION CODE):                                           
REMARK 525                                                                      
REMARK 525  M RES CSSEQI                                                        
REMARK 525    HOH A 424        DISTANCE =  5.86 ANGSTROMS                       
REMARK 620                                                                      
REMARK 620 METAL COORDINATION                                                   
REMARK 620 (M=MODEL NUMBER; RES=RESIDUE NAME; C=CHAIN IDENTIFIER;               
REMARK 620 SSEQ=SEQUENCE NUMBER; I=INSERTION CODE):                             
REMARK 620                                                                      
REMARK 620 COORDINATION ANGLES FOR:  M RES CSSEQI METAL                         
REMARK 620                              MG A 204  MG                            
REMARK 620 N RES CSSEQI ATOM                                                    
REMARK 620 1 SER A  27   OG                                                     
REMARK 620 2 GDP A 201   O2B  89.6                                              
REMARK 620 N                    1                                               
DBREF1 6L6O A    1   175  UNP                  A0A109NYM0_LEIDO                 
DBREF2 6L6O A     A0A109NYM0                          1         195             
SEQADV 6L6O GLY A   -1  UNP  A0A109NYM           EXPRESSION TAG                 
SEQADV 6L6O SER A    0  UNP  A0A109NYM           EXPRESSION TAG                 
SEQADV 6L6O ASP A   58  UNP  A0A109NYM PRO    58 ENGINEERED MUTATION            
SEQADV 6L6O GLY A   59  UNP  A0A109NYM PRO    59 ENGINEERED MUTATION            
SEQADV 6L6O     A       UNP  A0A109NYM PRO    60 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ARG    61 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM GLY    62 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    63 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    64 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    65 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    66 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM PRO    67 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM GLY    68 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM GLY    69 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    70 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM THR    71 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM SER    72 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    73 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM HIS    74 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM ALA    75 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM LEU    76 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM GLN    77 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM GLN    78 DELETION                       
SEQADV 6L6O     A       UNP  A0A109NYM MET    79 DELETION                       
SEQADV 6L6O LEU A   72  UNP  A0A109NYM GLN    92 ENGINEERED MUTATION            
SEQADV 6L6O SER A   87  UNP  A0A109NYM CYS   107 ENGINEERED MUTATION            
SEQRES   1 A  177  GLY SER MET ASN THR HIS PRO PRO GLN LEU MET GLU ALA          
SEQRES   2 A  177  THR SER ALA LYS ILE VAL MET LEU GLY GLU SER GLY ALA          
SEQRES   3 A  177  GLY LYS SER SER ILE ALA LEU ARG PHE THR ARG ASN GLU          
SEQRES   4 A  177  PHE LEU ALA ASN GLN GLU THR THR ILE GLY ALA ALA PHE          
SEQRES   5 A  177  LEU SER LYS THR VAL MET ILE ASP GLY ARG ALA LEU LYS          
SEQRES   6 A  177  TYR GLU ILE TRP ASP THR ALA GLY LEU GLU ARG PHE ARG          
SEQRES   7 A  177  SER LEU ALA PRO ILE TYR TYR ARG GLY ALA SER GLY ALA          
SEQRES   8 A  177  LEU VAL VAL TYR ASP ILE THR ASN SER GLU SER LEU LYS          
SEQRES   9 A  177  LYS ALA GLN THR TRP ILE LYS GLU LEU ARG ALA ASN ALA          
SEQRES  10 A  177  ASP PRO SER LEU ILE ILE VAL LEU VAL GLY ASN LYS LYS          
SEQRES  11 A  177  ASP LEU GLY SER LEU ARG GLN VAL SER PHE GLU ASP GLY          
SEQRES  12 A  177  GLN ARG LEU ALA ALA GLU GLU GLN LEU ALA ALA PHE TYR          
SEQRES  13 A  177  GLU ALA SER ALA LYS ASP ASN ASN ASN VAL GLU GLN VAL          
SEQRES  14 A  177  PHE LEU ASP LEU ALA ALA LYS LEU                              
HET    GDP  A 201      28                                                       
HET    GOL  A 202       6                                                       
HET    ACT  A 203       4                                                       
HET     MG  A 204       1                                                       
HETNAM     GDP GUANOSINE-5'-DIPHOSPHATE                                         
HETNAM     GOL GLYCEROL                                                         
HETNAM     ACT ACETATE ION                                                      
HETNAM      MG MAGNESIUM ION                                                    
HETSYN     GOL GLYCERIN; PROPANE-1,2,3-TRIOL                                    
FORMUL   2  GDP    C10 H15 N5 O11 P2                                            
FORMUL   3  GOL    C3 H8 O3                                                     
FORMUL   4  ACT    C2 H3 O2 1-                                                  
FORMUL   5   MG    MG 2+                                                        
FORMUL   6  HOH   *124(H2 O)                                                    
HELIX    1 AA1 GLY A   25  ASN A   36  1                                  12    
HELIX    2 AA2 GLY A   71  ARG A   76  5                                   6    
HELIX    3 AA3 ALA A   79  ARG A   84  1                                   6    
HELIX    4 AA4 ASN A   97  ALA A  115  1                                  19    
HELIX    5 AA5 LEU A  130  ARG A  134  5                                   5    
HELIX    6 AA6 SER A  137  GLU A  148  1                                  12    
HELIX    7 AA7 ASN A  163  LEU A  175  1                                  13    
SHEET    1 AA1 6 PHE A  50  MET A  56  0                                        
SHEET    2 AA1 6 ALA A  61  TRP A  67 -1  O  TYR A  64   N  LYS A  53           
SHEET    3 AA1 6 THR A  12  GLY A  20  1  N  ALA A  14   O  GLU A  65           
SHEET    4 AA1 6 GLY A  88  ASP A  94  1  O  LEU A  90   N  LEU A  19           
SHEET    5 AA1 6 ILE A 120  ASN A 126  1  O  ASN A 126   N  TYR A  93           
SHEET    6 AA1 6 ALA A 152  GLU A 155  1  O  TYR A 154   N  GLY A 125           
LINK         OG  SER A  27                MG    MG A 204     1555   1555  2.05  
LINK         O2B GDP A 201                MG    MG A 204     1555   1555  2.05  
CRYST1   58.018   58.018  103.418  90.00  90.00 120.00 P 31 2 1      6          
ORIGX1      1.000000  0.000000  0.000000        0.00000                         
ORIGX2      0.000000  1.000000  0.000000        0.00000                         
ORIGX3      0.000000  0.000000  1.000000        0.00000                         
SCALE1      0.017236  0.009951  0.000000        0.00000                         
SCALE2      0.000000  0.019902  0.000000        0.00000                         
SCALE3      0.000000  0.000000  0.009669        0.00000                         
ATOM      1  N   ALA A  11     -15.280  22.585   9.211  1.00 69.20           N  
ANISOU    1  N   ALA A  11     7760  11070   7459    358     89   -448       N  
ATOM      2  CA  ALA A  11     -15.592  22.751   7.745  1.00 61.89           C  
ANISOU    2  CA  ALA A  11     6859  10016   6641    325    102   -435       C  
ATOM      3  C   ALA A  11     -16.487  23.981   7.549  1.00 64.49           C  
ANISOU    3  C   ALA A  11     7190  10244   7068    206    129   -495       C  
ATOM      4  O   ALA A  11     -17.564  23.993   8.160  1.00 64.83           O  
ANISOU    4  O   ALA A  11     7284  10214   7133    186    153   -494       O  
ATOM      5  CB  ALA A  11     -16.289  21.525   7.204  1.00 58.34           C  
ANISOU    5  CB  ALA A  11     6504   9448   6215    401    118   -348       C  
ATOM      6  N   THR A  12     -16.116  24.940   6.682  1.00 59.34           N  
ANISOU    6  N   THR A  12     6493   9576   6476    133    130   -542       N  
ATOM      7  CA  THR A  12     -17.068  25.968   6.188  1.00 51.16           C  
ANISOU    7  CA  THR A  12     5480   8411   5546     40    162   -580       C  
ATOM      8  C   THR A  12     -17.825  25.276   5.051  1.00 45.01           C  
ANISOU    8  C   THR A  12     4772   7492   4837     77    168   -512       C  
ATOM      9  O   THR A  12     -17.237  24.450   4.405  1.00 43.69           O  
ANISOU    9  O   THR A  12     4610   7342   4646    143    150   -464       O  
ATOM     10  CB  THR A  12     -16.385  27.298   5.820  1.00 56.17           C  
ANISOU   10  CB  THR A  12     6049   9083   6209    -53    169   -658       C  
ATOM     11  OG1 THR A  12     -15.611  27.171   4.639  1.00 55.28           O  
ANISOU   11  OG1 THR A  12     5916   8974   6113    -36    156   -641       O  
ATOM     12  CG2 THR A  12     -15.451  27.828   6.892  1.00 60.47           C  
ANISOU   12  CG2 THR A  12     6515   9790   6669    -87    159   -728       C  
ATOM     13  N   SER A  13     -19.069  25.647   4.825  1.00 43.55           N  
ANISOU   13  N   SER A  13     4633   7178   4734     35    194   -513       N  
ATOM     14  CA  SER A  13     -19.964  24.993   3.830  1.00 41.21           C  
ANISOU   14  CA  SER A  13     4403   6750   4502     63    200   -454       C  
ATOM     15  C   SER A  13     -20.205  25.947   2.663  1.00 40.20           C  
ANISOU   15  C   SER A  13     4270   6537   4465      2    209   -477       C  
ATOM     16  O   SER A  13     -20.396  27.138   2.927  1.00 39.97           O  
ANISOU   16  O   SER A  13     4216   6499   4471    -70    227   -535       O  
ATOM     17  CB  SER A  13     -21.248  24.618   4.456  1.00 43.77           C  
ANISOU   17  CB  SER A  13     4782   7000   4847     67    223   -437       C  
ATOM     18  OG  SER A  13     -21.083  23.487   5.289  1.00 42.59           O  
ANISOU   18  OG  SER A  13     4659   6905   4615    139    220   -396       O  
ATOM     19  N   ALA A  14     -20.315  25.410   1.448  1.00 35.96           N  
ANISOU   19  N   ALA A  14     3767   5932   3965     32    200   -430       N  
ATOM     20  CA  ALA A  14     -20.743  26.135   0.224  1.00 32.76           C  
ANISOU   20  CA  ALA A  14     3372   5428   3644    -11    207   -435       C  
ATOM     21  C   ALA A  14     -21.822  25.275  -0.466  1.00 32.66           C  
ANISOU   21  C   ALA A  14     3423   5309   3674     22    207   -379       C  
ATOM     22  O   ALA A  14     -21.579  24.065  -0.745  1.00 31.64           O  
ANISOU   22  O   ALA A  14     3325   5188   3508     85    196   -328       O  
ATOM     23  CB  ALA A  14     -19.572  26.390  -0.693  1.00 33.79           C  
ANISOU   23  CB  ALA A  14     3471   5600   3766    -15    194   -442       C  
ATOM     24  N   LYS A  15     -22.981  25.888  -0.696  1.00 30.67           N  
ANISOU   24  N   LYS A  15     3190   4965   3496    -17    222   -390       N  
ATOM     25  CA  LYS A  15     -24.042  25.343  -1.537  1.00 28.09           C  
ANISOU   25  CA  LYS A  15     2911   4539   3221     -2    220   -350       C  
ATOM     26  C   LYS A  15     -23.643  25.512  -3.020  1.00 28.25           C  
ANISOU   26  C   LYS A  15     2938   4523   3273     -3    205   -332       C  
ATOM     27  O   LYS A  15     -23.362  26.640  -3.509  1.00 28.54           O  
ANISOU   27  O   LYS A  15     2952   4548   3344    -44    209   -362       O  
ATOM     28  CB  LYS A  15     -25.341  26.087  -1.274  1.00 27.24           C  
ANISOU   28  CB  LYS A  15     2807   4360   3179    -44    240   -374       C  
ATOM     29  CG  LYS A  15     -26.470  25.663  -2.198  1.00 26.05           C  
ANISOU   29  CG  LYS A  15     2694   4118   3086    -35    235   -341       C  
ATOM     30  CD  LYS A  15     -27.763  26.266  -1.864  1.00 26.52           C  
ANISOU   30  CD  LYS A  15     2751   4120   3205    -65    254   -363       C  
ATOM     31  CE  LYS A  15     -28.806  26.033  -2.964  1.00 26.34           C  
ANISOU   31  CE  LYS A  15     2749   4017   3239    -60    243   -336       C  
ATOM     32  NZ  LYS A  15     -30.123  26.488  -2.552  1.00 26.62           N  
ANISOU   32  NZ  LYS A  15     2776   4007   3329    -81    261   -355       N  
ATOM     33  N   ILE A  16     -23.646  24.398  -3.701  1.00 28.12           N  
ANISOU   33  N   ILE A  16     2957   4484   3240     41    193   -284       N  
ATOM     34  CA  ILE A  16     -23.321  24.344  -5.142  1.00 28.75           C  
ANISOU   34  CA  ILE A  16     3053   4527   3343     46    179   -260       C  
ATOM     35  C   ILE A  16     -24.523  23.655  -5.801  1.00 27.77           C  
ANISOU   35  C   ILE A  16     2976   4317   3257     56    176   -227       C  
ATOM     36  O   ILE A  16     -24.866  22.520  -5.427  1.00 29.11           O  
ANISOU   36  O   ILE A  16     3179   4483   3398     88    183   -200       O  
ATOM     37  CB  ILE A  16     -22.029  23.548  -5.390  1.00 28.78           C  
ANISOU   37  CB  ILE A  16     3054   4597   3284     93    169   -236       C  
ATOM     38  CG1 ILE A  16     -20.808  24.009  -4.573  1.00 32.22           C  
ANISOU   38  CG1 ILE A  16     3432   5141   3666     90    169   -271       C  
ATOM     39  CG2 ILE A  16     -21.753  23.438  -6.909  1.00 28.69           C  
ANISOU   39  CG2 ILE A  16     3065   4541   3295     97    158   -211       C  
ATOM     40  CD1 ILE A  16     -20.340  25.377  -4.931  1.00 34.80           C  
ANISOU   40  CD1 ILE A  16     3719   5477   4025     31    174   -317       C  
ATOM     41  N   VAL A  17     -25.075  24.242  -6.854  1.00 26.45           N  
ANISOU   41  N   VAL A  17     2817   4087   3147     31    168   -225       N  
ATOM     42  CA  VAL A  17     -26.274  23.674  -7.541  1.00 25.00           C  
ANISOU   42  CA  VAL A  17     2668   3830   2999     34    161   -201       C  
ATOM     43  C   VAL A  17     -25.880  23.095  -8.895  1.00 25.30           C  
ANISOU   43  C   VAL A  17     2737   3845   3029     52    145   -167       C  
ATOM     44  O   VAL A  17     -25.057  23.715  -9.602  1.00 25.52           O  
ANISOU   44  O   VAL A  17     2754   3884   3058     46    137   -170       O  
ATOM     45  CB  VAL A  17     -27.421  24.665  -7.675  1.00 25.84           C  
ANISOU   45  CB  VAL A  17     2760   3885   3172      0    161   -221       C  
ATOM     46  CG1 VAL A  17     -27.926  25.073  -6.257  1.00 25.51           C  
ANISOU   46  CG1 VAL A  17     2693   3860   3136    -16    184   -254       C  
ATOM     47  CG2 VAL A  17     -27.102  25.890  -8.486  1.00 24.83           C  
ANISOU   47  CG2 VAL A  17     2618   3737   3079    -19    155   -233       C  
ATOM     48  N   MET A  18     -26.477  21.955  -9.209  1.00 23.43           N  
ANISOU   48  N   MET A  18     2541   3577   2784     69    146   -140       N  
ATOM     49  CA  MET A  18     -26.362  21.362 -10.534  1.00 24.74           C  
ANISOU   49  CA  MET A  18     2742   3710   2947     79    134   -112       C  
ATOM     50  C   MET A  18     -27.495  21.900 -11.430  1.00 26.46           C  
ANISOU   50  C   MET A  18     2960   3871   3221     50    115   -116       C  
ATOM     51  O   MET A  18     -28.702  21.807 -11.067  1.00 25.29           O  
ANISOU   51  O   MET A  18     2808   3698   3102     34    118   -126       O  
ATOM     52  CB  MET A  18     -26.459  19.833 -10.424  1.00 25.47           C  
ANISOU   52  CB  MET A  18     2884   3794   2999    107    151    -85       C  
ATOM     53  CG  MET A  18     -25.437  19.153  -9.542  1.00 25.81           C  
ANISOU   53  CG  MET A  18     2934   3892   2980    151    170    -72       C  
ATOM     54  SD  MET A  18     -23.752  19.588  -9.858  1.00 27.70           S  
ANISOU   54  SD  MET A  18     3143   4195   3184    177    160    -70       S  
ATOM     55  CE  MET A  18     -23.557  18.900 -11.500  1.00 28.61           C  
ANISOU   55  CE  MET A  18     3308   4263   3300    186    154    -38       C  
ATOM     56  N   LEU A  19     -27.177  22.252 -12.683  1.00 26.33           N  
ANISOU   56  N   LEU A  19     2954   3835   3214     47     97   -103       N  
ATOM     57  CA  LEU A  19     -28.169  22.789 -13.629  1.00 24.53           C  
ANISOU   57  CA  LEU A  19     2726   3562   3032     29     74   -102       C  
ATOM     58  C   LEU A  19     -27.831  22.265 -15.021  1.00 23.74           C  
ANISOU   58  C   LEU A  19     2664   3443   2913     36     59    -76       C  
ATOM     59  O   LEU A  19     -26.721  21.743 -15.222  1.00 23.73           O  
ANISOU   59  O   LEU A  19     2682   3461   2871     54     69    -62       O  
ATOM     60  CB  LEU A  19     -28.105  24.327 -13.678  1.00 26.91           C  
ANISOU   60  CB  LEU A  19     2997   3857   3371     16     71   -119       C  
ATOM     61  CG  LEU A  19     -28.553  25.043 -12.424  1.00 31.07           C  
ANISOU   61  CG  LEU A  19     3487   4394   3923      3     88   -149       C  
ATOM     62  CD1 LEU A  19     -28.247  26.507 -12.552  1.00 36.17           C  
ANISOU   62  CD1 LEU A  19     4115   5028   4597     -9     95   -166       C  
ATOM     63  CD2 LEU A  19     -30.022  24.833 -12.212  1.00 33.46           C  
ANISOU   63  CD2 LEU A  19     3781   4672   4260     -2     82   -154       C  
ATOM     64  N   GLY A  20     -28.821  22.383 -15.910  1.00 23.11           N  
ANISOU   64  N   GLY A  20     2591   3329   2860     25     36    -70       N  
ATOM     65  CA  GLY A  20     -28.672  21.853 -17.279  1.00 23.92           C  
ANISOU   65  CA  GLY A  20     2732   3412   2942     26     19    -48       C  
ATOM     66  C   GLY A  20     -29.831  20.950 -17.658  1.00 23.70           C  
ANISOU   66  C   GLY A  20     2720   3367   2917     11      8    -48       C  
ATOM     67  O   GLY A  20     -30.635  20.485 -16.825  1.00 25.37           O  
ANISOU   67  O   GLY A  20     2919   3581   3138      0     21    -64       O  
ATOM     68  N   GLU A  21     -29.945  20.675 -18.931  1.00 24.54           N  
ANISOU   68  N   GLU A  21     2855   3457   3011      6    -11    -34       N  
ATOM     69  CA  GLU A  21     -31.024  19.846 -19.504  1.00 24.83           C  
ANISOU   69  CA  GLU A  21     2905   3483   3044    -17    -24    -40       C  
ATOM     70  C   GLU A  21     -31.011  18.454 -18.940  1.00 24.88           C  
ANISOU   70  C   GLU A  21     2945   3486   3022    -26     11    -46       C  
ATOM     71  O   GLU A  21     -29.921  17.907 -18.643  1.00 24.33           O  
ANISOU   71  O   GLU A  21     2907   3418   2918     -5     40    -31       O  
ATOM     72  CB  GLU A  21     -30.864  19.661 -21.008  1.00 29.78           C  
ANISOU   72  CB  GLU A  21     3567   4098   3648    -21    -47    -24       C  
ATOM     73  CG  GLU A  21     -31.305  20.870 -21.745  1.00 36.62           C  
ANISOU   73  CG  GLU A  21     4408   4964   4540    -14    -86    -17       C  
ATOM     74  CD  GLU A  21     -32.745  21.290 -21.487  1.00 36.56           C  
ANISOU   74  CD  GLU A  21     4351   4968   4571    -22   -111    -35       C  
ATOM     75  OE1 GLU A  21     -33.597  20.726 -22.187  0.70 34.60           O  
ANISOU   75  OE1 GLU A  21     4104   4728   4312    -43   -133    -43       O  
ATOM     76  OE2 GLU A  21     -33.014  22.134 -20.584  1.00 36.39           O  
ANISOU   76  OE2 GLU A  21     4289   4950   4587    -11   -105    -45       O  
ATOM     77  N   SER A  22     -32.201  17.883 -18.849  1.00 25.40           N  
ANISOU   77  N   SER A  22     3004   3547   3097    -57     12    -66       N  
ATOM     78  CA  SER A  22     -32.397  16.445 -18.555  1.00 26.60           C  
ANISOU   78  CA  SER A  22     3202   3684   3221    -77     52    -74       C  
ATOM     79  C   SER A  22     -31.432  15.620 -19.378  1.00 26.96           C  
ANISOU   79  C   SER A  22     3311   3711   3219    -67     69    -52       C  
ATOM     80  O   SER A  22     -31.363  15.844 -20.631  1.00 27.61           O  
ANISOU   80  O   SER A  22     3404   3791   3295    -74     38    -45       O  
ATOM     81  CB  SER A  22     -33.847  15.994 -18.834  1.00 31.24           C  
ANISOU   81  CB  SER A  22     3776   4270   3823   -126     45   -105       C  
ATOM     82  OG  SER A  22     -34.805  16.706 -18.021  1.00 34.68           O  
ANISOU   82  OG  SER A  22     4149   4724   4304   -134     34   -127       O  
ATOM     83  N   GLY A  23     -30.782  14.636 -18.788  1.00 26.26           N  
ANISOU   83  N   GLY A  23     3270   3609   3097    -49    117    -41       N  
ATOM     84  CA  GLY A  23     -29.923  13.694 -19.518  1.00 27.33           C  
ANISOU   84  CA  GLY A  23     3473   3722   3188    -36    143    -21       C  
ATOM     85  C   GLY A  23     -28.492  14.142 -19.717  1.00 26.94           C  
ANISOU   85  C   GLY A  23     3425   3689   3121     11    138      6       C  
ATOM     86  O   GLY A  23     -27.682  13.350 -20.240  1.00 29.66           O  
ANISOU   86  O   GLY A  23     3823   4018   3427     31    165     25       O  
ATOM     87  N   ALA A  24     -28.149  15.350 -19.334  1.00 27.07           N  
ANISOU   87  N   ALA A  24     3386   3736   3163     28    111      7       N  
ATOM     88  CA  ALA A  24     -26.796  15.888 -19.567  1.00 27.08           C  
ANISOU   88  CA  ALA A  24     3379   3758   3149     63    107     26       C  
ATOM     89  C   ALA A  24     -25.745  15.173 -18.697  1.00 26.46           C  
ANISOU   89  C   ALA A  24     3320   3700   3033    110    147     42       C  
ATOM     90  O   ALA A  24     -24.593  15.078 -19.147  1.00 26.10           O  
ANISOU   90  O   ALA A  24     3288   3667   2961    140    156     59       O  
ATOM     91  CB  ALA A  24     -26.814  17.344 -19.312  1.00 26.26           C  
ANISOU   91  CB  ALA A  24     3216   3679   3083     60     76     15       C  
ATOM     92  N   GLY A  25     -26.135  14.678 -17.508  1.00 25.83           N  
ANISOU   92  N   GLY A  25     3241   3624   2947    118    172     37       N  
ATOM     93  CA  GLY A  25     -25.182  14.075 -16.564  1.00 26.67           C  
ANISOU   93  CA  GLY A  25     3361   3757   3013    172    207     55       C  
ATOM     94  C   GLY A  25     -25.043  14.847 -15.251  1.00 26.74           C  
ANISOU   94  C   GLY A  25     3312   3814   3032    185    199     43       C  
ATOM     95  O   GLY A  25     -24.098  14.599 -14.568  1.00 25.36           O  
ANISOU   95  O   GLY A  25     3134   3679   2821    233    216     57       O  
ATOM     96  N   LYS A  26     -25.999  15.663 -14.856  1.00 24.00           N  
ANISOU   96  N   LYS A  26     2924   3465   2728    147    178     18       N  
ATOM     97  CA  LYS A  26     -25.942  16.424 -13.572  1.00 24.47           C  
ANISOU   97  CA  LYS A  26     2932   3567   2797    153    175      1       C  
ATOM     98  C   LYS A  26     -25.751  15.415 -12.429  1.00 25.54           C  
ANISOU   98  C   LYS A  26     3099   3716   2889    191    214     15       C  
ATOM     99  O   LYS A  26     -24.923  15.672 -11.526  1.00 25.42           O  
ANISOU   99  O   LYS A  26     3055   3756   2845    225    217     17       O  
ATOM    100  CB  LYS A  26     -27.223  17.235 -13.395  1.00 24.09           C  
ANISOU  100  CB  LYS A  26     2848   3500   2804    107    155    -26       C  
ATOM    101  CG  LYS A  26     -27.387  18.373 -14.413  1.00 24.27           C  
ANISOU  101  CG  LYS A  26     2840   3513   2867     81    118    -35       C  
ATOM    102  CD  LYS A  26     -28.659  19.216 -14.215  1.00 23.52           C  
ANISOU  102  CD  LYS A  26     2707   3403   2826     47    100    -60       C  
ATOM    103  CE  LYS A  26     -29.914  18.442 -14.346  1.00 22.88           C  
ANISOU  103  CE  LYS A  26     2644   3291   2756     22    105    -67       C  
ATOM    104  NZ  LYS A  26     -30.034  17.725 -15.625  1.00 22.79           N  
ANISOU  104  NZ  LYS A  26     2674   3254   2730     12     96    -54       N  
ATOM    105  N   SER A  27     -26.690  14.504 -12.342  1.00 26.41           N  
ANISOU  105  N   SER A  27     3255   3779   2997    174    241     16       N  
ATOM    106  CA  SER A  27     -26.743  13.538 -11.213  1.00 28.54           C  
ANISOU  106  CA  SER A  27     3566   4048   3228    205    286     29       C  
ATOM    107  C   SER A  27     -25.432  12.720 -11.196  1.00 29.88           C  
ANISOU  107  C   SER A  27     3775   4240   3336    275    310     66       C  
ATOM    108  O   SER A  27     -24.834  12.504 -10.106  1.00 29.27           O  
ANISOU  108  O   SER A  27     3697   4207   3217    326    327     81       O  
ATOM    109  CB  SER A  27     -27.967  12.700 -11.343  1.00 27.63           C  
ANISOU  109  CB  SER A  27     3500   3872   3126    164    317     19       C  
ATOM    110  OG  SER A  27     -29.155  13.486 -11.166  1.00 26.93           O  
ANISOU  110  OG  SER A  27     3362   3776   3091    108    295    -16       O  
ATOM    111  N   SER A  28     -24.929  12.349 -12.367  1.00 28.56           N  
ANISOU  111  N   SER A  28     3638   4053   3161    284    310     82       N  
ATOM    112  CA  SER A  28     -23.751  11.461 -12.481  1.00 28.17           C  
ANISOU  112  CA  SER A  28     3632   4016   3054    354    339    120       C  
ATOM    113  C   SER A  28     -22.512  12.281 -12.085  1.00 30.13           C  
ANISOU  113  C   SER A  28     3811   4351   3285    396    310    122       C  
ATOM    114  O   SER A  28     -21.607  11.729 -11.457  1.00 31.18           O  
ANISOU  114  O   SER A  28     3954   4526   3364    467    331    148       O  
ATOM    115  CB  SER A  28     -23.649  10.849 -13.883  1.00 28.50           C  
ANISOU  115  CB  SER A  28     3725   4006   3094    343    350    131       C  
ATOM    116  OG  SER A  28     -24.725   9.988 -14.211  1.00 26.93           O  
ANISOU  116  OG  SER A  28     3592   3734   2903    302    384    124       O  
ATOM    117  N   ILE A  29     -22.416  13.550 -12.466  1.00 25.41           N  
ANISOU  117  N   ILE A  29     3146   3781   2726    356    266     94       N  
ATOM    118  CA  ILE A  29     -21.285  14.377 -12.000  1.00 28.05           C  
ANISOU  118  CA  ILE A  29     3412   4201   3045    383    244     86       C  
ATOM    119  C   ILE A  29     -21.317  14.462 -10.448  1.00 31.09           C  
ANISOU  119  C   ILE A  29     3770   4637   3404    406    250     80       C  
ATOM    120  O   ILE A  29     -20.268  14.301  -9.830  1.00 29.23           O  
ANISOU  120  O   ILE A  29     3511   4475   3118    464    254     92       O  
ATOM    121  CB  ILE A  29     -21.283  15.728 -12.705  1.00 26.16           C  
ANISOU  121  CB  ILE A  29     3117   3966   2854    328    207     56       C  
ATOM    122  CG1 ILE A  29     -20.971  15.494 -14.193  1.00 28.57           C  
ANISOU  122  CG1 ILE A  29     3454   4233   3165    322    205     70       C  
ATOM    123  CG2 ILE A  29     -20.348  16.740 -12.063  1.00 29.22           C  
ANISOU  123  CG2 ILE A  29     3430   4439   3233    333    189     33       C  
ATOM    124  CD1 ILE A  29     -21.091  16.733 -14.990  1.00 30.75           C  
ANISOU  124  CD1 ILE A  29     3694   4500   3488    270    174     46       C  
ATOM    125  N   ALA A  30     -22.458  14.778  -9.887  1.00 29.31           N  
ANISOU  125  N   ALA A  30     3542   4382   3212    362    249     59       N  
ATOM    126  CA  ALA A  30     -22.579  15.009  -8.423  1.00 31.04           C  
ANISOU  126  CA  ALA A  30     3734   4648   3411    373    254     46       C  
ATOM    127  C   ALA A  30     -22.175  13.695  -7.756  1.00 32.17           C  
ANISOU  127  C   ALA A  30     3934   4802   3486    447    292     87       C  
ATOM    128  O   ALA A  30     -21.450  13.725  -6.735  1.00 34.57           O  
ANISOU  128  O   ALA A  30     4211   5183   3740    495    292     92       O  
ATOM    129  CB  ALA A  30     -24.003  15.427  -8.067  1.00 29.50           C  
ANISOU  129  CB  ALA A  30     3535   4404   3266    312    254     19       C  
ATOM    130  N   LEU A  31     -22.662  12.584  -8.279  1.00 30.65           N  
ANISOU  130  N   LEU A  31     3821   4535   3288    455    328    112       N  
ATOM    131  CA  LEU A  31     -22.464  11.279  -7.606  1.00 33.43           C  
ANISOU  131  CA  LEU A  31     4246   4878   3578    525    377    153       C  
ATOM    132  C   LEU A  31     -21.036  10.775  -7.807  1.00 35.88           C  
ANISOU  132  C   LEU A  31     4560   5241   3830    611    382    190       C  
ATOM    133  O   LEU A  31     -20.421  10.216  -6.853  1.00 36.94           O  
ANISOU  133  O   LEU A  31     4710   5426   3900    690    402    219       O  
ATOM    134  CB  LEU A  31     -23.473  10.285  -8.154  1.00 35.54           C  
ANISOU  134  CB  LEU A  31     4600   5040   3860    495    421    162       C  
ATOM    135  CG  LEU A  31     -23.419   8.907  -7.510  1.00 42.45           C  
ANISOU  135  CG  LEU A  31     5569   5884   4675    558    486    203       C  
ATOM    136  CD1 LEU A  31     -24.110   8.936  -6.124  1.00 46.16           C  
ANISOU  136  CD1 LEU A  31     6043   6361   5132    552    505    194       C  
ATOM    137  CD2 LEU A  31     -24.054   7.824  -8.396  1.00 44.02           C  
ANISOU  137  CD2 LEU A  31     5861   5981   4883    533    537    212       C  
ATOM    138  N   ARG A  32     -20.437  11.077  -8.934  1.00 31.65           N  
ANISOU  138  N   ARG A  32     4001   4710   3313    603    361    186       N  
ATOM    139  CA  ARG A  32     -19.002  10.789  -9.126  1.00 33.56           C  
ANISOU  139  CA  ARG A  32     4226   5018   3505    682    360    214       C  
ATOM    140  C   ARG A  32     -18.178  11.584  -8.121  1.00 35.02           C  
ANISOU  140  C   ARG A  32     4323   5322   3659    710    327    198       C  
ATOM    141  O   ARG A  32     -17.293  10.971  -7.494  1.00 34.12           O  
ANISOU  141  O   ARG A  32     4212   5274   3478    800    341    230       O  
ATOM    142  CB  ARG A  32     -18.559  10.979 -10.573  1.00 31.24           C  
ANISOU  142  CB  ARG A  32     3927   4702   3239    660    348    210       C  
ATOM    143  CG  ARG A  32     -17.075  10.833 -10.806  1.00 32.38           C  
ANISOU  143  CG  ARG A  32     4040   4923   3340    733    346    230       C  
ATOM    144  CD  ARG A  32     -16.654   9.418 -10.554  1.00 34.43           C  
ANISOU  144  CD  ARG A  32     4375   5168   3537    830    397    283       C  
ATOM    145  NE  ARG A  32     -16.957   8.529 -11.639  1.00 34.18           N  
ANISOU  145  NE  ARG A  32     4431   5038   3516    825    437    303       N  
ATOM    146  CZ  ARG A  32     -16.718   7.227 -11.619  1.00 39.94           C  
ANISOU  146  CZ  ARG A  32     5247   5727   4199    900    494    349       C  
ATOM    147  NH1 ARG A  32     -17.021   6.481 -12.659  1.00 41.94           N  
ANISOU  147  NH1 ARG A  32     5581   5888   4465    883    533    360       N  
ATOM    148  NH2 ARG A  32     -16.224   6.663 -10.516  1.00 41.50           N  
ANISOU  148  NH2 ARG A  32     5457   5976   4335    994    516    384       N  
ATOM    149  N   PHE A  33     -18.412  12.869  -7.953  1.00 32.48           N  
ANISOU  149  N   PHE A  33     3927   5032   3379    641    288    151       N  
ATOM    150  CA  PHE A  33     -17.549  13.664  -7.073  1.00 30.87           C  
ANISOU  150  CA  PHE A  33     3636   4947   3144    658    259    127       C  
ATOM    151  C   PHE A  33     -17.744  13.194  -5.632  1.00 35.45           C  
ANISOU  151  C   PHE A  33     4233   5565   3671    705    274    143       C  
ATOM    152  O   PHE A  33     -16.772  13.090  -4.900  1.00 34.42           O  
ANISOU  152  O   PHE A  33     4063   5537   3476    771    266    152       O  
ATOM    153  CB  PHE A  33     -17.887  15.128  -7.183  1.00 32.03           C  
ANISOU  153  CB  PHE A  33     3715   5103   3350    567    226     72       C  
ATOM    154  CG  PHE A  33     -17.140  16.008  -6.210  1.00 32.25           C  
ANISOU  154  CG  PHE A  33     3656   5247   3349    565    202     36       C  
ATOM    155  CD1 PHE A  33     -15.757  16.050  -6.195  1.00 35.64           C  
ANISOU  155  CD1 PHE A  33     4029   5781   3729    613    190     36       C  
ATOM    156  CD2 PHE A  33     -17.842  16.789  -5.328  1.00 33.25           C  
ANISOU  156  CD2 PHE A  33     3755   5379   3496    513    193      0       C  
ATOM    157  CE1 PHE A  33     -15.078  16.875  -5.325  1.00 35.01           C  
ANISOU  157  CE1 PHE A  33     3864   5816   3620    602    168     -4       C  
ATOM    158  CE2 PHE A  33     -17.161  17.588  -4.437  1.00 37.03           C  
ANISOU  158  CE2 PHE A  33     4158   5966   3945    505    175    -37       C  
ATOM    159  CZ  PHE A  33     -15.799  17.662  -4.478  1.00 36.74           C  
ANISOU  159  CZ  PHE A  33     4063   6036   3861    543    161    -42       C  
ATOM    160  N   THR A  34     -18.985  13.019  -5.217  1.00 33.61           N  
ANISOU  160  N   THR A  34     4047   5257   3464    666    294    139       N  
ATOM    161  CA  THR A  34     -19.263  12.823  -3.783  1.00 35.70           C  
ANISOU  161  CA  THR A  34     4321   5559   3685    694    306    143       C  
ATOM    162  C   THR A  34     -18.987  11.386  -3.376  1.00 39.80           C  
ANISOU  162  C   THR A  34     4922   6067   4132    792    350    204       C  
ATOM    163  O   THR A  34     -18.572  11.218  -2.219  1.00 41.81           O  
ANISOU  163  O   THR A  34     5166   6398   4321    851    352    217       O  
ATOM    164  CB  THR A  34     -20.663  13.276  -3.369  1.00 34.48           C  
ANISOU  164  CB  THR A  34     4178   5338   3582    614    313    112       C  
ATOM    165  OG1 THR A  34     -21.626  12.490  -4.049  1.00 32.29           O  
ANISOU  165  OG1 THR A  34     3981   4947   3339    591    348    129       O  
ATOM    166  CG2 THR A  34     -20.826  14.773  -3.531  1.00 36.48           C  
ANISOU  166  CG2 THR A  34     4348   5616   3896    532    273     55       C  
ATOM    167  N   ARG A  35     -19.303  10.397  -4.195  1.00 38.37           N  
ANISOU  167  N   ARG A  35     4826   5792   3960    807    390    237       N  
ATOM    168  CA  ARG A  35     -19.297   8.986  -3.771  1.00 43.65           C  
ANISOU  168  CA  ARG A  35     5595   6421   4567    892    448    293       C  
ATOM    169  C   ARG A  35     -18.274   8.213  -4.600  1.00 44.34           C  
ANISOU  169  C   ARG A  35     5712   6513   4621    971    464    335       C  
ATOM    170  O   ARG A  35     -18.113   7.032  -4.351  1.00 42.61           O  
ANISOU  170  O   ARG A  35     5579   6262   4347   1052    517    387       O  
ATOM    171  CB  ARG A  35     -20.710   8.428  -3.892  1.00 46.42           C  
ANISOU  171  CB  ARG A  35     6033   6647   4957    831    495    290       C  
ATOM    172  CG  ARG A  35     -21.641   8.898  -2.782  1.00 54.15           C  
ANISOU  172  CG  ARG A  35     6998   7626   5947    782    495    261       C  
ATOM    173  CD  ARG A  35     -22.949   8.091  -2.750  1.00 58.63           C  
ANISOU  173  CD  ARG A  35     7663   8077   6537    739    555    264       C  
ATOM    174  NE  ARG A  35     -22.744   6.634  -2.649  1.00 62.42           N  
ANISOU  174  NE  ARG A  35     8257   8503   6956    817    626    320       N  
ATOM    175  CZ  ARG A  35     -22.742   5.925  -1.513  1.00 61.83           C  
ANISOU  175  CZ  ARG A  35     8245   8431   6814    882    672    355       C  
ATOM    176  NH1 ARG A  35     -22.967   6.513  -0.352  1.00 59.64           N  
ANISOU  176  NH1 ARG A  35     7927   8210   6520    873    654    338       N  
ATOM    177  NH2 ARG A  35     -22.510   4.624  -1.547  1.00 66.03           N  
ANISOU  177  NH2 ARG A  35     8888   8906   7293    956    740    409       N  
ATOM    178  N   ASN A  36     -17.665   8.828  -5.620  1.00 42.29           N  
ANISOU  178  N   ASN A  36     5391   6280   4395    944    428    315       N  
ATOM    179  CA  ASN A  36     -16.782   8.122  -6.571  1.00 43.75           C  
ANISOU  179  CA  ASN A  36     5604   6457   4559   1007    448    349       C  
ATOM    180  C   ASN A  36     -17.518   6.886  -7.092  1.00 43.03           C  
ANISOU  180  C   ASN A  36     5641   6234   4472   1012    515    382       C  
ATOM    181  O   ASN A  36     -16.878   5.862  -7.185  1.00 44.26           O  
ANISOU  181  O   ASN A  36     5858   6381   4575   1105    558    431       O  
ATOM    182  CB  ASN A  36     -15.422   7.746  -5.958  1.00 47.23           C  
ANISOU  182  CB  ASN A  36     6014   7012   4917   1131    446    387       C  
ATOM    183  CG  ASN A  36     -14.414   7.383  -7.011  1.00 49.70           C  
ANISOU  183  CG  ASN A  36     6323   7337   5221   1181    453    407       C  
ATOM    184  OD1 ASN A  36     -14.629   7.609  -8.201  1.00 42.48           O  
ANISOU  184  OD1 ASN A  36     5416   6360   4364   1116    450    387       O  
ATOM    185  ND2 ASN A  36     -13.326   6.779  -6.581  1.00 48.89           N  
ANISOU  185  ND2 ASN A  36     6213   7316   5044   1303    464    450       N  
ATOM    186  N   GLU A  37     -18.809   7.006  -7.421  1.00 40.36           N  
ANISOU  186  N   GLU A  37     5338   5802   4192    914    524    353       N  
ATOM    187  CA  GLU A  37     -19.603   5.976  -8.133  1.00 41.15           C  
ANISOU  187  CA  GLU A  37     5549   5776   4308    888    584    366       C  
ATOM    188  C   GLU A  37     -20.157   6.504  -9.466  1.00 43.09           C  
ANISOU  188  C   GLU A  37     5777   5969   4626    788    559    327       C  
ATOM    189  O   GLU A  37     -20.251   7.727  -9.628  1.00 39.32           O  
ANISOU  189  O   GLU A  37     5209   5537   4194    729    498    287       O  
ATOM    190  CB  GLU A  37     -20.863   5.606  -7.372  1.00 44.76           C  
ANISOU  190  CB  GLU A  37     6066   6167   4773    844    623    358       C  
ATOM    191  CG  GLU A  37     -20.607   4.881  -6.087  1.00 54.45           C  
ANISOU  191  CG  GLU A  37     7344   7415   5927    934    665    400       C  
ATOM    192  CD  GLU A  37     -21.929   4.416  -5.509  1.00 58.89           C  
ANISOU  192  CD  GLU A  37     7980   7893   6502    879    716    389       C  
ATOM    193  OE1 GLU A  37     -22.343   3.302  -5.912  1.00 62.94           O  
ANISOU  193  OE1 GLU A  37     8603   8306   7006    880    788    408       O  
ATOM    194  OE2 GLU A  37     -22.578   5.219  -4.731  1.00 56.64           O  
ANISOU  194  OE2 GLU A  37     7639   7638   6241    825    685    354       O  
ATOM    195  N   PHE A  38     -20.599   5.587 -10.307  1.00 42.13           N  
ANISOU  195  N   PHE A  38     5745   5751   4511    769    608    337       N  
ATOM    196  CA  PHE A  38     -21.312   5.876 -11.565  1.00 43.20           C  
ANISOU  196  CA  PHE A  38     5881   5827   4706    673    592    301       C  
ATOM    197  C   PHE A  38     -22.432   4.853 -11.745  1.00 46.60           C  
ANISOU  197  C   PHE A  38     6415   6149   5141    626    656    297       C  
ATOM    198  O   PHE A  38     -22.146   3.642 -11.714  1.00 46.42           O  
ANISOU  198  O   PHE A  38     6490   6076   5072    683    726    334       O  
ATOM    199  CB  PHE A  38     -20.334   5.872 -12.726  1.00 39.35           C  
ANISOU  199  CB  PHE A  38     5385   5351   4214    699    581    313       C  
ATOM    200  CG  PHE A  38     -21.043   6.079 -14.036  1.00 40.03           C  
ANISOU  200  CG  PHE A  38     5482   5376   4351    607    567    281       C  
ATOM    201  CD1 PHE A  38     -21.387   7.371 -14.453  1.00 38.62           C  
ANISOU  201  CD1 PHE A  38     5218   5229   4225    536    499    241       C  
ATOM    202  CD2 PHE A  38     -21.363   5.000 -14.847  1.00 42.34           C  
ANISOU  202  CD2 PHE A  38     5872   5580   4632    592    623    289       C  
ATOM    203  CE1 PHE A  38     -22.023   7.559 -15.673  1.00 37.71           C  
ANISOU  203  CE1 PHE A  38     5112   5064   4148    460    483    216       C  
ATOM    204  CE2 PHE A  38     -21.982   5.203 -16.082  1.00 43.51           C  
ANISOU  204  CE2 PHE A  38     6026   5684   4820    507    606    257       C  
ATOM    205  CZ  PHE A  38     -22.316   6.483 -16.481  1.00 37.40           C  
ANISOU  205  CZ  PHE A  38     5165   4950   4096    445    533    223       C  
ATOM    206  N   LEU A  39     -23.658   5.324 -11.951  1.00 45.17           N  
ANISOU  206  N   LEU A  39     6212   5935   5013    526    635    252       N  
ATOM    207  CA  LEU A  39     -24.836   4.456 -12.211  1.00 50.38           C  
ANISOU  207  CA  LEU A  39     6955   6501   5684    460    692    233       C  
ATOM    208  C   LEU A  39     -25.389   4.804 -13.601  1.00 49.96           C  
ANISOU  208  C   LEU A  39     6883   6420   5678    373    660    196       C  
ATOM    209  O   LEU A  39     -25.356   6.036 -14.014  1.00 56.95           O  
ANISOU  209  O   LEU A  39     7673   7358   6604    342    583    174       O  
ATOM    210  CB  LEU A  39     -25.876   4.678 -11.103  1.00 52.72           C  
ANISOU  210  CB  LEU A  39     7237   6794   5997    418    699    210       C  
ATOM    211  CG  LEU A  39     -25.363   4.553  -9.656  1.00 57.54           C  
ANISOU  211  CG  LEU A  39     7853   7447   6560    500    718    243       C  
ATOM    212  CD1 LEU A  39     -26.443   4.932  -8.640  1.00 56.71           C  
ANISOU  212  CD1 LEU A  39     7724   7343   6479    448    719    213       C  
ATOM    213  CD2 LEU A  39     -24.798   3.156  -9.350  1.00 59.00           C  
ANISOU  213  CD2 LEU A  39     8154   7584   6676    585    803    295       C  
ATOM    214  N   ALA A  40     -25.756   3.771 -14.357  1.00 50.56           N  
ANISOU  214  N   ALA A  40     7048   6418   5742    342    717    192       N  
ATOM    215  CA  ALA A  40     -26.299   3.826 -15.749  1.00 54.02           C  
ANISOU  215  CA  ALA A  40     7489   6824   6211    260    698    158       C  
ATOM    216  C   ALA A  40     -27.841   3.902 -15.741  1.00 55.42           C  
ANISOU  216  C   ALA A  40     7655   6972   6427    156    697    106       C  
ATOM    217  O   ALA A  40     -28.463   3.214 -14.895  1.00 53.69           O  
ANISOU  217  O   ALA A  40     7489   6715   6196    143    756    101       O  
ATOM    218  CB  ALA A  40     -25.831   2.606 -16.503  1.00 51.92           C  
ANISOU  218  CB  ALA A  40     7329   6490   5904    282    768    178       C  
ATOM    219  N   ASN A  41     -28.447   4.621 -16.708  1.00 56.40           N  
ANISOU  219  N   ASN A  41     7721   7114   6592     84    637     69       N  
ATOM    220  CA  ASN A  41     -29.924   4.736 -16.959  1.00 58.26           C  
ANISOU  220  CA  ASN A  41     7933   7335   6865    -17    626     14       C  
ATOM    221  C   ASN A  41     -30.743   4.789 -15.655  1.00 56.10           C  
ANISOU  221  C   ASN A  41     7641   7064   6607    -34    647     -1       C  
ATOM    222  O   ASN A  41     -31.751   4.061 -15.595  1.00 57.41           O  
ANISOU  222  O   ASN A  41     7851   7186   6774   -102    697    -35       O  
ATOM    223  CB  ASN A  41     -30.465   3.612 -17.861  1.00 63.67           C  
ANISOU  223  CB  ASN A  41     8703   7955   7532    -82    683    -11       C  
ATOM    224  CG  ASN A  41     -31.897   3.841 -18.325  1.00 62.77           C  
ANISOU  224  CG  ASN A  41     8546   7848   7453   -189    657    -72       C  
ATOM    225  N   GLN A  42     -30.384   5.642 -14.675  1.00 50.61           N  
ANISOU  225  N   GLN A  42     6883   6421   5923     14    611     15       N  
ATOM    226  CA  GLN A  42     -31.206   5.839 -13.440  1.00 49.87           C  
ANISOU  226  CA  GLN A  42     6763   6335   5847     -5    625     -3       C  
ATOM    227  C   GLN A  42     -32.405   6.735 -13.774  1.00 49.15           C  
ANISOU  227  C   GLN A  42     6587   6272   5816    -84    569    -53       C  
ATOM    228  O   GLN A  42     -32.230   7.720 -14.512  1.00 47.32           O  
ANISOU  228  O   GLN A  42     6286   6081   5612    -86    498    -57       O  
ATOM    229  CB  GLN A  42     -30.429   6.408 -12.259  1.00 49.03           C  
ANISOU  229  CB  GLN A  42     6623   6278   5727     71    610     28       C  
ATOM    230  CG  GLN A  42     -29.278   5.504 -11.832  1.00 52.97           C  
ANISOU  230  CG  GLN A  42     7202   6761   6163    160    664     81       C  
ATOM    231  CD  GLN A  42     -29.715   4.231 -11.132  1.00 53.53           C  
ANISOU  231  CD  GLN A  42     7377   6765   6197    161    758     88       C  
ATOM    232  OE1 GLN A  42     -30.233   4.266 -10.008  1.00 53.66           O  
ANISOU  232  OE1 GLN A  42     7391   6784   6212    156    780     82       O  
ATOM    233  NE2 GLN A  42     -29.488   3.102 -11.792  1.00 48.29           N  
ANISOU  233  NE2 GLN A  42     6811   6037   5501    166    820    103       N  
ATOM    234  N   GLU A  43     -33.579   6.359 -13.264  1.00 47.88           N  
ANISOU  234  N   GLU A  43     6434   6088   5671   -146    607    -91       N  
ATOM    235  CA  GLU A  43     -34.803   7.186 -13.373  1.00 52.10           C  
ANISOU  235  CA  GLU A  43     6879   6655   6261   -214    560   -140       C  
ATOM    236  C   GLU A  43     -34.480   8.608 -12.823  1.00 46.56           C  
ANISOU  236  C   GLU A  43     6084   6013   5591   -171    493   -128       C  
ATOM    237  O   GLU A  43     -33.828   8.820 -11.720  1.00 45.35           O  
ANISOU  237  O   GLU A  43     5933   5876   5421   -113    505   -101       O  
ATOM    238  CB  GLU A  43     -35.995   6.428 -12.751  1.00 56.83           C  
ANISOU  238  CB  GLU A  43     7507   7219   6865   -282    626   -181       C  
ATOM    239  CG  GLU A  43     -37.357   6.836 -13.321  1.00 61.02           C  
ANISOU  239  CG  GLU A  43     7964   7775   7443   -370    591   -241       C  
ATOM    240  CD  GLU A  43     -37.836   8.184 -12.798  1.00 63.84           C  
ANISOU  240  CD  GLU A  43     8211   8191   7852   -362    528   -253       C  
ATOM    241  OE1 GLU A  43     -37.503   8.478 -11.630  1.00 67.02           O  
ANISOU  241  OE1 GLU A  43     8612   8598   8253   -318    544   -233       O  
ATOM    242  OE2 GLU A  43     -38.528   8.940 -13.539  1.00 59.86           O  
ANISOU  242  OE2 GLU A  43     7627   7728   7388   -396    466   -282       O  
ATOM    243  N   THR A  44     -34.841   9.619 -13.604  1.00 46.43           N  
ANISOU  243  N   THR A  44     5990   6035   5616   -193    422   -146       N  
ATOM    244  CA  THR A  44     -34.443  11.048 -13.378  1.00 42.68           C  
ANISOU  244  CA  THR A  44     5433   5609   5171   -154    358   -134       C  
ATOM    245  C   THR A  44     -34.887  11.499 -11.966  1.00 40.38           C  
ANISOU  245  C   THR A  44     5106   5335   4901   -151    372   -147       C  
ATOM    246  O   THR A  44     -34.196  12.317 -11.303  1.00 41.27           O  
ANISOU  246  O   THR A  44     5185   5479   5015   -104    351   -130       O  
ATOM    247  CB  THR A  44     -34.997  11.863 -14.562  1.00 45.00           C  
ANISOU  247  CB  THR A  44     5666   5927   5503   -186    292   -154       C  
ATOM    248  OG1 THR A  44     -34.266  13.071 -14.545  1.00 48.71           O  
ANISOU  248  OG1 THR A  44     6088   6431   5990   -140    244   -133       O  
ATOM    249  CG2 THR A  44     -36.500  12.094 -14.525  1.00 42.85           C  
ANISOU  249  CG2 THR A  44     5339   5667   5272   -247    281   -200       C  
ATOM    250  N   THR A  45     -36.019  11.002 -11.451  1.00 42.53           N  
ANISOU  250  N   THR A  45     5383   5588   5187   -202    412   -181       N  
ATOM    251  CA  THR A  45     -36.606  11.533 -10.187  1.00 42.50           C  
ANISOU  251  CA  THR A  45     5336   5601   5209   -207    424   -200       C  
ATOM    252  C   THR A  45     -35.955  10.850  -8.967  1.00 46.50           C  
ANISOU  252  C   THR A  45     5909   6090   5667   -166    484   -174       C  
ATOM    253  O   THR A  45     -36.224  11.292  -7.873  1.00 46.21           O  
ANISOU  253  O   THR A  45     5845   6070   5642   -161    494   -183       O  
ATOM    254  CB  THR A  45     -38.145  11.440 -10.156  1.00 44.92           C  
ANISOU  254  CB  THR A  45     5606   5905   5556   -281    437   -253       C  
ATOM    255  OG1 THR A  45     -38.373  10.027 -10.137  1.00 44.09           O  
ANISOU  255  OG1 THR A  45     5585   5751   5414   -316    508   -260       O  
ATOM    256  CG2 THR A  45     -38.825  12.098 -11.346  1.00 42.48           C  
ANISOU  256  CG2 THR A  45     5228   5625   5288   -314    374   -277       C  
ATOM    257  N   ILE A  46     -35.089   9.855  -9.127  1.00 48.26           N  
ANISOU  257  N   ILE A  46     6216   6283   5835   -130    521   -139       N  
ATOM    258  CA  ILE A  46     -34.632   9.055  -7.943  1.00 52.94           C  
ANISOU  258  CA  ILE A  46     6882   6856   6376    -88    587   -112       C  
ATOM    259  C   ILE A  46     -33.238   9.512  -7.450  1.00 49.71           C  
ANISOU  259  C   ILE A  46     6464   6492   5931     -2    561    -68       C  
ATOM    260  O   ILE A  46     -32.960   9.280  -6.259  1.00 51.87           O  
ANISOU  260  O   ILE A  46     6765   6773   6169     35    596    -52       O  
ATOM    261  CB  ILE A  46     -34.739   7.539  -8.233  1.00 55.50           C  
ANISOU  261  CB  ILE A  46     7314   7112   6659   -103    664   -104       C  
ATOM    262  CG1 ILE A  46     -33.736   7.064  -9.289  1.00 57.19           C  
ANISOU  262  CG1 ILE A  46     7574   7312   6841    -65    657    -70       C  
ATOM    263  CG2 ILE A  46     -36.192   7.170  -8.597  1.00 54.36           C  
ANISOU  263  CG2 ILE A  46     7166   6936   6552   -202    692   -160       C  
ATOM    264  CD1 ILE A  46     -33.777   5.546  -9.556  1.00 61.98           C  
ANISOU  264  CD1 ILE A  46     8299   7844   7404    -76    743    -61       C  
ATOM    265  N   GLY A  47     -32.399  10.176  -8.256  1.00 44.51           N  
ANISOU  265  N   GLY A  47     5765   5867   5279     26    504    -53       N  
ATOM    266  CA  GLY A  47     -31.131  10.716  -7.708  1.00 42.95           C  
ANISOU  266  CA  GLY A  47     5545   5724   5050     98    478    -22       C  
ATOM    267  C   GLY A  47     -31.316  11.525  -6.383  1.00 39.64           C  
ANISOU  267  C   GLY A  47     5074   5347   4639    102    471    -38       C  
ATOM    268  O   GLY A  47     -32.219  12.338  -6.324  1.00 36.77           O  
ANISOU  268  O   GLY A  47     4652   4988   4331     51    448    -75       O  
ATOM    269  N   ALA A  48     -30.429  11.352  -5.374  1.00 37.46           N  
ANISOU  269  N   ALA A  48     4815   5107   4307    165    487    -10       N  
ATOM    270  CA  ALA A  48     -30.425  12.154  -4.133  1.00 36.21           C  
ANISOU  270  CA  ALA A  48     4609   4999   4148    172    476    -25       C  
ATOM    271  C   ALA A  48     -30.448  13.653  -4.492  1.00 34.70           C  
ANISOU  271  C   ALA A  48     4322   4846   4013    141    414    -57       C  
ATOM    272  O   ALA A  48     -29.619  14.100  -5.352  1.00 35.46           O  
ANISOU  272  O   ALA A  48     4392   4967   4113    158    374    -46       O  
ATOM    273  CB  ALA A  48     -29.216  11.834  -3.298  1.00 38.19           C  
ANISOU  273  CB  ALA A  48     4883   5302   4324    252    487     11       C  
ATOM    274  N   ALA A  49     -31.323  14.404  -3.856  1.00 33.02           N  
ANISOU  274  N   ALA A  49     4065   4637   3842     99    411    -92       N  
ATOM    275  CA  ALA A  49     -31.477  15.866  -4.053  1.00 29.19           C  
ANISOU  275  CA  ALA A  49     3497   4179   3412     70    364   -124       C  
ATOM    276  C   ALA A  49     -30.299  16.579  -3.409  1.00 30.86           C  
ANISOU  276  C   ALA A  49     3674   4459   3590    107    344   -120       C  
ATOM    277  O   ALA A  49     -29.956  17.694  -3.863  1.00 28.47           O  
ANISOU  277  O   ALA A  49     3317   4180   3321     95    305   -136       O  
ATOM    278  CB  ALA A  49     -32.787  16.280  -3.505  1.00 32.19           C  
ANISOU  278  CB  ALA A  49     3849   4537   3841     20    379   -161       C  
ATOM    279  N   PHE A  50     -29.726  15.999  -2.328  1.00 28.39           N  
ANISOU  279  N   PHE A  50     3393   4181   3212    150    371   -102       N  
ATOM    280  CA  PHE A  50     -28.679  16.662  -1.533  1.00 29.86           C  
ANISOU  280  CA  PHE A  50     3539   4447   3358    181    352   -106       C  
ATOM    281  C   PHE A  50     -27.522  15.690  -1.319  1.00 31.98           C  
ANISOU  281  C   PHE A  50     3850   4755   3544    255    363    -62       C  
ATOM    282  O   PHE A  50     -27.735  14.580  -0.822  1.00 30.96           O  
ANISOU  282  O   PHE A  50     3789   4601   3372    286    405    -35       O  
ATOM    283  CB  PHE A  50     -29.248  17.154  -0.217  1.00 29.49           C  
ANISOU  283  CB  PHE A  50     3473   4419   3312    158    371   -136       C  
ATOM    284  CG  PHE A  50     -30.503  17.981  -0.348  1.00 27.96           C  
ANISOU  284  CG  PHE A  50     3242   4180   3198     93    369   -177       C  
ATOM    285  CD1 PHE A  50     -30.456  19.301  -0.751  1.00 27.74           C  
ANISOU  285  CD1 PHE A  50     3151   4166   3223     62    336   -207       C  
ATOM    286  CD2 PHE A  50     -31.722  17.447   0.012  1.00 28.09           C  
ANISOU  286  CD2 PHE A  50     3289   4146   3237     64    407   -186       C  
ATOM    287  CE1 PHE A  50     -31.616  20.046  -0.851  1.00 25.72           C  
ANISOU  287  CE1 PHE A  50     2863   3870   3038     14    338   -240       C  
ATOM    288  CE2 PHE A  50     -32.886  18.201  -0.088  1.00 29.43           C  
ANISOU  288  CE2 PHE A  50     3418   4284   3481     10    406   -224       C  
ATOM    289  CZ  PHE A  50     -32.811  19.509  -0.530  1.00 27.68           C  
ANISOU  289  CZ  PHE A  50     3132   4074   3308     -8    370   -248       C  
ATOM    290  N   LEU A  51     -26.340  16.094  -1.713  1.00 30.08           N  
ANISOU  290  N   LEU A  51     3573   4573   3282    284    330    -56       N  
ATOM    291  CA ALEU A  51     -25.103  15.283  -1.584  0.54 32.04           C  
ANISOU  291  CA ALEU A  51     3846   4874   3451    364    334    -14       C  
ATOM    292  CA BLEU A  51     -25.109  15.273  -1.555  0.46 32.38           C  
ANISOU  292  CA BLEU A  51     3890   4918   3494    364    335    -14       C  
ATOM    293  C   LEU A  51     -24.042  16.162  -0.934  1.00 35.56           C  
ANISOU  293  C   LEU A  51     4220   5427   3862    380    303    -35       C  
ATOM    294  O   LEU A  51     -24.238  17.440  -0.969  1.00 37.28           O  
ANISOU  294  O   LEU A  51     4374   5658   4130    319    278    -82       O  
ATOM    295  CB ALEU A  51     -24.678  14.829  -2.978  0.54 31.65           C  
ANISOU  295  CB ALEU A  51     3820   4791   3415    378    326     10       C  
ATOM    296  CB BLEU A  51     -24.646  14.754  -2.916  0.46 32.44           C  
ANISOU  296  CB BLEU A  51     3922   4892   3508    383    328     12       C  
ATOM    297  CG ALEU A  51     -25.789  14.196  -3.822  0.54 32.11           C  
ANISOU  297  CG ALEU A  51     3934   4747   3518    341    349     15       C  
ATOM    298  CG BLEU A  51     -25.571  13.756  -3.615  0.46 33.32           C  
ANISOU  298  CG BLEU A  51     4110   4905   3643    368    362     31       C  
ATOM    299  CD1ALEU A  51     -26.341  15.184  -4.846  0.54 29.28           C  
ANISOU  299  CD1ALEU A  51     3529   4357   3238    274    315    -16       C  
ATOM    300  CD1BLEU A  51     -25.116  13.547  -5.062  0.46 34.39           C  
ANISOU  300  CD1BLEU A  51     4255   5013   3795    371    348     47       C  
ATOM    301  CD2ALEU A  51     -25.281  12.920  -4.485  0.54 34.66           C  
ANISOU  301  CD2ALEU A  51     4329   5039   3800    394    377     61       C  
ATOM    302  CD2BLEU A  51     -25.629  12.430  -2.869  0.46 32.73           C  
ANISOU  302  CD2BLEU A  51     4119   4809   3506    422    417     69       C  
ATOM    303  N   SER A  52     -22.969  15.563  -0.372  1.00 32.99           N  
ANISOU  303  N   SER A  52     3901   5178   3454    456    304     -5       N  
ATOM    304  CA ASER A  52     -21.929  16.372   0.315  0.33 34.07           C  
ANISOU  304  CA ASER A  52     3962   5434   3549    469    273    -31       C  
ATOM    305  CA BSER A  52     -21.909  16.411   0.221  0.67 33.34           C  
ANISOU  305  CA BSER A  52     3866   5339   3460    466    272    -32       C  
ATOM    306  C   SER A  52     -20.565  15.696   0.198  1.00 35.23           C  
ANISOU  306  C   SER A  52     4104   5660   3621    557    264      6       C  
ATOM    307  O   SER A  52     -20.546  14.486   0.096  1.00 34.49           O  
ANISOU  307  O   SER A  52     4082   5531   3490    622    292     58       O  
ATOM    308  CB ASER A  52     -22.295  16.605   1.762  0.33 35.36           C  
ANISOU  308  CB ASER A  52     4117   5637   3678    462    285    -51       C  
ATOM    309  CB BSER A  52     -22.294  16.864   1.607  0.67 36.02           C  
ANISOU  309  CB BSER A  52     4188   5721   3777    447    278    -61       C  
ATOM    310  OG ASER A  52     -21.291  17.360   2.427  0.33 36.14           O  
ANISOU  310  OG ASER A  52     4142   5859   3731    468    255    -81       O  
ATOM    311  OG BSER A  52     -22.385  15.762   2.490  0.67 36.25           O  
ANISOU  311  OG BSER A  52     4280   5755   3736    512    310    -20       O  
ATOM    312  N   LYS A  53     -19.518  16.480   0.276  1.00 37.28           N  
ANISOU  312  N   LYS A  53     4283   6022   3859    556    230    -22       N  
ATOM    313  CA  LYS A  53     -18.146  15.967   0.435  1.00 37.86           C  
ANISOU  313  CA  LYS A  53     4331   6202   3850    643    217      5       C  
ATOM    314  C   LYS A  53     -17.371  17.114   1.062  1.00 40.39           C  
ANISOU  314  C   LYS A  53     4550   6647   4148    610    183    -51       C  
ATOM    315  O   LYS A  53     -17.624  18.302   0.670  1.00 37.50           O  
ANISOU  315  O   LYS A  53     4137   6260   3848    518    170   -105       O  
ATOM    316  CB  LYS A  53     -17.601  15.513  -0.917  1.00 39.81           C  
ANISOU  316  CB  LYS A  53     4593   6416   4117    670    216     33       C  
ATOM    317  CG  LYS A  53     -16.256  14.820  -0.814  1.00 41.93           C  
ANISOU  317  CG  LYS A  53     4843   6786   4303    772    209     69       C  
ATOM    318  CD  LYS A  53     -15.860  14.054  -2.056  1.00 44.38           C  
ANISOU  318  CD  LYS A  53     5194   7043   4623    814    224    110       C  
ATOM    319  CE  LYS A  53     -14.426  14.284  -2.512  1.00 47.69           C  
ANISOU  319  CE  LYS A  53     5538   7570   5012    852    198    103       C  
ATOM    320  NZ  LYS A  53     -14.124  13.752  -3.872  1.00 45.71           N  
ANISOU  320  NZ  LYS A  53     5323   7256   4788    872    213    132       N  
ATOM    321  N   THR A  54     -16.540  16.802   2.064  1.00 39.63           N  
ANISOU  321  N   THR A  54     4425   6674   3959    678    172    -41       N  
ATOM    322  CA  THR A  54     -15.674  17.811   2.705  1.00 42.60           C  
ANISOU  322  CA  THR A  54     4697   7188   4299    649    139    -99       C  
ATOM    323  C   THR A  54     -14.253  17.620   2.185  1.00 45.29           C  
ANISOU  323  C   THR A  54     4980   7634   4595    706    116    -90       C  
ATOM    324  O   THR A  54     -13.793  16.472   2.149  1.00 41.94           O  
ANISOU  324  O   THR A  54     4592   7228   4112    812    123    -28       O  
ATOM    325  CB  THR A  54     -15.747  17.688   4.220  1.00 44.50           C  
ANISOU  325  CB  THR A  54     4935   7509   4463    678    138   -103       C  
ATOM    326  OG1 THR A  54     -17.119  17.955   4.452  1.00 44.73           O  
ANISOU  326  OG1 THR A  54     5017   7424   4554    611    164   -117       O  
ATOM    327  CG2 THR A  54     -14.805  18.640   4.935  1.00 47.71           C  
ANISOU  327  CG2 THR A  54     5234   8073   4820    649    105   -166       C  
ATOM    328  N   VAL A  55     -13.593  18.698   1.791  1.00 45.87           N  
ANISOU  328  N   VAL A  55     4966   7768   4694    639     95   -151       N  
ATOM    329  CA  VAL A  55     -12.258  18.609   1.137  1.00 48.97           C  
ANISOU  329  CA  VAL A  55     5295   8253   5055    679     76   -151       C  
ATOM    330  C   VAL A  55     -11.300  19.572   1.835  1.00 48.56           C  
ANISOU  330  C   VAL A  55     5128   8364   4957    640     49   -222       C  
ATOM    331  O   VAL A  55     -11.743  20.664   2.200  1.00 45.08           O  
ANISOU  331  O   VAL A  55     4661   7914   4553    539     50   -286       O  
ATOM    332  CB  VAL A  55     -12.408  18.883  -0.373  1.00 50.71           C  
ANISOU  332  CB  VAL A  55     5536   8367   5363    628     88   -152       C  
ATOM    333  CG1 VAL A  55     -11.094  19.260  -1.059  1.00 54.12           C  
ANISOU  333  CG1 VAL A  55     5886   8892   5782    627     73   -180       C  
ATOM    334  CG2 VAL A  55     -13.047  17.681  -1.059  1.00 51.18           C  
ANISOU  334  CG2 VAL A  55     5700   8300   5442    689    113    -78       C  
ATOM    335  N   MET A  56     -10.022  19.193   1.988  1.00 54.92           N  
ANISOU  335  N   MET A  56     5866   9315   5683    714     27   -216       N  
ATOM    336  CA  MET A  56      -8.996  20.103   2.557  1.00 58.69           C  
ANISOU  336  CA  MET A  56     6221   9964   6113    671      0   -292       C  
ATOM    337  C   MET A  56      -8.460  20.979   1.424  1.00 58.31           C  
ANISOU  337  C   MET A  56     6119   9905   6130    586      5   -344       C  
ATOM    338  O   MET A  56      -7.828  20.455   0.519  1.00 59.19           O  
ANISOU  338  O   MET A  56     6227  10017   6243    638      6   -312       O  
ATOM    339  CB  MET A  56      -7.864  19.306   3.215  1.00 65.64           C  
ANISOU  339  CB  MET A  56     7044  11018   6877    793    -28   -263       C  
ATOM    340  CG  MET A  56      -8.206  18.919   4.645  1.00 72.25           C  
ANISOU  340  CG  MET A  56     7900  11916   7634    845    -39   -244       C  
ATOM    341  SD  MET A  56      -8.670  20.379   5.657  1.00 87.29           S  
ANISOU  341  SD  MET A  56     9751  13862   9550    702    -44   -347       S  
ATOM    342  CE  MET A  56      -7.163  21.374   5.648  1.00 80.91           C  
ANISOU  342  CE  MET A  56     8783  13257   8701    643    -75   -443       C  
ATOM    343  N   ILE A  57      -8.770  22.267   1.410  1.00 60.53           N  
ANISOU  343  N   ILE A  57     6372  10159   6467    459     15   -420       N  
ATOM    344  CA  ILE A  57      -8.250  23.147   0.320  1.00 68.27           C  
ANISOU  344  CA  ILE A  57     7309  11121   7506    374     28   -470       C  
ATOM    345  C   ILE A  57      -7.054  23.910   0.901  1.00 78.36           C  
ANISOU  345  C   ILE A  57     8462  12585   8725    329     13   -554       C  
ATOM    346  O   ILE A  57      -6.512  23.480   1.968  1.00 84.05           O  
ANISOU  346  O   ILE A  57     9128  13455   9350    393    -15   -554       O  
ATOM    347  CB  ILE A  57      -9.349  24.062  -0.235  1.00 66.40           C  
ANISOU  347  CB  ILE A  57     7133  10722   7373    268     58   -495       C  
ATOM    348  CG1 ILE A  57      -9.892  25.030   0.833  1.00 67.30           C  
ANISOU  348  CG1 ILE A  57     7229  10851   7489    184     65   -559       C  
ATOM    349  CG2 ILE A  57     -10.426  23.197  -0.885  1.00 64.00           C  
ANISOU  349  CG2 ILE A  57     6941  10255   7119    319     69   -414       C  
ATOM    350  N   ASP A  58      -6.603  24.971   0.227  1.00 83.02           N  
ANISOU  350  N   ASP A  58     9005  13175   9362    225     32   -623       N  
ATOM    351  CA  ASP A  58      -5.677  25.920   0.898  1.00 83.90           C  
ANISOU  351  CA  ASP A  58     9001  13449   9426    147     27   -722       C  
ATOM    352  C   ASP A  58      -6.543  26.711   1.893  1.00 81.59           C  
ANISOU  352  C   ASP A  58     8729  13125   9145     68     38   -769       C  
ATOM    353  O   ASP A  58      -7.754  27.051   1.603  1.00 82.97           O  
ANISOU  353  O   ASP A  58     8995  13128   9401     23     65   -752       O  
ATOM    354  CB  ASP A  58      -4.799  26.747  -0.055  1.00 82.56           C  
ANISOU  354  CB  ASP A  58     8772  13305   9292     62     52   -786       C  
ATOM    355  CG  ASP A  58      -3.784  27.573   0.728  1.00 84.23           C  
ANISOU  355  CG  ASP A  58     8858  13704   9441    -12     47   -890       C  
ATOM    356  OD1 ASP A  58      -2.824  26.971   1.281  1.00 82.23           O  
ANISOU  356  OD1 ASP A  58     8517  13632   9096     63     10   -890       O  
ATOM    357  OD2 ASP A  58      -4.005  28.807   0.857  1.00 67.87           O  
ANISOU  357  OD2 ASP A  58     6778  11599   7409   -143     81   -971       O  
ATOM    358  N   GLY A  59      -6.007  26.863   3.091  1.00 74.79           N  
ANISOU  358  N   GLY A  59     7790  12429   8198     65     16   -818       N  
ATOM    359  CA  GLY A  59      -6.720  27.595   4.137  1.00 72.91           C  
ANISOU  359  CA  GLY A  59     7563  12180   7957     -9     27   -868       C  
ATOM    360  C   GLY A  59      -7.522  26.696   5.058  1.00 71.73           C  
ANISOU  360  C   GLY A  59     7476  12012   7766     81      6   -801       C  
ATOM    361  O   GLY A  59      -7.484  27.003   6.283  1.00 72.01           O  
ANISOU  361  O   GLY A  59     7472  12151   7737     57     -4   -847       O  
ATOM    362  N   ARG A  60      -8.255  25.679   4.563  1.00 61.26           N  
ANISOU  362  N   ARG A  60     6244  10558   6472    171      6   -703       N  
ATOM    363  CA  ARG A  60      -9.466  25.248   5.328  1.00 63.33           C  
ANISOU  363  CA  ARG A  60     6593  10733   6736    203     12   -658       C  
ATOM    364  C   ARG A  60     -10.040  23.894   4.856  1.00 57.50           C  
ANISOU  364  C   ARG A  60     5948   9889   6008    319     10   -549       C  
ATOM    365  O   ARG A  60      -9.791  23.509   3.702  1.00 54.78           O  
ANISOU  365  O   ARG A  60     5622   9487   5703    348     14   -511       O  
ATOM    366  CB  ARG A  60     -10.503  26.383   5.221  1.00 68.57           C  
ANISOU  366  CB  ARG A  60     7299  11261   7494     81     51   -708       C  
ATOM    367  CG  ARG A  60     -11.230  26.413   3.871  1.00 78.21           C  
ANISOU  367  CG  ARG A  60     8594  12297   8822     64     76   -669       C  
ATOM    368  CD  ARG A  60     -11.407  27.774   3.212  1.00 83.94           C  
ANISOU  368  CD  ARG A  60     9314  12946   9634    -58    111   -736       C  
ATOM    369  NE  ARG A  60     -12.314  28.562   4.038  1.00 87.10           N  
ANISOU  369  NE  ARG A  60     9737  13296  10059   -130    136   -779       N  
ATOM    370  CZ  ARG A  60     -12.096  29.794   4.505  1.00 84.59           C  
ANISOU  370  CZ  ARG A  60     9374  13019   9746   -236    161   -871       C  
ATOM    371  NH1 ARG A  60     -10.999  30.475   4.210  1.00 81.87           N  
ANISOU  371  NH1 ARG A  60     8956  12766   9385   -297    168   -937       N  
ATOM    372  NH2 ARG A  60     -13.022  30.352   5.259  1.00 87.71           N  
ANISOU  372  NH2 ARG A  60     9803  13357  10165   -286    186   -899       N  
ATOM    373  N   ALA A  61     -10.825  23.212   5.717  1.00 52.88           N  
ANISOU  373  N   ALA A  61     5428   9273   5391    375     11   -502       N  
ATOM    374  CA  ALA A  61     -11.795  22.140   5.331  1.00 55.30           C  
ANISOU  374  CA  ALA A  61     5847   9432   5731    447     28   -413       C  
ATOM    375  C   ALA A  61     -13.040  22.799   4.709  1.00 47.33           C  
ANISOU  375  C   ALA A  61     4898   8245   4837    355     60   -427       C  
ATOM    376  O   ALA A  61     -13.652  23.669   5.341  1.00 47.12           O  
ANISOU  376  O   ALA A  61     4867   8199   4836    274     74   -480       O  
ATOM    377  CB  ALA A  61     -12.208  21.302   6.517  1.00 54.52           C  
ANISOU  377  CB  ALA A  61     5794   9362   5557    525     26   -368       C  
ATOM    378  N   LEU A  62     -13.393  22.417   3.498  1.00 46.82           N  
ANISOU  378  N   LEU A  62     4888   8060   4841    367     73   -384       N  
ATOM    379  CA  LEU A  62     -14.582  22.985   2.802  1.00 43.85           C  
ANISOU  379  CA  LEU A  62     4567   7519   4572    291     99   -391       C  
ATOM    380  C   LEU A  62     -15.618  21.873   2.621  1.00 41.20           C  
ANISOU  380  C   LEU A  62     4330   7065   4256    351    114   -317       C  
ATOM    381  O   LEU A  62     -15.250  20.859   2.041  1.00 41.72           O  
ANISOU  381  O   LEU A  62     4428   7123   4301    429    110   -259       O  
ATOM    382  CB  LEU A  62     -14.158  23.497   1.424  1.00 46.16           C  
ANISOU  382  CB  LEU A  62     4842   7769   4926    250    101   -405       C  
ATOM    383  CG  LEU A  62     -15.293  24.004   0.519  1.00 44.34           C  
ANISOU  383  CG  LEU A  62     4669   7375   4801    188    124   -403       C  
ATOM    384  CD1 LEU A  62     -16.031  25.118   1.219  1.00 46.40           C  
ANISOU  384  CD1 LEU A  62     4921   7608   5099    102    141   -461       C  
ATOM    385  CD2 LEU A  62     -14.698  24.493  -0.780  1.00 49.01           C  
ANISOU  385  CD2 LEU A  62     5241   7943   5437    155    125   -416       C  
ATOM    386  N   LYS A  63     -16.829  22.044   3.146  1.00 37.17           N  
ANISOU  386  N   LYS A  63     3866   6472   3782    315    134   -322       N  
ATOM    387  CA  LYS A  63     -17.910  21.067   2.921  1.00 35.61           C  
ANISOU  387  CA  LYS A  63     3762   6155   3613    353    155   -262       C  
ATOM    388  C   LYS A  63     -18.743  21.518   1.699  1.00 32.92           C  
ANISOU  388  C   LYS A  63     3449   5679   3377    294    166   -265       C  
ATOM    389  O   LYS A  63     -19.410  22.534   1.794  1.00 34.28           O  
ANISOU  389  O   LYS A  63     3608   5808   3607    217    175   -311       O  
ATOM    390  CB  LYS A  63     -18.816  20.945   4.117  1.00 37.75           C  
ANISOU  390  CB  LYS A  63     4066   6409   3866    348    174   -265       C  
ATOM    391  CG  LYS A  63     -19.796  19.793   3.978  1.00 38.91           C  
ANISOU  391  CG  LYS A  63     4307   6449   4026    392    200   -204       C  
ATOM    392  CD  LYS A  63     -20.499  19.445   5.299  1.00 41.30           C  
ANISOU  392  CD  LYS A  63     4648   6754   4288    404    223   -200       C  
ATOM    393  CE  LYS A  63     -21.633  18.475   5.082  1.00 45.14           C  
ANISOU  393  CE  LYS A  63     5226   7117   4805    422    260   -153       C  
ATOM    394  NZ  LYS A  63     -22.341  18.194   6.342  1.00 49.54           N  
ANISOU  394  NZ  LYS A  63     5823   7671   5327    426    288   -153       N  
ATOM    395  N   TYR A  64     -18.611  20.820   0.592  1.00 33.29           N  
ANISOU  395  N   TYR A  64     3531   5674   3442    331    165   -220       N  
ATOM    396  CA  TYR A  64     -19.460  21.040  -0.620  1.00 34.06           C  
ANISOU  396  CA  TYR A  64     3665   5644   3629    287    173   -213       C  
ATOM    397  C   TYR A  64     -20.851  20.504  -0.283  1.00 32.61           C  
ANISOU  397  C   TYR A  64     3548   5368   3474    284    195   -192       C  
ATOM    398  O   TYR A  64     -21.072  19.298   0.034  1.00 32.60           O  
ANISOU  398  O   TYR A  64     3603   5350   3432    344    211   -145       O  
ATOM    399  CB  TYR A  64     -18.885  20.358  -1.847  1.00 33.41           C  
ANISOU  399  CB  TYR A  64     3605   5540   3547    329    166   -173       C  
ATOM    400  CG  TYR A  64     -17.588  20.873  -2.382  1.00 35.55           C  
ANISOU  400  CG  TYR A  64     3815   5890   3802    326    149   -194       C  
ATOM    401  CD1 TYR A  64     -16.373  20.392  -1.906  1.00 40.11           C  
ANISOU  401  CD1 TYR A  64     4353   6587   4298    390    137   -185       C  
ATOM    402  CD2 TYR A  64     -17.548  21.887  -3.336  1.00 35.83           C  
ANISOU  402  CD2 TYR A  64     3827   5886   3900    259    146   -227       C  
ATOM    403  CE1 TYR A  64     -15.174  20.883  -2.413  1.00 43.51           C  
ANISOU  403  CE1 TYR A  64     4718   7096   4714    381    124   -211       C  
ATOM    404  CE2 TYR A  64     -16.368  22.396  -3.821  1.00 35.98           C  
ANISOU  404  CE2 TYR A  64     3790   5975   3905    247    137   -252       C  
ATOM    405  CZ  TYR A  64     -15.168  21.862  -3.403  1.00 40.48           C  
ANISOU  405  CZ  TYR A  64     4317   6664   4397    307    126   -245       C  
ATOM    406  OH  TYR A  64     -13.988  22.412  -3.879  1.00 42.76           O  
ANISOU  406  OH  TYR A  64     4542   7030   4674    288    120   -278       O  
ATOM    407  N   GLU A  65     -21.828  21.375  -0.257  1.00 30.54           N  
ANISOU  407  N   GLU A  65     3280   5044   3279    216    203   -227       N  
ATOM    408  CA  GLU A  65     -23.238  20.912  -0.133  1.00 29.54           C  
ANISOU  408  CA  GLU A  65     3209   4822   3192    205    226   -211       C  
ATOM    409  C   GLU A  65     -23.846  20.987  -1.544  1.00 31.45           C  
ANISOU  409  C   GLU A  65     3472   4970   3507    179    221   -199       C  
ATOM    410  O   GLU A  65     -24.315  22.051  -1.940  1.00 28.76           O  
ANISOU  410  O   GLU A  65     3105   4592   3229    125    216   -231       O  
ATOM    411  CB  GLU A  65     -24.041  21.782   0.793  1.00 32.15           C  
ANISOU  411  CB  GLU A  65     3518   5144   3551    151    240   -256       C  
ATOM    412  CG  GLU A  65     -23.529  21.693   2.253  1.00 36.81           C  
ANISOU  412  CG  GLU A  65     4091   5830   4063    173    246   -270       C  
ATOM    413  CD  GLU A  65     -24.060  20.460   3.002  1.00 46.75           C  
ANISOU  413  CD  GLU A  65     5413   7072   5276    223    270   -230       C  
ATOM    414  OE1 GLU A  65     -24.573  19.514   2.369  1.00 49.38           O  
ANISOU  414  OE1 GLU A  65     5803   7331   5625    248    284   -188       O  
ATOM    415  OE2 GLU A  65     -24.008  20.466   4.243  1.00 51.07           O  
ANISOU  415  OE2 GLU A  65     5956   7676   5771    231    281   -243       O  
ATOM    416  N   ILE A  66     -23.835  19.863  -2.205  1.00 30.60           N  
ANISOU  416  N   ILE A  66     3414   4826   3383    222    225   -153       N  
ATOM    417  CA  ILE A  66     -24.252  19.746  -3.646  1.00 32.42           C  
ANISOU  417  CA  ILE A  66     3670   4979   3668    205    218   -136       C  
ATOM    418  C   ILE A  66     -25.761  19.483  -3.715  1.00 31.02           C  
ANISOU  418  C   ILE A  66     3529   4716   3541    174    234   -137       C  
ATOM    419  O   ILE A  66     -26.270  18.458  -3.186  1.00 33.16           O  
ANISOU  419  O   ILE A  66     3848   4964   3785    196    262   -116       O  
ATOM    420  CB  ILE A  66     -23.485  18.625  -4.364  1.00 33.01           C  
ANISOU  420  CB  ILE A  66     3785   5057   3700    262    219    -91       C  
ATOM    421  CG1 ILE A  66     -21.955  18.672  -4.269  1.00 37.21           C  
ANISOU  421  CG1 ILE A  66     4280   5683   4175    306    205    -86       C  
ATOM    422  CG2 ILE A  66     -23.928  18.644  -5.822  1.00 32.58           C  
ANISOU  422  CG2 ILE A  66     3752   4928   3700    236    209    -82       C  
ATOM    423  CD1 ILE A  66     -21.406  20.026  -4.447  1.00 39.38           C  
ANISOU  423  CD1 ILE A  66     4486   6000   4475    260    184   -130       C  
ATOM    424  N   TRP A  67     -26.455  20.379  -4.400  1.00 27.91           N  
ANISOU  424  N   TRP A  67     3111   4275   3216    125    221   -159       N  
ATOM    425  CA  TRP A  67     -27.897  20.270  -4.661  1.00 24.51           C  
ANISOU  425  CA  TRP A  67     2699   3772   2840     93    230   -165       C  
ATOM    426  C   TRP A  67     -28.100  19.740  -6.084  1.00 25.77           C  
ANISOU  426  C   TRP A  67     2889   3881   3019     94    217   -140       C  
ATOM    427  O   TRP A  67     -27.390  20.180  -6.979  1.00 25.58           O  
ANISOU  427  O   TRP A  67     2852   3865   3000     97    195   -134       O  
ATOM    428  CB  TRP A  67     -28.536  21.628  -4.522  1.00 25.69           C  
ANISOU  428  CB  TRP A  67     2802   3909   3050     48    223   -204       C  
ATOM    429  CG  TRP A  67     -28.705  22.116  -3.107  1.00 25.49           C  
ANISOU  429  CG  TRP A  67     2752   3917   3015     35    242   -235       C  
ATOM    430  CD1 TRP A  67     -27.792  22.084  -2.100  1.00 28.60           C  
ANISOU  430  CD1 TRP A  67     3135   4381   3349     54    250   -241       C  
ATOM    431  CD2 TRP A  67     -29.876  22.702  -2.567  1.00 26.67           C  
ANISOU  431  CD2 TRP A  67     2883   4034   3213      0    258   -264       C  
ATOM    432  NE1 TRP A  67     -28.307  22.673  -0.961  1.00 27.06           N  
ANISOU  432  NE1 TRP A  67     2919   4199   3163     28    269   -276       N  
ATOM    433  CE2 TRP A  67     -29.599  23.040  -1.219  1.00 26.71           C  
ANISOU  433  CE2 TRP A  67     2871   4088   3187     -4    277   -290       C  
ATOM    434  CE3 TRP A  67     -31.135  23.004  -3.100  1.00 27.50           C  
ANISOU  434  CE3 TRP A  67     2981   4080   3386    -25    257   -273       C  
ATOM    435  CZ2 TRP A  67     -30.549  23.707  -0.461  1.00 25.67           C  
ANISOU  435  CZ2 TRP A  67     2721   3937   3095    -37    299   -324       C  
ATOM    436  CZ3 TRP A  67     -32.101  23.599  -2.337  1.00 27.99           C  
ANISOU  436  CZ3 TRP A  67     3020   4127   3487    -52    278   -305       C  
ATOM    437  CH2 TRP A  67     -31.789  23.929  -0.999  1.00 28.01           C  
ANISOU  437  CH2 TRP A  67     3012   4171   3460    -59    301   -330       C  
ATOM    438  N   ASP A  68     -28.959  18.755  -6.211  1.00 26.50           N  
ANISOU  438  N   ASP A  68     3025   3928   3114     90    236   -127       N  
ATOM    439  CA  ASP A  68     -29.322  18.127  -7.490  1.00 26.30           C  
ANISOU  439  CA  ASP A  68     3033   3854   3103     82    229   -109       C  
ATOM    440  C   ASP A  68     -30.835  18.287  -7.681  1.00 24.94           C  
ANISOU  440  C   ASP A  68     2850   3637   2988     36    229   -132       C  
ATOM    441  O   ASP A  68     -31.596  18.621  -6.729  1.00 25.25           O  
ANISOU  441  O   ASP A  68     2867   3678   3048     17    245   -157       O  
ATOM    442  CB  ASP A  68     -28.772  16.703  -7.586  1.00 25.73           C  
ANISOU  442  CB  ASP A  68     3027   3774   2973    121    256    -74       C  
ATOM    443  CG  ASP A  68     -28.774  16.117  -8.973  1.00 27.99           C  
ANISOU  443  CG  ASP A  68     3349   4021   3263    117    249    -56       C  
ATOM    444  OD1 ASP A  68     -28.830  16.915  -9.957  1.00 26.22           O  
ANISOU  444  OD1 ASP A  68     3094   3790   3077     95    213    -65       O  
ATOM    445  OD2 ASP A  68     -28.865  14.874  -9.054  1.00 27.68           O  
ANISOU  445  OD2 ASP A  68     3372   3951   3191    130    283    -36       O  
ATOM    446  N   THR A  69     -31.320  18.145  -8.900  1.00 25.17           N  
ANISOU  446  N   THR A  69     2887   3632   3042     18    211   -128       N  
ATOM    447  CA  THR A  69     -32.666  18.596  -9.319  1.00 26.96           C  
ANISOU  447  CA  THR A  69     3083   3833   3327    -21    196   -152       C  
ATOM    448  C   THR A  69     -33.801  17.617  -8.994  1.00 27.77           C  
ANISOU  448  C   THR A  69     3209   3908   3433    -51    228   -166       C  
ATOM    449  O   THR A  69     -34.981  18.029  -9.194  1.00 27.90           O  
ANISOU  449  O   THR A  69     3187   3915   3498    -84    217   -192       O  
ATOM    450  CB  THR A  69     -32.713  18.778 -10.846  1.00 25.72           C  
ANISOU  450  CB  THR A  69     2926   3659   3187    -28    159   -142       C  
ATOM    451  OG1 THR A  69     -32.508  17.523 -11.486  1.00 25.69           O  
ANISOU  451  OG1 THR A  69     2979   3635   3146    -27    174   -123       O  
ATOM    452  CG2 THR A  69     -31.660  19.762 -11.269  1.00 27.86           C  
ANISOU  452  CG2 THR A  69     3177   3949   3457     -6    134   -130       C  
ATOM    453  N   ALA A  70     -33.512  16.350  -8.687  1.00 28.90           N  
ANISOU  453  N   ALA A  70     3414   4037   3527    -41    268   -150       N  
ATOM    454  CA  ALA A  70     -34.534  15.292  -8.503  1.00 31.02           C  
ANISOU  454  CA  ALA A  70     3719   4273   3795    -76    309   -165       C  
ATOM    455  C   ALA A  70     -35.429  15.255  -9.731  1.00 32.60           C  
ANISOU  455  C   ALA A  70     3902   4455   4029   -119    284   -182       C  
ATOM    456  O   ALA A  70     -36.631  14.918  -9.576  1.00 33.68           O  
ANISOU  456  O   ALA A  70     4028   4578   4190   -165    304   -213       O  
ATOM    457  CB  ALA A  70     -35.355  15.591  -7.271  1.00 34.08           C  
ANISOU  457  CB  ALA A  70     4079   4665   4204    -97    335   -193       C  
ATOM    458  N   GLY A  71     -34.849  15.490 -10.913  1.00 29.56           N  
ANISOU  458  N   GLY A  71     3518   4073   3641   -105    245   -164       N  
ATOM    459  CA  GLY A  71     -35.602  15.307 -12.155  1.00 30.60           C  
ANISOU  459  CA  GLY A  71     3641   4192   3790   -142    221   -177       C  
ATOM    460  C   GLY A  71     -36.540  16.453 -12.470  1.00 29.36           C  
ANISOU  460  C   GLY A  71     3407   4056   3690   -159    176   -201       C  
ATOM    461  O   GLY A  71     -37.158  16.369 -13.521  1.00 27.56           O  
ANISOU  461  O   GLY A  71     3166   3830   3474   -184    148   -211       O  
ATOM    462  N   LEU A  72     -36.619  17.511 -11.675  1.00 28.05           N  
ANISOU  462  N   LEU A  72     3193   3909   3557   -143    167   -208       N  
ATOM    463  CA  LEU A  72     -37.688  18.525 -11.868  1.00 30.18           C  
ANISOU  463  CA  LEU A  72     3390   4193   3882   -155    135   -232       C  
ATOM    464  C   LEU A  72     -37.426  19.424 -13.071  1.00 28.39           C  
ANISOU  464  C   LEU A  72     3142   3974   3671   -133     81   -214       C  
ATOM    465  O   LEU A  72     -38.372  20.191 -13.505  1.00 26.71           O  
ANISOU  465  O   LEU A  72     2874   3775   3499   -135     49   -227       O  
ATOM    466  CB  LEU A  72     -37.882  19.299 -10.554  1.00 30.16           C  
ANISOU  466  CB  LEU A  72     3351   4199   3907   -146    155   -247       C  
ATOM    467  CG  LEU A  72     -38.512  18.466  -9.441  1.00 33.63           C  
ANISOU  467  CG  LEU A  72     3805   4632   4341   -176    208   -271       C  
ATOM    468  CD1 LEU A  72     -38.441  19.190  -8.141  1.00 34.80           C  
ANISOU  468  CD1 LEU A  72     3929   4789   4503   -163    229   -282       C  
ATOM    469  CD2 LEU A  72     -39.946  18.157  -9.762  1.00 37.26           C  
ANISOU  469  CD2 LEU A  72     4230   5095   4833   -220    208   -306       C  
ATOM    470  N   GLU A  73     -36.211  19.365 -13.640  1.00 26.47           N  
ANISOU  470  N   GLU A  73     2940   3725   3393   -108     72   -183       N  
ATOM    471  CA  GLU A  73     -35.885  20.139 -14.819  1.00 26.15           C  
ANISOU  471  CA  GLU A  73     2890   3685   3358    -89     28   -164       C  
ATOM    472  C   GLU A  73     -36.642  19.564 -16.003  1.00 25.53           C  
ANISOU  472  C   GLU A  73     2815   3608   3274   -114      2   -168       C  
ATOM    473  O   GLU A  73     -36.574  20.204 -17.052  1.00 27.11           O  
ANISOU  473  O   GLU A  73     3008   3813   3479    -98    -37   -153       O  
ATOM    474  CB  GLU A  73     -34.367  20.221 -15.107  1.00 26.66           C  
ANISOU  474  CB  GLU A  73     2995   3745   3388    -61     30   -134       C  
ATOM    475  CG  GLU A  73     -33.753  18.954 -15.630  1.00 26.28           C  
ANISOU  475  CG  GLU A  73     3008   3686   3291    -65     45   -119       C  
ATOM    476  CD  GLU A  73     -33.429  17.819 -14.662  1.00 26.57           C  
ANISOU  476  CD  GLU A  73     3084   3718   3294    -66     94   -119       C  
ATOM    477  OE1 GLU A  73     -33.976  17.843 -13.494  1.00 28.19           O  
ANISOU  477  OE1 GLU A  73     3268   3928   3514    -75    118   -138       O  
ATOM    478  OE2 GLU A  73     -32.620  16.907 -15.050  1.00 25.58           O  
ANISOU  478  OE2 GLU A  73     3014   3580   3124    -54    113    -99       O  
ATOM    479  N   ARG A  74     -37.278  18.413 -15.889  1.00 28.13           N  
ANISOU  479  N   ARG A  74     3161   3935   3588   -152     26   -189       N  
ATOM    480  CA  ARG A  74     -38.166  17.878 -16.929  1.00 31.82           C  
ANISOU  480  CA  ARG A  74     3623   4415   4051   -187      3   -206       C  
ATOM    481  C   ARG A  74     -39.269  18.913 -17.212  1.00 34.42           C  
ANISOU  481  C   ARG A  74     3874   4776   4426   -181    -41   -221       C  
ATOM    482  O   ARG A  74     -39.785  18.934 -18.371  1.00 33.99           O  
ANISOU  482  O   ARG A  74     3804   4744   4366   -190    -83   -224       O  
ATOM    483  CB  ARG A  74     -38.700  16.463 -16.665  1.00 34.85           C  
ANISOU  483  CB  ARG A  74     4039   4787   4412   -240     47   -235       C  
ATOM    484  CG  ARG A  74     -39.780  16.318 -15.600  1.00 36.07           C  
ANISOU  484  CG  ARG A  74     4154   4951   4597   -271     78   -273       C  
ATOM    485  CD  ARG A  74     -39.903  14.858 -15.237  1.00 41.50           C  
ANISOU  485  CD  ARG A  74     4903   5612   5252   -317    140   -292       C  
ATOM    486  NE  ARG A  74     -40.966  14.566 -14.275  1.00 44.47           N  
ANISOU  486  NE  ARG A  74     5249   5992   5652   -358    178   -332       N  
ATOM    487  CZ  ARG A  74     -40.890  14.710 -12.942  1.00 46.70           C  
ANISOU  487  CZ  ARG A  74     5534   6263   5947   -344    217   -333       C  
ATOM    488  NH1 ARG A  74     -41.927  14.382 -12.155  1.00 46.99           N  
ANISOU  488  NH1 ARG A  74     5547   6302   6004   -388    257   -373       N  
ATOM    489  NH2 ARG A  74     -39.802  15.203 -12.360  1.00 51.25           N  
ANISOU  489  NH2 ARG A  74     6131   6829   6512   -290    218   -296       N  
ATOM    490  N   PHE A  75     -39.625  19.759 -16.255  1.00 28.91           N  
ANISOU  490  N   PHE A  75     3130   4084   3770   -163    -33   -230       N  
ATOM    491  CA  PHE A  75     -40.730  20.744 -16.427  1.00 29.83           C  
ANISOU  491  CA  PHE A  75     3171   4230   3933   -149    -69   -244       C  
ATOM    492  C   PHE A  75     -40.166  22.086 -16.874  1.00 30.54           C  
ANISOU  492  C   PHE A  75     3254   4311   4037    -94   -100   -210       C  
ATOM    493  O   PHE A  75     -40.925  23.055 -16.999  1.00 29.34           O  
ANISOU  493  O   PHE A  75     3049   4176   3923    -67   -125   -211       O  
ATOM    494  CB  PHE A  75     -41.511  20.882 -15.133  1.00 29.36           C  
ANISOU  494  CB  PHE A  75     3068   4176   3911   -163    -35   -275       C  
ATOM    495  CG  PHE A  75     -42.136  19.596 -14.723  1.00 30.46           C  
ANISOU  495  CG  PHE A  75     3217   4320   4037   -221      2   -311       C  
ATOM    496  CD1 PHE A  75     -43.008  18.929 -15.539  1.00 29.29           C  
ANISOU  496  CD1 PHE A  75     3048   4201   3879   -261    -16   -337       C  
ATOM    497  CD2 PHE A  75     -41.789  19.026 -13.520  1.00 34.33           C  
ANISOU  497  CD2 PHE A  75     3742   4784   4516   -237     59   -319       C  
ATOM    498  CE1 PHE A  75     -43.584  17.755 -15.143  1.00 34.96           C  
ANISOU  498  CE1 PHE A  75     3779   4918   4584   -323     27   -375       C  
ATOM    499  CE2 PHE A  75     -42.373  17.850 -13.109  1.00 36.22           C  
ANISOU  499  CE2 PHE A  75     4000   5019   4741   -291    103   -351       C  
ATOM    500  CZ  PHE A  75     -43.240  17.177 -13.947  1.00 37.13           C  
ANISOU  500  CZ  PHE A  75     4098   5158   4851   -338     91   -380       C  
ATOM    501  N   ARG A  76     -38.843  22.142 -17.160  1.00 30.59           N  
ANISOU  501  N   ARG A  76     3317   4291   4013    -77    -95   -179       N  
ATOM    502  CA  ARG A  76     -38.143  23.244 -17.894  1.00 34.33           C  
ANISOU  502  CA  ARG A  76     3802   4751   4488    -35   -121   -146       C  
ATOM    503  C   ARG A  76     -37.952  24.511 -17.067  1.00 37.24           C  
ANISOU  503  C   ARG A  76     4148   5104   4896     -5   -104   -144       C  
ATOM    504  O   ARG A  76     -37.723  25.559 -17.658  1.00 39.37           O  
ANISOU  504  O   ARG A  76     4420   5361   5177     28   -121   -122       O  
ATOM    505  CB  ARG A  76     -38.839  23.807 -19.141  1.00 40.46           C  
ANISOU  505  CB  ARG A  76     4555   5546   5271    -12   -173   -132       C  
ATOM    506  CG  ARG A  76     -39.549  22.834 -20.067  1.00 46.17           C  
ANISOU  506  CG  ARG A  76     5274   6300   5966    -42   -203   -144       C  
ATOM    507  CD  ARG A  76     -38.879  21.508 -20.269  1.00 55.14           C  
ANISOU  507  CD  ARG A  76     6468   7425   7055    -82   -181   -148       C  
ATOM    508  NE  ARG A  76     -37.612  21.653 -20.947  1.00 57.04           N  
ANISOU  508  NE  ARG A  76     6767   7640   7265    -62   -183   -113       N  
ATOM    509  CZ  ARG A  76     -37.426  21.787 -22.261  1.00 61.64           C  
ANISOU  509  CZ  ARG A  76     7373   8227   7820    -51   -219    -92       C  
ATOM    510  NH1 ARG A  76     -36.183  21.842 -22.704  1.00 60.70           N  
ANISOU  510  NH1 ARG A  76     7309   8080   7673    -38   -208    -64       N  
ATOM    511  NH2 ARG A  76     -38.433  21.851 -23.123  1.00 61.90           N  
ANISOU  511  NH2 ARG A  76     7374   8295   7849    -53   -264    -98       N  
ATOM    512  N   SER A  77     -38.030  24.392 -15.768  1.00 35.95           N  
ANISOU  512  N   SER A  77     3970   4940   4748    -20    -66   -167       N  
ATOM    513  CA ASER A  77     -38.010  25.476 -14.755  0.50 37.63           C  
ANISOU  513  CA ASER A  77     4158   5141   4998     -3    -41   -177       C  
ATOM    514  CA BSER A  77     -38.074  25.478 -14.740  0.50 37.41           C  
ANISOU  514  CA BSER A  77     4127   5113   4971     -3    -41   -179       C  
ATOM    515  C   SER A  77     -37.539  24.815 -13.468  1.00 36.83           C  
ANISOU  515  C   SER A  77     4071   5042   4880    -29      2   -196       C  
ATOM    516  O   SER A  77     -37.704  23.529 -13.365  1.00 40.77           O  
ANISOU  516  O   SER A  77     4588   5551   5351    -56     11   -204       O  
ATOM    517  CB ASER A  77     -39.345  25.984 -14.505  0.50 38.20           C  
ANISOU  517  CB ASER A  77     4172   5225   5117      5    -47   -196       C  
ATOM    518  CB BSER A  77     -39.460  26.021 -14.447  0.50 38.13           C  
ANISOU  518  CB BSER A  77     4157   5217   5112      5    -47   -199       C  
ATOM    519  OG ASER A  77     -40.022  24.958 -13.796  0.50 38.92           O  
ANISOU  519  OG ASER A  77     4246   5335   5207    -32    -28   -226       O  
ATOM    520  OG BSER A  77     -39.881  27.095 -15.289  0.50 38.17           O  
ANISOU  520  OG BSER A  77     4143   5218   5143     48    -77   -179       O  
ATOM    521  N   LEU A  78     -36.929  25.574 -12.582  1.00 34.77           N  
ANISOU  521  N   LEU A  78     3808   4772   4628    -21     29   -203       N  
ATOM    522  CA  LEU A  78     -36.677  25.092 -11.214  1.00 30.85           C  
ANISOU  522  CA  LEU A  78     3316   4286   4117    -41     69   -224       C  
ATOM    523  C   LEU A  78     -37.110  26.196 -10.248  1.00 30.77           C  
ANISOU  523  C   LEU A  78     3270   4270   4150    -37     93   -248       C  
ATOM    524  O   LEU A  78     -37.067  27.389 -10.617  1.00 32.48           O  
ANISOU  524  O   LEU A  78     3474   4469   4395    -16     86   -242       O  
ATOM    525  CB  LEU A  78     -35.196  24.734 -11.103  1.00 32.21           C  
ANISOU  525  CB  LEU A  78     3532   4466   4240    -37     80   -208       C  
ATOM    526  CG  LEU A  78     -34.718  23.558 -11.958  1.00 31.77           C  
ANISOU  526  CG  LEU A  78     3518   4412   4140    -38     66   -185       C  
ATOM    527  CD1 LEU A  78     -33.193  23.512 -11.954  1.00 33.22           C  
ANISOU  527  CD1 LEU A  78     3733   4607   4281    -25     73   -169       C  
ATOM    528  CD2 LEU A  78     -35.286  22.248 -11.463  1.00 30.75           C  
ANISOU  528  CD2 LEU A  78     3404   4286   3991    -59     87   -195       C  
ATOM    529  N   ALA A  79     -37.375  25.819  -9.021  1.00 32.84           N  
ANISOU  529  N   ALA A  79     3523   4543   4410    -56    126   -272       N  
ATOM    530  CA  ALA A  79     -37.857  26.747  -7.970  1.00 33.92           C  
ANISOU  530  CA  ALA A  79     3628   4675   4585    -58    156   -301       C  
ATOM    531  C   ALA A  79     -36.773  27.767  -7.607  1.00 35.64           C  
ANISOU  531  C   ALA A  79     3857   4888   4796    -52    172   -303       C  
ATOM    532  O   ALA A  79     -35.604  27.424  -7.427  1.00 28.01           O  
ANISOU  532  O   ALA A  79     2919   3939   3783    -58    176   -296       O  
ATOM    533  CB  ALA A  79     -38.282  25.984  -6.767  1.00 32.62           C  
ANISOU  533  CB  ALA A  79     3461   4524   4410    -83    191   -325       C  
ATOM    534  N   PRO A  80     -37.148  29.056  -7.458  1.00 39.22           N  
ANISOU  534  N   PRO A  80     4288   5319   5296    -43    186   -317       N  
ATOM    535  CA  PRO A  80     -36.319  30.057  -6.791  1.00 37.40           C  
ANISOU  535  CA  PRO A  80     4064   5082   5063    -51    217   -335       C  
ATOM    536  C   PRO A  80     -35.480  29.530  -5.630  1.00 33.82           C  
ANISOU  536  C   PRO A  80     3623   4666   4561    -77    241   -355       C  
ATOM    537  O   PRO A  80     -34.293  29.779  -5.519  1.00 30.19           O  
ANISOU  537  O   PRO A  80     3179   4224   4066    -86    247   -358       O  
ATOM    538  CB  PRO A  80     -37.361  31.106  -6.349  1.00 44.40           C  
ANISOU  538  CB  PRO A  80     4919   5940   6009    -43    243   -357       C  
ATOM    539  CG  PRO A  80     -38.422  31.080  -7.503  1.00 43.05           C  
ANISOU  539  CG  PRO A  80     4728   5754   5873     -9    207   -332       C  
ATOM    540  CD  PRO A  80     -38.355  29.673  -8.059  1.00 43.77           C  
ANISOU  540  CD  PRO A  80     4830   5872   5925    -18    172   -313       C  
ATOM    541  N   ILE A  81     -36.096  28.792  -4.761  1.00 36.67           N  
ANISOU  541  N   ILE A  81     3975   5042   4915    -89    256   -369       N  
ATOM    542  CA  ILE A  81     -35.421  28.210  -3.580  1.00 37.41           C  
ANISOU  542  CA  ILE A  81     4082   5173   4956   -106    280   -384       C  
ATOM    543  C   ILE A  81     -34.218  27.344  -3.923  1.00 33.51           C  
ANISOU  543  C   ILE A  81     3620   4712   4399    -97    260   -358       C  
ATOM    544  O   ILE A  81     -33.283  27.264  -3.174  1.00 33.59           O  
ANISOU  544  O   ILE A  81     3638   4761   4363   -102    272   -368       O  
ATOM    545  CB  ILE A  81     -36.478  27.385  -2.834  1.00 50.33           C  
ANISOU  545  CB  ILE A  81     5713   6811   6598   -116    299   -395       C  
ATOM    546  CG1 ILE A  81     -37.534  28.339  -2.288  1.00 62.11           C  
ANISOU  546  CG1 ILE A  81     7168   8279   8149   -125    326   -427       C  
ATOM    547  CG2 ILE A  81     -35.837  26.530  -1.776  1.00 52.75           C  
ANISOU  547  CG2 ILE A  81     6046   7155   6841   -124    320   -399       C  
ATOM    548  CD1 ILE A  81     -36.962  29.331  -1.307  1.00 62.07           C  
ANISOU  548  CD1 ILE A  81     7160   8282   8138   -140    359   -458       C  
ATOM    549  N   TYR A  82     -34.279  26.624  -5.033  1.00 29.43           N  
ANISOU  549  N   TYR A  82     3120   4182   3877    -82    230   -326       N  
ATOM    550  CA  TYR A  82     -33.169  25.777  -5.486  1.00 28.53           C  
ANISOU  550  CA  TYR A  82     3039   4094   3707    -68    214   -299       C  
ATOM    551  C   TYR A  82     -31.953  26.662  -5.642  1.00 27.94           C  
ANISOU  551  C   TYR A  82     2959   4039   3618    -68    210   -304       C  
ATOM    552  O   TYR A  82     -30.879  26.339  -5.223  1.00 27.84           O  
ANISOU  552  O   TYR A  82     2954   4069   3552    -63    214   -303       O  
ATOM    553  CB  TYR A  82     -33.538  25.096  -6.808  1.00 28.43           C  
ANISOU  553  CB  TYR A  82     3044   4056   3702    -57    184   -269       C  
ATOM    554  CG  TYR A  82     -32.513  24.138  -7.332  1.00 27.79           C  
ANISOU  554  CG  TYR A  82     3000   3992   3565    -40    173   -240       C  
ATOM    555  CD1 TYR A  82     -32.390  22.877  -6.761  1.00 26.65           C  
ANISOU  555  CD1 TYR A  82     2887   3863   3376    -33    191   -230       C  
ATOM    556  CD2 TYR A  82     -31.687  24.444  -8.397  1.00 26.06           C  
ANISOU  556  CD2 TYR A  82     2791   3772   3338    -29    150   -221       C  
ATOM    557  CE1 TYR A  82     -31.481  21.947  -7.196  1.00 26.88           C  
ANISOU  557  CE1 TYR A  82     2954   3905   3353    -11    187   -201       C  
ATOM    558  CE2 TYR A  82     -30.769  23.510  -8.830  1.00 25.02           C  
ANISOU  558  CE2 TYR A  82     2692   3656   3156    -11    144   -195       C  
ATOM    559  CZ  TYR A  82     -30.656  22.256  -8.262  1.00 24.86           C  
ANISOU  559  CZ  TYR A  82     2702   3651   3092      0    162   -184       C  
ATOM    560  OH  TYR A  82     -29.799  21.309  -8.706  1.00 24.70           O  
ANISOU  560  OH  TYR A  82     2718   3641   3023     24    161   -157       O  
ATOM    561  N   TYR A  83     -32.112  27.776  -6.358  1.00 27.74           N  
ANISOU  561  N   TYR A  83     2921   3981   3636    -71    204   -308       N  
ATOM    562  CA  TYR A  83     -31.010  28.689  -6.701  1.00 28.15           C  
ANISOU  562  CA  TYR A  83     2974   4040   3680    -78    207   -315       C  
ATOM    563  C   TYR A  83     -30.547  29.462  -5.458  1.00 28.51           C  
ANISOU  563  C   TYR A  83     3000   4116   3717   -105    241   -357       C  
ATOM    564  O   TYR A  83     -29.407  29.878  -5.420  1.00 29.63           O  
ANISOU  564  O   TYR A  83     3139   4289   3829   -119    248   -371       O  
ATOM    565  CB  TYR A  83     -31.428  29.721  -7.756  1.00 29.62           C  
ANISOU  565  CB  TYR A  83     3162   4174   3917    -73    200   -306       C  
ATOM    566  CG  TYR A  83     -31.884  29.118  -9.059  1.00 29.54           C  
ANISOU  566  CG  TYR A  83     3169   4139   3914    -49    163   -268       C  
ATOM    567  CD1 TYR A  83     -30.992  28.580  -9.953  1.00 31.29           C  
ANISOU  567  CD1 TYR A  83     3416   4372   4100    -41    143   -242       C  
ATOM    568  CD2 TYR A  83     -33.229  28.990  -9.364  1.00 30.25           C  
ANISOU  568  CD2 TYR A  83     3247   4203   4043    -37    149   -260       C  
ATOM    569  CE1 TYR A  83     -31.417  27.997 -11.146  1.00 30.16           C  
ANISOU  569  CE1 TYR A  83     3291   4208   3958    -24    111   -210       C  
ATOM    570  CE2 TYR A  83     -33.672  28.462 -10.569  1.00 31.95           C  
ANISOU  570  CE2 TYR A  83     3474   4405   4260    -20    114   -230       C  
ATOM    571  CZ  TYR A  83     -32.763  27.946 -11.461  1.00 32.41           C  
ANISOU  571  CZ  TYR A  83     3563   4470   4280    -15     95   -205       C  
ATOM    572  OH  TYR A  83     -33.092  27.366 -12.664  1.00 32.26           O  
ANISOU  572  OH  TYR A  83     3561   4441   4255     -3     61   -177       O  
ATOM    573  N   ARG A  84     -31.469  29.873  -4.600  1.00 30.33           N  
ANISOU  573  N   ARG A  84     3213   4329   3978   -117    265   -383       N  
ATOM    574  CA  ARG A  84     -31.151  30.817  -3.513  1.00 30.97           C  
ANISOU  574  CA  ARG A  84     3278   4429   4059   -148    302   -429       C  
ATOM    575  C   ARG A  84     -30.034  30.267  -2.588  1.00 31.04           C  
ANISOU  575  C   ARG A  84     3282   4515   3995   -159    306   -444       C  
ATOM    576  O   ARG A  84     -30.112  29.086  -2.154  1.00 30.47           O  
ANISOU  576  O   ARG A  84     3219   4474   3884   -139    295   -426       O  
ATOM    577  CB  ARG A  84     -32.433  31.089  -2.748  1.00 34.20           C  
ANISOU  577  CB  ARG A  84     3674   4809   4511   -153    327   -449       C  
ATOM    578  CG  ARG A  84     -32.304  32.112  -1.626  1.00 43.34           C  
ANISOU  578  CG  ARG A  84     4818   5974   5674   -188    372   -499       C  
ATOM    579  CD  ARG A  84     -33.748  32.452  -1.171  1.00 51.21           C  
ANISOU  579  CD  ARG A  84     5802   6926   6728   -185    397   -512       C  
ATOM    580  NE  ARG A  84     -34.398  33.023  -2.389  1.00 57.03           N  
ANISOU  580  NE  ARG A  84     6541   7603   7524   -158    384   -487       N  
ATOM    581  CZ  ARG A  84     -35.681  32.885  -2.763  1.00 61.09           C  
ANISOU  581  CZ  ARG A  84     7041   8083   8087   -131    375   -471       C  
ATOM    582  NH1 ARG A  84     -36.535  32.210  -2.012  1.00 55.47           N  
ANISOU  582  NH1 ARG A  84     6311   7383   7378   -135    383   -481       N  
ATOM    583  NH2 ARG A  84     -36.097  33.444  -3.892  1.00 61.07           N  
ANISOU  583  NH2 ARG A  84     7040   8038   8126   -101    359   -445       N  
ATOM    584  N   GLY A  85     -29.108  31.156  -2.262  1.00 29.84           N  
ANISOU  584  N   GLY A  85     3117   4393   3826   -190    325   -480       N  
ATOM    585  CA  GLY A  85     -27.957  30.967  -1.359  1.00 32.72           C  
ANISOU  585  CA  GLY A  85     3464   4844   4122   -206    329   -506       C  
ATOM    586  C   GLY A  85     -26.836  30.166  -1.948  1.00 29.48           C  
ANISOU  586  C   GLY A  85     3056   4486   3659   -181    298   -478       C  
ATOM    587  O   GLY A  85     -25.890  29.984  -1.233  1.00 32.38           O  
ANISOU  587  O   GLY A  85     3402   4932   3965   -187    298   -498       O  
ATOM    588  N   ALA A  86     -26.869  29.748  -3.254  1.00 28.29           N  
ANISOU  588  N   ALA A  86     2927   4295   3526   -154    273   -435       N  
ATOM    589  CA  ALA A  86     -25.763  29.050  -3.920  1.00 28.86           C  
ANISOU  589  CA  ALA A  86     3002   4410   3551   -130    248   -409       C  
ATOM    590  C   ALA A  86     -24.538  29.958  -3.963  1.00 29.20           C  
ANISOU  590  C   ALA A  86     3019   4499   3576   -166    261   -447       C  
ATOM    591  O   ALA A  86     -24.697  31.175  -4.239  1.00 31.22           O  
ANISOU  591  O   ALA A  86     3274   4709   3876   -204    286   -475       O  
ATOM    592  CB  ALA A  86     -26.200  28.577  -5.304  1.00 27.86           C  
ANISOU  592  CB  ALA A  86     2908   4222   3456   -103    225   -362       C  
ATOM    593  N   SER A  87     -23.367  29.386  -3.678  1.00 29.14           N  
ANISOU  593  N   SER A  87     2990   4579   3502   -152    249   -449       N  
ATOM    594  CA  SER A  87     -22.046  30.023  -3.888  1.00 32.57           C  
ANISOU  594  CA  SER A  87     3392   5072   3909   -183    257   -483       C  
ATOM    595  C   SER A  87     -21.563  29.764  -5.297  1.00 32.00           C  
ANISOU  595  C   SER A  87     3340   4973   3846   -164    242   -448       C  
ATOM    596  O   SER A  87     -20.755  30.578  -5.824  1.00 31.09           O  
ANISOU  596  O   SER A  87     3210   4866   3735   -201    258   -476       O  
ATOM    597  CB  SER A  87     -21.050  29.551  -2.869  1.00 35.58           C  
ANISOU  597  CB  SER A  87     3732   5574   4213   -174    249   -504       C  
ATOM    598  OG  SER A  87     -21.449  29.978  -1.595  1.00 35.08           O  
ANISOU  598  OG  SER A  87     3651   5535   4139   -202    268   -544       O  
ATOM    599  N   GLY A  88     -21.959  28.601  -5.813  1.00 31.34           N  
ANISOU  599  N   GLY A  88     3287   4864   3756   -111    216   -393       N  
ATOM    600  CA  GLY A  88     -21.509  28.105  -7.118  1.00 30.52           C  
ANISOU  600  CA  GLY A  88     3206   4739   3651    -85    199   -355       C  
ATOM    601  C   GLY A  88     -22.593  27.335  -7.845  1.00 28.90           C  
ANISOU  601  C   GLY A  88     3047   4456   3475    -52    182   -305       C  
ATOM    602  O   GLY A  88     -23.561  26.849  -7.229  1.00 26.16           O  
ANISOU  602  O   GLY A  88     2712   4089   3136    -39    180   -295       O  
ATOM    603  N   ALA A  89     -22.387  27.144  -9.164  1.00 28.17           N  
ANISOU  603  N   ALA A  89     2982   4326   3394    -41    170   -275       N  
ATOM    604  CA  ALA A  89     -23.337  26.404 -10.004  1.00 27.35           C  
ANISOU  604  CA  ALA A  89     2922   4156   3313    -16    152   -232       C  
ATOM    605  C   ALA A  89     -22.529  25.689 -11.079  1.00 28.92           C  
ANISOU  605  C   ALA A  89     3143   4360   3483      9    141   -201       C  
ATOM    606  O   ALA A  89     -21.635  26.366 -11.631  1.00 29.98           O  
ANISOU  606  O   ALA A  89     3266   4509   3615     -9    148   -215       O  
ATOM    607  CB  ALA A  89     -24.318  27.396 -10.606  1.00 28.56           C  
ANISOU  607  CB  ALA A  89     3088   4234   3529    -40    153   -237       C  
ATOM    608  N   LEU A  90     -22.831  24.431 -11.337  1.00 26.24           N  
ANISOU  608  N   LEU A  90     2836   4008   3123     45    130   -165       N  
ATOM    609  CA  LEU A  90     -22.306  23.692 -12.504  1.00 27.37           C  
ANISOU  609  CA  LEU A  90     3013   4139   3246     68    122   -132       C  
ATOM    610  C   LEU A  90     -23.438  23.589 -13.520  1.00 27.89           C  
ANISOU  610  C   LEU A  90     3117   4127   3350     60    107   -111       C  
ATOM    611  O   LEU A  90     -24.458  23.008 -13.214  1.00 24.54           O  
ANISOU  611  O   LEU A  90     2708   3677   2936     64    103   -103       O  
ATOM    612  CB  LEU A  90     -21.821  22.291 -12.106  1.00 28.08           C  
ANISOU  612  CB  LEU A  90     3119   4267   3281    117    127   -107       C  
ATOM    613  CG  LEU A  90     -20.386  22.206 -11.559  1.00 31.47           C  
ANISOU  613  CG  LEU A  90     3512   4786   3658    141    135   -117       C  
ATOM    614  CD1 LEU A  90     -20.189  23.002 -10.302  1.00 32.23           C  
ANISOU  614  CD1 LEU A  90     3555   4940   3748    121    141   -157       C  
ATOM    615  CD2 LEU A  90     -20.032  20.746 -11.400  1.00 32.15           C  
ANISOU  615  CD2 LEU A  90     3629   4892   3692    202    142    -80       C  
ATOM    616  N   VAL A  91     -23.250  24.206 -14.681  1.00 26.49           N  
ANISOU  616  N   VAL A  91     2954   3918   3192     46    100   -105       N  
ATOM    617  CA  VAL A  91     -24.239  24.124 -15.786  1.00 24.86           C  
ANISOU  617  CA  VAL A  91     2782   3647   3013     41     80    -84       C  
ATOM    618  C   VAL A  91     -23.736  23.073 -16.752  1.00 24.38           C  
ANISOU  618  C   VAL A  91     2762   3582   2918     62     76    -54       C  
ATOM    619  O   VAL A  91     -22.628  23.267 -17.253  1.00 25.41           O  
ANISOU  619  O   VAL A  91     2894   3732   3028     65     85    -53       O  
ATOM    620  CB  VAL A  91     -24.400  25.483 -16.492  1.00 26.66           C  
ANISOU  620  CB  VAL A  91     3009   3839   3279     19     77    -91       C  
ATOM    621  CG1 VAL A  91     -25.363  25.322 -17.639  1.00 28.52           C  
ANISOU  621  CG1 VAL A  91     3278   4024   3533     23     51    -65       C  
ATOM    622  CG2 VAL A  91     -24.897  26.561 -15.557  1.00 28.67           C  
ANISOU  622  CG2 VAL A  91     3230   4092   3571      0     89   -121       C  
ATOM    623  N   VAL A  92     -24.400  21.913 -16.828  1.00 23.27           N  
ANISOU  623  N   VAL A  92     2651   3423   2764     74     71    -37       N  
ATOM    624  CA  VAL A  92     -23.910  20.732 -17.529  1.00 23.39           C  
ANISOU  624  CA  VAL A  92     2710   3434   2741     96     78    -12       C  
ATOM    625  C   VAL A  92     -24.651  20.648 -18.857  1.00 23.81           C  
ANISOU  625  C   VAL A  92     2799   3438   2808     79     57      0       C  
ATOM    626  O   VAL A  92     -25.900  20.821 -18.927  1.00 23.23           O  
ANISOU  626  O   VAL A  92     2722   3338   2765     60     39     -5       O  
ATOM    627  CB  VAL A  92     -24.130  19.457 -16.705  1.00 25.85           C  
ANISOU  627  CB  VAL A  92     3042   3755   3025    118     97     -4       C  
ATOM    628  CG1 VAL A  92     -23.536  18.210 -17.381  1.00 27.36           C  
ANISOU  628  CG1 VAL A  92     3285   3936   3172    145    114     22       C  
ATOM    629  CG2 VAL A  92     -23.565  19.677 -15.288  1.00 26.96           C  
ANISOU  629  CG2 VAL A  92     3142   3951   3150    136    112    -18       C  
ATOM    630  N   TYR A  93     -23.916  20.358 -19.901  1.00 22.79           N  
ANISOU  630  N   TYR A  93     2702   3300   2655     86     60     17       N  
ATOM    631  CA  TYR A  93     -24.536  19.914 -21.168  1.00 23.64           C  
ANISOU  631  CA  TYR A  93     2853   3367   2759     73     43     32       C  
ATOM    632  C   TYR A  93     -23.892  18.567 -21.540  1.00 24.79           C  
ANISOU  632  C   TYR A  93     3047   3511   2859     92     68     49       C  
ATOM    633  O   TYR A  93     -22.836  18.157 -21.017  1.00 23.87           O  
ANISOU  633  O   TYR A  93     2928   3425   2716    123     94     54       O  
ATOM    634  CB  TYR A  93     -24.422  20.954 -22.269  1.00 23.77           C  
ANISOU  634  CB  TYR A  93     2874   3365   2789     60     24     37       C  
ATOM    635  CG  TYR A  93     -23.019  21.268 -22.715  1.00 22.83           C  
ANISOU  635  CG  TYR A  93     2762   3260   2649     69     43     42       C  
ATOM    636  CD1 TYR A  93     -22.248  22.187 -22.034  1.00 24.38           C  
ANISOU  636  CD1 TYR A  93     2917   3487   2857     67     58     25       C  
ATOM    637  CD2 TYR A  93     -22.456  20.632 -23.822  1.00 25.09           C  
ANISOU  637  CD2 TYR A  93     3095   3533   2904     74     50     60       C  
ATOM    638  CE1 TYR A  93     -20.968  22.490 -22.441  1.00 23.99           C  
ANISOU  638  CE1 TYR A  93     2868   3457   2790     69     79     23       C  
ATOM    639  CE2 TYR A  93     -21.165  20.958 -24.279  1.00 25.06           C  
ANISOU  639  CE2 TYR A  93     3094   3544   2883     79     71     62       C  
ATOM    640  CZ  TYR A  93     -20.419  21.874 -23.567  1.00 25.43           C  
ANISOU  640  CZ  TYR A  93     3094   3625   2942     76     86     43       C  
ATOM    641  OH  TYR A  93     -19.157  22.214 -23.997  1.00 24.81           O  
ANISOU  641  OH  TYR A  93     3011   3566   2847     75    110     38       O  
ATOM    642  N   ASP A  94     -24.393  17.959 -22.586  1.00 26.12           N  
ANISOU  642  N   ASP A  94     3261   3646   3017     77     60     57       N  
ATOM    643  CA  ASP A  94     -23.911  16.673 -23.137  1.00 25.08           C  
ANISOU  643  CA  ASP A  94     3187   3498   2843     89     88     72       C  
ATOM    644  C   ASP A  94     -23.218  17.024 -24.483  1.00 24.64           C  
ANISOU  644  C   ASP A  94     3156   3431   2774     86     81     84       C  
ATOM    645  O   ASP A  94     -23.946  17.512 -25.417  1.00 23.35           O  
ANISOU  645  O   ASP A  94     3001   3247   2622     57     50     83       O  
ATOM    646  CB  ASP A  94     -25.161  15.818 -23.336  1.00 27.00           C  
ANISOU  646  CB  ASP A  94     3461   3710   3085     60     86     64       C  
ATOM    647  CG  ASP A  94     -24.976  14.465 -24.007  1.00 25.38           C  
ANISOU  647  CG  ASP A  94     3327   3476   2841     59    118     73       C  
ATOM    648  OD1 ASP A  94     -23.840  14.157 -24.475  1.00 26.55           O  
ANISOU  648  OD1 ASP A  94     3504   3624   2960     87    141     90       O  
ATOM    649  OD2 ASP A  94     -25.937  13.724 -23.982  1.00 28.39           O  
ANISOU  649  OD2 ASP A  94     3732   3835   3220     31    126     60       O  
ATOM    650  N   ILE A  95     -21.941  16.672 -24.640  1.00 23.96           N  
ANISOU  650  N   ILE A  95     3084   3359   2658    115    111     96       N  
ATOM    651  CA  ILE A  95     -21.172  17.018 -25.865  1.00 25.05           C  
ANISOU  651  CA  ILE A  95     3245   3488   2782    111    112    105       C  
ATOM    652  C   ILE A  95     -21.755  16.262 -27.055  1.00 24.79           C  
ANISOU  652  C   ILE A  95     3276   3413   2728     88    108    112       C  
ATOM    653  O   ILE A  95     -21.483  16.699 -28.166  1.00 27.03           O  
ANISOU  653  O   ILE A  95     3582   3684   3004     75     99    118       O  
ATOM    654  CB  ILE A  95     -19.664  16.746 -25.653  1.00 29.07           C  
ANISOU  654  CB  ILE A  95     3747   4031   3265    149    148    112       C  
ATOM    655  CG1 ILE A  95     -19.355  15.274 -25.366  1.00 30.60           C  
ANISOU  655  CG1 ILE A  95     3980   4220   3423    186    186    126       C  
ATOM    656  CG2 ILE A  95     -19.093  17.683 -24.589  1.00 28.64           C  
ANISOU  656  CG2 ILE A  95     3622   4028   3229    160    146     97       C  
ATOM    657  CD1 ILE A  95     -18.655  14.586 -26.498  1.00 35.58           C  
ANISOU  657  CD1 ILE A  95     4667   4829   4022    196    214    140       C  
ATOM    658  N   THR A  96     -22.506  15.163 -26.822  1.00 24.76           N  
ANISOU  658  N   THR A  96     3303   3390   2713     81    120    109       N  
ATOM    659  CA  THR A  96     -23.178  14.388 -27.903  1.00 24.32           C  
ANISOU  659  CA  THR A  96     3306   3298   2634     48    118    106       C  
ATOM    660  C   THR A  96     -24.535  14.996 -28.316  1.00 27.05           C  
ANISOU  660  C   THR A  96     3633   3641   3003      6     68     92       C  
ATOM    661  O   THR A  96     -25.226  14.397 -29.171  1.00 26.85           O  
ANISOU  661  O   THR A  96     3647   3598   2957    -27     60     83       O  
ATOM    662  CB  THR A  96     -23.357  12.912 -27.505  1.00 26.28           C  
ANISOU  662  CB  THR A  96     3603   3523   2858     52    163    104       C  
ATOM    663  OG1 THR A  96     -24.455  12.736 -26.603  1.00 26.87           O  
ANISOU  663  OG1 THR A  96     3656   3599   2954     33    156     87       O  
ATOM    664  CG2 THR A  96     -22.041  12.325 -27.035  1.00 26.85           C  
ANISOU  664  CG2 THR A  96     3691   3604   2907    107    212    123       C  
ATOM    665  N   ASN A  97     -24.961  16.114 -27.735  1.00 25.58           N  
ANISOU  665  N   ASN A  97     3388   3476   2855      8     35     87       N  
ATOM    666  CA  ASN A  97     -26.331  16.679 -27.903  1.00 26.02           C  
ANISOU  666  CA  ASN A  97     3414   3536   2935    -19    -10     74       C  
ATOM    667  C   ASN A  97     -26.223  18.211 -28.072  1.00 26.82           C  
ANISOU  667  C   ASN A  97     3478   3646   3064     -6    -41     83       C  
ATOM    668  O   ASN A  97     -26.188  18.987 -27.070  1.00 26.19           O  
ANISOU  668  O   ASN A  97     3350   3580   3018      7    -41     78       O  
ATOM    669  CB  ASN A  97     -27.230  16.290 -26.732  1.00 28.36           C  
ANISOU  669  CB  ASN A  97     3679   3841   3255    -29     -5     54       C  
ATOM    670  CG  ASN A  97     -28.659  16.801 -26.827  1.00 31.52           C  
ANISOU  670  CG  ASN A  97     4039   4253   3681    -54    -50     38       C  
ATOM    671  OD1 ASN A  97     -28.987  17.597 -27.666  1.00 31.95           O  
ANISOU  671  OD1 ASN A  97     4085   4313   3740    -56    -89     45       O  
ATOM    672  ND2 ASN A  97     -29.536  16.224 -26.026  1.00 35.19           N  
ANISOU  672  ND2 ASN A  97     4487   4723   4160    -74    -41     16       N  
ATOM    673  N   SER A  98     -26.227  18.715 -29.302  1.00 27.05           N  
ANISOU  673  N   SER A  98     3532   3666   3078    -12    -65     96       N  
ATOM    674  CA  SER A  98     -26.116  20.140 -29.601  1.00 26.66           C  
ANISOU  674  CA  SER A  98     3464   3615   3049      0    -86    109       C  
ATOM    675  C   SER A  98     -27.237  20.923 -28.935  1.00 26.41           C  
ANISOU  675  C   SER A  98     3379   3595   3059      4   -117    100       C  
ATOM    676  O   SER A  98     -26.959  22.016 -28.442  1.00 28.22           O  
ANISOU  676  O   SER A  98     3581   3822   3318     20   -112    103       O  
ATOM    677  CB  SER A  98     -26.158  20.318 -31.100  1.00 30.39           C  
ANISOU  677  CB  SER A  98     3982   4074   3489     -6   -108    126       C  
ATOM    678  OG  SER A  98     -26.226  21.664 -31.463  1.00 31.63           O  
ANISOU  678  OG  SER A  98     4131   4222   3662      9   -127    141       O  
ATOM    679  N   GLU A  99     -28.456  20.393 -28.876  1.00 26.20           N  
ANISOU  679  N   GLU A  99     3336   3581   3036    -12   -143     86       N  
ATOM    680  CA  GLU A  99     -29.601  21.072 -28.243  1.00 28.48           C  
ANISOU  680  CA  GLU A  99     3569   3886   3365     -6   -171     76       C  
ATOM    681  C   GLU A  99     -29.267  21.340 -26.760  1.00 27.46           C  
ANISOU  681  C   GLU A  99     3401   3759   3271      2   -141     63       C  
ATOM    682  O   GLU A  99     -29.694  22.378 -26.267  1.00 27.09           O  
ANISOU  682  O   GLU A  99     3316   3714   3262     17   -151     62       O  
ATOM    683  CB  GLU A  99     -30.885  20.247 -28.429  1.00 35.35           C  
ANISOU  683  CB  GLU A  99     4425   4777   4227    -34   -198     55       C  
ATOM    684  CG  GLU A  99     -32.094  20.853 -27.766  1.00 42.40           C  
ANISOU  684  CG  GLU A  99     5255   5693   5162    -28   -224     41       C  
ATOM    685  CD  GLU A  99     -32.477  22.276 -28.143  1.00 49.90           C  
ANISOU  685  CD  GLU A  99     6180   6644   6134      7   -258     61       C  
ATOM    686  OE1 GLU A  99     -32.136  22.742 -29.291  1.00 47.96           O  
ANISOU  686  OE1 GLU A  99     5971   6389   5861     22   -277     87       O  
ATOM    687  OE2 GLU A  99     -33.161  22.911 -27.277  0.80 57.00           O  
ANISOU  687  OE2 GLU A  99     7027   7552   7077     21   -263     51       O  
ATOM    688  N   SER A 100     -28.566  20.431 -26.079  1.00 25.13           N  
ANISOU  688  N   SER A 100     3119   3465   2962     -1   -103     55       N  
ATOM    689  CA  SER A 100     -28.246  20.536 -24.642  1.00 25.22           C  
ANISOU  689  CA  SER A 100     3096   3488   2997      8    -75     43       C  
ATOM    690  C   SER A 100     -27.342  21.730 -24.410  1.00 25.14           C  
ANISOU  690  C   SER A 100     3069   3477   3003     25    -64     49       C  
ATOM    691  O   SER A 100     -27.482  22.408 -23.356  1.00 25.20           O  
ANISOU  691  O   SER A 100     3035   3495   3042     29    -56     35       O  
ATOM    692  CB  SER A 100     -27.665  19.243 -24.061  1.00 28.23           C  
ANISOU  692  CB  SER A 100     3502   3872   3350      8    -37     39       C  
ATOM    693  OG  SER A 100     -26.326  19.100 -24.440  1.00 29.74           O  
ANISOU  693  OG  SER A 100     3722   4063   3513     25    -13     54       O  
ATOM    694  N   LEU A 101     -26.448  22.030 -25.352  1.00 24.63           N  
ANISOU  694  N   LEU A 101     3038   3401   2917     30    -59     65       N  
ATOM    695  CA  LEU A 101     -25.561  23.209 -25.205  1.00 26.05           C  
ANISOU  695  CA  LEU A 101     3206   3580   3112     37    -41     66       C  
ATOM    696  C   LEU A 101     -26.398  24.507 -25.403  1.00 27.41           C  
ANISOU  696  C   LEU A 101     3363   3732   3319     41    -64     69       C  
ATOM    697  O   LEU A 101     -26.257  25.489 -24.668  1.00 27.24           O  
ANISOU  697  O   LEU A 101     3313   3709   3327     42    -48     58       O  
ATOM    698  CB  LEU A 101     -24.403  23.142 -26.203  1.00 26.86           C  
ANISOU  698  CB  LEU A 101     3350   3673   3180     37    -24     80       C  
ATOM    699  CG  LEU A 101     -23.512  24.386 -26.176  1.00 28.89           C  
ANISOU  699  CG  LEU A 101     3599   3926   3451     34      0     76       C  
ATOM    700  CD1 LEU A 101     -22.918  24.636 -24.795  1.00 26.76           C  
ANISOU  700  CD1 LEU A 101     3280   3690   3197     32     26     50       C  
ATOM    701  CD2 LEU A 101     -22.416  24.331 -27.202  1.00 31.89           C  
ANISOU  701  CD2 LEU A 101     4019   4297   3800     31     19     87       C  
ATOM    702  N   LYS A 102     -27.314  24.518 -26.353  1.00 28.82           N  
ANISOU  702  N   LYS A 102     3559   3898   3492     45    -99     85       N  
ATOM    703  CA  LYS A 102     -28.216  25.698 -26.566  1.00 30.35           C  
ANISOU  703  CA  LYS A 102     3739   4076   3716     62   -123     94       C  
ATOM    704  C   LYS A 102     -28.989  25.954 -25.291  1.00 31.05           C  
ANISOU  704  C   LYS A 102     3773   4177   3847     64   -122     72       C  
ATOM    705  O   LYS A 102     -29.058  27.048 -24.864  1.00 30.88           O  
ANISOU  705  O   LYS A 102     3734   4140   3856     75   -109     70       O  
ATOM    706  CB  LYS A 102     -29.253  25.403 -27.647  1.00 34.73           C  
ANISOU  706  CB  LYS A 102     4308   4635   4252     69   -170    110       C  
ATOM    707  CG  LYS A 102     -28.668  25.376 -29.044  1.00 45.04           C  
ANISOU  707  CG  LYS A 102     5673   5925   5516     70   -176    135       C  
ATOM    708  CD  LYS A 102     -29.751  25.080 -30.099  1.00 52.06           C  
ANISOU  708  CD  LYS A 102     6571   6829   6379     77   -227    148       C  
ATOM    709  CE  LYS A 102     -29.181  24.521 -31.394  1.00 60.39           C  
ANISOU  709  CE  LYS A 102     7686   7877   7380     65   -231    164       C  
ATOM    710  NZ  LYS A 102     -27.926  25.233 -31.748  1.00 60.82           N  
ANISOU  710  NZ  LYS A 102     7783   7897   7427     72   -194    181       N  
ATOM    711  N   LYS A 103     -29.491  24.912 -24.672  1.00 29.54           N  
ANISOU  711  N   LYS A 103     3560   4010   3654     50   -127     55       N  
ATOM    712  CA  LYS A 103     -30.312  25.071 -23.444  1.00 29.34           C  
ANISOU  712  CA  LYS A 103     3483   3998   3667     49   -123     33       C  
ATOM    713  C   LYS A 103     -29.450  25.464 -22.230  1.00 31.51           C  
ANISOU  713  C   LYS A 103     3739   4276   3956     45    -83     15       C  
ATOM    714  O   LYS A 103     -29.997  26.122 -21.320  1.00 29.62           O  
ANISOU  714  O   LYS A 103     3463   4037   3753     48    -75      0       O  
ATOM    715  CB  LYS A 103     -30.984  23.744 -23.157  1.00 32.79           C  
ANISOU  715  CB  LYS A 103     3911   4455   4091     30   -131     18       C  
ATOM    716  CG  LYS A 103     -32.120  23.371 -24.144  1.00 38.75           C  
ANISOU  716  CG  LYS A 103     4666   5220   4836     24   -173     21       C  
ATOM    717  CD  LYS A 103     -33.075  24.500 -24.396  1.00 43.50           C  
ANISOU  717  CD  LYS A 103     5233   5824   5469     50   -204     28       C  
ATOM    718  CE  LYS A 103     -33.805  24.969 -23.162  1.00 49.29           C  
ANISOU  718  CE  LYS A 103     5913   6565   6251     54   -194      7       C  
ATOM    719  NZ  LYS A 103     -34.978  25.858 -23.445  1.00 54.81           N  
ANISOU  719  NZ  LYS A 103     6573   7273   6980     84   -227     12       N  
ATOM    720  N   ALA A 104     -28.145  25.108 -22.246  1.00 27.66           N  
ANISOU  720  N   ALA A 104     3275   3795   3438     39    -57     17       N  
ATOM    721  CA  ALA A 104     -27.205  25.547 -21.186  1.00 25.33           C  
ANISOU  721  CA  ALA A 104     2958   3517   3149     34    -22     -1       C  
ATOM    722  C   ALA A 104     -27.325  27.075 -21.082  1.00 24.53           C  
ANISOU  722  C   ALA A 104     2844   3392   3084     35    -12     -8       C  
ATOM    723  O   ALA A 104     -27.295  27.617 -19.982  1.00 25.47           O  
ANISOU  723  O   ALA A 104     2930   3520   3225     27      9    -32       O  
ATOM    724  CB  ALA A 104     -25.772  25.118 -21.482  1.00 24.78           C  
ANISOU  724  CB  ALA A 104     2910   3462   3040     33      0      2       C  
ATOM    725  N   GLN A 105     -27.412  27.793 -22.181  1.00 27.76           N  
ANISOU  725  N   GLN A 105     3283   3767   3495     44    -22     12       N  
ATOM    726  CA  GLN A 105     -27.465  29.285 -22.134  1.00 30.16           C  
ANISOU  726  CA  GLN A 105     3588   4038   3832     48     -1     10       C  
ATOM    727  C   GLN A 105     -28.767  29.749 -21.447  1.00 30.74           C  
ANISOU  727  C   GLN A 105     3626   4103   3947     63    -12      1       C  
ATOM    728  O   GLN A 105     -28.751  30.715 -20.670  1.00 33.09           O  
ANISOU  728  O   GLN A 105     3908   4387   4275     58     18    -17       O  
ATOM    729  CB  GLN A 105     -27.334  29.841 -23.543  1.00 32.97           C  
ANISOU  729  CB  GLN A 105     3994   4356   4174     62     -9     41       C  
ATOM    730  CG  GLN A 105     -27.381  31.352 -23.603  1.00 36.02           C  
ANISOU  730  CG  GLN A 105     4398   4696   4590     70     20     43       C  
ATOM    731  CD  GLN A 105     -26.747  31.886 -24.853  1.00 39.36           C  
ANISOU  731  CD  GLN A 105     4881   5083   4990     74     33     69       C  
ATOM    732  OE1 GLN A 105     -26.920  31.296 -25.908  1.00 43.43           O  
ANISOU  732  OE1 GLN A 105     5424   5600   5475     89      0     97       O  
ATOM    733  NE2 GLN A 105     -26.005  32.986 -24.733  1.00 41.84           N  
ANISOU  733  NE2 GLN A 105     5217   5363   5315     57     85     57       N  
ATOM    734  N   THR A 106     -29.889  29.073 -21.723  1.00 31.91           N  
ANISOU  734  N   THR A 106     3762   4264   4098     78    -52     12       N  
ATOM    735  CA  THR A 106     -31.177  29.313 -21.005  1.00 33.26           C  
ANISOU  735  CA  THR A 106     3888   4439   4307     90    -63      0       C  
ATOM    736  C   THR A 106     -30.992  29.111 -19.515  1.00 32.75           C  
ANISOU  736  C   THR A 106     3789   4396   4257     68    -34    -33       C  
ATOM    737  O   THR A 106     -31.410  30.001 -18.722  1.00 30.84           O  
ANISOU  737  O   THR A 106     3523   4141   4053     72    -13    -50       O  
ATOM    738  CB  THR A 106     -32.280  28.353 -21.474  1.00 36.81           C  
ANISOU  738  CB  THR A 106     4323   4913   4749     96   -108      7       C  
ATOM    739  OG1 THR A 106     -32.236  28.582 -22.870  1.00 37.54           O  
ANISOU  739  OG1 THR A 106     4453   4991   4819    115   -134     39       O  
ATOM    740  CG2 THR A 106     -33.639  28.640 -20.866  1.00 41.05           C  
ANISOU  740  CG2 THR A 106     4809   5459   5326    110   -120     -5       C  
ATOM    741  N   TRP A 107     -30.326  28.022 -19.091  1.00 29.81           N  
ANISOU  741  N   TRP A 107     3418   4054   3853     47    -27    -43       N  
ATOM    742  CA  TRP A 107     -30.139  27.783 -17.638  1.00 30.22           C  
ANISOU  742  CA  TRP A 107     3440   4132   3910     31      0    -74       C  
ATOM    743  C   TRP A 107     -29.250  28.884 -17.011  1.00 31.32           C  
ANISOU  743  C   TRP A 107     3573   4266   4058     19     37    -94       C  
ATOM    744  O   TRP A 107     -29.485  29.311 -15.833  1.00 35.09           O  
ANISOU  744  O   TRP A 107     4020   4753   4558      8     60   -122       O  
ATOM    745  CB  TRP A 107     -29.586  26.390 -17.399  1.00 30.33           C  
ANISOU  745  CB  TRP A 107     3464   4176   3881     23      1    -73       C  
ATOM    746  CG  TRP A 107     -30.608  25.355 -17.682  1.00 27.77           C  
ANISOU  746  CG  TRP A 107     3142   3854   3553     23    -22    -66       C  
ATOM    747  CD1 TRP A 107     -30.619  24.464 -18.706  1.00 28.29           C  
ANISOU  747  CD1 TRP A 107     3239   3917   3590     22    -42    -48       C  
ATOM    748  CD2 TRP A 107     -31.762  25.089 -16.888  1.00 29.87           C  
ANISOU  748  CD2 TRP A 107     3377   4127   3845     16    -22    -85       C  
ATOM    749  NE1 TRP A 107     -31.715  23.665 -18.631  1.00 29.86           N  
ANISOU  749  NE1 TRP A 107     3429   4121   3793     12    -54    -56       N  
ATOM    750  CE2 TRP A 107     -32.445  24.024 -17.522  1.00 30.90           C  
ANISOU  750  CE2 TRP A 107     3521   4260   3960      8    -43    -78       C  
ATOM    751  CE3 TRP A 107     -32.309  25.680 -15.742  1.00 30.97           C  
ANISOU  751  CE3 TRP A 107     3478   4269   4018     12     -4   -109       C  
ATOM    752  CZ2 TRP A 107     -33.629  23.503 -17.005  1.00 31.99           C  
ANISOU  752  CZ2 TRP A 107     3631   4406   4115     -6    -43    -97       C  
ATOM    753  CZ3 TRP A 107     -33.456  25.134 -15.202  1.00 32.14           C  
ANISOU  753  CZ3 TRP A 107     3601   4425   4183      2     -5   -125       C  
ATOM    754  CH2 TRP A 107     -34.122  24.084 -15.857  1.00 31.13           C  
ANISOU  754  CH2 TRP A 107     3484   4301   4041     -7    -25   -119       C  
ATOM    755  N   ILE A 108     -28.262  29.364 -17.749  1.00 32.53           N  
ANISOU  755  N   ILE A 108     3754   4407   4195     15     48    -85       N  
ATOM    756  CA  ILE A 108     -27.365  30.453 -17.254  1.00 33.39           C  
ANISOU  756  CA  ILE A 108     3860   4513   4312     -6     90   -110       C  
ATOM    757  C   ILE A 108     -28.246  31.709 -17.021  1.00 37.23           C  
ANISOU  757  C   ILE A 108     4342   4955   4848      0    107   -118       C  
ATOM    758  O   ILE A 108     -28.168  32.275 -15.936  1.00 37.48           O  
ANISOU  758  O   ILE A 108     4350   4994   4897    -19    138   -152       O  
ATOM    759  CB  ILE A 108     -26.179  30.644 -18.223  1.00 33.40           C  
ANISOU  759  CB  ILE A 108     3896   4508   4286    -16    102   -100       C  
ATOM    760  CG1 ILE A 108     -25.195  29.426 -18.202  1.00 27.09           C  
ANISOU  760  CG1 ILE A 108     3092   3760   3438    -19     95    -99       C  
ATOM    761  CG2 ILE A 108     -25.485  31.955 -17.900  1.00 35.76           C  
ANISOU  761  CG2 ILE A 108     4196   4790   4599    -44    150   -129       C  
ATOM    762  CD1 ILE A 108     -24.247  29.359 -19.405  1.00 27.12           C  
ANISOU  762  CD1 ILE A 108     3133   3756   3414    -21     99    -80       C  
ATOM    763  N   LYS A 109     -29.101  32.099 -17.956  1.00 40.74           N  
ANISOU  763  N   LYS A 109     4808   5359   5312     30     86    -88       N  
ATOM    764  CA  LYS A 109     -30.030  33.248 -17.728  1.00 44.81           C  
ANISOU  764  CA  LYS A 109     5318   5832   5874     50    102    -90       C  
ATOM    765  C   LYS A 109     -30.964  32.964 -16.539  1.00 42.75           C  
ANISOU  765  C   LYS A 109     5009   5593   5640     49    100   -113       C  
ATOM    766  O   LYS A 109     -31.084  33.833 -15.673  1.00 45.77           O  
ANISOU  766  O   LYS A 109     5379   5959   6052     39    138   -140       O  
ATOM    767  CB  LYS A 109     -30.711  33.623 -19.040  1.00 50.94           C  
ANISOU  767  CB  LYS A 109     6126   6571   6657     93     75    -46       C  
ATOM    768  CG  LYS A 109     -29.768  33.936 -20.213  1.00 54.80           C  
ANISOU  768  CG  LYS A 109     6670   7032   7116     91     83    -23       C  
ATOM    769  CD  LYS A 109     -30.540  34.446 -21.434  1.00 58.37           C  
ANISOU  769  CD  LYS A 109     7157   7446   7572    142     58     21       C  
ATOM    770  CE  LYS A 109     -29.821  34.364 -22.768  1.00 63.74           C  
ANISOU  770  CE  LYS A 109     7893   8110   8213    145     50     53       C  
ATOM    771  NZ  LYS A 109     -28.611  35.215 -22.809  1.00 65.37           N  
ANISOU  771  NZ  LYS A 109     8142   8280   8415    114    110     40       N  
ATOM    772  N   GLU A 110     -31.563  31.789 -16.392  1.00 39.31           N  
ANISOU  772  N   GLU A 110     4548   5193   5193     53     64   -110       N  
ATOM    773  CA  GLU A 110     -32.437  31.526 -15.224  1.00 39.50           C  
ANISOU  773  CA  GLU A 110     4528   5236   5241     48     70   -135       C  
ATOM    774  C   GLU A 110     -31.601  31.653 -13.955  1.00 44.56           C  
ANISOU  774  C   GLU A 110     5157   5899   5872     14    110   -172       C  
ATOM    775  O   GLU A 110     -32.088  32.153 -12.907  1.00 40.01           O  
ANISOU  775  O   GLU A 110     4556   5321   5325      6    137   -201       O  
ATOM    776  CB  GLU A 110     -33.117  30.161 -15.306  1.00 41.27           C  
ANISOU  776  CB  GLU A 110     4736   5495   5451     49     34   -129       C  
ATOM    777  CG  GLU A 110     -34.247  30.009 -14.290  1.00 47.44           C  
ANISOU  777  CG  GLU A 110     5473   6287   6263     47     40   -152       C  
ATOM    778  CD  GLU A 110     -35.355  28.995 -14.574  1.00 51.73           C  
ANISOU  778  CD  GLU A 110     5994   6852   6807     50      7   -148       C  
ATOM    779  OE1 GLU A 110     -35.967  29.183 -15.647  1.00 52.30           O  
ANISOU  779  OE1 GLU A 110     6066   6917   6888     75    -25   -126       O  
ATOM    780  OE2 GLU A 110     -35.625  28.019 -13.702  1.00 43.27           O  
ANISOU  780  OE2 GLU A 110     4907   5805   5725     26     18   -169       O  
ATOM    781  N   LEU A 111     -30.344  31.225 -14.004  1.00 40.38           N  
ANISOU  781  N   LEU A 111     4643   5396   5301     -5    116   -175       N  
ATOM    782  CA  LEU A 111     -29.551  31.158 -12.768  1.00 43.28           C  
ANISOU  782  CA  LEU A 111     4992   5804   5648    -35    146   -211       C  
ATOM    783  C   LEU A 111     -29.272  32.602 -12.378  1.00 42.53           C  
ANISOU  783  C   LEU A 111     4897   5682   5580    -56    189   -240       C  
ATOM    784  O   LEU A 111     -29.399  32.914 -11.162  1.00 47.79           O  
ANISOU  784  O   LEU A 111     5538   6364   6255    -76    217   -276       O  
ATOM    785  CB  LEU A 111     -28.277  30.360 -13.068  1.00 40.17           C  
ANISOU  785  CB  LEU A 111     4609   5450   5200    -43    138   -204       C  
ATOM    786  CG  LEU A 111     -27.213  30.371 -12.023  1.00 45.77           C  
ANISOU  786  CG  LEU A 111     5297   6213   5878    -68    164   -238       C  
ATOM    787  CD1 LEU A 111     -27.757  29.815 -10.706  1.00 47.21           C  
ANISOU  787  CD1 LEU A 111     5452   6427   6055    -69    168   -256       C  
ATOM    788  CD2 LEU A 111     -26.022  29.623 -12.633  1.00 44.19           C  
ANISOU  788  CD2 LEU A 111     5110   6049   5629    -63    153   -222       C  
ATOM    789  N   ARG A 112     -29.058  33.455 -13.362  1.00 42.55           N  
ANISOU  789  N   ARG A 112     4931   5638   5595    -49    199   -224       N  
ATOM    790  CA  ARG A 112     -28.752  34.873 -13.083  1.00 45.97           C  
ANISOU  790  CA  ARG A 112     5377   6033   6053    -72    251   -252       C  
ATOM    791  C   ARG A 112     -29.984  35.648 -12.631  1.00 51.83           C  
ANISOU  791  C   ARG A 112     6112   6731   6846    -53    269   -258       C  
ATOM    792  O   ARG A 112     -29.819  36.538 -11.800  1.00 53.15           O  
ANISOU  792  O   ARG A 112     6277   6885   7031    -81    319   -296       O  
ATOM    793  CB  ARG A 112     -28.142  35.477 -14.331  1.00 48.86           C  
ANISOU  793  CB  ARG A 112     5790   6358   6414    -69    262   -230       C  
ATOM    794  CG  ARG A 112     -26.664  35.083 -14.335  1.00 53.20           C  
ANISOU  794  CG  ARG A 112     6338   6958   6917   -107    270   -249       C  
ATOM    795  CD  ARG A 112     -25.837  35.779 -15.350  1.00 49.04           C  
ANISOU  795  CD  ARG A 112     5855   6396   6382   -121    297   -241       C  
ATOM    796  NE  ARG A 112     -24.405  35.520 -15.119  1.00 45.59           N  
ANISOU  796  NE  ARG A 112     5400   6016   5904   -165    314   -273       N  
ATOM    797  CZ  ARG A 112     -23.550  35.361 -16.097  1.00 42.77           C  
ANISOU  797  CZ  ARG A 112     5068   5661   5521   -170    313   -258       C  
ATOM    798  NH1 ARG A 112     -22.254  35.218 -15.843  1.00 45.93           N  
ANISOU  798  NH1 ARG A 112     5445   6120   5886   -210    333   -292       N  
ATOM    799  NH2 ARG A 112     -24.007  35.248 -17.327  1.00 42.90           N  
ANISOU  799  NH2 ARG A 112     5127   5628   5542   -133    289   -209       N  
ATOM    800  N   ALA A 113     -31.158  35.354 -13.194  1.00 49.51           N  
ANISOU  800  N   ALA A 113     5814   6419   6576     -7    233   -223       N  
ATOM    801  CA  ALA A 113     -32.454  35.851 -12.662  1.00 49.07           C  
ANISOU  801  CA  ALA A 113     5737   6338   6568     18    243   -228       C  
ATOM    802  C   ALA A 113     -32.613  35.479 -11.184  1.00 50.54           C  
ANISOU  802  C   ALA A 113     5883   6563   6755    -11    260   -270       C  
ATOM    803  O   ALA A 113     -33.195  36.259 -10.497  1.00 47.66           O  
ANISOU  803  O   ALA A 113     5509   6172   6427    -11    296   -292       O  
ATOM    804  CB  ALA A 113     -33.597  35.310 -13.486  1.00 52.06           C  
ANISOU  804  CB  ALA A 113     6103   6716   6960     67    191   -189       C  
ATOM    805  N   ASN A 114     -32.095  34.365 -10.665  1.00 48.78           N  
ANISOU  805  N   ASN A 114     5642   6399   6492    -36    242   -281       N  
ATOM    806  CA  ASN A 114     -32.606  33.821  -9.372  1.00 55.26           C  
ANISOU  806  CA  ASN A 114     6427   7254   7313    -50    249   -310       C  
ATOM    807  C   ASN A 114     -31.558  33.808  -8.283  1.00 58.56           C  
ANISOU  807  C   ASN A 114     6838   7715   7694    -94    278   -349       C  
ATOM    808  O   ASN A 114     -31.961  33.637  -7.118  1.00 66.14           O  
ANISOU  808  O   ASN A 114     7774   8697   8656   -108    295   -377       O  
ATOM    809  CB  ASN A 114     -33.147  32.386  -9.436  1.00 53.30           C  
ANISOU  809  CB  ASN A 114     6163   7040   7045    -37    207   -290       C  
ATOM    810  CG  ASN A 114     -34.487  32.349 -10.127  1.00 59.89           C  
ANISOU  810  CG  ASN A 114     6985   7849   7920     -2    181   -267       C  
ATOM    811  OD1 ASN A 114     -34.537  32.275 -11.361  1.00 55.28           O  
ANISOU  811  OD1 ASN A 114     6418   7250   7332     21    149   -233       O  
ATOM    812  ND2 ASN A 114     -35.556  32.438  -9.346  1.00 60.25           N  
ANISOU  812  ND2 ASN A 114     6998   7893   7999      0    195   -286       N  
ATOM    813  N   ALA A 115     -30.277  33.874  -8.620  1.00 55.95           N  
ANISOU  813  N   ALA A 115     6523   7406   7327   -114    282   -353       N  
ATOM    814  CA  ALA A 115     -29.256  33.736  -7.565  1.00 59.98           C  
ANISOU  814  CA  ALA A 115     7016   7978   7794   -152    302   -392       C  
ATOM    815  C   ALA A 115     -28.498  35.050  -7.529  1.00 54.38           C  
ANISOU  815  C   ALA A 115     6318   7250   7093   -191    349   -427       C  
ATOM    816  O   ALA A 115     -28.758  35.928  -8.373  1.00 50.22           O  
ANISOU  816  O   ALA A 115     5821   6657   6603   -181    365   -414       O  
ATOM    817  CB  ALA A 115     -28.377  32.521  -7.807  1.00 65.89           C  
ANISOU  817  CB  ALA A 115     7763   8785   8485   -144    268   -372       C  
ATOM    818  N   ASP A 116     -27.597  35.140  -6.572  1.00 56.02           N  
ANISOU  818  N   ASP A 116     6504   7517   7263   -232    371   -472       N  
ATOM    819  CA  ASP A 116     -26.713  36.294  -6.389  1.00 59.14           C  
ANISOU  819  CA  ASP A 116     6904   7910   7654   -285    420   -519       C  
ATOM    820  C   ASP A 116     -25.944  36.541  -7.691  1.00 58.36           C  
ANISOU  820  C   ASP A 116     6833   7788   7552   -286    418   -498       C  
ATOM    821  O   ASP A 116     -25.442  35.610  -8.334  1.00 52.25           O  
ANISOU  821  O   ASP A 116     6057   7049   6746   -263    378   -466       O  
ATOM    822  CB  ASP A 116     -25.817  36.004  -5.189  1.00 62.56           C  
ANISOU  822  CB  ASP A 116     7298   8439   8032   -325    428   -567       C  
ATOM    823  CG  ASP A 116     -24.893  37.148  -4.907  1.00 67.12           C  
ANISOU  823  CG  ASP A 116     7873   9028   8601   -391    481   -627       C  
ATOM    824  OD1 ASP A 116     -24.519  37.839  -5.880  1.00 66.04           O  
ANISOU  824  OD1 ASP A 116     7766   8841   8484   -404    503   -623       O  
ATOM    825  OD2 ASP A 116     -24.599  37.353  -3.731  1.00 75.69           O  
ANISOU  825  OD2 ASP A 116     8930  10169   9659   -431    503   -679       O  
ATOM    826  N   PRO A 117     -25.822  37.817  -8.114  1.00 63.25           N  
ANISOU  826  N   PRO A 117     7486   8344   8202   -312    468   -516       N  
ATOM    827  CA  PRO A 117     -24.755  38.236  -9.031  1.00 67.18           C  
ANISOU  827  CA  PRO A 117     8007   8833   8683   -338    487   -519       C  
ATOM    828  C   PRO A 117     -23.317  37.751  -8.735  1.00 63.26           C  
ANISOU  828  C   PRO A 117     7472   8435   8126   -378    481   -552       C  
ATOM    829  O   PRO A 117     -22.618  37.591  -9.659  1.00 66.79           O  
ANISOU  829  O   PRO A 117     7933   8884   8557   -377    473   -535       O  
ATOM    830  CB  PRO A 117     -24.795  39.774  -8.916  1.00 71.68           C  
ANISOU  830  CB  PRO A 117     8612   9331   9289   -380    563   -558       C  
ATOM    831  CG  PRO A 117     -26.251  40.084  -8.608  1.00 72.46           C  
ANISOU  831  CG  PRO A 117     8724   9366   9440   -338    568   -539       C  
ATOM    832  CD  PRO A 117     -26.733  38.922  -7.762  1.00 69.17           C  
ANISOU  832  CD  PRO A 117     8257   9017   9004   -316    516   -533       C  
ATOM    833  N   SER A 118     -22.877  37.559  -7.486  1.00 60.90           N  
ANISOU  833  N   SER A 118     7126   8218   7792   -412    486   -601       N  
ATOM    834  CA  SER A 118     -21.491  37.079  -7.165  1.00 62.42           C  
ANISOU  834  CA  SER A 118     7273   8521   7921   -442    476   -633       C  
ATOM    835  C   SER A 118     -21.327  35.555  -7.422  1.00 56.34           C  
ANISOU  835  C   SER A 118     6484   7810   7113   -381    410   -581       C  
ATOM    836  O   SER A 118     -20.254  35.006  -7.160  1.00 53.49           O  
ANISOU  836  O   SER A 118     6082   7544   6697   -389    395   -598       O  
ATOM    837  CB  SER A 118     -21.138  37.374  -5.723  1.00 60.37           C  
ANISOU  837  CB  SER A 118     6968   8338   7631   -492    499   -700       C  
ATOM    838  OG  SER A 118     -21.947  36.553  -4.875  1.00 66.16           O  
ANISOU  838  OG  SER A 118     7685   9095   8356   -450    464   -679       O  
ATOM    839  N   LEU A 119     -22.387  34.832  -7.770  1.00 49.35           N  
ANISOU  839  N   LEU A 119     5622   6877   6251   -323    373   -525       N  
ATOM    840  CA  LEU A 119     -22.287  33.368  -7.952  1.00 41.19           C  
ANISOU  840  CA  LEU A 119     4579   5890   5180   -270    321   -479       C  
ATOM    841  C   LEU A 119     -21.101  33.021  -8.871  1.00 38.18           C  
ANISOU  841  C   LEU A 119     4196   5543   4765   -267    311   -467       C  
ATOM    842  O   LEU A 119     -20.977  33.592  -9.975  1.00 36.38           O  
ANISOU  842  O   LEU A 119     4001   5256   4563   -277    325   -455       O  
ATOM    843  CB  LEU A 119     -23.612  32.952  -8.583  1.00 43.50           C  
ANISOU  843  CB  LEU A 119     4908   6104   5516   -223    296   -426       C  
ATOM    844  CG  LEU A 119     -23.793  31.484  -8.862  1.00 42.62           C  
ANISOU  844  CG  LEU A 119     4802   6015   5377   -172    251   -379       C  
ATOM    845  CD1 LEU A 119     -23.967  30.727  -7.600  1.00 42.03           C  
ANISOU  845  CD1 LEU A 119     4701   5998   5270   -160    243   -388       C  
ATOM    846  CD2 LEU A 119     -25.034  31.256  -9.686  1.00 46.53           C  
ANISOU  846  CD2 LEU A 119     5330   6433   5915   -140    230   -335       C  
ATOM    847  N   ILE A 120     -20.339  31.995  -8.525  1.00 33.57           N  
ANISOU  847  N   ILE A 120     3581   5048   4125   -243    285   -461       N  
ATOM    848  CA  ILE A 120     -19.363  31.351  -9.450  1.00 34.50           C  
ANISOU  848  CA  ILE A 120     3698   5197   4211   -221    269   -436       C  
ATOM    849  C   ILE A 120     -20.062  30.338 -10.350  1.00 32.40           C  
ANISOU  849  C   ILE A 120     3476   4876   3956   -164    235   -370       C  
ATOM    850  O   ILE A 120     -20.529  29.308  -9.833  1.00 31.38           O  
ANISOU  850  O   ILE A 120     3347   4766   3807   -123    211   -345       O  
ATOM    851  CB  ILE A 120     -18.261  30.674  -8.668  1.00 35.48           C  
ANISOU  851  CB  ILE A 120     3769   5443   4268   -209    258   -456       C  
ATOM    852  CG1 ILE A 120     -17.620  31.645  -7.683  1.00 38.63           C  
ANISOU  852  CG1 ILE A 120     4117   5909   4649   -272    289   -528       C  
ATOM    853  CG2 ILE A 120     -17.245  30.060  -9.596  1.00 38.96           C  
ANISOU  853  CG2 ILE A 120     4206   5917   4677   -185    246   -433       C  
ATOM    854  CD1 ILE A 120     -17.094  30.899  -6.527  1.00 46.67           C  
ANISOU  854  CD1 ILE A 120     5085   7043   5602   -247    269   -541       C  
ATOM    855  N   ILE A 121     -20.040  30.578 -11.671  1.00 28.66           N  
ANISOU  855  N   ILE A 121     3040   4342   3506   -164    236   -346       N  
ATOM    856  CA  ILE A 121     -20.789  29.749 -12.625  1.00 27.92           C  
ANISOU  856  CA  ILE A 121     2991   4191   3424   -120    205   -289       C  
ATOM    857  C   ILE A 121     -19.788  29.014 -13.507  1.00 30.51           C  
ANISOU  857  C   ILE A 121     3328   4549   3716    -99    196   -266       C  
ATOM    858  O   ILE A 121     -19.018  29.695 -14.136  1.00 30.70           O  
ANISOU  858  O   ILE A 121     3353   4569   3740   -128    218   -282       O  
ATOM    859  CB  ILE A 121     -21.754  30.602 -13.471  1.00 29.51           C  
ANISOU  859  CB  ILE A 121     3233   4296   3680   -128    210   -273       C  
ATOM    860  CG1 ILE A 121     -22.754  31.371 -12.606  1.00 29.47           C  
ANISOU  860  CG1 ILE A 121     3220   4261   3716   -143    225   -296       C  
ATOM    861  CG2 ILE A 121     -22.490  29.724 -14.462  1.00 31.26           C  
ANISOU  861  CG2 ILE A 121     3494   4474   3908    -87    175   -221       C  
ATOM    862  CD1 ILE A 121     -23.502  32.415 -13.365  1.00 31.41           C  
ANISOU  862  CD1 ILE A 121     3502   4420   4011   -149    239   -286       C  
ATOM    863  N   VAL A 122     -19.832  27.692 -13.496  1.00 27.49           N  
ANISOU  863  N   VAL A 122     2953   4189   3302    -53    172   -232       N  
ATOM    864  CA  VAL A 122     -18.930  26.834 -14.305  1.00 29.88           C  
ANISOU  864  CA  VAL A 122     3267   4516   3568    -24    165   -206       C  
ATOM    865  C   VAL A 122     -19.746  26.090 -15.377  1.00 26.94           C  
ANISOU  865  C   VAL A 122     2953   4074   3209      2    144   -158       C  
ATOM    866  O   VAL A 122     -20.789  25.486 -15.038  1.00 28.53           O  
ANISOU  866  O   VAL A 122     3170   4249   3420     20    128   -140       O  
ATOM    867  CB  VAL A 122     -18.204  25.872 -13.363  1.00 30.72           C  
ANISOU  867  CB  VAL A 122     3339   4713   3620     11    161   -208       C  
ATOM    868  CG1 VAL A 122     -17.432  24.857 -14.169  1.00 34.84           C  
ANISOU  868  CG1 VAL A 122     3879   5252   4106     52    157   -175       C  
ATOM    869  CG2 VAL A 122     -17.268  26.732 -12.468  1.00 35.61           C  
ANISOU  869  CG2 VAL A 122     3894   5413   4221    -23    180   -263       C  
ATOM    870  N   LEU A 123     -19.243  26.038 -16.597  1.00 25.20           N  
ANISOU  870  N   LEU A 123     2760   3829   2983      3    146   -141       N  
ATOM    871  CA  LEU A 123     -19.861  25.262 -17.695  1.00 23.29           C  
ANISOU  871  CA  LEU A 123     2573   3531   2743     25    127    -98       C  
ATOM    872  C   LEU A 123     -19.129  23.952 -17.849  1.00 24.77           C  
ANISOU  872  C   LEU A 123     2770   3755   2884     65    128    -77       C  
ATOM    873  O   LEU A 123     -17.886  23.935 -17.962  1.00 24.01           O  
ANISOU  873  O   LEU A 123     2653   3709   2759     70    144    -86       O  
ATOM    874  CB  LEU A 123     -19.819  26.097 -18.975  1.00 23.68           C  
ANISOU  874  CB  LEU A 123     2655   3526   2813      2    131    -92       C  
ATOM    875  CG  LEU A 123     -20.469  25.495 -20.198  1.00 25.03           C  
ANISOU  875  CG  LEU A 123     2882   3643   2985     18    110    -53       C  
ATOM    876  CD1 LEU A 123     -21.984  25.349 -19.989  1.00 25.10           C  
ANISOU  876  CD1 LEU A 123     2900   3614   3022     23     83    -42       C  
ATOM    877  CD2 LEU A 123     -20.114  26.379 -21.439  1.00 27.27           C  
ANISOU  877  CD2 LEU A 123     3198   3886   3277     -2    120    -47       C  
ATOM    878  N   VAL A 124     -19.872  22.853 -17.880  1.00 24.00           N  
ANISOU  878  N   VAL A 124     2706   3633   2777     92    115    -49       N  
ATOM    879  CA  VAL A 124     -19.268  21.530 -18.042  1.00 24.74           C  
ANISOU  879  CA  VAL A 124     2823   3748   2827    134    124    -24       C  
ATOM    880  C   VAL A 124     -19.891  20.774 -19.215  1.00 24.56           C  
ANISOU  880  C   VAL A 124     2863   3661   2804    138    116      5       C  
ATOM    881  O   VAL A 124     -21.084  20.445 -19.176  1.00 23.26           O  
ANISOU  881  O   VAL A 124     2721   3457   2658    130    102     12       O  
ATOM    882  CB  VAL A 124     -19.413  20.718 -16.759  1.00 26.81           C  
ANISOU  882  CB  VAL A 124     3072   4048   3064    167    129    -22       C  
ATOM    883  CG1 VAL A 124     -18.791  19.348 -16.957  1.00 27.40           C  
ANISOU  883  CG1 VAL A 124     3180   4137   3092    219    145      8       C  
ATOM    884  CG2 VAL A 124     -18.907  21.465 -15.541  1.00 28.26           C  
ANISOU  884  CG2 VAL A 124     3192   4300   3243    160    134    -55       C  
ATOM    885  N   GLY A 125     -19.081  20.476 -20.219  1.00 25.16           N  
ANISOU  885  N   GLY A 125     2964   3734   2859    147    126     19       N  
ATOM    886  CA  GLY A 125     -19.466  19.550 -21.299  1.00 23.83           C  
ANISOU  886  CA  GLY A 125     2859   3515   2677    154    125     46       C  
ATOM    887  C   GLY A 125     -19.188  18.138 -20.904  1.00 23.21           C  
ANISOU  887  C   GLY A 125     2807   3450   2560    198    147     64       C  
ATOM    888  O   GLY A 125     -17.970  17.718 -20.913  1.00 26.29           O  
ANISOU  888  O   GLY A 125     3190   3881   2917    235    170     72       O  
ATOM    889  N   ASN A 126     -20.225  17.381 -20.566  1.00 21.94           N  
ANISOU  889  N   ASN A 126     2676   3257   2403    198    145     72       N  
ATOM    890  CA  ASN A 126     -20.092  15.991 -20.073  1.00 25.34           C  
ANISOU  890  CA  ASN A 126     3144   3689   2796    241    175     91       C  
ATOM    891  C   ASN A 126     -20.208  14.954 -21.201  1.00 26.08           C  
ANISOU  891  C   ASN A 126     3310   3730   2868    242    194    110       C  
ATOM    892  O   ASN A 126     -20.615  15.265 -22.345  1.00 24.48           O  
ANISOU  892  O   ASN A 126     3129   3490   2681    204    176    107       O  
ATOM    893  CB  ASN A 126     -21.109  15.747 -18.970  1.00 25.23           C  
ANISOU  893  CB  ASN A 126     3124   3667   2793    235    175     84       C  
ATOM    894  CG  ASN A 126     -20.974  14.437 -18.238  1.00 26.86           C  
ANISOU  894  CG  ASN A 126     3369   3874   2959    282    212    104       C  
ATOM    895  OD1 ASN A 126     -19.827  14.059 -17.900  1.00 25.17           O  
ANISOU  895  OD1 ASN A 126     3150   3706   2708    337    232    119       O  
ATOM    896  ND2 ASN A 126     -22.128  13.772 -18.089  1.00 24.57           N  
ANISOU  896  ND2 ASN A 126     3120   3536   2677    259    223    102       N  
ATOM    897  N   LYS A 127     -19.843  13.738 -20.880  1.00 26.03           N  
ANISOU  897  N   LYS A 127     3344   3719   2824    286    231    130       N  
ATOM    898  CA  LYS A 127     -19.814  12.545 -21.794  1.00 27.34           C  
ANISOU  898  CA  LYS A 127     3590   3835   2963    295    265    149       C  
ATOM    899  C   LYS A 127     -18.768  12.702 -22.876  1.00 27.77           C  
ANISOU  899  C   LYS A 127     3651   3896   3003    306    270    157       C  
ATOM    900  O   LYS A 127     -18.965  12.154 -23.996  1.00 26.29           O  
ANISOU  900  O   LYS A 127     3524   3658   2804    285    283    162       O  
ATOM    901  CB  LYS A 127     -21.172  12.286 -22.442  1.00 28.08           C  
ANISOU  901  CB  LYS A 127     3726   3867   3075    236    254    136       C  
ATOM    902  CG  LYS A 127     -22.347  12.404 -21.481  1.00 29.72           C  
ANISOU  902  CG  LYS A 127     3913   4070   3307    210    242    120       C  
ATOM    903  CD  LYS A 127     -23.654  11.750 -21.980  1.00 28.32           C  
ANISOU  903  CD  LYS A 127     3783   3838   3137    157    246    106       C  
ATOM    904  CE  LYS A 127     -24.808  12.068 -21.069  1.00 28.98           C  
ANISOU  904  CE  LYS A 127     3831   3926   3251    128    230     85       C  
ATOM    905  NZ  LYS A 127     -26.085  11.585 -21.644  1.00 31.73           N  
ANISOU  905  NZ  LYS A 127     4210   4235   3609     69    228     63       N  
ATOM    906  N   LYS A 128     -17.597  13.257 -22.544  1.00 26.92           N  
ANISOU  906  N   LYS A 128     3489   3850   2886    340    270    157       N  
ATOM    907  CA  LYS A 128     -16.520  13.318 -23.543  1.00 28.88           C  
ANISOU  907  CA  LYS A 128     3744   4109   3119    353    284    163       C  
ATOM    908  C   LYS A 128     -15.966  11.957 -23.905  1.00 28.34           C  
ANISOU  908  C   LYS A 128     3739   4017   3009    404    333    190       C  
ATOM    909  O   LYS A 128     -15.288  11.886 -24.947  1.00 27.15           O  
ANISOU  909  O   LYS A 128     3611   3858   2847    405    349    194       O  
ATOM    910  CB  LYS A 128     -15.391  14.258 -23.160  1.00 32.34           C  
ANISOU  910  CB  LYS A 128     4104   4624   3559    368    276    150       C  
ATOM    911  CG  LYS A 128     -14.497  13.828 -22.048  1.00 38.26           C  
ANISOU  911  CG  LYS A 128     4813   5447   4276    437    295    158       C  
ATOM    912  CD  LYS A 128     -13.466  15.000 -22.002  1.00 44.84           C  
ANISOU  912  CD  LYS A 128     5563   6354   5117    424    282    131       C  
ATOM    913  CE  LYS A 128     -12.028  14.631 -21.940  1.00 54.19           C  
ANISOU  913  CE  LYS A 128     6713   7611   6264    484    308    137       C  
ATOM    914  NZ  LYS A 128     -11.740  14.333 -20.520  1.00 55.65           N  
ANISOU  914  NZ  LYS A 128     6852   7870   6421    540    307    141       N  
ATOM    915  N   ASP A 129     -16.320  10.932 -23.169  1.00 28.11           N  
ANISOU  915  N   ASP A 129     3749   3971   2960    440    361    206       N  
ATOM    916  CA  ASP A 129     -15.953   9.554 -23.518  1.00 29.80           C  
ANISOU  916  CA  ASP A 129     4041   4146   3135    488    418    233       C  
ATOM    917  C   ASP A 129     -16.671   9.110 -24.789  1.00 30.91           C  
ANISOU  917  C   ASP A 129     4258   4206   3279    431    428    227       C  
ATOM    918  O   ASP A 129     -16.217   8.092 -25.362  1.00 31.65           O  
ANISOU  918  O   ASP A 129     4420   4263   3342    463    479    244       O  
ATOM    919  CB  ASP A 129     -16.288   8.570 -22.429  1.00 29.40           C  
ANISOU  919  CB  ASP A 129     4027   4083   3061    535    452    252       C  
ATOM    920  CG  ASP A 129     -17.712   8.629 -21.940  1.00 30.12           C  
ANISOU  920  CG  ASP A 129     4130   4134   3177    479    435    235       C  
ATOM    921  OD1 ASP A 129     -18.060   9.690 -21.282  1.00 29.44           O  
ANISOU  921  OD1 ASP A 129     3971   4092   3122    451    387    215       O  
ATOM    922  OD2 ASP A 129     -18.468   7.735 -22.279  1.00 29.76           O  
ANISOU  922  OD2 ASP A 129     4162   4019   3124    454    467    236       O  
ATOM    923  N   LEU A 130     -17.782   9.748 -25.144  1.00 30.62           N  
ANISOU  923  N   LEU A 130     4213   4143   3275    356    386    203       N  
ATOM    924  CA  LEU A 130     -18.587   9.380 -26.346  1.00 30.93           C  
ANISOU  924  CA  LEU A 130     4318   4119   3314    295    388    192       C  
ATOM    925  C   LEU A 130     -18.082  10.162 -27.576  1.00 31.86           C  
ANISOU  925  C   LEU A 130     4425   4244   3437    269    364    186       C  
ATOM    926  O   LEU A 130     -18.877  10.786 -28.291  1.00 30.68           O  
ANISOU  926  O   LEU A 130     4273   4077   3305    209    324    170       O  
ATOM    927  CB  LEU A 130     -20.071   9.606 -26.062  1.00 31.00           C  
ANISOU  927  CB  LEU A 130     4320   4107   3350    235    355    169       C  
ATOM    928  CG  LEU A 130     -20.672   8.763 -24.928  1.00 34.19           C  
ANISOU  928  CG  LEU A 130     4748   4494   3749    250    387    171       C  
ATOM    929  CD1 LEU A 130     -22.160   9.031 -24.810  1.00 33.23           C  
ANISOU  929  CD1 LEU A 130     4614   4355   3656    181    355    143       C  
ATOM    930  CD2 LEU A 130     -20.425   7.253 -25.158  1.00 35.19           C  
ANISOU  930  CD2 LEU A 130     4970   4566   3834    277    460    187       C  
ATOM    931  N   GLY A 131     -16.785  10.011 -27.880  1.00 34.76           N  
ANISOU  931  N   GLY A 131     4792   4632   3782    317    394    201       N  
ATOM    932  CA  GLY A 131     -16.087  10.803 -28.907  1.00 33.74           C  
ANISOU  932  CA  GLY A 131     4647   4517   3656    299    381    197       C  
ATOM    933  C   GLY A 131     -16.736  10.660 -30.286  1.00 32.55           C  
ANISOU  933  C   GLY A 131     4560   4309   3497    241    374    189       C  
ATOM    934  O   GLY A 131     -16.872  11.684 -31.000  1.00 30.41           O  
ANISOU  934  O   GLY A 131     4269   4043   3241    200    336    179       O  
ATOM    935  N   SER A 132     -17.212   9.468 -30.620  1.00 30.02           N  
ANISOU  935  N   SER A 132     4316   3936   3152    232    409    191       N  
ATOM    936  CA ASER A 132     -17.791   9.208 -31.964  0.75 31.38           C  
ANISOU  936  CA ASER A 132     4553   4060   3307    174    406    179       C  
ATOM    937  CA BSER A 132     -17.803   9.194 -31.959  0.25 30.54           C  
ANISOU  937  CA BSER A 132     4447   3953   3200    174    407    179       C  
ATOM    938  C   SER A 132     -19.100   9.973 -32.162  1.00 29.66           C  
ANISOU  938  C   SER A 132     4311   3843   3113    109    343    159       C  
ATOM    939  O   SER A 132     -19.374  10.387 -33.340  1.00 28.62           O  
ANISOU  939  O   SER A 132     4201   3700   2972     66    316    151       O  
ATOM    940  CB ASER A 132     -17.932   7.703 -32.206  0.75 31.47           C  
ANISOU  940  CB ASER A 132     4655   4016   3284    178    469    180       C  
ATOM    941  CB BSER A 132     -18.017   7.723 -32.175  0.25 30.81           C  
ANISOU  941  CB BSER A 132     4570   3933   3203    175    466    179       C  
ATOM    942  OG ASER A 132     -18.935   7.155 -31.384  0.75 31.14           O  
ANISOU  942  OG ASER A 132     4624   3956   3250    162    473    171       O  
ATOM    943  OG BSER A 132     -16.766   7.070 -32.199  0.25 30.86           O  
ANISOU  943  OG BSER A 132     4604   3937   3185    240    526    201       O  
ATOM    944  N   LEU A 133     -19.842  10.233 -31.076  1.00 27.84           N  
ANISOU  944  N   LEU A 133     4034   3631   2911    107    317    152       N  
ATOM    945  CA  LEU A 133     -21.204  10.853 -31.145  1.00 28.22           C  
ANISOU  945  CA  LEU A 133     4055   3682   2982     52    260    132       C  
ATOM    946  C   LEU A 133     -21.158  12.354 -30.886  1.00 26.73           C  
ANISOU  946  C   LEU A 133     3791   3533   2829     55    209    134       C  
ATOM    947  O   LEU A 133     -22.181  13.038 -30.998  1.00 26.94           O  
ANISOU  947  O   LEU A 133     3791   3567   2878     21    160    122       O  
ATOM    948  CB  LEU A 133     -22.081  10.151 -30.132  1.00 27.66           C  
ANISOU  948  CB  LEU A 133     3985   3601   2921     45    274    120       C  
ATOM    949  CG  LEU A 133     -22.243   8.650 -30.322  1.00 29.61           C  
ANISOU  949  CG  LEU A 133     4316   3799   3134     35    335    115       C  
ATOM    950  CD1 LEU A 133     -23.073   8.076 -29.189  1.00 29.85           C  
ANISOU  950  CD1 LEU A 133     4345   3820   3176     28    353    103       C  
ATOM    951  CD2 LEU A 133     -22.845   8.315 -31.694  1.00 30.63           C  
ANISOU  951  CD2 LEU A 133     4498   3900   3237    -28    327     94       C  
ATOM    952  N   ARG A 134     -19.970  12.887 -30.620  1.00 27.11           N  
ANISOU  952  N   ARG A 134     3808   3609   2883     95    222    147       N  
ATOM    953  CA  ARG A 134     -19.806  14.331 -30.325  1.00 27.74           C  
ANISOU  953  CA  ARG A 134     3822   3723   2996     95    185    144       C  
ATOM    954  C   ARG A 134     -20.571  15.194 -31.330  1.00 26.79           C  
ANISOU  954  C   ARG A 134     3708   3587   2883     53    139    141       C  
ATOM    955  O   ARG A 134     -20.294  15.085 -32.543  1.00 27.78           O  
ANISOU  955  O   ARG A 134     3881   3691   2980     38    145    147       O  
ATOM    956  CB  ARG A 134     -18.347  14.738 -30.362  1.00 27.58           C  
ANISOU  956  CB  ARG A 134     3780   3730   2969    127    211    152       C  
ATOM    957  CG  ARG A 134     -18.124  16.209 -30.144  1.00 26.66           C  
ANISOU  957  CG  ARG A 134     3605   3641   2883    117    185    144       C  
ATOM    958  CD  ARG A 134     -16.663  16.572 -30.133  1.00 27.44           C  
ANISOU  958  CD  ARG A 134     3677   3774   2973    140    217    144       C  
ATOM    959  NE  ARG A 134     -15.966  16.108 -28.940  1.00 28.19           N  
ANISOU  959  NE  ARG A 134     3728   3916   3064    185    240    142       N  
ATOM    960  CZ  ARG A 134     -15.758  16.836 -27.875  1.00 30.00           C  
ANISOU  960  CZ  ARG A 134     3890   4192   3315    192    230    128       C  
ATOM    961  NH1 ARG A 134     -16.300  18.032 -27.798  1.00 28.95           N  
ANISOU  961  NH1 ARG A 134     3729   4054   3214    155    200    114       N  
ATOM    962  NH2 ARG A 134     -15.081  16.347 -26.861  1.00 30.07           N  
ANISOU  962  NH2 ARG A 134     3861   4251   3309    237    251    128       N  
ATOM    963  N   GLN A 135     -21.372  16.143 -30.860  1.00 23.96           N  
ANISOU  963  N   GLN A 135     3302   3241   2559     40     98    134       N  
ATOM    964  CA  GLN A 135     -22.108  17.049 -31.762  1.00 24.26           C  
ANISOU  964  CA  GLN A 135     3345   3270   2604     13     54    136       C  
ATOM    965  C   GLN A 135     -21.596  18.471 -31.615  1.00 28.06           C  
ANISOU  965  C   GLN A 135     3788   3762   3111     23     46    141       C  
ATOM    966  O   GLN A 135     -21.956  19.316 -32.460  1.00 26.91           O  
ANISOU  966  O   GLN A 135     3656   3603   2965     10     18    150       O  
ATOM    967  CB  GLN A 135     -23.615  17.045 -31.514  1.00 23.87           C  
ANISOU  967  CB  GLN A 135     3275   3223   2571     -9     13    124       C  
ATOM    968  CG  GLN A 135     -24.325  15.779 -32.002  1.00 24.81           C  
ANISOU  968  CG  GLN A 135     3439   3327   2659    -37     16    112       C  
ATOM    969  CD  GLN A 135     -25.819  15.758 -31.904  1.00 25.72           C  
ANISOU  969  CD  GLN A 135     3530   3453   2787    -67    -23     94       C  
ATOM    970  OE1 GLN A 135     -26.419  16.673 -31.392  1.00 25.49           O  
ANISOU  970  OE1 GLN A 135     3449   3443   2793    -60    -56     93       O  
ATOM    971  NE2 GLN A 135     -26.456  14.663 -32.308  1.00 27.24           N  
ANISOU  971  NE2 GLN A 135     3759   3637   2952   -102    -16     76       N  
ATOM    972  N   VAL A 136     -20.953  18.773 -30.495  1.00 25.48           N  
ANISOU  972  N   VAL A 136     3413   3461   2806     43     66    133       N  
ATOM    973  CA AVAL A 136     -20.423  20.145 -30.343  0.73 27.10           C  
ANISOU  973  CA AVAL A 136     3585   3676   3036     42     67    131       C  
ATOM    974  CA BVAL A 136     -20.479  20.130 -30.113  0.27 27.28           C  
ANISOU  974  CA BVAL A 136     3599   3702   3063     44     66    129       C  
ATOM    975  C   VAL A 136     -18.955  20.069 -29.971  1.00 27.79           C  
ANISOU  975  C   VAL A 136     3653   3791   3112     59    110    124       C  
ATOM    976  O   VAL A 136     -18.470  19.074 -29.416  1.00 29.26           O  
ANISOU  976  O   VAL A 136     3833   3999   3283     83    134    123       O  
ATOM    977  CB AVAL A 136     -21.229  20.965 -29.320  0.73 28.25           C  
ANISOU  977  CB AVAL A 136     3678   3832   3224     41     43    119       C  
ATOM    978  CB BVAL A 136     -21.200  20.532 -28.805  0.27 27.43           C  
ANISOU  978  CB BVAL A 136     3562   3740   3119     47     49    115       C  
ATOM    979  CG1AVAL A 136     -22.605  21.311 -29.869  0.73 31.74           C  
ANISOU  979  CG1AVAL A 136     4132   4251   3676     28     -1    127       C  
ATOM    980  CG1BVAL A 136     -20.494  21.603 -27.993  0.27 26.82           C  
ANISOU  980  CG1BVAL A 136     3435   3687   3068     50     66    100       C  
ATOM    981  CG2AVAL A 136     -21.304  20.219 -27.999  0.73 27.06           C  
ANISOU  981  CG2AVAL A 136     3491   3709   3080     55     54    107       C  
ATOM    982  CG2BVAL A 136     -22.629  20.960 -29.091  0.27 28.71           C  
ANISOU  982  CG2BVAL A 136     3725   3882   3301     33      6    117       C  
ATOM    983  N   SER A 137     -18.243  21.078 -30.425  1.00 27.01           N  
ANISOU  983  N   SER A 137     3551   3690   3018     47    124    122       N  
ATOM    984  CA  SER A 137     -16.786  21.175 -30.275  1.00 27.17           C  
ANISOU  984  CA  SER A 137     3550   3744   3029     55    167    111       C  
ATOM    985  C   SER A 137     -16.474  21.753 -28.910  1.00 26.59           C  
ANISOU  985  C   SER A 137     3404   3717   2980     58    173     87       C  
ATOM    986  O   SER A 137     -17.316  22.436 -28.267  1.00 26.63           O  
ANISOU  986  O   SER A 137     3384   3715   3017     48    149     79       O  
ATOM    987  CB  SER A 137     -16.188  22.028 -31.383  1.00 27.46           C  
ANISOU  987  CB  SER A 137     3618   3756   3058     31    185    113       C  
ATOM    988  OG  SER A 137     -16.604  23.352 -31.192  1.00 26.36           O  
ANISOU  988  OG  SER A 137     3463   3601   2949     10    175    106       O  
ATOM    989  N   PHE A 138     -15.239  21.565 -28.491  1.00 27.32           N  
ANISOU  989  N   PHE A 138     3460   3859   3059     73    206     72       N  
ATOM    990  CA  PHE A 138     -14.713  22.262 -27.310  1.00 28.69           C  
ANISOU  990  CA  PHE A 138     3561   4089   3249     68    216     43       C  
ATOM    991  C   PHE A 138     -14.930  23.768 -27.491  1.00 27.79           C  
ANISOU  991  C   PHE A 138     3443   3948   3167     24    217     26       C  
ATOM    992  O   PHE A 138     -15.384  24.426 -26.580  1.00 26.87           O  
ANISOU  992  O   PHE A 138     3290   3841   3076     12    207      9       O  
ATOM    993  CB  PHE A 138     -13.252  21.887 -27.133  1.00 28.61           C  
ANISOU  993  CB  PHE A 138     3513   4144   3213     87    252     29       C  
ATOM    994  CG  PHE A 138     -12.656  22.458 -25.894  1.00 30.36           C  
ANISOU  994  CG  PHE A 138     3654   4438   3441     83    260     -5       C  
ATOM    995  CD1 PHE A 138     -12.288  23.790 -25.854  1.00 31.89           C  
ANISOU  995  CD1 PHE A 138     3819   4639   3656     34    277    -38       C  
ATOM    996  CD2 PHE A 138     -12.483  21.691 -24.765  1.00 29.92           C  
ANISOU  996  CD2 PHE A 138     3556   4443   3369    126    254     -6       C  
ATOM    997  CE1 PHE A 138     -11.773  24.309 -24.687  1.00 32.28           C  
ANISOU  997  CE1 PHE A 138     3793   4761   3709     22    285    -77       C  
ATOM    998  CE2 PHE A 138     -11.968  22.234 -23.583  1.00 35.17           C  
ANISOU  998  CE2 PHE A 138     4142   5183   4034    120    257    -41       C  
ATOM    999  CZ  PHE A 138     -11.597  23.550 -23.572  1.00 32.13           C  
ANISOU  999  CZ  PHE A 138     3725   4810   3670     65    273    -79       C  
ATOM   1000  N   GLU A 139     -14.587  24.305 -28.653  1.00 26.59           N  
ANISOU 1000  N   GLU A 139     3334   3758   3009      0    235     32       N  
ATOM   1001  CA  GLU A 139     -14.733  25.773 -28.895  1.00 28.43           C  
ANISOU 1001  CA  GLU A 139     3577   3956   3268    -38    248     20       C  
ATOM   1002  C   GLU A 139     -16.182  26.234 -28.808  1.00 27.56           C  
ANISOU 1002  C   GLU A 139     3488   3796   3185    -36    210     37       C  
ATOM   1003  O   GLU A 139     -16.357  27.349 -28.382  1.00 29.50           O  
ANISOU 1003  O   GLU A 139     3718   4029   3458    -57    221     20       O  
ATOM   1004  CB  GLU A 139     -14.142  26.109 -30.275  1.00 31.74           C  
ANISOU 1004  CB  GLU A 139     4053   4336   3669    -57    277     30       C  
ATOM   1005  CG  GLU A 139     -12.665  25.840 -30.322  1.00 34.38           C  
ANISOU 1005  CG  GLU A 139     4356   4723   3982    -65    321      6       C  
ATOM   1006  CD  GLU A 139     -12.146  24.473 -30.788  1.00 37.28           C  
ANISOU 1006  CD  GLU A 139     4737   5113   4314    -30    324     23       C  
ATOM   1007  OE1 GLU A 139     -12.876  23.417 -30.691  0.80 33.42           O  
ANISOU 1007  OE1 GLU A 139     4266   4615   3814      5    291     48       O  
ATOM   1008  OE2 GLU A 139     -10.946  24.464 -31.113  0.80 34.88           O  
ANISOU 1008  OE2 GLU A 139     4418   4841   3994    -39    365      6       O  
ATOM   1009  N   ASP A 140     -17.161  25.408 -29.187  1.00 29.00           N  
ANISOU 1009  N   ASP A 140     3703   3956   3359    -12    171     66       N  
ATOM   1010  CA  ASP A 140     -18.602  25.746 -28.989  1.00 28.79           C  
ANISOU 1010  CA  ASP A 140     3682   3899   3359     -6    131     78       C  
ATOM   1011  C   ASP A 140     -18.787  26.070 -27.493  1.00 30.25           C  
ANISOU 1011  C   ASP A 140     3802   4117   3574     -7    131     51       C  
ATOM   1012  O   ASP A 140     -19.487  27.045 -27.145  1.00 28.32           O  
ANISOU 1012  O   ASP A 140     3549   3849   3361    -15    125     46       O  
ATOM   1013  CB  ASP A 140     -19.549  24.650 -29.485  1.00 30.37           C  
ANISOU 1013  CB  ASP A 140     3912   4085   3540     12     91    102       C  
ATOM   1014  CG  ASP A 140     -19.664  24.546 -31.007  1.00 33.69           C  
ANISOU 1014  CG  ASP A 140     4400   4468   3931      9     83    129       C  
ATOM   1015  OD1 ASP A 140     -19.364  25.554 -31.659  1.00 33.08           O  
ANISOU 1015  OD1 ASP A 140     4350   4362   3855     -1     98    135       O  
ATOM   1016  OD2 ASP A 140     -19.827  23.434 -31.490  1.00 32.81           O  
ANISOU 1016  OD2 ASP A 140     4315   4358   3791     16     71    139       O  
ATOM   1017  N   GLY A 141     -18.347  25.191 -26.606  1.00 29.31           N  
ANISOU 1017  N   GLY A 141     3643   4050   3443      6    136     38       N  
ATOM   1018  CA  GLY A 141     -18.545  25.428 -25.168  1.00 27.54           C  
ANISOU 1018  CA  GLY A 141     3361   3862   3241      6    135     13       C  
ATOM   1019  C   GLY A 141     -17.763  26.653 -24.674  1.00 29.49           C  
ANISOU 1019  C   GLY A 141     3572   4127   3503    -25    170    -21       C  
ATOM   1020  O   GLY A 141     -18.268  27.433 -23.910  1.00 28.34           O  
ANISOU 1020  O   GLY A 141     3402   3978   3387    -38    170    -38       O  
ATOM   1021  N   GLN A 142     -16.501  26.817 -25.106  1.00 27.98           N  
ANISOU 1021  N   GLN A 142     3378   3959   3291    -40    204    -34       N  
ATOM   1022  CA  GLN A 142     -15.639  27.942 -24.744  1.00 28.77           C  
ANISOU 1022  CA  GLN A 142     3446   4082   3402    -81    245    -75       C  
ATOM   1023  C   GLN A 142     -16.275  29.258 -25.187  1.00 27.88           C  
ANISOU 1023  C   GLN A 142     3373   3897   3322   -109    257    -73       C  
ATOM   1024  O   GLN A 142     -16.211  30.231 -24.432  1.00 28.24           O  
ANISOU 1024  O   GLN A 142     3391   3948   3391   -140    282   -107       O  
ATOM   1025  CB  GLN A 142     -14.314  27.612 -25.428  1.00 33.40           C  
ANISOU 1025  CB  GLN A 142     4032   4700   3956    -87    275    -81       C  
ATOM   1026  CG  GLN A 142     -13.114  28.334 -24.939  1.00 36.20           C  
ANISOU 1026  CG  GLN A 142     4333   5112   4308   -127    319   -131       C  
ATOM   1027  CD  GLN A 142     -11.861  27.912 -25.693  1.00 37.41           C  
ANISOU 1027  CD  GLN A 142     4484   5299   4429   -129    348   -136       C  
ATOM   1028  OE1 GLN A 142     -11.906  27.752 -26.920  1.00 32.28           O  
ANISOU 1028  OE1 GLN A 142     3898   4594   3772   -125    353   -107       O  
ATOM   1029  NE2 GLN A 142     -10.797  27.688 -24.929  1.00 33.93           N  
ANISOU 1029  NE2 GLN A 142     3969   4954   3969   -130    365   -173       N  
ATOM   1030  N   ARG A 143     -16.854  29.291 -26.369  1.00 30.79           N  
ANISOU 1030  N   ARG A 143     3807   4202   3688    -96    243    -35       N  
ATOM   1031  CA  ARG A 143     -17.545  30.498 -26.885  1.00 31.39           C  
ANISOU 1031  CA  ARG A 143     3931   4205   3791   -107    252    -23       C  
ATOM   1032  C   ARG A 143     -18.692  30.856 -25.945  1.00 32.95           C  
ANISOU 1032  C   ARG A 143     4103   4392   4023    -95    229    -26       C  
ATOM   1033  O   ARG A 143     -18.921  32.047 -25.665  1.00 29.21           O  
ANISOU 1033  O   ARG A 143     3636   3883   3578   -113    257    -41       O  
ATOM   1034  CB  ARG A 143     -17.992  30.309 -28.334  1.00 32.95           C  
ANISOU 1034  CB  ARG A 143     4200   4348   3969    -86    233     22       C  
ATOM   1035  CG  ARG A 143     -16.847  30.523 -29.330  1.00 37.60           C  
ANISOU 1035  CG  ARG A 143     4828   4925   4532   -111    276     20       C  
ATOM   1036  CD  ARG A 143     -17.321  30.554 -30.765  1.00 39.80           C  
ANISOU 1036  CD  ARG A 143     5186   5145   4789    -93    261     65       C  
ATOM   1037  NE  ARG A 143     -17.689  29.246 -31.319  1.00 40.17           N  
ANISOU 1037  NE  ARG A 143     5246   5208   4807    -64    216     92       N  
ATOM   1038  CZ  ARG A 143     -16.865  28.435 -32.050  1.00 43.50           C  
ANISOU 1038  CZ  ARG A 143     5689   5645   5194    -67    228     96       C  
ATOM   1039  NH1 ARG A 143     -15.618  28.776 -32.291  1.00 43.52           N  
ANISOU 1039  NH1 ARG A 143     5693   5656   5186    -96    282     75       N  
ATOM   1040  NH2 ARG A 143     -17.275  27.253 -32.484  1.00 44.34           N  
ANISOU 1040  NH2 ARG A 143     5811   5761   5275    -44    192    118       N  
ATOM   1041  N   LEU A 144     -19.405  29.866 -25.412  1.00 30.24           N  
ANISOU 1041  N   LEU A 144     3731   4077   3678    -66    185    -16       N  
ATOM   1042  CA  LEU A 144     -20.564  30.197 -24.557  1.00 29.31           C  
ANISOU 1042  CA  LEU A 144     3591   3950   3596    -54    164    -19       C  
ATOM   1043  C   LEU A 144     -20.057  30.759 -23.241  1.00 27.89           C  
ANISOU 1043  C   LEU A 144     3357   3806   3431    -83    197    -65       C  
ATOM   1044  O   LEU A 144     -20.621  31.719 -22.699  1.00 28.63           O  
ANISOU 1044  O   LEU A 144     3445   3872   3559    -93    211    -80       O  
ATOM   1045  CB  LEU A 144     -21.434  28.957 -24.342  1.00 28.09           C  
ANISOU 1045  CB  LEU A 144     3423   3815   3434    -24    116      0       C  
ATOM   1046  CG  LEU A 144     -22.590  29.195 -23.358  1.00 28.84           C  
ANISOU 1046  CG  LEU A 144     3484   3907   3563    -15     98     -9       C  
ATOM   1047  CD1 LEU A 144     -23.519  30.317 -23.823  1.00 32.07           C  
ANISOU 1047  CD1 LEU A 144     3920   4259   4004     -5     94      6       C  
ATOM   1048  CD2 LEU A 144     -23.423  27.929 -23.205  1.00 31.24           C  
ANISOU 1048  CD2 LEU A 144     3780   4231   3859      7     58      5       C  
ATOM   1049  N   ALA A 145     -18.983  30.163 -22.731  1.00 29.05           N  
ANISOU 1049  N   ALA A 145     3465   4020   3552    -95    210    -90       N  
ATOM   1050  CA  ALA A 145     -18.385  30.606 -21.454  1.00 28.49           C  
ANISOU 1050  CA  ALA A 145     3335   4003   3485   -124    237   -139       C  
ATOM   1051  C   ALA A 145     -17.891  32.048 -21.598  1.00 29.31           C  
ANISOU 1051  C   ALA A 145     3453   4076   3608   -173    290   -171       C  
ATOM   1052  O   ALA A 145     -18.083  32.832 -20.659  1.00 29.03           O  
ANISOU 1052  O   ALA A 145     3391   4043   3595   -199    312   -205       O  
ATOM   1053  CB  ALA A 145     -17.283  29.659 -21.063  1.00 28.16           C  
ANISOU 1053  CB  ALA A 145     3251   4045   3404   -118    238   -154       C  
ATOM   1054  N   ALA A 146     -17.332  32.376 -22.768  1.00 31.16           N  
ANISOU 1054  N   ALA A 146     3733   4274   3832   -186    314   -158       N  
ATOM   1055  CA  ALA A 146     -16.861  33.749 -23.064  1.00 34.16           C  
ANISOU 1055  CA  ALA A 146     4142   4609   4227   -234    374   -185       C  
ATOM   1056  C   ALA A 146     -18.041  34.723 -23.193  1.00 36.92           C  
ANISOU 1056  C   ALA A 146     4540   4873   4615   -223    380   -165       C  
ATOM   1057  O   ALA A 146     -18.052  35.781 -22.515  1.00 35.14           O  
ANISOU 1057  O   ALA A 146     4308   4628   4415   -258    424   -202       O  
ATOM   1058  CB  ALA A 146     -15.990  33.703 -24.306  1.00 35.46           C  
ANISOU 1058  CB  ALA A 146     4347   4757   4366   -247    398   -173       C  
ATOM   1059  N   GLU A 147     -19.037  34.371 -24.013  1.00 37.11           N  
ANISOU 1059  N   GLU A 147     4607   4849   4642   -173    336   -110       N  
ATOM   1060  CA  GLU A 147     -20.247  35.228 -24.220  1.00 37.71           C  
ANISOU 1060  CA  GLU A 147     4725   4849   4750   -146    334    -83       C  
ATOM   1061  C   GLU A 147     -20.914  35.511 -22.875  1.00 40.44           C  
ANISOU 1061  C   GLU A 147     5024   5211   5130   -147    332   -111       C  
ATOM   1062  O   GLU A 147     -21.325  36.659 -22.591  1.00 36.04           O  
ANISOU 1062  O   GLU A 147     4487   4600   4603   -156    371   -121       O  
ATOM   1063  CB  GLU A 147     -21.162  34.503 -25.194  1.00 40.67           C  
ANISOU 1063  CB  GLU A 147     5133   5204   5113    -90    274    -25       C  
ATOM   1064  CG  GLU A 147     -22.463  35.218 -25.541  1.00 49.36           C  
ANISOU 1064  CG  GLU A 147     6270   6242   6240    -48    259      9       C  
ATOM   1065  CD  GLU A 147     -23.314  34.380 -26.505  1.00 58.68           C  
ANISOU 1065  CD  GLU A 147     7472   7424   7401      0    193     59       C  
ATOM   1066  OE1 GLU A 147     -22.865  33.238 -26.910  1.00 60.87           O  
ANISOU 1066  OE1 GLU A 147     7741   7741   7644     -3    166     65       O  
ATOM   1067  OE2 GLU A 147     -24.445  34.823 -26.844  1.00 61.14           O  
ANISOU 1067  OE2 GLU A 147     7803   7699   7727     43    169     91       O  
ATOM   1068  N   GLU A 148     -20.992  34.519 -21.994  1.00 35.85           N  
ANISOU 1068  N   GLU A 148     4381   4698   4540   -141    296   -124       N  
ATOM   1069  CA  GLU A 148     -21.721  34.694 -20.720  1.00 33.86           C  
ANISOU 1069  CA  GLU A 148     4087   4461   4317   -140    292   -148       C  
ATOM   1070  C   GLU A 148     -20.825  35.132 -19.569  1.00 34.38           C  
ANISOU 1070  C   GLU A 148     4106   4575   4380   -193    336   -210       C  
ATOM   1071  O   GLU A 148     -21.351  35.188 -18.457  1.00 36.22           O  
ANISOU 1071  O   GLU A 148     4302   4828   4630   -195    333   -232       O  
ATOM   1072  CB  GLU A 148     -22.488  33.407 -20.420  1.00 33.73           C  
ANISOU 1072  CB  GLU A 148     4039   4483   4292   -101    231   -125       C  
ATOM   1073  CG  GLU A 148     -23.633  33.255 -21.399  1.00 34.65           C  
ANISOU 1073  CG  GLU A 148     4193   4550   4419    -55    191    -75       C  
ATOM   1074  CD  GLU A 148     -24.787  34.271 -21.282  1.00 39.93           C  
ANISOU 1074  CD  GLU A 148     4877   5163   5131    -33    197    -65       C  
ATOM   1075  OE1 GLU A 148     -24.780  35.038 -20.297  1.00 40.38           O  
ANISOU 1075  OE1 GLU A 148     4912   5215   5214    -56    235   -100       O  
ATOM   1076  OE2 GLU A 148     -25.747  34.234 -22.122  1.00 43.18           O  
ANISOU 1076  OE2 GLU A 148     5314   5542   5548      8    162    -24       O  
ATOM   1077  N   GLN A 149     -19.520  35.271 -19.813  1.00 35.03           N  
ANISOU 1077  N   GLN A 149     4184   4687   4436   -234    371   -237       N  
ATOM   1078  CA  GLN A 149     -18.525  35.693 -18.814  1.00 35.33           C  
ANISOU 1078  CA  GLN A 149     4172   4787   4464   -293    413   -303       C  
ATOM   1079  C   GLN A 149     -18.620  34.755 -17.611  1.00 33.09           C  
ANISOU 1079  C   GLN A 149     3820   4588   4163   -277    375   -318       C  
ATOM   1080  O   GLN A 149     -18.767  35.208 -16.479  1.00 34.72           O  
ANISOU 1080  O   GLN A 149     3993   4817   4380   -303    392   -358       O  
ATOM   1081  CB  GLN A 149     -18.765  37.174 -18.504  1.00 38.33           C  
ANISOU 1081  CB  GLN A 149     4580   5104   4879   -334    474   -336       C  
ATOM   1082  CG  GLN A 149     -18.634  38.100 -19.716  1.00 44.13           C  
ANISOU 1082  CG  GLN A 149     5393   5748   5624   -345    520   -317       C  
ATOM   1083  CD  GLN A 149     -18.890  39.513 -19.216  1.00 48.95           C  
ANISOU 1083  CD  GLN A 149     6032   6296   6270   -384    588   -353       C  
ATOM   1084  OE1 GLN A 149     -17.984  40.158 -18.768  1.00 57.59           O  
ANISOU 1084  OE1 GLN A 149     7112   7412   7357   -454    648   -414       O  
ATOM   1085  NE2 GLN A 149     -20.138  39.946 -19.125  1.00 50.36           N  
ANISOU 1085  NE2 GLN A 149     6241   6407   6483   -341    581   -322       N  
ATOM   1086  N   LEU A 150     -18.465  33.454 -17.833  1.00 30.60           N  
ANISOU 1086  N   LEU A 150     3490   4319   3817   -237    329   -287       N  
ATOM   1087  CA  LEU A 150     -18.504  32.471 -16.746  1.00 30.23           C  
ANISOU 1087  CA  LEU A 150     3388   4348   3747   -214    297   -294       C  
ATOM   1088  C   LEU A 150     -17.115  32.393 -16.080  1.00 32.39           C  
ANISOU 1088  C   LEU A 150     3602   4722   3981   -247    318   -343       C  
ATOM   1089  O   LEU A 150     -16.169  33.003 -16.629  1.00 31.01           O  
ANISOU 1089  O   LEU A 150     3430   4551   3798   -287    355   -368       O  
ATOM   1090  CB  LEU A 150     -18.936  31.125 -17.308  1.00 30.22           C  
ANISOU 1090  CB  LEU A 150     3406   4346   3729   -157    248   -240       C  
ATOM   1091  CG  LEU A 150     -20.247  31.081 -18.083  1.00 28.84           C  
ANISOU 1091  CG  LEU A 150     3282   4089   3586   -127    221   -195       C  
ATOM   1092  CD1 LEU A 150     -20.552  29.627 -18.503  1.00 28.37           C  
ANISOU 1092  CD1 LEU A 150     3234   4042   3501    -82    179   -154       C  
ATOM   1093  CD2 LEU A 150     -21.383  31.685 -17.272  1.00 29.84           C  
ANISOU 1093  CD2 LEU A 150     3399   4185   3751   -128    221   -206       C  
ATOM   1094  N   ALA A 151     -17.022  31.685 -14.946  1.00 29.65           N  
ANISOU 1094  N   ALA A 151     3205   4454   3607   -229    296   -356       N  
ATOM   1095  CA  ALA A 151     -15.812  31.497 -14.120  1.00 31.48           C  
ANISOU 1095  CA  ALA A 151     3367   4799   3792   -247    305   -401       C  
ATOM   1096  C   ALA A 151     -14.913  30.464 -14.779  1.00 33.26           C  
ANISOU 1096  C   ALA A 151     3585   5075   3978   -209    289   -374       C  
ATOM   1097  O   ALA A 151     -13.643  30.543 -14.694  1.00 30.79           O  
ANISOU 1097  O   ALA A 151     3222   4844   3631   -231    307   -411       O  
ATOM   1098  CB  ALA A 151     -16.226  31.075 -12.732  1.00 31.71           C  
ANISOU 1098  CB  ALA A 151     3358   4884   3806   -229    285   -413       C  
ATOM   1099  N   ALA A 152     -15.487  29.449 -15.420  1.00 28.61           N  
ANISOU 1099  N   ALA A 152     3038   4444   3389   -152    256   -315       N  
ATOM   1100  CA  ALA A 152     -14.643  28.347 -15.962  1.00 26.40           C  
ANISOU 1100  CA  ALA A 152     2753   4211   3067   -109    244   -289       C  
ATOM   1101  C   ALA A 152     -15.440  27.484 -16.913  1.00 27.07           C  
ANISOU 1101  C   ALA A 152     2902   4220   3162    -65    219   -228       C  
ATOM   1102  O   ALA A 152     -16.708  27.567 -16.906  1.00 25.72           O  
ANISOU 1102  O   ALA A 152     2767   3981   3025    -60    203   -208       O  
ATOM   1103  CB  ALA A 152     -14.131  27.504 -14.821  1.00 28.22           C  
ANISOU 1103  CB  ALA A 152     2926   4545   3250    -71    228   -297       C  
ATOM   1104  N   PHE A 153     -14.709  26.744 -17.736  1.00 26.76           N  
ANISOU 1104  N   PHE A 153     2876   4196   3095    -37    220   -205       N  
ATOM   1105  CA  PHE A 153     -15.248  25.789 -18.730  1.00 24.29           C  
ANISOU 1105  CA  PHE A 153     2625   3822   2781      1    201   -152       C  
ATOM   1106  C   PHE A 153     -14.398  24.538 -18.695  1.00 27.38           C  
ANISOU 1106  C   PHE A 153     3004   4275   3124     53    200   -134       C  
ATOM   1107  O   PHE A 153     -13.157  24.662 -18.803  1.00 26.43           O  
ANISOU 1107  O   PHE A 153     2844   4219   2979     49    220   -156       O  
ATOM   1108  CB  PHE A 153     -15.229  26.408 -20.118  1.00 25.72           C  
ANISOU 1108  CB  PHE A 153     2856   3935   2982    -27    214   -142       C  
ATOM   1109  CG  PHE A 153     -15.605  25.406 -21.177  1.00 26.17           C  
ANISOU 1109  CG  PHE A 153     2971   3943   3028      7    197    -95       C  
ATOM   1110  CD1 PHE A 153     -16.845  24.735 -21.137  1.00 26.83           C  
ANISOU 1110  CD1 PHE A 153     3090   3982   3122     32    167    -64       C  
ATOM   1111  CD2 PHE A 153     -14.739  25.112 -22.187  1.00 27.73           C  
ANISOU 1111  CD2 PHE A 153     3189   4141   3203     12    214    -84       C  
ATOM   1112  CE1 PHE A 153     -17.150  23.740 -22.062  1.00 26.24           C  
ANISOU 1112  CE1 PHE A 153     3068   3870   3032     57    155    -27       C  
ATOM   1113  CE2 PHE A 153     -15.062  24.131 -23.121  1.00 28.52           C  
ANISOU 1113  CE2 PHE A 153     3346   4200   3289     41    202    -44       C  
ATOM   1114  CZ  PHE A 153     -16.306  23.518 -23.104  1.00 26.64           C  
ANISOU 1114  CZ  PHE A 153     3144   3917   3060     60    172    -17       C  
ATOM   1115  N   TYR A 154     -15.050  23.387 -18.723  1.00 26.20           N  
ANISOU 1115  N   TYR A 154     2893   4098   2964     99    182    -94       N  
ATOM   1116  CA  TYR A 154     -14.374  22.069 -18.768  1.00 28.58           C  
ANISOU 1116  CA  TYR A 154     3200   4439   3219    160    187    -67       C  
ATOM   1117  C   TYR A 154     -15.169  21.125 -19.663  1.00 26.59           C  
ANISOU 1117  C   TYR A 154     3025   4108   2970    181    179    -24       C  
ATOM   1118  O   TYR A 154     -16.407  21.178 -19.637  1.00 26.37           O  
ANISOU 1118  O   TYR A 154     3027   4020   2970    165    162    -15       O  
ATOM   1119  CB  TYR A 154     -14.257  21.387 -17.406  1.00 29.55           C  
ANISOU 1119  CB  TYR A 154     3287   4631   3309    206    182    -66       C  
ATOM   1120  CG  TYR A 154     -13.664  22.257 -16.315  1.00 29.70           C  
ANISOU 1120  CG  TYR A 154     3227   4736   3319    182    184   -112       C  
ATOM   1121  CD1 TYR A 154     -14.479  23.148 -15.636  1.00 28.90           C  
ANISOU 1121  CD1 TYR A 154     3113   4615   3252    138    176   -139       C  
ATOM   1122  CD2 TYR A 154     -12.313  22.225 -16.015  1.00 31.76           C  
ANISOU 1122  CD2 TYR A 154     3426   5099   3540    201    195   -134       C  
ATOM   1123  CE1 TYR A 154     -13.966  23.929 -14.600  1.00 29.40           C  
ANISOU 1123  CE1 TYR A 154     3108   4757   3305    111    181   -186       C  
ATOM   1124  CE2 TYR A 154     -11.793  23.007 -14.981  1.00 32.52           C  
ANISOU 1124  CE2 TYR A 154     3447   5285   3625    174    196   -183       C  
ATOM   1125  CZ  TYR A 154     -12.611  23.885 -14.310  1.00 29.25           C  
ANISOU 1125  CZ  TYR A 154     3026   4844   3242    124    190   -211       C  
ATOM   1126  OH  TYR A 154     -12.173  24.674 -13.261  1.00 31.89           O  
ANISOU 1126  OH  TYR A 154     3290   5261   3563     89    194   -264       O  
ATOM   1127  N   GLU A 155     -14.467  20.163 -20.263  1.00 24.96           N  
ANISOU 1127  N   GLU A 155     2843   3910   2730    222    195      0       N  
ATOM   1128  CA  GLU A 155     -15.110  18.929 -20.752  1.00 26.26           C  
ANISOU 1128  CA  GLU A 155     3077   4017   2882    253    196     38       C  
ATOM   1129  C   GLU A 155     -14.765  17.828 -19.757  1.00 27.74           C  
ANISOU 1129  C   GLU A 155     3256   4253   3029    318    208     54       C  
ATOM   1130  O   GLU A 155     -13.573  17.780 -19.297  1.00 29.74           O  
ANISOU 1130  O   GLU A 155     3457   4589   3250    354    221     47       O  
ATOM   1131  CB  GLU A 155     -14.703  18.601 -22.187  1.00 26.93           C  
ANISOU 1131  CB  GLU A 155     3211   4062   2958    251    210     55       C  
ATOM   1132  CG  GLU A 155     -15.385  19.507 -23.189  1.00 27.42           C  
ANISOU 1132  CG  GLU A 155     3302   4059   3055    194    194     49       C  
ATOM   1133  CD  GLU A 155     -15.166  19.056 -24.607  1.00 30.53           C  
ANISOU 1133  CD  GLU A 155     3756   4407   3435    192    206     69       C  
ATOM   1134  OE1 GLU A 155     -14.288  18.179 -24.833  1.00 29.57           O  
ANISOU 1134  OE1 GLU A 155     3645   4308   3279    232    233     82       O  
ATOM   1135  OE2 GLU A 155     -15.788  19.673 -25.490  1.00 29.06           O  
ANISOU 1135  OE2 GLU A 155     3602   4168   3269    153    191     70       O  
ATOM   1136  N   ALA A 156     -15.710  16.929 -19.478  1.00 26.52           N  
ANISOU 1136  N   ALA A 156     3151   4052   2871    336    209     77       N  
ATOM   1137  CA  ALA A 156     -15.543  15.892 -18.451  1.00 26.74           C  
ANISOU 1137  CA  ALA A 156     3185   4114   2860    400    225     97       C  
ATOM   1138  C   ALA A 156     -16.228  14.620 -18.901  1.00 27.14           C  
ANISOU 1138  C   ALA A 156     3321   4090   2899    419    247    129       C  
ATOM   1139  O   ALA A 156     -16.979  14.633 -19.836  1.00 25.33           O  
ANISOU 1139  O   ALA A 156     3135   3792   2694    376    240    129       O  
ATOM   1140  CB  ALA A 156     -16.052  16.371 -17.128  1.00 26.16           C  
ANISOU 1140  CB  ALA A 156     3069   4075   2796    390    209     79       C  
ATOM   1141  N   SER A 157     -15.976  13.544 -18.201  1.00 27.46           N  
ANISOU 1141  N   SER A 157     3386   4146   2898    484    274    155       N  
ATOM   1142  CA  SER A 157     -16.694  12.251 -18.277  1.00 25.95           C  
ANISOU 1142  CA  SER A 157     3282   3885   2691    504    306    182       C  
ATOM   1143  C   SER A 157     -16.957  11.818 -16.830  1.00 27.77           C  
ANISOU 1143  C   SER A 157     3510   4143   2899    545    317    192       C  
ATOM   1144  O   SER A 157     -16.000  11.364 -16.100  1.00 28.46           O  
ANISOU 1144  O   SER A 157     3579   4295   2938    623    335    212       O  
ATOM   1145  CB  SER A 157     -15.998  11.158 -19.059  1.00 27.12           C  
ANISOU 1145  CB  SER A 157     3492   4008   2804    554    348    212       C  
ATOM   1146  OG  SER A 157     -16.748   9.933 -18.982  1.00 27.37           O  
ANISOU 1146  OG  SER A 157     3612   3967   2819    567    387    234       O  
ATOM   1147  N   ALA A 158     -18.216  11.888 -16.414  1.00 26.36           N  
ANISOU 1147  N   ALA A 158     3348   3919   2746    499    310    179       N  
ATOM   1148  CA  ALA A 158     -18.647  11.299 -15.114  1.00 28.07           C  
ANISOU 1148  CA  ALA A 158     3583   4142   2939    532    330    191       C  
ATOM   1149  C   ALA A 158     -18.408   9.788 -15.200  1.00 31.95           C  
ANISOU 1149  C   ALA A 158     4162   4592   3384    596    387    232       C  
ATOM   1150  O   ALA A 158     -17.995   9.170 -14.181  1.00 34.57           O  
ANISOU 1150  O   ALA A 158     4506   4957   3669    668    413    257       O  
ATOM   1151  CB  ALA A 158     -20.076  11.589 -14.791  1.00 28.74           C  
ANISOU 1151  CB  ALA A 158     3675   4179   3065    466    319    168       C  
ATOM   1152  N   LYS A 159     -18.631   9.199 -16.370  1.00 32.20           N  
ANISOU 1152  N   LYS A 159     4259   4553   3423    574    410    238       N  
ATOM   1153  CA  LYS A 159     -18.462   7.744 -16.485  1.00 34.23           C  
ANISOU 1153  CA  LYS A 159     4611   4758   3637    629    474    274       C  
ATOM   1154  C   LYS A 159     -17.016   7.307 -16.270  1.00 35.55           C  
ANISOU 1154  C   LYS A 159     4770   4985   3753    732    496    309       C  
ATOM   1155  O   LYS A 159     -16.809   6.352 -15.571  1.00 36.33           O  
ANISOU 1155  O   LYS A 159     4919   5076   3806    805    542    343       O  
ATOM   1156  CB  LYS A 159     -18.918   7.284 -17.848  1.00 33.84           C  
ANISOU 1156  CB  LYS A 159     4627   4627   3604    577    493    267       C  
ATOM   1157  CG  LYS A 159     -18.824   5.790 -17.975  1.00 37.63           C  
ANISOU 1157  CG  LYS A 159     5215   5042   4042    625    568    299       C  
ATOM   1158  CD  LYS A 159     -19.288   5.383 -19.293  1.00 40.11           C  
ANISOU 1158  CD  LYS A 159     5589   5280   4368    565    586    285       C  
ATOM   1159  CE  LYS A 159     -18.733   4.023 -19.599  1.00 49.75           C  
ANISOU 1159  CE  LYS A 159     6910   6449   5544    627    664    319       C  
ATOM   1160  NZ  LYS A 159     -19.293   3.609 -20.892  1.00 53.77           N  
ANISOU 1160  NZ  LYS A 159     7483   6882   6064    555    684    297       N  
ATOM   1161  N   ASP A 160     -16.054   7.946 -16.904  1.00 36.38           N  
ANISOU 1161  N   ASP A 160     4816   5144   3863    740    469    302       N  
ATOM   1162  CA  ASP A 160     -14.640   7.556 -16.820  1.00 37.80           C  
ANISOU 1162  CA  ASP A 160     4977   5389   3995    837    489    331       C  
ATOM   1163  C   ASP A 160     -13.957   8.314 -15.684  1.00 37.48           C  
ANISOU 1163  C   ASP A 160     4836   5468   3937    875    452    322       C  
ATOM   1164  O   ASP A 160     -12.731   8.166 -15.545  1.00 41.46           O  
ANISOU 1164  O   ASP A 160     5300   6051   4401    953    457    339       O  
ATOM   1165  CB  ASP A 160     -13.950   7.900 -18.136  1.00 39.50           C  
ANISOU 1165  CB  ASP A 160     5175   5605   4225    816    482    320       C  
ATOM   1166  CG  ASP A 160     -14.347   7.050 -19.333  1.00 43.44           C  
ANISOU 1166  CG  ASP A 160     5774   6001   4729    792    524    330       C  
ATOM   1167  OD1 ASP A 160     -15.038   6.012 -19.137  1.00 43.44           O  
ANISOU 1167  OD1 ASP A 160     5863   5926   4713    802    570    349       O  
ATOM   1168  OD2 ASP A 160     -13.907   7.457 -20.475  1.00 47.83           O  
ANISOU 1168  OD2 ASP A 160     6318   6554   5302    760    514    317       O  
ATOM   1169  N   ASN A 161     -14.670   9.148 -14.948  1.00 34.54           N  
ANISOU 1169  N   ASN A 161     4417   5113   3590    819    414    293       N  
ATOM   1170  CA  ASN A 161     -14.082  10.004 -13.884  1.00 38.71           C  
ANISOU 1170  CA  ASN A 161     4846   5756   4103    838    376    274       C  
ATOM   1171  C   ASN A 161     -12.933  10.845 -14.454  1.00 37.74           C  
ANISOU 1171  C   ASN A 161     4638   5713   3985    832    350    251       C  
ATOM   1172  O   ASN A 161     -11.803  10.868 -13.885  1.00 37.80           O  
ANISOU 1172  O   ASN A 161     4583   5830   3949    900    345    256       O  
ATOM   1173  CB  ASN A 161     -13.530   9.140 -12.739  1.00 41.48           C  
ANISOU 1173  CB  ASN A 161     5209   6165   4386    947    402    314       C  
ATOM   1174  CG  ASN A 161     -13.139   9.965 -11.543  1.00 44.76           C  
ANISOU 1174  CG  ASN A 161     5529   6697   4781    956    362    290       C  
ATOM   1175  OD1 ASN A 161     -13.547  11.114 -11.386  1.00 43.45           O  
ANISOU 1175  OD1 ASN A 161     5303   6548   4656    874    323    245       O  
ATOM   1176  ND2 ASN A 161     -12.369   9.345 -10.666  1.00 47.45           N  
ANISOU 1176  ND2 ASN A 161     5859   7116   5053   1061    375    323       N  
ATOM   1177  N   ASN A 162     -13.162  11.463 -15.589  1.00 32.81           N  
ANISOU 1177  N   ASN A 162     4014   5041   3409    757    337    227       N  
ATOM   1178  CA  ASN A 162     -12.150  12.322 -16.252  1.00 33.90           C  
ANISOU 1178  CA  ASN A 162     4081   5240   3557    736    319    200       C  
ATOM   1179  C   ASN A 162     -12.524  13.789 -16.048  1.00 33.05           C  
ANISOU 1179  C   ASN A 162     3906   5155   3495    648    279    150       C  
ATOM   1180  O   ASN A 162     -13.632  14.198 -16.464  1.00 31.71           O  
ANISOU 1180  O   ASN A 162     3770   4904   3371    578    266    138       O  
ATOM   1181  CB  ASN A 162     -12.011  11.856 -17.682  1.00 39.10           C  
ANISOU 1181  CB  ASN A 162     4800   5828   4227    728    344    214       C  
ATOM   1182  CG  ASN A 162     -10.934  12.620 -18.418  1.00 45.82           C  
ANISOU 1182  CG  ASN A 162     5588   6735   5084    711    336    190       C  
ATOM   1183  OD1 ASN A 162     -10.570  13.733 -18.037  1.00 47.35           O  
ANISOU 1183  OD1 ASN A 162     5698   6999   5292    673    308    152       O  
ATOM   1184  ND2 ASN A 162     -10.482  12.066 -19.537  1.00 54.57           N  
ANISOU 1184  ND2 ASN A 162     6742   7805   6187    728    366    207       N  
ATOM   1185  N   ASN A 163     -11.725  14.538 -15.277  1.00 34.16           N  
ANISOU 1185  N   ASN A 163     3955   5405   3619    654    259    122       N  
ATOM   1186  CA  ASN A 163     -11.897  16.004 -15.116  1.00 36.85           C  
ANISOU 1186  CA  ASN A 163     4231   5769   3999    569    230     69       C  
ATOM   1187  C   ASN A 163     -13.065  16.399 -14.227  1.00 36.43           C  
ANISOU 1187  C   ASN A 163     4184   5687   3971    529    213     56       C  
ATOM   1188  O   ASN A 163     -13.383  17.568 -14.209  1.00 42.58           O  
ANISOU 1188  O   ASN A 163     4926   6461   4788    458    196     17       O  
ATOM   1189  CB  ASN A 163     -12.136  16.704 -16.472  1.00 40.92           C  
ANISOU 1189  CB  ASN A 163     4768   6212   4565    495    229     53       C  
ATOM   1190  CG  ASN A 163     -10.988  17.612 -16.816  1.00 45.80           C  
ANISOU 1190  CG  ASN A 163     5315   6904   5184    468    230     16       C  
ATOM   1191  OD1 ASN A 163      -9.917  17.409 -16.277  1.00 53.15           O  
ANISOU 1191  OD1 ASN A 163     6185   7937   6071    517    234     10       O  
ATOM   1192  ND2 ASN A 163     -11.185  18.606 -17.672  1.00 48.00           N  
ANISOU 1192  ND2 ASN A 163     5596   7134   5506    393    227     -8       N  
ATOM   1193  N   VAL A 164     -13.632  15.513 -13.446  1.00 31.91           N  
ANISOU 1193  N   VAL A 164     3653   5097   3373    575    222     86       N  
ATOM   1194  CA  VAL A 164     -14.752  15.893 -12.544  1.00 32.59           C  
ANISOU 1194  CA  VAL A 164     3742   5157   3482    537    209     70       C  
ATOM   1195  C   VAL A 164     -14.221  16.536 -11.240  1.00 35.97           C  
ANISOU 1195  C   VAL A 164     4088   5696   3881    544    193     40       C  
ATOM   1196  O   VAL A 164     -14.684  17.634 -10.872  1.00 33.20           O  
ANISOU 1196  O   VAL A 164     3699   5348   3566    476    176     -1       O  
ATOM   1197  CB  VAL A 164     -15.609  14.647 -12.261  1.00 34.01           C  
ANISOU 1197  CB  VAL A 164     4006   5268   3646    576    234    111       C  
ATOM   1198  CG1 VAL A 164     -16.608  14.892 -11.168  1.00 34.68           C  
ANISOU 1198  CG1 VAL A 164     4090   5343   3743    550    227     97       C  
ATOM   1199  CG2 VAL A 164     -16.292  14.137 -13.527  1.00 34.98           C  
ANISOU 1199  CG2 VAL A 164     4205   5282   3801    549    248    129       C  
ATOM   1200  N   GLU A 165     -13.282  15.855 -10.557  1.00 33.29           N  
ANISOU 1200  N   GLU A 165     3725   5448   3475    627    199     60       N  
ATOM   1201  CA  GLU A 165     -12.731  16.380  -9.290  1.00 34.22           C  
ANISOU 1201  CA  GLU A 165     3764   5685   3553    638    181     30       C  
ATOM   1202  C   GLU A 165     -12.243  17.822  -9.514  1.00 34.66           C  
ANISOU 1202  C   GLU A 165     3736   5791   3640    557    163    -31       C  
ATOM   1203  O   GLU A 165     -12.501  18.724  -8.651  1.00 32.96           O  
ANISOU 1203  O   GLU A 165     3474   5614   3433    506    149    -75       O  
ATOM   1204  CB  GLU A 165     -11.608  15.446  -8.805  1.00 40.22           C  
ANISOU 1204  CB  GLU A 165     4502   6545   4233    748    188     64       C  
ATOM   1205  CG  GLU A 165     -11.210  15.739  -7.375  1.00 46.47           C  
ANISOU 1205  CG  GLU A 165     5226   7460   4970    773    169     43       C  
ATOM   1206  CD  GLU A 165     -10.106  14.832  -6.885  1.00 53.22           C  
ANISOU 1206  CD  GLU A 165     6056   8424   5740    892    172     79       C  
ATOM   1207  OE1 GLU A 165      -9.231  14.426  -7.707  0.70 54.00           O  
ANISOU 1207  OE1 GLU A 165     6145   8544   5827    938    182     97       O  
ATOM   1208  OE2 GLU A 165     -10.134  14.531  -5.693  0.70 57.15           O  
ANISOU 1208  OE2 GLU A 165     6545   8984   6182    942    165     91       O  
ATOM   1209  N   GLN A 166     -11.516  18.061 -10.613  1.00 34.57           N  
ANISOU 1209  N   GLN A 166     3709   5781   3645    542    168    -39       N  
ATOM   1210  CA  GLN A 166     -10.857  19.371 -10.860  1.00 37.62           C  
ANISOU 1210  CA  GLN A 166     4018   6221   4052    467    161   -100       C  
ATOM   1211  C   GLN A 166     -11.919  20.470 -10.878  1.00 34.18           C  
ANISOU 1211  C   GLN A 166     3597   5706   3680    373    157   -133       C  
ATOM   1212  O   GLN A 166     -11.659  21.587 -10.437  1.00 35.48           O  
ANISOU 1212  O   GLN A 166     3702   5922   3855    312    154   -188       O  
ATOM   1213  CB  GLN A 166     -10.074  19.317 -12.183  1.00 43.52           C  
ANISOU 1213  CB  GLN A 166     4768   6956   4810    467    176    -95       C  
ATOM   1214  CG  GLN A 166      -9.089  20.478 -12.376  1.00 55.82           C  
ANISOU 1214  CG  GLN A 166     6242   8593   6374    404    178   -157       C  
ATOM   1215  CD  GLN A 166      -7.990  20.536 -11.322  1.00 63.31           C  
ANISOU 1215  CD  GLN A 166     7090   9703   7259    437    168   -188       C  
ATOM   1216  OE1 GLN A 166      -7.841  21.513 -10.576  1.00 68.86           O  
ANISOU 1216  OE1 GLN A 166     7728  10473   7961    377    161   -246       O  
ATOM   1217  NE2 GLN A 166      -7.222  19.460 -11.215  1.00 65.52           N  
ANISOU 1217  NE2 GLN A 166     7357  10054   7483    537    169   -151       N  
ATOM   1218  N   VAL A 167     -13.080  20.204 -11.470  1.00 30.57           N  
ANISOU 1218  N   VAL A 167     3219   5126   3267    359    160   -104       N  
ATOM   1219  CA  VAL A 167     -14.164  21.215 -11.564  1.00 31.61           C  
ANISOU 1219  CA  VAL A 167     3366   5179   3462    280    156   -130       C  
ATOM   1220  C   VAL A 167     -14.475  21.749 -10.161  1.00 31.14           C  
ANISOU 1220  C   VAL A 167     3265   5171   3393    260    149   -164       C  
ATOM   1221  O   VAL A 167     -14.624  22.955  -9.998  1.00 32.83           O  
ANISOU 1221  O   VAL A 167     3448   5384   3641    192    151   -210       O  
ATOM   1222  CB  VAL A 167     -15.426  20.621 -12.197  1.00 31.15           C  
ANISOU 1222  CB  VAL A 167     3391   5002   3439    283    155    -90       C  
ATOM   1223  CG1 VAL A 167     -16.562  21.650 -12.225  1.00 34.88           C  
ANISOU 1223  CG1 VAL A 167     3873   5404   3974    214    149   -115       C  
ATOM   1224  CG2 VAL A 167     -15.146  20.130 -13.619  1.00 32.19           C  
ANISOU 1224  CG2 VAL A 167     3568   5082   3578    296    163    -61       C  
ATOM   1225  N   PHE A 168     -14.654  20.860  -9.225  1.00 33.49           N  
ANISOU 1225  N   PHE A 168     3573   5501   3648    318    145   -138       N  
ATOM   1226  CA  PHE A 168     -15.050  21.238  -7.824  1.00 31.51           C  
ANISOU 1226  CA  PHE A 168     3292   5295   3382    304    140   -166       C  
ATOM   1227  C   PHE A 168     -13.879  21.851  -7.052  1.00 36.41           C  
ANISOU 1227  C   PHE A 168     3824   6052   3957    296    134   -213       C  
ATOM   1228  O   PHE A 168     -14.112  22.846  -6.364  1.00 36.42           O  
ANISOU 1228  O   PHE A 168     3788   6074   3972    235    134   -263       O  
ATOM   1229  CB  PHE A 168     -15.627  20.009  -7.131  1.00 32.74           C  
ANISOU 1229  CB  PHE A 168     3500   5436   3504    371    144   -119       C  
ATOM   1230  CG  PHE A 168     -16.989  19.597  -7.641  1.00 31.65           C  
ANISOU 1230  CG  PHE A 168     3440   5169   3416    356    153    -91       C  
ATOM   1231  CD1 PHE A 168     -18.129  20.212  -7.157  1.00 32.08           C  
ANISOU 1231  CD1 PHE A 168     3501   5174   3514    303    154   -114       C  
ATOM   1232  CD2 PHE A 168     -17.152  18.560  -8.549  1.00 30.99           C  
ANISOU 1232  CD2 PHE A 168     3421   5020   3332    394    164    -44       C  
ATOM   1233  CE1 PHE A 168     -19.385  19.752  -7.532  1.00 32.06           C  
ANISOU 1233  CE1 PHE A 168     3561   5069   3551    292    161    -91       C  
ATOM   1234  CE2 PHE A 168     -18.410  18.159  -8.985  1.00 32.09           C  
ANISOU 1234  CE2 PHE A 168     3626   5053   3512    374    173    -25       C  
ATOM   1235  CZ  PHE A 168     -19.531  18.728  -8.460  1.00 31.24           C  
ANISOU 1235  CZ  PHE A 168     3517   4905   3445    324    170    -48       C  
ATOM   1236  N   LEU A 169     -12.668  21.332  -7.213  1.00 36.72           N  
ANISOU 1236  N   LEU A 169     3827   6181   3944    350    130   -203       N  
ATOM   1237  CA  LEU A 169     -11.509  21.881  -6.475  1.00 37.67           C  
ANISOU 1237  CA  LEU A 169     3851   6448   4013    342    121   -253       C  
ATOM   1238  C   LEU A 169     -11.247  23.302  -6.972  1.00 40.88           C  
ANISOU 1238  C   LEU A 169     4214   6849   4466    239    132   -318       C  
ATOM   1239  O   LEU A 169     -11.012  24.171  -6.143  1.00 35.95           O  
ANISOU 1239  O   LEU A 169     3532   6297   3830    186    132   -377       O  
ATOM   1240  CB  LEU A 169     -10.341  20.931  -6.652  1.00 41.44           C  
ANISOU 1240  CB  LEU A 169     4300   7017   4427    431    116   -221       C  
ATOM   1241  CG  LEU A 169     -10.538  19.498  -6.164  1.00 41.58           C  
ANISOU 1241  CG  LEU A 169     4370   7035   4393    542    115   -152       C  
ATOM   1242  CD1 LEU A 169      -9.225  18.726  -6.311  1.00 46.57           C  
ANISOU 1242  CD1 LEU A 169     4960   7774   4959    633    112   -128       C  
ATOM   1243  CD2 LEU A 169     -11.016  19.470  -4.712  1.00 46.84           C  
ANISOU 1243  CD2 LEU A 169     5028   7746   5020    554    104   -159       C  
ATOM   1244  N   ASP A 170     -11.398  23.568  -8.271  1.00 34.78           N  
ANISOU 1244  N   ASP A 170     3481   5983   3749    206    146   -309       N  
ATOM   1245  CA  ASP A 170     -11.116  24.916  -8.833  1.00 36.17           C  
ANISOU 1245  CA  ASP A 170     3629   6143   3968    111    165   -367       C  
ATOM   1246  C   ASP A 170     -12.140  25.885  -8.281  1.00 37.58           C  
ANISOU 1246  C   ASP A 170     3824   6261   4192     43    173   -399       C  
ATOM   1247  O   ASP A 170     -11.873  27.140  -8.181  1.00 35.95           O  
ANISOU 1247  O   ASP A 170     3581   6069   4006    -40    195   -463       O  
ATOM   1248  CB  ASP A 170     -11.127  24.902 -10.378  1.00 35.19           C  
ANISOU 1248  CB  ASP A 170     3557   5925   3888    101    179   -340       C  
ATOM   1249  CG  ASP A 170      -9.882  24.287 -10.995  1.00 40.44           C  
ANISOU 1249  CG  ASP A 170     4190   6661   4513    146    182   -328       C  
ATOM   1250  OD1 ASP A 170      -8.915  23.978 -10.190  1.00 40.49           O  
ANISOU 1250  OD1 ASP A 170     4121   6804   4457    183    172   -347       O  
ATOM   1251  OD2 ASP A 170      -9.885  24.074 -12.256  1.00 37.68           O  
ANISOU 1251  OD2 ASP A 170     3889   6235   4190    149    193   -299       O  
ATOM   1252  N   LEU A 171     -13.325  25.369  -7.961  1.00 37.39           N  
ANISOU 1252  N   LEU A 171     3857   6163   4186     72    163   -360       N  
ATOM   1253  CA  LEU A 171     -14.362  26.219  -7.358  1.00 43.90           C  
ANISOU 1253  CA  LEU A 171     4695   6931   5052     16    172   -388       C  
ATOM   1254  C   LEU A 171     -13.868  26.779  -6.034  1.00 47.86           C  
ANISOU 1254  C   LEU A 171     5129   7543   5513    -13    174   -446       C  
ATOM   1255  O   LEU A 171     -14.128  27.982  -5.742  1.00 46.97           O  
ANISOU 1255  O   LEU A 171     5001   7410   5432    -91    196   -501       O  
ATOM   1256  CB  LEU A 171     -15.610  25.375  -7.063  1.00 48.84           C  
ANISOU 1256  CB  LEU A 171     5381   7483   5691     61    160   -338       C  
ATOM   1257  CG  LEU A 171     -16.715  25.401  -8.083  1.00 45.73           C  
ANISOU 1257  CG  LEU A 171     5055   6956   5362     49    163   -305       C  
ATOM   1258  CD1 LEU A 171     -17.901  24.637  -7.544  1.00 43.99           C  
ANISOU 1258  CD1 LEU A 171     4878   6684   5148     82    156   -271       C  
ATOM   1259  CD2 LEU A 171     -17.151  26.804  -8.388  1.00 50.22           C  
ANISOU 1259  CD2 LEU A 171     5624   7465   5991    -25    181   -345       C  
ATOM   1260  N   ALA A 172     -13.222  25.932  -5.229  1.00 56.28           N  
ANISOU 1260  N   ALA A 172     6157   8719   6505     48    154   -435       N  
ATOM   1261  CA  ALA A 172     -12.862  26.244  -3.829  1.00 60.26           C  
ANISOU 1261  CA  ALA A 172     6600   9340   6956     33    149   -482       C  
ATOM   1262  C   ALA A 172     -12.151  27.581  -3.826  1.00 63.31           C  
ANISOU 1262  C   ALA A 172     6924   9778   7352    -60    170   -564       C  
ATOM   1263  O   ALA A 172     -12.625  28.542  -3.131  1.00 59.45           O  
ANISOU 1263  O   ALA A 172     6427   9276   6883   -130    189   -616       O  
ATOM   1264  CB  ALA A 172     -11.942  25.196  -3.240  1.00 63.12           C  
ANISOU 1264  CB  ALA A 172     6920   9831   7229    120    124   -458       C  
ATOM   1265  N   ALA A 173     -11.025  27.572  -4.538  1.00 61.85           N  
ANISOU 1265  N   ALA A 173     6697   9653   7148    -60    172   -576       N  
ATOM   1266  CA  ALA A 173     -10.188  28.734  -4.874  1.00 65.44           C  
ANISOU 1266  CA  ALA A 173     7098  10149   7615   -150    200   -651       C  
ATOM   1267  C   ALA A 173     -11.069  29.985  -4.873  1.00 65.78           C  
ANISOU 1267  C   ALA A 173     7180  10085   7726   -243    236   -691       C  
ATOM   1268  O   ALA A 173     -10.818  30.894  -4.042  1.00 64.95           O  
ANISOU 1268  O   ALA A 173     7029  10042   7607   -316    256   -765       O  
ATOM   1269  CB  ALA A 173      -9.530  28.480  -6.221  1.00 63.12           C  
ANISOU 1269  CB  ALA A 173     6813   9832   7337   -135    207   -626       C  
ATOM   1270  N   LYS A 174     -12.125  29.984  -5.711  1.00 59.95           N  
ANISOU 1270  N   LYS A 174     6526   9195   7056   -235    243   -642       N  
ATOM   1271  CA  LYS A 174     -12.831  31.213  -6.128  1.00 55.14           C  
ANISOU 1271  CA  LYS A 174     5961   8469   6518   -313    283   -671       C  
ATOM   1272  C   LYS A 174     -13.829  31.589  -5.033  1.00 55.30           C  
ANISOU 1272  C   LYS A 174     5995   8463   6553   -332    288   -688       C  
ATOM   1273  O   LYS A 174     -14.367  32.702  -5.096  1.00 56.88           O  
ANISOU 1273  O   LYS A 174     6222   8585   6805   -398    326   -723       O  
ATOM   1274  CB  LYS A 174     -13.443  31.060  -7.531  1.00 56.12           C  
ANISOU 1274  CB  LYS A 174     6161   8460   6700   -290    285   -612       C  
ATOM   1275  CG  LYS A 174     -12.494  30.792  -8.708  1.00 57.03           C  
ANISOU 1275  CG  LYS A 174     6273   8589   6807   -279    288   -597       C  
ATOM   1276  N   LEU A 175     -14.110  30.686  -4.090  1.00 55.21           N  
ANISOU 1276  N   LEU A 175     5972   8506   6497   -273    256   -663       N  
ATOM   1277  CA  LEU A 175     -15.089  30.918  -2.998  1.00 59.18           C  
ANISOU 1277  CA  LEU A 175     6489   8985   7008   -286    261   -676       C  
ATOM   1278  C   LEU A 175     -14.454  31.893  -2.001  1.00 69.50           C  
ANISOU 1278  C   LEU A 175     7734  10387   8283   -364    285   -764       C  
ATOM   1279  O   LEU A 175     -13.178  32.016  -1.862  1.00 66.63           O  
ANISOU 1279  O   LEU A 175     7301  10147   7865   -387    283   -810       O  
ATOM   1280  CB  LEU A 175     -15.510  29.590  -2.343  1.00 57.49           C  
ANISOU 1280  CB  LEU A 175     6290   8802   6753   -199    225   -619       C  
ATOM   1281  CG  LEU A 175     -16.312  28.632  -3.226  1.00 58.62           C  
ANISOU 1281  CG  LEU A 175     6500   8841   6930   -133    208   -539       C  
ATOM   1282  CD1 LEU A 175     -16.600  27.308  -2.541  1.00 60.18           C  
ANISOU 1282  CD1 LEU A 175     6715   9072   7079    -52    183   -489       C  
ATOM   1283  CD2 LEU A 175     -17.612  29.235  -3.685  1.00 56.36           C  
ANISOU 1283  CD2 LEU A 175     6270   8418   6726   -165    227   -531       C  
ATOM   1284  OXT LEU A 175     -15.248  32.605  -1.371  1.00 69.71           O  
ANISOU 1284  OXT LEU A 175     7781  10365   8340   -408    311   -795       O  
TER    1285      LEU A 175                                                      
HETATM 1286  PB  GDP A 201     -29.234  14.212 -15.521  1.00 27.19           P  
ANISOU 1286  PB  GDP A 201     3392   3763   3175     42    198    -17       P  
HETATM 1287  O1B GDP A 201     -30.594  14.006 -16.100  1.00 26.04           O  
ANISOU 1287  O1B GDP A 201     3247   3591   3057    -14    189    -42       O  
HETATM 1288  O2B GDP A 201     -29.146  14.149 -13.973  1.00 24.37           O  
ANISOU 1288  O2B GDP A 201     3024   3427   2808     65    226    -18       O  
HETATM 1289  O3B GDP A 201     -28.586  15.484 -16.071  1.00 24.36           O  
ANISOU 1289  O3B GDP A 201     2985   3432   2836     53    154    -13       O  
HETATM 1290  O3A GDP A 201     -28.288  13.033 -16.068  1.00 27.98           O  
ANISOU 1290  O3A GDP A 201     3565   3842   3222     73    234     11       O  
HETATM 1291  PA  GDP A 201     -27.856  11.620 -15.462  1.00 29.02           P  
ANISOU 1291  PA  GDP A 201     3771   3951   3303    110    297     33       P  
HETATM 1292  O1A GDP A 201     -29.044  10.989 -14.885  1.00 30.19           O  
ANISOU 1292  O1A GDP A 201     3944   4066   3459     70    330     12       O  
HETATM 1293  O2A GDP A 201     -26.711  11.798 -14.574  1.00 29.39           O  
ANISOU 1293  O2A GDP A 201     3802   4042   3320    174    305     56       O  
HETATM 1294  O5' GDP A 201     -27.288  10.845 -16.717  1.00 27.95           O  
ANISOU 1294  O5' GDP A 201     3697   3784   3138    116    313     51       O  
HETATM 1295  C5' GDP A 201     -28.140  10.717 -17.879  1.00 29.67           C  
ANISOU 1295  C5' GDP A 201     3929   3970   3374     56    298     30       C  
HETATM 1296  C4' GDP A 201     -27.671   9.465 -18.660  1.00 31.98           C  
ANISOU 1296  C4' GDP A 201     4309   4217   3623     65    345     46       C  
HETATM 1297  O4' GDP A 201     -26.373   9.676 -19.206  1.00 32.03           O  
ANISOU 1297  O4' GDP A 201     4317   4243   3608    114    336     74       O  
HETATM 1298  C3' GDP A 201     -27.536   8.251 -17.709  1.00 34.12           C  
ANISOU 1298  C3' GDP A 201     4649   4457   3857     97    419     62       C  
HETATM 1299  O3' GDP A 201     -27.911   7.087 -18.356  1.00 36.65           O  
ANISOU 1299  O3' GDP A 201     5051   4717   4154     65    469     55       O  
HETATM 1300  C2' GDP A 201     -26.100   8.171 -17.354  1.00 33.72           C  
ANISOU 1300  C2' GDP A 201     4606   4433   3771    182    432    102       C  
HETATM 1301  O2' GDP A 201     -25.685   6.847 -17.071  1.00 34.87           O  
ANISOU 1301  O2' GDP A 201     4841   4538   3869    226    505    129       O  
HETATM 1302  C1' GDP A 201     -25.459   8.736 -18.646  1.00 32.19           C  
ANISOU 1302  C1' GDP A 201     4391   4254   3584    179    392    105       C  
HETATM 1303  N9  GDP A 201     -24.161   9.425 -18.402  1.00 30.24           N  
ANISOU 1303  N9  GDP A 201     4097   4065   3327    241    369    128       N  
HETATM 1304  C8  GDP A 201     -23.972  10.380 -17.443  1.00 28.29           C  
ANISOU 1304  C8  GDP A 201     3777   3874   3097    258    337    123       C  
HETATM 1305  N7  GDP A 201     -22.761  10.839 -17.469  1.00 26.49           N  
ANISOU 1305  N7  GDP A 201     3514   3695   2853    305    324    138       N  
HETATM 1306  C5  GDP A 201     -22.117  10.147 -18.503  1.00 26.20           C  
ANISOU 1306  C5  GDP A 201     3531   3633   2791    324    348    157       C  
HETATM 1307  C6  GDP A 201     -20.816  10.097 -19.060  1.00 27.39           C  
ANISOU 1307  C6  GDP A 201     3681   3810   2916    372    355    177       C  
HETATM 1308  O6  GDP A 201     -19.920  10.875 -18.650  1.00 28.15           O  
ANISOU 1308  O6  GDP A 201     3711   3973   3010    403    332    178       O  
HETATM 1309  N1  GDP A 201     -20.634   9.318 -20.115  1.00 28.19           N  
ANISOU 1309  N1  GDP A 201     3848   3864   2999    371    384    188       N  
HETATM 1310  C2  GDP A 201     -21.554   8.410 -20.599  1.00 28.56           C  
ANISOU 1310  C2  GDP A 201     3970   3839   3042    331    415    182       C  
HETATM 1311  N2  GDP A 201     -21.247   7.625 -21.593  1.00 30.54           N  
ANISOU 1311  N2  GDP A 201     4287   4045   3269    333    450    192       N  
HETATM 1312  N3  GDP A 201     -22.798   8.390 -20.136  1.00 27.45           N  
ANISOU 1312  N3  GDP A 201     3831   3674   2924    280    410    160       N  
HETATM 1313  C4  GDP A 201     -23.078   9.241 -19.119  1.00 27.14           C  
ANISOU 1313  C4  GDP A 201     3722   3679   2909    279    377    149       C  
HETATM 1314  C1  GOL A 202     -16.040   5.944 -29.442  1.00 67.34           C  
ANISOU 1314  C1  GOL A 202     9193   8594   7797    389    592    243       C  
HETATM 1315  O1  GOL A 202     -15.472   7.250 -29.394  1.00 59.21           O  
ANISOU 1315  O1  GOL A 202     8071   7632   6791    391    539    238       O  
HETATM 1316  C2  GOL A 202     -17.273   5.836 -28.560  1.00 63.87           C  
ANISOU 1316  C2  GOL A 202     8752   8140   7375    356    574    231       C  
HETATM 1317  O2  GOL A 202     -16.919   5.661 -27.184  1.00 64.04           O  
ANISOU 1317  O2  GOL A 202     8740   8197   7393    426    588    252       O  
HETATM 1318  C3  GOL A 202     -18.184   7.034 -28.709  1.00 54.48           C  
ANISOU 1318  C3  GOL A 202     7501   6974   6223    284    498    204       C  
HETATM 1319  O3  GOL A 202     -19.569   6.729 -28.598  1.00 57.57           O  
ANISOU 1319  O3  GOL A 202     7920   7329   6624    222    488    182       O  
HETATM 1320  C   ACT A 203     -15.494  31.870 -34.156  1.00 63.14           C  
ANISOU 1320  C   ACT A 203     8333   7980   7675   -144    375    100       C  
HETATM 1321  O   ACT A 203     -16.670  31.425 -34.198  1.00 55.88           O  
ANISOU 1321  O   ACT A 203     7419   7057   6756   -103    313    132       O  
HETATM 1322  OXT ACT A 203     -15.237  33.068 -34.055  1.00 71.59           O  
ANISOU 1322  OXT ACT A 203     9424   9012   8763   -172    426     85       O  
HETATM 1323  CH3 ACT A 203     -14.277  30.937 -34.277  1.00 65.30           C  
ANISOU 1323  CH3 ACT A 203     8577   8308   7923   -163    397     77       C  
HETATM 1324 MG    MG A 204     -30.586  14.033 -12.520  1.00 26.09          MG  
HETATM 1325  O   HOH A 301      -0.984  27.961   2.286  1.00 40.68           O  
HETATM 1326  O   HOH A 302     -12.346  21.205 -31.515  1.00 51.94           O  
HETATM 1327  O   HOH A 303     -26.384  17.885   2.623  1.00 48.33           O  
HETATM 1328  O   HOH A 304     -19.878  22.867 -33.875  1.00 46.25           O  
HETATM 1329  O   HOH A 305     -27.685  29.240 -27.023  1.00 45.03           O  
HETATM 1330  O   HOH A 306     -31.099  22.210 -31.495  1.00 45.37           O  
HETATM 1331  O   HOH A 307     -22.470  35.781 -11.394  1.00 53.45           O  
HETATM 1332  O   HOH A 308     -17.790   5.370 -22.949  1.00 42.04           O  
HETATM 1333  O   HOH A 309      -7.988  27.615   8.714  1.00 46.54           O  
HETATM 1334  O   HOH A 310     -31.952  11.930 -16.766  1.00 34.73           O  
HETATM 1335  O   HOH A 311     -30.985   9.473 -15.938  1.00 34.98           O  
HETATM 1336  O   HOH A 312     -32.031  13.706 -11.068  1.00 26.27           O  
HETATM 1337  O   HOH A 313     -21.517   9.141 -11.489  1.00 33.21           O  
HETATM 1338  O   HOH A 314     -11.903  17.570 -24.024  1.00 42.01           O  
HETATM 1339  O   HOH A 315     -28.282  12.917  -7.429  1.00 31.23           O  
HETATM 1340  O   HOH A 316     -12.342  13.382 -11.890  1.00 40.55           O  
HETATM 1341  O   HOH A 317     -33.931  32.343  -5.954  1.00 52.05           O  
HETATM 1342  O   HOH A 318     -33.007  16.111 -22.670  1.00 44.83           O  
HETATM 1343  O   HOH A 319     -38.798  17.532 -20.375  1.00 43.91           O  
HETATM 1344  O   HOH A 320     -18.151  20.834 -26.007  1.00 26.21           O  
HETATM 1345  O   HOH A 321     -13.999   6.820 -24.673  1.00 51.26           O  
HETATM 1346  O   HOH A 322     -30.354  15.936 -11.891  1.00 25.36           O  
HETATM 1347  O   HOH A 323      -9.554  26.682 -30.678  1.00 39.56           O  
HETATM 1348  O   HOH A 324      -9.820  28.126 -28.521  1.00 35.57           O  
HETATM 1349  O   HOH A 325     -41.164  15.073  -9.701  1.00 58.15           O  
HETATM 1350  O   HOH A 326     -23.413  28.834  -0.210  1.00 29.73           O  
HETATM 1351  O   HOH A 327     -21.319  28.408 -28.513  1.00 34.20           O  
HETATM 1352  O   HOH A 328     -37.716  29.840 -11.429  1.00 53.98           O  
HETATM 1353  O   HOH A 329     -22.514  30.631 -27.358  1.00 59.72           O  
HETATM 1354  O   HOH A 330     -33.184  28.058  -0.628  1.00 40.19           O  
HETATM 1355  O   HOH A 331     -15.723  36.612 -21.505  1.00 44.50           O  
HETATM 1356  O   HOH A 332     -25.770  11.948 -30.127  1.00 37.83           O  
HETATM 1357  O   HOH A 333     -32.066  14.589 -13.811  1.00 27.34           O  
HETATM 1358  O   HOH A 334     -15.502  35.530 -17.275  1.00 45.52           O  
HETATM 1359  O   HOH A 335     -38.941  14.691  -8.211  1.00 44.07           O  
HETATM 1360  O   HOH A 336     -16.451  12.374 -33.569  1.00 45.99           O  
HETATM 1361  O   HOH A 337     -14.441  13.541 -26.903  1.00 42.11           O  
HETATM 1362  O   HOH A 338     -19.346  12.950 -34.188  1.00 27.57           O  
HETATM 1363  O   HOH A 339      -7.797  24.489  -7.780  1.00 51.65           O  
HETATM 1364  O   HOH A 340     -20.573   5.199 -32.325  1.00 35.49           O  
HETATM 1365  O   HOH A 341      -8.509  16.509 -14.118  1.00 52.65           O  
HETATM 1366  O   HOH A 342     -39.917  22.248 -12.372  1.00 31.54           O  
HETATM 1367  O   HOH A 343     -26.762  35.215 -18.404  1.00 43.65           O  
HETATM 1368  O   HOH A 344      -1.885  30.521   0.515  1.00 38.94           O  
HETATM 1369  O   HOH A 345     -26.252  19.055  -0.004  1.00 52.47           O  
HETATM 1370  O   HOH A 346     -19.305  15.974   3.746  1.00 49.61           O  
HETATM 1371  O   HOH A 347     -31.439  14.279  -8.259  1.00 28.82           O  
HETATM 1372  O   HOH A 348     -34.727  19.752 -19.054  1.00 31.40           O  
HETATM 1373  O   HOH A 349     -20.033  32.878  -4.477  1.00 41.10           O  
HETATM 1374  O   HOH A 350     -27.816  21.826 -20.644  1.00 24.67           O  
HETATM 1375  O   HOH A 351     -30.858  12.018 -13.066  1.00 25.89           O  
HETATM 1376  O   HOH A 352     -28.543  14.616 -23.687  1.00 30.27           O  
HETATM 1377  O   HOH A 353     -31.493  22.116 -14.753  1.00 27.19           O  
HETATM 1378  O   HOH A 354     -14.392  25.328 -11.417  1.00 31.80           O  
HETATM 1379  O   HOH A 355     -26.758  32.907  -4.919  1.00 55.60           O  
HETATM 1380  O   HOH A 356     -23.207  21.705 -33.131  1.00 50.83           O  
HETATM 1381  O   HOH A 357     -31.518  10.248 -11.109  1.00 34.56           O  
HETATM 1382  O   HOH A 358     -35.610  15.106 -15.890  1.00 37.19           O  
HETATM 1383  O   HOH A 359     -31.891  19.847  -4.242  1.00 28.67           O  
HETATM 1384  O   HOH A 360     -18.038  33.957 -27.497  1.00 43.29           O  
HETATM 1385  O   HOH A 361     -23.924   8.104 -11.996  1.00 34.78           O  
HETATM 1386  O   HOH A 362     -24.309  12.298 -32.652  1.00 27.03           O  
HETATM 1387  O   HOH A 363     -25.527  27.763 -26.128  1.00 46.24           O  
HETATM 1388  O   HOH A 364      -8.325  31.219   3.667  1.00 45.92           O  
HETATM 1389  O   HOH A 365     -19.278  33.108 -12.682  1.00 34.22           O  
HETATM 1390  O   HOH A 366     -14.950  13.643 -30.276  1.00 44.67           O  
HETATM 1391  O   HOH A 367     -16.535  14.146   3.085  1.00 43.54           O  
HETATM 1392  O   HOH A 368     -28.934  17.930 -30.953  1.00 33.25           O  
HETATM 1393  O   HOH A 369     -28.254   9.263 -12.764  1.00 39.43           O  
HETATM 1394  O   HOH A 370     -24.857  31.402 -27.874  1.00 53.58           O  
HETATM 1395  O   HOH A 371      -9.099  13.700 -14.544  1.00 38.96           O  
HETATM 1396  O   HOH A 372     -29.231  16.806 -22.265  1.00 32.32           O  
HETATM 1397  O   HOH A 373     -23.513  12.797   0.139  1.00 42.65           O  
HETATM 1398  O   HOH A 374     -25.808  10.199 -26.666  1.00 49.12           O  
HETATM 1399  O   HOH A 375     -27.923   7.292 -14.403  1.00 36.45           O  
HETATM 1400  O   HOH A 376     -11.594  20.463 -20.123  1.00 33.73           O  
HETATM 1401  O   HOH A 377     -28.966  33.784  -3.478  1.00 41.69           O  
HETATM 1402  O   HOH A 378     -17.755   3.638 -15.106  1.00 48.45           O  
HETATM 1403  O   HOH A 379     -27.359  12.575 -26.747  1.00 49.54           O  
HETATM 1404  O   HOH A 380     -35.855   8.906 -16.259  1.00 55.96           O  
HETATM 1405  O   HOH A 381     -22.708   5.227 -22.439  1.00 50.11           O  
HETATM 1406  O   HOH A 382     -33.999   3.683 -12.136  1.00 55.33           O  
HETATM 1407  O   HOH A 383     -10.093  16.007 -12.156  1.00 35.31           O  
HETATM 1408  O   HOH A 384     -13.576  19.586 -29.891  1.00 28.06           O  
HETATM 1409  O   HOH A 385      -8.180  27.458 -26.268  1.00 31.32           O  
HETATM 1410  O   HOH A 386     -15.480  25.125 -33.493  1.00 55.45           O  
HETATM 1411  O   HOH A 387     -35.236  20.836  -8.206  1.00 36.35           O  
HETATM 1412  O   HOH A 388     -19.524   2.881  -9.619  1.00 53.48           O  
HETATM 1413  O   HOH A 389     -26.187  18.737   5.369  1.00 49.94           O  
HETATM 1414  O   HOH A 390     -25.151   8.389 -22.017  1.00 43.22           O  
HETATM 1415  O   HOH A 391     -13.971   9.764 -26.767  1.00 52.71           O  
HETATM 1416  O   HOH A 392     -20.634  28.571 -31.016  1.00 44.38           O  
HETATM 1417  O   HOH A 393     -13.783  30.804 -30.916  1.00 61.19           O  
HETATM 1418  O   HOH A 394     -13.217  33.543 -16.024  1.00 53.06           O  
HETATM 1419  O   HOH A 395     -14.502  12.701  -8.942  1.00 48.85           O  
HETATM 1420  O   HOH A 396     -28.208   9.230  -5.826  1.00 41.72           O  
HETATM 1421  O   HOH A 397     -36.377  17.733 -20.517  1.00 38.47           O  
HETATM 1422  O   HOH A 398     -18.196  17.030 -33.812  1.00 41.50           O  
HETATM 1423  O   HOH A 399     -41.279  20.492 -22.770  1.00 57.64           O  
HETATM 1424  O   HOH A 400     -30.943   8.098 -18.149  1.00 51.97           O  
HETATM 1425  O   HOH A 401     -39.317  28.863  -4.985  1.00 49.41           O  
HETATM 1426  O   HOH A 402     -12.590  18.329 -27.586  1.00 44.42           O  
HETATM 1427  O   HOH A 403     -30.845  18.466 -24.071  1.00 47.85           O  
HETATM 1428  O   HOH A 404     -13.167  10.569 -21.162  1.00 45.11           O  
HETATM 1429  O   HOH A 405     -13.781  28.088 -10.687  1.00 41.57           O  
HETATM 1430  O   HOH A 406     -26.216   9.581 -10.907  1.00 42.13           O  
HETATM 1431  O   HOH A 407     -13.379  12.795  -6.983  1.00 60.86           O  
HETATM 1432  O   HOH A 408     -20.159  18.814 -35.342  1.00 53.94           O  
HETATM 1433  O   HOH A 409     -28.366  22.108 -34.121  1.00 48.14           O  
HETATM 1434  O   HOH A 410     -26.048  15.800   1.947  1.00 51.58           O  
HETATM 1435  O   HOH A 411     -31.278  31.862 -23.708  1.00 63.12           O  
HETATM 1436  O   HOH A 412     -33.119  12.025 -19.198  1.00 49.95           O  
HETATM 1437  O   HOH A 413     -29.666   8.902 -10.107  1.00 40.17           O  
HETATM 1438  O   HOH A 414     -24.061  33.128  -0.701  1.00 60.40           O  
HETATM 1439  O   HOH A 415     -12.096  10.661 -23.308  1.00 57.17           O  
HETATM 1440  O   HOH A 416     -30.120  12.611 -23.171  1.00 49.53           O  
HETATM 1441  O   HOH A 417     -29.940  19.991 -32.517  1.00 39.51           O  
HETATM 1442  O   HOH A 418     -34.587  30.039   1.070  1.00 54.21           O  
HETATM 1443  O   HOH A 419     -14.598  18.567 -32.184  1.00 39.90           O  
HETATM 1444  O   HOH A 420     -13.199  31.561 -28.466  1.00 55.91           O  
HETATM 1445  O   HOH A 421     -34.345  20.620  -3.956  1.00 39.92           O  
HETATM 1446  O   HOH A 422     -12.880  12.207 -28.756  1.00 57.92           O  
HETATM 1447  O   HOH A 423     -31.131  10.334 -20.123  1.00 49.61           O  
HETATM 1448  O   HOH A 424     -11.398  32.925 -29.623  1.00 57.27           O  
CONECT  110 1324                                                                
CONECT 1286 1287 1288 1289 1290                                                 
CONECT 1287 1286                                                                
CONECT 1288 1286 1324                                                           
CONECT 1289 1286                                                                
CONECT 1290 1286 1291                                                           
CONECT 1291 1290 1292 1293 1294                                                 
CONECT 1292 1291                                                                
CONECT 1293 1291                                                                
CONECT 1294 1291 1295                                                           
CONECT 1295 1294 1296                                                           
CONECT 1296 1295 1297 1298                                                      
CONECT 1297 1296 1302                                                           
CONECT 1298 1296 1299 1300                                                      
CONECT 1299 1298                                                                
CONECT 1300 1298 1301 1302                                                      
CONECT 1301 1300                                                                
CONECT 1302 1297 1300 1303                                                      
CONECT 1303 1302 1304 1313                                                      
CONECT 1304 1303 1305                                                           
CONECT 1305 1304 1306                                                           
CONECT 1306 1305 1307 1313                                                      
CONECT 1307 1306 1308 1309                                                      
CONECT 1308 1307                                                                
CONECT 1309 1307 1310                                                           
CONECT 1310 1309 1311 1312                                                      
CONECT 1311 1310                                                                
CONECT 1312 1310 1313                                                           
CONECT 1313 1303 1306 1312                                                      
CONECT 1314 1315 1316                                                           
CONECT 1315 1314                                                                
CONECT 1316 1314 1317 1318                                                      
CONECT 1317 1316                                                                
CONECT 1318 1316 1319                                                           
CONECT 1319 1318                                                                
CONECT 1320 1321 1322 1323                                                      
CONECT 1321 1320                                                                
CONECT 1322 1320                                                                
CONECT 1323 1320                                                                
CONECT 1324  110 1288                                                           
MASTER      358    0    4    7    6    0    0    6 1429    1   40   14          
END                                                                             



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